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***    ***

elNémo ID: 20072217202468518

Job options:

ID        	=	 20072217202468518
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


data_3D9S
# 
_entry.id   3D9S 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3D9S         
RCSB  RCSB047771   
WWPDB D_1000047771 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        3D9S 
_pdbx_database_status.recvd_initial_deposition_date   2008-05-27 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Horsefield, R.'                  1  
'Norden, K.'                      2  
'Fellert, M.'                     3  
'Backmark, A.'                    4  
'Tornroth-Horsefield, S.'         5  
'Terwisscha Van Scheltinga, A.C.' 6  
'Kvassman, J.'                    7  
'Kjellbom, P.'                    8  
'Johanson, U.'                    9  
'Neutze, R.'                      10 
# 
_citation.id                        primary 
_citation.title                     'High-resolution x-ray structure of human aquaporin 5' 
_citation.journal_abbrev            Proc.Natl.Acad.Sci.Usa 
_citation.journal_volume            105 
_citation.page_first                13327 
_citation.page_last                 13332 
_citation.year                      2008 
_citation.journal_id_ASTM           PNASA6 
_citation.country                   US 
_citation.journal_id_ISSN           0027-8424 
_citation.journal_id_CSD            0040 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   18768791 
_citation.pdbx_database_id_DOI      10.1073/pnas.0801466105 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Horsefield, R.'                  1  
primary 'Norden, K.'                      2  
primary 'Fellert, M.'                     3  
primary 'Backmark, A.'                    4  
primary 'Tornroth-Horsefield, S.'         5  
primary 'Terwisscha van Scheltinga, A.C.' 6  
primary 'Kvassman, J.'                    7  
primary 'Kjellbom, P.'                    8  
primary 'Johanson, U.'                    9  
primary 'Neutze, R.'                      10 
# 
_cell.entry_id           3D9S 
_cell.length_a           90.477 
_cell.length_b           90.644 
_cell.length_c           184.395 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              16 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         3D9S 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man Aquaporin-5                                                                                  28399.145 4   ? ? ? 
? 
2 non-polymer syn 'O-[(S)-{[(2S)-2-(hexanoyloxy)-3-(tetradecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-D-serine' 567.650   1   ? ? ? 
? 
3 water       nat water                                                                                        18.015    111 ? ? ? 
? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        AQP-5 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSKKEVCSVAFLKAVFAEFLATLIFVFFGLGSALKWPSALPTILQIALAFGLAIGTLAQALGPVSGGHINPAITLALLVG
NQISLLRAFFYVAAQLVGAIAGAGILYGVAPLNARGNLAVNALNNNTTQGQAMVVELILTFQLALCIFASTDSRRTSPVG
SPALSIGLSVTLGHLVGIYFTGCSMNPARSFGPAVVMNRFSPAHWVFWVGPIVGAVLAAILYFYLLFPNSLSLSERVAII
KGTYEPDEDWEEQREERKKTMELTTR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSKKEVCSVAFLKAVFAEFLATLIFVFFGLGSALKWPSALPTILQIALAFGLAIGTLAQALGPVSGGHINPAITLALLVG
NQISLLRAFFYVAAQLVGAIAGAGILYGVAPLNARGNLAVNALNNNTTQGQAMVVELILTFQLALCIFASTDSRRTSPVG
SPALSIGLSVTLGHLVGIYFTGCSMNPARSFGPAVVMNRFSPAHWVFWVGPIVGAVLAAILYFYLLFPNSLSLSERVAII
KGTYEPDEDWEEQREERKKTMELTTR
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   LYS n 
1 4   LYS n 
1 5   GLU n 
1 6   VAL n 
1 7   CYS n 
1 8   SER n 
1 9   VAL n 
1 10  ALA n 
1 11  PHE n 
1 12  LEU n 
1 13  LYS n 
1 14  ALA n 
1 15  VAL n 
1 16  PHE n 
1 17  ALA n 
1 18  GLU n 
1 19  PHE n 
1 20  LEU n 
1 21  ALA n 
1 22  THR n 
1 23  LEU n 
1 24  ILE n 
1 25  PHE n 
1 26  VAL n 
1 27  PHE n 
1 28  PHE n 
1 29  GLY n 
1 30  LEU n 
1 31  GLY n 
1 32  SER n 
1 33  ALA n 
1 34  LEU n 
1 35  LYS n 
1 36  TRP n 
1 37  PRO n 
1 38  SER n 
1 39  ALA n 
1 40  LEU n 
1 41  PRO n 
1 42  THR n 
1 43  ILE n 
1 44  LEU n 
1 45  GLN n 
1 46  ILE n 
1 47  ALA n 
1 48  LEU n 
1 49  ALA n 
1 50  PHE n 
1 51  GLY n 
1 52  LEU n 
1 53  ALA n 
1 54  ILE n 
1 55  GLY n 
1 56  THR n 
1 57  LEU n 
1 58  ALA n 
1 59  GLN n 
1 60  ALA n 
1 61  LEU n 
1 62  GLY n 
1 63  PRO n 
1 64  VAL n 
1 65  SER n 
1 66  GLY n 
1 67  GLY n 
1 68  HIS n 
1 69  ILE n 
1 70  ASN n 
1 71  PRO n 
1 72  ALA n 
1 73  ILE n 
1 74  THR n 
1 75  LEU n 
1 76  ALA n 
1 77  LEU n 
1 78  LEU n 
1 79  VAL n 
1 80  GLY n 
1 81  ASN n 
1 82  GLN n 
1 83  ILE n 
1 84  SER n 
1 85  LEU n 
1 86  LEU n 
1 87  ARG n 
1 88  ALA n 
1 89  PHE n 
1 90  PHE n 
1 91  TYR n 
1 92  VAL n 
1 93  ALA n 
1 94  ALA n 
1 95  GLN n 
1 96  LEU n 
1 97  VAL n 
1 98  GLY n 
1 99  ALA n 
1 100 ILE n 
1 101 ALA n 
1 102 GLY n 
1 103 ALA n 
1 104 GLY n 
1 105 ILE n 
1 106 LEU n 
1 107 TYR n 
1 108 GLY n 
1 109 VAL n 
1 110 ALA n 
1 111 PRO n 
1 112 LEU n 
1 113 ASN n 
1 114 ALA n 
1 115 ARG n 
1 116 GLY n 
1 117 ASN n 
1 118 LEU n 
1 119 ALA n 
1 120 VAL n 
1 121 ASN n 
1 122 ALA n 
1 123 LEU n 
1 124 ASN n 
1 125 ASN n 
1 126 ASN n 
1 127 THR n 
1 128 THR n 
1 129 GLN n 
1 130 GLY n 
1 131 GLN n 
1 132 ALA n 
1 133 MET n 
1 134 VAL n 
1 135 VAL n 
1 136 GLU n 
1 137 LEU n 
1 138 ILE n 
1 139 LEU n 
1 140 THR n 
1 141 PHE n 
1 142 GLN n 
1 143 LEU n 
1 144 ALA n 
1 145 LEU n 
1 146 CYS n 
1 147 ILE n 
1 148 PHE n 
1 149 ALA n 
1 150 SER n 
1 151 THR n 
1 152 ASP n 
1 153 SER n 
1 154 ARG n 
1 155 ARG n 
1 156 THR n 
1 157 SER n 
1 158 PRO n 
1 159 VAL n 
1 160 GLY n 
1 161 SER n 
1 162 PRO n 
1 163 ALA n 
1 164 LEU n 
1 165 SER n 
1 166 ILE n 
1 167 GLY n 
1 168 LEU n 
1 169 SER n 
1 170 VAL n 
1 171 THR n 
1 172 LEU n 
1 173 GLY n 
1 174 HIS n 
1 175 LEU n 
1 176 VAL n 
1 177 GLY n 
1 178 ILE n 
1 179 TYR n 
1 180 PHE n 
1 181 THR n 
1 182 GLY n 
1 183 CYS n 
1 184 SER n 
1 185 MET n 
1 186 ASN n 
1 187 PRO n 
1 188 ALA n 
1 189 ARG n 
1 190 SER n 
1 191 PHE n 
1 192 GLY n 
1 193 PRO n 
1 194 ALA n 
1 195 VAL n 
1 196 VAL n 
1 197 MET n 
1 198 ASN n 
1 199 ARG n 
1 200 PHE n 
1 201 SER n 
1 202 PRO n 
1 203 ALA n 
1 204 HIS n 
1 205 TRP n 
1 206 VAL n 
1 207 PHE n 
1 208 TRP n 
1 209 VAL n 
1 210 GLY n 
1 211 PRO n 
1 212 ILE n 
1 213 VAL n 
1 214 GLY n 
1 215 ALA n 
1 216 VAL n 
1 217 LEU n 
1 218 ALA n 
1 219 ALA n 
1 220 ILE n 
1 221 LEU n 
1 222 TYR n 
1 223 PHE n 
1 224 TYR n 
1 225 LEU n 
1 226 LEU n 
1 227 PHE n 
1 228 PRO n 
1 229 ASN n 
1 230 SER n 
1 231 LEU n 
1 232 SER n 
1 233 LEU n 
1 234 SER n 
1 235 GLU n 
1 236 ARG n 
1 237 VAL n 
1 238 ALA n 
1 239 ILE n 
1 240 ILE n 
1 241 LYS n 
1 242 GLY n 
1 243 THR n 
1 244 TYR n 
1 245 GLU n 
1 246 PRO n 
1 247 ASP n 
1 248 GLU n 
1 249 ASP n 
1 250 TRP n 
1 251 GLU n 
1 252 GLU n 
1 253 GLN n 
1 254 ARG n 
1 255 GLU n 
1 256 GLU n 
1 257 ARG n 
1 258 LYS n 
1 259 LYS n 
1 260 THR n 
1 261 MET n 
1 262 GLU n 
1 263 LEU n 
1 264 THR n 
1 265 THR n 
1 266 ARG n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 AQP5 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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      'Pichia pastoris' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     4922 
_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               X33 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pPICZB 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   'EasySelect Pichia Expression Kit (Invitrogen)' 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    AQP5_HUMAN 
_struct_ref.pdbx_db_accession          P55064 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;KKEVCSVAFLKAVFAEFLATLIFVFFGLGSALKWPSALPTILQIALAFGLAIGTLAQALGPVSGGHINPAITLALLVGNQ
ISLLRAFFYVAAQLVGAIAGAGILYGVAPLNARGNLAVNALNNNTTQGQAMVVELILTFQLALCIFASTDSRRTSPVGSP
ALSIGLSVTLGHLVGIYFTGCSMNPARSFGPAVVMNRFSPAHWVFWVGPIVGAVLAAILYFYLLFPNSLSLSERVAIIKG
TYEPDEDWEEQREERKKTMELTTR
;
_struct_ref.pdbx_align_begin           2 
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 3D9S A 3 ? 266 ? P55064 2 ? 265 ? 2 265 
2 1 3D9S B 3 ? 266 ? P55064 2 ? 265 ? 2 265 
3 1 3D9S C 3 ? 266 ? P55064 2 ? 265 ? 2 265 
4 1 3D9S D 3 ? 266 ? P55064 2 ? 265 ? 2 265 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 3D9S MET A 1 ? UNP P55064 ? ? 'INITIATING METHIONINE' 0 1 
1 3D9S SER A 2 ? UNP P55064 ? ? 'EXPRESSION TAG'        1 2 
2 3D9S MET B 1 ? UNP P55064 ? ? 'INITIATING METHIONINE' 0 3 
2 3D9S SER B 2 ? UNP P55064 ? ? 'EXPRESSION TAG'        1 4 
3 3D9S MET C 1 ? UNP P55064 ? ? 'INITIATING METHIONINE' 0 5 
3 3D9S SER C 2 ? UNP P55064 ? ? 'EXPRESSION TAG'        1 6 
4 3D9S MET D 1 ? UNP P55064 ? ? 'INITIATING METHIONINE' 0 7 
4 3D9S SER D 2 ? UNP P55064 ? ? 'EXPRESSION TAG'        1 8 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                                      ? 
'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE                                                                                     ? 
'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                                   ? 
'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                              ? 
'C4 H7 N O4'      133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                                     ? 
'C3 H7 N O2 S'    121.158 
GLN 'L-peptide linking' y GLUTAMINE                                                                                    ? 
'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                              ? 
'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE                                                                                      ? 
'C2 H5 N O2'      75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                                    ? 
'C6 H10 N3 O2 1'  156.162 
HOH non-polymer         . WATER                                                                                        ? 'H2 O' 
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                                   ? 
'C6 H13 N O2'     131.173 
LEU 'L-peptide linking' y LEUCINE                                                                                      ? 
'C6 H13 N O2'     131.173 
LYS 'L-peptide linking' y LYSINE                                                                                       ? 
'C6 H15 N2 O2 1'  147.195 
MET 'L-peptide linking' y METHIONINE                                                                                   ? 
'C5 H11 N O2 S'   149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                                                ? 
'C9 H11 N O2'     165.189 
PRO 'L-peptide linking' y PROLINE                                                                                      ? 
'C5 H9 N O2'      115.130 
PS6 non-polymer         . 'O-[(S)-{[(2S)-2-(hexanoyloxy)-3-(tetradecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-D-serine' ? 
'C26 H50 N O10 P' 567.650 
SER 'L-peptide linking' y SERINE                                                                                       ? 
'C3 H7 N O3'      105.093 
THR 'L-peptide linking' y THREONINE                                                                                    ? 
'C4 H9 N O3'      119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                                   ? 
'C11 H12 N2 O2'   204.225 
TYR 'L-peptide linking' y TYROSINE                                                                                     ? 
'C9 H11 N O3'     181.189 
VAL 'L-peptide linking' y VALINE                                                                                       ? 
'C5 H11 N O2'     117.146 
# 
_exptl.entry_id          3D9S 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.15 
_exptl_crystal.density_percent_sol   61.0 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            281 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.6 
_exptl_crystal_grow.pdbx_details    
;19% polyethylene glycol 400, 0.1M Tris HCl pH 7.6, 0.1M NaCl, 6% v/v 1,6-hexanediol, 3% v/v 1,4-butanediol or 3% v/v 1,3-propanediol, VAPOR DIFFUSION, HANGING DROP, temperature 281K
;
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           170.0 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 4' 
_diffrn_detector.pdbx_collection_date   2007-07-02 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.931 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ESRF BEAMLINE ID14-3' 
_diffrn_source.pdbx_synchrotron_site       ESRF 
_diffrn_source.pdbx_synchrotron_beamline   ID14-3 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.931 
# 
_reflns.entry_id                     3D9S 
_reflns.observed_criterion_sigma_F   ? 
_reflns.observed_criterion_sigma_I   3.0 
_reflns.d_resolution_high            2.0 
_reflns.d_resolution_low             52.56 
_reflns.number_all                   84751 
_reflns.number_obs                   84751 
_reflns.percent_possible_obs         82.9 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.061 
_reflns.pdbx_netI_over_sigmaI        8.3 
_reflns.B_iso_Wilson_estimate        26.15 
_reflns.pdbx_redundancy              3.7 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             2.0 
_reflns_shell.d_res_low              2.11 
_reflns_shell.percent_possible_all   82.6 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        0.494 
_reflns_shell.meanI_over_sigI_obs    1.5 
_reflns_shell.pdbx_redundancy        3.7 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      12232 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 3D9S 
_refine.ls_number_reflns_obs                     79673 
_refine.ls_number_reflns_all                     84751 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          4.0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             10.00 
_refine.ls_d_res_high                            2.00 
_refine.ls_percent_reflns_obs                    78.0 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.162 
_refine.ls_R_factor_R_free                       0.193 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  4174 
_refine.ls_number_parameters                     29577 
_refine.ls_number_restraints                     30558 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               37.2 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R' 
_refine.pdbx_starting_model                      'PDB ENTRY 1J4N' 
_refine.details                                  
;Firstly, a homology model for AQP5 was generated using the SWISS-MODEL web server with the bovine AQP1 structure (PDB 1J4N) as a template. The homology model was then used as search model in molecular replacement calculations. See primary citation for additional details.; This data is merohedrally twinned; THE TWINNING OPERATOR IS (H,K,L) -> (k, h, -l) AND THE TWINNING FRACTION IS 0.463. Diffraction data was from a crystal with near-perfect pseudo-merohedral twinning with the twin operator(010 100 00-1)swapping the a and b axes.  Therefore, conventional programs/maps are not recommended when analysing this PDB and structure factors. ShelX (with BASF and TWIN values set) is useful for map calculation but the twinning compatible scripts are best for reliable omit maps (see Supporting Information of primary citation).
;
_refine.pdbx_method_to_determine_struct          'AB INITIO' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            
;THIN RESOLUTION SHELLS (RANDOMLY) TO ACCOUNT FOR TWINNING; TWIN RELATED REFLECTIONS ALWAYS IN THE SAME SET (WORK OR TEST SET) NOT DIVIDED BETWEEN THEM.
;
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        3D9S 
_refine_analyze.Luzzati_coordinate_error_obs    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      0 
_refine_analyze.occupancy_sum_hydrogen          0.00 
_refine_analyze.occupancy_sum_non_hydrogen      7386.58 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        7241 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         38 
_refine_hist.number_atoms_solvent             111 
_refine_hist.number_atoms_total               7390 
_refine_hist.d_res_high                       2.00 
_refine_hist.d_res_low                        10.00 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
s_bond_d               0.006  ? ? ? 'X-RAY DIFFRACTION' ? 
s_angle_d              0.024  ? ? ? 'X-RAY DIFFRACTION' ? 
s_similar_dist         0.000  ? ? ? 'X-RAY DIFFRACTION' ? 
s_from_restr_planes    0.0241 ? ? ? 'X-RAY DIFFRACTION' ? 
s_zero_chiral_vol      0.033  ? ? ? 'X-RAY DIFFRACTION' ? 
s_non_zero_chiral_vol  0.035  ? ? ? 'X-RAY DIFFRACTION' ? 
s_anti_bump_dis_restr  0.013  ? ? ? 'X-RAY DIFFRACTION' ? 
s_rigid_bond_adp_cmpnt 0.000  ? ? ? 'X-RAY DIFFRACTION' ? 
s_similar_adp_cmpnt    0.103  ? ? ? 'X-RAY DIFFRACTION' ? 
s_approx_iso_adps      0.000  ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   ? 
_refine_ls_shell.d_res_high                       2.0 
_refine_ls_shell.d_res_low                        2.11 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.R_factor_R_work                  0.162 
_refine_ls_shell.percent_reflns_obs               ? 
_refine_ls_shell.R_factor_R_free                  0.193 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             ? 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_pdbx_refine.entry_id                                    3D9S 
_pdbx_refine.R_factor_all_no_cutoff                      0.1619 
_pdbx_refine.R_factor_obs_no_cutoff                      ? 
_pdbx_refine.free_R_factor_no_cutoff                     ? 
_pdbx_refine.free_R_val_test_set_size_perc_no_cutoff     ? 
_pdbx_refine.free_R_val_test_set_ct_no_cutoff            ? 
_pdbx_refine.R_factor_all_4sig_cutoff                    0.1531 
_pdbx_refine.R_factor_obs_4sig_cutoff                    ? 
_pdbx_refine.free_R_factor_4sig_cutoff                   ? 
_pdbx_refine.free_R_val_test_set_size_perc_4sig_cutoff   ? 
_pdbx_refine.free_R_val_test_set_ct_4sig_cutoff          ? 
_pdbx_refine.number_reflns_obs_4sig_cutoff               66554 
_pdbx_refine.pdbx_refine_id                              'X-RAY DIFFRACTION' 
_pdbx_refine.free_R_error_no_cutoff                      ? 
# 
_struct.entry_id                  3D9S 
_struct.title                     'Human Aquaporin 5 (AQP5) - High Resolution X-ray Structure' 
_struct.pdbx_descriptor           Aquaporin-5 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3D9S 
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
_struct_keywords.text            
;Aquaporin, AQP, Aquaglyceroporin, membrane protein, water transport, lipid, Phosphatidylserine, PSF, NPA, ar/R, Water channel, Glycoprotein, Membrane, Transmembrane, Transport
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  SER A 2   ? CYS A 7   ? SER A 1   CYS A 6   1 ? 6  
HELX_P HELX_P2  2  SER A 8   ? LEU A 34  ? SER A 7   LEU A 33  1 ? 27 
HELX_P HELX_P3  3  THR A 42  ? GLY A 66  ? THR A 41  GLY A 65  1 ? 25 
HELX_P HELX_P4  4  ASN A 70  ? GLY A 80  ? ASN A 69  GLY A 79  1 ? 11 
HELX_P HELX_P5  5  SER A 84  ? ALA A 110 ? SER A 83  ALA A 109 1 ? 27 
HELX_P HELX_P6  6  PRO A 111 ? GLY A 116 ? PRO A 110 GLY A 115 1 ? 6  
HELX_P HELX_P7  7  THR A 128 ? ASP A 152 ? THR A 127 ASP A 151 1 ? 25 
HELX_P HELX_P8  8  SER A 161 ? GLY A 182 ? SER A 160 GLY A 181 1 ? 22 
HELX_P HELX_P9  9  ASN A 186 ? ASN A 198 ? ASN A 185 ASN A 197 1 ? 13 
HELX_P HELX_P10 10 ALA A 203 ? LEU A 225 ? ALA A 202 LEU A 224 1 ? 23 
HELX_P HELX_P11 11 ARG A 236 ? LYS A 241 ? ARG A 235 LYS A 240 1 ? 6  
HELX_P HELX_P12 12 SER B 2   ? CYS B 7   ? SER B 1   CYS B 6   1 ? 6  
HELX_P HELX_P13 13 SER B 8   ? SER B 32  ? SER B 7   SER B 31  1 ? 25 
HELX_P HELX_P14 14 THR B 42  ? GLY B 66  ? THR B 41  GLY B 65  1 ? 25 
HELX_P HELX_P15 15 ASN B 70  ? GLY B 80  ? ASN B 69  GLY B 79  1 ? 11 
HELX_P HELX_P16 16 SER B 84  ? ALA B 110 ? SER B 83  ALA B 109 1 ? 27 
HELX_P HELX_P17 17 PRO B 111 ? GLY B 116 ? PRO B 110 GLY B 115 1 ? 6  
HELX_P HELX_P18 18 THR B 128 ? THR B 151 ? THR B 127 THR B 150 1 ? 24 
HELX_P HELX_P19 19 SER B 161 ? GLY B 182 ? SER B 160 GLY B 181 1 ? 22 
HELX_P HELX_P20 20 ASN B 186 ? MET B 197 ? ASN B 185 MET B 196 1 ? 12 
HELX_P HELX_P21 21 TRP B 205 ? TYR B 224 ? TRP B 204 TYR B 223 1 ? 20 
HELX_P HELX_P22 22 SER B 232 ? GLY B 242 ? SER B 231 GLY B 241 1 ? 11 
HELX_P HELX_P23 23 SER C 8   ? LEU C 34  ? SER C 7   LEU C 33  1 ? 27 
HELX_P HELX_P24 24 THR C 42  ? GLY C 66  ? THR C 41  GLY C 65  1 ? 25 
HELX_P HELX_P25 25 ASN C 70  ? GLY C 80  ? ASN C 69  GLY C 79  1 ? 11 
HELX_P HELX_P26 26 SER C 84  ? GLY C 108 ? SER C 83  GLY C 107 1 ? 25 
HELX_P HELX_P27 27 PRO C 111 ? GLY C 116 ? PRO C 110 GLY C 115 1 ? 6  
HELX_P HELX_P28 28 THR C 128 ? THR C 151 ? THR C 127 THR C 150 1 ? 24 
HELX_P HELX_P29 29 SER C 161 ? ILE C 178 ? SER C 160 ILE C 177 1 ? 18 
HELX_P HELX_P30 30 ASN C 186 ? MET C 197 ? ASN C 185 MET C 196 1 ? 12 
HELX_P HELX_P31 31 TRP C 205 ? TYR C 224 ? TRP C 204 TYR C 223 1 ? 20 
HELX_P HELX_P32 32 SER C 232 ? LYS C 241 ? SER C 231 LYS C 240 1 ? 10 
HELX_P HELX_P33 33 SER D 2   ? CYS D 7   ? SER D 1   CYS D 6   1 ? 6  
HELX_P HELX_P34 34 SER D 8   ? LEU D 34  ? SER D 7   LEU D 33  1 ? 27 
HELX_P HELX_P35 35 THR D 42  ? GLY D 66  ? THR D 41  GLY D 65  1 ? 25 
HELX_P HELX_P36 36 ASN D 70  ? GLY D 80  ? ASN D 69  GLY D 79  1 ? 11 
HELX_P HELX_P37 37 SER D 84  ? ALA D 110 ? SER D 83  ALA D 109 1 ? 27 
HELX_P HELX_P38 38 PRO D 111 ? GLY D 116 ? PRO D 110 GLY D 115 1 ? 6  
HELX_P HELX_P39 39 THR D 128 ? ASP D 152 ? THR D 127 ASP D 151 1 ? 25 
HELX_P HELX_P40 40 SER D 161 ? GLY D 182 ? SER D 160 GLY D 181 1 ? 22 
HELX_P HELX_P41 41 ASN D 186 ? VAL D 195 ? ASN D 185 VAL D 194 1 ? 10 
HELX_P HELX_P42 42 TRP D 205 ? LEU D 225 ? TRP D 204 LEU D 224 1 ? 21 
HELX_P HELX_P43 43 SER D 232 ? GLY D 242 ? SER D 231 GLY D 241 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
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 GLY 116 A . ? GLY 115 A ASN 117 A ? ASN 116 A 1 4.49  
2 LEU 231 A . ? LEU 230 A SER 232 A ? SER 231 A 1 6.36  
3 SER 232 A . ? SER 231 A LEU 233 A ? LEU 232 A 1 -3.31 
4 ASN 117 C . ? ASN 116 C LEU 118 C ? LEU 117 C 1 22.91 
5 GLU 245 C . ? GLU 244 C PRO 246 C ? PRO 245 C 1 -0.99 
# 
_struct_site.id                   AC1 
_struct_site.pdbx_evidence_code   Software 
_struct_site.pdbx_auth_asym_id    ? 
_struct_site.pdbx_auth_comp_id    ? 
_struct_site.pdbx_auth_seq_id     ? 
_struct_site.pdbx_auth_ins_code   ? 
_struct_site.pdbx_num_residues    16 
_struct_site.details              'BINDING SITE FOR RESIDUE PS6 D 266' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 16 LEU A 48  ? LEU A 47  . ? 1_555 ? 
2  AC1 16 GLY A 160 ? GLY A 159 . ? 1_555 ? 
3  AC1 16 LEU A 164 ? LEU A 163 . ? 1_555 ? 
4  AC1 16 LEU B 48  ? LEU B 47  . ? 1_555 ? 
5  AC1 16 GLY B 160 ? GLY B 159 . ? 1_555 ? 
6  AC1 16 PRO C 158 ? PRO C 157 . ? 1_555 ? 
7  AC1 16 VAL C 159 ? VAL C 158 . ? 1_555 ? 
8  AC1 16 GLY C 160 ? GLY C 159 . ? 1_555 ? 
9  AC1 16 SER C 161 ? SER C 160 . ? 1_555 ? 
10 AC1 16 LEU C 164 ? LEU C 163 . ? 1_555 ? 
11 AC1 16 SER D 157 ? SER D 156 . ? 1_555 ? 
12 AC1 16 PRO D 158 ? PRO D 157 . ? 1_555 ? 
13 AC1 16 VAL D 159 ? VAL D 158 . ? 1_555 ? 
14 AC1 16 GLY D 160 ? GLY D 159 . ? 1_555 ? 
15 AC1 16 SER D 161 ? SER D 160 . ? 1_555 ? 
16 AC1 16 LEU D 164 ? LEU D 163 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          3D9S 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.000000 
_database_PDB_matrix.origx_vector[2]   0.000000 
_database_PDB_matrix.origx_vector[3]   0.000000 
# 
_atom_sites.entry_id                    3D9S 
_atom_sites.fract_transf_matrix[1][1]   0.011053 
_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]   0.011032 
_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]   0.005423 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . SER A 1 2   ? -8.880  -20.923 7.115  1.00 79.60  ? 1   SER A N   1 
ATOM   2    C CA  . SER A 1 2   ? -8.340  -21.408 5.850  1.00 71.04  ? 1   SER A CA  1 
ATOM   3    C C   . SER A 1 2   ? -7.471  -22.645 6.024  1.00 72.78  ? 1   SER A C   1 
ATOM   4    O O   . SER A 1 2   ? -6.499  -22.624 6.780  0.75 31.51  ? 1   SER A O   1 
ATOM   5    C CB  . SER A 1 2   ? -7.513  -20.307 5.166  1.00 68.80  ? 1   SER A CB  1 
ATOM   6    O OG  . SER A 1 2   ? -6.630  -20.868 4.212  1.00 73.73  ? 1   SER A OG  1 
ATOM   7    N N   . LYS A 1 3   ? -7.807  -23.722 5.306  1.00 80.78  ? 2   LYS A N   1 
ATOM   8    C CA  . LYS A 1 3   ? -6.954  -24.906 5.269  1.00 82.59  ? 2   LYS A CA  1 
ATOM   9    C C   . LYS A 1 3   ? -5.668  -24.574 4.515  1.00 76.54  ? 2   LYS A C   1 
ATOM   10   O O   . LYS A 1 3   ? -4.642  -25.229 4.616  1.00 68.05  ? 2   LYS A O   1 
ATOM   11   C CB  . LYS A 1 3   ? -7.645  -26.097 4.608  1.00 94.27  ? 2   LYS A CB  1 
ATOM   12   C CG  . LYS A 1 3   ? -6.788  -27.345 4.530  1.00 98.66  ? 2   LYS A CG  1 
ATOM   13   C CD  . LYS A 1 3   ? -6.146  -27.542 3.167  1.00 91.82  ? 2   LYS A CD  1 
ATOM   14   C CE  . LYS A 1 3   ? -4.803  -28.264 3.265  1.00 81.72  ? 2   LYS A CE  1 
ATOM   15   N NZ  . LYS A 1 3   ? -3.768  -27.643 2.425  1.00 67.31  ? 2   LYS A NZ  1 
ATOM   16   N N   . LYS A 1 4   ? -5.765  -23.513 3.723  1.00 76.11  ? 3   LYS A N   1 
ATOM   17   C CA  . LYS A 1 4   ? -4.594  -23.028 3.007  1.00 79.93  ? 3   LYS A CA  1 
ATOM   18   C C   . LYS A 1 4   ? -3.484  -22.766 4.012  1.00 68.05  ? 3   LYS A C   1 
ATOM   19   O O   . LYS A 1 4   ? -2.341  -23.206 3.847  0.29 64.94  ? 3   LYS A O   1 
ATOM   20   C CB  . LYS A 1 4   ? -4.942  -21.792 2.178  1.00 92.32  ? 3   LYS A CB  1 
ATOM   21   C CG  . LYS A 1 4   ? -4.380  -20.450 2.650  1.00 101.85 ? 3   LYS A CG  1 
ATOM   22   C CD  . LYS A 1 4   ? -2.964  -20.191 2.167  1.00 108.17 ? 3   LYS A CD  1 
ATOM   23   C CE  . LYS A 1 4   ? -2.995  -19.942 0.652  1.00 114.50 ? 3   LYS A CE  1 
ATOM   24   N NZ  . LYS A 1 4   ? -2.466  -21.122 -0.101 1.00 116.43 ? 3   LYS A NZ  1 
ATOM   25   N N   . GLU A 1 5   ? -3.810  -22.038 5.092  1.00 59.75  ? 4   GLU A N   1 
ATOM   26   C CA  . GLU A 1 5   ? -2.688  -21.719 5.970  1.00 47.87  ? 4   GLU A CA  1 
ATOM   27   C C   . GLU A 1 5   ? -2.715  -22.551 7.232  1.00 43.57  ? 4   GLU A C   1 
ATOM   28   O O   . GLU A 1 5   ? -1.636  -22.839 7.762  1.00 55.19  ? 4   GLU A O   1 
ATOM   29   C CB  . GLU A 1 5   ? -2.656  -20.237 6.337  1.00 60.09  ? 4   GLU A CB  1 
ATOM   30   C CG  . GLU A 1 5   ? -4.010  -19.570 6.456  1.00 61.03  ? 4   GLU A CG  1 
ATOM   31   C CD  . GLU A 1 5   ? -4.010  -18.492 7.526  1.00 57.00  ? 4   GLU A CD  1 
ATOM   32   O OE1 . GLU A 1 5   ? -5.042  -18.328 8.213  1.00 62.02  ? 4   GLU A OE1 1 
ATOM   33   O OE2 . GLU A 1 5   ? -2.986  -17.803 7.691  1.00 38.88  ? 4   GLU A OE2 1 
ATOM   34   N N   . VAL A 1 6   ? -3.882  -22.932 7.751  1.00 42.36  ? 5   VAL A N   1 
ATOM   35   C CA  . VAL A 1 6   ? -3.787  -23.556 9.077  1.00 51.59  ? 5   VAL A CA  1 
ATOM   36   C C   . VAL A 1 6   ? -3.076  -24.902 8.984  1.00 60.35  ? 5   VAL A C   1 
ATOM   37   O O   . VAL A 1 6   ? -2.511  -25.391 9.963  1.00 85.68  ? 5   VAL A O   1 
ATOM   38   C CB  . VAL A 1 6   ? -5.147  -23.755 9.764  1.00 61.86  ? 5   VAL A CB  1 
ATOM   39   C CG1 . VAL A 1 6   ? -4.992  -24.622 11.009 1.00 60.87  ? 5   VAL A CG1 1 
ATOM   40   C CG2 . VAL A 1 6   ? -5.767  -22.410 10.110 1.00 67.14  ? 5   VAL A CG2 1 
ATOM   41   N N   . CYS A 1 7   ? -3.117  -25.468 7.781  1.00 61.36  ? 6   CYS A N   1 
ATOM   42   C CA  . CYS A 1 7   ? -2.481  -26.767 7.573  1.00 62.24  ? 6   CYS A CA  1 
ATOM   43   C C   . CYS A 1 7   ? -1.055  -26.599 7.078  1.00 61.65  ? 6   CYS A C   1 
ATOM   44   O O   . CYS A 1 7   ? -0.365  -27.576 6.773  1.00 72.25  ? 6   CYS A O   1 
ATOM   45   C CB  . CYS A 1 7   ? -3.335  -27.610 6.617  1.00 61.24  ? 6   CYS A CB  1 
ATOM   46   S SG  . CYS A 1 7   ? -4.771  -28.375 7.426  1.00 60.41  ? 6   CYS A SG  1 
ATOM   47   N N   . SER A 1 8   ? -0.572  -25.356 6.989  1.00 63.50  ? 7   SER A N   1 
ATOM   48   C CA  . SER A 1 8   ? 0.804   -25.188 6.520  1.00 60.86  ? 7   SER A CA  1 
ATOM   49   C C   . SER A 1 8   ? 1.769   -25.586 7.645  1.00 55.13  ? 7   SER A C   1 
ATOM   50   O O   . SER A 1 8   ? 1.357   -25.552 8.810  1.00 42.54  ? 7   SER A O   1 
ATOM   51   C CB  . SER A 1 8   ? 1.128   -23.782 6.040  1.00 64.69  ? 7   SER A CB  1 
ATOM   52   O OG  . SER A 1 8   ? 0.166   -22.803 6.371  1.00 74.17  ? 7   SER A OG  1 
ATOM   53   N N   . VAL A 1 9   ? 2.981   -25.927 7.223  1.00 40.67  ? 8   VAL A N   1 
ATOM   54   C CA  . VAL A 1 9   ? 4.081   -26.259 8.103  1.00 41.24  ? 8   VAL A CA  1 
ATOM   55   C C   . VAL A 1 9   ? 4.632   -25.007 8.781  1.00 42.68  ? 8   VAL A C   1 
ATOM   56   O O   . VAL A 1 9   ? 5.245   -25.056 9.842  1.00 67.56  ? 8   VAL A O   1 
ATOM   57   C CB  . VAL A 1 9   ? 5.257   -26.923 7.368  1.00 53.55  ? 8   VAL A CB  1 
ATOM   58   C CG1 . VAL A 1 9   ? 6.159   -25.868 6.753  1.00 52.88  ? 8   VAL A CG1 1 
ATOM   59   C CG2 . VAL A 1 9   ? 6.018   -27.803 8.348  1.00 79.42  ? 8   VAL A CG2 1 
ATOM   60   N N   . ALA A 1 10  ? 4.407   -23.867 8.131  1.00 46.16  ? 9   ALA A N   1 
ATOM   61   C CA  . ALA A 1 10  ? 4.820   -22.607 8.742  1.00 47.30  ? 9   ALA A CA  1 
ATOM   62   C C   . ALA A 1 10  ? 3.803   -22.176 9.800  1.00 42.30  ? 9   ALA A C   1 
ATOM   63   O O   . ALA A 1 10  ? 4.226   -21.826 10.906 1.00 38.79  ? 9   ALA A O   1 
ATOM   64   C CB  . ALA A 1 10  ? 5.035   -21.556 7.672  1.00 36.20  ? 9   ALA A CB  1 
ATOM   65   N N   . PHE A 1 11  ? 2.511   -22.210 9.500  1.00 32.40  ? 10  PHE A N   1 
ATOM   66   C CA  . PHE A 1 11  ? 1.477   -21.934 10.491 1.00 32.74  ? 10  PHE A CA  1 
ATOM   67   C C   . PHE A 1 11  ? 1.731   -22.746 11.755 1.00 37.98  ? 10  PHE A C   1 
ATOM   68   O O   . PHE A 1 11  ? 1.749   -22.288 12.892 1.00 36.10  ? 10  PHE A O   1 
ATOM   69   C CB  . PHE A 1 11  ? 0.103   -22.284 9.937  1.00 38.85  ? 10  PHE A CB  1 
ATOM   70   C CG  . PHE A 1 11  ? -1.074  -21.908 10.822 1.00 31.15  ? 10  PHE A CG  1 
ATOM   71   C CD1 . PHE A 1 11  ? -1.666  -20.664 10.698 1.00 27.52  ? 10  PHE A CD1 1 
ATOM   72   C CD2 . PHE A 1 11  ? -1.582  -22.785 11.756 1.00 29.83  ? 10  PHE A CD2 1 
ATOM   73   C CE1 . PHE A 1 11  ? -2.742  -20.309 11.483 1.00 27.03  ? 10  PHE A CE1 1 
ATOM   74   C CE2 . PHE A 1 11  ? -2.657  -22.441 12.555 1.00 31.48  ? 10  PHE A CE2 1 
ATOM   75   C CZ  . PHE A 1 11  ? -3.238  -21.197 12.419 1.00 32.03  ? 10  PHE A CZ  1 
ATOM   76   N N   . LEU A 1 12  ? 1.954   -24.028 11.487 1.00 40.02  ? 11  LEU A N   1 
ATOM   77   C CA  . LEU A 1 12  ? 2.441   -24.958 12.487 1.00 39.50  ? 11  LEU A CA  1 
ATOM   78   C C   . LEU A 1 12  ? 3.597   -24.355 13.276 1.00 35.90  ? 11  LEU A C   1 
ATOM   79   O O   . LEU A 1 12  ? 3.544   -24.265 14.492 1.00 29.20  ? 11  LEU A O   1 
ATOM   80   C CB  . LEU A 1 12  ? 2.911   -26.245 11.795 1.00 39.87  ? 11  LEU A CB  1 
ATOM   81   C CG  . LEU A 1 12  ? 3.559   -27.263 12.734 1.00 45.36  ? 11  LEU A CG  1 
ATOM   82   C CD1 . LEU A 1 12  ? 2.565   -27.656 13.815 1.00 44.34  ? 11  LEU A CD1 1 
ATOM   83   C CD2 . LEU A 1 12  ? 4.053   -28.468 11.956 1.00 63.37  ? 11  LEU A CD2 1 
ATOM   84   N N   . LYS A 1 13  ? 4.667   -23.945 12.591 1.00 31.02  ? 12  LYS A N   1 
ATOM   85   C CA  . LYS A 1 13  ? 5.831   -23.421 13.282 1.00 31.30  ? 12  LYS A CA  1 
ATOM   86   C C   . LYS A 1 13  ? 5.499   -22.157 14.066 1.00 37.12  ? 12  LYS A C   1 
ATOM   87   O O   . LYS A 1 13  ? 6.109   -21.825 15.077 1.00 39.41  ? 12  LYS A O   1 
ATOM   88   C CB  . LYS A 1 13  ? 6.942   -23.097 12.289 1.00 23.07  ? 12  LYS A CB  1 
ATOM   89   C CG  . LYS A 1 13  ? 7.661   -24.323 11.736 1.00 25.53  ? 12  LYS A CG  1 
ATOM   90   C CD  . LYS A 1 13  ? 8.367   -23.965 10.441 1.00 26.91  ? 12  LYS A CD  1 
ATOM   91   C CE  . LYS A 1 13  ? 9.468   -24.943 10.085 1.00 46.71  ? 12  LYS A CE  1 
ATOM   92   N NZ  . LYS A 1 13  ? 10.238  -24.517 8.876  1.00 39.32  ? 12  LYS A NZ  1 
ATOM   93   N N   . ALA A 1 14  ? 4.517   -21.410 13.576 1.00 36.36  ? 13  ALA A N   1 
ATOM   94   C CA  . ALA A 1 14  ? 4.269   -20.092 14.132 1.00 28.88  ? 13  ALA A CA  1 
ATOM   95   C C   . ALA A 1 14  ? 3.391   -20.251 15.360 1.00 32.08  ? 13  ALA A C   1 
ATOM   96   O O   . ALA A 1 14  ? 3.581   -19.612 16.383 1.00 31.23  ? 13  ALA A O   1 
ATOM   97   C CB  . ALA A 1 14  ? 3.581   -19.168 13.152 1.00 28.28  ? 13  ALA A CB  1 
ATOM   98   N N   . VAL A 1 15  ? 2.431   -21.151 15.158 1.00 23.16  ? 14  VAL A N   1 
ATOM   99   C CA  . VAL A 1 15  ? 1.531   -21.397 16.289 1.00 31.04  ? 14  VAL A CA  1 
ATOM   100  C C   . VAL A 1 15  ? 2.362   -21.891 17.457 1.00 42.75  ? 14  VAL A C   1 
ATOM   101  O O   . VAL A 1 15  ? 2.154   -21.534 18.620 1.00 31.92  ? 14  VAL A O   1 
ATOM   102  C CB  . VAL A 1 15  ? 0.431   -22.336 15.788 1.00 32.64  ? 14  VAL A CB  1 
ATOM   103  C CG1 . VAL A 1 15  ? -0.521  -22.761 16.881 1.00 32.98  ? 14  VAL A CG1 1 
ATOM   104  C CG2 . VAL A 1 15  ? -0.299  -21.566 14.688 1.00 27.34  ? 14  VAL A CG2 1 
ATOM   105  N N   . PHE A 1 16  ? 3.358   -22.703 17.118 1.00 37.48  ? 15  PHE A N   1 
ATOM   106  C CA  . PHE A 1 16  ? 4.252   -23.303 18.091 1.00 30.96  ? 15  PHE A CA  1 
ATOM   107  C C   . PHE A 1 16  ? 5.221   -22.297 18.704 1.00 25.05  ? 15  PHE A C   1 
ATOM   108  O O   . PHE A 1 16  ? 5.458   -22.356 19.917 1.00 38.11  ? 15  PHE A O   1 
ATOM   109  C CB  . PHE A 1 16  ? 5.042   -24.451 17.444 1.00 29.75  ? 15  PHE A CB  1 
ATOM   110  C CG  . PHE A 1 16  ? 6.269   -24.821 18.255 1.00 31.27  ? 15  PHE A CG  1 
ATOM   111  C CD1 . PHE A 1 16  ? 6.125   -25.523 19.435 1.00 27.39  ? 15  PHE A CD1 1 
ATOM   112  C CD2 . PHE A 1 16  ? 7.540   -24.468 17.838 1.00 42.73  ? 15  PHE A CD2 1 
ATOM   113  C CE1 . PHE A 1 16  ? 7.234   -25.857 20.184 1.00 36.19  ? 15  PHE A CE1 1 
ATOM   114  C CE2 . PHE A 1 16  ? 8.648   -24.795 18.602 1.00 40.55  ? 15  PHE A CE2 1 
ATOM   115  C CZ  . PHE A 1 16  ? 8.503   -25.493 19.781 1.00 33.12  ? 15  PHE A CZ  1 
ATOM   116  N N   . ALA A 1 17  ? 5.808   -21.408 17.915 1.00 25.17  ? 16  ALA A N   1 
ATOM   117  C CA  . ALA A 1 17  ? 6.703   -20.378 18.451 1.00 30.45  ? 16  ALA A CA  1 
ATOM   118  C C   . ALA A 1 17  ? 5.975   -19.505 19.474 1.00 33.48  ? 16  ALA A C   1 
ATOM   119  O O   . ALA A 1 17  ? 6.428   -19.170 20.560 1.00 31.77  ? 16  ALA A O   1 
ATOM   120  C CB  . ALA A 1 17  ? 7.256   -19.530 17.323 1.00 31.65  ? 16  ALA A CB  1 
ATOM   121  N N   . GLU A 1 18  ? 4.761   -19.105 19.127 1.00 36.79  ? 17  GLU A N   1 
ATOM   122  C CA  . GLU A 1 18  ? 3.890   -18.332 20.005 1.00 37.90  ? 17  GLU A CA  1 
ATOM   123  C C   . GLU A 1 18  ? 3.741   -19.014 21.359 1.00 35.66  ? 17  GLU A C   1 
ATOM   124  O O   . GLU A 1 18  ? 3.692   -18.363 22.400 1.00 29.66  ? 17  GLU A O   1 
ATOM   125  C CB  . GLU A 1 18  ? 2.542   -18.179 19.306 1.00 43.45  ? 17  GLU A CB  1 
ATOM   126  C CG  . GLU A 1 18  ? 1.780   -16.904 19.489 1.00 44.98  ? 17  GLU A CG  1 
ATOM   127  C CD  . GLU A 1 18  ? 2.379   -15.644 18.920 1.00 44.74  ? 17  GLU A CD  1 
ATOM   128  O OE1 . GLU A 1 18  ? 1.857   -14.582 19.339 1.00 47.95  ? 17  GLU A OE1 1 
ATOM   129  O OE2 . GLU A 1 18  ? 3.313   -15.665 18.093 1.00 42.21  ? 17  GLU A OE2 1 
ATOM   130  N N   . PHE A 1 19  ? 3.651   -20.336 21.339 1.00 31.08  ? 18  PHE A N   1 
ATOM   131  C CA  . PHE A 1 19  ? 3.566   -21.161 22.531 1.00 30.92  ? 18  PHE A CA  1 
ATOM   132  C C   . PHE A 1 19  ? 4.897   -21.083 23.269 1.00 24.85  ? 18  PHE A C   1 
ATOM   133  O O   . PHE A 1 19  ? 5.002   -20.921 24.475 1.00 25.59  ? 18  PHE A O   1 
ATOM   134  C CB  . PHE A 1 19  ? 3.248   -22.619 22.183 1.00 30.16  ? 18  PHE A CB  1 
ATOM   135  C CG  . PHE A 1 19  ? 3.697   -23.632 23.230 1.00 31.47  ? 18  PHE A CG  1 
ATOM   136  C CD1 . PHE A 1 19  ? 2.919   -23.834 24.364 1.00 33.43  ? 18  PHE A CD1 1 
ATOM   137  C CD2 . PHE A 1 19  ? 4.861   -24.365 23.089 1.00 25.39  ? 18  PHE A CD2 1 
ATOM   138  C CE1 . PHE A 1 19  ? 3.316   -24.746 25.320 1.00 30.11  ? 18  PHE A CE1 1 
ATOM   139  C CE2 . PHE A 1 19  ? 5.281   -25.262 24.041 1.00 27.77  ? 18  PHE A CE2 1 
ATOM   140  C CZ  . PHE A 1 19  ? 4.499   -25.451 25.171 1.00 31.42  ? 18  PHE A CZ  1 
ATOM   141  N N   . LEU A 1 20  ? 5.965   -21.232 22.486 1.00 24.08  ? 19  LEU A N   1 
ATOM   142  C CA  . LEU A 1 20  ? 7.281   -21.319 23.114 1.00 17.80  ? 19  LEU A CA  1 
ATOM   143  C C   . LEU A 1 20  ? 7.644   -19.972 23.710 1.00 25.62  ? 19  LEU A C   1 
ATOM   144  O O   . LEU A 1 20  ? 8.141   -19.837 24.822 1.00 28.59  ? 19  LEU A O   1 
ATOM   145  C CB  . LEU A 1 20  ? 8.274   -21.790 22.052 1.00 17.95  ? 19  LEU A CB  1 
ATOM   146  C CG  . LEU A 1 20  ? 9.722   -21.954 22.508 1.00 24.35  ? 19  LEU A CG  1 
ATOM   147  C CD1 . LEU A 1 20  ? 9.913   -23.309 23.172 1.00 46.82  ? 19  LEU A CD1 1 
ATOM   148  C CD2 . LEU A 1 20  ? 10.691  -21.768 21.340 1.00 25.75  ? 19  LEU A CD2 1 
ATOM   149  N N   . ALA A 1 21  ? 7.372   -18.913 22.952 1.00 21.47  ? 20  ALA A N   1 
ATOM   150  C CA  . ALA A 1 21  ? 7.701   -17.569 23.392 1.00 16.98  ? 20  ALA A CA  1 
ATOM   151  C C   . ALA A 1 21  ? 6.923   -17.172 24.641 1.00 20.47  ? 20  ALA A C   1 
ATOM   152  O O   . ALA A 1 21  ? 7.521   -16.646 25.582 1.00 20.96  ? 20  ALA A O   1 
ATOM   153  C CB  . ALA A 1 21  ? 7.430   -16.599 22.245 1.00 16.73  ? 20  ALA A CB  1 
ATOM   154  N N   . THR A 1 22  ? 5.604   -17.395 24.659 1.00 25.61  ? 21  THR A N   1 
ATOM   155  C CA  . THR A 1 22  ? 4.776   -17.051 25.823 1.00 19.68  ? 21  THR A CA  1 
ATOM   156  C C   . THR A 1 22  ? 5.280   -17.812 27.047 1.00 17.62  ? 21  THR A C   1 
ATOM   157  O O   . THR A 1 22  ? 5.480   -17.231 28.111 1.00 21.07  ? 21  THR A O   1 
ATOM   158  C CB  . THR A 1 22  ? 3.287   -17.349 25.624 1.00 16.94  ? 21  THR A CB  1 
ATOM   159  O OG1 . THR A 1 22  ? 2.871   -16.858 24.347 1.00 27.81  ? 21  THR A OG1 1 
ATOM   160  C CG2 . THR A 1 22  ? 2.408   -16.600 26.632 1.00 18.81  ? 21  THR A CG2 1 
ATOM   161  N N   . LEU A 1 23  ? 5.506   -19.114 26.881 1.00 16.79  ? 22  LEU A N   1 
ATOM   162  C CA  . LEU A 1 23  ? 6.105   -19.945 27.927 1.00 24.79  ? 22  LEU A CA  1 
ATOM   163  C C   . LEU A 1 23  ? 7.337   -19.284 28.520 1.00 26.17  ? 22  LEU A C   1 
ATOM   164  O O   . LEU A 1 23  ? 7.475   -19.009 29.709 1.00 26.02  ? 22  LEU A O   1 
ATOM   165  C CB  . LEU A 1 23  ? 6.477   -21.320 27.360 1.00 26.32  ? 22  LEU A CB  1 
ATOM   166  C CG  . LEU A 1 23  ? 6.851   -22.438 28.324 1.00 30.77  ? 22  LEU A CG  1 
ATOM   167  C CD1 . LEU A 1 23  ? 6.500   -23.812 27.755 1.00 26.50  ? 22  LEU A CD1 1 
ATOM   168  C CD2 . LEU A 1 23  ? 8.334   -22.414 28.667 1.00 26.14  ? 22  LEU A CD2 1 
ATOM   169  N N   . ILE A 1 24  ? 8.325   -19.039 27.649 1.00 24.11  ? 23  ILE A N   1 
ATOM   170  C CA  . ILE A 1 24  ? 9.556   -18.470 28.171 1.00 14.40  ? 23  ILE A CA  1 
ATOM   171  C C   . ILE A 1 24  ? 9.301   -17.108 28.784 1.00 15.90  ? 23  ILE A C   1 
ATOM   172  O O   . ILE A 1 24  ? 9.936   -16.778 29.779 1.00 17.39  ? 23  ILE A O   1 
ATOM   173  C CB  . ILE A 1 24  ? 10.620  -18.314 27.074 1.00 19.04  ? 23  ILE A CB  1 
ATOM   174  C CG1 . ILE A 1 24  ? 11.098  -19.650 26.525 1.00 17.73  ? 23  ILE A CG1 1 
ATOM   175  C CG2 . ILE A 1 24  ? 11.758  -17.472 27.637 1.00 23.24  ? 23  ILE A CG2 1 
ATOM   176  C CD1 . ILE A 1 24  ? 11.501  -19.617 25.061 1.00 35.70  ? 23  ILE A CD1 1 
ATOM   177  N N   . PHE A 1 25  ? 8.384   -16.362 28.161 1.00 17.05  ? 24  PHE A N   1 
ATOM   178  C CA  . PHE A 1 25  ? 8.151   -15.011 28.687 1.00 21.00  ? 24  PHE A CA  1 
ATOM   179  C C   . PHE A 1 25  ? 7.501   -15.019 30.070 1.00 37.71  ? 24  PHE A C   1 
ATOM   180  O O   . PHE A 1 25  ? 7.750   -14.138 30.903 1.00 32.51  ? 24  PHE A O   1 
ATOM   181  C CB  . PHE A 1 25  ? 7.277   -14.235 27.707 1.00 19.73  ? 24  PHE A CB  1 
ATOM   182  C CG  . PHE A 1 25  ? 6.641   -13.006 28.340 1.00 25.33  ? 24  PHE A CG  1 
ATOM   183  C CD1 . PHE A 1 25  ? 7.436   -11.968 28.787 1.00 22.00  ? 24  PHE A CD1 1 
ATOM   184  C CD2 . PHE A 1 25  ? 5.264   -12.937 28.470 1.00 25.98  ? 24  PHE A CD2 1 
ATOM   185  C CE1 . PHE A 1 25  ? 6.855   -10.858 29.370 1.00 20.44  ? 24  PHE A CE1 1 
ATOM   186  C CE2 . PHE A 1 25  ? 4.681   -11.825 29.045 1.00 23.85  ? 24  PHE A CE2 1 
ATOM   187  C CZ  . PHE A 1 25  ? 5.477   -10.792 29.483 1.00 22.48  ? 24  PHE A CZ  1 
ATOM   188  N N   . VAL A 1 26  ? 6.638   -15.994 30.359 1.00 31.10  ? 25  VAL A N   1 
ATOM   189  C CA  . VAL A 1 26  ? 5.949   -16.062 31.646 1.00 26.15  ? 25  VAL A CA  1 
ATOM   190  C C   . VAL A 1 26  ? 6.889   -16.599 32.714 1.00 23.37  ? 25  VAL A C   1 
ATOM   191  O O   . VAL A 1 26  ? 6.933   -16.090 33.837 1.00 26.48  ? 25  VAL A O   1 
ATOM   192  C CB  . VAL A 1 26  ? 4.691   -16.950 31.572 1.00 26.17  ? 25  VAL A CB  1 
ATOM   193  C CG1 . VAL A 1 26  ? 4.252   -17.372 32.966 1.00 19.73  ? 25  VAL A CG1 1 
ATOM   194  C CG2 . VAL A 1 26  ? 3.587   -16.216 30.826 1.00 28.08  ? 25  VAL A CG2 1 
ATOM   195  N N   . PHE A 1 27  ? 7.652   -17.624 32.322 1.00 30.49  ? 26  PHE A N   1 
ATOM   196  C CA  . PHE A 1 27  ? 8.727   -18.136 33.164 1.00 22.72  ? 26  PHE A CA  1 
ATOM   197  C C   . PHE A 1 27  ? 9.578   -16.992 33.714 1.00 28.54  ? 26  PHE A C   1 
ATOM   198  O O   . PHE A 1 27  ? 9.823   -16.884 34.915 1.00 20.73  ? 26  PHE A O   1 
ATOM   199  C CB  . PHE A 1 27  ? 9.636   -19.098 32.394 1.00 23.81  ? 26  PHE A CB  1 
ATOM   200  C CG  . PHE A 1 27  ? 10.820  -19.585 33.216 1.00 27.81  ? 26  PHE A CG  1 
ATOM   201  C CD1 . PHE A 1 27  ? 10.619  -20.622 34.122 1.00 27.58  ? 26  PHE A CD1 1 
ATOM   202  C CD2 . PHE A 1 27  ? 12.084  -19.034 33.090 1.00 22.40  ? 26  PHE A CD2 1 
ATOM   203  C CE1 . PHE A 1 27  ? 11.651  -21.098 34.904 1.00 22.64  ? 26  PHE A CE1 1 
ATOM   204  C CE2 . PHE A 1 27  ? 13.120  -19.495 33.892 1.00 20.68  ? 26  PHE A CE2 1 
ATOM   205  C CZ  . PHE A 1 27  ? 12.900  -20.518 34.796 1.00 20.27  ? 26  PHE A CZ  1 
ATOM   206  N N   . PHE A 1 28  ? 10.043  -16.148 32.788 1.00 29.67  ? 27  PHE A N   1 
ATOM   207  C CA  . PHE A 1 28  ? 10.956  -15.059 33.131 1.00 28.88  ? 27  PHE A CA  1 
ATOM   208  C C   . PHE A 1 28  ? 10.260  -13.913 33.858 1.00 24.66  ? 27  PHE A C   1 
ATOM   209  O O   . PHE A 1 28  ? 10.797  -13.438 34.858 1.00 26.58  ? 27  PHE A O   1 
ATOM   210  C CB  . PHE A 1 28  ? 11.665  -14.530 31.869 1.00 22.67  ? 27  PHE A CB  1 
ATOM   211  C CG  . PHE A 1 28  ? 13.058  -15.107 31.657 1.00 19.49  ? 27  PHE A CG  1 
ATOM   212  C CD1 . PHE A 1 28  ? 14.170  -14.550 32.244 1.00 17.74  ? 27  PHE A CD1 1 
ATOM   213  C CD2 . PHE A 1 28  ? 13.234  -16.223 30.853 1.00 26.80  ? 27  PHE A CD2 1 
ATOM   214  C CE1 . PHE A 1 28  ? 15.437  -15.072 32.068 1.00 18.68  ? 27  PHE A CE1 1 
ATOM   215  C CE2 . PHE A 1 28  ? 14.498  -16.757 30.676 1.00 25.51  ? 27  PHE A CE2 1 
ATOM   216  C CZ  . PHE A 1 28  ? 15.609  -16.193 31.277 1.00 14.63  ? 27  PHE A CZ  1 
ATOM   217  N N   . GLY A 1 29  ? 9.104   -13.426 33.402 1.00 16.84  ? 28  GLY A N   1 
ATOM   218  C CA  . GLY A 1 29  ? 8.460   -12.307 34.099 1.00 20.70  ? 28  GLY A CA  1 
ATOM   219  C C   . GLY A 1 29  ? 8.079   -12.714 35.512 1.00 23.90  ? 28  GLY A C   1 
ATOM   220  O O   . GLY A 1 29  ? 8.459   -12.054 36.476 1.00 18.72  ? 28  GLY A O   1 
ATOM   221  N N   . LEU A 1 30  ? 7.320   -13.797 35.627 1.00 24.11  ? 29  LEU A N   1 
ATOM   222  C CA  . LEU A 1 30  ? 6.970   -14.306 36.956 1.00 28.61  ? 29  LEU A CA  1 
ATOM   223  C C   . LEU A 1 30  ? 8.220   -14.548 37.778 1.00 19.44  ? 29  LEU A C   1 
ATOM   224  O O   . LEU A 1 30  ? 8.413   -14.117 38.911 1.00 18.65  ? 29  LEU A O   1 
ATOM   225  C CB  . LEU A 1 30  ? 6.159   -15.596 36.815 1.00 24.56  ? 29  LEU A CB  1 
ATOM   226  C CG  . LEU A 1 30  ? 4.926   -15.530 35.917 1.00 26.28  ? 29  LEU A CG  1 
ATOM   227  C CD1 . LEU A 1 30  ? 3.958   -16.656 36.259 1.00 20.09  ? 29  LEU A CD1 1 
ATOM   228  C CD2 . LEU A 1 30  ? 4.239   -14.180 36.034 1.00 40.02  ? 29  LEU A CD2 1 
ATOM   229  N N   . GLY A 1 31  ? 9.184   -15.266 37.197 1.00 24.40  ? 30  GLY A N   1 
ATOM   230  C CA  . GLY A 1 31  ? 10.396  -15.582 37.910 1.00 21.92  ? 30  GLY A CA  1 
ATOM   231  C C   . GLY A 1 31  ? 11.164  -14.424 38.488 1.00 24.95  ? 30  GLY A C   1 
ATOM   232  O O   . GLY A 1 31  ? 11.770  -14.571 39.560 1.00 27.49  ? 30  GLY A O   1 
ATOM   233  N N   . SER A 1 32  ? 11.166  -13.297 37.782 1.00 20.44  ? 31  SER A N   1 
ATOM   234  C CA  . SER A 1 32  ? 11.906  -12.113 38.168 1.00 23.34  ? 31  SER A CA  1 
ATOM   235  C C   . SER A 1 32  ? 11.258  -11.387 39.351 1.00 13.78  ? 31  SER A C   1 
ATOM   236  O O   . SER A 1 32  ? 11.969  -10.749 40.125 1.00 19.07  ? 31  SER A O   1 
ATOM   237  C CB  . SER A 1 32  ? 12.066  -11.156 36.970 1.00 9.72   ? 31  SER A CB  1 
ATOM   238  O OG  . SER A 1 32  ? 10.791  -10.621 36.617 1.00 22.20  ? 31  SER A OG  1 
ATOM   239  N N   . ALA A 1 33  ? 9.946   -11.484 39.460 1.00 15.92  ? 32  ALA A N   1 
ATOM   240  C CA  . ALA A 1 33  ? 9.078   -10.742 40.343 1.00 21.12  ? 32  ALA A CA  1 
ATOM   241  C C   . ALA A 1 33  ? 8.731   -11.468 41.644 1.00 34.38  ? 32  ALA A C   1 
ATOM   242  O O   . ALA A 1 33  ? 8.099   -10.840 42.500 1.00 24.78  ? 32  ALA A O   1 
ATOM   243  C CB  . ALA A 1 33  ? 7.772   -10.406 39.622 1.00 12.46  ? 32  ALA A CB  1 
ATOM   244  N N   . LEU A 1 34  ? 9.108   -12.730 41.807 1.00 37.43  ? 33  LEU A N   1 
ATOM   245  C CA  . LEU A 1 34  ? 8.982   -13.406 43.089 1.00 36.67  ? 33  LEU A CA  1 
ATOM   246  C C   . LEU A 1 34  ? 9.555   -12.518 44.193 1.00 31.74  ? 33  LEU A C   1 
ATOM   247  O O   . LEU A 1 34  ? 10.449  -11.714 43.940 1.00 24.36  ? 33  LEU A O   1 
ATOM   248  C CB  . LEU A 1 34  ? 9.745   -14.729 43.126 1.00 28.23  ? 33  LEU A CB  1 
ATOM   249  C CG  . LEU A 1 34  ? 9.370   -15.744 42.055 1.00 19.65  ? 33  LEU A CG  1 
ATOM   250  C CD1 . LEU A 1 34  ? 9.897   -17.125 42.409 1.00 24.15  ? 33  LEU A CD1 1 
ATOM   251  C CD2 . LEU A 1 34  ? 7.861   -15.719 41.871 1.00 23.87  ? 33  LEU A CD2 1 
ATOM   252  N N   . LYS A 1 35  ? 9.046   -12.676 45.412 1.00 37.10  ? 34  LYS A N   1 
ATOM   253  C CA  . LYS A 1 35  ? 9.633   -11.837 46.474 1.00 47.31  ? 34  LYS A CA  1 
ATOM   254  C C   . LYS A 1 35  ? 11.108  -12.188 46.658 1.00 48.44  ? 34  LYS A C   1 
ATOM   255  O O   . LYS A 1 35  ? 11.926  -11.262 46.684 1.00 73.30  ? 34  LYS A O   1 
ATOM   256  C CB  . LYS A 1 35  ? 8.809   -11.945 47.755 1.00 37.64  ? 34  LYS A CB  1 
ATOM   257  C CG  . LYS A 1 35  ? 7.429   -11.291 47.660 1.00 35.64  ? 34  LYS A CG  1 
ATOM   258  C CD  . LYS A 1 35  ? 7.456   -10.106 46.710 1.00 42.31  ? 34  LYS A CD  1 
ATOM   259  C CE  . LYS A 1 35  ? 6.206   -9.253  46.775 1.00 44.74  ? 34  LYS A CE  1 
ATOM   260  N NZ  . LYS A 1 35  ? 4.967   -10.034 46.510 1.00 53.08  ? 34  LYS A NZ  1 
ATOM   261  N N   . TRP A 1 36  ? 11.501  -13.453 46.754 1.00 38.74  ? 35  TRP A N   1 
ATOM   262  C CA  . TRP A 1 36  ? 12.911  -13.788 46.927 1.00 36.86  ? 35  TRP A CA  1 
ATOM   263  C C   . TRP A 1 36  ? 13.417  -13.083 48.188 1.00 41.57  ? 35  TRP A C   1 
ATOM   264  O O   . TRP A 1 36  ? 13.629  -11.864 48.153 1.00 38.46  ? 35  TRP A O   1 
ATOM   265  C CB  . TRP A 1 36  ? 13.775  -13.378 45.754 1.00 35.48  ? 35  TRP A CB  1 
ATOM   266  C CG  . TRP A 1 36  ? 13.615  -14.080 44.448 1.00 37.40  ? 35  TRP A CG  1 
ATOM   267  C CD1 . TRP A 1 36  ? 13.098  -13.535 43.302 1.00 31.06  ? 35  TRP A CD1 1 
ATOM   268  C CD2 . TRP A 1 36  ? 13.964  -15.437 44.128 1.00 44.27  ? 35  TRP A CD2 1 
ATOM   269  N NE1 . TRP A 1 36  ? 13.106  -14.470 42.295 1.00 37.51  ? 35  TRP A NE1 1 
ATOM   270  C CE2 . TRP A 1 36  ? 13.628  -15.643 42.771 1.00 45.94  ? 35  TRP A CE2 1 
ATOM   271  C CE3 . TRP A 1 36  ? 14.522  -16.507 44.841 1.00 37.98  ? 35  TRP A CE3 1 
ATOM   272  C CZ2 . TRP A 1 36  ? 13.844  -16.875 42.149 1.00 44.55  ? 35  TRP A CZ2 1 
ATOM   273  C CZ3 . TRP A 1 36  ? 14.741  -17.730 44.233 1.00 26.34  ? 35  TRP A CZ3 1 
ATOM   274  C CH2 . TRP A 1 36  ? 14.395  -17.898 42.882 1.00 37.28  ? 35  TRP A CH2 1 
ATOM   275  N N   . PRO A 1 37  ? 13.601  -13.780 49.296 1.00 36.20  ? 36  PRO A N   1 
ATOM   276  C CA  . PRO A 1 37  ? 13.958  -13.047 50.528 1.00 31.55  ? 36  PRO A CA  1 
ATOM   277  C C   . PRO A 1 37  ? 15.440  -12.695 50.473 1.00 25.95  ? 36  PRO A C   1 
ATOM   278  O O   . PRO A 1 37  ? 15.966  -11.774 51.077 1.00 42.92  ? 36  PRO A O   1 
ATOM   279  C CB  . PRO A 1 37  ? 13.659  -14.059 51.626 1.00 40.72  ? 36  PRO A CB  1 
ATOM   280  C CG  . PRO A 1 37  ? 12.702  -15.020 50.987 1.00 43.55  ? 36  PRO A CG  1 
ATOM   281  C CD  . PRO A 1 37  ? 13.200  -15.170 49.573 1.00 35.62  ? 36  PRO A CD  1 
ATOM   282  N N   . SER A 1 38  ? 16.095  -13.522 49.681 1.00 20.68  ? 37  SER A N   1 
ATOM   283  C CA  . SER A 1 38  ? 17.513  -13.386 49.380 1.00 29.00  ? 37  SER A CA  1 
ATOM   284  C C   . SER A 1 38  ? 17.771  -11.943 48.954 1.00 36.67  ? 37  SER A C   1 
ATOM   285  O O   . SER A 1 38  ? 18.704  -11.289 49.425 1.00 63.76  ? 37  SER A O   1 
ATOM   286  C CB  . SER A 1 38  ? 17.864  -14.460 48.346 1.00 40.90  ? 37  SER A CB  1 
ATOM   287  O OG  . SER A 1 38  ? 16.845  -15.447 48.120 1.00 23.88  ? 37  SER A OG  1 
ATOM   288  N N   . ALA A 1 39  ? 16.948  -11.373 48.085 1.00 33.11  ? 38  ALA A N   1 
ATOM   289  C CA  . ALA A 1 39  ? 17.030  -10.004 47.596 1.00 42.92  ? 38  ALA A CA  1 
ATOM   290  C C   . ALA A 1 39  ? 15.715  -9.568  46.962 1.00 48.37  ? 38  ALA A C   1 
ATOM   291  O O   . ALA A 1 39  ? 15.429  -9.919  45.813 1.00 52.95  ? 38  ALA A O   1 
ATOM   292  C CB  . ALA A 1 39  ? 18.144  -9.823  46.560 1.00 28.03  ? 38  ALA A CB  1 
ATOM   293  N N   . LEU A 1 40  ? 14.869  -8.808  47.664 1.00 45.91  ? 39  LEU A N   1 
ATOM   294  C CA  . LEU A 1 40  ? 13.599  -8.473  47.029 1.00 39.07  ? 39  LEU A CA  1 
ATOM   295  C C   . LEU A 1 40  ? 13.834  -7.602  45.786 1.00 29.82  ? 39  LEU A C   1 
ATOM   296  O O   . LEU A 1 40  ? 14.416  -6.535  45.959 1.00 23.85  ? 39  LEU A O   1 
ATOM   297  C CB  . LEU A 1 40  ? 12.598  -7.718  47.911 1.00 32.41  ? 39  LEU A CB  1 
ATOM   298  C CG  . LEU A 1 40  ? 11.512  -8.608  48.534 1.00 41.39  ? 39  LEU A CG  1 
ATOM   299  C CD1 . LEU A 1 40  ? 11.670  -8.630  50.046 1.00 36.89  ? 39  LEU A CD1 1 
ATOM   300  C CD2 . LEU A 1 40  ? 10.121  -8.144  48.140 1.00 76.15  ? 39  LEU A CD2 1 
ATOM   301  N N   . PRO A 1 41  ? 13.312  -8.166  44.704 1.00 25.23  ? 40  PRO A N   1 
ATOM   302  C CA  . PRO A 1 41  ? 13.244  -7.484  43.417 1.00 24.69  ? 40  PRO A CA  1 
ATOM   303  C C   . PRO A 1 41  ? 12.509  -6.152  43.579 1.00 19.44  ? 40  PRO A C   1 
ATOM   304  O O   . PRO A 1 41  ? 11.391  -6.173  44.104 1.00 28.64  ? 40  PRO A O   1 
ATOM   305  C CB  . PRO A 1 41  ? 12.432  -8.427  42.537 1.00 29.11  ? 40  PRO A CB  1 
ATOM   306  C CG  . PRO A 1 41  ? 12.404  -9.753  43.219 1.00 29.92  ? 40  PRO A CG  1 
ATOM   307  C CD  . PRO A 1 41  ? 12.739  -9.522  44.655 1.00 27.24  ? 40  PRO A CD  1 
ATOM   308  N N   . THR A 1 42  ? 13.146  -5.089  43.130 1.00 26.40  ? 41  THR A N   1 
ATOM   309  C CA  . THR A 1 42  ? 12.649  -3.717  43.052 1.00 19.49  ? 41  THR A CA  1 
ATOM   310  C C   . THR A 1 42  ? 11.781  -3.458  41.838 1.00 16.51  ? 41  THR A C   1 
ATOM   311  O O   . THR A 1 42  ? 11.659  -4.324  40.955 1.00 32.05  ? 41  THR A O   1 
ATOM   312  C CB  . THR A 1 42  ? 13.852  -2.751  43.016 1.00 37.07  ? 41  THR A CB  1 
ATOM   313  O OG1 . THR A 1 42  ? 14.497  -2.910  41.738 1.00 28.78  ? 41  THR A OG1 1 
ATOM   314  C CG2 . THR A 1 42  ? 14.838  -3.101  44.129 1.00 24.64  ? 41  THR A CG2 1 
ATOM   315  N N   . ILE A 1 43  ? 11.140  -2.287  41.740 1.00 17.86  ? 42  ILE A N   1 
ATOM   316  C CA  . ILE A 1 43  ? 10.204  -2.053  40.633 1.00 23.46  ? 42  ILE A CA  1 
ATOM   317  C C   . ILE A 1 43  ? 10.896  -2.037  39.266 1.00 27.94  ? 42  ILE A C   1 
ATOM   318  O O   . ILE A 1 43  ? 10.444  -2.669  38.302 1.00 17.57  ? 42  ILE A O   1 
ATOM   319  C CB  . ILE A 1 43  ? 9.416   -0.751  40.827 1.00 29.50  ? 42  ILE A CB  1 
ATOM   320  C CG1 . ILE A 1 43  ? 8.573   -0.678  42.111 1.00 29.74  ? 42  ILE A CG1 1 
ATOM   321  C CG2 . ILE A 1 43  ? 8.478   -0.481  39.656 1.00 23.81  ? 42  ILE A CG2 1 
ATOM   322  C CD1 . ILE A 1 43  ? 7.146   -1.142  41.847 1.00 27.24  ? 42  ILE A CD1 1 
ATOM   323  N N   . LEU A 1 44  ? 12.002  -1.322  39.148 1.00 24.07  ? 43  LEU A N   1 
ATOM   324  C CA  . LEU A 1 44  ? 12.693  -1.198  37.864 1.00 29.21  ? 43  LEU A CA  1 
ATOM   325  C C   . LEU A 1 44  ? 13.291  -2.547  37.471 1.00 28.50  ? 43  LEU A C   1 
ATOM   326  O O   . LEU A 1 44  ? 13.263  -2.917  36.292 1.00 25.25  ? 43  LEU A O   1 
ATOM   327  C CB  . LEU A 1 44  ? 13.772  -0.125  37.869 1.00 21.79  ? 43  LEU A CB  1 
ATOM   328  C CG  . LEU A 1 44  ? 14.676  0.031   36.640 1.00 21.58  ? 43  LEU A CG  1 
ATOM   329  C CD1 . LEU A 1 44  ? 14.025  0.867   35.557 1.00 16.23  ? 43  LEU A CD1 1 
ATOM   330  C CD2 . LEU A 1 44  ? 15.992  0.670   37.059 1.00 27.75  ? 43  LEU A CD2 1 
ATOM   331  N N   . GLN A 1 45  ? 13.804  -3.220  38.494 1.00 24.83  ? 44  GLN A N   1 
ATOM   332  C CA  . GLN A 1 45  ? 14.335  -4.565  38.313 1.00 20.99  ? 44  GLN A CA  1 
ATOM   333  C C   . GLN A 1 45  ? 13.342  -5.421  37.527 1.00 33.89  ? 44  GLN A C   1 
ATOM   334  O O   . GLN A 1 45  ? 13.643  -6.035  36.514 1.00 26.63  ? 44  GLN A O   1 
ATOM   335  C CB  . GLN A 1 45  ? 14.589  -5.220  39.665 1.00 15.70  ? 44  GLN A CB  1 
ATOM   336  C CG  . GLN A 1 45  ? 15.352  -6.532  39.585 1.00 21.21  ? 44  GLN A CG  1 
ATOM   337  C CD  . GLN A 1 45  ? 15.631  -7.077  40.980 1.00 29.96  ? 44  GLN A CD  1 
ATOM   338  O OE1 . GLN A 1 45  ? 15.890  -6.282  41.887 1.00 20.72  ? 44  GLN A OE1 1 
ATOM   339  N NE2 . GLN A 1 45  ? 15.567  -8.393  41.111 1.00 19.68  ? 44  GLN A NE2 1 
ATOM   340  N N   . ILE A 1 46  ? 12.121  -5.427  38.053 1.00 31.06  ? 45  ILE A N   1 
ATOM   341  C CA  . ILE A 1 46  ? 10.996  -6.112  37.465 1.00 21.84  ? 45  ILE A CA  1 
ATOM   342  C C   . ILE A 1 46  ? 10.556  -5.482  36.147 1.00 27.84  ? 45  ILE A C   1 
ATOM   343  O O   . ILE A 1 46  ? 10.284  -6.212  35.182 1.00 19.85  ? 45  ILE A O   1 
ATOM   344  C CB  . ILE A 1 46  ? 9.798   -6.106  38.433 1.00 19.38  ? 45  ILE A CB  1 
ATOM   345  C CG1 . ILE A 1 46  ? 10.005  -7.012  39.648 1.00 24.20  ? 45  ILE A CG1 1 
ATOM   346  C CG2 . ILE A 1 46  ? 8.525   -6.446  37.676 1.00 14.88  ? 45  ILE A CG2 1 
ATOM   347  C CD1 . ILE A 1 46  ? 9.648   -6.330  40.955 1.00 30.63  ? 45  ILE A CD1 1 
ATOM   348  N N   . ALA A 1 47  ? 10.483  -4.148  36.115 1.00 18.78  ? 46  ALA A N   1 
ATOM   349  C CA  . ALA A 1 47  ? 10.109  -3.534  34.833 1.00 17.14  ? 46  ALA A CA  1 
ATOM   350  C C   . ALA A 1 47  ? 11.091  -3.965  33.752 1.00 24.86  ? 46  ALA A C   1 
ATOM   351  O O   . ALA A 1 47  ? 10.758  -4.336  32.628 1.00 23.29  ? 46  ALA A O   1 
ATOM   352  C CB  . ALA A 1 47  ? 10.050  -2.020  34.917 1.00 16.77  ? 46  ALA A CB  1 
ATOM   353  N N   . LEU A 1 48  ? 12.380  -3.949  34.118 1.00 22.16  ? 47  LEU A N   1 
ATOM   354  C CA  . LEU A 1 48  ? 13.304  -4.335  33.058 1.00 18.77  ? 47  LEU A CA  1 
ATOM   355  C C   . LEU A 1 48  ? 13.166  -5.807  32.719 1.00 22.06  ? 47  LEU A C   1 
ATOM   356  O O   . LEU A 1 48  ? 13.275  -6.192  31.553 1.00 21.99  ? 47  LEU A O   1 
ATOM   357  C CB  . LEU A 1 48  ? 14.727  -3.970  33.484 1.00 18.41  ? 47  LEU A CB  1 
ATOM   358  C CG  . LEU A 1 48  ? 15.134  -2.546  33.084 1.00 27.88  ? 47  LEU A CG  1 
ATOM   359  C CD1 . LEU A 1 48  ? 14.007  -1.561  33.329 1.00 39.84  ? 47  LEU A CD1 1 
ATOM   360  C CD2 . LEU A 1 48  ? 16.382  -2.117  33.831 1.00 25.81  ? 47  LEU A CD2 1 
ATOM   361  N N   . ALA A 1 49  ? 12.932  -6.677  33.703 1.00 12.54  ? 48  ALA A N   1 
ATOM   362  C CA  . ALA A 1 49  ? 12.901  -8.099  33.373 1.00 10.20  ? 48  ALA A CA  1 
ATOM   363  C C   . ALA A 1 49  ? 11.803  -8.425  32.366 1.00 22.30  ? 48  ALA A C   1 
ATOM   364  O O   . ALA A 1 49  ? 12.098  -9.024  31.330 1.00 41.51  ? 48  ALA A O   1 
ATOM   365  C CB  . ALA A 1 49  ? 12.720  -8.954  34.613 1.00 16.52  ? 48  ALA A CB  1 
ATOM   366  N N   . PHE A 1 50  ? 10.583  -8.023  32.697 1.00 13.87  ? 49  PHE A N   1 
ATOM   367  C CA  . PHE A 1 50  ? 9.450   -8.211  31.803 1.00 23.53  ? 49  PHE A CA  1 
ATOM   368  C C   . PHE A 1 50  ? 9.698   -7.604  30.423 1.00 25.38  ? 49  PHE A C   1 
ATOM   369  O O   . PHE A 1 50  ? 9.323   -8.158  29.391 1.00 19.59  ? 49  PHE A O   1 
ATOM   370  C CB  . PHE A 1 50  ? 8.200   -7.588  32.437 1.00 25.14  ? 49  PHE A CB  1 
ATOM   371  C CG  . PHE A 1 50  ? 7.400   -8.554  33.306 1.00 27.72  ? 49  PHE A CG  1 
ATOM   372  C CD1 . PHE A 1 50  ? 7.735   -8.733  34.636 1.00 21.40  ? 49  PHE A CD1 1 
ATOM   373  C CD2 . PHE A 1 50  ? 6.328   -9.260  32.776 1.00 20.95  ? 49  PHE A CD2 1 
ATOM   374  C CE1 . PHE A 1 50  ? 6.996   -9.599  35.434 1.00 22.96  ? 49  PHE A CE1 1 
ATOM   375  C CE2 . PHE A 1 50  ? 5.578   -10.133 33.553 1.00 22.95  ? 49  PHE A CE2 1 
ATOM   376  C CZ  . PHE A 1 50  ? 5.924   -10.286 34.889 1.00 27.14  ? 49  PHE A CZ  1 
ATOM   377  N N   . GLY A 1 51  ? 10.359  -6.455  30.368 1.00 25.34  ? 50  GLY A N   1 
ATOM   378  C CA  . GLY A 1 51  ? 10.654  -5.798  29.114 1.00 24.90  ? 50  GLY A CA  1 
ATOM   379  C C   . GLY A 1 51  ? 11.710  -6.488  28.277 1.00 31.46  ? 50  GLY A C   1 
ATOM   380  O O   . GLY A 1 51  ? 11.534  -6.676  27.055 1.00 24.72  ? 50  GLY A O   1 
ATOM   381  N N   . LEU A 1 52  ? 12.831  -6.860  28.911 1.00 17.08  ? 51  LEU A N   1 
ATOM   382  C CA  . LEU A 1 52  ? 13.891  -7.480  28.118 1.00 14.06  ? 51  LEU A CA  1 
ATOM   383  C C   . LEU A 1 52  ? 13.471  -8.864  27.633 1.00 28.23  ? 51  LEU A C   1 
ATOM   384  O O   . LEU A 1 52  ? 14.095  -9.440  26.741 1.00 19.12  ? 51  LEU A O   1 
ATOM   385  C CB  . LEU A 1 52  ? 15.171  -7.626  28.931 1.00 20.55  ? 51  LEU A CB  1 
ATOM   386  C CG  . LEU A 1 52  ? 15.822  -6.365  29.483 1.00 24.26  ? 51  LEU A CG  1 
ATOM   387  C CD1 . LEU A 1 52  ? 16.991  -6.733  30.381 1.00 20.37  ? 51  LEU A CD1 1 
ATOM   388  C CD2 . LEU A 1 52  ? 16.265  -5.458  28.342 1.00 47.42  ? 51  LEU A CD2 1 
ATOM   389  N N   . ALA A 1 53  ? 12.423  -9.401  28.260 1.00 30.04  ? 52  ALA A N   1 
ATOM   390  C CA  . ALA A 1 53  ? 11.959  -10.740 27.931 1.00 24.54  ? 52  ALA A CA  1 
ATOM   391  C C   . ALA A 1 53  ? 11.235  -10.711 26.586 1.00 28.50  ? 52  ALA A C   1 
ATOM   392  O O   . ALA A 1 53  ? 11.485  -11.597 25.766 1.00 21.50  ? 52  ALA A O   1 
ATOM   393  C CB  . ALA A 1 53  ? 11.048  -11.312 28.998 1.00 31.99  ? 52  ALA A CB  1 
ATOM   394  N N   . ILE A 1 54  ? 10.400  -9.694  26.451 1.00 28.52  ? 53  ILE A N   1 
ATOM   395  C CA  . ILE A 1 54  ? 9.617   -9.436  25.247 1.00 30.10  ? 53  ILE A CA  1 
ATOM   396  C C   . ILE A 1 54  ? 10.552  -8.975  24.136 1.00 23.09  ? 53  ILE A C   1 
ATOM   397  O O   . ILE A 1 54  ? 10.500  -9.508  23.029 1.00 21.18  ? 53  ILE A O   1 
ATOM   398  C CB  . ILE A 1 54  ? 8.513   -8.397  25.478 1.00 25.41  ? 53  ILE A CB  1 
ATOM   399  C CG1 . ILE A 1 54  ? 7.357   -8.910  26.341 1.00 19.48  ? 53  ILE A CG1 1 
ATOM   400  C CG2 . ILE A 1 54  ? 7.982   -7.866  24.149 1.00 20.49  ? 53  ILE A CG2 1 
ATOM   401  C CD1 . ILE A 1 54  ? 6.807   -10.236 25.837 1.00 13.41  ? 53  ILE A CD1 1 
ATOM   402  N N   . GLY A 1 55  ? 11.417  -8.010  24.452 1.00 18.36  ? 54  GLY A N   1 
ATOM   403  C CA  . GLY A 1 55  ? 12.342  -7.528  23.430 1.00 21.19  ? 54  GLY A CA  1 
ATOM   404  C C   . GLY A 1 55  ? 13.227  -8.649  22.941 1.00 18.60  ? 54  GLY A C   1 
ATOM   405  O O   . GLY A 1 55  ? 13.646  -8.724  21.796 1.00 22.82  ? 54  GLY A O   1 
ATOM   406  N N   . THR A 1 56  ? 13.553  -9.583  23.824 1.00 26.00  ? 55  THR A N   1 
ATOM   407  C CA  . THR A 1 56  ? 14.400  -10.711 23.456 1.00 23.17  ? 55  THR A CA  1 
ATOM   408  C C   . THR A 1 56  ? 13.650  -11.695 22.562 1.00 28.99  ? 55  THR A C   1 
ATOM   409  O O   . THR A 1 56  ? 14.096  -12.054 21.474 1.00 42.42  ? 55  THR A O   1 
ATOM   410  C CB  . THR A 1 56  ? 14.926  -11.443 24.701 1.00 16.77  ? 55  THR A CB  1 
ATOM   411  O OG1 . THR A 1 56  ? 15.880  -10.611 25.371 1.00 22.41  ? 55  THR A OG1 1 
ATOM   412  C CG2 . THR A 1 56  ? 15.666  -12.712 24.307 1.00 25.12  ? 55  THR A CG2 1 
ATOM   413  N N   . LEU A 1 57  ? 12.497  -12.131 23.037 1.00 25.34  ? 56  LEU A N   1 
ATOM   414  C CA  . LEU A 1 57  ? 11.674  -13.123 22.371 1.00 30.16  ? 56  LEU A CA  1 
ATOM   415  C C   . LEU A 1 57  ? 11.155  -12.575 21.045 1.00 26.56  ? 56  LEU A C   1 
ATOM   416  O O   . LEU A 1 57  ? 11.007  -13.371 20.122 1.00 18.00  ? 56  LEU A O   1 
ATOM   417  C CB  . LEU A 1 57  ? 10.500  -13.568 23.252 1.00 28.35  ? 56  LEU A CB  1 
ATOM   418  C CG  . LEU A 1 57  ? 10.923  -14.391 24.476 1.00 25.71  ? 56  LEU A CG  1 
ATOM   419  C CD1 . LEU A 1 57  ? 9.743   -14.680 25.385 1.00 24.34  ? 56  LEU A CD1 1 
ATOM   420  C CD2 . LEU A 1 57  ? 11.618  -15.666 24.008 1.00 16.69  ? 56  LEU A CD2 1 
ATOM   421  N N   . ALA A 1 58  ? 10.913  -11.271 21.025 1.00 17.10  ? 57  ALA A N   1 
ATOM   422  C CA  . ALA A 1 58  ? 10.490  -10.601 19.793 1.00 23.30  ? 57  ALA A CA  1 
ATOM   423  C C   . ALA A 1 58  ? 11.565  -10.777 18.726 1.00 23.94  ? 57  ALA A C   1 
ATOM   424  O O   . ALA A 1 58  ? 11.315  -11.246 17.619 1.00 23.52  ? 57  ALA A O   1 
ATOM   425  C CB  . ALA A 1 58  ? 10.226  -9.133  20.059 1.00 25.58  ? 57  ALA A CB  1 
ATOM   426  N N   . GLN A 1 59  ? 12.783  -10.403 19.105 1.00 24.54  ? 58  GLN A N   1 
ATOM   427  C CA  . GLN A 1 59  ? 13.961  -10.577 18.266 1.00 20.45  ? 58  GLN A CA  1 
ATOM   428  C C   . GLN A 1 59  ? 14.071  -12.023 17.784 1.00 30.13  ? 58  GLN A C   1 
ATOM   429  O O   . GLN A 1 59  ? 14.130  -12.287 16.579 1.00 35.53  ? 58  GLN A O   1 
ATOM   430  C CB  . GLN A 1 59  ? 15.202  -10.159 19.044 1.00 12.87  ? 58  GLN A CB  1 
ATOM   431  C CG  . GLN A 1 59  ? 16.531  -10.130 18.326 1.00 15.98  ? 58  GLN A CG  1 
ATOM   432  C CD  . GLN A 1 59  ? 16.701  -8.927  17.422 1.00 20.29  ? 58  GLN A CD  1 
ATOM   433  O OE1 . GLN A 1 59  ? 15.772  -8.133  17.274 1.00 26.40  ? 58  GLN A OE1 1 
ATOM   434  N NE2 . GLN A 1 59  ? 17.867  -8.794  16.795 1.00 22.58  ? 58  GLN A NE2 1 
ATOM   435  N N   . ALA A 1 60  ? 14.097  -12.951 18.735 1.00 20.51  ? 59  ALA A N   1 
ATOM   436  C CA  . ALA A 1 60  ? 14.348  -14.351 18.458 1.00 14.80  ? 59  ALA A CA  1 
ATOM   437  C C   . ALA A 1 60  ? 13.275  -14.984 17.593 1.00 26.59  ? 59  ALA A C   1 
ATOM   438  O O   . ALA A 1 60  ? 13.597  -15.571 16.562 1.00 40.87  ? 59  ALA A O   1 
ATOM   439  C CB  . ALA A 1 60  ? 14.462  -15.141 19.757 1.00 20.48  ? 59  ALA A CB  1 
ATOM   440  N N   . LEU A 1 61  ? 12.025  -14.863 18.030 1.00 26.24  ? 60  LEU A N   1 
ATOM   441  C CA  . LEU A 1 61  ? 10.949  -15.670 17.484 1.00 23.93  ? 60  LEU A CA  1 
ATOM   442  C C   . LEU A 1 61  ? 9.962   -14.917 16.621 1.00 32.62  ? 60  LEU A C   1 
ATOM   443  O O   . LEU A 1 61  ? 9.136   -15.551 15.948 1.00 34.58  ? 60  LEU A O   1 
ATOM   444  C CB  . LEU A 1 61  ? 10.285  -16.388 18.689 1.00 22.62  ? 60  LEU A CB  1 
ATOM   445  C CG  . LEU A 1 61  ? 11.241  -17.386 19.377 1.00 16.53  ? 60  LEU A CG  1 
ATOM   446  C CD1 . LEU A 1 61  ? 10.700  -17.875 20.718 1.00 25.13  ? 60  LEU A CD1 1 
ATOM   447  C CD2 . LEU A 1 61  ? 11.525  -18.601 18.509 1.00 19.34  ? 60  LEU A CD2 1 
ATOM   448  N N   . GLY A 1 62  ? 10.003  -13.589 16.584 1.00 30.84  ? 61  GLY A N   1 
ATOM   449  C CA  . GLY A 1 62  ? 9.155   -12.799 15.717 1.00 29.64  ? 61  GLY A CA  1 
ATOM   450  C C   . GLY A 1 62  ? 9.174   -13.142 14.246 1.00 36.04  ? 61  GLY A C   1 
ATOM   451  O O   . GLY A 1 62  ? 8.120   -13.093 13.586 1.00 33.14  ? 61  GLY A O   1 
ATOM   452  N N   . PRO A 1 63  ? 10.287  -13.465 13.598 1.00 33.15  ? 62  PRO A N   1 
ATOM   453  C CA  . PRO A 1 63  ? 10.241  -13.837 12.175 1.00 28.54  ? 62  PRO A CA  1 
ATOM   454  C C   . PRO A 1 63  ? 9.536   -15.158 11.905 1.00 34.13  ? 62  PRO A C   1 
ATOM   455  O O   . PRO A 1 63  ? 9.142   -15.464 10.775 1.00 36.23  ? 62  PRO A O   1 
ATOM   456  C CB  . PRO A 1 63  ? 11.718  -14.017 11.796 1.00 37.38  ? 62  PRO A CB  1 
ATOM   457  C CG  . PRO A 1 63  ? 12.487  -13.297 12.848 1.00 35.82  ? 62  PRO A CG  1 
ATOM   458  C CD  . PRO A 1 63  ? 11.669  -13.467 14.106 1.00 33.33  ? 62  PRO A CD  1 
ATOM   459  N N   . VAL A 1 64  ? 9.398   -15.950 12.963 1.00 31.75  ? 63  VAL A N   1 
ATOM   460  C CA  . VAL A 1 64  ? 8.675   -17.201 12.863 1.00 27.68  ? 63  VAL A CA  1 
ATOM   461  C C   . VAL A 1 64  ? 7.166   -16.972 12.838 1.00 35.67  ? 63  VAL A C   1 
ATOM   462  O O   . VAL A 1 64  ? 6.491   -17.581 12.001 1.00 28.82  ? 63  VAL A O   1 
ATOM   463  C CB  . VAL A 1 64  ? 8.993   -18.122 14.054 1.00 31.82  ? 63  VAL A CB  1 
ATOM   464  C CG1 . VAL A 1 64  ? 8.368   -19.485 13.797 1.00 35.03  ? 63  VAL A CG1 1 
ATOM   465  C CG2 . VAL A 1 64  ? 10.494  -18.188 14.257 1.00 33.21  ? 63  VAL A CG2 1 
ATOM   466  N N   . SER A 1 65  ? 6.689   -16.121 13.753 1.00 21.96  ? 64  SER A N   1 
ATOM   467  C CA  . SER A 1 65  ? 5.260   -15.952 13.967 1.00 25.30  ? 64  SER A CA  1 
ATOM   468  C C   . SER A 1 65  ? 4.757   -14.527 13.859 1.00 25.93  ? 64  SER A C   1 
ATOM   469  O O   . SER A 1 65  ? 3.583   -14.275 13.560 1.00 28.88  ? 64  SER A O   1 
ATOM   470  C CB  . SER A 1 65  ? 4.863   -16.495 15.364 1.00 25.15  ? 64  SER A CB  1 
ATOM   471  O OG  . SER A 1 65  ? 5.402   -15.714 16.406 1.00 22.90  ? 64  SER A OG  1 
ATOM   472  N N   . GLY A 1 66  ? 5.588   -13.532 14.114 1.00 21.46  ? 65  GLY A N   1 
ATOM   473  C CA  . GLY A 1 66  ? 5.029   -12.189 14.303 1.00 32.16  ? 65  GLY A CA  1 
ATOM   474  C C   . GLY A 1 66  ? 5.191   -11.808 15.775 1.00 29.09  ? 65  GLY A C   1 
ATOM   475  O O   . GLY A 1 66  ? 5.157   -10.646 16.144 1.00 36.43  ? 65  GLY A O   1 
ATOM   476  N N   . GLY A 1 67  ? 5.390   -12.851 16.573 1.00 22.16  ? 66  GLY A N   1 
ATOM   477  C CA  . GLY A 1 67  ? 5.812   -12.720 17.940 1.00 16.52  ? 66  GLY A CA  1 
ATOM   478  C C   . GLY A 1 67  ? 4.866   -11.806 18.686 1.00 21.55  ? 66  GLY A C   1 
ATOM   479  O O   . GLY A 1 67  ? 5.264   -10.792 19.254 1.00 28.86  ? 66  GLY A O   1 
ATOM   480  N N   . HIS A 1 68  ? 3.599   -12.206 18.669 1.00 25.49  ? 67  HIS A N   1 
ATOM   481  C CA  . HIS A 1 68  ? 2.613   -11.413 19.399 1.00 19.95  ? 67  HIS A CA  1 
ATOM   482  C C   . HIS A 1 68  ? 2.789   -11.635 20.902 1.00 36.34  ? 67  HIS A C   1 
ATOM   483  O O   . HIS A 1 68  ? 2.809   -10.685 21.694 1.00 30.72  ? 67  HIS A O   1 
ATOM   484  C CB  . HIS A 1 68  ? 1.204   -11.768 18.951 1.00 17.42  ? 67  HIS A CB  1 
ATOM   485  C CG  . HIS A 1 68  ? 0.963   -11.671 17.482 1.00 28.84  ? 67  HIS A CG  1 
ATOM   486  N ND1 . HIS A 1 68  ? -0.258  -11.935 16.913 1.00 28.68  ? 67  HIS A ND1 1 
ATOM   487  C CD2 . HIS A 1 68  ? 1.782   -11.339 16.450 1.00 33.70  ? 67  HIS A CD2 1 
ATOM   488  C CE1 . HIS A 1 68  ? -0.183  -11.776 15.602 1.00 27.47  ? 67  HIS A CE1 1 
ATOM   489  N NE2 . HIS A 1 68  ? 1.056   -11.411 15.299 1.00 27.77  ? 67  HIS A NE2 1 
ATOM   490  N N   . ILE A 1 69  ? 2.926   -12.897 21.306 1.00 29.15  ? 68  ILE A N   1 
ATOM   491  C CA  . ILE A 1 69  ? 3.092   -13.327 22.683 1.00 29.68  ? 68  ILE A CA  1 
ATOM   492  C C   . ILE A 1 69  ? 2.076   -12.715 23.642 1.00 40.05  ? 68  ILE A C   1 
ATOM   493  O O   . ILE A 1 69  ? 2.345   -12.624 24.846 1.00 36.58  ? 68  ILE A O   1 
ATOM   494  C CB  . ILE A 1 69  ? 4.499   -12.945 23.187 1.00 21.46  ? 68  ILE A CB  1 
ATOM   495  C CG1 . ILE A 1 69  ? 5.557   -12.967 22.076 1.00 16.66  ? 68  ILE A CG1 1 
ATOM   496  C CG2 . ILE A 1 69  ? 4.916   -13.792 24.375 1.00 18.72  ? 68  ILE A CG2 1 
ATOM   497  C CD1 . ILE A 1 69  ? 6.912   -12.489 22.561 1.00 27.37  ? 68  ILE A CD1 1 
ATOM   498  N N   . ASN A 1 70  ? 0.919   -12.294 23.149 1.00 31.07  ? 69  ASN A N   1 
ATOM   499  C CA  . ASN A 1 70  ? -0.067  -11.561 23.936 1.00 26.63  ? 69  ASN A CA  1 
ATOM   500  C C   . ASN A 1 70  ? -1.425  -11.564 23.234 1.00 32.44  ? 69  ASN A C   1 
ATOM   501  O O   . ASN A 1 70  ? -1.611  -10.954 22.175 1.00 21.42  ? 69  ASN A O   1 
ATOM   502  C CB  . ASN A 1 70  ? 0.478   -10.156 24.174 1.00 24.90  ? 69  ASN A CB  1 
ATOM   503  C CG  . ASN A 1 70  ? -0.449  -9.248  24.954 1.00 33.47  ? 69  ASN A CG  1 
ATOM   504  O OD1 . ASN A 1 70  ? -1.598  -9.597  25.215 1.00 31.49  ? 69  ASN A OD1 1 
ATOM   505  N ND2 . ASN A 1 70  ? 0.024   -8.064  25.327 1.00 32.43  ? 69  ASN A ND2 1 
ATOM   506  N N   . PRO A 1 71  ? -2.393  -12.276 23.815 1.00 34.70  ? 70  PRO A N   1 
ATOM   507  C CA  . PRO A 1 71  ? -3.729  -12.386 23.210 1.00 26.22  ? 70  PRO A CA  1 
ATOM   508  C C   . PRO A 1 71  ? -4.357  -11.029 22.949 1.00 25.41  ? 70  PRO A C   1 
ATOM   509  O O   . PRO A 1 71  ? -5.131  -10.886 21.998 1.00 26.21  ? 70  PRO A O   1 
ATOM   510  C CB  . PRO A 1 71  ? -4.533  -13.174 24.242 1.00 27.13  ? 70  PRO A CB  1 
ATOM   511  C CG  . PRO A 1 71  ? -3.524  -13.888 25.081 1.00 27.79  ? 70  PRO A CG  1 
ATOM   512  C CD  . PRO A 1 71  ? -2.277  -13.046 25.075 1.00 32.22  ? 70  PRO A CD  1 
ATOM   513  N N   . ALA A 1 72  ? -4.030  -10.023 23.770 1.00 24.38  ? 71  ALA A N   1 
ATOM   514  C CA  . ALA A 1 72  ? -4.657  -8.730  23.475 1.00 19.70  ? 71  ALA A CA  1 
ATOM   515  C C   . ALA A 1 72  ? -4.160  -8.203  22.133 1.00 16.90  ? 71  ALA A C   1 
ATOM   516  O O   . ALA A 1 72  ? -4.972  -7.674  21.363 1.00 25.12  ? 71  ALA A O   1 
ATOM   517  C CB  . ALA A 1 72  ? -4.426  -7.706  24.570 1.00 26.38  ? 71  ALA A CB  1 
ATOM   518  N N   . ILE A 1 73  ? -2.861  -8.352  21.853 1.00 20.28  ? 72  ILE A N   1 
ATOM   519  C CA  . ILE A 1 73  ? -2.343  -7.775  20.595 1.00 32.30  ? 72  ILE A CA  1 
ATOM   520  C C   . ILE A 1 73  ? -2.694  -8.677  19.415 1.00 36.94  ? 72  ILE A C   1 
ATOM   521  O O   . ILE A 1 73  ? -2.985  -8.209  18.303 1.00 25.34  ? 72  ILE A O   1 
ATOM   522  C CB  . ILE A 1 73  ? -0.839  -7.479  20.705 1.00 38.19  ? 72  ILE A CB  1 
ATOM   523  C CG1 . ILE A 1 73  ? -0.540  -6.107  21.348 1.00 28.95  ? 72  ILE A CG1 1 
ATOM   524  C CG2 . ILE A 1 73  ? -0.126  -7.592  19.371 1.00 30.09  ? 72  ILE A CG2 1 
ATOM   525  C CD1 . ILE A 1 73  ? 0.189   -6.213  22.647 1.00 29.59  ? 72  ILE A CD1 1 
ATOM   526  N N   . THR A 1 74  ? -2.725  -9.989  19.643 1.00 23.81  ? 73  THR A N   1 
ATOM   527  C CA  . THR A 1 74  ? -3.277  -10.863 18.607 1.00 27.07  ? 73  THR A CA  1 
ATOM   528  C C   . THR A 1 74  ? -4.687  -10.419 18.235 1.00 28.37  ? 73  THR A C   1 
ATOM   529  O O   . THR A 1 74  ? -4.948  -10.050 17.085 1.00 29.93  ? 73  THR A O   1 
ATOM   530  C CB  . THR A 1 74  ? -3.251  -12.328 19.065 1.00 22.45  ? 73  THR A CB  1 
ATOM   531  O OG1 . THR A 1 74  ? -1.896  -12.786 19.103 1.00 27.33  ? 73  THR A OG1 1 
ATOM   532  C CG2 . THR A 1 74  ? -3.954  -13.229 18.060 1.00 26.50  ? 73  THR A CG2 1 
ATOM   533  N N   . LEU A 1 75  ? -5.625  -10.396 19.176 1.00 24.47  ? 74  LEU A N   1 
ATOM   534  C CA  . LEU A 1 75  ? -6.980  -9.951  18.830 1.00 26.11  ? 74  LEU A CA  1 
ATOM   535  C C   . LEU A 1 75  ? -7.053  -8.582  18.185 1.00 29.46  ? 74  LEU A C   1 
ATOM   536  O O   . LEU A 1 75  ? -7.769  -8.416  17.186 1.00 34.01  ? 74  LEU A O   1 
ATOM   537  C CB  . LEU A 1 75  ? -7.832  -9.993  20.108 1.00 26.16  ? 74  LEU A CB  1 
ATOM   538  C CG  . LEU A 1 75  ? -8.094  -11.449 20.531 1.00 28.05  ? 74  LEU A CG  1 
ATOM   539  C CD1 . LEU A 1 75  ? -8.594  -11.535 21.954 1.00 45.09  ? 74  LEU A CD1 1 
ATOM   540  C CD2 . LEU A 1 75  ? -9.069  -12.037 19.528 1.00 27.08  ? 74  LEU A CD2 1 
ATOM   541  N N   . ALA A 1 76  ? -6.314  -7.600  18.700 1.00 34.66  ? 75  ALA A N   1 
ATOM   542  C CA  . ALA A 1 76  ? -6.215  -6.310  18.007 1.00 36.29  ? 75  ALA A CA  1 
ATOM   543  C C   . ALA A 1 76  ? -5.710  -6.500  16.580 1.00 38.48  ? 75  ALA A C   1 
ATOM   544  O O   . ALA A 1 76  ? -6.205  -5.891  15.635 1.00 28.70  ? 75  ALA A O   1 
ATOM   545  C CB  . ALA A 1 76  ? -5.313  -5.338  18.754 1.00 41.48  ? 75  ALA A CB  1 
ATOM   546  N N   . LEU A 1 77  ? -4.706  -7.347  16.335 1.00 41.20  ? 76  LEU A N   1 
ATOM   547  C CA  . LEU A 1 77  ? -4.284  -7.480  14.939 1.00 37.48  ? 76  LEU A CA  1 
ATOM   548  C C   . LEU A 1 77  ? -5.390  -8.074  14.075 1.00 40.67  ? 76  LEU A C   1 
ATOM   549  O O   . LEU A 1 77  ? -5.401  -7.854  12.864 1.00 28.53  ? 76  LEU A O   1 
ATOM   550  C CB  . LEU A 1 77  ? -3.022  -8.332  14.844 1.00 25.70  ? 76  LEU A CB  1 
ATOM   551  C CG  . LEU A 1 77  ? -1.801  -7.566  15.367 1.00 24.23  ? 76  LEU A CG  1 
ATOM   552  C CD1 . LEU A 1 77  ? -0.640  -8.514  15.574 1.00 25.70  ? 76  LEU A CD1 1 
ATOM   553  C CD2 . LEU A 1 77  ? -1.430  -6.451  14.401 1.00 33.59  ? 76  LEU A CD2 1 
ATOM   554  N N   . LEU A 1 78  ? -6.278  -8.801  14.742 1.00 30.81  ? 77  LEU A N   1 
ATOM   555  C CA  . LEU A 1 78  ? -7.430  -9.370  14.058 1.00 34.23  ? 77  LEU A CA  1 
ATOM   556  C C   . LEU A 1 78  ? -8.379  -8.212  13.773 1.00 35.74  ? 77  LEU A C   1 
ATOM   557  O O   . LEU A 1 78  ? -8.824  -8.030  12.650 1.00 38.22  ? 77  LEU A O   1 
ATOM   558  C CB  . LEU A 1 78  ? -8.155  -10.441 14.861 1.00 35.61  ? 77  LEU A CB  1 
ATOM   559  C CG  . LEU A 1 78  ? -9.480  -10.917 14.255 1.00 41.37  ? 77  LEU A CG  1 
ATOM   560  C CD1 . LEU A 1 78  ? -9.269  -11.996 13.190 1.00 26.67  ? 77  LEU A CD1 1 
ATOM   561  C CD2 . LEU A 1 78  ? -10.408 -11.408 15.354 1.00 49.95  ? 77  LEU A CD2 1 
ATOM   562  N N   . VAL A 1 79  ? -8.631  -7.451  14.839 1.00 32.51  ? 78  VAL A N   1 
ATOM   563  C CA  . VAL A 1 79  ? -9.472  -6.270  14.615 1.00 32.77  ? 78  VAL A CA  1 
ATOM   564  C C   . VAL A 1 79  ? -8.894  -5.384  13.532 1.00 39.06  ? 78  VAL A C   1 
ATOM   565  O O   . VAL A 1 79  ? -9.555  -5.049  12.532 1.00 37.20  ? 78  VAL A O   1 
ATOM   566  C CB  . VAL A 1 79  ? -9.659  -5.549  15.955 1.00 27.79  ? 78  VAL A CB  1 
ATOM   567  C CG1 . VAL A 1 79  ? -10.298 -4.189  15.784 1.00 21.75  ? 78  VAL A CG1 1 
ATOM   568  C CG2 . VAL A 1 79  ? -10.501 -6.429  16.875 1.00 31.59  ? 78  VAL A CG2 1 
ATOM   569  N N   . GLY A 1 80  ? -7.633  -4.953  13.587 1.00 35.89  ? 79  GLY A N   1 
ATOM   570  C CA  . GLY A 1 80  ? -7.214  -4.050  12.517 1.00 33.50  ? 79  GLY A CA  1 
ATOM   571  C C   . GLY A 1 80  ? -6.947  -4.735  11.195 1.00 42.26  ? 79  GLY A C   1 
ATOM   572  O O   . GLY A 1 80  ? -6.324  -4.128  10.308 1.00 30.73  ? 79  GLY A O   1 
ATOM   573  N N   . ASN A 1 81  ? -7.359  -5.987  10.996 1.00 47.76  ? 80  ASN A N   1 
ATOM   574  C CA  . ASN A 1 81  ? -6.964  -6.765  9.815  1.00 44.68  ? 80  ASN A CA  1 
ATOM   575  C C   . ASN A 1 81  ? -5.443  -6.971  9.808  1.00 61.60  ? 80  ASN A C   1 
ATOM   576  O O   . ASN A 1 81  ? -4.735  -6.327  10.595 1.00 94.73  ? 80  ASN A O   1 
ATOM   577  C CB  . ASN A 1 81  ? -7.445  -6.095  8.542  1.00 39.72  ? 80  ASN A CB  1 
ATOM   578  C CG  . ASN A 1 81  ? -8.519  -6.809  7.767  1.00 50.45  ? 80  ASN A CG  1 
ATOM   579  O OD1 . ASN A 1 81  ? -8.693  -6.560  6.570  1.00 51.19  ? 80  ASN A OD1 1 
ATOM   580  N ND2 . ASN A 1 81  ? -9.272  -7.697  8.400  1.00 70.12  ? 80  ASN A ND2 1 
ATOM   581  N N   . GLN A 1 82  ? -4.944  -7.848  8.961  1.00 66.34  ? 81  GLN A N   1 
ATOM   582  C CA  . GLN A 1 82  ? -3.573  -8.234  8.680  1.00 64.72  ? 81  GLN A CA  1 
ATOM   583  C C   . GLN A 1 82  ? -3.195  -9.577  9.323  1.00 40.28  ? 81  GLN A C   1 
ATOM   584  O O   . GLN A 1 82  ? -2.031  -9.978  9.227  1.00 30.22  ? 81  GLN A O   1 
ATOM   585  C CB  . GLN A 1 82  ? -2.551  -7.164  9.081  1.00 87.35  ? 81  GLN A CB  1 
ATOM   586  C CG  . GLN A 1 82  ? -2.071  -7.216  10.521 1.00 99.97  ? 81  GLN A CG  1 
ATOM   587  C CD  . GLN A 1 82  ? -0.706  -7.876  10.637 1.00 115.33 ? 81  GLN A CD  1 
ATOM   588  O OE1 . GLN A 1 82  ? -0.143  -7.974  11.728 1.00 142.85 ? 81  GLN A OE1 1 
ATOM   589  N NE2 . GLN A 1 82  ? -0.171  -8.339  9.508  1.00 122.12 ? 81  GLN A NE2 1 
ATOM   590  N N   . ILE A 1 83  ? -4.131  -10.263 9.947  1.00 32.09  ? 82  ILE A N   1 
ATOM   591  C CA  . ILE A 1 83  ? -4.083  -11.670 10.273 1.00 35.57  ? 82  ILE A CA  1 
ATOM   592  C C   . ILE A 1 83  ? -5.480  -12.274 10.085 1.00 38.42  ? 82  ILE A C   1 
ATOM   593  O O   . ILE A 1 83  ? -6.483  -11.562 10.081 1.00 38.26  ? 82  ILE A O   1 
ATOM   594  C CB  . ILE A 1 83  ? -3.629  -12.046 11.699 1.00 31.68  ? 82  ILE A CB  1 
ATOM   595  C CG1 . ILE A 1 83  ? -4.604  -11.644 12.808 1.00 27.69  ? 82  ILE A CG1 1 
ATOM   596  C CG2 . ILE A 1 83  ? -2.227  -11.528 11.985 1.00 22.25  ? 82  ILE A CG2 1 
ATOM   597  C CD1 . ILE A 1 83  ? -4.322  -12.333 14.137 1.00 26.90  ? 82  ILE A CD1 1 
ATOM   598  N N   . SER A 1 84  ? -5.544  -13.592 9.943  1.00 38.90  ? 83  SER A N   1 
ATOM   599  C CA  . SER A 1 84  ? -6.845  -14.227 9.795  1.00 41.10  ? 83  SER A CA  1 
ATOM   600  C C   . SER A 1 84  ? -7.468  -14.606 11.136 1.00 39.80  ? 83  SER A C   1 
ATOM   601  O O   . SER A 1 84  ? -6.794  -14.708 12.163 1.00 25.18  ? 83  SER A O   1 
ATOM   602  C CB  . SER A 1 84  ? -6.722  -15.489 8.935  1.00 44.09  ? 83  SER A CB  1 
ATOM   603  O OG  . SER A 1 84  ? -6.150  -16.519 9.736  1.00 60.15  ? 83  SER A OG  1 
ATOM   604  N N   . LEU A 1 85  ? -8.784  -14.815 11.068 1.00 29.40  ? 84  LEU A N   1 
ATOM   605  C CA  . LEU A 1 85  ? -9.547  -15.264 12.225 1.00 33.57  ? 84  LEU A CA  1 
ATOM   606  C C   . LEU A 1 85  ? -8.855  -16.486 12.811 1.00 37.63  ? 84  LEU A C   1 
ATOM   607  O O   . LEU A 1 85  ? -8.511  -16.539 13.981 1.00 43.02  ? 84  LEU A O   1 
ATOM   608  C CB  . LEU A 1 85  ? -10.980 -15.606 11.841 1.00 33.10  ? 84  LEU A CB  1 
ATOM   609  C CG  . LEU A 1 85  ? -12.120 -15.451 12.838 1.00 43.02  ? 84  LEU A CG  1 
ATOM   610  C CD1 . LEU A 1 85  ? -13.221 -16.462 12.527 1.00 27.50  ? 84  LEU A CD1 1 
ATOM   611  C CD2 . LEU A 1 85  ? -11.674 -15.614 14.283 1.00 31.87  ? 84  LEU A CD2 1 
ATOM   612  N N   . LEU A 1 86  ? -8.656  -17.494 11.961 1.00 34.76  ? 85  LEU A N   1 
ATOM   613  C CA  . LEU A 1 86  ? -8.094  -18.741 12.472 1.00 36.89  ? 85  LEU A CA  1 
ATOM   614  C C   . LEU A 1 86  ? -6.695  -18.537 13.042 1.00 33.36  ? 85  LEU A C   1 
ATOM   615  O O   . LEU A 1 86  ? -6.351  -19.156 14.053 1.00 33.59  ? 85  LEU A O   1 
ATOM   616  C CB  . LEU A 1 86  ? -8.068  -19.811 11.379 1.00 32.61  ? 85  LEU A CB  1 
ATOM   617  C CG  . LEU A 1 86  ? -9.153  -20.886 11.419 1.00 41.69  ? 85  LEU A CG  1 
ATOM   618  C CD1 . LEU A 1 86  ? -10.387 -20.414 12.167 1.00 42.63  ? 85  LEU A CD1 1 
ATOM   619  C CD2 . LEU A 1 86  ? -9.527  -21.318 10.002 1.00 42.98  ? 85  LEU A CD2 1 
ATOM   620  N N   . ARG A 1 87  ? -5.863  -17.706 12.423 1.00 35.47  ? 86  ARG A N   1 
ATOM   621  C CA  . ARG A 1 87  ? -4.514  -17.537 12.963 1.00 33.43  ? 86  ARG A CA  1 
ATOM   622  C C   . ARG A 1 87  ? -4.607  -16.996 14.389 1.00 35.58  ? 86  ARG A C   1 
ATOM   623  O O   . ARG A 1 87  ? -3.836  -17.348 15.271 1.00 38.23  ? 86  ARG A O   1 
ATOM   624  C CB  . ARG A 1 87  ? -3.666  -16.579 12.139 1.00 31.73  ? 86  ARG A CB  1 
ATOM   625  C CG  . ARG A 1 87  ? -2.305  -16.355 12.802 1.00 36.98  ? 86  ARG A CG  1 
ATOM   626  C CD  . ARG A 1 87  ? -1.411  -15.507 11.905 1.00 35.03  ? 86  ARG A CD  1 
ATOM   627  N NE  . ARG A 1 87  ? -1.351  -16.033 10.537 1.00 33.88  ? 86  ARG A NE  1 
ATOM   628  C CZ  . ARG A 1 87  ? -0.359  -16.808 10.109 1.00 38.24  ? 86  ARG A CZ  1 
ATOM   629  N NH1 . ARG A 1 87  ? 0.617   -17.125 10.957 1.00 19.72  ? 86  ARG A NH1 1 
ATOM   630  N NH2 . ARG A 1 87  ? -0.321  -17.273 8.865  1.00 37.98  ? 86  ARG A NH2 1 
ATOM   631  N N   . ALA A 1 88  ? -5.624  -16.148 14.528 1.00 28.58  ? 87  ALA A N   1 
ATOM   632  C CA  . ALA A 1 88  ? -5.942  -15.543 15.804 1.00 32.18  ? 87  ALA A CA  1 
ATOM   633  C C   . ALA A 1 88  ? -6.343  -16.614 16.824 1.00 32.96  ? 87  ALA A C   1 
ATOM   634  O O   . ALA A 1 88  ? -5.822  -16.567 17.942 1.00 37.78  ? 87  ALA A O   1 
ATOM   635  C CB  . ALA A 1 88  ? -7.024  -14.480 15.654 1.00 33.12  ? 87  ALA A CB  1 
ATOM   636  N N   . PHE A 1 89  ? -7.218  -17.545 16.460 1.00 32.43  ? 88  PHE A N   1 
ATOM   637  C CA  . PHE A 1 89  ? -7.687  -18.598 17.357 1.00 35.49  ? 88  PHE A CA  1 
ATOM   638  C C   . PHE A 1 89  ? -6.550  -19.433 17.937 1.00 31.56  ? 88  PHE A C   1 
ATOM   639  O O   . PHE A 1 89  ? -6.404  -19.589 19.154 1.00 31.49  ? 88  PHE A O   1 
ATOM   640  C CB  . PHE A 1 89  ? -8.678  -19.542 16.644 1.00 38.01  ? 88  PHE A CB  1 
ATOM   641  C CG  . PHE A 1 89  ? -8.757  -20.897 17.347 1.00 43.48  ? 88  PHE A CG  1 
ATOM   642  C CD1 . PHE A 1 89  ? -9.372  -21.015 18.583 1.00 48.50  ? 88  PHE A CD1 1 
ATOM   643  C CD2 . PHE A 1 89  ? -8.208  -22.032 16.776 1.00 42.70  ? 88  PHE A CD2 1 
ATOM   644  C CE1 . PHE A 1 89  ? -9.435  -22.235 19.234 1.00 47.68  ? 88  PHE A CE1 1 
ATOM   645  C CE2 . PHE A 1 89  ? -8.269  -23.258 17.410 1.00 41.64  ? 88  PHE A CE2 1 
ATOM   646  C CZ  . PHE A 1 89  ? -8.883  -23.359 18.647 1.00 46.42  ? 88  PHE A CZ  1 
ATOM   647  N N   . PHE A 1 90  ? -5.732  -20.006 17.052 1.00 36.20  ? 89  PHE A N   1 
ATOM   648  C CA  . PHE A 1 90  ? -4.621  -20.820 17.536 1.00 43.49  ? 89  PHE A CA  1 
ATOM   649  C C   . PHE A 1 90  ? -3.570  -19.965 18.223 1.00 37.01  ? 89  PHE A C   1 
ATOM   650  O O   . PHE A 1 90  ? -2.896  -20.431 19.137 1.00 46.19  ? 89  PHE A O   1 
ATOM   651  C CB  . PHE A 1 90  ? -3.973  -21.604 16.392 1.00 46.07  ? 89  PHE A CB  1 
ATOM   652  C CG  . PHE A 1 90  ? -4.993  -22.413 15.605 1.00 63.95  ? 89  PHE A CG  1 
ATOM   653  C CD1 . PHE A 1 90  ? -5.219  -23.744 15.913 1.00 67.06  ? 89  PHE A CD1 1 
ATOM   654  C CD2 . PHE A 1 90  ? -5.701  -21.821 14.575 1.00 72.21  ? 89  PHE A CD2 1 
ATOM   655  C CE1 . PHE A 1 90  ? -6.149  -24.464 15.188 1.00 72.54  ? 89  PHE A CE1 1 
ATOM   656  C CE2 . PHE A 1 90  ? -6.631  -22.537 13.846 1.00 74.63  ? 89  PHE A CE2 1 
ATOM   657  C CZ  . PHE A 1 90  ? -6.850  -23.865 14.157 1.00 74.22  ? 89  PHE A CZ  1 
ATOM   658  N N   . TYR A 1 91  ? -3.399  -18.710 17.797 1.00 38.75  ? 90  TYR A N   1 
ATOM   659  C CA  . TYR A 1 91  ? -2.377  -17.929 18.496 1.00 35.65  ? 90  TYR A CA  1 
ATOM   660  C C   . TYR A 1 91  ? -2.782  -17.703 19.952 1.00 24.19  ? 90  TYR A C   1 
ATOM   661  O O   . TYR A 1 91  ? -1.970  -17.918 20.846 1.00 33.60  ? 90  TYR A O   1 
ATOM   662  C CB  . TYR A 1 91  ? -2.115  -16.593 17.809 1.00 38.17  ? 90  TYR A CB  1 
ATOM   663  C CG  . TYR A 1 91  ? -1.027  -16.651 16.757 1.00 36.49  ? 90  TYR A CG  1 
ATOM   664  C CD1 . TYR A 1 91  ? -0.766  -17.844 16.080 1.00 36.97  ? 90  TYR A CD1 1 
ATOM   665  C CD2 . TYR A 1 91  ? -0.274  -15.531 16.439 1.00 34.46  ? 90  TYR A CD2 1 
ATOM   666  C CE1 . TYR A 1 91  ? 0.224   -17.913 15.118 1.00 32.76  ? 90  TYR A CE1 1 
ATOM   667  C CE2 . TYR A 1 91  ? 0.719   -15.597 15.468 1.00 36.96  ? 90  TYR A CE2 1 
ATOM   668  C CZ  . TYR A 1 91  ? 0.963   -16.788 14.811 1.00 26.51  ? 90  TYR A CZ  1 
ATOM   669  O OH  . TYR A 1 91  ? 1.946   -16.854 13.851 1.00 38.98  ? 90  TYR A OH  1 
ATOM   670  N N   . VAL A 1 92  ? -4.016  -17.263 20.149 1.00 24.91  ? 91  VAL A N   1 
ATOM   671  C CA  . VAL A 1 92  ? -4.516  -17.001 21.487 1.00 25.23  ? 91  VAL A CA  1 
ATOM   672  C C   . VAL A 1 92  ? -4.599  -18.281 22.301 1.00 37.52  ? 91  VAL A C   1 
ATOM   673  O O   . VAL A 1 92  ? -4.497  -18.292 23.527 1.00 50.03  ? 91  VAL A O   1 
ATOM   674  C CB  . VAL A 1 92  ? -5.928  -16.396 21.458 1.00 22.62  ? 91  VAL A CB  1 
ATOM   675  C CG1 . VAL A 1 92  ? -6.464  -16.411 22.878 1.00 31.30  ? 91  VAL A CG1 1 
ATOM   676  C CG2 . VAL A 1 92  ? -5.903  -15.002 20.860 1.00 28.21  ? 91  VAL A CG2 1 
ATOM   677  N N   . ALA A 1 93  ? -4.797  -19.391 21.582 1.00 30.00  ? 92  ALA A N   1 
ATOM   678  C CA  . ALA A 1 93  ? -4.879  -20.666 22.301 1.00 33.71  ? 92  ALA A CA  1 
ATOM   679  C C   . ALA A 1 93  ? -3.496  -21.076 22.797 1.00 42.53  ? 92  ALA A C   1 
ATOM   680  O O   . ALA A 1 93  ? -3.337  -21.664 23.865 1.00 37.62  ? 92  ALA A O   1 
ATOM   681  C CB  . ALA A 1 93  ? -5.453  -21.741 21.399 1.00 46.06  ? 92  ALA A CB  1 
ATOM   682  N N   . ALA A 1 94  ? -2.509  -20.742 21.960 1.00 32.82  ? 93  ALA A N   1 
ATOM   683  C CA  . ALA A 1 94  ? -1.135  -21.170 22.162 1.00 29.79  ? 93  ALA A CA  1 
ATOM   684  C C   . ALA A 1 94  ? -0.478  -20.327 23.251 1.00 24.17  ? 93  ALA A C   1 
ATOM   685  O O   . ALA A 1 94  ? 0.374   -20.869 23.944 1.00 27.29  ? 93  ALA A O   1 
ATOM   686  C CB  . ALA A 1 94  ? -0.323  -21.077 20.877 1.00 37.26  ? 93  ALA A CB  1 
ATOM   687  N N   . GLN A 1 95  ? -0.911  -19.074 23.302 1.00 20.77  ? 94  GLN A N   1 
ATOM   688  C CA  . GLN A 1 95  ? -0.418  -18.114 24.296 1.00 26.54  ? 94  GLN A CA  1 
ATOM   689  C C   . GLN A 1 95  ? -0.897  -18.499 25.693 1.00 22.53  ? 94  GLN A C   1 
ATOM   690  O O   . GLN A 1 95  ? -0.174  -18.574 26.688 1.00 25.26  ? 94  GLN A O   1 
ATOM   691  C CB  . GLN A 1 95  ? -0.845  -16.698 23.903 1.00 24.20  ? 94  GLN A CB  1 
ATOM   692  C CG  . GLN A 1 95  ? -0.297  -16.240 22.543 1.00 24.32  ? 94  GLN A CG  1 
ATOM   693  C CD  . GLN A 1 95  ? -1.148  -15.141 21.935 1.00 29.12  ? 94  GLN A CD  1 
ATOM   694  O OE1 . GLN A 1 95  ? -0.812  -14.490 20.950 1.00 22.88  ? 94  GLN A OE1 1 
ATOM   695  N NE2 . GLN A 1 95  ? -2.309  -14.936 22.549 1.00 32.06  ? 94  GLN A NE2 1 
ATOM   696  N N   . LEU A 1 96  ? -2.195  -18.796 25.779 1.00 21.98  ? 95  LEU A N   1 
ATOM   697  C CA  . LEU A 1 96  ? -2.755  -19.247 27.049 1.00 34.25  ? 95  LEU A CA  1 
ATOM   698  C C   . LEU A 1 96  ? -2.129  -20.569 27.446 1.00 34.90  ? 95  LEU A C   1 
ATOM   699  O O   . LEU A 1 96  ? -1.815  -20.749 28.627 1.00 30.37  ? 95  LEU A O   1 
ATOM   700  C CB  . LEU A 1 96  ? -4.284  -19.319 26.955 1.00 38.67  ? 95  LEU A CB  1 
ATOM   701  C CG  . LEU A 1 96  ? -4.972  -18.004 26.558 1.00 37.93  ? 95  LEU A CG  1 
ATOM   702  C CD1 . LEU A 1 96  ? -6.427  -18.226 26.191 1.00 25.27  ? 95  LEU A CD1 1 
ATOM   703  C CD2 . LEU A 1 96  ? -4.884  -16.963 27.670 1.00 26.29  ? 95  LEU A CD2 1 
ATOM   704  N N   . VAL A 1 97  ? -1.891  -21.503 26.516 1.00 28.40  ? 96  VAL A N   1 
ATOM   705  C CA  . VAL A 1 97  ? -1.263  -22.738 26.981 1.00 30.10  ? 96  VAL A CA  1 
ATOM   706  C C   . VAL A 1 97  ? 0.193   -22.550 27.368 1.00 32.46  ? 96  VAL A C   1 
ATOM   707  O O   . VAL A 1 97  ? 0.716   -23.191 28.289 1.00 34.06  ? 96  VAL A O   1 
ATOM   708  C CB  . VAL A 1 97  ? -1.285  -23.875 25.942 1.00 32.53  ? 96  VAL A CB  1 
ATOM   709  C CG1 . VAL A 1 97  ? -0.424  -25.032 26.449 1.00 26.39  ? 96  VAL A CG1 1 
ATOM   710  C CG2 . VAL A 1 97  ? -2.719  -24.294 25.686 1.00 55.43  ? 96  VAL A CG2 1 
ATOM   711  N N   . GLY A 1 98  ? 0.907   -21.681 26.656 1.00 24.52  ? 97  GLY A N   1 
ATOM   712  C CA  . GLY A 1 98  ? 2.326   -21.608 27.051 1.00 24.33  ? 97  GLY A CA  1 
ATOM   713  C C   . GLY A 1 98  ? 2.417   -20.855 28.367 1.00 17.42  ? 97  GLY A C   1 
ATOM   714  O O   . GLY A 1 98  ? 3.283   -21.132 29.196 1.00 28.18  ? 97  GLY A O   1 
ATOM   715  N N   . ALA A 1 99  ? 1.499   -19.898 28.523 1.00 21.89  ? 98  ALA A N   1 
ATOM   716  C CA  . ALA A 1 99  ? 1.524   -19.125 29.775 1.00 22.16  ? 98  ALA A CA  1 
ATOM   717  C C   . ALA A 1 99  ? 1.380   -20.079 30.951 1.00 19.78  ? 98  ALA A C   1 
ATOM   718  O O   . ALA A 1 99  ? 2.139   -20.044 31.922 1.00 21.01  ? 98  ALA A O   1 
ATOM   719  C CB  . ALA A 1 99  ? 0.451   -18.059 29.755 1.00 14.23  ? 98  ALA A CB  1 
ATOM   720  N N   . ILE A 1 100 ? 0.386   -20.958 30.832 1.00 28.96  ? 99  ILE A N   1 
ATOM   721  C CA  . ILE A 1 100 ? 0.194   -21.987 31.855 1.00 30.29  ? 99  ILE A CA  1 
ATOM   722  C C   . ILE A 1 100 ? 1.430   -22.874 31.902 1.00 31.90  ? 99  ILE A C   1 
ATOM   723  O O   . ILE A 1 100 ? 1.971   -23.212 32.958 1.00 29.47  ? 99  ILE A O   1 
ATOM   724  C CB  . ILE A 1 100 ? -1.065  -22.834 31.595 1.00 27.27  ? 99  ILE A CB  1 
ATOM   725  C CG1 . ILE A 1 100 ? -2.381  -22.072 31.715 1.00 24.79  ? 99  ILE A CG1 1 
ATOM   726  C CG2 . ILE A 1 100 ? -1.057  -24.059 32.502 1.00 27.71  ? 99  ILE A CG2 1 
ATOM   727  C CD1 . ILE A 1 100 ? -3.507  -22.522 30.808 1.00 18.21  ? 99  ILE A CD1 1 
ATOM   728  N N   . ALA A 1 101 ? 1.892   -23.259 30.700 1.00 23.56  ? 100 ALA A N   1 
ATOM   729  C CA  . ALA A 1 101 ? 3.090   -24.071 30.620 1.00 23.29  ? 100 ALA A CA  1 
ATOM   730  C C   . ALA A 1 101 ? 4.260   -23.427 31.362 1.00 27.74  ? 100 ALA A C   1 
ATOM   731  O O   . ALA A 1 101 ? 4.912   -24.154 32.121 1.00 23.22  ? 100 ALA A O   1 
ATOM   732  C CB  . ALA A 1 101 ? 3.467   -24.339 29.172 1.00 37.42  ? 100 ALA A CB  1 
ATOM   733  N N   . GLY A 1 102 ? 4.542   -22.145 31.159 1.00 27.93  ? 101 GLY A N   1 
ATOM   734  C CA  . GLY A 1 102 ? 5.650   -21.449 31.788 1.00 32.08  ? 101 GLY A CA  1 
ATOM   735  C C   . GLY A 1 102 ? 5.552   -21.177 33.282 1.00 22.93  ? 101 GLY A C   1 
ATOM   736  O O   . GLY A 1 102 ? 6.536   -21.234 34.032 1.00 13.21  ? 101 GLY A O   1 
ATOM   737  N N   . ALA A 1 103 ? 4.358   -20.851 33.743 1.00 15.86  ? 102 ALA A N   1 
ATOM   738  C CA  . ALA A 1 103 ? 4.022   -20.685 35.159 1.00 20.60  ? 102 ALA A CA  1 
ATOM   739  C C   . ALA A 1 103 ? 4.235   -21.994 35.910 1.00 19.79  ? 102 ALA A C   1 
ATOM   740  O O   . ALA A 1 103 ? 4.789   -22.004 37.003 1.00 28.29  ? 102 ALA A O   1 
ATOM   741  C CB  . ALA A 1 103 ? 2.591   -20.193 35.282 1.00 14.34  ? 102 ALA A CB  1 
ATOM   742  N N   . GLY A 1 104 ? 3.822   -23.104 35.300 1.00 20.21  ? 103 GLY A N   1 
ATOM   743  C CA  . GLY A 1 104 ? 4.033   -24.430 35.860 1.00 15.32  ? 103 GLY A CA  1 
ATOM   744  C C   . GLY A 1 104 ? 5.493   -24.759 36.024 1.00 23.54  ? 103 GLY A C   1 
ATOM   745  O O   . GLY A 1 104 ? 5.905   -25.269 37.055 1.00 28.57  ? 103 GLY A O   1 
ATOM   746  N N   . ILE A 1 105 ? 6.317   -24.484 35.008 1.00 23.97  ? 104 ILE A N   1 
ATOM   747  C CA  . ILE A 1 105 ? 7.722   -24.845 35.107 1.00 17.07  ? 104 ILE A CA  1 
ATOM   748  C C   . ILE A 1 105 ? 8.429   -24.012 36.155 1.00 20.53  ? 104 ILE A C   1 
ATOM   749  O O   . ILE A 1 105 ? 9.365   -24.422 36.849 1.00 29.77  ? 104 ILE A O   1 
ATOM   750  C CB  . ILE A 1 105 ? 8.457   -24.653 33.770 1.00 33.19  ? 104 ILE A CB  1 
ATOM   751  C CG1 . ILE A 1 105 ? 7.890   -25.439 32.592 1.00 25.44  ? 104 ILE A CG1 1 
ATOM   752  C CG2 . ILE A 1 105 ? 9.929   -24.974 34.000 1.00 35.53  ? 104 ILE A CG2 1 
ATOM   753  C CD1 . ILE A 1 105 ? 7.568   -24.613 31.372 1.00 34.86  ? 104 ILE A CD1 1 
ATOM   754  N N   . LEU A 1 106 ? 7.990   -22.759 36.308 1.00 26.60  ? 105 LEU A N   1 
ATOM   755  C CA  . LEU A 1 106 ? 8.592   -22.012 37.426 1.00 15.95  ? 105 LEU A CA  1 
ATOM   756  C C   . LEU A 1 106 ? 8.182   -22.653 38.753 1.00 20.08  ? 105 LEU A C   1 
ATOM   757  O O   . LEU A 1 106 ? 9.049   -22.803 39.618 1.00 31.68  ? 105 LEU A O   1 
ATOM   758  C CB  . LEU A 1 106 ? 8.174   -20.561 37.383 1.00 17.71  ? 105 LEU A CB  1 
ATOM   759  C CG  . LEU A 1 106 ? 8.862   -19.550 38.289 1.00 19.92  ? 105 LEU A CG  1 
ATOM   760  C CD1 . LEU A 1 106 ? 10.341  -19.419 37.949 1.00 18.29  ? 105 LEU A CD1 1 
ATOM   761  C CD2 . LEU A 1 106 ? 8.118   -18.230 38.169 1.00 23.41  ? 105 LEU A CD2 1 
ATOM   762  N N   . TYR A 1 107 ? 6.913   -23.018 38.899 1.00 29.59  ? 106 TYR A N   1 
ATOM   763  C CA  . TYR A 1 107 ? 6.410   -23.597 40.148 1.00 28.27  ? 106 TYR A CA  1 
ATOM   764  C C   . TYR A 1 107 ? 7.296   -24.778 40.538 1.00 30.41  ? 106 TYR A C   1 
ATOM   765  O O   . TYR A 1 107 ? 7.792   -24.897 41.655 1.00 30.27  ? 106 TYR A O   1 
ATOM   766  C CB  . TYR A 1 107 ? 4.962   -24.068 40.023 1.00 23.22  ? 106 TYR A CB  1 
ATOM   767  C CG  . TYR A 1 107 ? 4.369   -24.633 41.296 1.00 33.07  ? 106 TYR A CG  1 
ATOM   768  C CD1 . TYR A 1 107 ? 3.731   -23.820 42.232 1.00 48.45  ? 106 TYR A CD1 1 
ATOM   769  C CD2 . TYR A 1 107 ? 4.423   -25.986 41.603 1.00 32.14  ? 106 TYR A CD2 1 
ATOM   770  C CE1 . TYR A 1 107 ? 3.186   -24.336 43.398 1.00 42.89  ? 106 TYR A CE1 1 
ATOM   771  C CE2 . TYR A 1 107 ? 3.891   -26.527 42.756 1.00 31.96  ? 106 TYR A CE2 1 
ATOM   772  C CZ  . TYR A 1 107 ? 3.268   -25.690 43.658 1.00 43.99  ? 106 TYR A CZ  1 
ATOM   773  O OH  . TYR A 1 107 ? 2.731   -26.217 44.813 1.00 60.12  ? 106 TYR A OH  1 
ATOM   774  N N   . GLY A 1 108 ? 7.458   -25.642 39.534 1.00 26.02  ? 107 GLY A N   1 
ATOM   775  C CA  . GLY A 1 108 ? 8.321   -26.797 39.644 1.00 27.73  ? 107 GLY A CA  1 
ATOM   776  C C   . GLY A 1 108 ? 9.721   -26.441 40.096 1.00 41.08  ? 107 GLY A C   1 
ATOM   777  O O   . GLY A 1 108 ? 10.414  -27.205 40.769 1.00 57.34  ? 107 GLY A O   1 
ATOM   778  N N   . VAL A 1 109 ? 10.179  -25.247 39.726 1.00 35.30  ? 108 VAL A N   1 
ATOM   779  C CA  . VAL A 1 109 ? 11.607  -24.937 39.880 1.00 25.87  ? 108 VAL A CA  1 
ATOM   780  C C   . VAL A 1 109 ? 11.841  -24.012 41.051 1.00 23.51  ? 108 VAL A C   1 
ATOM   781  O O   . VAL A 1 109 ? 12.869  -24.083 41.736 1.00 28.15  ? 108 VAL A O   1 
ATOM   782  C CB  . VAL A 1 109 ? 12.043  -24.427 38.486 1.00 37.79  ? 108 VAL A CB  1 
ATOM   783  C CG1 . VAL A 1 109 ? 12.637  -23.039 38.499 1.00 16.36  ? 108 VAL A CG1 1 
ATOM   784  C CG2 . VAL A 1 109 ? 13.001  -25.441 37.862 1.00 28.31  ? 108 VAL A CG2 1 
ATOM   785  N N   . ALA A 1 110 ? 10.888  -23.137 41.359 1.00 17.01  ? 109 ALA A N   1 
ATOM   786  C CA  . ALA A 1 110 ? 11.015  -22.153 42.420 1.00 26.13  ? 109 ALA A CA  1 
ATOM   787  C C   . ALA A 1 110 ? 11.055  -22.749 43.827 1.00 30.27  ? 109 ALA A C   1 
ATOM   788  O O   . ALA A 1 110 ? 10.200  -23.558 44.202 1.00 37.67  ? 109 ALA A O   1 
ATOM   789  C CB  . ALA A 1 110 ? 9.848   -21.157 42.375 1.00 21.75  ? 109 ALA A CB  1 
ATOM   790  N N   . PRO A 1 111 ? 12.037  -22.340 44.617 1.00 27.27  ? 110 PRO A N   1 
ATOM   791  C CA  . PRO A 1 111 ? 12.098  -22.723 46.030 1.00 41.92  ? 110 PRO A CA  1 
ATOM   792  C C   . PRO A 1 111 ? 10.943  -22.143 46.859 1.00 46.79  ? 110 PRO A C   1 
ATOM   793  O O   . PRO A 1 111 ? 10.447  -21.035 46.650 1.00 32.41  ? 110 PRO A O   1 
ATOM   794  C CB  . PRO A 1 111 ? 13.429  -22.144 46.521 1.00 37.50  ? 110 PRO A CB  1 
ATOM   795  C CG  . PRO A 1 111 ? 13.758  -21.067 45.552 1.00 39.03  ? 110 PRO A CG  1 
ATOM   796  C CD  . PRO A 1 111 ? 13.181  -21.502 44.230 1.00 32.62  ? 110 PRO A CD  1 
ATOM   797  N N   . LEU A 1 112 ? 10.535  -22.961 47.830 1.00 33.86  ? 111 LEU A N   1 
ATOM   798  C CA  . LEU A 1 112 ? 9.416   -22.703 48.718 1.00 36.96  ? 111 LEU A CA  1 
ATOM   799  C C   . LEU A 1 112 ? 9.418   -21.276 49.239 1.00 22.97  ? 111 LEU A C   1 
ATOM   800  O O   . LEU A 1 112 ? 8.425   -20.554 49.188 1.00 24.29  ? 111 LEU A O   1 
ATOM   801  C CB  . LEU A 1 112 ? 9.414   -23.691 49.904 1.00 23.71  ? 111 LEU A CB  1 
ATOM   802  C CG  . LEU A 1 112 ? 9.122   -25.146 49.517 1.00 26.40  ? 111 LEU A CG  1 
ATOM   803  C CD1 . LEU A 1 112 ? 9.413   -26.093 50.661 1.00 31.89  ? 111 LEU A CD1 1 
ATOM   804  C CD2 . LEU A 1 112 ? 7.673   -25.292 49.059 1.00 50.93  ? 111 LEU A CD2 1 
ATOM   805  N N   . ASN A 1 113 ? 10.553  -20.833 49.757 1.00 18.67  ? 112 ASN A N   1 
ATOM   806  C CA  . ASN A 1 113 ? 10.551  -19.538 50.437 1.00 25.27  ? 112 ASN A CA  1 
ATOM   807  C C   . ASN A 1 113 ? 10.410  -18.354 49.494 1.00 34.08  ? 112 ASN A C   1 
ATOM   808  O O   . ASN A 1 113 ? 10.403  -17.186 49.906 1.00 25.18  ? 112 ASN A O   1 
ATOM   809  C CB  . ASN A 1 113 ? 11.844  -19.477 51.259 1.00 37.12  ? 112 ASN A CB  1 
ATOM   810  C CG  . ASN A 1 113 ? 13.077  -19.496 50.375 1.00 35.02  ? 112 ASN A CG  1 
ATOM   811  O OD1 . ASN A 1 113 ? 13.008  -19.909 49.222 1.00 60.34  ? 112 ASN A OD1 1 
ATOM   812  N ND2 . ASN A 1 113 ? 14.206  -19.043 50.911 1.00 51.21  ? 112 ASN A ND2 1 
ATOM   813  N N   . ALA A 1 114 ? 10.274  -18.606 48.192 1.00 29.52  ? 113 ALA A N   1 
ATOM   814  C CA  . ALA A 1 114 ? 10.162  -17.510 47.238 1.00 21.83  ? 113 ALA A CA  1 
ATOM   815  C C   . ALA A 1 114 ? 8.967   -17.679 46.312 1.00 37.35  ? 113 ALA A C   1 
ATOM   816  O O   . ALA A 1 114 ? 8.483   -16.710 45.723 1.00 43.56  ? 113 ALA A O   1 
ATOM   817  C CB  . ALA A 1 114 ? 11.461  -17.428 46.443 1.00 27.81  ? 113 ALA A CB  1 
ATOM   818  N N   . ARG A 1 115 ? 8.492   -18.911 46.172 1.00 38.30  ? 114 ARG A N   1 
ATOM   819  C CA  . ARG A 1 115 ? 7.358   -19.253 45.326 1.00 38.50  ? 114 ARG A CA  1 
ATOM   820  C C   . ARG A 1 115 ? 6.160   -18.338 45.552 1.00 36.80  ? 114 ARG A C   1 
ATOM   821  O O   . ARG A 1 115 ? 5.632   -17.702 44.634 1.00 26.51  ? 114 ARG A O   1 
ATOM   822  C CB  . ARG A 1 115 ? 6.977   -20.701 45.616 1.00 49.12  ? 114 ARG A CB  1 
ATOM   823  C CG  . ARG A 1 115 ? 6.577   -21.591 44.460 1.00 63.41  ? 114 ARG A CG  1 
ATOM   824  C CD  . ARG A 1 115 ? 6.074   -22.944 44.953 1.00 80.12  ? 114 ARG A CD  1 
ATOM   825  N NE  . ARG A 1 115 ? 6.870   -24.073 44.482 1.00 89.26  ? 114 ARG A NE  1 
ATOM   826  C CZ  . ARG A 1 115 ? 6.991   -25.255 45.073 1.00 93.43  ? 114 ARG A CZ  1 
ATOM   827  N NH1 . ARG A 1 115 ? 7.760   -26.192 44.523 1.00 101.39 ? 114 ARG A NH1 1 
ATOM   828  N NH2 . ARG A 1 115 ? 6.353   -25.527 46.207 1.00 86.09  ? 114 ARG A NH2 1 
ATOM   829  N N   . GLY A 1 116 ? 5.688   -18.271 46.801 1.00 33.96  ? 115 GLY A N   1 
ATOM   830  C CA  . GLY A 1 116 ? 4.475   -17.496 47.098 1.00 25.85  ? 115 GLY A CA  1 
ATOM   831  C C   . GLY A 1 116 ? 3.307   -18.219 46.443 1.00 37.28  ? 115 GLY A C   1 
ATOM   832  O O   . GLY A 1 116 ? 3.216   -19.447 46.680 1.00 58.95  ? 115 GLY A O   1 
ATOM   833  N N   . ASN A 1 117 ? 2.453   -17.652 45.674 1.00 42.51  ? 116 ASN A N   1 
ATOM   834  C CA  . ASN A 1 117 ? 2.011   -16.495 44.976 1.00 51.27  ? 116 ASN A CA  1 
ATOM   835  C C   . ASN A 1 117 ? 2.277   -16.635 43.467 1.00 36.76  ? 116 ASN A C   1 
ATOM   836  O O   . ASN A 1 117 ? 1.393   -16.399 42.636 1.00 26.60  ? 116 ASN A O   1 
ATOM   837  C CB  . ASN A 1 117 ? 2.680   -15.228 45.522 1.00 75.80  ? 116 ASN A CB  1 
ATOM   838  C CG  . ASN A 1 117 ? 2.343   -13.964 44.775 1.00 95.09  ? 116 ASN A CG  1 
ATOM   839  O OD1 . ASN A 1 117 ? 1.174   -13.591 44.662 1.00 117.34 ? 116 ASN A OD1 1 
ATOM   840  N ND2 . ASN A 1 117 ? 3.374   -13.280 44.258 1.00 107.67 ? 116 ASN A ND2 1 
ATOM   841  N N   . LEU A 1 118 ? 3.502   -17.011 43.120 1.00 28.21  ? 117 LEU A N   1 
ATOM   842  C CA  . LEU A 1 118 ? 3.900   -17.101 41.710 1.00 27.53  ? 117 LEU A CA  1 
ATOM   843  C C   . LEU A 1 118 ? 3.609   -15.839 40.911 1.00 22.53  ? 117 LEU A C   1 
ATOM   844  O O   . LEU A 1 118 ? 3.409   -15.866 39.690 1.00 25.54  ? 117 LEU A O   1 
ATOM   845  C CB  . LEU A 1 118 ? 3.235   -18.316 41.049 1.00 23.55  ? 117 LEU A CB  1 
ATOM   846  C CG  . LEU A 1 118 ? 4.086   -18.995 39.962 1.00 29.40  ? 117 LEU A CG  1 
ATOM   847  C CD1 . LEU A 1 118 ? 5.306   -19.646 40.597 1.00 18.66  ? 117 LEU A CD1 1 
ATOM   848  C CD2 . LEU A 1 118 ? 3.275   -19.997 39.154 1.00 21.58  ? 117 LEU A CD2 1 
ATOM   849  N N   . ALA A 1 119 ? 3.596   -14.673 41.545 1.00 22.76  ? 118 ALA A N   1 
ATOM   850  C CA  . ALA A 1 119 ? 3.528   -13.385 40.854 1.00 24.38  ? 118 ALA A CA  1 
ATOM   851  C C   . ALA A 1 119 ? 2.263   -13.193 40.032 1.00 24.39  ? 118 ALA A C   1 
ATOM   852  O O   . ALA A 1 119 ? 2.220   -12.605 38.956 1.00 24.07  ? 118 ALA A O   1 
ATOM   853  C CB  . ALA A 1 119 ? 4.764   -13.163 39.984 1.00 18.90  ? 118 ALA A CB  1 
ATOM   854  N N   . VAL A 1 120 ? 1.142   -13.649 40.574 1.00 26.22  ? 119 VAL A N   1 
ATOM   855  C CA  . VAL A 1 120 ? -0.166  -13.327 40.017 1.00 27.79  ? 119 VAL A CA  1 
ATOM   856  C C   . VAL A 1 120 ? -0.418  -11.833 39.941 1.00 24.05  ? 119 VAL A C   1 
ATOM   857  O O   . VAL A 1 120 ? 0.102   -11.005 40.700 1.00 26.62  ? 119 VAL A O   1 
ATOM   858  C CB  . VAL A 1 120 ? -1.230  -14.017 40.906 1.00 37.04  ? 119 VAL A CB  1 
ATOM   859  C CG1 . VAL A 1 120 ? -2.616  -13.455 40.678 1.00 35.01  ? 119 VAL A CG1 1 
ATOM   860  C CG2 . VAL A 1 120 ? -1.211  -15.520 40.645 1.00 37.80  ? 119 VAL A CG2 1 
ATOM   861  N N   . ASN A 1 121 ? -1.251  -11.376 39.007 1.00 22.27  ? 120 ASN A N   1 
ATOM   862  C CA  . ASN A 1 121 ? -1.692  -9.988  39.059 1.00 25.63  ? 120 ASN A CA  1 
ATOM   863  C C   . ASN A 1 121 ? -2.672  -9.784  40.212 1.00 33.99  ? 120 ASN A C   1 
ATOM   864  O O   . ASN A 1 121 ? -3.340  -10.755 40.594 1.00 40.26  ? 120 ASN A O   1 
ATOM   865  C CB  . ASN A 1 121 ? -2.366  -9.614  37.738 1.00 24.05  ? 120 ASN A CB  1 
ATOM   866  C CG  . ASN A 1 121 ? -1.293  -9.258  36.718 1.00 26.55  ? 120 ASN A CG  1 
ATOM   867  O OD1 . ASN A 1 121 ? -1.099  -9.989  35.754 1.00 39.62  ? 120 ASN A OD1 1 
ATOM   868  N ND2 . ASN A 1 121 ? -0.619  -8.145  36.968 1.00 26.61  ? 120 ASN A ND2 1 
ATOM   869  N N   . ALA A 1 122 ? -2.788  -8.589  40.768 1.00 25.58  ? 121 ALA A N   1 
ATOM   870  C CA  . ALA A 1 122 ? -3.641  -8.346  41.937 1.00 31.90  ? 121 ALA A CA  1 
ATOM   871  C C   . ALA A 1 122 ? -3.855  -6.851  42.119 1.00 25.72  ? 121 ALA A C   1 
ATOM   872  O O   . ALA A 1 122 ? -2.875  -6.112  42.174 1.00 43.41  ? 121 ALA A O   1 
ATOM   873  C CB  . ALA A 1 122 ? -3.053  -8.921  43.224 1.00 18.44  ? 121 ALA A CB  1 
ATOM   874  N N   . LEU A 1 123 ? -5.088  -6.386  42.200 1.00 28.85  ? 122 LEU A N   1 
ATOM   875  C CA  . LEU A 1 123 ? -5.359  -4.972  42.396 1.00 33.50  ? 122 LEU A CA  1 
ATOM   876  C C   . LEU A 1 123 ? -4.702  -4.392  43.644 1.00 33.18  ? 122 LEU A C   1 
ATOM   877  O O   . LEU A 1 123 ? -4.617  -5.029  44.682 1.00 33.21  ? 122 LEU A O   1 
ATOM   878  C CB  . LEU A 1 123 ? -6.867  -4.740  42.519 1.00 32.41  ? 122 LEU A CB  1 
ATOM   879  C CG  . LEU A 1 123 ? -7.640  -4.633  41.210 1.00 44.05  ? 122 LEU A CG  1 
ATOM   880  C CD1 . LEU A 1 123 ? -8.759  -3.617  41.360 1.00 35.26  ? 122 LEU A CD1 1 
ATOM   881  C CD2 . LEU A 1 123 ? -6.701  -4.280  40.066 1.00 55.99  ? 122 LEU A CD2 1 
ATOM   882  N N   . ASN A 1 124 ? -4.248  -3.147  43.527 1.00 46.05  ? 123 ASN A N   1 
ATOM   883  C CA  . ASN A 1 124 ? -3.909  -2.358  44.696 1.00 46.08  ? 123 ASN A CA  1 
ATOM   884  C C   . ASN A 1 124 ? -5.145  -2.305  45.588 1.00 48.82  ? 123 ASN A C   1 
ATOM   885  O O   . ASN A 1 124 ? -6.253  -2.042  45.089 1.00 31.67  ? 123 ASN A O   1 
ATOM   886  C CB  . ASN A 1 124 ? -3.492  -0.929  44.346 1.00 48.37  ? 123 ASN A CB  1 
ATOM   887  C CG  . ASN A 1 124 ? -2.976  -0.219  45.593 1.00 61.34  ? 123 ASN A CG  1 
ATOM   888  O OD1 . ASN A 1 124 ? -3.580  0.714   46.117 1.00 45.60  ? 123 ASN A OD1 1 
ATOM   889  N ND2 . ASN A 1 124 ? -1.834  -0.700  46.079 1.00 85.97  ? 123 ASN A ND2 1 
ATOM   890  N N   . ASN A 1 125 ? -5.011  -2.546  46.901 1.00 45.73  ? 124 ASN A N   1 
ATOM   891  C CA  . ASN A 1 125 ? -6.294  -2.515  47.617 1.00 56.83  ? 124 ASN A CA  1 
ATOM   892  C C   . ASN A 1 125 ? -6.860  -1.099  47.650 1.00 57.47  ? 124 ASN A C   1 
ATOM   893  O O   . ASN A 1 125 ? -8.057  -0.912  47.898 1.00 35.66  ? 124 ASN A O   1 
ATOM   894  C CB  . ASN A 1 125 ? -6.166  -3.111  49.017 1.00 68.51  ? 124 ASN A CB  1 
ATOM   895  C CG  . ASN A 1 125 ? -7.197  -4.206  49.251 1.00 72.72  ? 124 ASN A CG  1 
ATOM   896  O OD1 . ASN A 1 125 ? -6.838  -5.369  49.432 1.00 58.10  ? 124 ASN A OD1 1 
ATOM   897  N ND2 . ASN A 1 125 ? -8.483  -3.867  49.251 1.00 77.45  ? 124 ASN A ND2 1 
ATOM   898  N N   . ASN A 1 126 ? -6.036  -0.089  47.390 1.00 60.45  ? 125 ASN A N   1 
ATOM   899  C CA  . ASN A 1 126 ? -6.509  1.292   47.347 1.00 57.54  ? 125 ASN A CA  1 
ATOM   900  C C   . ASN A 1 126 ? -7.025  1.651   45.959 1.00 45.25  ? 125 ASN A C   1 
ATOM   901  O O   . ASN A 1 126 ? -7.402  2.792   45.712 1.00 34.19  ? 125 ASN A O   1 
ATOM   902  C CB  . ASN A 1 126 ? -5.388  2.250   47.762 1.00 62.35  ? 125 ASN A CB  1 
ATOM   903  C CG  . ASN A 1 126 ? -4.746  1.841   49.076 1.00 63.00  ? 125 ASN A CG  1 
ATOM   904  O OD1 . ASN A 1 126 ? -5.049  2.378   50.135 1.00 65.41  ? 125 ASN A OD1 1 
ATOM   905  N ND2 . ASN A 1 126 ? -3.839  0.873   49.027 1.00 56.70  ? 125 ASN A ND2 1 
ATOM   906  N N   . THR A 1 127 ? -7.034  0.677   45.062 1.00 47.88  ? 126 THR A N   1 
ATOM   907  C CA  . THR A 1 127 ? -7.371  0.868   43.663 1.00 43.29  ? 126 THR A CA  1 
ATOM   908  C C   . THR A 1 127 ? -8.697  0.182   43.316 1.00 39.04  ? 126 THR A C   1 
ATOM   909  O O   . THR A 1 127 ? -8.878  -0.979  43.667 1.00 35.06  ? 126 THR A O   1 
ATOM   910  C CB  . THR A 1 127 ? -6.304  0.298   42.708 1.00 40.89  ? 126 THR A CB  1 
ATOM   911  O OG1 . THR A 1 127 ? -5.054  0.980   42.856 1.00 36.02  ? 126 THR A OG1 1 
ATOM   912  C CG2 . THR A 1 127 ? -6.744  0.492   41.265 1.00 37.58  ? 126 THR A CG2 1 
ATOM   913  N N   . THR A 1 128 ? -9.533  0.924   42.642 1.00 35.13  ? 127 THR A N   1 
ATOM   914  C CA  . THR A 1 128 ? -10.849 0.616   42.121 1.00 37.92  ? 127 THR A CA  1 
ATOM   915  C C   . THR A 1 128 ? -10.743 -0.202  40.843 1.00 45.37  ? 127 THR A C   1 
ATOM   916  O O   . THR A 1 128 ? -9.933  0.080   39.953 1.00 51.42  ? 127 THR A O   1 
ATOM   917  C CB  . THR A 1 128 ? -11.592 1.952   41.915 1.00 43.97  ? 127 THR A CB  1 
ATOM   918  O OG1 . THR A 1 128 ? -12.631 2.088   42.910 1.00 47.25  ? 127 THR A OG1 1 
ATOM   919  C CG2 . THR A 1 128 ? -12.261 2.035   40.562 1.00 34.81  ? 127 THR A CG2 1 
ATOM   920  N N   . GLN A 1 129 ? -11.544 -1.265  40.727 1.00 38.86  ? 128 GLN A N   1 
ATOM   921  C CA  . GLN A 1 129 ? -11.486 -2.141  39.561 1.00 38.86  ? 128 GLN A CA  1 
ATOM   922  C C   . GLN A 1 129 ? -11.654 -1.353  38.275 1.00 36.71  ? 128 GLN A C   1 
ATOM   923  O O   . GLN A 1 129 ? -11.144 -1.673  37.213 1.00 46.43  ? 128 GLN A O   1 
ATOM   924  C CB  . GLN A 1 129 ? -12.571 -3.217  39.643 1.00 36.54  ? 128 GLN A CB  1 
ATOM   925  C CG  . GLN A 1 129 ? -12.332 -4.282  40.688 1.00 30.39  ? 128 GLN A CG  1 
ATOM   926  C CD  . GLN A 1 129 ? -13.443 -5.314  40.760 1.00 45.94  ? 128 GLN A CD  1 
ATOM   927  O OE1 . GLN A 1 129 ? -14.377 -5.320  39.957 1.00 45.56  ? 128 GLN A OE1 1 
ATOM   928  N NE2 . GLN A 1 129 ? -13.334 -6.212  41.742 1.00 53.92  ? 128 GLN A NE2 1 
ATOM   929  N N   . GLY A 1 130 ? -12.417 -0.261  38.357 1.00 38.71  ? 129 GLY A N   1 
ATOM   930  C CA  . GLY A 1 130 ? -12.606 0.544   37.153 1.00 37.34  ? 129 GLY A CA  1 
ATOM   931  C C   . GLY A 1 130 ? -11.327 1.318   36.865 1.00 37.66  ? 129 GLY A C   1 
ATOM   932  O O   . GLY A 1 130 ? -10.820 1.309   35.751 1.00 30.73  ? 129 GLY A O   1 
ATOM   933  N N   . GLN A 1 131 ? -10.850 1.962   37.925 1.00 39.20  ? 130 GLN A N   1 
ATOM   934  C CA  . GLN A 1 131 ? -9.596  2.682   37.938 1.00 38.81  ? 130 GLN A CA  1 
ATOM   935  C C   . GLN A 1 131 ? -8.490  1.807   37.344 1.00 45.20  ? 130 GLN A C   1 
ATOM   936  O O   . GLN A 1 131 ? -7.725  2.232   36.482 1.00 26.49  ? 130 GLN A O   1 
ATOM   937  C CB  . GLN A 1 131 ? -9.231  3.086   39.362 1.00 31.88  ? 130 GLN A CB  1 
ATOM   938  C CG  . GLN A 1 131 ? -9.783  4.423   39.827 1.00 42.78  ? 130 GLN A CG  1 
ATOM   939  C CD  . GLN A 1 131 ? -9.427  4.683   41.286 1.00 48.92  ? 130 GLN A CD  1 
ATOM   940  O OE1 . GLN A 1 131 ? -9.278  3.759   42.095 1.00 29.00  ? 130 GLN A OE1 1 
ATOM   941  N NE2 . GLN A 1 131 ? -9.279  5.956   41.630 1.00 30.13  ? 130 GLN A NE2 1 
ATOM   942  N N   . ALA A 1 132 ? -8.416  0.567   37.831 1.00 50.70  ? 131 ALA A N   1 
ATOM   943  C CA  . ALA A 1 132 ? -7.346  -0.336  37.401 1.00 47.56  ? 131 ALA A CA  1 
ATOM   944  C C   . ALA A 1 132 ? -7.497  -0.689  35.926 1.00 34.68  ? 131 ALA A C   1 
ATOM   945  O O   . ALA A 1 132 ? -6.532  -0.904  35.193 1.00 37.12  ? 131 ALA A O   1 
ATOM   946  C CB  . ALA A 1 132 ? -7.321  -1.585  38.274 1.00 39.93  ? 131 ALA A CB  1 
ATOM   947  N N   . MET A 1 133 ? -8.751  -0.735  35.494 1.00 35.20  ? 132 MET A N   1 
ATOM   948  C CA  . MET A 1 133 ? -9.066  -1.097  34.114 1.00 41.30  ? 132 MET A CA  1 
ATOM   949  C C   . MET A 1 133 ? -8.656  0.003   33.146 1.00 46.06  ? 132 MET A C   1 
ATOM   950  O O   . MET A 1 133 ? -8.028  -0.224  32.105 1.00 37.76  ? 132 MET A O   1 
ATOM   951  C CB  . MET A 1 133 ? -10.557 -1.401  34.065 1.00 44.73  ? 132 MET A CB  1 
ATOM   952  C CG  . MET A 1 133 ? -11.326 -0.641  32.986 1.00 61.05  ? 132 MET A CG  1 
ATOM   953  S SD  . MET A 1 133 ? -12.012 -1.836  31.815 1.00 118.36 ? 132 MET A SD  1 
ATOM   954  C CE  . MET A 1 133 ? -10.994 -3.255  32.245 1.00 45.72  ? 132 MET A CE  1 
ATOM   955  N N   . VAL A 1 134 ? -8.992  1.246   33.489 1.00 35.83  ? 133 VAL A N   1 
ATOM   956  C CA  . VAL A 1 134 ? -8.583  2.381   32.672 1.00 29.60  ? 133 VAL A CA  1 
ATOM   957  C C   . VAL A 1 134 ? -7.068  2.388   32.494 1.00 35.01  ? 133 VAL A C   1 
ATOM   958  O O   . VAL A 1 134 ? -6.570  2.630   31.393 1.00 30.04  ? 133 VAL A O   1 
ATOM   959  C CB  . VAL A 1 134 ? -9.032  3.701   33.317 1.00 25.45  ? 133 VAL A CB  1 
ATOM   960  C CG1 . VAL A 1 134 ? -8.566  4.901   32.506 1.00 30.27  ? 133 VAL A CG1 1 
ATOM   961  C CG2 . VAL A 1 134 ? -10.545 3.704   33.459 1.00 32.68  ? 133 VAL A CG2 1 
ATOM   962  N N   . VAL A 1 135 ? -6.379  2.133   33.604 1.00 25.07  ? 134 VAL A N   1 
ATOM   963  C CA  . VAL A 1 135 ? -4.918  2.116   33.637 1.00 23.59  ? 134 VAL A CA  1 
ATOM   964  C C   . VAL A 1 135 ? -4.411  1.030   32.696 1.00 26.96  ? 134 VAL A C   1 
ATOM   965  O O   . VAL A 1 135 ? -3.594  1.300   31.825 1.00 23.55  ? 134 VAL A O   1 
ATOM   966  C CB  . VAL A 1 135 ? -4.381  1.859   35.054 1.00 32.34  ? 134 VAL A CB  1 
ATOM   967  C CG1 . VAL A 1 135 ? -2.933  1.400   35.010 1.00 30.95  ? 134 VAL A CG1 1 
ATOM   968  C CG2 . VAL A 1 135 ? -4.509  3.095   35.945 1.00 28.43  ? 134 VAL A CG2 1 
ATOM   969  N N   . GLU A 1 136 ? -4.908  -0.197  32.874 1.00 30.40  ? 135 GLU A N   1 
ATOM   970  C CA  . GLU A 1 136 ? -4.502  -1.304  32.006 1.00 31.33  ? 135 GLU A CA  1 
ATOM   971  C C   . GLU A 1 136 ? -4.838  -1.004  30.543 1.00 38.24  ? 135 GLU A C   1 
ATOM   972  O O   . GLU A 1 136 ? -4.083  -1.306  29.622 1.00 27.88  ? 135 GLU A O   1 
ATOM   973  C CB  . GLU A 1 136 ? -5.138  -2.637  32.404 1.00 22.06  ? 135 GLU A CB  1 
ATOM   974  C CG  . GLU A 1 136 ? -4.572  -3.324  33.634 1.00 30.41  ? 135 GLU A CG  1 
ATOM   975  C CD  . GLU A 1 136 ? -3.270  -4.060  33.430 1.00 32.33  ? 135 GLU A CD  1 
ATOM   976  O OE1 . GLU A 1 136 ? -2.483  -4.204  34.394 1.00 33.70  ? 135 GLU A OE1 1 
ATOM   977  O OE2 . GLU A 1 136 ? -2.994  -4.505  32.294 1.00 40.21  ? 135 GLU A OE2 1 
ATOM   978  N N   . LEU A 1 137 ? -5.997  -0.393  30.327 1.00 37.02  ? 136 LEU A N   1 
ATOM   979  C CA  . LEU A 1 137 ? -6.384  0.055   28.993 1.00 32.29  ? 136 LEU A CA  1 
ATOM   980  C C   . LEU A 1 137 ? -5.276  0.882   28.360 1.00 27.09  ? 136 LEU A C   1 
ATOM   981  O O   . LEU A 1 137 ? -4.747  0.629   27.282 1.00 33.57  ? 136 LEU A O   1 
ATOM   982  C CB  . LEU A 1 137 ? -7.644  0.898   29.138 1.00 36.32  ? 136 LEU A CB  1 
ATOM   983  C CG  . LEU A 1 137 ? -8.536  1.141   27.931 1.00 33.93  ? 136 LEU A CG  1 
ATOM   984  C CD1 . LEU A 1 137 ? -9.978  1.312   28.398 1.00 25.18  ? 136 LEU A CD1 1 
ATOM   985  C CD2 . LEU A 1 137 ? -8.051  2.336   27.127 1.00 29.23  ? 136 LEU A CD2 1 
ATOM   986  N N   . ILE A 1 138 ? -4.926  1.933   29.097 1.00 20.32  ? 137 ILE A N   1 
ATOM   987  C CA  . ILE A 1 138 ? -3.932  2.887   28.637 1.00 18.51  ? 137 ILE A CA  1 
ATOM   988  C C   . ILE A 1 138 ? -2.556  2.267   28.505 1.00 24.29  ? 137 ILE A C   1 
ATOM   989  O O   . ILE A 1 138 ? -1.782  2.639   27.623 1.00 21.39  ? 137 ILE A O   1 
ATOM   990  C CB  . ILE A 1 138 ? -3.901  4.066   29.639 1.00 26.88  ? 137 ILE A CB  1 
ATOM   991  C CG1 . ILE A 1 138 ? -5.181  4.900   29.613 1.00 27.29  ? 137 ILE A CG1 1 
ATOM   992  C CG2 . ILE A 1 138 ? -2.653  4.897   29.420 1.00 18.33  ? 137 ILE A CG2 1 
ATOM   993  C CD1 . ILE A 1 138 ? -5.374  5.925   30.702 1.00 26.46  ? 137 ILE A CD1 1 
ATOM   994  N N   . LEU A 1 139 ? -2.205  1.310   29.367 1.00 17.23  ? 138 LEU A N   1 
ATOM   995  C CA  . LEU A 1 139 ? -0.886  0.703   29.340 1.00 20.86  ? 138 LEU A CA  1 
ATOM   996  C C   . LEU A 1 139 ? -0.700  -0.144  28.081 1.00 21.16  ? 138 LEU A C   1 
ATOM   997  O O   . LEU A 1 139 ? 0.350   -0.241  27.455 1.00 18.88  ? 138 LEU A O   1 
ATOM   998  C CB  . LEU A 1 139 ? -0.663  -0.208  30.554 1.00 23.72  ? 138 LEU A CB  1 
ATOM   999  C CG  . LEU A 1 139 ? -0.773  0.328   31.968 1.00 30.90  ? 138 LEU A CG  1 
ATOM   1000 C CD1 . LEU A 1 139 ? -0.441  -0.776  32.971 1.00 31.47  ? 138 LEU A CD1 1 
ATOM   1001 C CD2 . LEU A 1 139 ? 0.134   1.531   32.198 1.00 18.37  ? 138 LEU A CD2 1 
ATOM   1002 N N   . THR A 1 140 ? -1.772  -0.837  27.697 1.00 19.29  ? 139 THR A N   1 
ATOM   1003 C CA  . THR A 1 140 ? -1.599  -1.777  26.575 1.00 22.55  ? 139 THR A CA  1 
ATOM   1004 C C   . THR A 1 140 ? -1.743  -1.001  25.277 1.00 19.10  ? 139 THR A C   1 
ATOM   1005 O O   . THR A 1 140 ? -1.112  -1.313  24.265 1.00 38.33  ? 139 THR A O   1 
ATOM   1006 C CB  . THR A 1 140 ? -2.603  -2.923  26.745 1.00 33.12  ? 139 THR A CB  1 
ATOM   1007 O OG1 . THR A 1 140 ? -3.912  -2.493  26.362 1.00 73.98  ? 139 THR A OG1 1 
ATOM   1008 C CG2 . THR A 1 140 ? -2.724  -3.297  28.227 1.00 15.96  ? 139 THR A CG2 1 
ATOM   1009 N N   . PHE A 1 141 ? -2.558  0.052   25.333 1.00 26.03  ? 140 PHE A N   1 
ATOM   1010 C CA  . PHE A 1 141 ? -2.758  1.002   24.243 1.00 23.16  ? 140 PHE A CA  1 
ATOM   1011 C C   . PHE A 1 141 ? -1.420  1.557   23.786 1.00 20.47  ? 140 PHE A C   1 
ATOM   1012 O O   . PHE A 1 141 ? -1.067  1.574   22.605 1.00 22.19  ? 140 PHE A O   1 
ATOM   1013 C CB  . PHE A 1 141 ? -3.660  2.168   24.657 1.00 27.29  ? 140 PHE A CB  1 
ATOM   1014 C CG  . PHE A 1 141 ? -3.883  3.205   23.566 1.00 31.27  ? 140 PHE A CG  1 
ATOM   1015 C CD1 . PHE A 1 141 ? -4.932  3.006   22.671 1.00 32.16  ? 140 PHE A CD1 1 
ATOM   1016 C CD2 . PHE A 1 141 ? -3.110  4.341   23.410 1.00 16.36  ? 140 PHE A CD2 1 
ATOM   1017 C CE1 . PHE A 1 141 ? -5.175  3.924   21.668 1.00 26.40  ? 140 PHE A CE1 1 
ATOM   1018 C CE2 . PHE A 1 141 ? -3.330  5.255   22.397 1.00 32.07  ? 140 PHE A CE2 1 
ATOM   1019 C CZ  . PHE A 1 141 ? -4.374  5.040   21.504 1.00 31.53  ? 140 PHE A CZ  1 
ATOM   1020 N N   . GLN A 1 142 ? -0.626  2.092   24.727 1.00 17.64  ? 141 GLN A N   1 
ATOM   1021 C CA  . GLN A 1 142 ? 0.655   2.606   24.204 1.00 25.77  ? 141 GLN A CA  1 
ATOM   1022 C C   . GLN A 1 142 ? 1.529   1.488   23.637 1.00 31.54  ? 141 GLN A C   1 
ATOM   1023 O O   . GLN A 1 142 ? 2.311   1.673   22.693 1.00 26.59  ? 141 GLN A O   1 
ATOM   1024 C CB  . GLN A 1 142 ? 1.388   3.400   25.283 1.00 21.07  ? 141 GLN A CB  1 
ATOM   1025 C CG  . GLN A 1 142 ? 1.831   2.657   26.508 1.00 20.84  ? 141 GLN A CG  1 
ATOM   1026 C CD  . GLN A 1 142 ? 3.167   1.956   26.450 1.00 20.14  ? 141 GLN A CD  1 
ATOM   1027 O OE1 . GLN A 1 142 ? 4.000   2.210   25.580 1.00 24.93  ? 141 GLN A OE1 1 
ATOM   1028 N NE2 . GLN A 1 142 ? 3.392   1.040   27.388 1.00 19.88  ? 141 GLN A NE2 1 
ATOM   1029 N N   . LEU A 1 143 ? 1.426   0.291   24.225 1.00 31.42  ? 142 LEU A N   1 
ATOM   1030 C CA  . LEU A 1 143 ? 2.303   -0.789  23.785 1.00 28.42  ? 142 LEU A CA  1 
ATOM   1031 C C   . LEU A 1 143 ? 1.868   -1.238  22.387 1.00 18.82  ? 142 LEU A C   1 
ATOM   1032 O O   . LEU A 1 143 ? 2.730   -1.380  21.520 1.00 19.54  ? 142 LEU A O   1 
ATOM   1033 C CB  . LEU A 1 143 ? 2.342   -1.978  24.743 1.00 23.95  ? 142 LEU A CB  1 
ATOM   1034 C CG  . LEU A 1 143 ? 2.886   -3.309  24.200 1.00 16.85  ? 142 LEU A CG  1 
ATOM   1035 C CD1 . LEU A 1 143 ? 4.395   -3.286  23.981 1.00 13.48  ? 142 LEU A CD1 1 
ATOM   1036 C CD2 . LEU A 1 143 ? 2.524   -4.446  25.143 1.00 17.10  ? 142 LEU A CD2 1 
ATOM   1037 N N   . ALA A 1 144 ? 0.568   -1.429  22.224 1.00 18.71  ? 143 ALA A N   1 
ATOM   1038 C CA  . ALA A 1 144 ? 0.020   -1.860  20.938 1.00 22.59  ? 143 ALA A CA  1 
ATOM   1039 C C   . ALA A 1 144 ? 0.277   -0.843  19.835 1.00 19.91  ? 143 ALA A C   1 
ATOM   1040 O O   . ALA A 1 144 ? 0.545   -1.235  18.705 1.00 23.53  ? 143 ALA A O   1 
ATOM   1041 C CB  . ALA A 1 144 ? -1.481  -2.089  21.063 1.00 34.85  ? 143 ALA A CB  1 
ATOM   1042 N N   . LEU A 1 145 ? 0.183   0.446   20.163 1.00 14.28  ? 144 LEU A N   1 
ATOM   1043 C CA  . LEU A 1 145 ? 0.488   1.504   19.200 1.00 22.58  ? 144 LEU A CA  1 
ATOM   1044 C C   . LEU A 1 145 ? 1.925   1.442   18.702 1.00 33.44  ? 144 LEU A C   1 
ATOM   1045 O O   . LEU A 1 145 ? 2.252   1.539   17.522 1.00 29.65  ? 144 LEU A O   1 
ATOM   1046 C CB  . LEU A 1 145 ? 0.213   2.846   19.867 1.00 31.09  ? 144 LEU A CB  1 
ATOM   1047 C CG  . LEU A 1 145 ? -0.148  4.009   18.950 1.00 31.67  ? 144 LEU A CG  1 
ATOM   1048 C CD1 . LEU A 1 145 ? -1.182  3.556   17.936 1.00 33.17  ? 144 LEU A CD1 1 
ATOM   1049 C CD2 . LEU A 1 145 ? -0.608  5.191   19.804 1.00 20.45  ? 144 LEU A CD2 1 
ATOM   1050 N N   . CYS A 1 146 ? 2.849   1.255   19.636 1.00 32.79  ? 145 CYS A N   1 
ATOM   1051 C CA  . CYS A 1 146 ? 4.274   1.179   19.325 1.00 22.10  ? 145 CYS A CA  1 
ATOM   1052 C C   . CYS A 1 146 ? 4.619   -0.063  18.529 1.00 22.56  ? 145 CYS A C   1 
ATOM   1053 O O   . CYS A 1 146 ? 5.531   -0.105  17.700 1.00 23.82  ? 145 CYS A O   1 
ATOM   1054 C CB  . CYS A 1 146 ? 5.013   1.209   20.669 1.00 20.57  ? 145 CYS A CB  1 
ATOM   1055 S SG  . CYS A 1 146 ? 6.795   1.035   20.602 1.00 26.31  ? 145 CYS A SG  1 
ATOM   1056 N N   . ILE A 1 147 ? 3.872   -1.139  18.789 1.00 19.28  ? 146 ILE A N   1 
ATOM   1057 C CA  . ILE A 1 147 ? 4.087   -2.376  18.069 1.00 17.38  ? 146 ILE A CA  1 
ATOM   1058 C C   . ILE A 1 147 ? 3.684   -2.193  16.614 1.00 26.07  ? 146 ILE A C   1 
ATOM   1059 O O   . ILE A 1 147 ? 4.337   -2.584  15.657 1.00 19.58  ? 146 ILE A O   1 
ATOM   1060 C CB  . ILE A 1 147 ? 3.254   -3.516  18.671 1.00 17.50  ? 146 ILE A CB  1 
ATOM   1061 C CG1 . ILE A 1 147 ? 3.756   -4.059  20.000 1.00 14.87  ? 146 ILE A CG1 1 
ATOM   1062 C CG2 . ILE A 1 147 ? 3.144   -4.647  17.649 1.00 31.71  ? 146 ILE A CG2 1 
ATOM   1063 C CD1 . ILE A 1 147 ? 2.785   -5.048  20.634 1.00 28.19  ? 146 ILE A CD1 1 
ATOM   1064 N N   . PHE A 1 148 ? 2.516   -1.560  16.461 1.00 29.53  ? 147 PHE A N   1 
ATOM   1065 C CA  . PHE A 1 148 ? 2.048   -1.443  15.083 1.00 30.07  ? 147 PHE A CA  1 
ATOM   1066 C C   . PHE A 1 148 ? 2.997   -0.526  14.317 1.00 34.19  ? 147 PHE A C   1 
ATOM   1067 O O   . PHE A 1 148 ? 3.333   -0.823  13.168 1.00 40.57  ? 147 PHE A O   1 
ATOM   1068 C CB  . PHE A 1 148 ? 0.612   -0.941  15.038 1.00 34.65  ? 147 PHE A CB  1 
ATOM   1069 C CG  . PHE A 1 148 ? -0.377  -1.736  15.869 1.00 22.74  ? 147 PHE A CG  1 
ATOM   1070 C CD1 . PHE A 1 148 ? -1.491  -1.129  16.421 1.00 21.67  ? 147 PHE A CD1 1 
ATOM   1071 C CD2 . PHE A 1 148 ? -0.181  -3.088  16.089 1.00 22.65  ? 147 PHE A CD2 1 
ATOM   1072 C CE1 . PHE A 1 148 ? -2.377  -1.863  17.186 1.00 22.28  ? 147 PHE A CE1 1 
ATOM   1073 C CE2 . PHE A 1 148 ? -1.068  -3.823  16.860 1.00 21.42  ? 147 PHE A CE2 1 
ATOM   1074 C CZ  . PHE A 1 148 ? -2.180  -3.218  17.415 1.00 19.64  ? 147 PHE A CZ  1 
ATOM   1075 N N   . ALA A 1 149 ? 3.435   0.565   14.942 1.00 26.85  ? 148 ALA A N   1 
ATOM   1076 C CA  . ALA A 1 149 ? 4.279   1.562   14.289 1.00 23.08  ? 148 ALA A CA  1 
ATOM   1077 C C   . ALA A 1 149 ? 5.633   0.984   13.888 1.00 36.51  ? 148 ALA A C   1 
ATOM   1078 O O   . ALA A 1 149 ? 6.208   1.379   12.870 1.00 25.38  ? 148 ALA A O   1 
ATOM   1079 C CB  . ALA A 1 149 ? 4.443   2.786   15.179 1.00 17.52  ? 148 ALA A CB  1 
ATOM   1080 N N   . SER A 1 150 ? 6.132   0.047   14.681 1.00 40.83  ? 149 SER A N   1 
ATOM   1081 C CA  . SER A 1 150 ? 7.438   -0.569  14.524 1.00 30.59  ? 149 SER A CA  1 
ATOM   1082 C C   . SER A 1 150 ? 7.455   -1.753  13.568 1.00 29.66  ? 149 SER A C   1 
ATOM   1083 O O   . SER A 1 150 ? 8.501   -2.311  13.259 1.00 24.81  ? 149 SER A O   1 
ATOM   1084 C CB  . SER A 1 150 ? 7.913   -1.048  15.909 1.00 27.54  ? 149 SER A CB  1 
ATOM   1085 O OG  . SER A 1 150 ? 8.257   0.066   16.701 1.00 32.76  ? 149 SER A OG  1 
ATOM   1086 N N   . THR A 1 151 ? 6.301   -2.190  13.089 1.00 28.95  ? 150 THR A N   1 
ATOM   1087 C CA  . THR A 1 151 ? 6.226   -3.391  12.267 1.00 26.47  ? 150 THR A CA  1 
ATOM   1088 C C   . THR A 1 151 ? 5.482   -3.139  10.953 1.00 27.73  ? 150 THR A C   1 
ATOM   1089 O O   . THR A 1 151 ? 5.270   -4.067  10.167 1.00 27.03  ? 150 THR A O   1 
ATOM   1090 C CB  . THR A 1 151 ? 5.534   -4.552  13.011 1.00 25.32  ? 150 THR A CB  1 
ATOM   1091 O OG1 . THR A 1 151 ? 4.256   -4.146  13.531 1.00 38.20  ? 150 THR A OG1 1 
ATOM   1092 C CG2 . THR A 1 151 ? 6.393   -4.997  14.188 1.00 29.98  ? 150 THR A CG2 1 
ATOM   1093 N N   . ASP A 1 152 ? 5.102   -1.879  10.761 1.00 25.09  ? 151 ASP A N   1 
ATOM   1094 C CA  . ASP A 1 152 ? 4.449   -1.433  9.557  1.00 21.77  ? 151 ASP A CA  1 
ATOM   1095 C C   . ASP A 1 152 ? 5.469   -1.498  8.415  1.00 34.94  ? 151 ASP A C   1 
ATOM   1096 O O   . ASP A 1 152 ? 6.511   -0.860  8.555  1.00 22.46  ? 151 ASP A O   1 
ATOM   1097 C CB  . ASP A 1 152 ? 3.906   -0.008  9.629  1.00 24.52  ? 151 ASP A CB  1 
ATOM   1098 C CG  . ASP A 1 152 ? 2.922   0.222   8.491  1.00 35.94  ? 151 ASP A CG  1 
ATOM   1099 O OD1 . ASP A 1 152 ? 3.283   -0.092  7.335  1.00 44.55  ? 151 ASP A OD1 1 
ATOM   1100 O OD2 . ASP A 1 152 ? 1.799   0.692   8.754  1.00 38.74  ? 151 ASP A OD2 1 
ATOM   1101 N N   . SER A 1 153 ? 5.146   -2.242  7.369  1.00 24.49  ? 152 SER A N   1 
ATOM   1102 C CA  . SER A 1 153 ? 6.049   -2.321  6.226  1.00 34.00  ? 152 SER A CA  1 
ATOM   1103 C C   . SER A 1 153 ? 6.143   -0.999  5.480  1.00 36.20  ? 152 SER A C   1 
ATOM   1104 O O   . SER A 1 153 ? 7.087   -0.745  4.723  1.00 58.37  ? 152 SER A O   1 
ATOM   1105 C CB  . SER A 1 153 ? 5.579   -3.408  5.242  1.00 32.70  ? 152 SER A CB  1 
ATOM   1106 O OG  . SER A 1 153 ? 4.254   -3.123  4.800  1.00 45.28  ? 152 SER A OG  1 
ATOM   1107 N N   . ARG A 1 154 ? 5.137   -0.144  5.667  1.00 25.79  ? 153 ARG A N   1 
ATOM   1108 C CA  . ARG A 1 154 ? 5.156   1.103   4.905  1.00 34.49  ? 153 ARG A CA  1 
ATOM   1109 C C   . ARG A 1 154 ? 5.969   2.175   5.609  1.00 39.83  ? 153 ARG A C   1 
ATOM   1110 O O   . ARG A 1 154 ? 6.158   3.282   5.098  1.00 50.26  ? 153 ARG A O   1 
ATOM   1111 C CB  . ARG A 1 154 ? 3.747   1.645   4.661  1.00 35.91  ? 153 ARG A CB  1 
ATOM   1112 C CG  . ARG A 1 154 ? 2.679   0.591   4.427  1.00 42.96  ? 153 ARG A CG  1 
ATOM   1113 C CD  . ARG A 1 154 ? 1.301   1.181   4.730  1.00 38.43  ? 153 ARG A CD  1 
ATOM   1114 N NE  . ARG A 1 154 ? 0.951   1.022   6.139  1.00 26.44  ? 153 ARG A NE  1 
ATOM   1115 C CZ  . ARG A 1 154 ? -0.305  1.015   6.561  1.00 33.79  ? 153 ARG A CZ  1 
ATOM   1116 N NH1 . ARG A 1 154 ? -1.279  1.160   5.672  1.00 42.49  ? 153 ARG A NH1 1 
ATOM   1117 N NH2 . ARG A 1 154 ? -0.575  0.867   7.848  1.00 36.89  ? 153 ARG A NH2 1 
ATOM   1118 N N   . ARG A 1 155 ? 6.459   1.867   6.811  1.00 37.74  ? 154 ARG A N   1 
ATOM   1119 C CA  . ARG A 1 155 ? 7.192   2.934   7.496  1.00 36.54  ? 154 ARG A CA  1 
ATOM   1120 C C   . ARG A 1 155 ? 8.487   3.284   6.760  1.00 22.94  ? 154 ARG A C   1 
ATOM   1121 O O   . ARG A 1 155 ? 9.264   2.399   6.405  1.00 33.34  ? 154 ARG A O   1 
ATOM   1122 C CB  . ARG A 1 155 ? 7.425   2.529   8.953  1.00 42.04  ? 154 ARG A CB  1 
ATOM   1123 C CG  . ARG A 1 155 ? 8.050   3.613   9.818  1.00 38.56  ? 154 ARG A CG  1 
ATOM   1124 C CD  . ARG A 1 155 ? 8.496   3.063   11.168 1.00 39.97  ? 154 ARG A CD  1 
ATOM   1125 N NE  . ARG A 1 155 ? 9.424   4.005   11.802 1.00 40.31  ? 154 ARG A NE  1 
ATOM   1126 C CZ  . ARG A 1 155 ? 9.297   4.400   13.063 1.00 32.70  ? 154 ARG A CZ  1 
ATOM   1127 N NH1 . ARG A 1 155 ? 8.289   3.904   13.765 1.00 36.36  ? 154 ARG A NH1 1 
ATOM   1128 N NH2 . ARG A 1 155 ? 10.169  5.257   13.571 1.00 24.91  ? 154 ARG A NH2 1 
ATOM   1129 N N   . THR A 1 156 ? 8.695   4.577   6.553  1.00 27.78  ? 155 THR A N   1 
ATOM   1130 C CA  . THR A 1 156 ? 9.784   5.261   5.895  1.00 39.93  ? 155 THR A CA  1 
ATOM   1131 C C   . THR A 1 156 ? 10.900  5.729   6.815  1.00 39.26  ? 155 THR A C   1 
ATOM   1132 O O   . THR A 1 156 ? 12.089  5.527   6.583  1.00 33.32  ? 155 THR A O   1 
ATOM   1133 C CB  . THR A 1 156 ? 9.222   6.530   5.205  1.00 50.41  ? 155 THR A CB  1 
ATOM   1134 O OG1 . THR A 1 156 ? 9.805   7.700   5.797  1.00 84.53  ? 155 THR A OG1 1 
ATOM   1135 C CG2 . THR A 1 156 ? 7.727   6.622   5.458  1.00 56.23  ? 155 THR A CG2 1 
ATOM   1136 N N   . SER A 1 157 ? 10.548  6.430   7.900  1.00 41.25  ? 156 SER A N   1 
ATOM   1137 C CA  . SER A 1 157 ? 11.596  6.865   8.823  1.00 31.14  ? 156 SER A CA  1 
ATOM   1138 C C   . SER A 1 157 ? 12.210  5.659   9.526  1.00 29.52  ? 156 SER A C   1 
ATOM   1139 O O   . SER A 1 157 ? 11.613  4.602   9.743  1.00 20.82  ? 156 SER A O   1 
ATOM   1140 C CB  . SER A 1 157 ? 11.030  7.845   9.849  1.00 25.51  ? 156 SER A CB  1 
ATOM   1141 O OG  . SER A 1 157 ? 9.905   7.260   10.497 1.00 33.39  ? 156 SER A OG  1 
ATOM   1142 N N   . PRO A 1 158 ? 13.468  5.831   9.910  1.00 24.87  ? 157 PRO A N   1 
ATOM   1143 C CA  . PRO A 1 158 ? 14.222  4.763   10.570 1.00 20.73  ? 157 PRO A CA  1 
ATOM   1144 C C   . PRO A 1 158 ? 13.489  4.161   11.767 1.00 20.83  ? 157 PRO A C   1 
ATOM   1145 O O   . PRO A 1 158 ? 13.064  4.879   12.676 1.00 33.80  ? 157 PRO A O   1 
ATOM   1146 C CB  . PRO A 1 158 ? 15.492  5.504   11.010 1.00 27.45  ? 157 PRO A CB  1 
ATOM   1147 C CG  . PRO A 1 158 ? 15.637  6.608   10.016 1.00 32.05  ? 157 PRO A CG  1 
ATOM   1148 C CD  . PRO A 1 158 ? 14.232  7.071   9.727  1.00 24.84  ? 157 PRO A CD  1 
ATOM   1149 N N   . VAL A 1 159 ? 13.315  2.840   11.793 1.00 14.72  ? 158 VAL A N   1 
ATOM   1150 C CA  . VAL A 1 159 ? 12.590  2.141   12.849 1.00 18.03  ? 158 VAL A CA  1 
ATOM   1151 C C   . VAL A 1 159 ? 13.440  1.821   14.076 1.00 19.59  ? 158 VAL A C   1 
ATOM   1152 O O   . VAL A 1 159 ? 12.929  1.488   15.147 1.00 32.46  ? 158 VAL A O   1 
ATOM   1153 C CB  . VAL A 1 159 ? 12.010  0.812   12.321 1.00 28.72  ? 158 VAL A CB  1 
ATOM   1154 C CG1 . VAL A 1 159 ? 13.158  -0.131  11.982 1.00 30.08  ? 158 VAL A CG1 1 
ATOM   1155 C CG2 . VAL A 1 159 ? 11.042  0.200   13.321 1.00 30.37  ? 158 VAL A CG2 1 
ATOM   1156 N N   . GLY A 1 160 ? 14.751  1.922   13.918 1.00 19.18  ? 159 GLY A N   1 
ATOM   1157 C CA  . GLY A 1 160 ? 15.724  1.553   14.932 1.00 27.50  ? 159 GLY A CA  1 
ATOM   1158 C C   . GLY A 1 160 ? 15.625  0.066   15.220 1.00 31.78  ? 159 GLY A C   1 
ATOM   1159 O O   . GLY A 1 160 ? 15.763  -0.758  14.311 1.00 26.05  ? 159 GLY A O   1 
ATOM   1160 N N   . SER A 1 161 ? 15.370  -0.269  16.485 1.00 27.44  ? 160 SER A N   1 
ATOM   1161 C CA  . SER A 1 161 ? 15.196  -1.683  16.827 1.00 18.64  ? 160 SER A CA  1 
ATOM   1162 C C   . SER A 1 161 ? 13.718  -1.862  17.141 1.00 24.24  ? 160 SER A C   1 
ATOM   1163 O O   . SER A 1 161 ? 13.267  -1.333  18.163 1.00 30.69  ? 160 SER A O   1 
ATOM   1164 C CB  . SER A 1 161 ? 16.100  -2.092  17.987 1.00 19.78  ? 160 SER A CB  1 
ATOM   1165 O OG  . SER A 1 161 ? 15.805  -3.427  18.425 1.00 17.72  ? 160 SER A OG  1 
ATOM   1166 N N   . PRO A 1 162 ? 12.925  -2.529  16.317 1.00 17.80  ? 161 PRO A N   1 
ATOM   1167 C CA  . PRO A 1 162 ? 11.524  -2.692  16.710 1.00 17.47  ? 161 PRO A CA  1 
ATOM   1168 C C   . PRO A 1 162 ? 11.492  -3.561  17.972 1.00 22.27  ? 161 PRO A C   1 
ATOM   1169 O O   . PRO A 1 162 ? 10.658  -3.332  18.832 1.00 19.97  ? 161 PRO A O   1 
ATOM   1170 C CB  . PRO A 1 162 ? 10.857  -3.400  15.537 1.00 21.64  ? 161 PRO A CB  1 
ATOM   1171 C CG  . PRO A 1 162 ? 11.807  -3.200  14.391 1.00 30.80  ? 161 PRO A CG  1 
ATOM   1172 C CD  . PRO A 1 162 ? 13.183  -3.158  15.015 1.00 28.55  ? 161 PRO A CD  1 
ATOM   1173 N N   . ALA A 1 163 ? 12.387  -4.538  18.079 1.00 20.67  ? 162 ALA A N   1 
ATOM   1174 C CA  . ALA A 1 163 ? 12.335  -5.453  19.215 1.00 24.27  ? 162 ALA A CA  1 
ATOM   1175 C C   . ALA A 1 163 ? 12.637  -4.753  20.537 1.00 22.78  ? 162 ALA A C   1 
ATOM   1176 O O   . ALA A 1 163 ? 12.025  -5.036  21.573 1.00 22.66  ? 162 ALA A O   1 
ATOM   1177 C CB  . ALA A 1 163 ? 13.290  -6.603  18.969 1.00 13.72  ? 162 ALA A CB  1 
ATOM   1178 N N   . LEU A 1 164 ? 13.593  -3.834  20.524 1.00 21.86  ? 163 LEU A N   1 
ATOM   1179 C CA  . LEU A 1 164 ? 14.037  -3.214  21.780 1.00 20.77  ? 163 LEU A CA  1 
ATOM   1180 C C   . LEU A 1 164 ? 13.112  -2.069  22.170 1.00 29.27  ? 163 LEU A C   1 
ATOM   1181 O O   . LEU A 1 164 ? 12.934  -1.821  23.365 1.00 30.82  ? 163 LEU A O   1 
ATOM   1182 C CB  . LEU A 1 164 ? 15.510  -2.812  21.655 1.00 9.83   ? 163 LEU A CB  1 
ATOM   1183 C CG  . LEU A 1 164 ? 16.523  -3.911  22.008 1.00 31.01  ? 163 LEU A CG  1 
ATOM   1184 C CD1 . LEU A 1 164 ? 17.927  -3.359  22.201 1.00 26.27  ? 163 LEU A CD1 1 
ATOM   1185 C CD2 . LEU A 1 164 ? 16.081  -4.673  23.257 1.00 26.18  ? 163 LEU A CD2 1 
ATOM   1186 N N   . SER A 1 165 ? 12.508  -1.399  21.189 1.00 24.54  ? 164 SER A N   1 
ATOM   1187 C CA  . SER A 1 165 ? 11.445  -0.437  21.424 1.00 28.52  ? 164 SER A CA  1 
ATOM   1188 C C   . SER A 1 165 ? 10.221  -1.119  22.051 1.00 32.55  ? 164 SER A C   1 
ATOM   1189 O O   . SER A 1 165 ? 9.720   -0.657  23.075 1.00 26.26  ? 164 SER A O   1 
ATOM   1190 C CB  . SER A 1 165 ? 10.945  0.273   20.161 1.00 21.83  ? 164 SER A CB  1 
ATOM   1191 O OG  . SER A 1 165 ? 11.861  1.258   19.725 1.00 23.36  ? 164 SER A OG  1 
ATOM   1192 N N   . ILE A 1 166 ? 9.771   -2.182  21.377 1.00 27.05  ? 165 ILE A N   1 
ATOM   1193 C CA  . ILE A 1 166 ? 8.624   -2.936  21.878 1.00 30.88  ? 165 ILE A CA  1 
ATOM   1194 C C   . ILE A 1 166 ? 8.934   -3.370  23.320 1.00 21.44  ? 165 ILE A C   1 
ATOM   1195 O O   . ILE A 1 166 ? 8.090   -3.234  24.199 1.00 19.17  ? 165 ILE A O   1 
ATOM   1196 C CB  . ILE A 1 166 ? 8.254   -4.160  21.030 1.00 33.26  ? 165 ILE A CB  1 
ATOM   1197 C CG1 . ILE A 1 166 ? 7.895   -3.915  19.553 1.00 31.17  ? 165 ILE A CG1 1 
ATOM   1198 C CG2 . ILE A 1 166 ? 7.100   -4.923  21.672 1.00 8.66   ? 165 ILE A CG2 1 
ATOM   1199 C CD1 . ILE A 1 166 ? 7.693   -2.458  19.233 1.00 29.36  ? 165 ILE A CD1 1 
ATOM   1200 N N   . GLY A 1 167 ? 10.149  -3.876  23.508 1.00 22.19  ? 166 GLY A N   1 
ATOM   1201 C CA  . GLY A 1 167 ? 10.599  -4.379  24.792 1.00 21.55  ? 166 GLY A CA  1 
ATOM   1202 C C   . GLY A 1 167 ? 10.554  -3.286  25.840 1.00 20.37  ? 166 GLY A C   1 
ATOM   1203 O O   . GLY A 1 167 ? 10.013  -3.442  26.925 1.00 21.09  ? 166 GLY A O   1 
ATOM   1204 N N   . LEU A 1 168 ? 11.129  -2.137  25.507 1.00 18.65  ? 167 LEU A N   1 
ATOM   1205 C CA  . LEU A 1 168 ? 11.216  -1.014  26.440 1.00 17.72  ? 167 LEU A CA  1 
ATOM   1206 C C   . LEU A 1 168 ? 9.862   -0.380  26.709 1.00 22.36  ? 167 LEU A C   1 
ATOM   1207 O O   . LEU A 1 168 ? 9.616   0.239   27.750 1.00 17.46  ? 167 LEU A O   1 
ATOM   1208 C CB  . LEU A 1 168 ? 12.261  -0.026  25.908 1.00 13.11  ? 167 LEU A CB  1 
ATOM   1209 C CG  . LEU A 1 168 ? 13.690  -0.597  26.013 1.00 22.95  ? 167 LEU A CG  1 
ATOM   1210 C CD1 . LEU A 1 168 ? 14.655  0.184   25.152 1.00 17.02  ? 167 LEU A CD1 1 
ATOM   1211 C CD2 . LEU A 1 168 ? 14.144  -0.645  27.476 1.00 22.26  ? 167 LEU A CD2 1 
ATOM   1212 N N   . SER A 1 169 ? 8.952   -0.570  25.765 1.00 23.05  ? 168 SER A N   1 
ATOM   1213 C CA  . SER A 1 169 ? 7.557   -0.195  25.909 1.00 17.40  ? 168 SER A CA  1 
ATOM   1214 C C   . SER A 1 169 ? 6.855   -1.035  26.968 1.00 21.45  ? 168 SER A C   1 
ATOM   1215 O O   . SER A 1 169 ? 6.070   -0.555  27.791 1.00 27.71  ? 168 SER A O   1 
ATOM   1216 C CB  . SER A 1 169 ? 6.816   -0.359  24.578 1.00 20.77  ? 168 SER A CB  1 
ATOM   1217 O OG  . SER A 1 169 ? 5.461   0.010   24.801 1.00 18.99  ? 168 SER A OG  1 
ATOM   1218 N N   . VAL A 1 170 ? 7.133   -2.348  26.983 1.00 16.11  ? 169 VAL A N   1 
ATOM   1219 C CA  . VAL A 1 170 ? 6.473   -3.083  28.067 1.00 19.02  ? 169 VAL A CA  1 
ATOM   1220 C C   . VAL A 1 170 ? 7.095   -2.667  29.406 1.00 25.90  ? 169 VAL A C   1 
ATOM   1221 O O   . VAL A 1 170 ? 6.363   -2.666  30.401 1.00 17.88  ? 169 VAL A O   1 
ATOM   1222 C CB  . VAL A 1 170 ? 6.523   -4.608  27.911 1.00 34.20  ? 169 VAL A CB  1 
ATOM   1223 C CG1 . VAL A 1 170 ? 7.757   -5.073  27.163 1.00 61.60  ? 169 VAL A CG1 1 
ATOM   1224 C CG2 . VAL A 1 170 ? 6.455   -5.297  29.279 1.00 16.45  ? 169 VAL A CG2 1 
ATOM   1225 N N   . THR A 1 171 ? 8.380   -2.344  29.411 1.00 14.86  ? 170 THR A N   1 
ATOM   1226 C CA  . THR A 1 171 ? 9.115   -1.897  30.584 1.00 22.96  ? 170 THR A CA  1 
ATOM   1227 C C   . THR A 1 171 ? 8.508   -0.584  31.099 1.00 28.13  ? 170 THR A C   1 
ATOM   1228 O O   . THR A 1 171 ? 8.287   -0.496  32.308 1.00 32.11  ? 170 THR A O   1 
ATOM   1229 C CB  . THR A 1 171 ? 10.612  -1.698  30.312 1.00 25.81  ? 170 THR A CB  1 
ATOM   1230 O OG1 . THR A 1 171 ? 11.293  -2.959  30.274 1.00 21.89  ? 170 THR A OG1 1 
ATOM   1231 C CG2 . THR A 1 171 ? 11.279  -0.916  31.439 1.00 13.56  ? 170 THR A CG2 1 
ATOM   1232 N N   . LEU A 1 172 ? 8.247   0.344   30.188 1.00 19.85  ? 171 LEU A N   1 
ATOM   1233 C CA  . LEU A 1 172 ? 7.527   1.581   30.424 1.00 14.77  ? 171 LEU A CA  1 
ATOM   1234 C C   . LEU A 1 172 ? 6.189   1.318   31.109 1.00 23.50  ? 171 LEU A C   1 
ATOM   1235 O O   . LEU A 1 172 ? 5.759   1.893   32.098 1.00 18.31  ? 171 LEU A O   1 
ATOM   1236 C CB  . LEU A 1 172 ? 7.220   2.357   29.125 1.00 12.76  ? 171 LEU A CB  1 
ATOM   1237 C CG  . LEU A 1 172 ? 6.278   3.547   29.371 1.00 24.26  ? 171 LEU A CG  1 
ATOM   1238 C CD1 . LEU A 1 172 ? 6.923   4.546   30.333 1.00 19.53  ? 171 LEU A CD1 1 
ATOM   1239 C CD2 . LEU A 1 172 ? 5.884   4.237   28.079 1.00 15.27  ? 171 LEU A CD2 1 
ATOM   1240 N N   . GLY A 1 173 ? 5.415   0.383   30.554 1.00 21.36  ? 172 GLY A N   1 
ATOM   1241 C CA  . GLY A 1 173 ? 4.101   0.187   31.123 1.00 21.05  ? 172 GLY A CA  1 
ATOM   1242 C C   . GLY A 1 173 ? 4.143   -0.435  32.507 1.00 24.50  ? 172 GLY A C   1 
ATOM   1243 O O   . GLY A 1 173 ? 3.135   -0.330  33.214 1.00 23.86  ? 172 GLY A O   1 
ATOM   1244 N N   . HIS A 1 174 ? 5.254   -1.054  32.887 1.00 17.64  ? 173 HIS A N   1 
ATOM   1245 C CA  . HIS A 1 174 ? 5.385   -1.708  34.182 1.00 14.87  ? 173 HIS A CA  1 
ATOM   1246 C C   . HIS A 1 174 ? 5.735   -0.686  35.265 1.00 27.35  ? 173 HIS A C   1 
ATOM   1247 O O   . HIS A 1 174 ? 5.413   -0.923  36.431 1.00 26.93  ? 173 HIS A O   1 
ATOM   1248 C CB  . HIS A 1 174 ? 6.443   -2.813  34.168 1.00 18.46  ? 173 HIS A CB  1 
ATOM   1249 C CG  . HIS A 1 174 ? 5.921   -4.165  33.767 1.00 28.19  ? 173 HIS A CG  1 
ATOM   1250 N ND1 . HIS A 1 174 ? 5.598   -5.162  34.663 1.00 31.34  ? 173 HIS A ND1 1 
ATOM   1251 C CD2 . HIS A 1 174 ? 5.660   -4.687  32.541 1.00 18.69  ? 173 HIS A CD2 1 
ATOM   1252 C CE1 . HIS A 1 174 ? 5.165   -6.233  34.020 1.00 21.44  ? 173 HIS A CE1 1 
ATOM   1253 N NE2 . HIS A 1 174 ? 5.192   -5.968  32.725 1.00 25.18  ? 173 HIS A NE2 1 
ATOM   1254 N N   . LEU A 1 175 ? 6.387   0.405   34.872 1.00 23.36  ? 174 LEU A N   1 
ATOM   1255 C CA  . LEU A 1 175 ? 6.886   1.378   35.836 1.00 22.51  ? 174 LEU A CA  1 
ATOM   1256 C C   . LEU A 1 175 ? 5.723   2.207   36.382 1.00 19.33  ? 174 LEU A C   1 
ATOM   1257 O O   . LEU A 1 175 ? 5.896   2.890   37.394 1.00 18.41  ? 174 LEU A O   1 
ATOM   1258 C CB  . LEU A 1 175 ? 7.964   2.282   35.258 1.00 22.32  ? 174 LEU A CB  1 
ATOM   1259 C CG  . LEU A 1 175 ? 9.269   1.657   34.787 1.00 19.20  ? 174 LEU A CG  1 
ATOM   1260 C CD1 . LEU A 1 175 ? 10.069  2.648   33.933 1.00 17.91  ? 174 LEU A CD1 1 
ATOM   1261 C CD2 . LEU A 1 175 ? 10.102  1.177   35.955 1.00 13.20  ? 174 LEU A CD2 1 
ATOM   1262 N N   . VAL A 1 176 ? 4.570   2.114   35.719 1.00 19.68  ? 175 VAL A N   1 
ATOM   1263 C CA  . VAL A 1 176 ? 3.374   2.746   36.271 1.00 21.44  ? 175 VAL A CA  1 
ATOM   1264 C C   . VAL A 1 176 ? 2.381   1.667   36.715 1.00 26.52  ? 175 VAL A C   1 
ATOM   1265 O O   . VAL A 1 176 ? 1.871   1.743   37.837 1.00 20.13  ? 175 VAL A O   1 
ATOM   1266 C CB  . VAL A 1 176 ? 2.674   3.716   35.311 1.00 24.26  ? 175 VAL A CB  1 
ATOM   1267 C CG1 . VAL A 1 176 ? 1.317   4.148   35.869 1.00 14.98  ? 175 VAL A CG1 1 
ATOM   1268 C CG2 . VAL A 1 176 ? 3.507   4.966   35.067 1.00 25.44  ? 175 VAL A CG2 1 
ATOM   1269 N N   . GLY A 1 177 ? 2.130   0.695   35.858 1.00 22.18  ? 176 GLY A N   1 
ATOM   1270 C CA  . GLY A 1 177 ? 1.175   -0.382  36.002 1.00 9.66   ? 176 GLY A CA  1 
ATOM   1271 C C   . GLY A 1 177 ? 1.391   -1.253  37.209 1.00 19.46  ? 176 GLY A C   1 
ATOM   1272 O O   . GLY A 1 177 ? 0.439   -1.741  37.819 1.00 21.65  ? 176 GLY A O   1 
ATOM   1273 N N   . ILE A 1 178 ? 2.648   -1.486  37.595 1.00 22.44  ? 177 ILE A N   1 
ATOM   1274 C CA  . ILE A 1 178 ? 2.837   -2.362  38.753 1.00 24.13  ? 177 ILE A CA  1 
ATOM   1275 C C   . ILE A 1 178 ? 2.168   -1.831  40.017 1.00 37.04  ? 177 ILE A C   1 
ATOM   1276 O O   . ILE A 1 178 ? 1.486   -2.614  40.696 1.00 31.07  ? 177 ILE A O   1 
ATOM   1277 C CB  . ILE A 1 178 ? 4.331   -2.641  38.994 1.00 21.04  ? 177 ILE A CB  1 
ATOM   1278 C CG1 . ILE A 1 178 ? 4.974   -3.410  37.828 1.00 23.57  ? 177 ILE A CG1 1 
ATOM   1279 C CG2 . ILE A 1 178 ? 4.533   -3.358  40.314 1.00 17.55  ? 177 ILE A CG2 1 
ATOM   1280 C CD1 . ILE A 1 178 ? 6.371   -3.901  38.089 1.00 26.85  ? 177 ILE A CD1 1 
ATOM   1281 N N   . TYR A 1 179 ? 2.291   -0.562  40.364 1.00 33.63  ? 178 TYR A N   1 
ATOM   1282 C CA  . TYR A 1 179 ? 1.643   0.077   41.491 1.00 17.44  ? 178 TYR A CA  1 
ATOM   1283 C C   . TYR A 1 179 ? 0.124   -0.011  41.498 1.00 24.69  ? 178 TYR A C   1 
ATOM   1284 O O   . TYR A 1 179 ? -0.478  0.309   42.524 1.00 26.15  ? 178 TYR A O   1 
ATOM   1285 C CB  . TYR A 1 179 ? 1.970   1.590   41.465 1.00 11.60  ? 178 TYR A CB  1 
ATOM   1286 C CG  . TYR A 1 179 ? 3.431   1.804   41.753 1.00 18.38  ? 178 TYR A CG  1 
ATOM   1287 C CD1 . TYR A 1 179 ? 4.282   2.361   40.804 1.00 16.31  ? 178 TYR A CD1 1 
ATOM   1288 C CD2 . TYR A 1 179 ? 3.925   1.423   42.983 1.00 18.56  ? 178 TYR A CD2 1 
ATOM   1289 C CE1 . TYR A 1 179 ? 5.613   2.525   41.134 1.00 23.33  ? 178 TYR A CE1 1 
ATOM   1290 C CE2 . TYR A 1 179 ? 5.255   1.582   43.315 1.00 26.33  ? 178 TYR A CE2 1 
ATOM   1291 C CZ  . TYR A 1 179 ? 6.083   2.136   42.365 1.00 20.49  ? 178 TYR A CZ  1 
ATOM   1292 O OH  . TYR A 1 179 ? 7.405   2.299   42.698 1.00 25.09  ? 178 TYR A OH  1 
ATOM   1293 N N   . PHE A 1 180 ? -0.481  -0.378  40.377 1.00 24.57  ? 179 PHE A N   1 
ATOM   1294 C CA  . PHE A 1 180 ? -1.911  -0.330  40.164 1.00 25.19  ? 179 PHE A CA  1 
ATOM   1295 C C   . PHE A 1 180 ? -2.508  -1.736  40.159 1.00 37.83  ? 179 PHE A C   1 
ATOM   1296 O O   . PHE A 1 180 ? -3.339  -2.090  41.000 1.00 43.37  ? 179 PHE A O   1 
ATOM   1297 C CB  . PHE A 1 180 ? -2.252  0.345   38.836 1.00 21.26  ? 179 PHE A CB  1 
ATOM   1298 C CG  . PHE A 1 180 ? -2.296  1.858   38.851 1.00 25.50  ? 179 PHE A CG  1 
ATOM   1299 C CD1 . PHE A 1 180 ? -1.293  2.613   38.273 1.00 20.59  ? 179 PHE A CD1 1 
ATOM   1300 C CD2 . PHE A 1 180 ? -3.350  2.537   39.448 1.00 28.73  ? 179 PHE A CD2 1 
ATOM   1301 C CE1 . PHE A 1 180 ? -1.317  3.994   38.279 1.00 23.44  ? 179 PHE A CE1 1 
ATOM   1302 C CE2 . PHE A 1 180 ? -3.384  3.923   39.454 1.00 27.00  ? 179 PHE A CE2 1 
ATOM   1303 C CZ  . PHE A 1 180 ? -2.376  4.660   38.880 1.00 23.54  ? 179 PHE A CZ  1 
ATOM   1304 N N   . THR A 1 181 ? -2.071  -2.539  39.189 1.00 36.90  ? 180 THR A N   1 
ATOM   1305 C CA  . THR A 1 181 ? -2.546  -3.918  39.107 1.00 29.60  ? 180 THR A CA  1 
ATOM   1306 C C   . THR A 1 181 ? -1.408  -4.923  39.195 1.00 36.91  ? 180 THR A C   1 
ATOM   1307 O O   . THR A 1 181 ? -1.611  -6.129  39.032 1.00 44.70  ? 180 THR A O   1 
ATOM   1308 C CB  . THR A 1 181 ? -3.257  -4.153  37.760 1.00 29.55  ? 180 THR A CB  1 
ATOM   1309 O OG1 . THR A 1 181 ? -2.379  -3.587  36.776 1.00 46.23  ? 180 THR A OG1 1 
ATOM   1310 C CG2 . THR A 1 181 ? -4.585  -3.438  37.686 1.00 19.53  ? 180 THR A CG2 1 
ATOM   1311 N N   . GLY A 1 182 ? -0.179  -4.459  39.434 1.00 36.87  ? 181 GLY A N   1 
ATOM   1312 C CA  . GLY A 1 182 ? 0.964   -5.356  39.367 1.00 27.76  ? 181 GLY A CA  1 
ATOM   1313 C C   . GLY A 1 182 ? 1.386   -5.524  37.899 1.00 36.25  ? 181 GLY A C   1 
ATOM   1314 O O   . GLY A 1 182 ? 2.340   -6.266  37.673 1.00 32.06  ? 181 GLY A O   1 
ATOM   1315 N N   . CYS A 1 183 ? 0.700   -4.857  36.993 1.00 34.11  ? 182 CYS A N   1 
ATOM   1316 C CA  . CYS A 1 183 ? 0.868   -4.708  35.563 1.00 21.54  ? 182 CYS A CA  1 
ATOM   1317 C C   . CYS A 1 183 ? 0.598   -6.002  34.804 1.00 15.53  ? 182 CYS A C   1 
ATOM   1318 O O   . CYS A 1 183 ? 1.342   -6.972  34.786 1.00 22.31  ? 182 CYS A O   1 
ATOM   1319 C CB  . CYS A 1 183 ? 2.275   -4.212  35.188 1.00 21.91  ? 182 CYS A CB  1 
ATOM   1320 S SG  . CYS A 1 183 ? 2.337   -3.681  33.445 1.00 25.95  ? 182 CYS A SG  1 
ATOM   1321 N N   . SER A 1 184 ? -0.530  -6.028  34.134 1.00 21.76  ? 183 SER A N   1 
ATOM   1322 C CA  . SER A 1 184 ? -0.927  -7.104  33.242 1.00 34.40  ? 183 SER A CA  1 
ATOM   1323 C C   . SER A 1 184 ? -0.458  -6.820  31.815 1.00 22.28  ? 183 SER A C   1 
ATOM   1324 O O   . SER A 1 184 ? 0.622   -7.231  31.389 1.00 24.97  ? 183 SER A O   1 
ATOM   1325 C CB  . SER A 1 184 ? -2.454  -7.254  33.290 1.00 32.39  ? 183 SER A CB  1 
ATOM   1326 O OG  . SER A 1 184 ? -2.842  -8.436  32.621 1.00 31.48  ? 183 SER A OG  1 
ATOM   1327 N N   . MET A 1 185 ? -1.272  -6.086  31.072 1.00 23.24  ? 184 MET A N   1 
ATOM   1328 C CA  . MET A 1 185 ? -1.016  -5.702  29.690 1.00 35.25  ? 184 MET A CA  1 
ATOM   1329 C C   . MET A 1 185 ? -1.066  -6.919  28.757 1.00 31.48  ? 184 MET A C   1 
ATOM   1330 O O   . MET A 1 185 ? -0.671  -6.791  27.601 1.00 26.78  ? 184 MET A O   1 
ATOM   1331 C CB  . MET A 1 185 ? 0.338   -5.030  29.484 1.00 32.99  ? 184 MET A CB  1 
ATOM   1332 C CG  . MET A 1 185 ? 0.631   -3.803  30.320 1.00 35.73  ? 184 MET A CG  1 
ATOM   1333 S SD  . MET A 1 185 ? 2.226   -3.061  29.910 1.00 42.10  ? 184 MET A SD  1 
ATOM   1334 C CE  . MET A 1 185 ? 2.019   -2.754  28.168 1.00 23.46  ? 184 MET A CE  1 
ATOM   1335 N N   . ASN A 1 186 ? -1.534  -8.031  29.297 1.00 28.94  ? 185 ASN A N   1 
ATOM   1336 C CA  . ASN A 1 186 ? -1.453  -9.341  28.657 1.00 24.36  ? 185 ASN A CA  1 
ATOM   1337 C C   . ASN A 1 186 ? -2.300  -10.373 29.388 1.00 20.47  ? 185 ASN A C   1 
ATOM   1338 O O   . ASN A 1 186 ? -1.858  -10.928 30.387 1.00 22.15  ? 185 ASN A O   1 
ATOM   1339 C CB  . ASN A 1 186 ? 0.021   -9.724  28.639 1.00 17.42  ? 185 ASN A CB  1 
ATOM   1340 C CG  . ASN A 1 186 ? 0.394   -10.874 27.732 1.00 25.46  ? 185 ASN A CG  1 
ATOM   1341 O OD1 . ASN A 1 186 ? 1.505   -10.842 27.197 1.00 22.88  ? 185 ASN A OD1 1 
ATOM   1342 N ND2 . ASN A 1 186 ? -0.469  -11.866 27.547 1.00 16.97  ? 185 ASN A ND2 1 
ATOM   1343 N N   . PRO A 1 187 ? -3.501  -10.656 28.913 1.00 24.47  ? 186 PRO A N   1 
ATOM   1344 C CA  . PRO A 1 187 ? -4.382  -11.670 29.511 1.00 23.84  ? 186 PRO A CA  1 
ATOM   1345 C C   . PRO A 1 187 ? -3.681  -12.979 29.852 1.00 27.86  ? 186 PRO A C   1 
ATOM   1346 O O   . PRO A 1 187 ? -3.934  -13.546 30.919 1.00 25.35  ? 186 PRO A O   1 
ATOM   1347 C CB  . PRO A 1 187 ? -5.411  -11.891 28.387 1.00 20.56  ? 186 PRO A CB  1 
ATOM   1348 C CG  . PRO A 1 187 ? -5.536  -10.511 27.811 1.00 30.03  ? 186 PRO A CG  1 
ATOM   1349 C CD  . PRO A 1 187 ? -4.119  -9.999  27.742 1.00 26.18  ? 186 PRO A CD  1 
ATOM   1350 N N   . ALA A 1 188 ? -2.805  -13.442 28.966 1.00 29.37  ? 187 ALA A N   1 
ATOM   1351 C CA  . ALA A 1 188 ? -2.007  -14.648 29.080 1.00 19.58  ? 187 ALA A CA  1 
ATOM   1352 C C   . ALA A 1 188 ? -1.012  -14.604 30.232 1.00 24.26  ? 187 ALA A C   1 
ATOM   1353 O O   . ALA A 1 188 ? -0.800  -15.603 30.934 1.00 33.37  ? 187 ALA A O   1 
ATOM   1354 C CB  . ALA A 1 188 ? -1.254  -14.911 27.777 1.00 30.55  ? 187 ALA A CB  1 
ATOM   1355 N N   . ARG A 1 189 ? -0.370  -13.467 30.482 1.00 35.21  ? 188 ARG A N   1 
ATOM   1356 C CA  . ARG A 1 189 ? 0.495   -13.375 31.667 1.00 33.04  ? 188 ARG A CA  1 
ATOM   1357 C C   . ARG A 1 189 ? -0.330  -13.482 32.944 1.00 32.65  ? 188 ARG A C   1 
ATOM   1358 O O   . ARG A 1 189 ? 0.023   -14.049 33.981 1.00 22.52  ? 188 ARG A O   1 
ATOM   1359 C CB  . ARG A 1 189 ? 1.283   -12.064 31.613 1.00 27.02  ? 188 ARG A CB  1 
ATOM   1360 C CG  . ARG A 1 189 ? 2.011   -11.705 32.897 1.00 22.83  ? 188 ARG A CG  1 
ATOM   1361 C CD  . ARG A 1 189 ? 1.233   -10.671 33.708 1.00 19.76  ? 188 ARG A CD  1 
ATOM   1362 N NE  . ARG A 1 189 ? 1.942   -10.347 34.941 1.00 21.39  ? 188 ARG A NE  1 
ATOM   1363 C CZ  . ARG A 1 189 ? 1.928   -11.085 36.047 1.00 22.36  ? 188 ARG A CZ  1 
ATOM   1364 N NH1 . ARG A 1 189 ? 1.252   -12.219 36.148 1.00 26.04  ? 188 ARG A NH1 1 
ATOM   1365 N NH2 . ARG A 1 189 ? 2.624   -10.671 37.102 1.00 18.71  ? 188 ARG A NH2 1 
ATOM   1366 N N   . SER A 1 190 ? -1.537  -12.911 32.903 1.00 35.66  ? 189 SER A N   1 
ATOM   1367 C CA  . SER A 1 190 ? -2.360  -12.951 34.115 1.00 35.36  ? 189 SER A CA  1 
ATOM   1368 C C   . SER A 1 190 ? -2.993  -14.323 34.309 1.00 35.83  ? 189 SER A C   1 
ATOM   1369 O O   . SER A 1 190 ? -3.203  -14.747 35.443 1.00 24.85  ? 189 SER A O   1 
ATOM   1370 C CB  . SER A 1 190 ? -3.426  -11.858 34.039 1.00 29.03  ? 189 SER A CB  1 
ATOM   1371 O OG  . SER A 1 190 ? -2.787  -10.586 33.972 1.00 28.08  ? 189 SER A OG  1 
ATOM   1372 N N   . PHE A 1 191 ? -3.272  -14.990 33.199 1.00 26.46  ? 190 PHE A N   1 
ATOM   1373 C CA  . PHE A 1 191 ? -3.995  -16.240 33.145 1.00 22.62  ? 190 PHE A CA  1 
ATOM   1374 C C   . PHE A 1 191 ? -3.178  -17.451 33.552 1.00 24.84  ? 190 PHE A C   1 
ATOM   1375 O O   . PHE A 1 191 ? -3.718  -18.296 34.278 1.00 36.32  ? 190 PHE A O   1 
ATOM   1376 C CB  . PHE A 1 191 ? -4.502  -16.450 31.699 1.00 36.65  ? 190 PHE A CB  1 
ATOM   1377 C CG  . PHE A 1 191 ? -5.563  -17.540 31.654 1.00 44.18  ? 190 PHE A CG  1 
ATOM   1378 C CD1 . PHE A 1 191 ? -6.629  -17.498 32.538 1.00 48.83  ? 190 PHE A CD1 1 
ATOM   1379 C CD2 . PHE A 1 191 ? -5.475  -18.570 30.740 1.00 38.21  ? 190 PHE A CD2 1 
ATOM   1380 C CE1 . PHE A 1 191 ? -7.607  -18.474 32.516 1.00 46.01  ? 190 PHE A CE1 1 
ATOM   1381 C CE2 . PHE A 1 191 ? -6.443  -19.552 30.717 1.00 36.13  ? 190 PHE A CE2 1 
ATOM   1382 C CZ  . PHE A 1 191 ? -7.504  -19.505 31.602 1.00 39.56  ? 190 PHE A CZ  1 
ATOM   1383 N N   . GLY A 1 192 ? -1.940  -17.520 33.089 1.00 28.41  ? 191 GLY A N   1 
ATOM   1384 C CA  . GLY A 1 192 ? -0.943  -18.521 33.395 1.00 21.96  ? 191 GLY A CA  1 
ATOM   1385 C C   . GLY A 1 192 ? -0.777  -18.820 34.877 1.00 31.02  ? 191 GLY A C   1 
ATOM   1386 O O   . GLY A 1 192 ? -1.123  -19.923 35.333 1.00 37.42  ? 191 GLY A O   1 
ATOM   1387 N N   . PRO A 1 193 ? -0.285  -17.883 35.683 1.00 23.04  ? 192 PRO A N   1 
ATOM   1388 C CA  . PRO A 1 193 ? -0.111  -18.081 37.124 1.00 28.36  ? 192 PRO A CA  1 
ATOM   1389 C C   . PRO A 1 193 ? -1.421  -18.437 37.841 1.00 33.54  ? 192 PRO A C   1 
ATOM   1390 O O   . PRO A 1 193 ? -1.454  -19.257 38.758 1.00 28.20  ? 192 PRO A O   1 
ATOM   1391 C CB  . PRO A 1 193 ? 0.376   -16.722 37.635 1.00 26.89  ? 192 PRO A CB  1 
ATOM   1392 C CG  . PRO A 1 193 ? 0.072   -15.749 36.549 1.00 30.66  ? 192 PRO A CG  1 
ATOM   1393 C CD  . PRO A 1 193 ? 0.107   -16.529 35.263 1.00 28.63  ? 192 PRO A CD  1 
ATOM   1394 N N   . ALA A 1 194 ? -2.508  -17.801 37.417 1.00 29.64  ? 193 ALA A N   1 
ATOM   1395 C CA  . ALA A 1 194 ? -3.838  -18.018 37.958 1.00 27.98  ? 193 ALA A CA  1 
ATOM   1396 C C   . ALA A 1 194 ? -4.263  -19.479 37.882 1.00 36.22  ? 193 ALA A C   1 
ATOM   1397 O O   . ALA A 1 194 ? -4.720  -20.078 38.854 1.00 36.37  ? 193 ALA A O   1 
ATOM   1398 C CB  . ALA A 1 194 ? -4.857  -17.169 37.206 1.00 20.30  ? 193 ALA A CB  1 
ATOM   1399 N N   . VAL A 1 195 ? -4.103  -20.014 36.676 1.00 32.26  ? 194 VAL A N   1 
ATOM   1400 C CA  . VAL A 1 195 ? -4.449  -21.411 36.435 1.00 32.38  ? 194 VAL A CA  1 
ATOM   1401 C C   . VAL A 1 195 ? -3.635  -22.289 37.379 1.00 39.17  ? 194 VAL A C   1 
ATOM   1402 O O   . VAL A 1 195 ? -4.168  -23.145 38.079 1.00 35.85  ? 194 VAL A O   1 
ATOM   1403 C CB  . VAL A 1 195 ? -4.188  -21.829 34.978 1.00 32.44  ? 194 VAL A CB  1 
ATOM   1404 C CG1 . VAL A 1 195 ? -3.993  -23.331 34.869 1.00 37.23  ? 194 VAL A CG1 1 
ATOM   1405 C CG2 . VAL A 1 195 ? -5.330  -21.388 34.074 1.00 22.31  ? 194 VAL A CG2 1 
ATOM   1406 N N   . VAL A 1 196 ? -2.327  -22.020 37.363 1.00 38.09  ? 195 VAL A N   1 
ATOM   1407 C CA  . VAL A 1 196 ? -1.429  -22.813 38.198 1.00 30.91  ? 195 VAL A CA  1 
ATOM   1408 C C   . VAL A 1 196 ? -1.716  -22.577 39.664 1.00 37.35  ? 195 VAL A C   1 
ATOM   1409 O O   . VAL A 1 196 ? -1.579  -23.507 40.468 1.00 30.98  ? 195 VAL A O   1 
ATOM   1410 C CB  . VAL A 1 196 ? 0.040   -22.521 37.857 1.00 23.57  ? 195 VAL A CB  1 
ATOM   1411 C CG1 . VAL A 1 196 ? 1.010   -23.217 38.785 1.00 15.41  ? 195 VAL A CG1 1 
ATOM   1412 C CG2 . VAL A 1 196 ? 0.287   -22.966 36.411 1.00 22.71  ? 195 VAL A CG2 1 
ATOM   1413 N N   . MET A 1 197 ? -2.126  -21.380 40.102 1.00 43.41  ? 196 MET A N   1 
ATOM   1414 C CA  . MET A 1 197 ? -2.318  -21.291 41.558 1.00 42.33  ? 196 MET A CA  1 
ATOM   1415 C C   . MET A 1 197 ? -3.772  -21.392 41.993 1.00 44.96  ? 196 MET A C   1 
ATOM   1416 O O   . MET A 1 197 ? -4.042  -21.348 43.192 1.00 46.55  ? 196 MET A O   1 
ATOM   1417 C CB  . MET A 1 197 ? -1.752  -19.972 42.090 1.00 24.97  ? 196 MET A CB  1 
ATOM   1418 C CG  . MET A 1 197 ? -0.257  -19.852 41.922 1.00 22.50  ? 196 MET A CG  1 
ATOM   1419 S SD  . MET A 1 197 ? 0.690   -20.946 42.964 1.00 45.05  ? 196 MET A SD  1 
ATOM   1420 C CE  . MET A 1 197 ? 0.745   -22.436 41.976 1.00 68.22  ? 196 MET A CE  1 
ATOM   1421 N N   . ASN A 1 198 ? -4.706  -21.505 41.057 1.00 49.68  ? 197 ASN A N   1 
ATOM   1422 C CA  . ASN A 1 198 ? -6.114  -21.476 41.433 1.00 51.20  ? 197 ASN A CA  1 
ATOM   1423 C C   . ASN A 1 198 ? -6.411  -20.210 42.235 1.00 46.04  ? 197 ASN A C   1 
ATOM   1424 O O   . ASN A 1 198 ? -6.953  -20.280 43.335 1.00 42.68  ? 197 ASN A O   1 
ATOM   1425 C CB  . ASN A 1 198 ? -6.529  -22.706 42.242 1.00 52.55  ? 197 ASN A CB  1 
ATOM   1426 C CG  . ASN A 1 198 ? -7.557  -23.529 41.493 1.00 58.61  ? 197 ASN A CG  1 
ATOM   1427 O OD1 . ASN A 1 198 ? -7.478  -24.758 41.473 1.00 69.89  ? 197 ASN A OD1 1 
ATOM   1428 N ND2 . ASN A 1 198 ? -8.512  -22.855 40.860 1.00 53.22  ? 197 ASN A ND2 1 
ATOM   1429 N N   . ARG A 1 199 ? -6.028  -19.089 41.647 1.00 36.36  ? 198 ARG A N   1 
ATOM   1430 C CA  . ARG A 1 199 ? -6.331  -17.769 42.153 1.00 28.72  ? 198 ARG A CA  1 
ATOM   1431 C C   . ARG A 1 199 ? -6.984  -16.937 41.054 1.00 26.37  ? 198 ARG A C   1 
ATOM   1432 O O   . ARG A 1 199 ? -6.319  -16.381 40.193 1.00 42.73  ? 198 ARG A O   1 
ATOM   1433 C CB  . ARG A 1 199 ? -5.113  -16.978 42.623 1.00 40.60  ? 198 ARG A CB  1 
ATOM   1434 C CG  . ARG A 1 199 ? -4.361  -17.573 43.774 1.00 50.78  ? 198 ARG A CG  1 
ATOM   1435 C CD  . ARG A 1 199 ? -4.285  -16.689 45.017 1.00 50.28  ? 198 ARG A CD  1 
ATOM   1436 N NE  . ARG A 1 199 ? -3.172  -17.225 45.829 1.00 53.01  ? 198 ARG A NE  1 
ATOM   1437 C CZ  . ARG A 1 199 ? -3.267  -18.403 46.440 1.00 48.89  ? 198 ARG A CZ  1 
ATOM   1438 N NH1 . ARG A 1 199 ? -4.380  -19.113 46.342 1.00 36.23  ? 198 ARG A NH1 1 
ATOM   1439 N NH2 . ARG A 1 199 ? -2.242  -18.848 47.151 1.00 55.65  ? 198 ARG A NH2 1 
ATOM   1440 N N   . PHE A 1 200 ? -8.302  -16.852 41.094 1.00 33.55  ? 199 PHE A N   1 
ATOM   1441 C CA  . PHE A 1 200 ? -8.993  -15.896 40.239 1.00 38.73  ? 199 PHE A CA  1 
ATOM   1442 C C   . PHE A 1 200 ? -9.656  -14.846 41.127 1.00 44.74  ? 199 PHE A C   1 
ATOM   1443 O O   . PHE A 1 200 ? -10.837 -14.934 41.451 1.00 71.91  ? 199 PHE A O   1 
ATOM   1444 C CB  . PHE A 1 200 ? -9.999  -16.600 39.328 1.00 31.84  ? 199 PHE A CB  1 
ATOM   1445 C CG  . PHE A 1 200 ? -9.232  -17.375 38.261 1.00 41.87  ? 199 PHE A CG  1 
ATOM   1446 C CD1 . PHE A 1 200 ? -9.216  -16.940 36.949 1.00 32.09  ? 199 PHE A CD1 1 
ATOM   1447 C CD2 . PHE A 1 200 ? -8.544  -18.517 38.615 1.00 46.97  ? 199 PHE A CD2 1 
ATOM   1448 C CE1 . PHE A 1 200 ? -8.510  -17.657 36.008 1.00 36.41  ? 199 PHE A CE1 1 
ATOM   1449 C CE2 . PHE A 1 200 ? -7.834  -19.238 37.676 1.00 42.59  ? 199 PHE A CE2 1 
ATOM   1450 C CZ  . PHE A 1 200 ? -7.821  -18.793 36.369 1.00 38.66  ? 199 PHE A CZ  1 
ATOM   1451 N N   . SER A 1 201 ? -8.842  -13.879 41.512 1.00 47.65  ? 200 SER A N   1 
ATOM   1452 C CA  . SER A 1 201 ? -9.268  -12.661 42.186 1.00 57.72  ? 200 SER A CA  1 
ATOM   1453 C C   . SER A 1 201 ? -10.576 -12.152 41.592 1.00 64.19  ? 200 SER A C   1 
ATOM   1454 O O   . SER A 1 201 ? -10.793 -12.240 40.375 1.00 97.89  ? 200 SER A O   1 
ATOM   1455 C CB  . SER A 1 201 ? -8.168  -11.603 42.053 1.00 69.27  ? 200 SER A CB  1 
ATOM   1456 O OG  . SER A 1 201 ? -7.240  -11.978 41.038 1.00 78.70  ? 200 SER A OG  1 
ATOM   1457 N N   . PRO A 1 202 ? -11.462 -11.617 42.418 1.00 59.43  ? 201 PRO A N   1 
ATOM   1458 C CA  . PRO A 1 202 ? -12.713 -11.041 41.905 1.00 54.49  ? 201 PRO A CA  1 
ATOM   1459 C C   . PRO A 1 202 ? -12.529 -10.077 40.729 1.00 45.87  ? 201 PRO A C   1 
ATOM   1460 O O   . PRO A 1 202 ? -13.462 -9.901  39.939 1.00 36.28  ? 201 PRO A O   1 
ATOM   1461 C CB  . PRO A 1 202 ? -13.251 -10.289 43.134 1.00 50.15  ? 201 PRO A CB  1 
ATOM   1462 C CG  . PRO A 1 202 ? -12.708 -11.051 44.305 1.00 47.54  ? 201 PRO A CG  1 
ATOM   1463 C CD  . PRO A 1 202 ? -11.351 -11.538 43.885 1.00 52.85  ? 201 PRO A CD  1 
ATOM   1464 N N   . ALA A 1 203 ? -11.371 -9.445  40.582 1.00 34.90  ? 202 ALA A N   1 
ATOM   1465 C CA  . ALA A 1 203 ? -11.092 -8.467  39.551 1.00 33.19  ? 202 ALA A CA  1 
ATOM   1466 C C   . ALA A 1 203 ? -10.327 -9.047  38.364 1.00 30.76  ? 202 ALA A C   1 
ATOM   1467 O O   . ALA A 1 203 ? -9.805  -8.280  37.554 1.00 31.89  ? 202 ALA A O   1 
ATOM   1468 C CB  . ALA A 1 203 ? -10.289 -7.302  40.118 1.00 53.53  ? 202 ALA A CB  1 
ATOM   1469 N N   . HIS A 1 204 ? -10.279 -10.366 38.269 1.00 30.96  ? 203 HIS A N   1 
ATOM   1470 C CA  . HIS A 1 204 ? -9.621  -11.007 37.134 1.00 37.83  ? 203 HIS A CA  1 
ATOM   1471 C C   . HIS A 1 204 ? -10.020 -10.428 35.786 1.00 36.76  ? 203 HIS A C   1 
ATOM   1472 O O   . HIS A 1 204 ? -9.185  -10.255 34.891 1.00 35.75  ? 203 HIS A O   1 
ATOM   1473 C CB  . HIS A 1 204 ? -9.922  -12.515 37.117 1.00 38.23  ? 203 HIS A CB  1 
ATOM   1474 C CG  . HIS A 1 204 ? -8.641  -13.282 36.997 1.00 58.61  ? 203 HIS A CG  1 
ATOM   1475 N ND1 . HIS A 1 204 ? -7.801  -13.479 38.076 1.00 72.71  ? 203 HIS A ND1 1 
ATOM   1476 C CD2 . HIS A 1 204 ? -8.050  -13.881 35.939 1.00 66.50  ? 203 HIS A CD2 1 
ATOM   1477 C CE1 . HIS A 1 204 ? -6.750  -14.179 37.691 1.00 78.48  ? 203 HIS A CE1 1 
ATOM   1478 N NE2 . HIS A 1 204 ? -6.874  -14.432 36.398 1.00 77.58  ? 203 HIS A NE2 1 
ATOM   1479 N N   . TRP A 1 205 ? -11.296 -10.098 35.629 1.00 34.60  ? 204 TRP A N   1 
ATOM   1480 C CA  . TRP A 1 205 ? -11.824 -9.585  34.375 1.00 39.16  ? 204 TRP A CA  1 
ATOM   1481 C C   . TRP A 1 205 ? -11.004 -8.401  33.851 1.00 43.42  ? 204 TRP A C   1 
ATOM   1482 O O   . TRP A 1 205 ? -10.942 -8.213  32.632 1.00 32.51  ? 204 TRP A O   1 
ATOM   1483 C CB  . TRP A 1 205 ? -13.289 -9.129  34.519 1.00 37.70  ? 204 TRP A CB  1 
ATOM   1484 C CG  . TRP A 1 205 ? -13.370 -7.881  35.353 1.00 45.73  ? 204 TRP A CG  1 
ATOM   1485 C CD1 . TRP A 1 205 ? -13.317 -7.825  36.715 1.00 46.29  ? 204 TRP A CD1 1 
ATOM   1486 C CD2 . TRP A 1 205 ? -13.506 -6.530  34.901 1.00 54.95  ? 204 TRP A CD2 1 
ATOM   1487 N NE1 . TRP A 1 205 ? -13.413 -6.519  37.139 1.00 51.97  ? 204 TRP A NE1 1 
ATOM   1488 C CE2 . TRP A 1 205 ? -13.534 -5.705  36.045 1.00 57.08  ? 204 TRP A CE2 1 
ATOM   1489 C CE3 . TRP A 1 205 ? -13.612 -5.926  33.643 1.00 55.44  ? 204 TRP A CE3 1 
ATOM   1490 C CZ2 . TRP A 1 205 ? -13.660 -4.317  35.974 1.00 54.99  ? 204 TRP A CZ2 1 
ATOM   1491 C CZ3 . TRP A 1 205 ? -13.737 -4.551  33.570 1.00 57.42  ? 204 TRP A CZ3 1 
ATOM   1492 C CH2 . TRP A 1 205 ? -13.761 -3.763  34.729 1.00 57.91  ? 204 TRP A CH2 1 
ATOM   1493 N N   . VAL A 1 206 ? -10.438 -7.641  34.790 1.00 34.61  ? 205 VAL A N   1 
ATOM   1494 C CA  . VAL A 1 206 ? -9.717  -6.425  34.470 1.00 35.06  ? 205 VAL A CA  1 
ATOM   1495 C C   . VAL A 1 206 ? -8.542  -6.797  33.567 1.00 40.52  ? 205 VAL A C   1 
ATOM   1496 O O   . VAL A 1 206 ? -8.304  -6.173  32.533 1.00 66.72  ? 205 VAL A O   1 
ATOM   1497 C CB  . VAL A 1 206 ? -9.200  -5.680  35.711 1.00 40.02  ? 205 VAL A CB  1 
ATOM   1498 C CG1 . VAL A 1 206 ? -8.486  -4.392  35.320 1.00 39.53  ? 205 VAL A CG1 1 
ATOM   1499 C CG2 . VAL A 1 206 ? -10.326 -5.354  36.679 1.00 39.88  ? 205 VAL A CG2 1 
ATOM   1500 N N   . PHE A 1 207 ? -7.831  -7.834  33.998 1.00 33.76  ? 206 PHE A N   1 
ATOM   1501 C CA  . PHE A 1 207 ? -6.593  -8.209  33.325 1.00 27.96  ? 206 PHE A CA  1 
ATOM   1502 C C   . PHE A 1 207 ? -6.845  -8.673  31.902 1.00 28.24  ? 206 PHE A C   1 
ATOM   1503 O O   . PHE A 1 207 ? -5.906  -8.757  31.107 1.00 51.39  ? 206 PHE A O   1 
ATOM   1504 C CB  . PHE A 1 207 ? -5.870  -9.294  34.131 1.00 33.33  ? 206 PHE A CB  1 
ATOM   1505 C CG  . PHE A 1 207 ? -5.759  -8.933  35.602 1.00 35.10  ? 206 PHE A CG  1 
ATOM   1506 C CD1 . PHE A 1 207 ? -5.597  -7.612  35.979 1.00 36.21  ? 206 PHE A CD1 1 
ATOM   1507 C CD2 . PHE A 1 207 ? -5.820  -9.907  36.579 1.00 40.22  ? 206 PHE A CD2 1 
ATOM   1508 C CE1 . PHE A 1 207 ? -5.502  -7.269  37.316 1.00 35.60  ? 206 PHE A CE1 1 
ATOM   1509 C CE2 . PHE A 1 207 ? -5.727  -9.569  37.918 1.00 43.78  ? 206 PHE A CE2 1 
ATOM   1510 C CZ  . PHE A 1 207 ? -5.580  -8.248  38.287 1.00 39.80  ? 206 PHE A CZ  1 
ATOM   1511 N N   . TRP A 1 208 ? -8.093  -8.963  31.548 1.00 33.66  ? 207 TRP A N   1 
ATOM   1512 C CA  . TRP A 1 208 ? -8.389  -9.305  30.153 1.00 35.54  ? 207 TRP A CA  1 
ATOM   1513 C C   . TRP A 1 208 ? -8.940  -8.115  29.369 1.00 23.91  ? 207 TRP A C   1 
ATOM   1514 O O   . TRP A 1 208 ? -8.365  -7.682  28.370 1.00 32.37  ? 207 TRP A O   1 
ATOM   1515 C CB  . TRP A 1 208 ? -9.368  -10.477 30.116 1.00 40.19  ? 207 TRP A CB  1 
ATOM   1516 C CG  . TRP A 1 208 ? -8.813  -11.764 30.649 1.00 43.58  ? 207 TRP A CG  1 
ATOM   1517 C CD1 . TRP A 1 208 ? -8.511  -12.057 31.944 1.00 47.54  ? 207 TRP A CD1 1 
ATOM   1518 C CD2 . TRP A 1 208 ? -8.494  -12.943 29.892 1.00 48.51  ? 207 TRP A CD2 1 
ATOM   1519 N NE1 . TRP A 1 208 ? -8.024  -13.338 32.053 1.00 46.74  ? 207 TRP A NE1 1 
ATOM   1520 C CE2 . TRP A 1 208 ? -8.004  -13.902 30.803 1.00 48.29  ? 207 TRP A CE2 1 
ATOM   1521 C CE3 . TRP A 1 208 ? -8.576  -13.274 28.531 1.00 41.20  ? 207 TRP A CE3 1 
ATOM   1522 C CZ2 . TRP A 1 208 ? -7.597  -15.176 30.400 1.00 42.57  ? 207 TRP A CZ2 1 
ATOM   1523 C CZ3 . TRP A 1 208 ? -8.170  -14.539 28.135 1.00 33.97  ? 207 TRP A CZ3 1 
ATOM   1524 C CH2 . TRP A 1 208 ? -7.692  -15.462 29.066 1.00 40.72  ? 207 TRP A CH2 1 
ATOM   1525 N N   . VAL A 1 209 ? -10.058 -7.578  29.813 1.00 23.43  ? 208 VAL A N   1 
ATOM   1526 C CA  . VAL A 1 209 ? -10.828 -6.536  29.171 1.00 28.55  ? 208 VAL A CA  1 
ATOM   1527 C C   . VAL A 1 209 ? -10.064 -5.226  29.059 1.00 17.63  ? 208 VAL A C   1 
ATOM   1528 O O   . VAL A 1 209 ? -10.113 -4.560  28.030 1.00 37.55  ? 208 VAL A O   1 
ATOM   1529 C CB  . VAL A 1 209 ? -12.133 -6.257  29.955 1.00 39.64  ? 208 VAL A CB  1 
ATOM   1530 C CG1 . VAL A 1 209 ? -12.779 -4.979  29.433 1.00 27.28  ? 208 VAL A CG1 1 
ATOM   1531 C CG2 . VAL A 1 209 ? -13.087 -7.436  29.879 1.00 37.25  ? 208 VAL A CG2 1 
ATOM   1532 N N   . GLY A 1 210 ? -9.359  -4.839  30.112 1.00 22.31  ? 209 GLY A N   1 
ATOM   1533 C CA  . GLY A 1 210 ? -8.555  -3.623  30.040 1.00 21.84  ? 209 GLY A CA  1 
ATOM   1534 C C   . GLY A 1 210 ? -7.525  -3.763  28.932 1.00 26.70  ? 209 GLY A C   1 
ATOM   1535 O O   . GLY A 1 210 ? -7.521  -3.001  27.953 1.00 33.33  ? 209 GLY A O   1 
ATOM   1536 N N   . PRO A 1 211 ? -6.642  -4.744  29.065 1.00 29.97  ? 210 PRO A N   1 
ATOM   1537 C CA  . PRO A 1 211 ? -5.651  -4.997  28.009 1.00 35.66  ? 210 PRO A CA  1 
ATOM   1538 C C   . PRO A 1 211 ? -6.276  -5.181  26.636 1.00 35.12  ? 210 PRO A C   1 
ATOM   1539 O O   . PRO A 1 211 ? -5.822  -4.598  25.639 1.00 27.96  ? 210 PRO A O   1 
ATOM   1540 C CB  . PRO A 1 211 ? -4.995  -6.302  28.485 1.00 38.28  ? 210 PRO A CB  1 
ATOM   1541 C CG  . PRO A 1 211 ? -5.117  -6.240  29.981 1.00 20.87  ? 210 PRO A CG  1 
ATOM   1542 C CD  . PRO A 1 211 ? -6.488  -5.672  30.204 1.00 22.73  ? 210 PRO A CD  1 
ATOM   1543 N N   . ILE A 1 212 ? -7.339  -5.978  26.493 1.00 27.53  ? 211 ILE A N   1 
ATOM   1544 C CA  . ILE A 1 212 ? -7.869  -6.163  25.138 1.00 29.61  ? 211 ILE A CA  1 
ATOM   1545 C C   . ILE A 1 212 ? -8.537  -4.919  24.581 1.00 40.01  ? 211 ILE A C   1 
ATOM   1546 O O   . ILE A 1 212 ? -8.501  -4.659  23.368 1.00 31.08  ? 211 ILE A O   1 
ATOM   1547 C CB  . ILE A 1 212 ? -8.854  -7.349  25.114 1.00 24.48  ? 211 ILE A CB  1 
ATOM   1548 C CG1 . ILE A 1 212 ? -8.145  -8.666  25.420 1.00 30.95  ? 211 ILE A CG1 1 
ATOM   1549 C CG2 . ILE A 1 212 ? -9.611  -7.394  23.797 1.00 20.97  ? 211 ILE A CG2 1 
ATOM   1550 C CD1 . ILE A 1 212 ? -9.009  -9.906  25.473 1.00 21.30  ? 211 ILE A CD1 1 
ATOM   1551 N N   . VAL A 1 213 ? -9.166  -4.108  25.439 1.00 35.20  ? 212 VAL A N   1 
ATOM   1552 C CA  . VAL A 1 213 ? -9.793  -2.906  24.889 1.00 36.70  ? 212 VAL A CA  1 
ATOM   1553 C C   . VAL A 1 213 ? -8.744  -1.961  24.304 1.00 28.83  ? 212 VAL A C   1 
ATOM   1554 O O   . VAL A 1 213 ? -8.797  -1.611  23.124 1.00 35.05  ? 212 VAL A O   1 
ATOM   1555 C CB  . VAL A 1 213 ? -10.615 -2.151  25.950 1.00 38.24  ? 212 VAL A CB  1 
ATOM   1556 C CG1 . VAL A 1 213 ? -10.914 -0.733  25.478 1.00 36.77  ? 212 VAL A CG1 1 
ATOM   1557 C CG2 . VAL A 1 213 ? -11.906 -2.885  26.256 1.00 43.44  ? 212 VAL A CG2 1 
ATOM   1558 N N   . GLY A 1 214 ? -7.811  -1.559  25.153 1.00 29.19  ? 213 GLY A N   1 
ATOM   1559 C CA  . GLY A 1 214 ? -6.730  -0.629  24.882 1.00 29.18  ? 213 GLY A CA  1 
ATOM   1560 C C   . GLY A 1 214 ? -5.991  -0.953  23.595 1.00 25.04  ? 213 GLY A C   1 
ATOM   1561 O O   . GLY A 1 214 ? -5.592  -0.024  22.884 1.00 36.47  ? 213 GLY A O   1 
ATOM   1562 N N   . ALA A 1 215 ? -5.848  -2.244  23.346 1.00 25.91  ? 214 ALA A N   1 
ATOM   1563 C CA  . ALA A 1 215 ? -5.194  -2.849  22.198 1.00 42.01  ? 214 ALA A CA  1 
ATOM   1564 C C   . ALA A 1 215 ? -5.988  -2.636  20.906 1.00 45.78  ? 214 ALA A C   1 
ATOM   1565 O O   . ALA A 1 215 ? -5.522  -1.987  19.974 1.00 26.09  ? 214 ALA A O   1 
ATOM   1566 C CB  . ALA A 1 215 ? -4.972  -4.338  22.449 1.00 47.41  ? 214 ALA A CB  1 
ATOM   1567 N N   . VAL A 1 216 ? -7.195  -3.180  20.878 1.00 44.67  ? 215 VAL A N   1 
ATOM   1568 C CA  . VAL A 1 216 ? -8.183  -2.974  19.831 1.00 31.43  ? 215 VAL A CA  1 
ATOM   1569 C C   . VAL A 1 216 ? -8.353  -1.498  19.516 1.00 27.52  ? 215 VAL A C   1 
ATOM   1570 O O   . VAL A 1 216 ? -8.410  -1.028  18.378 1.00 26.21  ? 215 VAL A O   1 
ATOM   1571 C CB  . VAL A 1 216 ? -9.523  -3.581  20.287 1.00 25.04  ? 215 VAL A CB  1 
ATOM   1572 C CG1 . VAL A 1 216 ? -10.590 -3.375  19.232 1.00 33.51  ? 215 VAL A CG1 1 
ATOM   1573 C CG2 . VAL A 1 216 ? -9.322  -5.060  20.605 1.00 24.32  ? 215 VAL A CG2 1 
ATOM   1574 N N   . LEU A 1 217 ? -8.427  -0.714  20.595 1.00 32.34  ? 216 LEU A N   1 
ATOM   1575 C CA  . LEU A 1 217 ? -8.520  0.731   20.427 1.00 27.49  ? 216 LEU A CA  1 
ATOM   1576 C C   . LEU A 1 217 ? -7.303  1.266   19.694 1.00 27.59  ? 216 LEU A C   1 
ATOM   1577 O O   . LEU A 1 217 ? -7.417  2.123   18.816 1.00 37.30  ? 216 LEU A O   1 
ATOM   1578 C CB  . LEU A 1 217 ? -8.674  1.395   21.798 1.00 29.02  ? 216 LEU A CB  1 
ATOM   1579 C CG  . LEU A 1 217 ? -10.083 1.255   22.390 1.00 24.87  ? 216 LEU A CG  1 
ATOM   1580 C CD1 . LEU A 1 217 ? -10.229 2.182   23.586 1.00 25.65  ? 216 LEU A CD1 1 
ATOM   1581 C CD2 . LEU A 1 217 ? -11.128 1.529   21.324 1.00 33.23  ? 216 LEU A CD2 1 
ATOM   1582 N N   . ALA A 1 218 ? -6.118  0.761   20.052 1.00 28.60  ? 217 ALA A N   1 
ATOM   1583 C CA  . ALA A 1 218 ? -4.920  1.256   19.370 1.00 26.99  ? 217 ALA A CA  1 
ATOM   1584 C C   . ALA A 1 218 ? -4.875  0.823   17.905 1.00 37.81  ? 217 ALA A C   1 
ATOM   1585 O O   . ALA A 1 218 ? -4.423  1.566   17.033 1.00 38.80  ? 217 ALA A O   1 
ATOM   1586 C CB  . ALA A 1 218 ? -3.684  0.760   20.091 1.00 23.06  ? 217 ALA A CB  1 
ATOM   1587 N N   . ALA A 1 219 ? -5.336  -0.402  17.660 1.00 35.93  ? 218 ALA A N   1 
ATOM   1588 C CA  . ALA A 1 219 ? -5.435  -0.976  16.332 1.00 38.06  ? 218 ALA A CA  1 
ATOM   1589 C C   . ALA A 1 219 ? -6.491  -0.226  15.532 1.00 37.03  ? 218 ALA A C   1 
ATOM   1590 O O   . ALA A 1 219 ? -6.252  0.039   14.357 1.00 29.81  ? 218 ALA A O   1 
ATOM   1591 C CB  . ALA A 1 219 ? -5.754  -2.461  16.392 1.00 34.25  ? 218 ALA A CB  1 
ATOM   1592 N N   . ILE A 1 220 ? -7.640  0.136   16.123 1.00 26.90  ? 219 ILE A N   1 
ATOM   1593 C CA  . ILE A 1 220 ? -8.565  0.875   15.263 1.00 25.86  ? 219 ILE A CA  1 
ATOM   1594 C C   . ILE A 1 220 ? -7.956  2.202   14.825 1.00 26.97  ? 219 ILE A C   1 
ATOM   1595 O O   . ILE A 1 220 ? -7.923  2.487   13.632 1.00 41.81  ? 219 ILE A O   1 
ATOM   1596 C CB  . ILE A 1 220 ? -9.909  1.150   15.942 1.00 27.31  ? 219 ILE A CB  1 
ATOM   1597 C CG1 . ILE A 1 220 ? -10.794 -0.096  16.044 1.00 37.63  ? 219 ILE A CG1 1 
ATOM   1598 C CG2 . ILE A 1 220 ? -10.642 2.294   15.246 1.00 27.66  ? 219 ILE A CG2 1 
ATOM   1599 C CD1 . ILE A 1 220 ? -11.769 -0.058  17.202 1.00 48.26  ? 219 ILE A CD1 1 
ATOM   1600 N N   . LEU A 1 221 ? -7.489  2.988   15.793 1.00 26.65  ? 220 LEU A N   1 
ATOM   1601 C CA  . LEU A 1 221 ? -6.909  4.279   15.458 1.00 25.07  ? 220 LEU A CA  1 
ATOM   1602 C C   . LEU A 1 221 ? -5.818  4.155   14.391 1.00 29.63  ? 220 LEU A C   1 
ATOM   1603 O O   . LEU A 1 221 ? -5.866  4.810   13.346 1.00 41.06  ? 220 LEU A O   1 
ATOM   1604 C CB  . LEU A 1 221 ? -6.357  4.966   16.715 1.00 34.62  ? 220 LEU A CB  1 
ATOM   1605 C CG  . LEU A 1 221 ? -5.636  6.294   16.445 1.00 39.07  ? 220 LEU A CG  1 
ATOM   1606 C CD1 . LEU A 1 221 ? -6.399  7.454   17.064 1.00 54.83  ? 220 LEU A CD1 1 
ATOM   1607 C CD2 . LEU A 1 221 ? -4.203  6.239   16.951 1.00 52.00  ? 220 LEU A CD2 1 
ATOM   1608 N N   . TYR A 1 222 ? -4.828  3.309   14.612 1.00 24.54  ? 221 TYR A N   1 
ATOM   1609 C CA  . TYR A 1 222 ? -3.655  3.195   13.789 1.00 22.11  ? 221 TYR A CA  1 
ATOM   1610 C C   . TYR A 1 222 ? -3.980  2.758   12.364 1.00 31.20  ? 221 TYR A C   1 
ATOM   1611 O O   . TYR A 1 222 ? -3.435  3.297   11.403 1.00 23.00  ? 221 TYR A O   1 
ATOM   1612 C CB  . TYR A 1 222 ? -2.666  2.178   14.400 1.00 25.67  ? 221 TYR A CB  1 
ATOM   1613 C CG  . TYR A 1 222 ? -1.347  2.180   13.648 1.00 26.42  ? 221 TYR A CG  1 
ATOM   1614 C CD1 . TYR A 1 222 ? -0.358  3.089   13.974 1.00 20.04  ? 221 TYR A CD1 1 
ATOM   1615 C CD2 . TYR A 1 222 ? -1.063  1.290   12.613 1.00 28.35  ? 221 TYR A CD2 1 
ATOM   1616 C CE1 . TYR A 1 222 ? 0.861   3.131   13.318 1.00 25.77  ? 221 TYR A CE1 1 
ATOM   1617 C CE2 . TYR A 1 222 ? 0.148   1.333   11.957 1.00 30.89  ? 221 TYR A CE2 1 
ATOM   1618 C CZ  . TYR A 1 222 ? 1.117   2.245   12.294 1.00 28.00  ? 221 TYR A CZ  1 
ATOM   1619 O OH  . TYR A 1 222 ? 2.328   2.257   11.624 1.00 24.88  ? 221 TYR A OH  1 
ATOM   1620 N N   . PHE A 1 223 ? -4.802  1.723   12.279 1.00 32.99  ? 222 PHE A N   1 
ATOM   1621 C CA  . PHE A 1 223 ? -5.010  1.055   11.000 1.00 43.04  ? 222 PHE A CA  1 
ATOM   1622 C C   . PHE A 1 223 ? -6.057  1.780   10.165 1.00 35.86  ? 222 PHE A C   1 
ATOM   1623 O O   . PHE A 1 223 ? -5.811  2.100   9.005  1.00 41.44  ? 222 PHE A O   1 
ATOM   1624 C CB  . PHE A 1 223 ? -5.392  -0.412  11.257 1.00 38.69  ? 222 PHE A CB  1 
ATOM   1625 C CG  . PHE A 1 223 ? -4.178  -1.186  11.771 1.00 36.89  ? 222 PHE A CG  1 
ATOM   1626 C CD1 . PHE A 1 223 ? -3.063  -1.317  10.967 1.00 40.22  ? 222 PHE A CD1 1 
ATOM   1627 C CD2 . PHE A 1 223 ? -4.163  -1.759  13.025 1.00 38.53  ? 222 PHE A CD2 1 
ATOM   1628 C CE1 . PHE A 1 223 ? -1.956  -2.011  11.422 1.00 42.46  ? 222 PHE A CE1 1 
ATOM   1629 C CE2 . PHE A 1 223 ? -3.060  -2.449  13.493 1.00 38.62  ? 222 PHE A CE2 1 
ATOM   1630 C CZ  . PHE A 1 223 ? -1.947  -2.571  12.686 1.00 39.14  ? 222 PHE A CZ  1 
ATOM   1631 N N   . TYR A 1 224 ? -7.182  2.022   10.816 1.00 37.41  ? 223 TYR A N   1 
ATOM   1632 C CA  . TYR A 1 224 ? -8.373  2.591   10.213 1.00 34.95  ? 223 TYR A CA  1 
ATOM   1633 C C   . TYR A 1 224 ? -8.430  4.104   10.212 1.00 46.46  ? 223 TYR A C   1 
ATOM   1634 O O   . TYR A 1 224 ? -9.188  4.692   9.432  1.00 55.90  ? 223 TYR A O   1 
ATOM   1635 C CB  . TYR A 1 224 ? -9.575  1.992   10.975 1.00 25.89  ? 223 TYR A CB  1 
ATOM   1636 C CG  . TYR A 1 224 ? -9.597  0.485   10.777 1.00 36.85  ? 223 TYR A CG  1 
ATOM   1637 C CD1 . TYR A 1 224 ? -9.329  -0.044  9.517  1.00 37.91  ? 223 TYR A CD1 1 
ATOM   1638 C CD2 . TYR A 1 224 ? -9.867  -0.390  11.814 1.00 42.97  ? 223 TYR A CD2 1 
ATOM   1639 C CE1 . TYR A 1 224 ? -9.331  -1.407  9.283  1.00 35.94  ? 223 TYR A CE1 1 
ATOM   1640 C CE2 . TYR A 1 224 ? -9.879  -1.758  11.593 1.00 53.23  ? 223 TYR A CE2 1 
ATOM   1641 C CZ  . TYR A 1 224 ? -9.611  -2.256  10.333 1.00 48.43  ? 223 TYR A CZ  1 
ATOM   1642 O OH  . TYR A 1 224 ? -9.624  -3.618  10.124 1.00 46.34  ? 223 TYR A OH  1 
ATOM   1643 N N   . LEU A 1 225 ? -7.666  4.807   11.050 1.00 51.75  ? 224 LEU A N   1 
ATOM   1644 C CA  . LEU A 1 225 ? -7.747  6.269   11.019 1.00 41.88  ? 224 LEU A CA  1 
ATOM   1645 C C   . LEU A 1 225 ? -6.438  6.908   10.572 1.00 40.59  ? 224 LEU A C   1 
ATOM   1646 O O   . LEU A 1 225 ? -6.450  7.713   9.638  1.00 54.48  ? 224 LEU A O   1 
ATOM   1647 C CB  . LEU A 1 225 ? -8.140  6.829   12.383 1.00 29.13  ? 224 LEU A CB  1 
ATOM   1648 C CG  . LEU A 1 225 ? -9.529  6.481   12.908 1.00 31.41  ? 224 LEU A CG  1 
ATOM   1649 C CD1 . LEU A 1 225 ? -9.564  5.032   13.370 1.00 54.13  ? 224 LEU A CD1 1 
ATOM   1650 C CD2 . LEU A 1 225 ? -9.936  7.403   14.047 1.00 37.55  ? 224 LEU A CD2 1 
ATOM   1651 N N   . LEU A 1 226 ? -5.337  6.563   11.232 1.00 39.03  ? 225 LEU A N   1 
ATOM   1652 C CA  . LEU A 1 226 ? -4.027  7.145   10.938 1.00 33.84  ? 225 LEU A CA  1 
ATOM   1653 C C   . LEU A 1 226 ? -3.446  6.593   9.636  1.00 37.17  ? 225 LEU A C   1 
ATOM   1654 O O   . LEU A 1 226 ? -3.147  7.328   8.687  1.00 37.15  ? 225 LEU A O   1 
ATOM   1655 C CB  . LEU A 1 226 ? -3.034  6.912   12.076 1.00 25.13  ? 225 LEU A CB  1 
ATOM   1656 C CG  . LEU A 1 226 ? -3.265  7.507   13.453 1.00 23.24  ? 225 LEU A CG  1 
ATOM   1657 C CD1 . LEU A 1 226 ? -2.115  7.161   14.388 1.00 21.65  ? 225 LEU A CD1 1 
ATOM   1658 C CD2 . LEU A 1 226 ? -3.422  9.020   13.395 1.00 28.15  ? 225 LEU A CD2 1 
ATOM   1659 N N   . PHE A 1 227 ? -3.258  5.273   9.581  1.00 29.63  ? 226 PHE A N   1 
ATOM   1660 C CA  . PHE A 1 227 ? -2.523  4.693   8.457  1.00 37.29  ? 226 PHE A CA  1 
ATOM   1661 C C   . PHE A 1 227 ? -3.340  3.607   7.781  1.00 39.43  ? 226 PHE A C   1 
ATOM   1662 O O   . PHE A 1 227 ? -3.109  2.406   7.873  1.00 41.45  ? 226 PHE A O   1 
ATOM   1663 C CB  . PHE A 1 227 ? -1.169  4.172   8.944  1.00 40.87  ? 226 PHE A CB  1 
ATOM   1664 C CG  . PHE A 1 227 ? -0.316  5.288   9.540  1.00 35.67  ? 226 PHE A CG  1 
ATOM   1665 C CD1 . PHE A 1 227 ? 0.084   6.357   8.760  1.00 43.12  ? 226 PHE A CD1 1 
ATOM   1666 C CD2 . PHE A 1 227 ? 0.068   5.260   10.865 1.00 45.25  ? 226 PHE A CD2 1 
ATOM   1667 C CE1 . PHE A 1 227 ? 0.853   7.376   9.290  1.00 42.31  ? 226 PHE A CE1 1 
ATOM   1668 C CE2 . PHE A 1 227 ? 0.851   6.268   11.405 1.00 43.65  ? 226 PHE A CE2 1 
ATOM   1669 C CZ  . PHE A 1 227 ? 1.251   7.326   10.615 1.00 38.44  ? 226 PHE A CZ  1 
ATOM   1670 N N   . PRO A 1 228 ? -4.339  4.097   7.060  1.00 40.10  ? 227 PRO A N   1 
ATOM   1671 C CA  . PRO A 1 228 ? -5.306  3.198   6.436  1.00 43.49  ? 227 PRO A CA  1 
ATOM   1672 C C   . PRO A 1 228 ? -4.671  2.607   5.181  1.00 45.39  ? 227 PRO A C   1 
ATOM   1673 O O   . PRO A 1 228 ? -3.900  3.278   4.496  1.00 37.83  ? 227 PRO A O   1 
ATOM   1674 C CB  . PRO A 1 228 ? -6.468  4.118   6.102  1.00 45.27  ? 227 PRO A CB  1 
ATOM   1675 C CG  . PRO A 1 228 ? -6.101  5.495   6.534  1.00 42.32  ? 227 PRO A CG  1 
ATOM   1676 C CD  . PRO A 1 228 ? -4.617  5.510   6.751  1.00 42.41  ? 227 PRO A CD  1 
ATOM   1677 N N   . ASN A 1 229 ? -4.978  1.348   4.894  1.00 60.53  ? 228 ASN A N   1 
ATOM   1678 C CA  . ASN A 1 229 ? -4.415  0.693   3.712  1.00 75.16  ? 228 ASN A CA  1 
ATOM   1679 C C   . ASN A 1 229 ? -5.374  0.820   2.535  1.00 76.54  ? 228 ASN A C   1 
ATOM   1680 O O   . ASN A 1 229 ? -6.592  0.749   2.698  1.00 56.56  ? 228 ASN A O   1 
ATOM   1681 C CB  . ASN A 1 229 ? -4.105  -0.775  3.994  1.00 79.07  ? 228 ASN A CB  1 
ATOM   1682 C CG  . ASN A 1 229 ? -5.287  -1.557  4.528  1.00 82.88  ? 228 ASN A CG  1 
ATOM   1683 O OD1 . ASN A 1 229 ? -6.142  -2.021  3.759  1.00 70.65  ? 228 ASN A OD1 1 
ATOM   1684 N ND2 . ASN A 1 229 ? -5.363  -1.702  5.848  1.00 118.05 ? 228 ASN A ND2 1 
ATOM   1685 N N   . SER A 1 230 ? -4.821  1.026   1.345  1.00 81.59  ? 229 SER A N   1 
ATOM   1686 C CA  . SER A 1 230 ? -5.662  1.269   0.174  1.00 87.68  ? 229 SER A CA  1 
ATOM   1687 C C   . SER A 1 230 ? -6.700  0.177   -0.015 1.00 85.90  ? 229 SER A C   1 
ATOM   1688 O O   . SER A 1 230 ? -7.782  0.391   -0.563 1.00 108.32 ? 229 SER A O   1 
ATOM   1689 C CB  . SER A 1 230 ? -4.783  1.393   -1.075 1.00 89.42  ? 229 SER A CB  1 
ATOM   1690 O OG  . SER A 1 230 ? -5.141  0.465   -2.089 1.00 85.72  ? 229 SER A OG  1 
ATOM   1691 N N   . LEU A 1 231 ? -6.400  -1.048  0.427  1.00 75.39  ? 230 LEU A N   1 
ATOM   1692 C CA  . LEU A 1 231 ? -7.290  -2.118  -0.003 1.00 72.04  ? 230 LEU A CA  1 
ATOM   1693 C C   . LEU A 1 231 ? -7.662  -3.146  1.044  1.00 63.13  ? 230 LEU A C   1 
ATOM   1694 O O   . LEU A 1 231 ? -6.814  -3.812  1.653  1.00 60.16  ? 230 LEU A O   1 
ATOM   1695 C CB  . LEU A 1 231 ? -6.616  -2.838  -1.188 1.00 90.29  ? 230 LEU A CB  1 
ATOM   1696 C CG  . LEU A 1 231 ? -5.167  -3.268  -0.951 1.00 101.36 ? 230 LEU A CG  1 
ATOM   1697 C CD1 . LEU A 1 231 ? -5.106  -4.668  -0.357 1.00 99.44  ? 230 LEU A CD1 1 
ATOM   1698 C CD2 . LEU A 1 231 ? -4.365  -3.191  -2.247 1.00 112.20 ? 230 LEU A CD2 1 
ATOM   1699 N N   . SER A 1 232 ? -8.939  -3.332  1.278  1.00 61.44  ? 231 SER A N   1 
ATOM   1700 C CA  . SER A 1 232 ? -10.168 -2.866  0.697  1.00 67.78  ? 231 SER A CA  1 
ATOM   1701 C C   . SER A 1 232 ? -10.301 -3.189  -0.792 1.00 77.80  ? 231 SER A C   1 
ATOM   1702 O O   . SER A 1 232 ? -9.377  -3.053  -1.593 1.00 73.55  ? 231 SER A O   1 
ATOM   1703 C CB  . SER A 1 232 ? -10.365 -1.355  0.919  1.00 60.38  ? 231 SER A CB  1 
ATOM   1704 O OG  . SER A 1 232 ? -11.631 -1.145  1.542  1.00 68.96  ? 231 SER A OG  1 
ATOM   1705 N N   . LEU A 1 233 ? -11.502 -3.629  -1.182 1.00 83.02  ? 232 LEU A N   1 
ATOM   1706 C CA  . LEU A 1 233 ? -12.565 -3.843  -0.191 1.00 78.01  ? 232 LEU A CA  1 
ATOM   1707 C C   . LEU A 1 233 ? -12.435 -5.278  0.301  1.00 73.84  ? 232 LEU A C   1 
ATOM   1708 O O   . LEU A 1 233 ? -11.347 -5.581  0.816  1.00 47.52  ? 232 LEU A O   1 
ATOM   1709 C CB  . LEU A 1 233 ? -13.935 -3.521  -0.774 1.00 73.53  ? 232 LEU A CB  1 
ATOM   1710 C CG  . LEU A 1 233 ? -14.203 -2.029  -1.042 1.00 65.12  ? 232 LEU A CG  1 
ATOM   1711 C CD1 . LEU A 1 233 ? -13.718 -1.643  -2.429 1.00 36.11  ? 232 LEU A CD1 1 
ATOM   1712 C CD2 . LEU A 1 233 ? -15.675 -1.692  -0.861 1.00 47.38  ? 232 LEU A CD2 1 
ATOM   1713 N N   . SER A 1 234 ? -13.414 -6.130  0.131  1.00 78.97  ? 233 SER A N   1 
ATOM   1714 C CA  . SER A 1 234 ? -13.510 -7.536  0.461  1.00 85.36  ? 233 SER A CA  1 
ATOM   1715 C C   . SER A 1 234 ? -12.302 -8.424  0.212  1.00 78.59  ? 233 SER A C   1 
ATOM   1716 O O   . SER A 1 234 ? -12.439 -9.656  0.192  1.00 42.87  ? 233 SER A O   1 
ATOM   1717 C CB  . SER A 1 234 ? -14.669 -8.151  -0.361 1.00 97.95  ? 233 SER A CB  1 
ATOM   1718 O OG  . SER A 1 234 ? -14.151 -9.144  -1.254 1.00 109.48 ? 233 SER A OG  1 
ATOM   1719 N N   . GLU A 1 235 ? -11.095 -7.929  0.016  1.00 84.44  ? 234 GLU A N   1 
ATOM   1720 C CA  . GLU A 1 235 ? -9.871  -8.704  0.137  1.00 79.29  ? 234 GLU A CA  1 
ATOM   1721 C C   . GLU A 1 235 ? -9.437  -8.599  1.610  1.00 66.32  ? 234 GLU A C   1 
ATOM   1722 O O   . GLU A 1 235 ? -8.451  -9.182  2.038  1.00 66.74  ? 234 GLU A O   1 
ATOM   1723 C CB  . GLU A 1 235 ? -8.778  -8.235  -0.799 1.00 82.10  ? 234 GLU A CB  1 
ATOM   1724 C CG  . GLU A 1 235 ? -8.192  -6.862  -0.485 1.00 84.67  ? 234 GLU A CG  1 
ATOM   1725 C CD  . GLU A 1 235 ? -7.621  -6.251  -1.759 1.00 88.59  ? 234 GLU A CD  1 
ATOM   1726 O OE1 . GLU A 1 235 ? -7.987  -5.096  -2.058 1.00 91.04  ? 234 GLU A OE1 1 
ATOM   1727 O OE2 . GLU A 1 235 ? -6.835  -6.943  -2.447 1.00 91.29  ? 234 GLU A OE2 1 
ATOM   1728 N N   . ARG A 1 236 ? -10.256 -7.831  2.316  1.00 52.35  ? 235 ARG A N   1 
ATOM   1729 C CA  . ARG A 1 236 ? -10.299 -7.779  3.766  1.00 49.11  ? 235 ARG A CA  1 
ATOM   1730 C C   . ARG A 1 236 ? -10.969 -9.049  4.269  1.00 41.18  ? 235 ARG A C   1 
ATOM   1731 O O   . ARG A 1 236 ? -10.540 -9.688  5.221  1.00 38.39  ? 235 ARG A O   1 
ATOM   1732 C CB  . ARG A 1 236 ? -11.027 -6.528  4.256  1.00 50.10  ? 235 ARG A CB  1 
ATOM   1733 C CG  . ARG A 1 236 ? -10.203 -5.260  4.161  1.00 54.64  ? 235 ARG A CG  1 
ATOM   1734 C CD  . ARG A 1 236 ? -10.960 -4.004  4.576  1.00 59.97  ? 235 ARG A CD  1 
ATOM   1735 N NE  . ARG A 1 236 ? -10.363 -2.812  3.970  1.00 62.96  ? 235 ARG A NE  1 
ATOM   1736 C CZ  . ARG A 1 236 ? -9.341  -2.104  4.430  1.00 54.34  ? 235 ARG A CZ  1 
ATOM   1737 N NH1 . ARG A 1 236 ? -8.726  -2.427  5.560  1.00 54.21  ? 235 ARG A NH1 1 
ATOM   1738 N NH2 . ARG A 1 236 ? -8.920  -1.047  3.747  1.00 51.16  ? 235 ARG A NH2 1 
ATOM   1739 N N   . VAL A 1 237 ? -12.048 -9.488  3.608  1.00 42.68  ? 236 VAL A N   1 
ATOM   1740 C CA  . VAL A 1 237 ? -12.617 -10.752 4.091  1.00 42.83  ? 236 VAL A CA  1 
ATOM   1741 C C   . VAL A 1 237 ? -11.710 -11.928 3.737  1.00 32.40  ? 236 VAL A C   1 
ATOM   1742 O O   . VAL A 1 237 ? -11.750 -12.942 4.441  1.00 42.83  ? 236 VAL A O   1 
ATOM   1743 C CB  . VAL A 1 237 ? -14.034 -10.981 3.547  1.00 50.76  ? 236 VAL A CB  1 
ATOM   1744 C CG1 . VAL A 1 237 ? -14.511 -9.726  2.820  1.00 67.21  ? 236 VAL A CG1 1 
ATOM   1745 C CG2 . VAL A 1 237 ? -14.055 -12.197 2.635  1.00 42.69  ? 236 VAL A CG2 1 
ATOM   1746 N N   . ALA A 1 238 ? -10.891 -11.794 2.704  1.00 29.32  ? 237 ALA A N   1 
ATOM   1747 C CA  . ALA A 1 238 ? -9.848  -12.763 2.358  1.00 45.68  ? 237 ALA A CA  1 
ATOM   1748 C C   . ALA A 1 238 ? -8.667  -12.770 3.335  1.00 44.64  ? 237 ALA A C   1 
ATOM   1749 O O   . ALA A 1 238 ? -7.910  -13.745 3.432  1.00 25.20  ? 237 ALA A O   1 
ATOM   1750 C CB  . ALA A 1 238 ? -9.344  -12.516 0.939  1.00 43.97  ? 237 ALA A CB  1 
ATOM   1751 N N   . ILE A 1 239 ? -8.509  -11.677 4.066  1.00 48.68  ? 238 ILE A N   1 
ATOM   1752 C CA  . ILE A 1 239 ? -7.638  -11.540 5.214  1.00 44.39  ? 238 ILE A CA  1 
ATOM   1753 C C   . ILE A 1 239 ? -8.173  -12.387 6.380  1.00 34.62  ? 238 ILE A C   1 
ATOM   1754 O O   . ILE A 1 239 ? -7.460  -13.241 6.896  1.00 35.96  ? 238 ILE A O   1 
ATOM   1755 C CB  . ILE A 1 239 ? -7.534  -10.100 5.757  1.00 42.25  ? 238 ILE A CB  1 
ATOM   1756 C CG1 . ILE A 1 239 ? -7.096  -9.042  4.752  1.00 44.74  ? 238 ILE A CG1 1 
ATOM   1757 C CG2 . ILE A 1 239 ? -6.642  -10.129 7.002  1.00 31.00  ? 238 ILE A CG2 1 
ATOM   1758 C CD1 . ILE A 1 239 ? -5.656  -9.061  4.322  1.00 44.84  ? 238 ILE A CD1 1 
ATOM   1759 N N   . ILE A 1 240 ? -9.422  -12.093 6.728  1.00 24.88  ? 239 ILE A N   1 
ATOM   1760 C CA  . ILE A 1 240 ? -10.218 -12.796 7.718  1.00 32.39  ? 239 ILE A CA  1 
ATOM   1761 C C   . ILE A 1 240 ? -10.228 -14.299 7.445  1.00 42.03  ? 239 ILE A C   1 
ATOM   1762 O O   . ILE A 1 240 ? -9.896  -15.095 8.325  1.00 33.16  ? 239 ILE A O   1 
ATOM   1763 C CB  . ILE A 1 240 ? -11.673 -12.290 7.714  1.00 33.84  ? 239 ILE A CB  1 
ATOM   1764 C CG1 . ILE A 1 240 ? -11.791 -10.815 8.107  1.00 45.33  ? 239 ILE A CG1 1 
ATOM   1765 C CG2 . ILE A 1 240 ? -12.571 -13.157 8.574  1.00 26.94  ? 239 ILE A CG2 1 
ATOM   1766 C CD1 . ILE A 1 240 ? -12.831 -10.054 7.309  1.00 65.74  ? 239 ILE A CD1 1 
ATOM   1767 N N   . LYS A 1 241 ? -10.609 -14.625 6.211  1.00 38.50  ? 240 LYS A N   1 
ATOM   1768 C CA  . LYS A 1 241 ? -10.705 -16.000 5.742  1.00 38.43  ? 240 LYS A CA  1 
ATOM   1769 C C   . LYS A 1 241 ? -9.342  -16.640 5.558  1.00 34.45  ? 240 LYS A C   1 
ATOM   1770 O O   . LYS A 1 241 ? -9.239  -17.866 5.528  1.00 40.67  ? 240 LYS A O   1 
ATOM   1771 C CB  . LYS A 1 241 ? -11.489 -16.058 4.424  1.00 46.27  ? 240 LYS A CB  1 
ATOM   1772 C CG  . LYS A 1 241 ? -12.939 -15.617 4.588  1.00 57.02  ? 240 LYS A CG  1 
ATOM   1773 C CD  . LYS A 1 241 ? -13.710 -15.740 3.283  1.00 59.48  ? 240 LYS A CD  1 
ATOM   1774 C CE  . LYS A 1 241 ? -15.205 -15.888 3.525  1.00 61.52  ? 240 LYS A CE  1 
ATOM   1775 N NZ  . LYS A 1 241 ? -15.978 -15.778 2.253  1.00 79.56  ? 240 LYS A NZ  1 
ATOM   1776 N N   . GLY A 1 242 ? -8.280  -15.855 5.432  1.00 40.29  ? 241 GLY A N   1 
ATOM   1777 C CA  . GLY A 1 242 ? -6.945  -16.429 5.358  1.00 43.62  ? 241 GLY A CA  1 
ATOM   1778 C C   . GLY A 1 242 ? -6.505  -16.800 3.961  1.00 51.94  ? 241 GLY A C   1 
ATOM   1779 O O   . GLY A 1 242 ? -5.499  -17.471 3.731  1.00 45.95  ? 241 GLY A O   1 
ATOM   1780 N N   . THR A 1 243 ? -7.259  -16.361 2.953  1.00 54.02  ? 242 THR A N   1 
ATOM   1781 C CA  . THR A 1 243 ? -6.938  -16.760 1.591  1.00 49.13  ? 242 THR A CA  1 
ATOM   1782 C C   . THR A 1 243 ? -6.267  -15.653 0.803  1.00 55.98  ? 242 THR A C   1 
ATOM   1783 O O   . THR A 1 243 ? -6.191  -15.783 -0.420 1.00 44.25  ? 242 THR A O   1 
ATOM   1784 C CB  . THR A 1 243 ? -8.229  -17.153 0.852  1.00 50.90  ? 242 THR A CB  1 
ATOM   1785 O OG1 . THR A 1 243 ? -9.063  -15.991 0.729  1.00 56.73  ? 242 THR A OG1 1 
ATOM   1786 C CG2 . THR A 1 243 ? -9.008  -18.183 1.657  1.00 43.81  ? 242 THR A CG2 1 
ATOM   1787 N N   . TYR A 1 244 ? -5.808  -14.590 1.452  1.00 64.28  ? 243 TYR A N   1 
ATOM   1788 C CA  . TYR A 1 244 ? -5.316  -13.419 0.729  1.00 71.13  ? 243 TYR A CA  1 
ATOM   1789 C C   . TYR A 1 244 ? -3.853  -13.538 0.283  1.00 76.96  ? 243 TYR A C   1 
ATOM   1790 O O   . TYR A 1 244 ? -3.050  -14.181 0.964  1.00 57.72  ? 243 TYR A O   1 
ATOM   1791 C CB  . TYR A 1 244 ? -5.507  -12.155 1.582  1.00 73.47  ? 243 TYR A CB  1 
ATOM   1792 C CG  . TYR A 1 244 ? -4.781  -10.933 1.054  1.00 74.43  ? 243 TYR A CG  1 
ATOM   1793 C CD1 . TYR A 1 244 ? -5.292  -10.176 0.008  1.00 70.53  ? 243 TYR A CD1 1 
ATOM   1794 C CD2 . TYR A 1 244 ? -3.571  -10.526 1.601  1.00 73.31  ? 243 TYR A CD2 1 
ATOM   1795 C CE1 . TYR A 1 244 ? -4.624  -9.062  -0.468 1.00 71.39  ? 243 TYR A CE1 1 
ATOM   1796 C CE2 . TYR A 1 244 ? -2.895  -9.415  1.132  1.00 73.27  ? 243 TYR A CE2 1 
ATOM   1797 C CZ  . TYR A 1 244 ? -3.425  -8.683  0.093  1.00 74.58  ? 243 TYR A CZ  1 
ATOM   1798 O OH  . TYR A 1 244 ? -2.756  -7.576  -0.378 1.00 72.78  ? 243 TYR A OH  1 
ATOM   1799 N N   . GLU A 1 245 ? -3.577  -12.907 -0.850 1.00 78.32  ? 244 GLU A N   1 
ATOM   1800 C CA  . GLU A 1 245 ? -2.357  -12.691 -1.590 1.00 75.13  ? 244 GLU A CA  1 
ATOM   1801 C C   . GLU A 1 245 ? -1.630  -13.993 -1.939 1.00 84.98  ? 244 GLU A C   1 
ATOM   1802 O O   . GLU A 1 245 ? -0.478  -14.149 -1.529 1.00 95.32  ? 244 GLU A O   1 
ATOM   1803 C CB  . GLU A 1 245 ? -1.392  -11.799 -0.795 1.00 76.96  ? 244 GLU A CB  1 
ATOM   1804 C CG  . GLU A 1 245 ? -1.095  -10.461 -1.427 1.00 81.51  ? 244 GLU A CG  1 
ATOM   1805 C CD  . GLU A 1 245 ? -1.217  -10.494 -2.940 1.00 87.18  ? 244 GLU A CD  1 
ATOM   1806 O OE1 . GLU A 1 245 ? -0.731  -11.493 -3.520 1.00 101.91 ? 244 GLU A OE1 1 
ATOM   1807 O OE2 . GLU A 1 245 ? -1.801  -9.551  -3.523 1.00 89.05  ? 244 GLU A OE2 1 
ATOM   1808 N N   . PRO A 1 246 ? -2.265  -14.899 -2.673 1.00 92.42  ? 245 PRO A N   1 
ATOM   1809 C CA  . PRO A 1 246 ? -1.664  -16.203 -2.995 1.00 92.80  ? 245 PRO A CA  1 
ATOM   1810 C C   . PRO A 1 246 ? -0.665  -16.118 -4.137 1.00 94.84  ? 245 PRO A C   1 
ATOM   1811 O O   . PRO A 1 246 ? -0.920  -16.654 -5.250 0.11 94.38  ? 245 PRO A O   1 
ATOM   1812 C CB  . PRO A 1 246 ? -2.880  -17.027 -3.444 1.00 88.04  ? 245 PRO A CB  1 
ATOM   1813 C CG  . PRO A 1 246 ? -3.705  -15.987 -4.138 1.00 90.82  ? 245 PRO A CG  1 
ATOM   1814 C CD  . PRO A 1 246 ? -3.612  -14.764 -3.263 1.00 92.44  ? 245 PRO A CD  1 
ATOM   1815 N N   . SER B 1 2   ? 48.375  21.465  9.044  1.00 56.50  ? 1   SER B N   1 
ATOM   1816 C CA  . SER B 1 2   ? 48.021  21.855  7.688  1.00 68.76  ? 1   SER B CA  1 
ATOM   1817 C C   . SER B 1 2   ? 47.287  23.195  7.684  1.00 75.53  ? 1   SER B C   1 
ATOM   1818 O O   . SER B 1 2   ? 46.208  23.308  8.266  1.00 84.78  ? 1   SER B O   1 
ATOM   1819 C CB  . SER B 1 2   ? 47.160  20.784  7.024  1.00 63.50  ? 1   SER B CB  1 
ATOM   1820 O OG  . SER B 1 2   ? 46.580  21.267  5.815  1.00 51.38  ? 1   SER B OG  1 
ATOM   1821 N N   . LYS B 1 3   ? 47.883  24.184  7.027  1.00 75.36  ? 2   LYS B N   1 
ATOM   1822 C CA  . LYS B 1 3   ? 47.273  25.498  6.895  1.00 75.10  ? 2   LYS B CA  1 
ATOM   1823 C C   . LYS B 1 3   ? 45.842  25.374  6.414  1.00 69.64  ? 2   LYS B C   1 
ATOM   1824 O O   . LYS B 1 3   ? 44.857  25.866  6.957  1.00 52.21  ? 2   LYS B O   1 
ATOM   1825 C CB  . LYS B 1 3   ? 48.083  26.356  5.914  1.00 84.68  ? 2   LYS B CB  1 
ATOM   1826 C CG  . LYS B 1 3   ? 48.649  27.626  6.538  1.00 98.92  ? 2   LYS B CG  1 
ATOM   1827 C CD  . LYS B 1 3   ? 48.189  28.889  5.751  1.00 107.98 ? 2   LYS B CD  1 
ATOM   1828 C CE  . LYS B 1 3   ? 49.131  30.064  6.045  1.00 110.44 ? 2   LYS B CE  1 
ATOM   1829 N NZ  . LYS B 1 3   ? 48.628  30.984  7.139  1.00 105.54 ? 2   LYS B NZ  1 
ATOM   1830 N N   . LYS B 1 4   ? 45.644  24.668  5.299  1.00 75.52  ? 3   LYS B N   1 
ATOM   1831 C CA  . LYS B 1 4   ? 44.260  24.680  4.797  1.00 79.59  ? 3   LYS B CA  1 
ATOM   1832 C C   . LYS B 1 4   ? 43.344  23.871  5.702  1.00 66.04  ? 3   LYS B C   1 
ATOM   1833 O O   . LYS B 1 4   ? 42.128  24.064  5.690  1.00 45.68  ? 3   LYS B O   1 
ATOM   1834 C CB  . LYS B 1 4   ? 44.258  24.195  3.345  1.00 88.82  ? 3   LYS B CB  1 
ATOM   1835 C CG  . LYS B 1 4   ? 45.606  24.377  2.643  1.00 96.56  ? 3   LYS B CG  1 
ATOM   1836 C CD  . LYS B 1 4   ? 46.025  25.839  2.570  1.00 98.29  ? 3   LYS B CD  1 
ATOM   1837 C CE  . LYS B 1 4   ? 47.530  26.014  2.682  1.00 93.32  ? 3   LYS B CE  1 
ATOM   1838 N NZ  . LYS B 1 4   ? 47.955  27.431  2.841  1.00 63.86  ? 3   LYS B NZ  1 
ATOM   1839 N N   . GLU B 1 5   ? 43.907  22.968  6.497  1.00 55.62  ? 4   GLU B N   1 
ATOM   1840 C CA  . GLU B 1 5   ? 43.120  22.100  7.362  1.00 53.24  ? 4   GLU B CA  1 
ATOM   1841 C C   . GLU B 1 5   ? 42.631  22.799  8.625  1.00 45.28  ? 4   GLU B C   1 
ATOM   1842 O O   . GLU B 1 5   ? 41.458  22.742  8.992  1.00 38.97  ? 4   GLU B O   1 
ATOM   1843 C CB  . GLU B 1 5   ? 43.949  20.874  7.767  1.00 47.17  ? 4   GLU B CB  1 
ATOM   1844 C CG  . GLU B 1 5   ? 43.217  19.932  8.708  1.00 45.42  ? 4   GLU B CG  1 
ATOM   1845 C CD  . GLU B 1 5   ? 44.125  19.320  9.759  1.00 56.62  ? 4   GLU B CD  1 
ATOM   1846 O OE1 . GLU B 1 5   ? 45.034  20.015  10.276 1.00 75.99  ? 4   GLU B OE1 1 
ATOM   1847 O OE2 . GLU B 1 5   ? 43.900  18.114  10.058 1.00 51.28  ? 4   GLU B OE2 1 
ATOM   1848 N N   . VAL B 1 6   ? 43.560  23.455  9.296  1.00 39.89  ? 5   VAL B N   1 
ATOM   1849 C CA  . VAL B 1 6   ? 43.359  24.038  10.609 1.00 42.34  ? 5   VAL B CA  1 
ATOM   1850 C C   . VAL B 1 6   ? 42.573  25.340  10.551 1.00 59.32  ? 5   VAL B C   1 
ATOM   1851 O O   . VAL B 1 6   ? 41.894  25.728  11.504 1.00 43.32  ? 5   VAL B O   1 
ATOM   1852 C CB  . VAL B 1 6   ? 44.719  24.324  11.289 1.00 27.37  ? 5   VAL B CB  1 
ATOM   1853 C CG1 . VAL B 1 6   ? 44.572  25.468  12.275 1.00 33.69  ? 5   VAL B CG1 1 
ATOM   1854 C CG2 . VAL B 1 6   ? 45.222  23.059  11.955 1.00 28.34  ? 5   VAL B CG2 1 
ATOM   1855 N N   . CYS B 1 7   ? 42.715  25.990  9.398  1.00 63.64  ? 6   CYS B N   1 
ATOM   1856 C CA  . CYS B 1 7   ? 42.107  27.299  9.181  1.00 70.76  ? 6   CYS B CA  1 
ATOM   1857 C C   . CYS B 1 7   ? 40.695  27.163  8.634  1.00 73.45  ? 6   CYS B C   1 
ATOM   1858 O O   . CYS B 1 7   ? 39.908  28.112  8.629  1.00 91.87  ? 6   CYS B O   1 
ATOM   1859 C CB  . CYS B 1 7   ? 43.032  28.121  8.265  1.00 67.50  ? 6   CYS B CB  1 
ATOM   1860 S SG  . CYS B 1 7   ? 44.739  28.136  8.894  1.00 65.97  ? 6   CYS B SG  1 
ATOM   1861 N N   . SER B 1 8   ? 40.347  25.963  8.177  1.00 67.63  ? 7   SER B N   1 
ATOM   1862 C CA  . SER B 1 8   ? 39.031  25.687  7.616  1.00 61.49  ? 7   SER B CA  1 
ATOM   1863 C C   . SER B 1 8   ? 37.906  25.834  8.638  1.00 54.68  ? 7   SER B C   1 
ATOM   1864 O O   . SER B 1 8   ? 38.004  25.664  9.852  1.00 38.71  ? 7   SER B O   1 
ATOM   1865 C CB  . SER B 1 8   ? 39.001  24.280  6.999  1.00 65.63  ? 7   SER B CB  1 
ATOM   1866 O OG  . SER B 1 8   ? 37.692  23.687  7.243  1.00 94.67  ? 7   SER B OG  1 
ATOM   1867 N N   . VAL B 1 9   ? 36.754  26.183  8.076  1.00 49.40  ? 8   VAL B N   1 
ATOM   1868 C CA  . VAL B 1 9   ? 35.561  26.486  8.860  1.00 38.59  ? 8   VAL B CA  1 
ATOM   1869 C C   . VAL B 1 9   ? 35.074  25.228  9.556  1.00 37.64  ? 8   VAL B C   1 
ATOM   1870 O O   . VAL B 1 9   ? 34.602  25.260  10.695 1.00 37.74  ? 8   VAL B O   1 
ATOM   1871 C CB  . VAL B 1 9   ? 34.500  27.118  7.938  1.00 39.10  ? 8   VAL B CB  1 
ATOM   1872 C CG1 . VAL B 1 9   ? 33.746  26.064  7.142  1.00 39.67  ? 8   VAL B CG1 1 
ATOM   1873 C CG2 . VAL B 1 9   ? 33.541  27.973  8.754  1.00 52.02  ? 8   VAL B CG2 1 
ATOM   1874 N N   . ALA B 1 10  ? 35.210  24.093  8.870  1.00 28.52  ? 9   ALA B N   1 
ATOM   1875 C CA  . ALA B 1 10  ? 34.739  22.831  9.436  1.00 34.63  ? 9   ALA B CA  1 
ATOM   1876 C C   . ALA B 1 10  ? 35.517  22.448  10.690 1.00 36.52  ? 9   ALA B C   1 
ATOM   1877 O O   . ALA B 1 10  ? 34.925  21.987  11.669 1.00 41.20  ? 9   ALA B O   1 
ATOM   1878 C CB  . ALA B 1 10  ? 34.829  21.739  8.389  1.00 28.29  ? 9   ALA B CB  1 
ATOM   1879 N N   . PHE B 1 11  ? 36.827  22.644  10.637 1.00 36.93  ? 10  PHE B N   1 
ATOM   1880 C CA  . PHE B 1 11  ? 37.732  22.427  11.759 1.00 31.39  ? 10  PHE B CA  1 
ATOM   1881 C C   . PHE B 1 11  ? 37.337  23.343  12.902 1.00 22.54  ? 10  PHE B C   1 
ATOM   1882 O O   . PHE B 1 11  ? 37.276  22.970  14.065 1.00 42.14  ? 10  PHE B O   1 
ATOM   1883 C CB  . PHE B 1 11  ? 39.172  22.705  11.350 1.00 26.77  ? 10  PHE B CB  1 
ATOM   1884 C CG  . PHE B 1 11  ? 40.279  22.369  12.325 1.00 28.99  ? 10  PHE B CG  1 
ATOM   1885 C CD1 . PHE B 1 11  ? 40.853  21.111  12.372 1.00 36.48  ? 10  PHE B CD1 1 
ATOM   1886 C CD2 . PHE B 1 11  ? 40.771  23.316  13.213 1.00 33.92  ? 10  PHE B CD2 1 
ATOM   1887 C CE1 . PHE B 1 11  ? 41.882  20.810  13.251 1.00 34.39  ? 10  PHE B CE1 1 
ATOM   1888 C CE2 . PHE B 1 11  ? 41.799  23.031  14.090 1.00 31.62  ? 10  PHE B CE2 1 
ATOM   1889 C CZ  . PHE B 1 11  ? 42.365  21.770  14.126 1.00 26.63  ? 10  PHE B CZ  1 
ATOM   1890 N N   . LEU B 1 12  ? 37.062  24.603  12.549 1.00 21.00  ? 11  LEU B N   1 
ATOM   1891 C CA  . LEU B 1 12  ? 36.720  25.517  13.636 1.00 29.07  ? 11  LEU B CA  1 
ATOM   1892 C C   . LEU B 1 12  ? 35.425  25.053  14.301 1.00 41.54  ? 11  LEU B C   1 
ATOM   1893 O O   . LEU B 1 12  ? 35.185  25.304  15.484 1.00 41.70  ? 11  LEU B O   1 
ATOM   1894 C CB  . LEU B 1 12  ? 36.616  26.941  13.119 1.00 36.44  ? 11  LEU B CB  1 
ATOM   1895 C CG  . LEU B 1 12  ? 35.706  27.875  13.918 1.00 40.31  ? 11  LEU B CG  1 
ATOM   1896 C CD1 . LEU B 1 12  ? 36.442  28.439  15.124 1.00 26.31  ? 11  LEU B CD1 1 
ATOM   1897 C CD2 . LEU B 1 12  ? 35.179  28.978  13.008 1.00 42.54  ? 11  LEU B CD2 1 
ATOM   1898 N N   . LYS B 1 13  ? 34.587  24.350  13.542 1.00 39.91  ? 12  LYS B N   1 
ATOM   1899 C CA  . LYS B 1 13  ? 33.380  23.771  14.120 1.00 42.50  ? 12  LYS B CA  1 
ATOM   1900 C C   . LYS B 1 13  ? 33.745  22.572  14.997 1.00 43.14  ? 12  LYS B C   1 
ATOM   1901 O O   . LYS B 1 13  ? 33.350  22.515  16.160 1.00 48.18  ? 12  LYS B O   1 
ATOM   1902 C CB  . LYS B 1 13  ? 32.381  23.340  13.052 1.00 35.82  ? 12  LYS B CB  1 
ATOM   1903 C CG  . LYS B 1 13  ? 31.458  24.459  12.577 1.00 28.16  ? 12  LYS B CG  1 
ATOM   1904 C CD  . LYS B 1 13  ? 31.292  24.397  11.065 1.00 29.40  ? 12  LYS B CD  1 
ATOM   1905 C CE  . LYS B 1 13  ? 29.847  24.122  10.687 1.00 36.35  ? 12  LYS B CE  1 
ATOM   1906 N NZ  . LYS B 1 13  ? 29.514  24.672  9.345  1.00 33.72  ? 12  LYS B NZ  1 
ATOM   1907 N N   . ALA B 1 14  ? 34.504  21.657  14.407 1.00 28.52  ? 13  ALA B N   1 
ATOM   1908 C CA  . ALA B 1 14  ? 34.969  20.468  15.105 1.00 31.92  ? 13  ALA B CA  1 
ATOM   1909 C C   . ALA B 1 14  ? 35.565  20.826  16.464 1.00 40.71  ? 13  ALA B C   1 
ATOM   1910 O O   . ALA B 1 14  ? 35.224  20.254  17.507 1.00 28.72  ? 13  ALA B O   1 
ATOM   1911 C CB  . ALA B 1 14  ? 35.984  19.727  14.253 1.00 22.37  ? 13  ALA B CB  1 
ATOM   1912 N N   . VAL B 1 15  ? 36.486  21.792  16.483 1.00 33.04  ? 14  VAL B N   1 
ATOM   1913 C CA  . VAL B 1 15  ? 37.057  22.172  17.782 1.00 38.68  ? 14  VAL B CA  1 
ATOM   1914 C C   . VAL B 1 15  ? 35.984  22.767  18.686 1.00 33.98  ? 14  VAL B C   1 
ATOM   1915 O O   . VAL B 1 15  ? 36.006  22.593  19.908 1.00 29.26  ? 14  VAL B O   1 
ATOM   1916 C CB  . VAL B 1 15  ? 38.230  23.162  17.637 1.00 34.81  ? 14  VAL B CB  1 
ATOM   1917 C CG1 . VAL B 1 15  ? 39.040  23.261  18.931 1.00 24.80  ? 14  VAL B CG1 1 
ATOM   1918 C CG2 . VAL B 1 15  ? 39.109  22.751  16.470 1.00 24.42  ? 14  VAL B CG2 1 
ATOM   1919 N N   . PHE B 1 16  ? 35.005  23.483  18.122 1.00 30.69  ? 15  PHE B N   1 
ATOM   1920 C CA  . PHE B 1 16  ? 33.956  24.010  18.989 1.00 40.81  ? 15  PHE B CA  1 
ATOM   1921 C C   . PHE B 1 16  ? 33.145  22.881  19.641 1.00 33.54  ? 15  PHE B C   1 
ATOM   1922 O O   . PHE B 1 16  ? 32.901  22.921  20.845 1.00 27.57  ? 15  PHE B O   1 
ATOM   1923 C CB  . PHE B 1 16  ? 33.006  24.922  18.221 1.00 44.23  ? 15  PHE B CB  1 
ATOM   1924 C CG  . PHE B 1 16  ? 31.729  25.219  18.993 1.00 47.48  ? 15  PHE B CG  1 
ATOM   1925 C CD1 . PHE B 1 16  ? 31.767  26.124  20.042 1.00 48.96  ? 15  PHE B CD1 1 
ATOM   1926 C CD2 . PHE B 1 16  ? 30.524  24.619  18.673 1.00 46.85  ? 15  PHE B CD2 1 
ATOM   1927 C CE1 . PHE B 1 16  ? 30.619  26.425  20.747 1.00 51.34  ? 15  PHE B CE1 1 
ATOM   1928 C CE2 . PHE B 1 16  ? 29.375  24.915  19.381 1.00 45.52  ? 15  PHE B CE2 1 
ATOM   1929 C CZ  . PHE B 1 16  ? 29.418  25.827  20.419 1.00 48.36  ? 15  PHE B CZ  1 
ATOM   1930 N N   . ALA B 1 17  ? 32.749  21.927  18.813 1.00 24.86  ? 16  ALA B N   1 
ATOM   1931 C CA  . ALA B 1 17  ? 32.012  20.742  19.221 1.00 31.40  ? 16  ALA B CA  1 
ATOM   1932 C C   . ALA B 1 17  ? 32.798  19.908  20.234 1.00 31.63  ? 16  ALA B C   1 
ATOM   1933 O O   . ALA B 1 17  ? 32.212  19.428  21.214 1.00 30.92  ? 16  ALA B O   1 
ATOM   1934 C CB  . ALA B 1 17  ? 31.639  19.885  18.017 1.00 15.10  ? 16  ALA B CB  1 
ATOM   1935 N N   . GLU B 1 18  ? 34.104  19.709  20.042 1.00 26.76  ? 17  GLU B N   1 
ATOM   1936 C CA  . GLU B 1 18  ? 34.844  18.908  21.023 1.00 28.55  ? 17  GLU B CA  1 
ATOM   1937 C C   . GLU B 1 18  ? 34.875  19.650  22.351 1.00 30.24  ? 17  GLU B C   1 
ATOM   1938 O O   . GLU B 1 18  ? 34.974  19.062  23.421 1.00 40.20  ? 17  GLU B O   1 
ATOM   1939 C CB  . GLU B 1 18  ? 36.252  18.578  20.550 1.00 36.56  ? 17  GLU B CB  1 
ATOM   1940 C CG  . GLU B 1 18  ? 36.319  17.488  19.489 1.00 30.18  ? 17  GLU B CG  1 
ATOM   1941 C CD  . GLU B 1 18  ? 35.835  16.144  20.002 1.00 32.60  ? 17  GLU B CD  1 
ATOM   1942 O OE1 . GLU B 1 18  ? 36.311  15.719  21.081 1.00 33.36  ? 17  GLU B OE1 1 
ATOM   1943 O OE2 . GLU B 1 18  ? 34.982  15.516  19.334 1.00 24.65  ? 17  GLU B OE2 1 
ATOM   1944 N N   . PHE B 1 19  ? 34.755  20.972  22.271 1.00 40.79  ? 18  PHE B N   1 
ATOM   1945 C CA  . PHE B 1 19  ? 34.709  21.795  23.480 1.00 42.24  ? 18  PHE B CA  1 
ATOM   1946 C C   . PHE B 1 19  ? 33.324  21.728  24.117 1.00 36.71  ? 18  PHE B C   1 
ATOM   1947 O O   . PHE B 1 19  ? 33.189  21.498  25.312 1.00 28.95  ? 18  PHE B O   1 
ATOM   1948 C CB  . PHE B 1 19  ? 35.080  23.241  23.154 1.00 36.75  ? 18  PHE B CB  1 
ATOM   1949 C CG  . PHE B 1 19  ? 34.511  24.280  24.099 1.00 36.00  ? 18  PHE B CG  1 
ATOM   1950 C CD1 . PHE B 1 19  ? 35.123  24.512  25.322 1.00 34.95  ? 18  PHE B CD1 1 
ATOM   1951 C CD2 . PHE B 1 19  ? 33.385  25.006  23.753 1.00 30.93  ? 18  PHE B CD2 1 
ATOM   1952 C CE1 . PHE B 1 19  ? 34.625  25.456  26.205 1.00 28.37  ? 18  PHE B CE1 1 
ATOM   1953 C CE2 . PHE B 1 19  ? 32.873  25.946  24.629 1.00 30.47  ? 18  PHE B CE2 1 
ATOM   1954 C CZ  . PHE B 1 19  ? 33.492  26.163  25.849 1.00 32.29  ? 18  PHE B CZ  1 
ATOM   1955 N N   . LEU B 1 20  ? 32.308  21.937  23.285 1.00 24.62  ? 19  LEU B N   1 
ATOM   1956 C CA  . LEU B 1 20  ? 30.930  21.979  23.732 1.00 25.48  ? 19  LEU B CA  1 
ATOM   1957 C C   . LEU B 1 20  ? 30.504  20.702  24.441 1.00 36.70  ? 19  LEU B C   1 
ATOM   1958 O O   . LEU B 1 20  ? 29.877  20.701  25.500 1.00 29.38  ? 19  LEU B O   1 
ATOM   1959 C CB  . LEU B 1 20  ? 29.999  22.194  22.528 1.00 20.77  ? 19  LEU B CB  1 
ATOM   1960 C CG  . LEU B 1 20  ? 28.523  22.272  22.929 1.00 22.84  ? 19  LEU B CG  1 
ATOM   1961 C CD1 . LEU B 1 20  ? 28.403  23.289  24.052 1.00 27.28  ? 19  LEU B CD1 1 
ATOM   1962 C CD2 . LEU B 1 20  ? 27.644  22.612  21.735 1.00 21.30  ? 19  LEU B CD2 1 
ATOM   1963 N N   . ALA B 1 21  ? 30.873  19.595  23.802 1.00 39.32  ? 20  ALA B N   1 
ATOM   1964 C CA  . ALA B 1 21  ? 30.499  18.279  24.310 1.00 47.16  ? 20  ALA B CA  1 
ATOM   1965 C C   . ALA B 1 21  ? 31.109  18.020  25.690 1.00 41.61  ? 20  ALA B C   1 
ATOM   1966 O O   . ALA B 1 21  ? 30.353  17.862  26.659 1.00 43.93  ? 20  ALA B O   1 
ATOM   1967 C CB  . ALA B 1 21  ? 30.898  17.201  23.312 1.00 34.20  ? 20  ALA B CB  1 
ATOM   1968 N N   . THR B 1 22  ? 32.435  17.981  25.760 1.00 29.69  ? 21  THR B N   1 
ATOM   1969 C CA  . THR B 1 22  ? 33.167  17.664  26.982 1.00 27.73  ? 21  THR B CA  1 
ATOM   1970 C C   . THR B 1 22  ? 32.627  18.500  28.153 1.00 26.71  ? 21  THR B C   1 
ATOM   1971 O O   . THR B 1 22  ? 32.441  17.992  29.261 1.00 31.19  ? 21  THR B O   1 
ATOM   1972 C CB  . THR B 1 22  ? 34.684  17.862  26.829 1.00 25.46  ? 21  THR B CB  1 
ATOM   1973 O OG1 . THR B 1 22  ? 35.189  17.328  25.607 1.00 16.87  ? 21  THR B OG1 1 
ATOM   1974 C CG2 . THR B 1 22  ? 35.463  17.099  27.905 1.00 37.47  ? 21  THR B CG2 1 
ATOM   1975 N N   . LEU B 1 23  ? 32.367  19.777  27.904 1.00 33.02  ? 22  LEU B N   1 
ATOM   1976 C CA  . LEU B 1 23  ? 31.724  20.655  28.894 1.00 38.77  ? 22  LEU B CA  1 
ATOM   1977 C C   . LEU B 1 23  ? 30.394  20.044  29.322 1.00 32.60  ? 22  LEU B C   1 
ATOM   1978 O O   . LEU B 1 23  ? 30.014  20.089  30.488 1.00 28.87  ? 22  LEU B O   1 
ATOM   1979 C CB  . LEU B 1 23  ? 31.576  22.048  28.331 1.00 33.72  ? 22  LEU B CB  1 
ATOM   1980 C CG  . LEU B 1 23  ? 30.568  23.147  28.248 1.00 25.95  ? 22  LEU B CG  1 
ATOM   1981 C CD1 . LEU B 1 23  ? 29.416  23.165  29.246 1.00 46.60  ? 22  LEU B CD1 1 
ATOM   1982 C CD2 . LEU B 1 23  ? 31.265  24.513  28.429 1.00 31.28  ? 22  LEU B CD2 1 
ATOM   1983 N N   . ILE B 1 24  ? 29.630  19.542  28.355 1.00 31.39  ? 23  ILE B N   1 
ATOM   1984 C CA  . ILE B 1 24  ? 28.243  19.232  28.696 1.00 25.53  ? 23  ILE B CA  1 
ATOM   1985 C C   . ILE B 1 24  ? 28.266  17.918  29.466 1.00 26.98  ? 23  ILE B C   1 
ATOM   1986 O O   . ILE B 1 24  ? 27.586  17.840  30.494 1.00 24.53  ? 23  ILE B O   1 
ATOM   1987 C CB  . ILE B 1 24  ? 27.373  19.196  27.442 1.00 27.17  ? 23  ILE B CB  1 
ATOM   1988 C CG1 . ILE B 1 24  ? 27.101  20.587  26.853 1.00 20.83  ? 23  ILE B CG1 1 
ATOM   1989 C CG2 . ILE B 1 24  ? 26.059  18.476  27.700 1.00 38.43  ? 23  ILE B CG2 1 
ATOM   1990 C CD1 . ILE B 1 24  ? 26.427  20.480  25.490 1.00 27.06  ? 23  ILE B CD1 1 
ATOM   1991 N N   . PHE B 1 25  ? 29.070  17.016  28.929 1.00 24.90  ? 24  PHE B N   1 
ATOM   1992 C CA  . PHE B 1 25  ? 29.439  15.728  29.491 1.00 33.87  ? 24  PHE B CA  1 
ATOM   1993 C C   . PHE B 1 25  ? 30.014  15.817  30.906 1.00 40.52  ? 24  PHE B C   1 
ATOM   1994 O O   . PHE B 1 25  ? 29.789  14.936  31.741 1.00 32.18  ? 24  PHE B O   1 
ATOM   1995 C CB  . PHE B 1 25  ? 30.492  15.009  28.634 1.00 24.88  ? 24  PHE B CB  1 
ATOM   1996 C CG  . PHE B 1 25  ? 31.235  13.904  29.370 1.00 24.14  ? 24  PHE B CG  1 
ATOM   1997 C CD1 . PHE B 1 25  ? 30.589  12.747  29.772 1.00 30.41  ? 24  PHE B CD1 1 
ATOM   1998 C CD2 . PHE B 1 25  ? 32.582  14.020  29.655 1.00 26.97  ? 24  PHE B CD2 1 
ATOM   1999 C CE1 . PHE B 1 25  ? 31.270  11.742  30.433 1.00 31.99  ? 24  PHE B CE1 1 
ATOM   2000 C CE2 . PHE B 1 25  ? 33.272  13.019  30.311 1.00 28.72  ? 24  PHE B CE2 1 
ATOM   2001 C CZ  . PHE B 1 25  ? 32.620  11.863  30.697 1.00 24.97  ? 24  PHE B CZ  1 
ATOM   2002 N N   . VAL B 1 26  ? 30.776  16.868  31.205 1.00 42.10  ? 25  VAL B N   1 
ATOM   2003 C CA  . VAL B 1 26  ? 31.344  16.948  32.562 1.00 39.13  ? 25  VAL B CA  1 
ATOM   2004 C C   . VAL B 1 26  ? 30.262  17.486  33.492 1.00 30.74  ? 25  VAL B C   1 
ATOM   2005 O O   . VAL B 1 26  ? 30.112  17.060  34.638 1.00 44.13  ? 25  VAL B O   1 
ATOM   2006 C CB  . VAL B 1 26  ? 32.637  17.773  32.580 1.00 30.88  ? 25  VAL B CB  1 
ATOM   2007 C CG1 . VAL B 1 26  ? 33.208  17.850  33.987 1.00 48.58  ? 25  VAL B CG1 1 
ATOM   2008 C CG2 . VAL B 1 26  ? 33.700  17.180  31.662 1.00 23.28  ? 25  VAL B CG2 1 
ATOM   2009 N N   . PHE B 1 27  ? 29.455  18.408  32.989 1.00 28.68  ? 26  PHE B N   1 
ATOM   2010 C CA  . PHE B 1 27  ? 28.302  18.915  33.692 1.00 33.52  ? 26  PHE B CA  1 
ATOM   2011 C C   . PHE B 1 27  ? 27.352  17.826  34.187 1.00 41.96  ? 26  PHE B C   1 
ATOM   2012 O O   . PHE B 1 27  ? 26.974  17.816  35.358 1.00 38.58  ? 26  PHE B O   1 
ATOM   2013 C CB  . PHE B 1 27  ? 27.430  19.810  32.800 1.00 26.36  ? 26  PHE B CB  1 
ATOM   2014 C CG  . PHE B 1 27  ? 26.275  20.409  33.591 1.00 24.96  ? 26  PHE B CG  1 
ATOM   2015 C CD1 . PHE B 1 27  ? 26.564  21.460  34.459 1.00 26.94  ? 26  PHE B CD1 1 
ATOM   2016 C CD2 . PHE B 1 27  ? 24.970  19.967  33.476 1.00 22.96  ? 26  PHE B CD2 1 
ATOM   2017 C CE1 . PHE B 1 27  ? 25.565  22.058  35.204 1.00 24.68  ? 26  PHE B CE1 1 
ATOM   2018 C CE2 . PHE B 1 27  ? 23.968  20.549  34.232 1.00 21.21  ? 26  PHE B CE2 1 
ATOM   2019 C CZ  . PHE B 1 27  ? 24.272  21.584  35.095 1.00 27.18  ? 26  PHE B CZ  1 
ATOM   2020 N N   . PHE B 1 28  ? 26.935  16.987  33.240 1.00 39.52  ? 27  PHE B N   1 
ATOM   2021 C CA  . PHE B 1 28  ? 26.022  15.902  33.576 1.00 27.95  ? 27  PHE B CA  1 
ATOM   2022 C C   . PHE B 1 28  ? 26.734  14.840  34.411 1.00 22.53  ? 27  PHE B C   1 
ATOM   2023 O O   . PHE B 1 28  ? 26.154  14.246  35.318 1.00 31.20  ? 27  PHE B O   1 
ATOM   2024 C CB  . PHE B 1 28  ? 25.426  15.254  32.318 1.00 12.84  ? 27  PHE B CB  1 
ATOM   2025 C CG  . PHE B 1 28  ? 24.282  16.114  31.812 1.00 16.92  ? 27  PHE B CG  1 
ATOM   2026 C CD1 . PHE B 1 28  ? 23.022  15.991  32.370 1.00 26.47  ? 27  PHE B CD1 1 
ATOM   2027 C CD2 . PHE B 1 28  ? 24.489  17.039  30.805 1.00 25.01  ? 27  PHE B CD2 1 
ATOM   2028 C CE1 . PHE B 1 28  ? 21.978  16.777  31.910 1.00 37.75  ? 27  PHE B CE1 1 
ATOM   2029 C CE2 . PHE B 1 28  ? 23.448  17.815  30.321 1.00 25.03  ? 27  PHE B CE2 1 
ATOM   2030 C CZ  . PHE B 1 28  ? 22.187  17.686  30.885 1.00 29.76  ? 27  PHE B CZ  1 
ATOM   2031 N N   . GLY B 1 29  ? 27.991  14.613  34.058 1.00 26.27  ? 28  GLY B N   1 
ATOM   2032 C CA  . GLY B 1 29  ? 28.801  13.596  34.683 1.00 23.74  ? 28  GLY B CA  1 
ATOM   2033 C C   . GLY B 1 29  ? 28.944  13.868  36.168 1.00 30.56  ? 28  GLY B C   1 
ATOM   2034 O O   . GLY B 1 29  ? 28.564  13.060  37.017 1.00 27.95  ? 28  GLY B O   1 
ATOM   2035 N N   . LEU B 1 30  ? 29.519  15.017  36.487 1.00 23.01  ? 29  LEU B N   1 
ATOM   2036 C CA  . LEU B 1 30  ? 29.752  15.314  37.897 1.00 26.39  ? 29  LEU B CA  1 
ATOM   2037 C C   . LEU B 1 30  ? 28.427  15.512  38.617 1.00 35.07  ? 29  LEU B C   1 
ATOM   2038 O O   . LEU B 1 30  ? 28.219  15.017  39.726 1.00 39.03  ? 29  LEU B O   1 
ATOM   2039 C CB  . LEU B 1 30  ? 30.642  16.553  37.967 1.00 26.04  ? 29  LEU B CB  1 
ATOM   2040 C CG  . LEU B 1 30  ? 31.989  16.389  37.251 1.00 32.14  ? 29  LEU B CG  1 
ATOM   2041 C CD1 . LEU B 1 30  ? 32.989  17.431  37.736 1.00 60.37  ? 29  LEU B CD1 1 
ATOM   2042 C CD2 . LEU B 1 30  ? 32.526  14.985  37.460 1.00 29.74  ? 29  LEU B CD2 1 
ATOM   2043 N N   . GLY B 1 31  ? 27.545  16.247  37.944 1.00 28.23  ? 30  GLY B N   1 
ATOM   2044 C CA  . GLY B 1 31  ? 26.250  16.635  38.463 1.00 22.16  ? 30  GLY B CA  1 
ATOM   2045 C C   . GLY B 1 31  ? 25.415  15.456  38.914 1.00 31.03  ? 30  GLY B C   1 
ATOM   2046 O O   . GLY B 1 31  ? 24.712  15.548  39.923 1.00 31.33  ? 30  GLY B O   1 
ATOM   2047 N N   . SER B 1 32  ? 25.467  14.339  38.188 1.00 23.47  ? 31  SER B N   1 
ATOM   2048 C CA  . SER B 1 32  ? 24.683  13.173  38.568 1.00 25.48  ? 31  SER B CA  1 
ATOM   2049 C C   . SER B 1 32  ? 25.313  12.353  39.696 1.00 34.53  ? 31  SER B C   1 
ATOM   2050 O O   . SER B 1 32  ? 24.640  11.455  40.205 1.00 25.61  ? 31  SER B O   1 
ATOM   2051 C CB  . SER B 1 32  ? 24.509  12.236  37.363 1.00 16.14  ? 31  SER B CB  1 
ATOM   2052 O OG  . SER B 1 32  ? 25.745  11.543  37.230 1.00 29.85  ? 31  SER B OG  1 
ATOM   2053 N N   . ALA B 1 33  ? 26.550  12.670  40.035 1.00 32.34  ? 32  ALA B N   1 
ATOM   2054 C CA  . ALA B 1 33  ? 27.427  11.981  40.960 1.00 28.95  ? 32  ALA B CA  1 
ATOM   2055 C C   . ALA B 1 33  ? 27.543  12.665  42.321 1.00 40.87  ? 32  ALA B C   1 
ATOM   2056 O O   . ALA B 1 33  ? 28.102  12.086  43.260 1.00 39.28  ? 32  ALA B O   1 
ATOM   2057 C CB  . ALA B 1 33  ? 28.814  11.880  40.332 1.00 26.62  ? 32  ALA B CB  1 
ATOM   2058 N N   . LEU B 1 34  ? 27.013  13.882  42.396 1.00 39.51  ? 33  LEU B N   1 
ATOM   2059 C CA  . LEU B 1 34  ? 27.016  14.690  43.609 1.00 34.17  ? 33  LEU B CA  1 
ATOM   2060 C C   . LEU B 1 34  ? 26.271  13.995  44.734 1.00 33.81  ? 33  LEU B C   1 
ATOM   2061 O O   . LEU B 1 34  ? 25.194  13.443  44.523 1.00 31.85  ? 33  LEU B O   1 
ATOM   2062 C CB  . LEU B 1 34  ? 26.393  16.073  43.372 1.00 24.99  ? 33  LEU B CB  1 
ATOM   2063 C CG  . LEU B 1 34  ? 27.199  16.936  42.389 1.00 26.68  ? 33  LEU B CG  1 
ATOM   2064 C CD1 . LEU B 1 34  ? 26.872  18.413  42.536 1.00 31.74  ? 33  LEU B CD1 1 
ATOM   2065 C CD2 . LEU B 1 34  ? 28.700  16.705  42.551 1.00 29.76  ? 33  LEU B CD2 1 
ATOM   2066 N N   . LYS B 1 35  ? 26.854  14.030  45.931 1.00 23.86  ? 34  LYS B N   1 
ATOM   2067 C CA  . LYS B 1 35  ? 26.173  13.438  47.075 1.00 29.18  ? 34  LYS B CA  1 
ATOM   2068 C C   . LYS B 1 35  ? 24.949  14.268  47.432 1.00 30.62  ? 34  LYS B C   1 
ATOM   2069 O O   . LYS B 1 35  ? 24.932  14.919  48.475 1.00 56.57  ? 34  LYS B O   1 
ATOM   2070 C CB  . LYS B 1 35  ? 27.115  13.326  48.280 1.00 34.46  ? 34  LYS B CB  1 
ATOM   2071 C CG  . LYS B 1 35  ? 28.521  12.853  47.925 1.00 28.99  ? 34  LYS B CG  1 
ATOM   2072 C CD  . LYS B 1 35  ? 28.845  11.508  48.538 1.00 32.92  ? 34  LYS B CD  1 
ATOM   2073 C CE  . LYS B 1 35  ? 28.982  10.414  47.493 1.00 35.08  ? 34  LYS B CE  1 
ATOM   2074 N NZ  . LYS B 1 35  ? 30.351  10.402  46.899 1.00 37.39  ? 34  LYS B NZ  1 
ATOM   2075 N N   . TRP B 1 36  ? 23.936  14.250  46.584 1.00 28.02  ? 35  TRP B N   1 
ATOM   2076 C CA  . TRP B 1 36  ? 22.663  14.895  46.855 1.00 26.92  ? 35  TRP B CA  1 
ATOM   2077 C C   . TRP B 1 36  ? 22.045  14.287  48.111 1.00 39.45  ? 35  TRP B C   1 
ATOM   2078 O O   . TRP B 1 36  ? 21.699  13.102  48.094 1.00 39.58  ? 35  TRP B O   1 
ATOM   2079 C CB  . TRP B 1 36  ? 21.718  14.760  45.661 1.00 19.35  ? 35  TRP B CB  1 
ATOM   2080 C CG  . TRP B 1 36  ? 22.261  15.471  44.456 1.00 30.16  ? 35  TRP B CG  1 
ATOM   2081 C CD1 . TRP B 1 36  ? 23.088  14.971  43.496 1.00 37.85  ? 35  TRP B CD1 1 
ATOM   2082 C CD2 . TRP B 1 36  ? 22.005  16.836  44.094 1.00 40.08  ? 35  TRP B CD2 1 
ATOM   2083 N NE1 . TRP B 1 36  ? 23.365  15.932  42.554 1.00 40.66  ? 35  TRP B NE1 1 
ATOM   2084 C CE2 . TRP B 1 36  ? 22.711  17.087  42.899 1.00 40.14  ? 35  TRP B CE2 1 
ATOM   2085 C CE3 . TRP B 1 36  ? 21.245  17.863  44.670 1.00 37.37  ? 35  TRP B CE3 1 
ATOM   2086 C CZ2 . TRP B 1 36  ? 22.675  18.332  42.271 1.00 37.54  ? 35  TRP B CZ2 1 
ATOM   2087 C CZ3 . TRP B 1 36  ? 21.212  19.094  44.047 1.00 35.54  ? 35  TRP B CZ3 1 
ATOM   2088 C CH2 . TRP B 1 36  ? 21.925  19.314  42.856 1.00 42.04  ? 35  TRP B CH2 1 
ATOM   2089 N N   . PRO B 1 37  ? 21.931  15.115  49.145 1.00 37.75  ? 36  PRO B N   1 
ATOM   2090 C CA  . PRO B 1 37  ? 21.512  14.641  50.472 1.00 38.45  ? 36  PRO B CA  1 
ATOM   2091 C C   . PRO B 1 37  ? 20.080  14.117  50.359 1.00 40.05  ? 36  PRO B C   1 
ATOM   2092 O O   . PRO B 1 37  ? 19.605  13.180  50.980 1.00 33.85  ? 36  PRO B O   1 
ATOM   2093 C CB  . PRO B 1 37  ? 21.570  15.899  51.336 1.00 34.56  ? 36  PRO B CB  1 
ATOM   2094 C CG  . PRO B 1 37  ? 21.460  17.038  50.375 1.00 36.25  ? 36  PRO B CG  1 
ATOM   2095 C CD  . PRO B 1 37  ? 22.158  16.571  49.123 1.00 36.40  ? 36  PRO B CD  1 
ATOM   2096 N N   . SER B 1 38  ? 19.407  14.825  49.470 1.00 40.15  ? 37  SER B N   1 
ATOM   2097 C CA  . SER B 1 38  ? 18.063  14.580  48.978 1.00 52.72  ? 37  SER B CA  1 
ATOM   2098 C C   . SER B 1 38  ? 17.855  13.115  48.630 1.00 54.24  ? 37  SER B C   1 
ATOM   2099 O O   . SER B 1 38  ? 16.846  12.461  48.918 1.00 42.40  ? 37  SER B O   1 
ATOM   2100 C CB  . SER B 1 38  ? 17.917  15.568  47.805 1.00 66.67  ? 37  SER B CB  1 
ATOM   2101 O OG  . SER B 1 38  ? 18.891  16.627  47.947 1.00 42.32  ? 37  SER B OG  1 
ATOM   2102 N N   . ALA B 1 39  ? 18.839  12.498  47.986 1.00 48.52  ? 38  ALA B N   1 
ATOM   2103 C CA  . ALA B 1 39  ? 18.815  11.105  47.586 1.00 46.58  ? 38  ALA B CA  1 
ATOM   2104 C C   . ALA B 1 39  ? 20.188  10.765  47.015 1.00 38.50  ? 38  ALA B C   1 
ATOM   2105 O O   . ALA B 1 39  ? 20.459  11.130  45.868 1.00 48.05  ? 38  ALA B O   1 
ATOM   2106 C CB  . ALA B 1 39  ? 17.773  10.771  46.527 1.00 33.83  ? 38  ALA B CB  1 
ATOM   2107 N N   . LEU B 1 40  ? 21.021  10.110  47.802 1.00 27.77  ? 39  LEU B N   1 
ATOM   2108 C CA  . LEU B 1 40  ? 22.351  9.831   47.260 1.00 39.97  ? 39  LEU B CA  1 
ATOM   2109 C C   . LEU B 1 40  ? 22.319  9.045   45.959 1.00 35.79  ? 39  LEU B C   1 
ATOM   2110 O O   . LEU B 1 40  ? 21.682  7.998   45.857 1.00 37.24  ? 39  LEU B O   1 
ATOM   2111 C CB  . LEU B 1 40  ? 23.154  9.063   48.323 1.00 46.46  ? 39  LEU B CB  1 
ATOM   2112 C CG  . LEU B 1 40  ? 23.251  9.802   49.661 1.00 41.41  ? 39  LEU B CG  1 
ATOM   2113 C CD1 . LEU B 1 40  ? 24.410  9.279   50.488 1.00 68.87  ? 39  LEU B CD1 1 
ATOM   2114 C CD2 . LEU B 1 40  ? 23.382  11.290  49.389 1.00 30.06  ? 39  LEU B CD2 1 
ATOM   2115 N N   . PRO B 1 41  ? 23.007  9.517   44.928 1.00 26.95  ? 40  PRO B N   1 
ATOM   2116 C CA  . PRO B 1 41  ? 23.078  8.727   43.692 1.00 30.52  ? 40  PRO B CA  1 
ATOM   2117 C C   . PRO B 1 41  ? 23.594  7.317   43.941 1.00 31.97  ? 40  PRO B C   1 
ATOM   2118 O O   . PRO B 1 41  ? 24.598  7.074   44.619 1.00 33.01  ? 40  PRO B O   1 
ATOM   2119 C CB  . PRO B 1 41  ? 24.060  9.515   42.831 1.00 34.76  ? 40  PRO B CB  1 
ATOM   2120 C CG  . PRO B 1 41  ? 24.660  10.566  43.696 1.00 32.22  ? 40  PRO B CG  1 
ATOM   2121 C CD  . PRO B 1 41  ? 23.729  10.787  44.845 1.00 23.80  ? 40  PRO B CD  1 
ATOM   2122 N N   . THR B 1 42  ? 22.914  6.295   43.398 1.00 30.38  ? 41  THR B N   1 
ATOM   2123 C CA  . THR B 1 42  ? 23.512  4.970   43.575 1.00 27.16  ? 41  THR B CA  1 
ATOM   2124 C C   . THR B 1 42  ? 24.556  4.755   42.478 1.00 35.32  ? 41  THR B C   1 
ATOM   2125 O O   . THR B 1 42  ? 24.854  5.661   41.695 1.00 30.46  ? 41  THR B O   1 
ATOM   2126 C CB  . THR B 1 42  ? 22.542  3.787   43.521 1.00 24.64  ? 41  THR B CB  1 
ATOM   2127 O OG1 . THR B 1 42  ? 22.008  3.692   42.191 1.00 27.04  ? 41  THR B OG1 1 
ATOM   2128 C CG2 . THR B 1 42  ? 21.370  3.989   44.463 1.00 26.51  ? 41  THR B CG2 1 
ATOM   2129 N N   . ILE B 1 43  ? 25.096  3.536   42.441 1.00 22.97  ? 42  ILE B N   1 
ATOM   2130 C CA  . ILE B 1 43  ? 26.156  3.328   41.437 1.00 31.36  ? 42  ILE B CA  1 
ATOM   2131 C C   . ILE B 1 43  ? 25.579  3.120   40.045 1.00 29.14  ? 42  ILE B C   1 
ATOM   2132 O O   . ILE B 1 43  ? 26.204  3.544   39.053 1.00 26.46  ? 42  ILE B O   1 
ATOM   2133 C CB  . ILE B 1 43  ? 27.069  2.185   41.904 1.00 38.51  ? 42  ILE B CB  1 
ATOM   2134 C CG1 . ILE B 1 43  ? 28.196  2.715   42.819 1.00 42.18  ? 42  ILE B CG1 1 
ATOM   2135 C CG2 . ILE B 1 43  ? 27.681  1.368   40.787 1.00 29.25  ? 42  ILE B CG2 1 
ATOM   2136 C CD1 . ILE B 1 43  ? 28.600  1.709   43.859 1.00 32.70  ? 42  ILE B CD1 1 
ATOM   2137 N N   . LEU B 1 44  ? 24.416  2.495   39.899 1.00 21.55  ? 43  LEU B N   1 
ATOM   2138 C CA  . LEU B 1 44  ? 23.872  2.278   38.548 1.00 26.60  ? 43  LEU B CA  1 
ATOM   2139 C C   . LEU B 1 44  ? 23.404  3.626   38.003 1.00 24.90  ? 43  LEU B C   1 
ATOM   2140 O O   . LEU B 1 44  ? 23.481  3.918   36.811 1.00 19.71  ? 43  LEU B O   1 
ATOM   2141 C CB  . LEU B 1 44  ? 22.753  1.249   38.544 1.00 29.15  ? 43  LEU B CB  1 
ATOM   2142 C CG  . LEU B 1 44  ? 22.080  0.848   37.223 1.00 22.48  ? 43  LEU B CG  1 
ATOM   2143 C CD1 . LEU B 1 44  ? 23.080  0.225   36.256 1.00 18.76  ? 43  LEU B CD1 1 
ATOM   2144 C CD2 . LEU B 1 44  ? 20.929  -0.107  37.505 1.00 13.87  ? 43  LEU B CD2 1 
ATOM   2145 N N   . GLN B 1 45  ? 22.943  4.427   38.951 1.00 19.12  ? 44  GLN B N   1 
ATOM   2146 C CA  . GLN B 1 45  ? 22.453  5.780   38.716 1.00 31.39  ? 44  GLN B CA  1 
ATOM   2147 C C   . GLN B 1 45  ? 23.501  6.640   38.022 1.00 32.29  ? 44  GLN B C   1 
ATOM   2148 O O   . GLN B 1 45  ? 23.361  7.309   37.002 1.00 21.93  ? 44  GLN B O   1 
ATOM   2149 C CB  . GLN B 1 45  ? 22.055  6.367   40.072 1.00 38.45  ? 44  GLN B CB  1 
ATOM   2150 C CG  . GLN B 1 45  ? 21.626  7.817   40.073 1.00 47.56  ? 44  GLN B CG  1 
ATOM   2151 C CD  . GLN B 1 45  ? 20.425  8.099   40.959 1.00 38.59  ? 44  GLN B CD  1 
ATOM   2152 O OE1 . GLN B 1 45  ? 19.741  7.186   41.417 1.00 32.77  ? 44  GLN B OE1 1 
ATOM   2153 N NE2 . GLN B 1 45  ? 20.174  9.383   41.183 1.00 25.99  ? 44  GLN B NE2 1 
ATOM   2154 N N   . ILE B 1 46  ? 24.675  6.610   38.638 1.00 25.37  ? 45  ILE B N   1 
ATOM   2155 C CA  . ILE B 1 46  ? 25.797  7.397   38.172 1.00 23.15  ? 45  ILE B CA  1 
ATOM   2156 C C   . ILE B 1 46  ? 26.349  6.840   36.877 1.00 30.15  ? 45  ILE B C   1 
ATOM   2157 O O   . ILE B 1 46  ? 26.627  7.573   35.925 1.00 28.48  ? 45  ILE B O   1 
ATOM   2158 C CB  . ILE B 1 46  ? 26.882  7.390   39.267 1.00 17.10  ? 45  ILE B CB  1 
ATOM   2159 C CG1 . ILE B 1 46  ? 26.447  8.173   40.508 1.00 30.99  ? 45  ILE B CG1 1 
ATOM   2160 C CG2 . ILE B 1 46  ? 28.202  7.868   38.698 1.00 22.91  ? 45  ILE B CG2 1 
ATOM   2161 C CD1 . ILE B 1 46  ? 27.187  7.799   41.778 1.00 28.55  ? 45  ILE B CD1 1 
ATOM   2162 N N   . ALA B 1 47  ? 26.502  5.508   36.857 1.00 21.51  ? 46  ALA B N   1 
ATOM   2163 C CA  . ALA B 1 47  ? 27.049  4.925   35.630 1.00 29.14  ? 46  ALA B CA  1 
ATOM   2164 C C   . ALA B 1 47  ? 26.127  5.247   34.450 1.00 42.80  ? 46  ALA B C   1 
ATOM   2165 O O   . ALA B 1 47  ? 26.627  5.675   33.401 1.00 46.95  ? 46  ALA B O   1 
ATOM   2166 C CB  . ALA B 1 47  ? 27.302  3.436   35.779 1.00 18.78  ? 46  ALA B CB  1 
ATOM   2167 N N   . LEU B 1 48  ? 24.814  5.070   34.581 1.00 30.66  ? 47  LEU B N   1 
ATOM   2168 C CA  . LEU B 1 48  ? 23.909  5.326   33.462 1.00 20.83  ? 47  LEU B CA  1 
ATOM   2169 C C   . LEU B 1 48  ? 23.976  6.787   33.039 1.00 25.37  ? 47  LEU B C   1 
ATOM   2170 O O   . LEU B 1 48  ? 23.854  7.139   31.863 1.00 29.66  ? 47  LEU B O   1 
ATOM   2171 C CB  . LEU B 1 48  ? 22.473  4.975   33.835 1.00 32.54  ? 47  LEU B CB  1 
ATOM   2172 C CG  . LEU B 1 48  ? 21.896  3.651   33.343 1.00 42.16  ? 47  LEU B CG  1 
ATOM   2173 C CD1 . LEU B 1 48  ? 20.606  3.322   34.086 1.00 42.66  ? 47  LEU B CD1 1 
ATOM   2174 C CD2 . LEU B 1 48  ? 21.643  3.694   31.844 1.00 35.40  ? 47  LEU B CD2 1 
ATOM   2175 N N   . ALA B 1 49  ? 24.156  7.684   34.014 1.00 23.65  ? 48  ALA B N   1 
ATOM   2176 C CA  . ALA B 1 49  ? 24.218  9.101   33.649 1.00 27.61  ? 48  ALA B CA  1 
ATOM   2177 C C   . ALA B 1 49  ? 25.488  9.366   32.857 1.00 29.47  ? 48  ALA B C   1 
ATOM   2178 O O   . ALA B 1 49  ? 25.555  10.151  31.910 1.00 31.46  ? 48  ALA B O   1 
ATOM   2179 C CB  . ALA B 1 49  ? 24.147  10.010  34.870 1.00 25.54  ? 48  ALA B CB  1 
ATOM   2180 N N   . PHE B 1 50  ? 26.584  8.706   33.240 1.00 23.39  ? 49  PHE B N   1 
ATOM   2181 C CA  . PHE B 1 50  ? 27.782  9.020   32.464 1.00 23.75  ? 49  PHE B CA  1 
ATOM   2182 C C   . PHE B 1 50  ? 27.708  8.472   31.043 1.00 26.48  ? 49  PHE B C   1 
ATOM   2183 O O   . PHE B 1 50  ? 28.105  9.171   30.108 1.00 28.40  ? 49  PHE B O   1 
ATOM   2184 C CB  . PHE B 1 50  ? 29.009  8.443   33.163 1.00 30.17  ? 49  PHE B CB  1 
ATOM   2185 C CG  . PHE B 1 50  ? 29.715  9.479   34.024 1.00 32.43  ? 49  PHE B CG  1 
ATOM   2186 C CD1 . PHE B 1 50  ? 30.856  10.113  33.565 1.00 27.79  ? 49  PHE B CD1 1 
ATOM   2187 C CD2 . PHE B 1 50  ? 29.207  9.783   35.275 1.00 35.55  ? 49  PHE B CD2 1 
ATOM   2188 C CE1 . PHE B 1 50  ? 31.508  11.050  34.344 1.00 27.71  ? 49  PHE B CE1 1 
ATOM   2189 C CE2 . PHE B 1 50  ? 29.869  10.710  36.061 1.00 39.15  ? 49  PHE B CE2 1 
ATOM   2190 C CZ  . PHE B 1 50  ? 31.016  11.335  35.600 1.00 31.61  ? 49  PHE B CZ  1 
ATOM   2191 N N   . GLY B 1 51  ? 27.236  7.244   30.902 1.00 21.03  ? 50  GLY B N   1 
ATOM   2192 C CA  . GLY B 1 51  ? 27.080  6.532   29.651 1.00 19.71  ? 50  GLY B CA  1 
ATOM   2193 C C   . GLY B 1 51  ? 26.125  7.240   28.705 1.00 19.58  ? 50  GLY B C   1 
ATOM   2194 O O   . GLY B 1 51  ? 26.418  7.399   27.517 1.00 23.01  ? 50  GLY B O   1 
ATOM   2195 N N   . LEU B 1 52  ? 24.970  7.673   29.214 1.00 17.99  ? 51  LEU B N   1 
ATOM   2196 C CA  . LEU B 1 52  ? 23.982  8.294   28.336 1.00 17.52  ? 51  LEU B CA  1 
ATOM   2197 C C   . LEU B 1 52  ? 24.344  9.713   27.918 1.00 22.51  ? 51  LEU B C   1 
ATOM   2198 O O   . LEU B 1 52  ? 23.818  10.257  26.943 1.00 18.26  ? 51  LEU B O   1 
ATOM   2199 C CB  . LEU B 1 52  ? 22.608  8.309   29.018 1.00 17.36  ? 51  LEU B CB  1 
ATOM   2200 C CG  . LEU B 1 52  ? 22.013  6.926   29.301 1.00 25.43  ? 51  LEU B CG  1 
ATOM   2201 C CD1 . LEU B 1 52  ? 20.653  7.111   29.962 1.00 25.11  ? 51  LEU B CD1 1 
ATOM   2202 C CD2 . LEU B 1 52  ? 21.899  6.068   28.053 1.00 18.29  ? 51  LEU B CD2 1 
ATOM   2203 N N   . ALA B 1 53  ? 25.237  10.355  28.646 1.00 22.47  ? 52  ALA B N   1 
ATOM   2204 C CA  . ALA B 1 53  ? 25.769  11.666  28.299 1.00 25.03  ? 52  ALA B CA  1 
ATOM   2205 C C   . ALA B 1 53  ? 26.659  11.543  27.067 1.00 24.43  ? 52  ALA B C   1 
ATOM   2206 O O   . ALA B 1 53  ? 26.539  12.284  26.097 1.00 31.04  ? 52  ALA B O   1 
ATOM   2207 C CB  . ALA B 1 53  ? 26.537  12.228  29.487 1.00 17.09  ? 52  ALA B CB  1 
ATOM   2208 N N   . ILE B 1 54  ? 27.569  10.570  27.105 1.00 21.43  ? 53  ILE B N   1 
ATOM   2209 C CA  . ILE B 1 54  ? 28.452  10.337  25.962 1.00 26.74  ? 53  ILE B CA  1 
ATOM   2210 C C   . ILE B 1 54  ? 27.653  9.813   24.775 1.00 34.59  ? 53  ILE B C   1 
ATOM   2211 O O   . ILE B 1 54  ? 27.807  10.276  23.651 1.00 33.66  ? 53  ILE B O   1 
ATOM   2212 C CB  . ILE B 1 54  ? 29.572  9.339   26.279 1.00 16.74  ? 53  ILE B CB  1 
ATOM   2213 C CG1 . ILE B 1 54  ? 30.596  9.845   27.296 1.00 24.80  ? 53  ILE B CG1 1 
ATOM   2214 C CG2 . ILE B 1 54  ? 30.257  8.907   24.989 1.00 28.79  ? 53  ILE B CG2 1 
ATOM   2215 C CD1 . ILE B 1 54  ? 31.268  11.134  26.849 1.00 41.80  ? 53  ILE B CD1 1 
ATOM   2216 N N   . GLY B 1 55  ? 26.782  8.834   25.035 1.00 37.82  ? 54  GLY B N   1 
ATOM   2217 C CA  . GLY B 1 55  ? 25.919  8.337   23.973 1.00 24.31  ? 54  GLY B CA  1 
ATOM   2218 C C   . GLY B 1 55  ? 25.147  9.493   23.352 1.00 22.78  ? 54  GLY B C   1 
ATOM   2219 O O   . GLY B 1 55  ? 25.109  9.643   22.137 1.00 27.53  ? 54  GLY B O   1 
ATOM   2220 N N   . THR B 1 56  ? 24.539  10.325  24.195 1.00 21.49  ? 55  THR B N   1 
ATOM   2221 C CA  . THR B 1 56  ? 23.721  11.422  23.697 1.00 25.71  ? 55  THR B CA  1 
ATOM   2222 C C   . THR B 1 56  ? 24.604  12.330  22.840 1.00 33.72  ? 55  THR B C   1 
ATOM   2223 O O   . THR B 1 56  ? 24.290  12.672  21.699 1.00 31.69  ? 55  THR B O   1 
ATOM   2224 C CB  . THR B 1 56  ? 23.066  12.221  24.834 1.00 26.91  ? 55  THR B CB  1 
ATOM   2225 O OG1 . THR B 1 56  ? 22.159  11.361  25.539 1.00 28.21  ? 55  THR B OG1 1 
ATOM   2226 C CG2 . THR B 1 56  ? 22.241  13.371  24.264 1.00 24.01  ? 55  THR B CG2 1 
ATOM   2227 N N   . LEU B 1 57  ? 25.728  12.677  23.450 1.00 30.85  ? 56  LEU B N   1 
ATOM   2228 C CA  . LEU B 1 57  ? 26.677  13.626  22.885 1.00 23.88  ? 56  LEU B CA  1 
ATOM   2229 C C   . LEU B 1 57  ? 27.245  13.139  21.556 1.00 33.10  ? 56  LEU B C   1 
ATOM   2230 O O   . LEU B 1 57  ? 27.457  13.892  20.597 1.00 18.68  ? 56  LEU B O   1 
ATOM   2231 C CB  . LEU B 1 57  ? 27.764  13.861  23.941 1.00 22.66  ? 56  LEU B CB  1 
ATOM   2232 C CG  . LEU B 1 57  ? 27.303  14.814  25.061 1.00 27.11  ? 56  LEU B CG  1 
ATOM   2233 C CD1 . LEU B 1 57  ? 28.470  15.209  25.940 1.00 36.67  ? 56  LEU B CD1 1 
ATOM   2234 C CD2 . LEU B 1 57  ? 26.617  16.031  24.449 1.00 26.83  ? 56  LEU B CD2 1 
ATOM   2235 N N   . ALA B 1 58  ? 27.473  11.826  21.526 1.00 31.13  ? 57  ALA B N   1 
ATOM   2236 C CA  . ALA B 1 58  ? 27.991  11.163  20.339 1.00 34.10  ? 57  ALA B CA  1 
ATOM   2237 C C   . ALA B 1 58  ? 26.978  11.275  19.197 1.00 37.25  ? 57  ALA B C   1 
ATOM   2238 O O   . ALA B 1 58  ? 27.414  11.610  18.093 1.00 27.97  ? 57  ALA B O   1 
ATOM   2239 C CB  . ALA B 1 58  ? 28.348  9.720   20.627 1.00 15.80  ? 57  ALA B CB  1 
ATOM   2240 N N   . GLN B 1 59  ? 25.702  11.024  19.477 1.00 31.92  ? 58  GLN B N   1 
ATOM   2241 C CA  . GLN B 1 59  ? 24.638  11.177  18.501 1.00 42.74  ? 58  GLN B CA  1 
ATOM   2242 C C   . GLN B 1 59  ? 24.601  12.626  17.975 1.00 33.63  ? 58  GLN B C   1 
ATOM   2243 O O   . GLN B 1 59  ? 24.553  12.796  16.766 1.00 30.57  ? 58  GLN B O   1 
ATOM   2244 C CB  . GLN B 1 59  ? 23.243  10.902  19.038 1.00 44.35  ? 58  GLN B CB  1 
ATOM   2245 C CG  . GLN B 1 59  ? 22.537  9.634   18.717 1.00 47.88  ? 58  GLN B CG  1 
ATOM   2246 C CD  . GLN B 1 59  ? 22.309  9.170   17.307 1.00 20.68  ? 58  GLN B CD  1 
ATOM   2247 O OE1 . GLN B 1 59  ? 21.286  9.472   16.677 1.00 27.60  ? 58  GLN B OE1 1 
ATOM   2248 N NE2 . GLN B 1 59  ? 23.255  8.368   16.844 1.00 22.99  ? 58  GLN B NE2 1 
ATOM   2249 N N   . ALA B 1 60  ? 24.606  13.555  18.921 1.00 27.57  ? 59  ALA B N   1 
ATOM   2250 C CA  . ALA B 1 60  ? 24.393  14.975  18.681 1.00 29.25  ? 59  ALA B CA  1 
ATOM   2251 C C   . ALA B 1 60  ? 25.588  15.658  18.041 1.00 32.95  ? 59  ALA B C   1 
ATOM   2252 O O   . ALA B 1 60  ? 25.401  16.534  17.191 1.00 25.88  ? 59  ALA B O   1 
ATOM   2253 C CB  . ALA B 1 60  ? 23.998  15.631  20.003 1.00 19.05  ? 59  ALA B CB  1 
ATOM   2254 N N   . LEU B 1 61  ? 26.854  15.355  18.368 1.00 23.87  ? 60  LEU B N   1 
ATOM   2255 C CA  . LEU B 1 61  ? 27.864  16.272  17.816 1.00 20.25  ? 60  LEU B CA  1 
ATOM   2256 C C   . LEU B 1 61  ? 28.964  15.474  17.150 1.00 24.99  ? 60  LEU B C   1 
ATOM   2257 O O   . LEU B 1 61  ? 29.883  16.004  16.547 1.00 25.34  ? 60  LEU B O   1 
ATOM   2258 C CB  . LEU B 1 61  ? 28.442  17.209  18.875 1.00 23.76  ? 60  LEU B CB  1 
ATOM   2259 C CG  . LEU B 1 61  ? 27.504  18.238  19.515 1.00 18.87  ? 60  LEU B CG  1 
ATOM   2260 C CD1 . LEU B 1 61  ? 28.142  18.954  20.711 1.00 21.19  ? 60  LEU B CD1 1 
ATOM   2261 C CD2 . LEU B 1 61  ? 27.049  19.290  18.527 1.00 33.11  ? 60  LEU B CD2 1 
ATOM   2262 N N   . GLY B 1 62  ? 28.808  14.160  17.281 1.00 22.83  ? 61  GLY B N   1 
ATOM   2263 C CA  . GLY B 1 62  ? 29.664  13.272  16.525 1.00 29.14  ? 61  GLY B CA  1 
ATOM   2264 C C   . GLY B 1 62  ? 29.722  13.640  15.059 1.00 35.97  ? 61  GLY B C   1 
ATOM   2265 O O   . GLY B 1 62  ? 30.817  13.644  14.474 1.00 31.02  ? 61  GLY B O   1 
ATOM   2266 N N   . PRO B 1 63  ? 28.633  13.947  14.370 1.00 34.05  ? 62  PRO B N   1 
ATOM   2267 C CA  . PRO B 1 63  ? 28.797  14.239  12.931 1.00 33.44  ? 62  PRO B CA  1 
ATOM   2268 C C   . PRO B 1 63  ? 29.536  15.553  12.713 1.00 35.66  ? 62  PRO B C   1 
ATOM   2269 O O   . PRO B 1 63  ? 29.998  15.873  11.611 1.00 29.20  ? 62  PRO B O   1 
ATOM   2270 C CB  . PRO B 1 63  ? 27.356  14.305  12.415 1.00 35.45  ? 62  PRO B CB  1 
ATOM   2271 C CG  . PRO B 1 63  ? 26.560  13.585  13.465 1.00 26.06  ? 62  PRO B CG  1 
ATOM   2272 C CD  . PRO B 1 63  ? 27.216  14.048  14.748 1.00 29.68  ? 62  PRO B CD  1 
ATOM   2273 N N   . VAL B 1 64  ? 29.676  16.349  13.772 1.00 32.01  ? 63  VAL B N   1 
ATOM   2274 C CA  . VAL B 1 64  ? 30.426  17.591  13.624 1.00 26.15  ? 63  VAL B CA  1 
ATOM   2275 C C   . VAL B 1 64  ? 31.916  17.317  13.788 1.00 31.93  ? 63  VAL B C   1 
ATOM   2276 O O   . VAL B 1 64  ? 32.725  17.694  12.934 1.00 40.48  ? 63  VAL B O   1 
ATOM   2277 C CB  . VAL B 1 64  ? 29.955  18.650  14.627 1.00 24.76  ? 63  VAL B CB  1 
ATOM   2278 C CG1 . VAL B 1 64  ? 30.621  19.992  14.330 1.00 57.06  ? 63  VAL B CG1 1 
ATOM   2279 C CG2 . VAL B 1 64  ? 28.452  18.838  14.609 1.00 16.92  ? 63  VAL B CG2 1 
ATOM   2280 N N   . SER B 1 65  ? 32.355  16.657  14.853 1.00 32.68  ? 64  SER B N   1 
ATOM   2281 C CA  . SER B 1 65  ? 33.785  16.464  15.071 1.00 34.98  ? 64  SER B CA  1 
ATOM   2282 C C   . SER B 1 65  ? 34.286  15.034  15.138 1.00 36.62  ? 64  SER B C   1 
ATOM   2283 O O   . SER B 1 65  ? 35.491  14.785  15.300 1.00 40.60  ? 64  SER B O   1 
ATOM   2284 C CB  . SER B 1 65  ? 34.150  17.080  16.442 1.00 28.78  ? 64  SER B CB  1 
ATOM   2285 O OG  . SER B 1 65  ? 33.886  16.050  17.395 1.00 35.95  ? 64  SER B OG  1 
ATOM   2286 N N   . GLY B 1 66  ? 33.421  14.029  15.046 1.00 33.04  ? 65  GLY B N   1 
ATOM   2287 C CA  . GLY B 1 66  ? 33.894  12.673  15.337 1.00 30.94  ? 65  GLY B CA  1 
ATOM   2288 C C   . GLY B 1 66  ? 33.611  12.397  16.820 1.00 33.93  ? 65  GLY B C   1 
ATOM   2289 O O   . GLY B 1 66  ? 33.625  11.240  17.243 1.00 24.00  ? 65  GLY B O   1 
ATOM   2290 N N   . GLY B 1 67  ? 33.362  13.482  17.549 1.00 32.19  ? 66  GLY B N   1 
ATOM   2291 C CA  . GLY B 1 67  ? 32.980  13.499  18.942 1.00 34.90  ? 66  GLY B CA  1 
ATOM   2292 C C   . GLY B 1 67  ? 33.828  12.668  19.874 1.00 33.32  ? 66  GLY B C   1 
ATOM   2293 O O   . GLY B 1 67  ? 33.382  11.746  20.568 1.00 36.41  ? 66  GLY B O   1 
ATOM   2294 N N   . HIS B 1 68  ? 35.116  13.005  19.905 1.00 27.07  ? 67  HIS B N   1 
ATOM   2295 C CA  . HIS B 1 68  ? 36.037  12.303  20.786 1.00 24.85  ? 67  HIS B CA  1 
ATOM   2296 C C   . HIS B 1 68  ? 35.603  12.471  22.235 1.00 35.32  ? 67  HIS B C   1 
ATOM   2297 O O   . HIS B 1 68  ? 35.365  11.506  22.959 1.00 26.17  ? 67  HIS B O   1 
ATOM   2298 C CB  . HIS B 1 68  ? 37.455  12.833  20.578 1.00 34.63  ? 67  HIS B CB  1 
ATOM   2299 C CG  . HIS B 1 68  ? 38.006  12.538  19.219 1.00 38.65  ? 67  HIS B CG  1 
ATOM   2300 N ND1 . HIS B 1 68  ? 39.239  12.973  18.791 1.00 45.27  ? 67  HIS B ND1 1 
ATOM   2301 C CD2 . HIS B 1 68  ? 37.500  11.833  18.185 1.00 41.66  ? 67  HIS B CD2 1 
ATOM   2302 C CE1 . HIS B 1 68  ? 39.469  12.562  17.557 1.00 41.92  ? 67  HIS B CE1 1 
ATOM   2303 N NE2 . HIS B 1 68  ? 38.422  11.866  17.165 1.00 42.32  ? 67  HIS B NE2 1 
ATOM   2304 N N   . ILE B 1 69  ? 35.507  13.737  22.647 1.00 28.90  ? 68  ILE B N   1 
ATOM   2305 C CA  . ILE B 1 69  ? 35.144  14.036  24.023 1.00 30.83  ? 68  ILE B CA  1 
ATOM   2306 C C   . ILE B 1 69  ? 36.054  13.293  25.000 1.00 41.64  ? 68  ILE B C   1 
ATOM   2307 O O   . ILE B 1 69  ? 35.627  12.931  26.102 1.00 44.12  ? 68  ILE B O   1 
ATOM   2308 C CB  . ILE B 1 69  ? 33.686  13.644  24.311 1.00 28.71  ? 68  ILE B CB  1 
ATOM   2309 C CG1 . ILE B 1 69  ? 32.743  13.854  23.117 1.00 36.10  ? 68  ILE B CG1 1 
ATOM   2310 C CG2 . ILE B 1 69  ? 33.152  14.348  25.544 1.00 19.25  ? 68  ILE B CG2 1 
ATOM   2311 C CD1 . ILE B 1 69  ? 31.484  13.011  23.244 1.00 33.42  ? 68  ILE B CD1 1 
ATOM   2312 N N   . ASN B 1 70  ? 37.312  13.065  24.621 1.00 35.88  ? 69  ASN B N   1 
ATOM   2313 C CA  . ASN B 1 70  ? 38.220  12.366  25.537 1.00 36.64  ? 69  ASN B CA  1 
ATOM   2314 C C   . ASN B 1 70  ? 39.620  12.272  24.937 1.00 36.23  ? 69  ASN B C   1 
ATOM   2315 O O   . ASN B 1 70  ? 39.867  11.638  23.917 1.00 28.62  ? 69  ASN B O   1 
ATOM   2316 C CB  . ASN B 1 70  ? 37.638  10.998  25.873 1.00 23.27  ? 69  ASN B CB  1 
ATOM   2317 C CG  . ASN B 1 70  ? 38.523  10.100  26.695 1.00 21.18  ? 69  ASN B CG  1 
ATOM   2318 O OD1 . ASN B 1 70  ? 39.680  10.367  26.987 1.00 27.06  ? 69  ASN B OD1 1 
ATOM   2319 N ND2 . ASN B 1 70  ? 37.963  8.957   27.099 1.00 27.84  ? 69  ASN B ND2 1 
ATOM   2320 N N   . PRO B 1 71  ? 40.550  12.952  25.606 1.00 42.76  ? 70  PRO B N   1 
ATOM   2321 C CA  . PRO B 1 71  ? 41.971  12.964  25.253 1.00 39.79  ? 70  PRO B CA  1 
ATOM   2322 C C   . PRO B 1 71  ? 42.554  11.603  24.891 1.00 41.44  ? 70  PRO B C   1 
ATOM   2323 O O   . PRO B 1 71  ? 43.193  11.456  23.843 1.00 42.42  ? 70  PRO B O   1 
ATOM   2324 C CB  . PRO B 1 71  ? 42.620  13.468  26.554 1.00 33.07  ? 70  PRO B CB  1 
ATOM   2325 C CG  . PRO B 1 71  ? 41.604  14.432  27.087 1.00 28.47  ? 70  PRO B CG  1 
ATOM   2326 C CD  . PRO B 1 71  ? 40.264  13.815  26.779 1.00 33.83  ? 70  PRO B CD  1 
ATOM   2327 N N   . ALA B 1 72  ? 42.335  10.628  25.763 1.00 36.59  ? 71  ALA B N   1 
ATOM   2328 C CA  . ALA B 1 72  ? 42.858  9.278   25.581 1.00 34.78  ? 71  ALA B CA  1 
ATOM   2329 C C   . ALA B 1 72  ? 42.563  8.752   24.178 1.00 34.35  ? 71  ALA B C   1 
ATOM   2330 O O   . ALA B 1 72  ? 43.426  8.191   23.504 1.00 59.06  ? 71  ALA B O   1 
ATOM   2331 C CB  . ALA B 1 72  ? 42.284  8.354   26.660 1.00 24.89  ? 71  ALA B CB  1 
ATOM   2332 N N   . ILE B 1 73  ? 41.320  8.952   23.762 1.00 40.93  ? 72  ILE B N   1 
ATOM   2333 C CA  . ILE B 1 73  ? 40.795  8.443   22.502 1.00 44.59  ? 72  ILE B CA  1 
ATOM   2334 C C   . ILE B 1 73  ? 41.315  9.270   21.335 1.00 46.78  ? 72  ILE B C   1 
ATOM   2335 O O   . ILE B 1 73  ? 41.680  8.741   20.289 1.00 45.04  ? 72  ILE B O   1 
ATOM   2336 C CB  . ILE B 1 73  ? 39.255  8.428   22.521 1.00 25.30  ? 72  ILE B CB  1 
ATOM   2337 C CG1 . ILE B 1 73  ? 38.693  7.238   23.311 1.00 25.86  ? 72  ILE B CG1 1 
ATOM   2338 C CG2 . ILE B 1 73  ? 38.694  8.452   21.116 1.00 25.07  ? 72  ILE B CG2 1 
ATOM   2339 C CD1 . ILE B 1 73  ? 37.337  7.519   23.905 1.00 39.40  ? 72  ILE B CD1 1 
ATOM   2340 N N   . THR B 1 74  ? 41.350  10.586  21.535 1.00 48.04  ? 73  THR B N   1 
ATOM   2341 C CA  . THR B 1 74  ? 41.889  11.441  20.479 1.00 43.73  ? 73  THR B CA  1 
ATOM   2342 C C   . THR B 1 74  ? 43.328  10.998  20.236 1.00 41.83  ? 73  THR B C   1 
ATOM   2343 O O   . THR B 1 74  ? 43.719  10.676  19.117 1.00 41.88  ? 73  THR B O   1 
ATOM   2344 C CB  . THR B 1 74  ? 41.826  12.923  20.865 1.00 41.41  ? 73  THR B CB  1 
ATOM   2345 O OG1 . THR B 1 74  ? 40.452  13.324  20.945 1.00 33.25  ? 73  THR B OG1 1 
ATOM   2346 C CG2 . THR B 1 74  ? 42.480  13.807  19.813 1.00 43.60  ? 73  THR B CG2 1 
ATOM   2347 N N   . LEU B 1 75  ? 44.078  10.977  21.333 1.00 28.63  ? 74  LEU B N   1 
ATOM   2348 C CA  . LEU B 1 75  ? 45.480  10.592  21.282 1.00 30.67  ? 74  LEU B CA  1 
ATOM   2349 C C   . LEU B 1 75  ? 45.623  9.246   20.575 1.00 41.52  ? 74  LEU B C   1 
ATOM   2350 O O   . LEU B 1 75  ? 46.532  9.006   19.778 1.00 55.98  ? 74  LEU B O   1 
ATOM   2351 C CB  . LEU B 1 75  ? 46.058  10.518  22.696 1.00 29.74  ? 74  LEU B CB  1 
ATOM   2352 C CG  . LEU B 1 75  ? 45.944  11.816  23.505 1.00 39.18  ? 74  LEU B CG  1 
ATOM   2353 C CD1 . LEU B 1 75  ? 46.084  11.587  25.001 1.00 26.21  ? 74  LEU B CD1 1 
ATOM   2354 C CD2 . LEU B 1 75  ? 46.992  12.807  23.021 1.00 57.81  ? 74  LEU B CD2 1 
ATOM   2355 N N   . ALA B 1 76  ? 44.682  8.354   20.887 1.00 31.77  ? 75  ALA B N   1 
ATOM   2356 C CA  . ALA B 1 76  ? 44.768  7.008   20.337 1.00 29.75  ? 75  ALA B CA  1 
ATOM   2357 C C   . ALA B 1 76  ? 44.408  6.981   18.860 1.00 31.93  ? 75  ALA B C   1 
ATOM   2358 O O   . ALA B 1 76  ? 44.918  6.151   18.096 1.00 28.31  ? 75  ALA B O   1 
ATOM   2359 C CB  . ALA B 1 76  ? 43.859  6.080   21.125 1.00 32.69  ? 75  ALA B CB  1 
ATOM   2360 N N   . LEU B 1 77  ? 43.519  7.886   18.435 1.00 33.15  ? 76  LEU B N   1 
ATOM   2361 C CA  . LEU B 1 77  ? 43.220  7.896   17.000 1.00 39.95  ? 76  LEU B CA  1 
ATOM   2362 C C   . LEU B 1 77  ? 44.386  8.447   16.183 1.00 30.53  ? 76  LEU B C   1 
ATOM   2363 O O   . LEU B 1 77  ? 44.486  8.146   15.006 1.00 40.06  ? 76  LEU B O   1 
ATOM   2364 C CB  . LEU B 1 77  ? 41.966  8.718   16.721 1.00 38.54  ? 76  LEU B CB  1 
ATOM   2365 C CG  . LEU B 1 77  ? 40.687  8.054   17.245 1.00 34.50  ? 76  LEU B CG  1 
ATOM   2366 C CD1 . LEU B 1 77  ? 39.652  9.117   17.571 1.00 27.29  ? 76  LEU B CD1 1 
ATOM   2367 C CD2 . LEU B 1 77  ? 40.194  7.045   16.223 1.00 25.20  ? 76  LEU B CD2 1 
ATOM   2368 N N   . LEU B 1 78  ? 45.228  9.234   16.829 1.00 37.16  ? 77  LEU B N   1 
ATOM   2369 C CA  . LEU B 1 78  ? 46.445  9.807   16.274 1.00 36.73  ? 77  LEU B CA  1 
ATOM   2370 C C   . LEU B 1 78  ? 47.433  8.693   15.939 1.00 33.48  ? 77  LEU B C   1 
ATOM   2371 O O   . LEU B 1 78  ? 47.721  8.413   14.788 1.00 31.08  ? 77  LEU B O   1 
ATOM   2372 C CB  . LEU B 1 78  ? 47.082  10.762  17.278 1.00 35.53  ? 77  LEU B CB  1 
ATOM   2373 C CG  . LEU B 1 78  ? 48.384  11.411  16.813 1.00 37.83  ? 77  LEU B CG  1 
ATOM   2374 C CD1 . LEU B 1 78  ? 48.250  11.832  15.355 1.00 45.98  ? 77  LEU B CD1 1 
ATOM   2375 C CD2 . LEU B 1 78  ? 48.735  12.582  17.705 1.00 18.45  ? 77  LEU B CD2 1 
ATOM   2376 N N   . VAL B 1 79  ? 47.893  8.088   17.019 1.00 43.87  ? 78  VAL B N   1 
ATOM   2377 C CA  . VAL B 1 79  ? 48.730  6.902   17.028 1.00 48.13  ? 78  VAL B CA  1 
ATOM   2378 C C   . VAL B 1 79  ? 48.214  5.853   16.058 1.00 39.04  ? 78  VAL B C   1 
ATOM   2379 O O   . VAL B 1 79  ? 48.972  5.211   15.336 1.00 29.35  ? 78  VAL B O   1 
ATOM   2380 C CB  . VAL B 1 79  ? 48.794  6.285   18.441 1.00 57.65  ? 78  VAL B CB  1 
ATOM   2381 C CG1 . VAL B 1 79  ? 49.778  5.120   18.460 1.00 76.58  ? 78  VAL B CG1 1 
ATOM   2382 C CG2 . VAL B 1 79  ? 49.153  7.347   19.476 1.00 27.53  ? 78  VAL B CG2 1 
ATOM   2383 N N   . GLY B 1 80  ? 46.896  5.669   16.001 1.00 34.23  ? 79  GLY B N   1 
ATOM   2384 C CA  . GLY B 1 80  ? 46.354  4.739   15.022 1.00 30.43  ? 79  GLY B CA  1 
ATOM   2385 C C   . GLY B 1 80  ? 46.355  5.306   13.614 1.00 40.67  ? 79  GLY B C   1 
ATOM   2386 O O   . GLY B 1 80  ? 45.798  4.705   12.688 1.00 36.98  ? 79  GLY B O   1 
ATOM   2387 N N   . ASN B 1 81  ? 46.976  6.469   13.406 1.00 38.47  ? 80  ASN B N   1 
ATOM   2388 C CA  . ASN B 1 81  ? 47.050  7.052   12.081 1.00 40.12  ? 80  ASN B CA  1 
ATOM   2389 C C   . ASN B 1 81  ? 45.658  7.349   11.537 1.00 45.13  ? 80  ASN B C   1 
ATOM   2390 O O   . ASN B 1 81  ? 45.391  7.218   10.339 1.00 49.73  ? 80  ASN B O   1 
ATOM   2391 C CB  . ASN B 1 81  ? 47.772  6.115   11.105 1.00 38.36  ? 80  ASN B CB  1 
ATOM   2392 C CG  . ASN B 1 81  ? 48.608  6.909   10.116 1.00 36.41  ? 80  ASN B CG  1 
ATOM   2393 O OD1 . ASN B 1 81  ? 49.117  6.359   9.146  1.00 52.95  ? 80  ASN B OD1 1 
ATOM   2394 N ND2 . ASN B 1 81  ? 48.763  8.208   10.354 1.00 27.87  ? 80  ASN B ND2 1 
ATOM   2395 N N   . GLN B 1 82  ? 44.777  7.740   12.453 1.00 32.61  ? 81  GLN B N   1 
ATOM   2396 C CA  . GLN B 1 82  ? 43.420  8.055   12.055 1.00 23.94  ? 81  GLN B CA  1 
ATOM   2397 C C   . GLN B 1 82  ? 43.210  9.553   11.913 1.00 24.23  ? 81  GLN B C   1 
ATOM   2398 O O   . GLN B 1 82  ? 42.242  9.926   11.252 1.00 35.55  ? 81  GLN B O   1 
ATOM   2399 C CB  . GLN B 1 82  ? 42.399  7.533   13.081 1.00 23.34  ? 81  GLN B CB  1 
ATOM   2400 C CG  . GLN B 1 82  ? 41.352  6.665   12.404 1.00 40.79  ? 81  GLN B CG  1 
ATOM   2401 C CD  . GLN B 1 82  ? 42.015  5.442   11.788 1.00 45.68  ? 81  GLN B CD  1 
ATOM   2402 O OE1 . GLN B 1 82  ? 41.495  4.860   10.838 1.00 42.50  ? 81  GLN B OE1 1 
ATOM   2403 N NE2 . GLN B 1 82  ? 43.163  5.085   12.354 1.00 49.70  ? 81  GLN B NE2 1 
ATOM   2404 N N   . ILE B 1 83  ? 44.058  10.368  12.529 1.00 31.80  ? 82  ILE B N   1 
ATOM   2405 C CA  . ILE B 1 83  ? 43.871  11.816  12.465 1.00 39.54  ? 82  ILE B CA  1 
ATOM   2406 C C   . ILE B 1 83  ? 45.217  12.545  12.440 1.00 39.66  ? 82  ILE B C   1 
ATOM   2407 O O   . ILE B 1 83  ? 46.248  11.975  12.778 1.00 43.53  ? 82  ILE B O   1 
ATOM   2408 C CB  . ILE B 1 83  ? 43.076  12.404  13.652 1.00 39.59  ? 82  ILE B CB  1 
ATOM   2409 C CG1 . ILE B 1 83  ? 43.661  12.015  15.010 1.00 30.27  ? 82  ILE B CG1 1 
ATOM   2410 C CG2 . ILE B 1 83  ? 41.596  12.051  13.580 1.00 31.03  ? 82  ILE B CG2 1 
ATOM   2411 C CD1 . ILE B 1 83  ? 43.269  12.963  16.131 1.00 50.97  ? 82  ILE B CD1 1 
ATOM   2412 N N   . SER B 1 84  ? 45.143  13.806  12.052 1.00 42.11  ? 83  SER B N   1 
ATOM   2413 C CA  . SER B 1 84  ? 46.264  14.718  11.974 1.00 37.09  ? 83  SER B CA  1 
ATOM   2414 C C   . SER B 1 84  ? 46.732  15.167  13.355 1.00 34.75  ? 83  SER B C   1 
ATOM   2415 O O   . SER B 1 84  ? 45.923  15.379  14.250 1.00 43.37  ? 83  SER B O   1 
ATOM   2416 C CB  . SER B 1 84  ? 45.888  15.973  11.171 1.00 29.35  ? 83  SER B CB  1 
ATOM   2417 O OG  . SER B 1 84  ? 45.602  17.053  12.056 1.00 29.28  ? 83  SER B OG  1 
ATOM   2418 N N   . LEU B 1 85  ? 48.037  15.331  13.510 1.00 29.07  ? 84  LEU B N   1 
ATOM   2419 C CA  . LEU B 1 85  ? 48.615  15.868  14.733 1.00 38.27  ? 84  LEU B CA  1 
ATOM   2420 C C   . LEU B 1 85  ? 47.956  17.176  15.122 1.00 41.71  ? 84  LEU B C   1 
ATOM   2421 O O   . LEU B 1 85  ? 47.808  17.495  16.305 1.00 42.23  ? 84  LEU B O   1 
ATOM   2422 C CB  . LEU B 1 85  ? 50.126  16.063  14.536 1.00 56.84  ? 84  LEU B CB  1 
ATOM   2423 C CG  . LEU B 1 85  ? 50.920  16.628  15.715 1.00 60.08  ? 84  LEU B CG  1 
ATOM   2424 C CD1 . LEU B 1 85  ? 51.723  15.527  16.396 1.00 49.87  ? 84  LEU B CD1 1 
ATOM   2425 C CD2 . LEU B 1 85  ? 51.813  17.783  15.264 1.00 31.57  ? 84  LEU B CD2 1 
ATOM   2426 N N   . LEU B 1 86  ? 47.542  17.995  14.147 1.00 46.02  ? 85  LEU B N   1 
ATOM   2427 C CA  . LEU B 1 86  ? 47.000  19.283  14.600 1.00 52.13  ? 85  LEU B CA  1 
ATOM   2428 C C   . LEU B 1 86  ? 45.533  19.187  14.975 1.00 52.97  ? 85  LEU B C   1 
ATOM   2429 O O   . LEU B 1 86  ? 44.995  20.035  15.689 1.00 64.63  ? 85  LEU B O   1 
ATOM   2430 C CB  . LEU B 1 86  ? 47.196  20.361  13.532 1.00 55.37  ? 85  LEU B CB  1 
ATOM   2431 C CG  . LEU B 1 86  ? 48.382  21.287  13.834 1.00 56.41  ? 85  LEU B CG  1 
ATOM   2432 C CD1 . LEU B 1 86  ? 49.510  20.999  12.852 1.00 55.71  ? 85  LEU B CD1 1 
ATOM   2433 C CD2 . LEU B 1 86  ? 47.932  22.738  13.805 1.00 57.46  ? 85  LEU B CD2 1 
ATOM   2434 N N   . ARG B 1 87  ? 44.842  18.149  14.504 1.00 49.44  ? 86  ARG B N   1 
ATOM   2435 C CA  . ARG B 1 87  ? 43.468  18.025  15.001 1.00 43.58  ? 86  ARG B CA  1 
ATOM   2436 C C   . ARG B 1 87  ? 43.488  17.455  16.427 1.00 34.63  ? 86  ARG B C   1 
ATOM   2437 O O   . ARG B 1 87  ? 42.586  17.769  17.202 1.00 46.36  ? 86  ARG B O   1 
ATOM   2438 C CB  . ARG B 1 87  ? 42.609  17.183  14.072 1.00 33.24  ? 86  ARG B CB  1 
ATOM   2439 C CG  . ARG B 1 87  ? 41.213  16.943  14.627 1.00 42.38  ? 86  ARG B CG  1 
ATOM   2440 C CD  . ARG B 1 87  ? 40.460  15.925  13.769 1.00 50.85  ? 86  ARG B CD  1 
ATOM   2441 N NE  . ARG B 1 87  ? 40.598  16.322  12.362 1.00 47.04  ? 86  ARG B NE  1 
ATOM   2442 C CZ  . ARG B 1 87  ? 39.747  17.166  11.792 1.00 39.58  ? 86  ARG B CZ  1 
ATOM   2443 N NH1 . ARG B 1 87  ? 38.748  17.649  12.521 1.00 39.15  ? 86  ARG B NH1 1 
ATOM   2444 N NH2 . ARG B 1 87  ? 39.920  17.490  10.521 1.00 25.42  ? 86  ARG B NH2 1 
ATOM   2445 N N   . ALA B 1 88  ? 44.503  16.685  16.737 1.00 21.38  ? 87  ALA B N   1 
ATOM   2446 C CA  . ALA B 1 88  ? 44.852  16.036  17.975 1.00 34.23  ? 87  ALA B CA  1 
ATOM   2447 C C   . ALA B 1 88  ? 45.224  16.984  19.113 1.00 48.57  ? 87  ALA B C   1 
ATOM   2448 O O   . ALA B 1 88  ? 44.827  16.752  20.265 1.00 35.73  ? 87  ALA B O   1 
ATOM   2449 C CB  . ALA B 1 88  ? 46.018  15.071  17.723 1.00 42.06  ? 87  ALA B CB  1 
ATOM   2450 N N   . PHE B 1 89  ? 45.989  18.028  18.815 1.00 52.63  ? 88  PHE B N   1 
ATOM   2451 C CA  . PHE B 1 89  ? 46.408  19.024  19.806 1.00 45.03  ? 88  PHE B CA  1 
ATOM   2452 C C   . PHE B 1 89  ? 45.246  19.960  20.136 1.00 39.00  ? 88  PHE B C   1 
ATOM   2453 O O   . PHE B 1 89  ? 44.950  20.244  21.295 1.00 35.11  ? 88  PHE B O   1 
ATOM   2454 C CB  . PHE B 1 89  ? 47.624  19.784  19.285 1.00 41.32  ? 88  PHE B CB  1 
ATOM   2455 C CG  . PHE B 1 89  ? 47.868  21.157  19.883 1.00 53.54  ? 88  PHE B CG  1 
ATOM   2456 C CD1 . PHE B 1 89  ? 48.592  21.294  21.057 1.00 57.84  ? 88  PHE B CD1 1 
ATOM   2457 C CD2 . PHE B 1 89  ? 47.389  22.310  19.276 1.00 58.69  ? 88  PHE B CD2 1 
ATOM   2458 C CE1 . PHE B 1 89  ? 48.828  22.531  21.625 1.00 51.72  ? 88  PHE B CE1 1 
ATOM   2459 C CE2 . PHE B 1 89  ? 47.605  23.552  19.840 1.00 59.01  ? 88  PHE B CE2 1 
ATOM   2460 C CZ  . PHE B 1 89  ? 48.322  23.666  21.017 1.00 54.64  ? 88  PHE B CZ  1 
ATOM   2461 N N   . PHE B 1 90  ? 44.608  20.431  19.060 1.00 39.14  ? 89  PHE B N   1 
ATOM   2462 C CA  . PHE B 1 90  ? 43.414  21.257  19.185 1.00 33.89  ? 89  PHE B CA  1 
ATOM   2463 C C   . PHE B 1 90  ? 42.324  20.471  19.904 1.00 41.82  ? 89  PHE B C   1 
ATOM   2464 O O   . PHE B 1 90  ? 41.796  20.967  20.904 1.00 47.12  ? 89  PHE B O   1 
ATOM   2465 C CB  . PHE B 1 90  ? 42.929  21.769  17.827 1.00 24.89  ? 89  PHE B CB  1 
ATOM   2466 C CG  . PHE B 1 90  ? 43.720  22.995  17.381 1.00 40.04  ? 89  PHE B CG  1 
ATOM   2467 C CD1 . PHE B 1 90  ? 44.797  22.880  16.523 1.00 42.93  ? 89  PHE B CD1 1 
ATOM   2468 C CD2 . PHE B 1 90  ? 43.375  24.256  17.832 1.00 49.64  ? 89  PHE B CD2 1 
ATOM   2469 C CE1 . PHE B 1 90  ? 45.508  23.996  16.128 1.00 48.63  ? 89  PHE B CE1 1 
ATOM   2470 C CE2 . PHE B 1 90  ? 44.070  25.381  17.438 1.00 51.47  ? 89  PHE B CE2 1 
ATOM   2471 C CZ  . PHE B 1 90  ? 45.144  25.253  16.575 1.00 51.47  ? 89  PHE B CZ  1 
ATOM   2472 N N   . TYR B 1 91  ? 41.995  19.270  19.437 1.00 45.62  ? 90  TYR B N   1 
ATOM   2473 C CA  . TYR B 1 91  ? 40.977  18.467  20.118 1.00 38.54  ? 90  TYR B CA  1 
ATOM   2474 C C   . TYR B 1 91  ? 41.285  18.309  21.602 1.00 34.75  ? 90  TYR B C   1 
ATOM   2475 O O   . TYR B 1 91  ? 40.427  18.522  22.468 1.00 28.91  ? 90  TYR B O   1 
ATOM   2476 C CB  . TYR B 1 91  ? 40.842  17.086  19.476 1.00 33.45  ? 90  TYR B CB  1 
ATOM   2477 C CG  . TYR B 1 91  ? 39.902  17.036  18.292 1.00 28.55  ? 90  TYR B CG  1 
ATOM   2478 C CD1 . TYR B 1 91  ? 39.609  18.172  17.544 1.00 33.45  ? 90  TYR B CD1 1 
ATOM   2479 C CD2 . TYR B 1 91  ? 39.295  15.844  17.909 1.00 18.32  ? 90  TYR B CD2 1 
ATOM   2480 C CE1 . TYR B 1 91  ? 38.745  18.122  16.467 1.00 25.46  ? 90  TYR B CE1 1 
ATOM   2481 C CE2 . TYR B 1 91  ? 38.438  15.774  16.833 1.00 18.09  ? 90  TYR B CE2 1 
ATOM   2482 C CZ  . TYR B 1 91  ? 38.170  16.921  16.111 1.00 29.73  ? 90  TYR B CZ  1 
ATOM   2483 O OH  . TYR B 1 91  ? 37.318  16.873  15.029 1.00 43.94  ? 90  TYR B OH  1 
ATOM   2484 N N   . VAL B 1 92  ? 42.524  17.940  21.925 1.00 35.26  ? 91  VAL B N   1 
ATOM   2485 C CA  . VAL B 1 92  ? 42.817  17.783  23.355 1.00 42.32  ? 91  VAL B CA  1 
ATOM   2486 C C   . VAL B 1 92  ? 42.623  19.098  24.106 1.00 51.22  ? 91  VAL B C   1 
ATOM   2487 O O   . VAL B 1 92  ? 41.918  19.144  25.127 1.00 43.78  ? 91  VAL B O   1 
ATOM   2488 C CB  . VAL B 1 92  ? 44.237  17.244  23.581 1.00 37.78  ? 91  VAL B CB  1 
ATOM   2489 C CG1 . VAL B 1 92  ? 44.655  17.347  25.046 1.00 23.74  ? 91  VAL B CG1 1 
ATOM   2490 C CG2 . VAL B 1 92  ? 44.309  15.795  23.126 1.00 29.83  ? 91  VAL B CG2 1 
ATOM   2491 N N   . ALA B 1 93  ? 43.232  20.178  23.612 1.00 44.49  ? 92  ALA B N   1 
ATOM   2492 C CA  . ALA B 1 93  ? 43.090  21.471  24.287 1.00 32.48  ? 92  ALA B CA  1 
ATOM   2493 C C   . ALA B 1 93  ? 41.627  21.850  24.478 1.00 22.22  ? 92  ALA B C   1 
ATOM   2494 O O   . ALA B 1 93  ? 41.218  22.239  25.576 1.00 40.07  ? 92  ALA B O   1 
ATOM   2495 C CB  . ALA B 1 93  ? 43.831  22.559  23.522 1.00 28.78  ? 92  ALA B CB  1 
ATOM   2496 N N   . ALA B 1 94  ? 40.810  21.747  23.434 1.00 25.30  ? 93  ALA B N   1 
ATOM   2497 C CA  . ALA B 1 94  ? 39.410  22.138  23.535 1.00 26.93  ? 93  ALA B CA  1 
ATOM   2498 C C   . ALA B 1 94  ? 38.676  21.327  24.601 1.00 32.65  ? 93  ALA B C   1 
ATOM   2499 O O   . ALA B 1 94  ? 37.736  21.819  25.201 1.00 40.29  ? 93  ALA B O   1 
ATOM   2500 C CB  . ALA B 1 94  ? 38.688  21.931  22.221 1.00 17.88  ? 93  ALA B CB  1 
ATOM   2501 N N   . GLN B 1 95  ? 39.122  20.091  24.764 1.00 38.34  ? 94  GLN B N   1 
ATOM   2502 C CA  . GLN B 1 95  ? 38.499  19.131  25.656 1.00 35.91  ? 94  GLN B CA  1 
ATOM   2503 C C   . GLN B 1 95  ? 38.786  19.517  27.101 1.00 31.07  ? 94  GLN B C   1 
ATOM   2504 O O   . GLN B 1 95  ? 37.865  19.623  27.904 1.00 32.05  ? 94  GLN B O   1 
ATOM   2505 C CB  . GLN B 1 95  ? 39.010  17.712  25.399 1.00 32.92  ? 94  GLN B CB  1 
ATOM   2506 C CG  . GLN B 1 95  ? 38.192  16.925  24.394 1.00 32.54  ? 94  GLN B CG  1 
ATOM   2507 C CD  . GLN B 1 95  ? 39.028  15.955  23.589 1.00 29.29  ? 94  GLN B CD  1 
ATOM   2508 O OE1 . GLN B 1 95  ? 40.094  15.526  24.029 1.00 29.40  ? 94  GLN B OE1 1 
ATOM   2509 N NE2 . GLN B 1 95  ? 38.531  15.611  22.409 1.00 35.19  ? 94  GLN B NE2 1 
ATOM   2510 N N   . LEU B 1 96  ? 40.076  19.712  27.358 1.00 28.52  ? 95  LEU B N   1 
ATOM   2511 C CA  . LEU B 1 96  ? 40.495  20.101  28.708 1.00 34.32  ? 95  LEU B CA  1 
ATOM   2512 C C   . LEU B 1 96  ? 39.819  21.390  29.159 1.00 29.45  ? 95  LEU B C   1 
ATOM   2513 O O   . LEU B 1 96  ? 39.414  21.582  30.312 1.00 45.02  ? 95  LEU B O   1 
ATOM   2514 C CB  . LEU B 1 96  ? 42.017  20.210  28.738 1.00 29.94  ? 95  LEU B CB  1 
ATOM   2515 C CG  . LEU B 1 96  ? 42.844  18.948  28.524 1.00 29.69  ? 95  LEU B CG  1 
ATOM   2516 C CD1 . LEU B 1 96  ? 44.332  19.291  28.522 1.00 40.88  ? 95  LEU B CD1 1 
ATOM   2517 C CD2 . LEU B 1 96  ? 42.572  17.870  29.562 1.00 24.58  ? 95  LEU B CD2 1 
ATOM   2518 N N   . VAL B 1 97  ? 39.643  22.349  28.261 1.00 24.64  ? 96  VAL B N   1 
ATOM   2519 C CA  . VAL B 1 97  ? 39.005  23.614  28.608 1.00 30.95  ? 96  VAL B CA  1 
ATOM   2520 C C   . VAL B 1 97  ? 37.501  23.468  28.805 1.00 47.03  ? 96  VAL B C   1 
ATOM   2521 O O   . VAL B 1 97  ? 36.892  24.049  29.709 1.00 39.77  ? 96  VAL B O   1 
ATOM   2522 C CB  . VAL B 1 97  ? 39.270  24.639  27.488 1.00 25.42  ? 96  VAL B CB  1 
ATOM   2523 C CG1 . VAL B 1 97  ? 38.485  25.915  27.709 1.00 30.97  ? 96  VAL B CG1 1 
ATOM   2524 C CG2 . VAL B 1 97  ? 40.772  24.886  27.413 1.00 29.73  ? 96  VAL B CG2 1 
ATOM   2525 N N   . GLY B 1 98  ? 36.920  22.660  27.908 1.00 40.39  ? 97  GLY B N   1 
ATOM   2526 C CA  . GLY B 1 98  ? 35.511  22.311  28.019 1.00 36.89  ? 97  GLY B CA  1 
ATOM   2527 C C   . GLY B 1 98  ? 35.237  21.684  29.382 1.00 31.18  ? 97  GLY B C   1 
ATOM   2528 O O   . GLY B 1 98  ? 34.314  22.094  30.089 1.00 30.35  ? 97  GLY B O   1 
ATOM   2529 N N   . ALA B 1 99  ? 36.054  20.684  29.734 1.00 32.93  ? 98  ALA B N   1 
ATOM   2530 C CA  . ALA B 1 99  ? 35.848  20.019  31.021 1.00 32.60  ? 98  ALA B CA  1 
ATOM   2531 C C   . ALA B 1 99  ? 35.896  21.055  32.146 1.00 40.06  ? 98  ALA B C   1 
ATOM   2532 O O   . ALA B 1 99  ? 35.031  20.983  33.018 1.00 31.85  ? 98  ALA B O   1 
ATOM   2533 C CB  . ALA B 1 99  ? 36.843  18.907  31.241 1.00 19.00  ? 98  ALA B CB  1 
ATOM   2534 N N   . ILE B 1 100 ? 36.838  21.987  32.095 1.00 49.46  ? 99  ILE B N   1 
ATOM   2535 C CA  . ILE B 1 100 ? 36.958  23.049  33.083 1.00 46.16  ? 99  ILE B CA  1 
ATOM   2536 C C   . ILE B 1 100 ? 35.691  23.901  33.149 1.00 43.72  ? 99  ILE B C   1 
ATOM   2537 O O   . ILE B 1 100 ? 35.199  24.212  34.240 1.00 30.47  ? 99  ILE B O   1 
ATOM   2538 C CB  . ILE B 1 100 ? 38.145  23.992  32.814 1.00 45.95  ? 99  ILE B CB  1 
ATOM   2539 C CG1 . ILE B 1 100 ? 39.488  23.325  32.529 1.00 48.30  ? 99  ILE B CG1 1 
ATOM   2540 C CG2 . ILE B 1 100 ? 38.289  24.948  33.990 1.00 34.69  ? 99  ILE B CG2 1 
ATOM   2541 C CD1 . ILE B 1 100 ? 40.674  24.265  32.645 1.00 32.58  ? 99  ILE B CD1 1 
ATOM   2542 N N   . ALA B 1 101 ? 35.151  24.284  31.991 1.00 36.78  ? 100 ALA B N   1 
ATOM   2543 C CA  . ALA B 1 101 ? 33.929  25.092  32.006 1.00 39.59  ? 100 ALA B CA  1 
ATOM   2544 C C   . ALA B 1 101 ? 32.727  24.307  32.520 1.00 40.35  ? 100 ALA B C   1 
ATOM   2545 O O   . ALA B 1 101 ? 31.824  24.850  33.161 1.00 34.11  ? 100 ALA B O   1 
ATOM   2546 C CB  . ALA B 1 101 ? 33.649  25.630  30.610 1.00 34.12  ? 100 ALA B CB  1 
ATOM   2547 N N   . GLY B 1 102 ? 32.729  23.009  32.215 1.00 34.73  ? 101 GLY B N   1 
ATOM   2548 C CA  . GLY B 1 102 ? 31.655  22.148  32.664 1.00 36.49  ? 101 GLY B CA  1 
ATOM   2549 C C   . GLY B 1 102 ? 31.642  22.049  34.181 1.00 31.78  ? 101 GLY B C   1 
ATOM   2550 O O   . GLY B 1 102 ? 30.595  22.258  34.794 1.00 29.32  ? 101 GLY B O   1 
ATOM   2551 N N   . ALA B 1 103 ? 32.783  21.734  34.777 1.00 34.25  ? 102 ALA B N   1 
ATOM   2552 C CA  . ALA B 1 103 ? 32.945  21.720  36.229 1.00 33.12  ? 102 ALA B CA  1 
ATOM   2553 C C   . ALA B 1 103 ? 32.619  23.097  36.808 1.00 27.91  ? 102 ALA B C   1 
ATOM   2554 O O   . ALA B 1 103 ? 32.046  23.165  37.890 1.00 41.62  ? 102 ALA B O   1 
ATOM   2555 C CB  . ALA B 1 103 ? 34.350  21.304  36.635 1.00 21.82  ? 102 ALA B CB  1 
ATOM   2556 N N   . GLY B 1 104 ? 32.980  24.130  36.060 1.00 29.88  ? 103 GLY B N   1 
ATOM   2557 C CA  . GLY B 1 104 ? 32.732  25.525  36.335 1.00 27.24  ? 103 GLY B CA  1 
ATOM   2558 C C   . GLY B 1 104 ? 31.278  25.916  36.418 1.00 34.14  ? 103 GLY B C   1 
ATOM   2559 O O   . GLY B 1 104 ? 30.825  26.488  37.423 1.00 32.37  ? 103 GLY B O   1 
ATOM   2560 N N   . ILE B 1 105 ? 30.497  25.624  35.373 1.00 27.73  ? 104 ILE B N   1 
ATOM   2561 C CA  . ILE B 1 105 ? 29.059  25.883  35.471 1.00 21.65  ? 104 ILE B CA  1 
ATOM   2562 C C   . ILE B 1 105 ? 28.409  25.098  36.609 1.00 25.49  ? 104 ILE B C   1 
ATOM   2563 O O   . ILE B 1 105 ? 27.616  25.657  37.375 1.00 25.57  ? 104 ILE B O   1 
ATOM   2564 C CB  . ILE B 1 105 ? 28.346  25.563  34.147 1.00 20.09  ? 104 ILE B CB  1 
ATOM   2565 C CG1 . ILE B 1 105 ? 28.915  26.320  32.943 1.00 26.71  ? 104 ILE B CG1 1 
ATOM   2566 C CG2 . ILE B 1 105 ? 26.854  25.796  34.315 1.00 29.49  ? 104 ILE B CG2 1 
ATOM   2567 C CD1 . ILE B 1 105 ? 29.405  25.379  31.861 1.00 44.68  ? 104 ILE B CD1 1 
ATOM   2568 N N   . LEU B 1 106 ? 28.724  23.814  36.784 1.00 39.02  ? 105 LEU B N   1 
ATOM   2569 C CA  . LEU B 1 106 ? 28.143  23.023  37.872 1.00 35.18  ? 105 LEU B CA  1 
ATOM   2570 C C   . LEU B 1 106 ? 28.468  23.636  39.236 1.00 25.43  ? 105 LEU B C   1 
ATOM   2571 O O   . LEU B 1 106 ? 27.530  23.833  40.005 1.00 31.57  ? 105 LEU B O   1 
ATOM   2572 C CB  . LEU B 1 106 ? 28.599  21.563  37.852 1.00 33.46  ? 105 LEU B CB  1 
ATOM   2573 C CG  . LEU B 1 106 ? 28.041  20.674  38.972 1.00 37.08  ? 105 LEU B CG  1 
ATOM   2574 C CD1 . LEU B 1 106 ? 26.544  20.476  38.779 1.00 39.39  ? 105 LEU B CD1 1 
ATOM   2575 C CD2 . LEU B 1 106 ? 28.749  19.331  39.055 1.00 15.93  ? 105 LEU B CD2 1 
ATOM   2576 N N   . TYR B 1 107 ? 29.734  23.903  39.490 1.00 32.66  ? 106 TYR B N   1 
ATOM   2577 C CA  . TYR B 1 107 ? 30.201  24.558  40.702 1.00 36.50  ? 106 TYR B CA  1 
ATOM   2578 C C   . TYR B 1 107 ? 29.299  25.733  41.051 1.00 39.88  ? 106 TYR B C   1 
ATOM   2579 O O   . TYR B 1 107 ? 28.861  25.940  42.176 1.00 37.13  ? 106 TYR B O   1 
ATOM   2580 C CB  . TYR B 1 107 ? 31.643  25.069  40.554 1.00 40.81  ? 106 TYR B CB  1 
ATOM   2581 C CG  . TYR B 1 107 ? 32.109  25.879  41.751 1.00 56.56  ? 106 TYR B CG  1 
ATOM   2582 C CD1 . TYR B 1 107 ? 32.574  25.223  42.886 1.00 60.64  ? 106 TYR B CD1 1 
ATOM   2583 C CD2 . TYR B 1 107 ? 32.104  27.268  41.792 1.00 62.40  ? 106 TYR B CD2 1 
ATOM   2584 C CE1 . TYR B 1 107 ? 33.008  25.918  43.999 1.00 67.84  ? 106 TYR B CE1 1 
ATOM   2585 C CE2 . TYR B 1 107 ? 32.528  27.983  42.899 1.00 66.38  ? 106 TYR B CE2 1 
ATOM   2586 C CZ  . TYR B 1 107 ? 32.980  27.297  44.005 1.00 70.49  ? 106 TYR B CZ  1 
ATOM   2587 O OH  . TYR B 1 107 ? 33.409  27.992  45.113 1.00 89.99  ? 106 TYR B OH  1 
ATOM   2588 N N   . GLY B 1 108 ? 29.042  26.558  40.039 1.00 45.38  ? 107 GLY B N   1 
ATOM   2589 C CA  . GLY B 1 108 ? 28.252  27.757  40.278 1.00 53.59  ? 107 GLY B CA  1 
ATOM   2590 C C   . GLY B 1 108 ? 26.770  27.463  40.333 1.00 57.42  ? 107 GLY B C   1 
ATOM   2591 O O   . GLY B 1 108 ? 25.974  28.299  40.759 1.00 42.96  ? 107 GLY B O   1 
ATOM   2592 N N   . VAL B 1 109 ? 26.388  26.261  39.902 1.00 53.89  ? 108 VAL B N   1 
ATOM   2593 C CA  . VAL B 1 109 ? 24.966  25.920  39.930 1.00 36.27  ? 108 VAL B CA  1 
ATOM   2594 C C   . VAL B 1 109 ? 24.627  24.990  41.068 1.00 29.67  ? 108 VAL B C   1 
ATOM   2595 O O   . VAL B 1 109 ? 23.485  24.785  41.497 1.00 43.89  ? 108 VAL B O   1 
ATOM   2596 C CB  . VAL B 1 109 ? 24.578  25.301  38.569 1.00 40.53  ? 108 VAL B CB  1 
ATOM   2597 C CG1 . VAL B 1 109 ? 24.493  23.787  38.646 1.00 31.16  ? 108 VAL B CG1 1 
ATOM   2598 C CG2 . VAL B 1 109 ? 23.268  25.912  38.090 1.00 47.52  ? 108 VAL B CG2 1 
ATOM   2599 N N   . ALA B 1 110 ? 25.609  24.312  41.666 1.00 18.98  ? 109 ALA B N   1 
ATOM   2600 C CA  . ALA B 1 110 ? 25.082  23.318  42.622 1.00 30.21  ? 109 ALA B CA  1 
ATOM   2601 C C   . ALA B 1 110 ? 24.939  23.917  44.013 1.00 48.36  ? 109 ALA B C   1 
ATOM   2602 O O   . ALA B 1 110 ? 25.756  24.753  44.414 1.00 65.41  ? 109 ALA B O   1 
ATOM   2603 C CB  . ALA B 1 110 ? 25.966  22.090  42.624 1.00 24.68  ? 109 ALA B CB  1 
ATOM   2604 N N   . PRO B 1 111 ? 23.913  23.503  44.753 1.00 47.86  ? 110 PRO B N   1 
ATOM   2605 C CA  . PRO B 1 111 ? 23.743  24.029  46.121 1.00 44.86  ? 110 PRO B CA  1 
ATOM   2606 C C   . PRO B 1 111 ? 24.948  23.637  46.972 1.00 47.35  ? 110 PRO B C   1 
ATOM   2607 O O   . PRO B 1 111 ? 25.578  22.593  46.780 1.00 29.01  ? 110 PRO B O   1 
ATOM   2608 C CB  . PRO B 1 111 ? 22.458  23.382  46.623 1.00 36.26  ? 110 PRO B CB  1 
ATOM   2609 C CG  . PRO B 1 111 ? 21.771  22.881  45.399 1.00 48.36  ? 110 PRO B CG  1 
ATOM   2610 C CD  . PRO B 1 111 ? 22.856  22.546  44.405 1.00 42.53  ? 110 PRO B CD  1 
ATOM   2611 N N   . LEU B 1 112 ? 25.288  24.507  47.921 1.00 45.05  ? 111 LEU B N   1 
ATOM   2612 C CA  . LEU B 1 112 ? 26.469  24.256  48.740 1.00 40.62  ? 111 LEU B CA  1 
ATOM   2613 C C   . LEU B 1 112 ? 26.391  22.909  49.436 1.00 37.47  ? 111 LEU B C   1 
ATOM   2614 O O   . LEU B 1 112 ? 27.374  22.198  49.658 1.00 45.87  ? 111 LEU B O   1 
ATOM   2615 C CB  . LEU B 1 112 ? 26.616  25.397  49.752 1.00 45.89  ? 111 LEU B CB  1 
ATOM   2616 C CG  . LEU B 1 112 ? 27.940  26.161  49.603 1.00 49.66  ? 111 LEU B CG  1 
ATOM   2617 C CD1 . LEU B 1 112 ? 27.664  27.622  49.288 1.00 53.68  ? 111 LEU B CD1 1 
ATOM   2618 C CD2 . LEU B 1 112 ? 28.781  25.984  50.858 1.00 57.06  ? 111 LEU B CD2 1 
ATOM   2619 N N   . ASN B 1 113 ? 25.160  22.539  49.798 1.00 38.40  ? 112 ASN B N   1 
ATOM   2620 C CA  . ASN B 1 113 ? 25.009  21.249  50.465 1.00 52.50  ? 112 ASN B CA  1 
ATOM   2621 C C   . ASN B 1 113 ? 25.412  20.110  49.540 1.00 60.95  ? 112 ASN B C   1 
ATOM   2622 O O   . ASN B 1 113 ? 25.812  19.047  50.025 1.00 59.68  ? 112 ASN B O   1 
ATOM   2623 C CB  . ASN B 1 113 ? 23.567  21.099  50.958 1.00 65.77  ? 112 ASN B CB  1 
ATOM   2624 C CG  . ASN B 1 113 ? 23.386  21.928  52.223 1.00 80.52  ? 112 ASN B CG  1 
ATOM   2625 O OD1 . ASN B 1 113 ? 24.317  22.046  53.023 1.00 75.52  ? 112 ASN B OD1 1 
ATOM   2626 N ND2 . ASN B 1 113 ? 22.208  22.490  52.388 1.00 105.61 ? 112 ASN B ND2 1 
ATOM   2627 N N   . ALA B 1 114 ? 25.319  20.347  48.228 1.00 50.22  ? 113 ALA B N   1 
ATOM   2628 C CA  . ALA B 1 114 ? 25.561  19.287  47.258 1.00 40.25  ? 113 ALA B CA  1 
ATOM   2629 C C   . ALA B 1 114 ? 26.990  19.285  46.717 1.00 36.85  ? 113 ALA B C   1 
ATOM   2630 O O   . ALA B 1 114 ? 27.527  18.198  46.488 1.00 39.53  ? 113 ALA B O   1 
ATOM   2631 C CB  . ALA B 1 114 ? 24.568  19.395  46.102 1.00 46.25  ? 113 ALA B CB  1 
ATOM   2632 N N   . ARG B 1 115 ? 27.518  20.475  46.527 1.00 32.89  ? 114 ARG B N   1 
ATOM   2633 C CA  . ARG B 1 115 ? 28.826  20.757  45.965 1.00 43.36  ? 114 ARG B CA  1 
ATOM   2634 C C   . ARG B 1 115 ? 29.872  19.701  46.317 1.00 42.39  ? 114 ARG B C   1 
ATOM   2635 O O   . ARG B 1 115 ? 30.421  19.046  45.421 1.00 32.34  ? 114 ARG B O   1 
ATOM   2636 C CB  . ARG B 1 115 ? 29.311  22.132  46.449 1.00 43.51  ? 114 ARG B CB  1 
ATOM   2637 C CG  . ARG B 1 115 ? 29.652  23.121  45.346 1.00 58.01  ? 114 ARG B CG  1 
ATOM   2638 C CD  . ARG B 1 115 ? 30.552  24.237  45.861 1.00 68.61  ? 114 ARG B CD  1 
ATOM   2639 N NE  . ARG B 1 115 ? 30.034  25.563  45.546 1.00 74.14  ? 114 ARG B NE  1 
ATOM   2640 C CZ  . ARG B 1 115 ? 30.088  26.644  46.315 1.00 72.45  ? 114 ARG B CZ  1 
ATOM   2641 N NH1 . ARG B 1 115 ? 30.664  26.575  47.512 1.00 61.77  ? 114 ARG B NH1 1 
ATOM   2642 N NH2 . ARG B 1 115 ? 29.568  27.790  45.888 1.00 56.25  ? 114 ARG B NH2 1 
ATOM   2643 N N   . GLY B 1 116 ? 30.129  19.549  47.617 1.00 24.76  ? 115 GLY B N   1 
ATOM   2644 C CA  . GLY B 1 116 ? 31.135  18.609  48.097 1.00 18.73  ? 115 GLY B CA  1 
ATOM   2645 C C   . GLY B 1 116 ? 32.438  18.832  47.343 1.00 31.10  ? 115 GLY B C   1 
ATOM   2646 O O   . GLY B 1 116 ? 32.753  19.988  47.036 1.00 53.01  ? 115 GLY B O   1 
ATOM   2647 N N   . ASN B 1 117 ? 33.174  17.777  47.006 1.00 36.71  ? 116 ASN B N   1 
ATOM   2648 C CA  . ASN B 1 117 ? 34.425  17.992  46.263 1.00 43.08  ? 116 ASN B CA  1 
ATOM   2649 C C   . ASN B 1 117 ? 34.197  17.938  44.753 1.00 36.55  ? 116 ASN B C   1 
ATOM   2650 O O   . ASN B 1 117 ? 35.107  17.704  43.964 1.00 27.63  ? 116 ASN B O   1 
ATOM   2651 C CB  . ASN B 1 117 ? 35.483  16.996  46.729 1.00 52.15  ? 116 ASN B CB  1 
ATOM   2652 C CG  . ASN B 1 117 ? 36.196  17.486  47.982 1.00 68.24  ? 116 ASN B CG  1 
ATOM   2653 O OD1 . ASN B 1 117 ? 35.804  18.456  48.636 1.00 81.22  ? 116 ASN B OD1 1 
ATOM   2654 N ND2 . ASN B 1 117 ? 37.284  16.808  48.334 1.00 91.70  ? 116 ASN B ND2 1 
ATOM   2655 N N   . LEU B 1 118 ? 32.951  18.201  44.380 1.00 36.11  ? 117 LEU B N   1 
ATOM   2656 C CA  . LEU B 1 118 ? 32.494  18.348  43.014 1.00 36.04  ? 117 LEU B CA  1 
ATOM   2657 C C   . LEU B 1 118 ? 32.853  17.140  42.143 1.00 43.36  ? 117 LEU B C   1 
ATOM   2658 O O   . LEU B 1 118 ? 33.285  17.271  40.995 1.00 44.55  ? 117 LEU B O   1 
ATOM   2659 C CB  . LEU B 1 118 ? 33.066  19.622  42.383 1.00 35.85  ? 117 LEU B CB  1 
ATOM   2660 C CG  . LEU B 1 118 ? 32.413  20.004  41.048 1.00 42.08  ? 117 LEU B CG  1 
ATOM   2661 C CD1 . LEU B 1 118 ? 31.579  21.264  41.214 1.00 39.92  ? 117 LEU B CD1 1 
ATOM   2662 C CD2 . LEU B 1 118 ? 33.475  20.162  39.972 1.00 56.66  ? 117 LEU B CD2 1 
ATOM   2663 N N   . ALA B 1 119 ? 32.645  15.973  42.729 1.00 37.42  ? 118 ALA B N   1 
ATOM   2664 C CA  . ALA B 1 119 ? 32.804  14.678  42.110 1.00 39.14  ? 118 ALA B CA  1 
ATOM   2665 C C   . ALA B 1 119 ? 34.173  14.487  41.476 1.00 38.45  ? 118 ALA B C   1 
ATOM   2666 O O   . ALA B 1 119 ? 34.285  13.976  40.360 1.00 44.13  ? 118 ALA B O   1 
ATOM   2667 C CB  . ALA B 1 119 ? 31.707  14.438  41.066 1.00 42.89  ? 118 ALA B CB  1 
ATOM   2668 N N   . VAL B 1 120 ? 35.240  14.857  42.179 1.00 31.25  ? 119 VAL B N   1 
ATOM   2669 C CA  . VAL B 1 120 ? 36.560  14.532  41.629 1.00 22.25  ? 119 VAL B CA  1 
ATOM   2670 C C   . VAL B 1 120 ? 36.823  13.037  41.723 1.00 29.50  ? 119 VAL B C   1 
ATOM   2671 O O   . VAL B 1 120 ? 36.303  12.308  42.575 1.00 27.01  ? 119 VAL B O   1 
ATOM   2672 C CB  . VAL B 1 120 ? 37.663  15.305  42.368 1.00 34.03  ? 119 VAL B CB  1 
ATOM   2673 C CG1 . VAL B 1 120 ? 37.799  16.718  41.817 1.00 30.27  ? 119 VAL B CG1 1 
ATOM   2674 C CG2 . VAL B 1 120 ? 37.355  15.317  43.861 1.00 44.99  ? 119 VAL B CG2 1 
ATOM   2675 N N   . ASN B 1 121 ? 37.668  12.558  40.807 1.00 21.99  ? 120 ASN B N   1 
ATOM   2676 C CA  . ASN B 1 121 ? 38.030  11.146  40.906 1.00 36.13  ? 120 ASN B CA  1 
ATOM   2677 C C   . ASN B 1 121 ? 38.843  10.965  42.182 1.00 50.82  ? 120 ASN B C   1 
ATOM   2678 O O   . ASN B 1 121 ? 39.255  11.946  42.804 1.00 38.86  ? 120 ASN B O   1 
ATOM   2679 C CB  . ASN B 1 121 ? 38.792  10.642  39.676 1.00 25.20  ? 120 ASN B CB  1 
ATOM   2680 C CG  . ASN B 1 121 ? 37.863  10.544  38.480 1.00 33.17  ? 120 ASN B CG  1 
ATOM   2681 O OD1 . ASN B 1 121 ? 36.937  9.730   38.482 1.00 48.29  ? 120 ASN B OD1 1 
ATOM   2682 N ND2 . ASN B 1 121 ? 38.108  11.387  37.477 1.00 47.39  ? 120 ASN B ND2 1 
ATOM   2683 N N   . ALA B 1 122 ? 39.050  9.707   42.561 1.00 51.19  ? 121 ALA B N   1 
ATOM   2684 C CA  . ALA B 1 122 ? 39.608  9.454   43.880 1.00 54.80  ? 121 ALA B CA  1 
ATOM   2685 C C   . ALA B 1 122 ? 39.746  7.958   44.151 1.00 57.63  ? 121 ALA B C   1 
ATOM   2686 O O   . ALA B 1 122 ? 38.762  7.269   44.440 1.00 39.87  ? 121 ALA B O   1 
ATOM   2687 C CB  . ALA B 1 122 ? 38.735  10.100  44.947 1.00 29.67  ? 121 ALA B CB  1 
ATOM   2688 N N   . LEU B 1 123 ? 41.000  7.525   44.046 1.00 55.91  ? 122 LEU B N   1 
ATOM   2689 C CA  . LEU B 1 123 ? 41.336  6.145   44.331 1.00 63.94  ? 122 LEU B CA  1 
ATOM   2690 C C   . LEU B 1 123 ? 40.914  5.779   45.758 1.00 57.61  ? 122 LEU B C   1 
ATOM   2691 O O   . LEU B 1 123 ? 41.106  6.511   46.726 1.00 43.40  ? 122 LEU B O   1 
ATOM   2692 C CB  . LEU B 1 123 ? 42.828  5.865   44.142 1.00 77.59  ? 122 LEU B CB  1 
ATOM   2693 C CG  . LEU B 1 123 ? 43.319  4.564   44.793 1.00 96.45  ? 122 LEU B CG  1 
ATOM   2694 C CD1 . LEU B 1 123 ? 44.191  3.776   43.831 1.00 106.88 ? 122 LEU B CD1 1 
ATOM   2695 C CD2 . LEU B 1 123 ? 44.061  4.844   46.092 1.00 118.75 ? 122 LEU B CD2 1 
ATOM   2696 N N   . ASN B 1 124 ? 40.324  4.594   45.808 1.00 49.39  ? 123 ASN B N   1 
ATOM   2697 C CA  . ASN B 1 124 ? 39.910  3.968   47.049 1.00 44.61  ? 123 ASN B CA  1 
ATOM   2698 C C   . ASN B 1 124 ? 41.157  3.661   47.872 1.00 47.55  ? 123 ASN B C   1 
ATOM   2699 O O   . ASN B 1 124 ? 42.174  3.206   47.353 1.00 39.41  ? 123 ASN B O   1 
ATOM   2700 C CB  . ASN B 1 124 ? 39.089  2.720   46.761 1.00 48.24  ? 123 ASN B CB  1 
ATOM   2701 C CG  . ASN B 1 124 ? 39.497  1.497   47.547 1.00 59.67  ? 123 ASN B CG  1 
ATOM   2702 O OD1 . ASN B 1 124 ? 40.543  0.908   47.272 1.00 82.94  ? 123 ASN B OD1 1 
ATOM   2703 N ND2 . ASN B 1 124 ? 38.672  1.114   48.519 1.00 37.35  ? 123 ASN B ND2 1 
ATOM   2704 N N   . ASN B 1 125 ? 41.045  3.945   49.163 1.00 46.83  ? 124 ASN B N   1 
ATOM   2705 C CA  . ASN B 1 125 ? 42.148  3.749   50.087 1.00 49.29  ? 124 ASN B CA  1 
ATOM   2706 C C   . ASN B 1 125 ? 42.673  2.320   50.059 1.00 60.29  ? 124 ASN B C   1 
ATOM   2707 O O   . ASN B 1 125 ? 43.852  2.084   50.336 1.00 76.39  ? 124 ASN B O   1 
ATOM   2708 C CB  . ASN B 1 125 ? 41.661  4.108   51.492 1.00 55.26  ? 124 ASN B CB  1 
ATOM   2709 C CG  . ASN B 1 125 ? 41.129  5.530   51.521 1.00 65.32  ? 124 ASN B CG  1 
ATOM   2710 O OD1 . ASN B 1 125 ? 40.458  5.938   52.472 1.00 88.13  ? 124 ASN B OD1 1 
ATOM   2711 N ND2 . ASN B 1 125 ? 41.437  6.272   50.467 1.00 68.19  ? 124 ASN B ND2 1 
ATOM   2712 N N   . ASN B 1 126 ? 41.784  1.394   49.730 1.00 68.82  ? 125 ASN B N   1 
ATOM   2713 C CA  . ASN B 1 126 ? 42.010  -0.037  49.675 1.00 72.22  ? 125 ASN B CA  1 
ATOM   2714 C C   . ASN B 1 126 ? 42.800  -0.455  48.443 1.00 69.48  ? 125 ASN B C   1 
ATOM   2715 O O   . ASN B 1 126 ? 43.139  -1.632  48.297 1.00 48.33  ? 125 ASN B O   1 
ATOM   2716 C CB  . ASN B 1 126 ? 40.684  -0.811  49.669 1.00 79.79  ? 125 ASN B CB  1 
ATOM   2717 C CG  . ASN B 1 126 ? 40.161  -1.078  51.065 1.00 86.51  ? 125 ASN B CG  1 
ATOM   2718 O OD1 . ASN B 1 126 ? 39.317  -0.332  51.574 1.00 98.95  ? 125 ASN B OD1 1 
ATOM   2719 N ND2 . ASN B 1 126 ? 40.669  -2.139  51.685 1.00 90.11  ? 125 ASN B ND2 1 
ATOM   2720 N N   . THR B 1 127 ? 43.084  0.502   47.551 1.00 72.83  ? 126 THR B N   1 
ATOM   2721 C CA  . THR B 1 127 ? 43.724  0.081   46.309 1.00 64.33  ? 126 THR B CA  1 
ATOM   2722 C C   . THR B 1 127 ? 45.002  0.795   45.924 1.00 48.82  ? 126 THR B C   1 
ATOM   2723 O O   . THR B 1 127 ? 45.217  2.001   45.978 1.00 44.88  ? 126 THR B O   1 
ATOM   2724 C CB  . THR B 1 127 ? 42.733  0.221   45.127 1.00 63.65  ? 126 THR B CB  1 
ATOM   2725 O OG1 . THR B 1 127 ? 42.093  -1.050  44.947 1.00 87.21  ? 126 THR B OG1 1 
ATOM   2726 C CG2 . THR B 1 127 ? 43.488  0.555   43.858 1.00 64.01  ? 126 THR B CG2 1 
ATOM   2727 N N   . THR B 1 128 ? 45.943  -0.042  45.477 1.00 41.67  ? 127 THR B N   1 
ATOM   2728 C CA  . THR B 1 128 ? 47.218  0.542   45.069 1.00 55.31  ? 127 THR B CA  1 
ATOM   2729 C C   . THR B 1 128 ? 47.014  1.388   43.817 1.00 58.42  ? 127 THR B C   1 
ATOM   2730 O O   . THR B 1 128 ? 46.091  1.164   43.032 1.00 58.77  ? 127 THR B O   1 
ATOM   2731 C CB  . THR B 1 128 ? 48.279  -0.547  44.841 1.00 65.10  ? 127 THR B CB  1 
ATOM   2732 O OG1 . THR B 1 128 ? 48.279  -0.998  43.486 1.00 48.45  ? 127 THR B OG1 1 
ATOM   2733 C CG2 . THR B 1 128 ? 47.954  -1.772  45.692 1.00 97.33  ? 127 THR B CG2 1 
ATOM   2734 N N   . GLN B 1 129 ? 47.894  2.374   43.657 1.00 50.61  ? 128 GLN B N   1 
ATOM   2735 C CA  . GLN B 1 129 ? 47.870  3.171   42.434 1.00 49.61  ? 128 GLN B CA  1 
ATOM   2736 C C   . GLN B 1 129 ? 47.964  2.216   41.242 1.00 51.67  ? 128 GLN B C   1 
ATOM   2737 O O   . GLN B 1 129 ? 46.990  2.118   40.488 1.00 48.37  ? 128 GLN B O   1 
ATOM   2738 C CB  . GLN B 1 129 ? 48.990  4.202   42.458 1.00 45.38  ? 128 GLN B CB  1 
ATOM   2739 C CG  . GLN B 1 129 ? 48.835  5.209   43.588 1.00 45.27  ? 128 GLN B CG  1 
ATOM   2740 C CD  . GLN B 1 129 ? 49.789  6.379   43.451 1.00 53.33  ? 128 GLN B CD  1 
ATOM   2741 O OE1 . GLN B 1 129 ? 49.481  7.516   43.813 1.00 58.17  ? 128 GLN B OE1 1 
ATOM   2742 N NE2 . GLN B 1 129 ? 50.966  6.066   42.909 1.00 58.53  ? 128 GLN B NE2 1 
ATOM   2743 N N   . GLY B 1 130 ? 49.102  1.542   41.156 1.00 40.85  ? 129 GLY B N   1 
ATOM   2744 C CA  . GLY B 1 130 ? 49.346  0.447   40.244 1.00 46.08  ? 129 GLY B CA  1 
ATOM   2745 C C   . GLY B 1 130 ? 48.103  -0.400  40.042 1.00 49.14  ? 129 GLY B C   1 
ATOM   2746 O O   . GLY B 1 130 ? 47.718  -0.732  38.921 1.00 64.43  ? 129 GLY B O   1 
ATOM   2747 N N   . GLN B 1 131 ? 47.439  -0.732  41.146 1.00 49.52  ? 130 GLN B N   1 
ATOM   2748 C CA  . GLN B 1 131 ? 46.127  -1.365  41.072 1.00 47.80  ? 130 GLN B CA  1 
ATOM   2749 C C   . GLN B 1 131 ? 45.183  -0.500  40.235 1.00 42.45  ? 130 GLN B C   1 
ATOM   2750 O O   . GLN B 1 131 ? 44.726  -0.952  39.188 1.00 42.67  ? 130 GLN B O   1 
ATOM   2751 C CB  . GLN B 1 131 ? 45.550  -1.599  42.467 1.00 48.95  ? 130 GLN B CB  1 
ATOM   2752 C CG  . GLN B 1 131 ? 46.169  -2.809  43.161 1.00 56.96  ? 130 GLN B CG  1 
ATOM   2753 C CD  . GLN B 1 131 ? 45.338  -3.306  44.320 1.00 61.34  ? 130 GLN B CD  1 
ATOM   2754 O OE1 . GLN B 1 131 ? 45.408  -4.467  44.725 1.00 78.63  ? 130 GLN B OE1 1 
ATOM   2755 N NE2 . GLN B 1 131 ? 44.530  -2.408  44.864 1.00 68.57  ? 130 GLN B NE2 1 
ATOM   2756 N N   . ALA B 1 132 ? 44.933  0.715   40.704 1.00 29.56  ? 131 ALA B N   1 
ATOM   2757 C CA  . ALA B 1 132 ? 44.168  1.693   39.960 1.00 29.23  ? 131 ALA B CA  1 
ATOM   2758 C C   . ALA B 1 132 ? 44.604  1.757   38.497 1.00 48.93  ? 131 ALA B C   1 
ATOM   2759 O O   . ALA B 1 132 ? 43.793  1.610   37.574 1.00 45.15  ? 131 ALA B O   1 
ATOM   2760 C CB  . ALA B 1 132 ? 44.317  3.049   40.616 1.00 22.26  ? 131 ALA B CB  1 
ATOM   2761 N N   . MET B 1 133 ? 45.892  1.981   38.251 1.00 56.38  ? 132 MET B N   1 
ATOM   2762 C CA  . MET B 1 133 ? 46.420  2.102   36.896 1.00 49.48  ? 132 MET B CA  1 
ATOM   2763 C C   . MET B 1 133 ? 45.999  0.969   35.978 1.00 46.00  ? 132 MET B C   1 
ATOM   2764 O O   . MET B 1 133 ? 45.603  1.178   34.827 1.00 44.55  ? 132 MET B O   1 
ATOM   2765 C CB  . MET B 1 133 ? 47.951  2.154   36.942 1.00 59.75  ? 132 MET B CB  1 
ATOM   2766 C CG  . MET B 1 133 ? 48.584  1.748   35.615 1.00 64.49  ? 132 MET B CG  1 
ATOM   2767 S SD  . MET B 1 133 ? 48.905  3.192   34.578 1.00 69.56  ? 132 MET B SD  1 
ATOM   2768 C CE  . MET B 1 133 ? 49.993  2.465   33.340 1.00 146.90 ? 132 MET B CE  1 
ATOM   2769 N N   . VAL B 1 134 ? 46.062  -0.275  36.453 1.00 45.88  ? 133 VAL B N   1 
ATOM   2770 C CA  . VAL B 1 134 ? 45.651  -1.386  35.598 1.00 43.94  ? 133 VAL B CA  1 
ATOM   2771 C C   . VAL B 1 134 ? 44.160  -1.495  35.327 1.00 41.24  ? 133 VAL B C   1 
ATOM   2772 O O   . VAL B 1 134 ? 43.797  -2.015  34.261 1.00 40.33  ? 133 VAL B O   1 
ATOM   2773 C CB  . VAL B 1 134 ? 46.092  -2.726  36.227 1.00 49.02  ? 133 VAL B CB  1 
ATOM   2774 C CG1 . VAL B 1 134 ? 45.689  -3.873  35.314 1.00 36.78  ? 133 VAL B CG1 1 
ATOM   2775 C CG2 . VAL B 1 134 ? 47.587  -2.678  36.486 1.00 51.85  ? 133 VAL B CG2 1 
ATOM   2776 N N   . VAL B 1 135 ? 43.272  -1.052  36.218 1.00 41.46  ? 134 VAL B N   1 
ATOM   2777 C CA  . VAL B 1 135 ? 41.849  -1.143  35.895 1.00 48.48  ? 134 VAL B CA  1 
ATOM   2778 C C   . VAL B 1 135 ? 41.427  -0.012  34.947 1.00 36.10  ? 134 VAL B C   1 
ATOM   2779 O O   . VAL B 1 135 ? 40.560  -0.270  34.117 1.00 32.12  ? 134 VAL B O   1 
ATOM   2780 C CB  . VAL B 1 135 ? 40.881  -1.109  37.098 1.00 50.50  ? 134 VAL B CB  1 
ATOM   2781 C CG1 . VAL B 1 135 ? 41.255  -2.161  38.135 1.00 27.30  ? 134 VAL B CG1 1 
ATOM   2782 C CG2 . VAL B 1 135 ? 40.844  0.287   37.697 1.00 50.37  ? 134 VAL B CG2 1 
ATOM   2783 N N   . GLU B 1 136 ? 42.000  1.175   35.075 1.00 38.83  ? 135 GLU B N   1 
ATOM   2784 C CA  . GLU B 1 136 ? 41.695  2.281   34.171 1.00 38.73  ? 135 GLU B CA  1 
ATOM   2785 C C   . GLU B 1 136 ? 42.282  2.000   32.788 1.00 36.72  ? 135 GLU B C   1 
ATOM   2786 O O   . GLU B 1 136 ? 41.742  2.498   31.801 1.00 38.99  ? 135 GLU B O   1 
ATOM   2787 C CB  . GLU B 1 136 ? 42.218  3.621   34.681 1.00 36.74  ? 135 GLU B CB  1 
ATOM   2788 C CG  . GLU B 1 136 ? 41.532  4.140   35.930 1.00 40.74  ? 135 GLU B CG  1 
ATOM   2789 C CD  . GLU B 1 136 ? 40.276  4.942   35.664 1.00 47.83  ? 135 GLU B CD  1 
ATOM   2790 O OE1 . GLU B 1 136 ? 40.148  5.468   34.536 1.00 47.38  ? 135 GLU B OE1 1 
ATOM   2791 O OE2 . GLU B 1 136 ? 39.420  5.034   36.576 1.00 35.62  ? 135 GLU B OE2 1 
ATOM   2792 N N   . LEU B 1 137 ? 43.347  1.206   32.771 1.00 30.88  ? 136 LEU B N   1 
ATOM   2793 C CA  . LEU B 1 137 ? 43.892  0.644   31.548 1.00 31.62  ? 136 LEU B CA  1 
ATOM   2794 C C   . LEU B 1 137 ? 42.847  -0.244  30.877 1.00 41.59  ? 136 LEU B C   1 
ATOM   2795 O O   . LEU B 1 137 ? 42.594  -0.145  29.674 1.00 38.67  ? 136 LEU B O   1 
ATOM   2796 C CB  . LEU B 1 137 ? 45.158  -0.171  31.811 1.00 32.55  ? 136 LEU B CB  1 
ATOM   2797 C CG  . LEU B 1 137 ? 46.154  -0.384  30.669 1.00 36.53  ? 136 LEU B CG  1 
ATOM   2798 C CD1 . LEU B 1 137 ? 47.501  -0.852  31.219 1.00 42.54  ? 136 LEU B CD1 1 
ATOM   2799 C CD2 . LEU B 1 137 ? 45.677  -1.382  29.620 1.00 26.95  ? 136 LEU B CD2 1 
ATOM   2800 N N   . ILE B 1 138 ? 42.242  -1.146  31.651 1.00 40.10  ? 137 ILE B N   1 
ATOM   2801 C CA  . ILE B 1 138 ? 41.296  -2.097  31.082 1.00 35.03  ? 137 ILE B CA  1 
ATOM   2802 C C   . ILE B 1 138 ? 40.035  -1.373  30.610 1.00 35.65  ? 137 ILE B C   1 
ATOM   2803 O O   . ILE B 1 138 ? 39.530  -1.571  29.509 1.00 41.25  ? 137 ILE B O   1 
ATOM   2804 C CB  . ILE B 1 138 ? 40.876  -3.162  32.103 1.00 34.17  ? 137 ILE B CB  1 
ATOM   2805 C CG1 . ILE B 1 138 ? 41.781  -4.391  32.209 1.00 53.23  ? 137 ILE B CG1 1 
ATOM   2806 C CG2 . ILE B 1 138 ? 39.458  -3.635  31.817 1.00 36.36  ? 137 ILE B CG2 1 
ATOM   2807 C CD1 . ILE B 1 138 ? 41.047  -5.665  31.819 1.00 72.24  ? 137 ILE B CD1 1 
ATOM   2808 N N   . LEU B 1 139 ? 39.569  -0.541  31.536 1.00 25.39  ? 138 LEU B N   1 
ATOM   2809 C CA  . LEU B 1 139 ? 38.348  0.216   31.383 1.00 30.37  ? 138 LEU B CA  1 
ATOM   2810 C C   . LEU B 1 139 ? 38.332  1.062   30.113 1.00 37.68  ? 138 LEU B C   1 
ATOM   2811 O O   . LEU B 1 139 ? 37.267  1.275   29.514 1.00 34.46  ? 138 LEU B O   1 
ATOM   2812 C CB  . LEU B 1 139 ? 38.155  1.136   32.594 1.00 30.53  ? 138 LEU B CB  1 
ATOM   2813 C CG  . LEU B 1 139 ? 37.428  0.498   33.784 1.00 38.55  ? 138 LEU B CG  1 
ATOM   2814 C CD1 . LEU B 1 139 ? 37.772  -0.977  33.896 1.00 45.15  ? 138 LEU B CD1 1 
ATOM   2815 C CD2 . LEU B 1 139 ? 37.768  1.255   35.044 1.00 24.70  ? 138 LEU B CD2 1 
ATOM   2816 N N   . THR B 1 140 ? 39.497  1.573   29.707 1.00 21.97  ? 139 THR B N   1 
ATOM   2817 C CA  . THR B 1 140 ? 39.456  2.474   28.545 1.00 29.75  ? 139 THR B CA  1 
ATOM   2818 C C   . THR B 1 140 ? 39.853  1.705   27.289 1.00 22.30  ? 139 THR B C   1 
ATOM   2819 O O   . THR B 1 140 ? 39.603  2.149   26.174 1.00 30.30  ? 139 THR B O   1 
ATOM   2820 C CB  . THR B 1 140 ? 40.331  3.717   28.755 1.00 45.61  ? 139 THR B CB  1 
ATOM   2821 O OG1 . THR B 1 140 ? 40.296  4.115   30.133 1.00 34.51  ? 139 THR B OG1 1 
ATOM   2822 C CG2 . THR B 1 140 ? 39.767  4.878   27.947 1.00 50.74  ? 139 THR B CG2 1 
ATOM   2823 N N   . PHE B 1 141 ? 40.422  0.532   27.513 1.00 25.23  ? 140 PHE B N   1 
ATOM   2824 C CA  . PHE B 1 141 ? 40.752  -0.427  26.471 1.00 28.61  ? 140 PHE B CA  1 
ATOM   2825 C C   . PHE B 1 141 ? 39.488  -0.928  25.782 1.00 32.51  ? 140 PHE B C   1 
ATOM   2826 O O   . PHE B 1 141 ? 39.381  -0.858  24.554 1.00 34.81  ? 140 PHE B O   1 
ATOM   2827 C CB  . PHE B 1 141 ? 41.531  -1.622  27.028 1.00 24.81  ? 140 PHE B CB  1 
ATOM   2828 C CG  . PHE B 1 141 ? 41.978  -2.617  25.963 1.00 25.39  ? 140 PHE B CG  1 
ATOM   2829 C CD1 . PHE B 1 141 ? 43.036  -2.326  25.124 1.00 27.36  ? 140 PHE B CD1 1 
ATOM   2830 C CD2 . PHE B 1 141 ? 41.340  -3.834  25.815 1.00 25.90  ? 140 PHE B CD2 1 
ATOM   2831 C CE1 . PHE B 1 141 ? 43.446  -3.225  24.164 1.00 31.14  ? 140 PHE B CE1 1 
ATOM   2832 C CE2 . PHE B 1 141 ? 41.743  -4.739  24.850 1.00 27.86  ? 140 PHE B CE2 1 
ATOM   2833 C CZ  . PHE B 1 141 ? 42.801  -4.438  24.015 1.00 27.08  ? 140 PHE B CZ  1 
ATOM   2834 N N   . GLN B 1 142 ? 38.545  -1.428  26.586 1.00 28.64  ? 141 GLN B N   1 
ATOM   2835 C CA  . GLN B 1 142 ? 37.290  -1.892  25.989 1.00 28.17  ? 141 GLN B CA  1 
ATOM   2836 C C   . GLN B 1 142 ? 36.490  -0.735  25.405 1.00 18.94  ? 141 GLN B C   1 
ATOM   2837 O O   . GLN B 1 142 ? 35.780  -0.890  24.423 1.00 24.62  ? 141 GLN B O   1 
ATOM   2838 C CB  . GLN B 1 142 ? 36.443  -2.662  27.004 1.00 39.88  ? 141 GLN B CB  1 
ATOM   2839 C CG  . GLN B 1 142 ? 35.940  -1.925  28.232 1.00 23.56  ? 141 GLN B CG  1 
ATOM   2840 C CD  . GLN B 1 142 ? 34.581  -1.279  28.008 1.00 25.52  ? 141 GLN B CD  1 
ATOM   2841 O OE1 . GLN B 1 142 ? 33.796  -1.721  27.168 1.00 29.86  ? 141 GLN B OE1 1 
ATOM   2842 N NE2 . GLN B 1 142 ? 34.318  -0.191  28.713 1.00 29.18  ? 141 GLN B NE2 1 
ATOM   2843 N N   . LEU B 1 143 ? 36.528  0.446   26.033 1.00 17.46  ? 142 LEU B N   1 
ATOM   2844 C CA  . LEU B 1 143 ? 35.846  1.576   25.388 1.00 21.37  ? 142 LEU B CA  1 
ATOM   2845 C C   . LEU B 1 143 ? 36.464  1.864   24.020 1.00 28.93  ? 142 LEU B C   1 
ATOM   2846 O O   . LEU B 1 143 ? 35.787  1.938   22.995 1.00 25.43  ? 142 LEU B O   1 
ATOM   2847 C CB  . LEU B 1 143 ? 35.909  2.794   26.294 1.00 21.09  ? 142 LEU B CB  1 
ATOM   2848 C CG  . LEU B 1 143 ? 35.506  4.157   25.743 1.00 22.61  ? 142 LEU B CG  1 
ATOM   2849 C CD1 . LEU B 1 143 ? 34.058  4.177   25.281 1.00 25.95  ? 142 LEU B CD1 1 
ATOM   2850 C CD2 . LEU B 1 143 ? 35.717  5.243   26.791 1.00 24.08  ? 142 LEU B CD2 1 
ATOM   2851 N N   . ALA B 1 144 ? 37.785  2.028   23.966 1.00 28.59  ? 143 ALA B N   1 
ATOM   2852 C CA  . ALA B 1 144 ? 38.486  2.271   22.720 1.00 19.42  ? 143 ALA B CA  1 
ATOM   2853 C C   . ALA B 1 144 ? 38.143  1.241   21.655 1.00 22.10  ? 143 ALA B C   1 
ATOM   2854 O O   . ALA B 1 144 ? 37.707  1.608   20.559 1.00 37.39  ? 143 ALA B O   1 
ATOM   2855 C CB  . ALA B 1 144 ? 39.989  2.299   22.944 1.00 23.82  ? 143 ALA B CB  1 
ATOM   2856 N N   . LEU B 1 145 ? 38.320  -0.033  21.962 1.00 23.74  ? 144 LEU B N   1 
ATOM   2857 C CA  . LEU B 1 145 ? 37.975  -1.098  21.025 1.00 28.05  ? 144 LEU B CA  1 
ATOM   2858 C C   . LEU B 1 145 ? 36.555  -0.944  20.488 1.00 27.83  ? 144 LEU B C   1 
ATOM   2859 O O   . LEU B 1 145 ? 36.294  -1.007  19.283 1.00 41.41  ? 144 LEU B O   1 
ATOM   2860 C CB  . LEU B 1 145 ? 38.144  -2.467  21.702 1.00 37.87  ? 144 LEU B CB  1 
ATOM   2861 C CG  . LEU B 1 145 ? 39.430  -3.238  21.409 1.00 41.40  ? 144 LEU B CG  1 
ATOM   2862 C CD1 . LEU B 1 145 ? 39.363  -4.673  21.922 1.00 31.57  ? 144 LEU B CD1 1 
ATOM   2863 C CD2 . LEU B 1 145 ? 39.734  -3.242  19.918 1.00 32.13  ? 144 LEU B CD2 1 
ATOM   2864 N N   . CYS B 1 146 ? 35.585  -0.738  21.377 1.00 23.68  ? 145 CYS B N   1 
ATOM   2865 C CA  . CYS B 1 146 ? 34.197  -0.648  20.947 1.00 23.56  ? 145 CYS B CA  1 
ATOM   2866 C C   . CYS B 1 146 ? 33.982  0.520   19.986 1.00 26.72  ? 145 CYS B C   1 
ATOM   2867 O O   . CYS B 1 146 ? 33.194  0.459   19.035 1.00 21.07  ? 145 CYS B O   1 
ATOM   2868 C CB  . CYS B 1 146 ? 33.311  -0.532  22.199 1.00 16.23  ? 145 CYS B CB  1 
ATOM   2869 S SG  . CYS B 1 146 ? 31.568  -0.229  21.840 1.00 27.47  ? 145 CYS B SG  1 
ATOM   2870 N N   . ILE B 1 147 ? 34.676  1.625   20.234 1.00 23.95  ? 146 ILE B N   1 
ATOM   2871 C CA  . ILE B 1 147 ? 34.551  2.848   19.457 1.00 24.24  ? 146 ILE B CA  1 
ATOM   2872 C C   . ILE B 1 147 ? 35.071  2.683   18.033 1.00 33.81  ? 146 ILE B C   1 
ATOM   2873 O O   . ILE B 1 147 ? 34.366  2.958   17.055 1.00 29.22  ? 146 ILE B O   1 
ATOM   2874 C CB  . ILE B 1 147 ? 35.319  3.986   20.155 1.00 27.64  ? 146 ILE B CB  1 
ATOM   2875 C CG1 . ILE B 1 147 ? 34.710  4.422   21.495 1.00 25.33  ? 146 ILE B CG1 1 
ATOM   2876 C CG2 . ILE B 1 147 ? 35.482  5.177   19.234 1.00 27.85  ? 146 ILE B CG2 1 
ATOM   2877 C CD1 . ILE B 1 147 ? 35.299  5.694   22.061 1.00 21.30  ? 146 ILE B CD1 1 
ATOM   2878 N N   . PHE B 1 148 ? 36.312  2.222   17.937 1.00 34.44  ? 147 PHE B N   1 
ATOM   2879 C CA  . PHE B 1 148 ? 36.949  1.942   16.651 1.00 33.38  ? 147 PHE B CA  1 
ATOM   2880 C C   . PHE B 1 148 ? 36.115  0.952   15.851 1.00 27.11  ? 147 PHE B C   1 
ATOM   2881 O O   . PHE B 1 148 ? 35.749  1.163   14.702 1.00 27.25  ? 147 PHE B O   1 
ATOM   2882 C CB  . PHE B 1 148 ? 38.351  1.373   16.849 1.00 27.95  ? 147 PHE B CB  1 
ATOM   2883 C CG  . PHE B 1 148 ? 39.240  2.214   17.739 1.00 25.87  ? 147 PHE B CG  1 
ATOM   2884 C CD1 . PHE B 1 148 ? 39.031  3.585   17.813 1.00 36.78  ? 147 PHE B CD1 1 
ATOM   2885 C CD2 . PHE B 1 148 ? 40.258  1.641   18.477 1.00 28.64  ? 147 PHE B CD2 1 
ATOM   2886 C CE1 . PHE B 1 148 ? 39.838  4.370   18.615 1.00 30.40  ? 147 PHE B CE1 1 
ATOM   2887 C CE2 . PHE B 1 148 ? 41.070  2.428   19.280 1.00 31.10  ? 147 PHE B CE2 1 
ATOM   2888 C CZ  . PHE B 1 148 ? 40.858  3.795   19.350 1.00 29.75  ? 147 PHE B CZ  1 
ATOM   2889 N N   . ALA B 1 149 ? 35.787  -0.167  16.481 1.00 29.15  ? 148 ALA B N   1 
ATOM   2890 C CA  . ALA B 1 149 ? 34.939  -1.153  15.830 1.00 31.49  ? 148 ALA B CA  1 
ATOM   2891 C C   . ALA B 1 149 ? 33.609  -0.546  15.398 1.00 36.92  ? 148 ALA B C   1 
ATOM   2892 O O   . ALA B 1 149 ? 33.065  -0.888  14.337 1.00 26.97  ? 148 ALA B O   1 
ATOM   2893 C CB  . ALA B 1 149 ? 34.717  -2.342  16.761 1.00 25.43  ? 148 ALA B CB  1 
ATOM   2894 N N   . SER B 1 150 ? 33.078  0.350   16.233 1.00 33.49  ? 149 SER B N   1 
ATOM   2895 C CA  . SER B 1 150 ? 31.758  0.919   15.974 1.00 37.10  ? 149 SER B CA  1 
ATOM   2896 C C   . SER B 1 150 ? 31.771  1.989   14.893 1.00 46.38  ? 149 SER B C   1 
ATOM   2897 O O   . SER B 1 150 ? 30.766  2.220   14.220 1.00 36.77  ? 149 SER B O   1 
ATOM   2898 C CB  . SER B 1 150 ? 31.194  1.510   17.275 1.00 32.54  ? 149 SER B CB  1 
ATOM   2899 O OG  . SER B 1 150 ? 30.919  0.446   18.167 1.00 27.08  ? 149 SER B OG  1 
ATOM   2900 N N   . THR B 1 151 ? 32.904  2.660   14.715 1.00 50.13  ? 150 THR B N   1 
ATOM   2901 C CA  . THR B 1 151 ? 33.000  3.799   13.808 1.00 36.59  ? 150 THR B CA  1 
ATOM   2902 C C   . THR B 1 151 ? 33.855  3.521   12.581 1.00 50.12  ? 150 THR B C   1 
ATOM   2903 O O   . THR B 1 151 ? 34.418  4.430   11.966 1.00 41.80  ? 150 THR B O   1 
ATOM   2904 C CB  . THR B 1 151 ? 33.569  5.010   14.575 1.00 27.10  ? 150 THR B CB  1 
ATOM   2905 O OG1 . THR B 1 151 ? 34.947  4.787   14.892 1.00 25.55  ? 150 THR B OG1 1 
ATOM   2906 C CG2 . THR B 1 151 ? 32.872  5.212   15.921 1.00 33.82  ? 150 THR B CG2 1 
ATOM   2907 N N   . ASP B 1 152 ? 33.992  2.259   12.170 1.00 55.35  ? 151 ASP B N   1 
ATOM   2908 C CA  . ASP B 1 152 ? 34.846  1.948   11.021 1.00 45.59  ? 151 ASP B CA  1 
ATOM   2909 C C   . ASP B 1 152 ? 33.989  1.728   9.767  1.00 36.68  ? 151 ASP B C   1 
ATOM   2910 O O   . ASP B 1 152 ? 33.133  0.854   9.722  1.00 23.44  ? 151 ASP B O   1 
ATOM   2911 C CB  . ASP B 1 152 ? 35.737  0.751   11.312 1.00 51.71  ? 151 ASP B CB  1 
ATOM   2912 C CG  . ASP B 1 152 ? 36.657  0.233   10.229 1.00 51.79  ? 151 ASP B CG  1 
ATOM   2913 O OD1 . ASP B 1 152 ? 36.816  0.837   9.149  1.00 40.14  ? 151 ASP B OD1 1 
ATOM   2914 O OD2 . ASP B 1 152 ? 37.265  -0.845  10.442 1.00 38.70  ? 151 ASP B OD2 1 
ATOM   2915 N N   . SER B 1 153 ? 34.281  2.563   8.796  1.00 33.96  ? 152 SER B N   1 
ATOM   2916 C CA  . SER B 1 153 ? 33.853  2.620   7.430  1.00 40.05  ? 152 SER B CA  1 
ATOM   2917 C C   . SER B 1 153 ? 33.647  1.229   6.831  1.00 38.59  ? 152 SER B C   1 
ATOM   2918 O O   . SER B 1 153 ? 32.621  0.957   6.207  1.00 35.97  ? 152 SER B O   1 
ATOM   2919 C CB  . SER B 1 153 ? 34.934  3.338   6.600  1.00 44.01  ? 152 SER B CB  1 
ATOM   2920 O OG  . SER B 1 153 ? 34.475  3.601   5.281  1.00 70.12  ? 152 SER B OG  1 
ATOM   2921 N N   . ARG B 1 154 ? 34.672  0.417   7.062  1.00 27.14  ? 153 ARG B N   1 
ATOM   2922 C CA  . ARG B 1 154 ? 34.810  -0.885  6.429  1.00 24.35  ? 153 ARG B CA  1 
ATOM   2923 C C   . ARG B 1 154 ? 33.750  -1.875  6.884  1.00 30.98  ? 153 ARG B C   1 
ATOM   2924 O O   . ARG B 1 154 ? 33.026  -2.381  6.015  1.00 54.48  ? 153 ARG B O   1 
ATOM   2925 C CB  . ARG B 1 154 ? 36.231  -1.415  6.670  1.00 35.28  ? 153 ARG B CB  1 
ATOM   2926 C CG  . ARG B 1 154 ? 37.280  -0.631  5.884  1.00 38.12  ? 153 ARG B CG  1 
ATOM   2927 C CD  . ARG B 1 154 ? 38.685  -0.997  6.324  1.00 40.12  ? 153 ARG B CD  1 
ATOM   2928 N NE  . ARG B 1 154 ? 39.147  -0.233  7.478  1.00 58.57  ? 153 ARG B NE  1 
ATOM   2929 C CZ  . ARG B 1 154 ? 40.110  -0.603  8.320  1.00 62.60  ? 153 ARG B CZ  1 
ATOM   2930 N NH1 . ARG B 1 154 ? 40.740  -1.762  8.129  1.00 62.23  ? 153 ARG B NH1 1 
ATOM   2931 N NH2 . ARG B 1 154 ? 40.452  0.167   9.345  1.00 65.59  ? 153 ARG B NH2 1 
ATOM   2932 N N   . ARG B 1 155 ? 33.646  -2.144  8.167  1.00 49.71  ? 154 ARG B N   1 
ATOM   2933 C CA  . ARG B 1 155 ? 32.725  -3.040  8.841  1.00 45.21  ? 154 ARG B CA  1 
ATOM   2934 C C   . ARG B 1 155 ? 31.455  -3.393  8.086  1.00 36.92  ? 154 ARG B C   1 
ATOM   2935 O O   . ARG B 1 155 ? 30.745  -2.470  7.666  1.00 32.02  ? 154 ARG B O   1 
ATOM   2936 C CB  . ARG B 1 155 ? 32.284  -2.366  10.156 1.00 52.77  ? 154 ARG B CB  1 
ATOM   2937 C CG  . ARG B 1 155 ? 31.124  -3.128  10.781 1.00 55.02  ? 154 ARG B CG  1 
ATOM   2938 C CD  . ARG B 1 155 ? 31.289  -3.232  12.285 1.00 49.77  ? 154 ARG B CD  1 
ATOM   2939 N NE  . ARG B 1 155 ? 30.204  -4.024  12.874 1.00 41.71  ? 154 ARG B NE  1 
ATOM   2940 C CZ  . ARG B 1 155 ? 30.121  -4.149  14.196 1.00 29.51  ? 154 ARG B CZ  1 
ATOM   2941 N NH1 . ARG B 1 155 ? 31.028  -3.541  14.944 1.00 23.40  ? 154 ARG B NH1 1 
ATOM   2942 N NH2 . ARG B 1 155 ? 29.140  -4.861  14.714 1.00 38.11  ? 154 ARG B NH2 1 
ATOM   2943 N N   . THR B 1 156 ? 31.135  -4.672  7.897  1.00 26.61  ? 155 THR B N   1 
ATOM   2944 C CA  . THR B 1 156 ? 29.983  -5.035  7.062  1.00 24.25  ? 155 THR B CA  1 
ATOM   2945 C C   . THR B 1 156 ? 28.795  -5.592  7.831  1.00 35.44  ? 155 THR B C   1 
ATOM   2946 O O   . THR B 1 156 ? 27.690  -5.807  7.328  1.00 25.51  ? 155 THR B O   1 
ATOM   2947 C CB  . THR B 1 156 ? 30.439  -6.111  6.062  1.00 25.81  ? 155 THR B CB  1 
ATOM   2948 O OG1 . THR B 1 156 ? 31.295  -7.013  6.769  1.00 52.49  ? 155 THR B OG1 1 
ATOM   2949 C CG2 . THR B 1 156 ? 31.250  -5.473  4.942  1.00 36.66  ? 155 THR B CG2 1 
ATOM   2950 N N   . SER B 1 157 ? 29.105  -5.846  9.099  1.00 34.12  ? 156 SER B N   1 
ATOM   2951 C CA  . SER B 1 157 ? 28.143  -6.396  10.039 1.00 36.90  ? 156 SER B CA  1 
ATOM   2952 C C   . SER B 1 157 ? 27.349  -5.245  10.635 1.00 31.22  ? 156 SER B C   1 
ATOM   2953 O O   . SER B 1 157 ? 27.919  -4.191  10.877 1.00 28.23  ? 156 SER B O   1 
ATOM   2954 C CB  . SER B 1 157 ? 28.869  -7.191  11.118 1.00 37.88  ? 156 SER B CB  1 
ATOM   2955 O OG  . SER B 1 157 ? 30.160  -7.539  10.631 1.00 48.05  ? 156 SER B OG  1 
ATOM   2956 N N   . PRO B 1 158 ? 26.064  -5.478  10.803 1.00 25.57  ? 157 PRO B N   1 
ATOM   2957 C CA  . PRO B 1 158 ? 25.146  -4.465  11.337 1.00 25.71  ? 157 PRO B CA  1 
ATOM   2958 C C   . PRO B 1 158 ? 25.724  -3.783  12.564 1.00 30.73  ? 157 PRO B C   1 
ATOM   2959 O O   . PRO B 1 158 ? 26.064  -4.440  13.550 1.00 24.97  ? 157 PRO B O   1 
ATOM   2960 C CB  . PRO B 1 158 ? 23.925  -5.323  11.666 1.00 32.14  ? 157 PRO B CB  1 
ATOM   2961 C CG  . PRO B 1 158 ? 23.935  -6.329  10.544 1.00 37.19  ? 157 PRO B CG  1 
ATOM   2962 C CD  . PRO B 1 158 ? 25.385  -6.733  10.451 1.00 31.92  ? 157 PRO B CD  1 
ATOM   2963 N N   . VAL B 1 159 ? 25.875  -2.454  12.493 1.00 25.40  ? 158 VAL B N   1 
ATOM   2964 C CA  . VAL B 1 159 ? 26.520  -1.782  13.617 1.00 27.63  ? 158 VAL B CA  1 
ATOM   2965 C C   . VAL B 1 159 ? 25.536  -1.342  14.711 1.00 28.85  ? 158 VAL B C   1 
ATOM   2966 O O   . VAL B 1 159 ? 26.008  -0.955  15.784 1.00 22.20  ? 158 VAL B O   1 
ATOM   2967 C CB  . VAL B 1 159 ? 27.292  -0.536  13.155 1.00 26.49  ? 158 VAL B CB  1 
ATOM   2968 C CG1 . VAL B 1 159 ? 28.173  -0.014  14.283 1.00 35.97  ? 158 VAL B CG1 1 
ATOM   2969 C CG2 . VAL B 1 159 ? 28.114  -0.852  11.917 1.00 68.73  ? 158 VAL B CG2 1 
ATOM   2970 N N   . GLY B 1 160 ? 24.248  -1.381  14.410 1.00 23.71  ? 159 GLY B N   1 
ATOM   2971 C CA  . GLY B 1 160 ? 23.171  -0.920  15.263 1.00 18.03  ? 159 GLY B CA  1 
ATOM   2972 C C   . GLY B 1 160 ? 23.292  0.563   15.534 1.00 17.52  ? 159 GLY B C   1 
ATOM   2973 O O   . GLY B 1 160 ? 23.208  1.373   14.625 1.00 21.52  ? 159 GLY B O   1 
ATOM   2974 N N   . SER B 1 161 ? 23.516  0.948   16.782 1.00 28.50  ? 160 SER B N   1 
ATOM   2975 C CA  . SER B 1 161 ? 23.746  2.319   17.198 1.00 15.82  ? 160 SER B CA  1 
ATOM   2976 C C   . SER B 1 161 ? 25.158  2.488   17.734 1.00 25.74  ? 160 SER B C   1 
ATOM   2977 O O   . SER B 1 161 ? 25.421  2.022   18.844 1.00 28.23  ? 160 SER B O   1 
ATOM   2978 C CB  . SER B 1 161 ? 22.771  2.726   18.301 1.00 16.21  ? 160 SER B CB  1 
ATOM   2979 O OG  . SER B 1 161 ? 22.928  4.062   18.721 1.00 19.11  ? 160 SER B OG  1 
ATOM   2980 N N   . PRO B 1 162 ? 26.051  3.130   16.993 1.00 30.69  ? 161 PRO B N   1 
ATOM   2981 C CA  . PRO B 1 162 ? 27.400  3.380   17.520 1.00 24.65  ? 161 PRO B CA  1 
ATOM   2982 C C   . PRO B 1 162 ? 27.304  4.217   18.795 1.00 28.15  ? 161 PRO B C   1 
ATOM   2983 O O   . PRO B 1 162 ? 27.917  3.871   19.802 1.00 21.99  ? 161 PRO B O   1 
ATOM   2984 C CB  . PRO B 1 162 ? 28.105  4.168   16.416 1.00 18.39  ? 161 PRO B CB  1 
ATOM   2985 C CG  . PRO B 1 162 ? 27.343  3.776   15.184 1.00 33.91  ? 161 PRO B CG  1 
ATOM   2986 C CD  . PRO B 1 162 ? 25.903  3.651   15.628 1.00 32.49  ? 161 PRO B CD  1 
ATOM   2987 N N   . ALA B 1 163 ? 26.530  5.298   18.721 1.00 23.16  ? 162 ALA B N   1 
ATOM   2988 C CA  . ALA B 1 163 ? 26.382  6.165   19.881 1.00 18.48  ? 162 ALA B CA  1 
ATOM   2989 C C   . ALA B 1 163 ? 25.832  5.347   21.044 1.00 18.14  ? 162 ALA B C   1 
ATOM   2990 O O   . ALA B 1 163 ? 26.383  5.380   22.139 1.00 24.01  ? 162 ALA B O   1 
ATOM   2991 C CB  . ALA B 1 163 ? 25.487  7.347   19.575 1.00 10.20  ? 162 ALA B CB  1 
ATOM   2992 N N   . LEU B 1 164 ? 24.751  4.586   20.864 1.00 20.95  ? 163 LEU B N   1 
ATOM   2993 C CA  . LEU B 1 164 ? 24.260  3.952   22.101 1.00 17.69  ? 163 LEU B CA  1 
ATOM   2994 C C   . LEU B 1 164 ? 25.223  2.864   22.534 1.00 25.86  ? 163 LEU B C   1 
ATOM   2995 O O   . LEU B 1 164 ? 25.603  2.870   23.707 1.00 29.56  ? 163 LEU B O   1 
ATOM   2996 C CB  . LEU B 1 164 ? 22.822  3.461   21.946 1.00 21.30  ? 163 LEU B CB  1 
ATOM   2997 C CG  . LEU B 1 164 ? 21.772  4.576   22.064 1.00 19.74  ? 163 LEU B CG  1 
ATOM   2998 C CD1 . LEU B 1 164 ? 20.478  4.210   21.364 1.00 14.44  ? 163 LEU B CD1 1 
ATOM   2999 C CD2 . LEU B 1 164 ? 21.484  4.913   23.520 1.00 33.02  ? 163 LEU B CD2 1 
ATOM   3000 N N   . SER B 1 165 ? 25.634  1.977   21.640 1.00 20.92  ? 164 SER B N   1 
ATOM   3001 C CA  . SER B 1 165 ? 26.705  1.032   21.936 1.00 26.77  ? 164 SER B CA  1 
ATOM   3002 C C   . SER B 1 165 ? 27.885  1.628   22.703 1.00 28.00  ? 164 SER B C   1 
ATOM   3003 O O   . SER B 1 165 ? 28.354  1.059   23.692 1.00 21.67  ? 164 SER B O   1 
ATOM   3004 C CB  . SER B 1 165 ? 27.210  0.438   20.605 1.00 27.16  ? 164 SER B CB  1 
ATOM   3005 O OG  . SER B 1 165 ? 26.716  -0.874  20.437 1.00 18.46  ? 164 SER B OG  1 
ATOM   3006 N N   . ILE B 1 166 ? 28.404  2.777   22.282 1.00 19.75  ? 165 ILE B N   1 
ATOM   3007 C CA  . ILE B 1 166 ? 29.561  3.429   22.871 1.00 16.73  ? 165 ILE B CA  1 
ATOM   3008 C C   . ILE B 1 166 ? 29.257  3.987   24.263 1.00 29.40  ? 165 ILE B C   1 
ATOM   3009 O O   . ILE B 1 166 ? 30.085  3.877   25.173 1.00 22.06  ? 165 ILE B O   1 
ATOM   3010 C CB  . ILE B 1 166 ? 30.068  4.600   22.006 1.00 19.67  ? 165 ILE B CB  1 
ATOM   3011 C CG1 . ILE B 1 166 ? 30.567  4.232   20.603 1.00 32.32  ? 165 ILE B CG1 1 
ATOM   3012 C CG2 . ILE B 1 166 ? 31.158  5.363   22.751 1.00 17.93  ? 165 ILE B CG2 1 
ATOM   3013 C CD1 . ILE B 1 166 ? 31.451  3.023   20.554 1.00 64.66  ? 165 ILE B CD1 1 
ATOM   3014 N N   . GLY B 1 167 ? 28.078  4.589   24.358 1.00 26.48  ? 166 GLY B N   1 
ATOM   3015 C CA  . GLY B 1 167 ? 27.559  5.152   25.602 1.00 21.15  ? 166 GLY B CA  1 
ATOM   3016 C C   . GLY B 1 167 ? 27.482  4.057   26.654 1.00 21.92  ? 166 GLY B C   1 
ATOM   3017 O O   . GLY B 1 167 ? 27.901  4.216   27.801 1.00 31.14  ? 166 GLY B O   1 
ATOM   3018 N N   . LEU B 1 168 ? 26.940  2.903   26.260 1.00 23.36  ? 167 LEU B N   1 
ATOM   3019 C CA  . LEU B 1 168 ? 26.770  1.847   27.265 1.00 26.06  ? 167 LEU B CA  1 
ATOM   3020 C C   . LEU B 1 168 ? 28.094  1.157   27.538 1.00 28.31  ? 167 LEU B C   1 
ATOM   3021 O O   . LEU B 1 168 ? 28.258  0.447   28.531 1.00 20.64  ? 167 LEU B O   1 
ATOM   3022 C CB  . LEU B 1 168 ? 25.680  0.880   26.828 1.00 20.08  ? 167 LEU B CB  1 
ATOM   3023 C CG  . LEU B 1 168 ? 24.296  1.508   26.613 1.00 17.62  ? 167 LEU B CG  1 
ATOM   3024 C CD1 . LEU B 1 168 ? 23.454  0.593   25.729 1.00 16.97  ? 167 LEU B CD1 1 
ATOM   3025 C CD2 . LEU B 1 168 ? 23.595  1.775   27.932 1.00 23.21  ? 167 LEU B CD2 1 
ATOM   3026 N N   . SER B 1 169 ? 29.053  1.406   26.643 1.00 21.43  ? 168 SER B N   1 
ATOM   3027 C CA  . SER B 1 169 ? 30.412  0.978   26.925 1.00 20.62  ? 168 SER B CA  1 
ATOM   3028 C C   . SER B 1 169 ? 30.976  1.720   28.138 1.00 17.54  ? 168 SER B C   1 
ATOM   3029 O O   . SER B 1 169 ? 31.547  1.076   29.016 1.00 21.16  ? 168 SER B O   1 
ATOM   3030 C CB  . SER B 1 169 ? 31.361  1.220   25.743 1.00 23.84  ? 168 SER B CB  1 
ATOM   3031 O OG  . SER B 1 169 ? 32.682  0.850   26.129 1.00 19.12  ? 168 SER B OG  1 
ATOM   3032 N N   . VAL B 1 170 ? 30.839  3.033   28.164 1.00 18.45  ? 169 VAL B N   1 
ATOM   3033 C CA  . VAL B 1 170 ? 31.125  3.916   29.274 1.00 23.29  ? 169 VAL B CA  1 
ATOM   3034 C C   . VAL B 1 170 ? 30.423  3.485   30.557 1.00 25.05  ? 169 VAL B C   1 
ATOM   3035 O O   . VAL B 1 170 ? 30.988  3.364   31.644 1.00 21.69  ? 169 VAL B O   1 
ATOM   3036 C CB  . VAL B 1 170 ? 30.654  5.357   28.990 1.00 21.61  ? 169 VAL B CB  1 
ATOM   3037 C CG1 . VAL B 1 170 ? 30.764  6.205   30.254 1.00 25.91  ? 169 VAL B CG1 1 
ATOM   3038 C CG2 . VAL B 1 170 ? 31.455  6.015   27.878 1.00 23.35  ? 169 VAL B CG2 1 
ATOM   3039 N N   . THR B 1 171 ? 29.109  3.258   30.429 1.00 23.75  ? 170 THR B N   1 
ATOM   3040 C CA  . THR B 1 171 ? 28.362  2.790   31.600 1.00 30.36  ? 170 THR B CA  1 
ATOM   3041 C C   . THR B 1 171 ? 28.955  1.549   32.270 1.00 31.06  ? 170 THR B C   1 
ATOM   3042 O O   . THR B 1 171 ? 29.195  1.596   33.478 1.00 38.41  ? 170 THR B O   1 
ATOM   3043 C CB  . THR B 1 171 ? 26.901  2.501   31.198 1.00 12.75  ? 170 THR B CB  1 
ATOM   3044 O OG1 . THR B 1 171 ? 26.300  3.780   30.940 1.00 12.62  ? 170 THR B OG1 1 
ATOM   3045 C CG2 . THR B 1 171 ? 26.165  1.800   32.328 1.00 16.56  ? 170 THR B CG2 1 
ATOM   3046 N N   . LEU B 1 172 ? 29.184  0.484   31.535 1.00 31.19  ? 171 LEU B N   1 
ATOM   3047 C CA  . LEU B 1 172 ? 29.845  -0.746  31.878 1.00 33.21  ? 171 LEU B CA  1 
ATOM   3048 C C   . LEU B 1 172 ? 31.135  -0.537  32.675 1.00 39.69  ? 171 LEU B C   1 
ATOM   3049 O O   . LEU B 1 172 ? 31.422  -1.188  33.684 1.00 20.97  ? 171 LEU B O   1 
ATOM   3050 C CB  . LEU B 1 172 ? 30.220  -1.512  30.587 1.00 23.46  ? 171 LEU B CB  1 
ATOM   3051 C CG  . LEU B 1 172 ? 31.349  -2.521  30.853 1.00 26.01  ? 171 LEU B CG  1 
ATOM   3052 C CD1 . LEU B 1 172 ? 30.815  -3.671  31.704 1.00 24.59  ? 171 LEU B CD1 1 
ATOM   3053 C CD2 . LEU B 1 172 ? 31.963  -3.034  29.568 1.00 29.65  ? 171 LEU B CD2 1 
ATOM   3054 N N   . GLY B 1 173 ? 31.915  0.407   32.156 1.00 40.72  ? 172 GLY B N   1 
ATOM   3055 C CA  . GLY B 1 173 ? 33.171  0.831   32.747 1.00 38.73  ? 172 GLY B CA  1 
ATOM   3056 C C   . GLY B 1 173 ? 32.975  1.431   34.122 1.00 36.22  ? 172 GLY B C   1 
ATOM   3057 O O   . GLY B 1 173 ? 33.843  1.318   34.986 1.00 27.62  ? 172 GLY B O   1 
ATOM   3058 N N   . HIS B 1 174 ? 31.846  2.084   34.381 1.00 34.10  ? 173 HIS B N   1 
ATOM   3059 C CA  . HIS B 1 174 ? 31.638  2.670   35.706 1.00 36.95  ? 173 HIS B CA  1 
ATOM   3060 C C   . HIS B 1 174 ? 31.184  1.607   36.702 1.00 35.63  ? 173 HIS B C   1 
ATOM   3061 O O   . HIS B 1 174 ? 31.444  1.725   37.895 1.00 32.40  ? 173 HIS B O   1 
ATOM   3062 C CB  . HIS B 1 174 ? 30.588  3.780   35.677 1.00 40.06  ? 173 HIS B CB  1 
ATOM   3063 C CG  . HIS B 1 174 ? 31.040  5.016   34.963 1.00 44.66  ? 173 HIS B CG  1 
ATOM   3064 N ND1 . HIS B 1 174 ? 31.493  6.126   35.639 1.00 38.04  ? 173 HIS B ND1 1 
ATOM   3065 C CD2 . HIS B 1 174 ? 31.102  5.317   33.641 1.00 36.14  ? 173 HIS B CD2 1 
ATOM   3066 C CE1 . HIS B 1 174 ? 31.819  7.054   34.758 1.00 40.57  ? 173 HIS B CE1 1 
ATOM   3067 N NE2 . HIS B 1 174 ? 31.594  6.592   33.540 1.00 41.97  ? 173 HIS B NE2 1 
ATOM   3068 N N   . LEU B 1 175 ? 30.497  0.599   36.175 1.00 37.94  ? 174 LEU B N   1 
ATOM   3069 C CA  . LEU B 1 175 ? 29.953  -0.479  37.000 1.00 31.52  ? 174 LEU B CA  1 
ATOM   3070 C C   . LEU B 1 175 ? 31.098  -1.189  37.710 1.00 27.32  ? 174 LEU B C   1 
ATOM   3071 O O   . LEU B 1 175 ? 30.904  -1.761  38.791 1.00 34.81  ? 174 LEU B O   1 
ATOM   3072 C CB  . LEU B 1 175 ? 29.084  -1.426  36.168 1.00 26.21  ? 174 LEU B CB  1 
ATOM   3073 C CG  . LEU B 1 175 ? 27.678  -0.924  35.835 1.00 25.74  ? 174 LEU B CG  1 
ATOM   3074 C CD1 . LEU B 1 175 ? 27.042  -1.705  34.702 1.00 22.02  ? 174 LEU B CD1 1 
ATOM   3075 C CD2 . LEU B 1 175 ? 26.793  -0.995  37.076 1.00 37.51  ? 174 LEU B CD2 1 
ATOM   3076 N N   . VAL B 1 176 ? 32.307  -1.139  37.135 1.00 19.98  ? 175 VAL B N   1 
ATOM   3077 C CA  . VAL B 1 176 ? 33.417  -1.757  37.879 1.00 26.03  ? 175 VAL B CA  1 
ATOM   3078 C C   . VAL B 1 176 ? 34.334  -0.666  38.429 1.00 40.33  ? 175 VAL B C   1 
ATOM   3079 O O   . VAL B 1 176 ? 34.693  -0.591  39.613 1.00 35.98  ? 175 VAL B O   1 
ATOM   3080 C CB  . VAL B 1 176 ? 34.173  -2.769  37.019 1.00 22.31  ? 175 VAL B CB  1 
ATOM   3081 C CG1 . VAL B 1 176 ? 35.589  -2.979  37.528 1.00 31.84  ? 175 VAL B CG1 1 
ATOM   3082 C CG2 . VAL B 1 176 ? 33.451  -4.116  37.005 1.00 27.34  ? 175 VAL B CG2 1 
ATOM   3083 N N   . GLY B 1 177 ? 34.695  0.231   37.521 1.00 33.54  ? 176 GLY B N   1 
ATOM   3084 C CA  . GLY B 1 177 ? 35.550  1.358   37.764 1.00 18.88  ? 176 GLY B CA  1 
ATOM   3085 C C   . GLY B 1 177 ? 35.216  2.274   38.916 1.00 21.59  ? 176 GLY B C   1 
ATOM   3086 O O   . GLY B 1 177 ? 36.141  2.804   39.560 1.00 19.84  ? 176 GLY B O   1 
ATOM   3087 N N   . ILE B 1 178 ? 33.940  2.502   39.198 1.00 22.88  ? 177 ILE B N   1 
ATOM   3088 C CA  . ILE B 1 178 ? 33.571  3.389   40.308 1.00 28.33  ? 177 ILE B CA  1 
ATOM   3089 C C   . ILE B 1 178 ? 34.229  2.865   41.580 1.00 31.19  ? 177 ILE B C   1 
ATOM   3090 O O   . ILE B 1 178 ? 34.709  3.627   42.413 1.00 33.12  ? 177 ILE B O   1 
ATOM   3091 C CB  . ILE B 1 178 ? 32.041  3.541   40.429 1.00 29.84  ? 177 ILE B CB  1 
ATOM   3092 C CG1 . ILE B 1 178 ? 31.404  4.378   39.312 1.00 27.20  ? 177 ILE B CG1 1 
ATOM   3093 C CG2 . ILE B 1 178 ? 31.646  4.106   41.786 1.00 34.00  ? 177 ILE B CG2 1 
ATOM   3094 C CD1 . ILE B 1 178 ? 29.946  4.745   39.470 1.00 21.43  ? 177 ILE B CD1 1 
ATOM   3095 N N   . TYR B 1 179 ? 34.324  1.545   41.708 1.00 32.65  ? 178 TYR B N   1 
ATOM   3096 C CA  . TYR B 1 179 ? 34.842  0.927   42.928 1.00 32.14  ? 178 TYR B CA  1 
ATOM   3097 C C   . TYR B 1 179 ? 36.335  1.060   43.119 1.00 42.10  ? 178 TYR B C   1 
ATOM   3098 O O   . TYR B 1 179 ? 36.845  0.782   44.214 1.00 43.52  ? 178 TYR B O   1 
ATOM   3099 C CB  . TYR B 1 179 ? 34.480  -0.577  42.931 1.00 23.03  ? 178 TYR B CB  1 
ATOM   3100 C CG  . TYR B 1 179 ? 32.990  -0.778  43.114 1.00 31.70  ? 178 TYR B CG  1 
ATOM   3101 C CD1 . TYR B 1 179 ? 32.213  -1.419  42.161 1.00 40.37  ? 178 TYR B CD1 1 
ATOM   3102 C CD2 . TYR B 1 179 ? 32.366  -0.296  44.260 1.00 24.55  ? 178 TYR B CD2 1 
ATOM   3103 C CE1 . TYR B 1 179 ? 30.850  -1.587  42.345 1.00 35.16  ? 178 TYR B CE1 1 
ATOM   3104 C CE2 . TYR B 1 179 ? 31.008  -0.461  44.450 1.00 28.20  ? 178 TYR B CE2 1 
ATOM   3105 C CZ  . TYR B 1 179 ? 30.259  -1.111  43.490 1.00 30.04  ? 178 TYR B CZ  1 
ATOM   3106 O OH  . TYR B 1 179 ? 28.910  -1.252  43.720 1.00 26.85  ? 178 TYR B OH  1 
ATOM   3107 N N   . PHE B 1 180 ? 37.100  1.461   42.101 1.00 45.09  ? 179 PHE B N   1 
ATOM   3108 C CA  . PHE B 1 180 ? 38.537  1.580   42.387 1.00 43.34  ? 179 PHE B CA  1 
ATOM   3109 C C   . PHE B 1 180 ? 39.009  3.027   42.371 1.00 45.01  ? 179 PHE B C   1 
ATOM   3110 O O   . PHE B 1 180 ? 39.925  3.478   43.070 1.00 30.71  ? 179 PHE B O   1 
ATOM   3111 C CB  . PHE B 1 180 ? 39.329  0.753   41.384 1.00 33.39  ? 179 PHE B CB  1 
ATOM   3112 C CG  . PHE B 1 180 ? 38.906  -0.677  41.151 1.00 33.56  ? 179 PHE B CG  1 
ATOM   3113 C CD1 . PHE B 1 180 ? 37.735  -0.977  40.474 1.00 27.82  ? 179 PHE B CD1 1 
ATOM   3114 C CD2 . PHE B 1 180 ? 39.685  -1.726  41.604 1.00 37.44  ? 179 PHE B CD2 1 
ATOM   3115 C CE1 . PHE B 1 180 ? 37.375  -2.288  40.247 1.00 32.81  ? 179 PHE B CE1 1 
ATOM   3116 C CE2 . PHE B 1 180 ? 39.341  -3.046  41.366 1.00 32.22  ? 179 PHE B CE2 1 
ATOM   3117 C CZ  . PHE B 1 180 ? 38.178  -3.326  40.677 1.00 34.56  ? 179 PHE B CZ  1 
ATOM   3118 N N   . THR B 1 181 ? 38.372  3.825   41.510 1.00 43.85  ? 180 THR B N   1 
ATOM   3119 C CA  . THR B 1 181 ? 38.881  5.168   41.275 1.00 42.72  ? 180 THR B CA  1 
ATOM   3120 C C   . THR B 1 181 ? 37.794  6.216   41.110 1.00 43.08  ? 180 THR B C   1 
ATOM   3121 O O   . THR B 1 181 ? 38.099  7.407   41.006 1.00 34.40  ? 180 THR B O   1 
ATOM   3122 C CB  . THR B 1 181 ? 39.734  5.185   39.986 1.00 40.81  ? 180 THR B CB  1 
ATOM   3123 O OG1 . THR B 1 181 ? 39.051  4.456   38.960 1.00 31.24  ? 180 THR B OG1 1 
ATOM   3124 C CG2 . THR B 1 181 ? 41.061  4.497   40.250 1.00 43.66  ? 180 THR B CG2 1 
ATOM   3125 N N   . GLY B 1 182 ? 36.545  5.762   41.069 1.00 43.38  ? 181 GLY B N   1 
ATOM   3126 C CA  . GLY B 1 182 ? 35.454  6.657   40.696 1.00 44.26  ? 181 GLY B CA  1 
ATOM   3127 C C   . GLY B 1 182 ? 35.393  6.779   39.175 1.00 45.08  ? 181 GLY B C   1 
ATOM   3128 O O   . GLY B 1 182 ? 34.819  7.722   38.636 1.00 61.44  ? 181 GLY B O   1 
ATOM   3129 N N   . CYS B 1 183 ? 36.009  5.805   38.514 1.00 37.45  ? 182 CYS B N   1 
ATOM   3130 C CA  . CYS B 1 183 ? 36.017  5.663   37.076 1.00 28.62  ? 182 CYS B CA  1 
ATOM   3131 C C   . CYS B 1 183 ? 36.509  6.911   36.349 1.00 30.93  ? 182 CYS B C   1 
ATOM   3132 O O   . CYS B 1 183 ? 35.792  7.901   36.228 1.00 30.32  ? 182 CYS B O   1 
ATOM   3133 C CB  . CYS B 1 183 ? 34.610  5.338   36.541 1.00 32.87  ? 182 CYS B CB  1 
ATOM   3134 S SG  . CYS B 1 183 ? 34.732  4.468   34.953 1.00 31.74  ? 182 CYS B SG  1 
ATOM   3135 N N   . SER B 1 184 ? 37.743  6.841   35.849 1.00 26.34  ? 183 SER B N   1 
ATOM   3136 C CA  . SER B 1 184 ? 38.246  7.936   35.033 1.00 31.47  ? 183 SER B CA  1 
ATOM   3137 C C   . SER B 1 184 ? 37.989  7.650   33.553 1.00 26.44  ? 183 SER B C   1 
ATOM   3138 O O   . SER B 1 184 ? 37.031  8.183   32.993 1.00 19.59  ? 183 SER B O   1 
ATOM   3139 C CB  . SER B 1 184 ? 39.742  8.181   35.225 1.00 33.41  ? 183 SER B CB  1 
ATOM   3140 O OG  . SER B 1 184 ? 40.202  9.001   34.155 1.00 44.00  ? 183 SER B OG  1 
ATOM   3141 N N   . MET B 1 185 ? 38.821  6.830   32.918 1.00 26.16  ? 184 MET B N   1 
ATOM   3142 C CA  . MET B 1 185 ? 38.624  6.493   31.509 1.00 36.83  ? 184 MET B CA  1 
ATOM   3143 C C   . MET B 1 185 ? 38.730  7.714   30.592 1.00 44.92  ? 184 MET B C   1 
ATOM   3144 O O   . MET B 1 185 ? 38.329  7.642   29.425 1.00 48.06  ? 184 MET B O   1 
ATOM   3145 C CB  . MET B 1 185 ? 37.247  5.877   31.281 1.00 32.22  ? 184 MET B CB  1 
ATOM   3146 C CG  . MET B 1 185 ? 37.043  4.429   31.672 1.00 32.17  ? 184 MET B CG  1 
ATOM   3147 S SD  . MET B 1 185 ? 35.285  3.992   31.579 1.00 41.13  ? 184 MET B SD  1 
ATOM   3148 C CE  . MET B 1 185 ? 35.267  3.109   30.019 1.00 57.00  ? 184 MET B CE  1 
ATOM   3149 N N   . ASN B 1 186 ? 39.233  8.830   31.099 1.00 30.75  ? 185 ASN B N   1 
ATOM   3150 C CA  . ASN B 1 186 ? 39.192  10.107  30.394 1.00 28.97  ? 185 ASN B CA  1 
ATOM   3151 C C   . ASN B 1 186 ? 39.940  11.156  31.196 1.00 32.51  ? 185 ASN B C   1 
ATOM   3152 O O   . ASN B 1 186 ? 39.544  11.572  32.277 1.00 32.88  ? 185 ASN B O   1 
ATOM   3153 C CB  . ASN B 1 186 ? 37.726  10.458  30.174 1.00 29.26  ? 185 ASN B CB  1 
ATOM   3154 C CG  . ASN B 1 186 ? 37.489  11.774  29.469 1.00 29.77  ? 185 ASN B CG  1 
ATOM   3155 O OD1 . ASN B 1 186 ? 38.345  12.649  29.446 1.00 37.11  ? 185 ASN B OD1 1 
ATOM   3156 N ND2 . ASN B 1 186 ? 36.296  11.887  28.890 1.00 24.22  ? 185 ASN B ND2 1 
ATOM   3157 N N   . PRO B 1 187 ? 41.084  11.588  30.688 1.00 38.84  ? 186 PRO B N   1 
ATOM   3158 C CA  . PRO B 1 187 ? 41.909  12.556  31.411 1.00 37.05  ? 186 PRO B CA  1 
ATOM   3159 C C   . PRO B 1 187 ? 41.183  13.854  31.737 1.00 41.66  ? 186 PRO B C   1 
ATOM   3160 O O   . PRO B 1 187 ? 41.438  14.497  32.759 1.00 48.08  ? 186 PRO B O   1 
ATOM   3161 C CB  . PRO B 1 187 ? 43.040  12.829  30.406 1.00 39.99  ? 186 PRO B CB  1 
ATOM   3162 C CG  . PRO B 1 187 ? 43.121  11.570  29.605 1.00 40.15  ? 186 PRO B CG  1 
ATOM   3163 C CD  . PRO B 1 187 ? 41.680  11.165  29.409 1.00 43.71  ? 186 PRO B CD  1 
ATOM   3164 N N   . ALA B 1 188 ? 40.263  14.298  30.884 1.00 36.42  ? 187 ALA B N   1 
ATOM   3165 C CA  . ALA B 1 188 ? 39.666  15.611  31.101 1.00 26.18  ? 187 ALA B CA  1 
ATOM   3166 C C   . ALA B 1 188 ? 38.550  15.568  32.129 1.00 30.19  ? 187 ALA B C   1 
ATOM   3167 O O   . ALA B 1 188 ? 38.310  16.522  32.870 1.00 39.98  ? 187 ALA B O   1 
ATOM   3168 C CB  . ALA B 1 188 ? 39.168  16.182  29.777 1.00 17.35  ? 187 ALA B CB  1 
ATOM   3169 N N   . ARG B 1 189 ? 37.831  14.448  32.189 1.00 30.72  ? 188 ARG B N   1 
ATOM   3170 C CA  . ARG B 1 189 ? 36.759  14.361  33.175 1.00 29.21  ? 188 ARG B CA  1 
ATOM   3171 C C   . ARG B 1 189 ? 37.386  14.504  34.566 1.00 35.45  ? 188 ARG B C   1 
ATOM   3172 O O   . ARG B 1 189 ? 36.774  15.044  35.480 1.00 49.56  ? 188 ARG B O   1 
ATOM   3173 C CB  . ARG B 1 189 ? 35.987  13.048  33.066 1.00 27.76  ? 188 ARG B CB  1 
ATOM   3174 C CG  . ARG B 1 189 ? 35.281  12.615  34.350 1.00 27.41  ? 188 ARG B CG  1 
ATOM   3175 C CD  . ARG B 1 189 ? 36.059  11.528  35.088 1.00 18.13  ? 188 ARG B CD  1 
ATOM   3176 N NE  . ARG B 1 189 ? 35.232  10.996  36.178 1.00 28.88  ? 188 ARG B NE  1 
ATOM   3177 C CZ  . ARG B 1 189 ? 34.849  11.728  37.220 1.00 35.75  ? 188 ARG B CZ  1 
ATOM   3178 N NH1 . ARG B 1 189 ? 35.203  13.004  37.339 1.00 35.51  ? 188 ARG B NH1 1 
ATOM   3179 N NH2 . ARG B 1 189 ? 34.096  11.196  38.178 1.00 40.31  ? 188 ARG B NH2 1 
ATOM   3180 N N   . SER B 1 190 ? 38.613  14.009  34.688 1.00 35.87  ? 189 SER B N   1 
ATOM   3181 C CA  . SER B 1 190 ? 39.332  14.050  35.958 1.00 36.20  ? 189 SER B CA  1 
ATOM   3182 C C   . SER B 1 190 ? 39.946  15.432  36.168 1.00 40.97  ? 189 SER B C   1 
ATOM   3183 O O   . SER B 1 190 ? 39.898  15.973  37.273 1.00 40.13  ? 189 SER B O   1 
ATOM   3184 C CB  . SER B 1 190 ? 40.417  12.973  36.018 1.00 26.83  ? 189 SER B CB  1 
ATOM   3185 O OG  . SER B 1 190 ? 39.878  11.686  35.738 1.00 29.69  ? 189 SER B OG  1 
ATOM   3186 N N   . PHE B 1 191 ? 40.509  15.984  35.100 1.00 37.88  ? 190 PHE B N   1 
ATOM   3187 C CA  . PHE B 1 191 ? 41.299  17.214  35.168 1.00 29.67  ? 190 PHE B CA  1 
ATOM   3188 C C   . PHE B 1 191 ? 40.377  18.389  35.454 1.00 33.25  ? 190 PHE B C   1 
ATOM   3189 O O   . PHE B 1 191 ? 40.724  19.324  36.161 1.00 38.37  ? 190 PHE B O   1 
ATOM   3190 C CB  . PHE B 1 191 ? 42.074  17.394  33.874 1.00 36.37  ? 190 PHE B CB  1 
ATOM   3191 C CG  . PHE B 1 191 ? 42.928  18.639  33.741 1.00 41.52  ? 190 PHE B CG  1 
ATOM   3192 C CD1 . PHE B 1 191 ? 44.160  18.724  34.359 1.00 42.42  ? 190 PHE B CD1 1 
ATOM   3193 C CD2 . PHE B 1 191 ? 42.489  19.714  32.989 1.00 40.03  ? 190 PHE B CD2 1 
ATOM   3194 C CE1 . PHE B 1 191 ? 44.942  19.858  34.234 1.00 41.52  ? 190 PHE B CE1 1 
ATOM   3195 C CE2 . PHE B 1 191 ? 43.253  20.858  32.852 1.00 35.19  ? 190 PHE B CE2 1 
ATOM   3196 C CZ  . PHE B 1 191 ? 44.478  20.920  33.488 1.00 42.33  ? 190 PHE B CZ  1 
ATOM   3197 N N   . GLY B 1 192 ? 39.177  18.289  34.890 1.00 42.35  ? 191 GLY B N   1 
ATOM   3198 C CA  . GLY B 1 192 ? 38.144  19.294  35.004 1.00 37.40  ? 191 GLY B CA  1 
ATOM   3199 C C   . GLY B 1 192 ? 37.912  19.721  36.443 1.00 44.93  ? 191 GLY B C   1 
ATOM   3200 O O   . GLY B 1 192 ? 38.311  20.831  36.804 1.00 41.54  ? 191 GLY B O   1 
ATOM   3201 N N   . PRO B 1 193 ? 37.271  18.846  37.215 1.00 45.72  ? 192 PRO B N   1 
ATOM   3202 C CA  . PRO B 1 193 ? 36.917  19.136  38.607 1.00 50.36  ? 192 PRO B CA  1 
ATOM   3203 C C   . PRO B 1 193 ? 38.167  19.413  39.446 1.00 51.60  ? 192 PRO B C   1 
ATOM   3204 O O   . PRO B 1 193 ? 38.097  20.231  40.366 1.00 37.03  ? 192 PRO B O   1 
ATOM   3205 C CB  . PRO B 1 193 ? 36.211  17.870  39.097 1.00 39.72  ? 192 PRO B CB  1 
ATOM   3206 C CG  . PRO B 1 193 ? 36.555  16.803  38.116 1.00 36.21  ? 192 PRO B CG  1 
ATOM   3207 C CD  . PRO B 1 193 ? 36.829  17.501  36.814 1.00 44.91  ? 192 PRO B CD  1 
ATOM   3208 N N   . ALA B 1 194 ? 39.254  18.733  39.090 1.00 50.66  ? 193 ALA B N   1 
ATOM   3209 C CA  . ALA B 1 194 ? 40.539  18.848  39.767 1.00 49.76  ? 193 ALA B CA  1 
ATOM   3210 C C   . ALA B 1 194 ? 41.058  20.274  39.615 1.00 43.61  ? 193 ALA B C   1 
ATOM   3211 O O   . ALA B 1 194 ? 41.837  20.753  40.426 1.00 54.92  ? 193 ALA B O   1 
ATOM   3212 C CB  . ALA B 1 194 ? 41.593  17.879  39.248 1.00 29.00  ? 193 ALA B CB  1 
ATOM   3213 N N   . VAL B 1 195 ? 40.600  20.912  38.541 1.00 39.89  ? 194 VAL B N   1 
ATOM   3214 C CA  . VAL B 1 195 ? 41.011  22.280  38.295 1.00 40.63  ? 194 VAL B CA  1 
ATOM   3215 C C   . VAL B 1 195 ? 40.064  23.242  39.004 1.00 40.55  ? 194 VAL B C   1 
ATOM   3216 O O   . VAL B 1 195 ? 40.542  24.141  39.694 1.00 37.64  ? 194 VAL B O   1 
ATOM   3217 C CB  . VAL B 1 195 ? 41.045  22.667  36.805 1.00 43.66  ? 194 VAL B CB  1 
ATOM   3218 C CG1 . VAL B 1 195 ? 40.879  24.175  36.661 1.00 32.10  ? 194 VAL B CG1 1 
ATOM   3219 C CG2 . VAL B 1 195 ? 42.338  22.206  36.150 1.00 55.65  ? 194 VAL B CG2 1 
ATOM   3220 N N   . VAL B 1 196 ? 38.761  23.054  38.805 1.00 46.09  ? 195 VAL B N   1 
ATOM   3221 C CA  . VAL B 1 196 ? 37.843  24.029  39.405 1.00 49.58  ? 195 VAL B CA  1 
ATOM   3222 C C   . VAL B 1 196 ? 38.029  24.055  40.918 1.00 50.76  ? 195 VAL B C   1 
ATOM   3223 O O   . VAL B 1 196 ? 37.908  25.086  41.573 1.00 53.06  ? 195 VAL B O   1 
ATOM   3224 C CB  . VAL B 1 196 ? 36.379  23.741  39.053 1.00 49.54  ? 195 VAL B CB  1 
ATOM   3225 C CG1 . VAL B 1 196 ? 35.447  24.504  39.988 1.00 29.88  ? 195 VAL B CG1 1 
ATOM   3226 C CG2 . VAL B 1 196 ? 36.133  24.091  37.593 1.00 61.27  ? 195 VAL B CG2 1 
ATOM   3227 N N   . MET B 1 197 ? 38.350  22.875  41.439 1.00 49.62  ? 196 MET B N   1 
ATOM   3228 C CA  . MET B 1 197 ? 38.793  22.762  42.822 1.00 58.30  ? 196 MET B CA  1 
ATOM   3229 C C   . MET B 1 197 ? 40.305  22.668  42.809 1.00 67.86  ? 196 MET B C   1 
ATOM   3230 O O   . MET B 1 197 ? 40.869  21.717  42.259 1.00 83.42  ? 196 MET B O   1 
ATOM   3231 C CB  . MET B 1 197 ? 38.167  21.543  43.488 1.00 57.29  ? 196 MET B CB  1 
ATOM   3232 C CG  . MET B 1 197 ? 36.745  21.253  43.031 1.00 58.43  ? 196 MET B CG  1 
ATOM   3233 S SD  . MET B 1 197 ? 35.561  21.444  44.381 1.00 64.06  ? 196 MET B SD  1 
ATOM   3234 C CE  . MET B 1 197 ? 34.730  22.950  43.911 1.00 19.25  ? 196 MET B CE  1 
ATOM   3235 N N   . ASN B 1 198 ? 41.068  23.600  43.373 1.00 73.46  ? 197 ASN B N   1 
ATOM   3236 C CA  . ASN B 1 198 ? 42.520  23.407  43.232 1.00 79.35  ? 197 ASN B CA  1 
ATOM   3237 C C   . ASN B 1 198 ? 43.013  22.341  44.196 1.00 74.26  ? 197 ASN B C   1 
ATOM   3238 O O   . ASN B 1 198 ? 43.764  22.602  45.133 1.00 85.67  ? 197 ASN B O   1 
ATOM   3239 C CB  . ASN B 1 198 ? 43.228  24.747  43.438 1.00 90.13  ? 197 ASN B CB  1 
ATOM   3240 C CG  . ASN B 1 198 ? 42.372  25.895  42.921 1.00 99.37  ? 197 ASN B CG  1 
ATOM   3241 O OD1 . ASN B 1 198 ? 41.296  26.170  43.480 1.00 120.75 ? 197 ASN B OD1 1 
ATOM   3242 N ND2 . ASN B 1 198 ? 42.833  26.551  41.873 1.00 104.43 ? 197 ASN B ND2 1 
ATOM   3243 N N   . ARG B 1 199 ? 42.577  21.107  43.974 1.00 69.90  ? 198 ARG B N   1 
ATOM   3244 C CA  . ARG B 1 199 ? 42.854  19.996  44.871 1.00 70.07  ? 198 ARG B CA  1 
ATOM   3245 C C   . ARG B 1 199 ? 43.007  18.712  44.059 1.00 61.74  ? 198 ARG B C   1 
ATOM   3246 O O   . ARG B 1 199 ? 42.290  17.738  44.256 1.00 70.02  ? 198 ARG B O   1 
ATOM   3247 C CB  . ARG B 1 199 ? 41.746  19.836  45.910 1.00 78.40  ? 198 ARG B CB  1 
ATOM   3248 C CG  . ARG B 1 199 ? 42.226  19.531  47.324 1.00 93.78  ? 198 ARG B CG  1 
ATOM   3249 C CD  . ARG B 1 199 ? 43.655  19.007  47.349 1.00 105.06 ? 198 ARG B CD  1 
ATOM   3250 N NE  . ARG B 1 199 ? 43.729  17.603  47.731 1.00 113.20 ? 198 ARG B NE  1 
ATOM   3251 C CZ  . ARG B 1 199 ? 44.687  16.756  47.352 1.00 113.39 ? 198 ARG B CZ  1 
ATOM   3252 N NH1 . ARG B 1 199 ? 45.664  17.181  46.566 1.00 109.03 ? 198 ARG B NH1 1 
ATOM   3253 N NH2 . ARG B 1 199 ? 44.663  15.495  47.759 1.00 118.80 ? 198 ARG B NH2 1 
ATOM   3254 N N   . PHE B 1 200 ? 43.963  18.760  43.145 1.00 53.15  ? 199 PHE B N   1 
ATOM   3255 C CA  . PHE B 1 200 ? 44.223  17.652  42.242 1.00 48.53  ? 199 PHE B CA  1 
ATOM   3256 C C   . PHE B 1 200 ? 44.261  16.283  42.910 1.00 60.38  ? 199 PHE B C   1 
ATOM   3257 O O   . PHE B 1 200 ? 43.640  15.361  42.362 1.00 100.26 ? 199 PHE B O   1 
ATOM   3258 C CB  . PHE B 1 200 ? 45.538  17.939  41.505 1.00 39.19  ? 199 PHE B CB  1 
ATOM   3259 C CG  . PHE B 1 200 ? 45.235  18.757  40.248 1.00 49.11  ? 199 PHE B CG  1 
ATOM   3260 C CD1 . PHE B 1 200 ? 44.639  20.002  40.360 1.00 49.93  ? 199 PHE B CD1 1 
ATOM   3261 C CD2 . PHE B 1 200 ? 45.540  18.261  38.994 1.00 60.22  ? 199 PHE B CD2 1 
ATOM   3262 C CE1 . PHE B 1 200 ? 44.359  20.736  39.217 1.00 55.06  ? 199 PHE B CE1 1 
ATOM   3263 C CE2 . PHE B 1 200 ? 45.267  18.992  37.846 1.00 59.86  ? 199 PHE B CE2 1 
ATOM   3264 C CZ  . PHE B 1 200 ? 44.671  20.235  37.966 1.00 57.42  ? 199 PHE B CZ  1 
ATOM   3265 N N   . SER B 1 201 ? 44.936  16.140  44.035 1.00 65.16  ? 200 SER B N   1 
ATOM   3266 C CA  . SER B 1 201 ? 45.101  14.873  44.744 1.00 74.40  ? 200 SER B CA  1 
ATOM   3267 C C   . SER B 1 201 ? 46.171  14.024  44.065 1.00 81.51  ? 200 SER B C   1 
ATOM   3268 O O   . SER B 1 201 ? 46.533  14.309  42.917 1.00 70.52  ? 200 SER B O   1 
ATOM   3269 C CB  . SER B 1 201 ? 43.765  14.140  44.869 1.00 73.91  ? 200 SER B CB  1 
ATOM   3270 O OG  . SER B 1 201 ? 43.491  13.310  43.759 1.00 75.48  ? 200 SER B OG  1 
ATOM   3271 N N   . PRO B 1 202 ? 46.696  13.006  44.742 1.00 91.00  ? 201 PRO B N   1 
ATOM   3272 C CA  . PRO B 1 202 ? 47.718  12.129  44.158 1.00 86.06  ? 201 PRO B CA  1 
ATOM   3273 C C   . PRO B 1 202 ? 47.100  11.007  43.328 1.00 81.61  ? 201 PRO B C   1 
ATOM   3274 O O   . PRO B 1 202 ? 45.882  10.796  43.350 1.00 83.69  ? 201 PRO B O   1 
ATOM   3275 C CB  . PRO B 1 202 ? 48.397  11.522  45.389 1.00 87.54  ? 201 PRO B CB  1 
ATOM   3276 C CG  . PRO B 1 202 ? 47.269  11.399  46.363 1.00 95.22  ? 201 PRO B CG  1 
ATOM   3277 C CD  . PRO B 1 202 ? 46.386  12.590  46.124 1.00 98.79  ? 201 PRO B CD  1 
ATOM   3278 N N   . ALA B 1 203 ? 47.959  10.309  42.587 1.00 72.58  ? 202 ALA B N   1 
ATOM   3279 C CA  . ALA B 1 203 ? 47.540  9.246   41.680 1.00 66.74  ? 202 ALA B CA  1 
ATOM   3280 C C   . ALA B 1 203 ? 46.876  9.797   40.425 1.00 66.02  ? 202 ALA B C   1 
ATOM   3281 O O   . ALA B 1 203 ? 46.563  9.043   39.497 1.00 78.15  ? 202 ALA B O   1 
ATOM   3282 C CB  . ALA B 1 203 ? 46.603  8.273   42.383 1.00 64.29  ? 202 ALA B CB  1 
ATOM   3283 N N   . HIS B 1 204 ? 46.660  11.104  40.371 1.00 58.49  ? 203 HIS B N   1 
ATOM   3284 C CA  . HIS B 1 204 ? 46.042  11.797  39.245 1.00 52.80  ? 203 HIS B CA  1 
ATOM   3285 C C   . HIS B 1 204 ? 46.683  11.359  37.934 1.00 50.18  ? 203 HIS B C   1 
ATOM   3286 O O   . HIS B 1 204 ? 46.048  11.232  36.887 1.00 42.58  ? 203 HIS B O   1 
ATOM   3287 C CB  . HIS B 1 204 ? 46.154  13.304  39.465 1.00 42.39  ? 203 HIS B CB  1 
ATOM   3288 C CG  . HIS B 1 204 ? 45.631  14.178  38.372 1.00 38.90  ? 203 HIS B CG  1 
ATOM   3289 N ND1 . HIS B 1 204 ? 44.391  14.774  38.394 1.00 40.78  ? 203 HIS B ND1 1 
ATOM   3290 C CD2 . HIS B 1 204 ? 46.193  14.584  37.211 1.00 41.83  ? 203 HIS B CD2 1 
ATOM   3291 C CE1 . HIS B 1 204 ? 44.217  15.490  37.296 1.00 42.47  ? 203 HIS B CE1 1 
ATOM   3292 N NE2 . HIS B 1 204 ? 45.302  15.391  36.551 1.00 40.85  ? 203 HIS B NE2 1 
ATOM   3293 N N   . TRP B 1 205 ? 47.988  11.096  37.976 1.00 43.93  ? 204 TRP B N   1 
ATOM   3294 C CA  . TRP B 1 205 ? 48.702  10.625  36.801 1.00 52.44  ? 204 TRP B CA  1 
ATOM   3295 C C   . TRP B 1 205 ? 48.028  9.358   36.284 1.00 47.82  ? 204 TRP B C   1 
ATOM   3296 O O   . TRP B 1 205 ? 47.988  9.155   35.072 1.00 50.50  ? 204 TRP B O   1 
ATOM   3297 C CB  . TRP B 1 205 ? 50.167  10.357  37.151 1.00 52.42  ? 204 TRP B CB  1 
ATOM   3298 C CG  . TRP B 1 205 ? 50.252  9.381   38.292 1.00 60.35  ? 204 TRP B CG  1 
ATOM   3299 C CD1 . TRP B 1 205 ? 50.088  9.630   39.621 1.00 60.21  ? 204 TRP B CD1 1 
ATOM   3300 C CD2 . TRP B 1 205 ? 50.527  7.980   38.173 1.00 70.03  ? 204 TRP B CD2 1 
ATOM   3301 N NE1 . TRP B 1 205 ? 50.244  8.473   40.343 1.00 61.04  ? 204 TRP B NE1 1 
ATOM   3302 C CE2 . TRP B 1 205 ? 50.512  7.446   39.475 1.00 65.71  ? 204 TRP B CE2 1 
ATOM   3303 C CE3 . TRP B 1 205 ? 50.780  7.134   37.086 1.00 77.72  ? 204 TRP B CE3 1 
ATOM   3304 C CZ2 . TRP B 1 205 ? 50.746  6.092   39.711 1.00 70.14  ? 204 TRP B CZ2 1 
ATOM   3305 C CZ3 . TRP B 1 205 ? 51.010  5.793   37.329 1.00 77.32  ? 204 TRP B CZ3 1 
ATOM   3306 C CH2 . TRP B 1 205 ? 50.991  5.287   38.635 1.00 72.64  ? 204 TRP B CH2 1 
ATOM   3307 N N   . VAL B 1 206 ? 47.524  8.574   37.240 1.00 35.93  ? 205 VAL B N   1 
ATOM   3308 C CA  . VAL B 1 206 ? 46.862  7.313   36.943 1.00 35.83  ? 205 VAL B CA  1 
ATOM   3309 C C   . VAL B 1 206 ? 45.703  7.586   35.972 1.00 41.80  ? 205 VAL B C   1 
ATOM   3310 O O   . VAL B 1 206 ? 45.517  6.783   35.059 1.00 31.81  ? 205 VAL B O   1 
ATOM   3311 C CB  . VAL B 1 206 ? 46.318  6.591   38.177 1.00 36.58  ? 205 VAL B CB  1 
ATOM   3312 C CG1 . VAL B 1 206 ? 45.744  5.234   37.794 1.00 28.46  ? 205 VAL B CG1 1 
ATOM   3313 C CG2 . VAL B 1 206 ? 47.403  6.389   39.217 1.00 49.53  ? 205 VAL B CG2 1 
ATOM   3314 N N   . PHE B 1 207 ? 45.045  8.698   36.253 1.00 36.21  ? 206 PHE B N   1 
ATOM   3315 C CA  . PHE B 1 207 ? 43.927  9.253   35.513 1.00 44.13  ? 206 PHE B CA  1 
ATOM   3316 C C   . PHE B 1 207 ? 44.377  9.860   34.192 1.00 48.19  ? 206 PHE B C   1 
ATOM   3317 O O   . PHE B 1 207 ? 43.561  10.307  33.390 1.00 53.30  ? 206 PHE B O   1 
ATOM   3318 C CB  . PHE B 1 207 ? 43.200  10.316  36.349 1.00 45.23  ? 206 PHE B CB  1 
ATOM   3319 C CG  . PHE B 1 207 ? 42.812  9.786   37.725 1.00 44.48  ? 206 PHE B CG  1 
ATOM   3320 C CD1 . PHE B 1 207 ? 42.484  8.451   37.889 1.00 33.30  ? 206 PHE B CD1 1 
ATOM   3321 C CD2 . PHE B 1 207 ? 42.779  10.613  38.831 1.00 49.18  ? 206 PHE B CD2 1 
ATOM   3322 C CE1 . PHE B 1 207 ? 42.134  7.945   39.121 1.00 26.09  ? 206 PHE B CE1 1 
ATOM   3323 C CE2 . PHE B 1 207 ? 42.425  10.119  40.070 1.00 45.66  ? 206 PHE B CE2 1 
ATOM   3324 C CZ  . PHE B 1 207 ? 42.101  8.785   40.218 1.00 39.81  ? 206 PHE B CZ  1 
ATOM   3325 N N   . TRP B 1 208 ? 45.690  9.864   33.966 1.00 43.00  ? 207 TRP B N   1 
ATOM   3326 C CA  . TRP B 1 208 ? 46.172  10.299  32.659 1.00 44.42  ? 207 TRP B CA  1 
ATOM   3327 C C   . TRP B 1 208 ? 46.739  9.127   31.878 1.00 44.93  ? 207 TRP B C   1 
ATOM   3328 O O   . TRP B 1 208 ? 46.302  8.843   30.764 1.00 40.60  ? 207 TRP B O   1 
ATOM   3329 C CB  . TRP B 1 208 ? 47.240  11.392  32.797 1.00 51.14  ? 207 TRP B CB  1 
ATOM   3330 C CG  . TRP B 1 208 ? 46.592  12.727  33.018 1.00 46.83  ? 207 TRP B CG  1 
ATOM   3331 C CD1 . TRP B 1 208 ? 46.175  13.225  34.213 1.00 45.15  ? 207 TRP B CD1 1 
ATOM   3332 C CD2 . TRP B 1 208 ? 46.290  13.715  32.028 1.00 45.58  ? 207 TRP B CD2 1 
ATOM   3333 N NE1 . TRP B 1 208 ? 45.628  14.474  34.032 1.00 51.31  ? 207 TRP B NE1 1 
ATOM   3334 C CE2 . TRP B 1 208 ? 45.683  14.799  32.701 1.00 44.38  ? 207 TRP B CE2 1 
ATOM   3335 C CE3 . TRP B 1 208 ? 46.471  13.794  30.644 1.00 38.90  ? 207 TRP B CE3 1 
ATOM   3336 C CZ2 . TRP B 1 208 ? 45.261  15.942  32.028 1.00 47.05  ? 207 TRP B CZ2 1 
ATOM   3337 C CZ3 . TRP B 1 208 ? 46.048  14.936  29.988 1.00 41.05  ? 207 TRP B CZ3 1 
ATOM   3338 C CH2 . TRP B 1 208 ? 45.451  16.000  30.669 1.00 38.96  ? 207 TRP B CH2 1 
ATOM   3339 N N   . VAL B 1 209 ? 47.725  8.471   32.498 1.00 50.27  ? 208 VAL B N   1 
ATOM   3340 C CA  . VAL B 1 209 ? 48.440  7.407   31.781 1.00 49.18  ? 208 VAL B CA  1 
ATOM   3341 C C   . VAL B 1 209 ? 47.602  6.143   31.687 1.00 45.22  ? 208 VAL B C   1 
ATOM   3342 O O   . VAL B 1 209 ? 47.682  5.455   30.669 1.00 33.23  ? 208 VAL B O   1 
ATOM   3343 C CB  . VAL B 1 209 ? 49.823  7.144   32.411 1.00 53.50  ? 208 VAL B CB  1 
ATOM   3344 C CG1 . VAL B 1 209 ? 50.091  8.174   33.509 1.00 46.99  ? 208 VAL B CG1 1 
ATOM   3345 C CG2 . VAL B 1 209 ? 49.966  5.730   32.949 1.00 27.12  ? 208 VAL B CG2 1 
ATOM   3346 N N   . GLY B 1 210 ? 46.796  5.812   32.698 1.00 45.52  ? 209 GLY B N   1 
ATOM   3347 C CA  . GLY B 1 210 ? 45.952  4.630   32.580 1.00 48.12  ? 209 GLY B CA  1 
ATOM   3348 C C   . GLY B 1 210 ? 45.080  4.708   31.337 1.00 49.41  ? 209 GLY B C   1 
ATOM   3349 O O   . GLY B 1 210 ? 45.244  3.915   30.404 1.00 48.55  ? 209 GLY B O   1 
ATOM   3350 N N   . PRO B 1 211 ? 44.171  5.675   31.303 1.00 40.57  ? 210 PRO B N   1 
ATOM   3351 C CA  . PRO B 1 211 ? 43.277  5.799   30.146 1.00 34.65  ? 210 PRO B CA  1 
ATOM   3352 C C   . PRO B 1 211 ? 44.058  5.904   28.841 1.00 39.02  ? 210 PRO B C   1 
ATOM   3353 O O   . PRO B 1 211 ? 43.770  5.177   27.883 1.00 39.15  ? 210 PRO B O   1 
ATOM   3354 C CB  . PRO B 1 211 ? 42.516  7.099   30.422 1.00 29.75  ? 210 PRO B CB  1 
ATOM   3355 C CG  . PRO B 1 211 ? 42.586  7.260   31.911 1.00 40.94  ? 210 PRO B CG  1 
ATOM   3356 C CD  . PRO B 1 211 ? 43.932  6.715   32.317 1.00 35.41  ? 210 PRO B CD  1 
ATOM   3357 N N   . ILE B 1 212 ? 45.051  6.794   28.783 1.00 35.18  ? 211 ILE B N   1 
ATOM   3358 C CA  . ILE B 1 212 ? 45.730  7.017   27.500 1.00 36.35  ? 211 ILE B CA  1 
ATOM   3359 C C   . ILE B 1 212 ? 46.422  5.757   26.987 1.00 38.43  ? 211 ILE B C   1 
ATOM   3360 O O   . ILE B 1 212 ? 46.373  5.465   25.784 1.00 35.89  ? 211 ILE B O   1 
ATOM   3361 C CB  . ILE B 1 212 ? 46.718  8.193   27.609 1.00 32.20  ? 211 ILE B CB  1 
ATOM   3362 C CG1 . ILE B 1 212 ? 46.033  9.554   27.596 1.00 34.43  ? 211 ILE B CG1 1 
ATOM   3363 C CG2 . ILE B 1 212 ? 47.763  8.080   26.515 1.00 23.56  ? 211 ILE B CG2 1 
ATOM   3364 C CD1 . ILE B 1 212 ? 46.813  10.737  28.096 1.00 17.88  ? 211 ILE B CD1 1 
ATOM   3365 N N   . VAL B 1 213 ? 47.040  5.007   27.892 1.00 36.60  ? 212 VAL B N   1 
ATOM   3366 C CA  . VAL B 1 213 ? 47.722  3.760   27.558 1.00 35.02  ? 212 VAL B CA  1 
ATOM   3367 C C   . VAL B 1 213 ? 46.712  2.739   27.056 1.00 33.38  ? 212 VAL B C   1 
ATOM   3368 O O   . VAL B 1 213 ? 46.829  2.256   25.928 1.00 44.37  ? 212 VAL B O   1 
ATOM   3369 C CB  . VAL B 1 213 ? 48.533  3.217   28.750 1.00 37.69  ? 212 VAL B CB  1 
ATOM   3370 C CG1 . VAL B 1 213 ? 49.139  1.858   28.429 1.00 28.53  ? 212 VAL B CG1 1 
ATOM   3371 C CG2 . VAL B 1 213 ? 49.643  4.191   29.131 1.00 24.68  ? 212 VAL B CG2 1 
ATOM   3372 N N   . GLY B 1 214 ? 45.691  2.425   27.848 1.00 28.01  ? 213 GLY B N   1 
ATOM   3373 C CA  . GLY B 1 214 ? 44.662  1.507   27.366 1.00 32.26  ? 213 GLY B CA  1 
ATOM   3374 C C   . GLY B 1 214 ? 44.054  1.917   26.037 1.00 27.37  ? 213 GLY B C   1 
ATOM   3375 O O   . GLY B 1 214 ? 43.907  1.092   25.127 1.00 31.84  ? 213 GLY B O   1 
ATOM   3376 N N   . ALA B 1 215 ? 43.699  3.187   25.877 1.00 25.12  ? 214 ALA B N   1 
ATOM   3377 C CA  . ALA B 1 215 ? 43.292  3.714   24.575 1.00 37.82  ? 214 ALA B CA  1 
ATOM   3378 C C   . ALA B 1 215 ? 44.290  3.385   23.465 1.00 42.23  ? 214 ALA B C   1 
ATOM   3379 O O   . ALA B 1 215 ? 43.996  2.759   22.440 1.00 33.47  ? 214 ALA B O   1 
ATOM   3380 C CB  . ALA B 1 215 ? 43.119  5.230   24.643 1.00 30.17  ? 214 ALA B CB  1 
ATOM   3381 N N   . VAL B 1 216 ? 45.523  3.850   23.679 1.00 36.92  ? 215 VAL B N   1 
ATOM   3382 C CA  . VAL B 1 216 ? 46.572  3.586   22.692 1.00 29.00  ? 215 VAL B CA  1 
ATOM   3383 C C   . VAL B 1 216 ? 46.715  2.102   22.418 1.00 29.59  ? 215 VAL B C   1 
ATOM   3384 O O   . VAL B 1 216 ? 46.765  1.704   21.249 1.00 57.49  ? 215 VAL B O   1 
ATOM   3385 C CB  . VAL B 1 216 ? 47.885  4.225   23.176 1.00 28.99  ? 215 VAL B CB  1 
ATOM   3386 C CG1 . VAL B 1 216 ? 49.079  3.732   22.385 1.00 37.84  ? 215 VAL B CG1 1 
ATOM   3387 C CG2 . VAL B 1 216 ? 47.728  5.741   23.072 1.00 28.45  ? 215 VAL B CG2 1 
ATOM   3388 N N   . LEU B 1 217 ? 46.773  1.241   23.427 1.00 34.78  ? 216 LEU B N   1 
ATOM   3389 C CA  . LEU B 1 217 ? 46.882  -0.198  23.180 1.00 35.32  ? 216 LEU B CA  1 
ATOM   3390 C C   . LEU B 1 217 ? 45.779  -0.708  22.261 1.00 31.98  ? 216 LEU B C   1 
ATOM   3391 O O   . LEU B 1 217 ? 45.971  -1.558  21.394 1.00 38.06  ? 216 LEU B O   1 
ATOM   3392 C CB  . LEU B 1 217 ? 46.804  -0.985  24.487 1.00 40.65  ? 216 LEU B CB  1 
ATOM   3393 C CG  . LEU B 1 217 ? 48.026  -1.056  25.397 1.00 49.85  ? 216 LEU B CG  1 
ATOM   3394 C CD1 . LEU B 1 217 ? 48.741  0.281   25.483 1.00 45.07  ? 216 LEU B CD1 1 
ATOM   3395 C CD2 . LEU B 1 217 ? 47.641  -1.522  26.801 1.00 46.32  ? 216 LEU B CD2 1 
ATOM   3396 N N   . ALA B 1 218 ? 44.567  -0.184  22.461 1.00 30.13  ? 217 ALA B N   1 
ATOM   3397 C CA  . ALA B 1 218 ? 43.457  -0.661  21.638 1.00 39.79  ? 217 ALA B CA  1 
ATOM   3398 C C   . ALA B 1 218 ? 43.580  -0.168  20.204 1.00 37.80  ? 217 ALA B C   1 
ATOM   3399 O O   . ALA B 1 218 ? 43.114  -0.779  19.240 1.00 47.43  ? 217 ALA B O   1 
ATOM   3400 C CB  . ALA B 1 218 ? 42.125  -0.236  22.239 1.00 45.51  ? 217 ALA B CB  1 
ATOM   3401 N N   . ALA B 1 219 ? 44.233  0.980   20.041 1.00 42.12  ? 218 ALA B N   1 
ATOM   3402 C CA  . ALA B 1 219 ? 44.483  1.464   18.682 1.00 32.03  ? 218 ALA B CA  1 
ATOM   3403 C C   . ALA B 1 219 ? 45.439  0.525   17.957 1.00 33.90  ? 218 ALA B C   1 
ATOM   3404 O O   . ALA B 1 219 ? 45.190  0.103   16.823 1.00 48.21  ? 218 ALA B O   1 
ATOM   3405 C CB  . ALA B 1 219 ? 45.041  2.867   18.745 1.00 34.20  ? 218 ALA B CB  1 
ATOM   3406 N N   . ILE B 1 220 ? 46.536  0.224   18.660 1.00 28.63  ? 219 ILE B N   1 
ATOM   3407 C CA  . ILE B 1 220 ? 47.571  -0.633  18.105 1.00 34.17  ? 219 ILE B CA  1 
ATOM   3408 C C   . ILE B 1 220 ? 47.003  -1.919  17.495 1.00 30.33  ? 219 ILE B C   1 
ATOM   3409 O O   . ILE B 1 220 ? 47.332  -2.239  16.357 1.00 31.34  ? 219 ILE B O   1 
ATOM   3410 C CB  . ILE B 1 220 ? 48.615  -1.065  19.156 1.00 38.51  ? 219 ILE B CB  1 
ATOM   3411 C CG1 . ILE B 1 220 ? 49.129  0.041   20.070 1.00 47.54  ? 219 ILE B CG1 1 
ATOM   3412 C CG2 . ILE B 1 220 ? 49.770  -1.773  18.455 1.00 49.83  ? 219 ILE B CG2 1 
ATOM   3413 C CD1 . ILE B 1 220 ? 49.636  1.283   19.386 1.00 40.38  ? 219 ILE B CD1 1 
ATOM   3414 N N   . LEU B 1 221 ? 46.198  -2.611  18.286 1.00 31.92  ? 220 LEU B N   1 
ATOM   3415 C CA  . LEU B 1 221 ? 45.576  -3.895  18.016 1.00 41.25  ? 220 LEU B CA  1 
ATOM   3416 C C   . LEU B 1 221 ? 44.503  -3.799  16.944 1.00 35.97  ? 220 LEU B C   1 
ATOM   3417 O O   . LEU B 1 221 ? 44.374  -4.596  16.019 1.00 39.07  ? 220 LEU B O   1 
ATOM   3418 C CB  . LEU B 1 221 ? 44.929  -4.456  19.297 1.00 49.74  ? 220 LEU B CB  1 
ATOM   3419 C CG  . LEU B 1 221 ? 44.446  -5.906  19.225 1.00 49.75  ? 220 LEU B CG  1 
ATOM   3420 C CD1 . LEU B 1 221 ? 45.611  -6.874  19.393 1.00 35.83  ? 220 LEU B CD1 1 
ATOM   3421 C CD2 . LEU B 1 221 ? 43.366  -6.178  20.266 1.00 49.19  ? 220 LEU B CD2 1 
ATOM   3422 N N   . TYR B 1 222 ? 43.691  -2.749  17.103 1.00 32.78  ? 221 TYR B N   1 
ATOM   3423 C CA  . TYR B 1 222 ? 42.631  -2.579  16.124 1.00 31.15  ? 221 TYR B CA  1 
ATOM   3424 C C   . TYR B 1 222 ? 43.203  -2.140  14.784 1.00 33.16  ? 221 TYR B C   1 
ATOM   3425 O O   . TYR B 1 222 ? 42.984  -2.715  13.712 1.00 26.23  ? 221 TYR B O   1 
ATOM   3426 C CB  . TYR B 1 222 ? 41.573  -1.565  16.617 1.00 24.83  ? 221 TYR B CB  1 
ATOM   3427 C CG  . TYR B 1 222 ? 40.370  -1.694  15.699 1.00 30.50  ? 221 TYR B CG  1 
ATOM   3428 C CD1 . TYR B 1 222 ? 39.466  -2.735  15.863 1.00 37.71  ? 221 TYR B CD1 1 
ATOM   3429 C CD2 . TYR B 1 222 ? 40.165  -0.798  14.663 1.00 27.91  ? 221 TYR B CD2 1 
ATOM   3430 C CE1 . TYR B 1 222 ? 38.374  -2.853  15.014 1.00 37.83  ? 221 TYR B CE1 1 
ATOM   3431 C CE2 . TYR B 1 222 ? 39.075  -0.918  13.814 1.00 25.82  ? 221 TYR B CE2 1 
ATOM   3432 C CZ  . TYR B 1 222 ? 38.183  -1.951  13.994 1.00 35.84  ? 221 TYR B CZ  1 
ATOM   3433 O OH  . TYR B 1 222 ? 37.092  -2.082  13.156 1.00 35.04  ? 221 TYR B OH  1 
ATOM   3434 N N   . PHE B 1 223 ? 43.974  -1.052  14.823 1.00 39.73  ? 222 PHE B N   1 
ATOM   3435 C CA  . PHE B 1 223 ? 44.318  -0.458  13.532 1.00 51.59  ? 222 PHE B CA  1 
ATOM   3436 C C   . PHE B 1 223 ? 45.530  -1.073  12.842 1.00 51.90  ? 222 PHE B C   1 
ATOM   3437 O O   . PHE B 1 223 ? 45.533  -0.977  11.608 1.00 36.03  ? 222 PHE B O   1 
ATOM   3438 C CB  . PHE B 1 223 ? 44.538  1.048   13.710 1.00 47.97  ? 222 PHE B CB  1 
ATOM   3439 C CG  . PHE B 1 223 ? 43.227  1.776   13.989 1.00 41.16  ? 222 PHE B CG  1 
ATOM   3440 C CD1 . PHE B 1 223 ? 42.239  1.810   13.019 1.00 29.69  ? 222 PHE B CD1 1 
ATOM   3441 C CD2 . PHE B 1 223 ? 43.036  2.394   15.213 1.00 34.88  ? 222 PHE B CD2 1 
ATOM   3442 C CE1 . PHE B 1 223 ? 41.055  2.481   13.272 1.00 27.04  ? 222 PHE B CE1 1 
ATOM   3443 C CE2 . PHE B 1 223 ? 41.864  3.081   15.471 1.00 34.82  ? 222 PHE B CE2 1 
ATOM   3444 C CZ  . PHE B 1 223 ? 40.882  3.119   14.491 1.00 36.67  ? 222 PHE B CZ  1 
ATOM   3445 N N   . TYR B 1 224 ? 46.471  -1.653  13.572 1.00 46.75  ? 223 TYR B N   1 
ATOM   3446 C CA  . TYR B 1 224 ? 47.688  -2.224  13.016 1.00 45.92  ? 223 TYR B CA  1 
ATOM   3447 C C   . TYR B 1 224 ? 47.763  -3.737  13.171 1.00 42.50  ? 223 TYR B C   1 
ATOM   3448 O O   . TYR B 1 224 ? 48.498  -4.394  12.423 1.00 36.23  ? 223 TYR B O   1 
ATOM   3449 C CB  . TYR B 1 224 ? 48.944  -1.621  13.664 1.00 56.63  ? 223 TYR B CB  1 
ATOM   3450 C CG  . TYR B 1 224 ? 48.977  -0.110  13.583 1.00 54.59  ? 223 TYR B CG  1 
ATOM   3451 C CD1 . TYR B 1 224 ? 49.486  0.658   14.617 1.00 43.30  ? 223 TYR B CD1 1 
ATOM   3452 C CD2 . TYR B 1 224 ? 48.485  0.538   12.458 1.00 50.67  ? 223 TYR B CD2 1 
ATOM   3453 C CE1 . TYR B 1 224 ? 49.502  2.037   14.521 1.00 45.07  ? 223 TYR B CE1 1 
ATOM   3454 C CE2 . TYR B 1 224 ? 48.502  1.916   12.361 1.00 45.81  ? 223 TYR B CE2 1 
ATOM   3455 C CZ  . TYR B 1 224 ? 49.015  2.660   13.398 1.00 44.08  ? 223 TYR B CZ  1 
ATOM   3456 O OH  . TYR B 1 224 ? 49.031  4.033   13.302 1.00 38.76  ? 223 TYR B OH  1 
ATOM   3457 N N   . LEU B 1 225 ? 47.021  -4.304  14.119 1.00 43.43  ? 224 LEU B N   1 
ATOM   3458 C CA  . LEU B 1 225 ? 47.094  -5.758  14.286 1.00 47.09  ? 224 LEU B CA  1 
ATOM   3459 C C   . LEU B 1 225 ? 45.914  -6.458  13.628 1.00 56.77  ? 224 LEU B C   1 
ATOM   3460 O O   . LEU B 1 225 ? 46.074  -7.408  12.849 1.00 44.59  ? 224 LEU B O   1 
ATOM   3461 C CB  . LEU B 1 225 ? 47.176  -6.135  15.771 1.00 41.27  ? 224 LEU B CB  1 
ATOM   3462 C CG  . LEU B 1 225 ? 48.605  -6.345  16.284 1.00 35.95  ? 224 LEU B CG  1 
ATOM   3463 C CD1 . LEU B 1 225 ? 49.578  -6.105  15.139 1.00 57.83  ? 224 LEU B CD1 1 
ATOM   3464 C CD2 . LEU B 1 225 ? 48.934  -5.435  17.456 1.00 46.56  ? 224 LEU B CD2 1 
ATOM   3465 N N   . LEU B 1 226 ? 44.693  -6.001  13.934 1.00 51.82  ? 225 LEU B N   1 
ATOM   3466 C CA  . LEU B 1 226 ? 43.559  -6.767  13.413 1.00 43.94  ? 225 LEU B CA  1 
ATOM   3467 C C   . LEU B 1 226 ? 43.050  -6.255  12.075 1.00 38.91  ? 225 LEU B C   1 
ATOM   3468 O O   . LEU B 1 226 ? 42.793  -7.063  11.174 1.00 34.48  ? 225 LEU B O   1 
ATOM   3469 C CB  . LEU B 1 226 ? 42.402  -6.758  14.408 1.00 43.76  ? 225 LEU B CB  1 
ATOM   3470 C CG  . LEU B 1 226 ? 42.651  -7.271  15.828 1.00 37.52  ? 225 LEU B CG  1 
ATOM   3471 C CD1 . LEU B 1 226 ? 41.543  -6.710  16.710 1.00 39.59  ? 225 LEU B CD1 1 
ATOM   3472 C CD2 . LEU B 1 226 ? 42.719  -8.789  15.891 1.00 17.30  ? 225 LEU B CD2 1 
ATOM   3473 N N   . PHE B 1 227 ? 42.884  -4.942  11.918 1.00 39.48  ? 226 PHE B N   1 
ATOM   3474 C CA  . PHE B 1 227 ? 42.259  -4.461  10.678 1.00 49.35  ? 226 PHE B CA  1 
ATOM   3475 C C   . PHE B 1 227 ? 43.081  -3.378  9.994  1.00 48.81  ? 226 PHE B C   1 
ATOM   3476 O O   . PHE B 1 227 ? 42.575  -2.279  9.733  1.00 53.26  ? 226 PHE B O   1 
ATOM   3477 C CB  . PHE B 1 227 ? 40.847  -3.933  10.971 1.00 44.98  ? 226 PHE B CB  1 
ATOM   3478 C CG  . PHE B 1 227 ? 39.869  -5.008  11.417 1.00 47.95  ? 226 PHE B CG  1 
ATOM   3479 C CD1 . PHE B 1 227 ? 39.519  -5.128  12.758 1.00 47.54  ? 226 PHE B CD1 1 
ATOM   3480 C CD2 . PHE B 1 227 ? 39.323  -5.887  10.501 1.00 38.68  ? 226 PHE B CD2 1 
ATOM   3481 C CE1 . PHE B 1 227 ? 38.646  -6.099  13.206 1.00 33.20  ? 226 PHE B CE1 1 
ATOM   3482 C CE2 . PHE B 1 227 ? 38.442  -6.857  10.939 1.00 41.25  ? 226 PHE B CE2 1 
ATOM   3483 C CZ  . PHE B 1 227 ? 38.103  -6.974  12.278 1.00 42.94  ? 226 PHE B CZ  1 
ATOM   3484 N N   . PRO B 1 228 ? 44.344  -3.644  9.692  1.00 45.23  ? 227 PRO B N   1 
ATOM   3485 C CA  . PRO B 1 228 ? 45.185  -2.596  9.093  1.00 37.37  ? 227 PRO B CA  1 
ATOM   3486 C C   . PRO B 1 228 ? 44.577  -2.072  7.790  1.00 28.39  ? 227 PRO B C   1 
ATOM   3487 O O   . PRO B 1 228 ? 43.877  -2.820  7.104  1.00 42.30  ? 227 PRO B O   1 
ATOM   3488 C CB  . PRO B 1 228 ? 46.516  -3.299  8.835  1.00 38.77  ? 227 PRO B CB  1 
ATOM   3489 C CG  . PRO B 1 228 ? 46.221  -4.758  8.893  1.00 40.67  ? 227 PRO B CG  1 
ATOM   3490 C CD  . PRO B 1 228 ? 45.081  -4.901  9.865  1.00 45.68  ? 227 PRO B CD  1 
ATOM   3491 N N   . ASN B 1 229 ? 44.840  -0.813  7.486  1.00 25.39  ? 228 ASN B N   1 
ATOM   3492 C CA  . ASN B 1 229 ? 44.451  -0.126  6.264  1.00 41.74  ? 228 ASN B CA  1 
ATOM   3493 C C   . ASN B 1 229 ? 45.529  -0.303  5.196  1.00 60.95  ? 228 ASN B C   1 
ATOM   3494 O O   . ASN B 1 229 ? 46.596  -0.879  5.440  1.00 63.55  ? 228 ASN B O   1 
ATOM   3495 C CB  . ASN B 1 229 ? 44.182  1.356   6.542  1.00 32.75  ? 228 ASN B CB  1 
ATOM   3496 C CG  . ASN B 1 229 ? 45.299  2.015   7.327  1.00 49.33  ? 228 ASN B CG  1 
ATOM   3497 O OD1 . ASN B 1 229 ? 46.409  1.483   7.397  1.00 80.25  ? 228 ASN B OD1 1 
ATOM   3498 N ND2 . ASN B 1 229 ? 45.048  3.205   7.868  1.00 58.45  ? 228 ASN B ND2 1 
ATOM   3499 N N   . SER B 1 230 ? 45.309  0.169   3.964  1.00 67.54  ? 229 SER B N   1 
ATOM   3500 C CA  . SER B 1 230 ? 46.363  -0.064  2.973  1.00 75.28  ? 229 SER B CA  1 
ATOM   3501 C C   . SER B 1 230 ? 47.032  1.232   2.521  1.00 69.04  ? 229 SER B C   1 
ATOM   3502 O O   . SER B 1 230 ? 47.725  1.221   1.503  1.00 69.49  ? 229 SER B O   1 
ATOM   3503 C CB  . SER B 1 230 ? 45.806  -0.803  1.751  1.00 85.03  ? 229 SER B CB  1 
ATOM   3504 O OG  . SER B 1 230 ? 46.864  -1.456  1.042  1.00 97.83  ? 229 SER B OG  1 
ATOM   3505 N N   . LEU B 1 231 ? 46.808  2.290   3.274  1.00 63.75  ? 230 LEU B N   1 
ATOM   3506 C CA  . LEU B 1 231 ? 47.355  3.617   3.087  1.00 59.61  ? 230 LEU B CA  1 
ATOM   3507 C C   . LEU B 1 231 ? 48.836  3.495   2.692  1.00 61.90  ? 230 LEU B C   1 
ATOM   3508 O O   . LEU B 1 231 ? 49.563  2.599   3.111  1.00 54.81  ? 230 LEU B O   1 
ATOM   3509 C CB  . LEU B 1 231 ? 47.303  4.526   4.287  1.00 62.14  ? 230 LEU B CB  1 
ATOM   3510 C CG  . LEU B 1 231 ? 46.270  4.693   5.376  1.00 74.62  ? 230 LEU B CG  1 
ATOM   3511 C CD1 . LEU B 1 231 ? 45.446  5.989   5.093  1.00 94.74  ? 230 LEU B CD1 1 
ATOM   3512 C CD2 . LEU B 1 231 ? 45.288  3.545   5.525  1.00 81.57  ? 230 LEU B CD2 1 
ATOM   3513 N N   . SER B 1 232 ? 49.271  4.432   1.854  1.00 60.13  ? 231 SER B N   1 
ATOM   3514 C CA  . SER B 1 232 ? 50.659  4.368   1.421  1.00 63.69  ? 231 SER B CA  1 
ATOM   3515 C C   . SER B 1 232 ? 51.554  4.768   2.594  1.00 61.15  ? 231 SER B C   1 
ATOM   3516 O O   . SER B 1 232 ? 51.100  5.500   3.467  1.00 66.84  ? 231 SER B O   1 
ATOM   3517 C CB  . SER B 1 232 ? 50.951  5.257   0.215  1.00 62.94  ? 231 SER B CB  1 
ATOM   3518 O OG  . SER B 1 232 ? 52.192  4.895   -0.366 1.00 64.98  ? 231 SER B OG  1 
ATOM   3519 N N   . LEU B 1 233 ? 52.769  4.262   2.530  1.00 60.98  ? 232 LEU B N   1 
ATOM   3520 C CA  . LEU B 1 233 ? 53.810  4.595   3.492  1.00 66.23  ? 232 LEU B CA  1 
ATOM   3521 C C   . LEU B 1 233 ? 53.815  6.102   3.728  1.00 72.26  ? 232 LEU B C   1 
ATOM   3522 O O   . LEU B 1 233 ? 53.887  6.575   4.866  1.00 93.40  ? 232 LEU B O   1 
ATOM   3523 C CB  . LEU B 1 233 ? 55.132  4.058   2.957  1.00 72.62  ? 232 LEU B CB  1 
ATOM   3524 C CG  . LEU B 1 233 ? 56.410  4.692   3.503  1.00 87.23  ? 232 LEU B CG  1 
ATOM   3525 C CD1 . LEU B 1 233 ? 57.488  3.640   3.710  1.00 107.63 ? 232 LEU B CD1 1 
ATOM   3526 C CD2 . LEU B 1 233 ? 56.886  5.794   2.561  1.00 98.35  ? 232 LEU B CD2 1 
ATOM   3527 N N   . SER B 1 234 ? 53.701  6.858   2.643  1.00 71.99  ? 233 SER B N   1 
ATOM   3528 C CA  . SER B 1 234 ? 53.634  8.310   2.664  1.00 69.53  ? 233 SER B CA  1 
ATOM   3529 C C   . SER B 1 234 ? 52.229  8.809   2.974  1.00 65.39  ? 233 SER B C   1 
ATOM   3530 O O   . SER B 1 234 ? 52.041  9.865   3.582  1.00 67.48  ? 233 SER B O   1 
ATOM   3531 C CB  . SER B 1 234 ? 54.077  8.877   1.310  1.00 72.51  ? 233 SER B CB  1 
ATOM   3532 O OG  . SER B 1 234 ? 53.801  7.948   0.268  1.00 91.21  ? 233 SER B OG  1 
ATOM   3533 N N   . GLU B 1 235 ? 51.227  8.039   2.550  1.00 58.09  ? 234 GLU B N   1 
ATOM   3534 C CA  . GLU B 1 235 ? 49.837  8.425   2.776  1.00 57.06  ? 234 GLU B CA  1 
ATOM   3535 C C   . GLU B 1 235 ? 49.616  8.655   4.272  1.00 48.88  ? 234 GLU B C   1 
ATOM   3536 O O   . GLU B 1 235 ? 48.838  9.525   4.654  1.00 69.20  ? 234 GLU B O   1 
ATOM   3537 C CB  . GLU B 1 235 ? 48.872  7.377   2.232  1.00 63.72  ? 234 GLU B CB  1 
ATOM   3538 C CG  . GLU B 1 235 ? 48.502  7.503   0.764  1.00 62.61  ? 234 GLU B CG  1 
ATOM   3539 C CD  . GLU B 1 235 ? 47.575  6.420   0.252  1.00 66.21  ? 234 GLU B CD  1 
ATOM   3540 O OE1 . GLU B 1 235 ? 46.340  6.621   0.192  1.00 76.81  ? 234 GLU B OE1 1 
ATOM   3541 O OE2 . GLU B 1 235 ? 48.047  5.326   -0.129 1.00 81.35  ? 234 GLU B OE2 1 
ATOM   3542 N N   . ARG B 1 236 ? 50.318  7.875   5.080  1.00 42.40  ? 235 ARG B N   1 
ATOM   3543 C CA  . ARG B 1 236 ? 50.324  7.940   6.527  1.00 35.06  ? 235 ARG B CA  1 
ATOM   3544 C C   . ARG B 1 236 ? 50.848  9.276   7.022  1.00 44.05  ? 235 ARG B C   1 
ATOM   3545 O O   . ARG B 1 236 ? 50.311  9.882   7.951  1.00 49.47  ? 235 ARG B O   1 
ATOM   3546 C CB  . ARG B 1 236 ? 51.176  6.813   7.120  1.00 43.15  ? 235 ARG B CB  1 
ATOM   3547 C CG  . ARG B 1 236 ? 50.713  5.415   6.749  1.00 56.65  ? 235 ARG B CG  1 
ATOM   3548 C CD  . ARG B 1 236 ? 51.170  4.385   7.780  1.00 74.70  ? 235 ARG B CD  1 
ATOM   3549 N NE  . ARG B 1 236 ? 50.150  3.362   8.021  1.00 92.03  ? 235 ARG B NE  1 
ATOM   3550 C CZ  . ARG B 1 236 ? 49.898  2.341   7.212  1.00 100.22 ? 235 ARG B CZ  1 
ATOM   3551 N NH1 . ARG B 1 236 ? 50.594  2.201   6.099  1.00 125.96 ? 235 ARG B NH1 1 
ATOM   3552 N NH2 . ARG B 1 236 ? 48.957  1.449   7.494  1.00 89.70  ? 235 ARG B NH2 1 
ATOM   3553 N N   . VAL B 1 237 ? 51.931  9.750   6.405  1.00 48.98  ? 236 VAL B N   1 
ATOM   3554 C CA  . VAL B 1 237 ? 52.514  11.013  6.888  1.00 46.09  ? 236 VAL B CA  1 
ATOM   3555 C C   . VAL B 1 237 ? 51.521  12.148  6.646  1.00 39.78  ? 236 VAL B C   1 
ATOM   3556 O O   . VAL B 1 237 ? 51.357  13.048  7.476  1.00 37.02  ? 236 VAL B O   1 
ATOM   3557 C CB  . VAL B 1 237 ? 53.876  11.235  6.225  1.00 52.70  ? 236 VAL B CB  1 
ATOM   3558 C CG1 . VAL B 1 237 ? 54.683  9.937   6.233  1.00 34.08  ? 236 VAL B CG1 1 
ATOM   3559 C CG2 . VAL B 1 237 ? 53.748  11.723  4.793  1.00 69.40  ? 236 VAL B CG2 1 
ATOM   3560 N N   . ALA B 1 238 ? 50.857  12.048  5.507  1.00 37.43  ? 237 ALA B N   1 
ATOM   3561 C CA  . ALA B 1 238 ? 49.827  12.923  4.994  1.00 37.75  ? 237 ALA B CA  1 
ATOM   3562 C C   . ALA B 1 238 ? 48.638  13.009  5.935  1.00 40.66  ? 237 ALA B C   1 
ATOM   3563 O O   . ALA B 1 238 ? 48.052  14.084  6.066  1.00 49.05  ? 237 ALA B O   1 
ATOM   3564 C CB  . ALA B 1 238 ? 49.341  12.464  3.618  1.00 38.29  ? 237 ALA B CB  1 
ATOM   3565 N N   . ILE B 1 239 ? 48.273  11.902  6.587  1.00 48.88  ? 238 ILE B N   1 
ATOM   3566 C CA  . ILE B 1 239 ? 47.176  12.023  7.558  1.00 54.75  ? 238 ILE B CA  1 
ATOM   3567 C C   . ILE B 1 239 ? 47.711  12.614  8.863  1.00 42.70  ? 238 ILE B C   1 
ATOM   3568 O O   . ILE B 1 239 ? 46.952  13.203  9.628  1.00 38.32  ? 238 ILE B O   1 
ATOM   3569 C CB  . ILE B 1 239 ? 46.452  10.698  7.808  1.00 61.96  ? 238 ILE B CB  1 
ATOM   3570 C CG1 . ILE B 1 239 ? 47.303  9.432   7.687  1.00 62.07  ? 238 ILE B CG1 1 
ATOM   3571 C CG2 . ILE B 1 239 ? 45.245  10.566  6.874  1.00 71.09  ? 238 ILE B CG2 1 
ATOM   3572 C CD1 . ILE B 1 239 ? 46.562  8.344   6.939  1.00 49.10  ? 238 ILE B CD1 1 
ATOM   3573 N N   . ILE B 1 240 ? 49.011  12.471  9.093  1.00 35.58  ? 239 ILE B N   1 
ATOM   3574 C CA  . ILE B 1 240 ? 49.696  13.074  10.218 1.00 35.60  ? 239 ILE B CA  1 
ATOM   3575 C C   . ILE B 1 240 ? 49.819  14.589  10.080 1.00 54.60  ? 239 ILE B C   1 
ATOM   3576 O O   . ILE B 1 240 ? 49.841  15.349  11.050 1.00 54.08  ? 239 ILE B O   1 
ATOM   3577 C CB  . ILE B 1 240 ? 51.142  12.558  10.361 1.00 33.65  ? 239 ILE B CB  1 
ATOM   3578 C CG1 . ILE B 1 240 ? 51.304  11.047  10.294 1.00 35.84  ? 239 ILE B CG1 1 
ATOM   3579 C CG2 . ILE B 1 240 ? 51.759  13.113  11.642 1.00 42.33  ? 239 ILE B CG2 1 
ATOM   3580 C CD1 . ILE B 1 240 ? 52.475  10.546  11.112 1.00 32.62  ? 239 ILE B CD1 1 
ATOM   3581 N N   . LYS B 1 241 ? 49.941  15.017  8.826  1.00 65.73  ? 240 LYS B N   1 
ATOM   3582 C CA  . LYS B 1 241 ? 50.154  16.441  8.572  1.00 80.13  ? 240 LYS B CA  1 
ATOM   3583 C C   . LYS B 1 241 ? 48.841  17.141  8.270  1.00 76.67  ? 240 LYS B C   1 
ATOM   3584 O O   . LYS B 1 241 ? 48.699  18.329  8.560  1.00 92.12  ? 240 LYS B O   1 
ATOM   3585 C CB  . LYS B 1 241 ? 51.157  16.614  7.430  1.00 98.29  ? 240 LYS B CB  1 
ATOM   3586 C CG  . LYS B 1 241 ? 52.428  15.796  7.642  1.00 112.57 ? 240 LYS B CG  1 
ATOM   3587 C CD  . LYS B 1 241 ? 52.867  15.112  6.351  1.00 122.13 ? 240 LYS B CD  1 
ATOM   3588 C CE  . LYS B 1 241 ? 52.568  16.014  5.114  1.00 129.05 ? 240 LYS B CE  1 
ATOM   3589 N NZ  . LYS B 1 241 ? 53.782  16.075  4.079  1.00 146.09 ? 240 LYS B NZ  1 
ATOM   3590 N N   . GLY B 1 242 ? 47.877  16.409  7.728  1.00 72.91  ? 241 GLY B N   1 
ATOM   3591 C CA  . GLY B 1 242 ? 46.557  16.974  7.490  1.00 67.98  ? 241 GLY B CA  1 
ATOM   3592 C C   . GLY B 1 242 ? 46.344  17.308  6.027  1.00 63.44  ? 241 GLY B C   1 
ATOM   3593 O O   . GLY B 1 242 ? 45.410  18.021  5.669  1.00 61.44  ? 241 GLY B O   1 
ATOM   3594 N N   . THR B 1 243 ? 47.223  16.774  5.183  1.00 60.30  ? 242 THR B N   1 
ATOM   3595 C CA  . THR B 1 243 ? 47.142  16.977  3.746  1.00 49.73  ? 242 THR B CA  1 
ATOM   3596 C C   . THR B 1 243 ? 46.618  15.732  3.040  1.00 50.78  ? 242 THR B C   1 
ATOM   3597 O O   . THR B 1 243 ? 46.328  15.826  1.848  1.00 57.37  ? 242 THR B O   1 
ATOM   3598 C CB  . THR B 1 243 ? 48.511  17.344  3.146  1.00 41.71  ? 242 THR B CB  1 
ATOM   3599 O OG1 . THR B 1 243 ? 49.341  16.177  3.149  1.00 48.90  ? 242 THR B OG1 1 
ATOM   3600 C CG2 . THR B 1 243 ? 49.200  18.392  4.004  1.00 36.16  ? 242 THR B CG2 1 
ATOM   3601 N N   . TYR B 1 244 ? 46.503  14.613  3.756  1.00 54.49  ? 243 TYR B N   1 
ATOM   3602 C CA  . TYR B 1 244 ? 45.989  13.388  3.151  1.00 55.30  ? 243 TYR B CA  1 
ATOM   3603 C C   . TYR B 1 244 ? 44.597  13.686  2.566  1.00 58.44  ? 243 TYR B C   1 
ATOM   3604 O O   . TYR B 1 244 ? 43.847  14.441  3.175  1.00 44.14  ? 243 TYR B O   1 
ATOM   3605 C CB  . TYR B 1 244 ? 45.920  12.194  4.096  1.00 55.64  ? 243 TYR B CB  1 
ATOM   3606 C CG  . TYR B 1 244 ? 45.158  10.990  3.574  1.00 51.48  ? 243 TYR B CG  1 
ATOM   3607 C CD1 . TYR B 1 244 ? 45.768  10.043  2.757  1.00 52.33  ? 243 TYR B CD1 1 
ATOM   3608 C CD2 . TYR B 1 244 ? 43.820  10.775  3.887  1.00 52.77  ? 243 TYR B CD2 1 
ATOM   3609 C CE1 . TYR B 1 244 ? 45.074  8.941   2.279  1.00 51.29  ? 243 TYR B CE1 1 
ATOM   3610 C CE2 . TYR B 1 244 ? 43.114  9.687   3.418  1.00 48.56  ? 243 TYR B CE2 1 
ATOM   3611 C CZ  . TYR B 1 244 ? 43.747  8.767   2.610  1.00 48.48  ? 243 TYR B CZ  1 
ATOM   3612 O OH  . TYR B 1 244 ? 43.032  7.687   2.150  1.00 47.14  ? 243 TYR B OH  1 
ATOM   3613 N N   . GLU B 1 245 ? 44.382  13.052  1.436  1.00 65.28  ? 244 GLU B N   1 
ATOM   3614 C CA  . GLU B 1 245 ? 43.289  13.110  0.499  1.00 68.43  ? 244 GLU B CA  1 
ATOM   3615 C C   . GLU B 1 245 ? 43.089  11.748  -0.166 1.00 65.88  ? 244 GLU B C   1 
ATOM   3616 O O   . GLU B 1 245 ? 43.932  11.237  -0.905 1.00 62.15  ? 244 GLU B O   1 
ATOM   3617 C CB  . GLU B 1 245 ? 43.558  14.157  -0.579 1.00 74.66  ? 244 GLU B CB  1 
ATOM   3618 C CG  . GLU B 1 245 ? 42.345  14.976  -0.994 1.00 78.00  ? 244 GLU B CG  1 
ATOM   3619 C CD  . GLU B 1 245 ? 42.656  16.462  -0.935 1.00 85.50  ? 244 GLU B CD  1 
ATOM   3620 O OE1 . GLU B 1 245 ? 43.677  16.800  -0.268 1.00 91.02  ? 244 GLU B OE1 1 
ATOM   3621 O OE2 . GLU B 1 245 ? 41.940  17.299  -1.522 1.00 98.07  ? 244 GLU B OE2 1 
ATOM   3622 N N   . PRO B 1 246 ? 41.945  11.164  0.127  1.00 62.05  ? 245 PRO B N   1 
ATOM   3623 C CA  . PRO B 1 246 ? 41.608  9.817   -0.342 1.00 69.17  ? 245 PRO B CA  1 
ATOM   3624 C C   . PRO B 1 246 ? 40.692  9.812   -1.557 1.00 74.08  ? 245 PRO B C   1 
ATOM   3625 O O   . PRO B 1 246 ? 39.734  9.025   -1.622 0.21 71.91  ? 245 PRO B O   1 
ATOM   3626 C CB  . PRO B 1 246 ? 40.874  9.278   0.898  1.00 64.76  ? 245 PRO B CB  1 
ATOM   3627 C CG  . PRO B 1 246 ? 40.172  10.466  1.464  1.00 57.91  ? 245 PRO B CG  1 
ATOM   3628 C CD  . PRO B 1 246 ? 40.869  11.706  0.973  1.00 59.37  ? 245 PRO B CD  1 
ATOM   3629 N N   . LYS C 1 4   ? 43.849  -25.295 5.040  1.00 63.51  ? 3   LYS C N   1 
ATOM   3630 C CA  . LYS C 1 4   ? 42.693  -25.337 5.915  1.00 49.36  ? 3   LYS C CA  1 
ATOM   3631 C C   . LYS C 1 4   ? 42.526  -24.053 6.714  1.00 45.49  ? 3   LYS C C   1 
ATOM   3632 O O   . LYS C 1 4   ? 42.906  -22.954 6.316  1.00 54.55  ? 3   LYS C O   1 
ATOM   3633 C CB  . LYS C 1 4   ? 42.842  -26.520 6.875  1.00 55.18  ? 3   LYS C CB  1 
ATOM   3634 C CG  . LYS C 1 4   ? 41.547  -27.334 6.999  1.00 50.43  ? 3   LYS C CG  1 
ATOM   3635 C CD  . LYS C 1 4   ? 41.705  -28.294 8.177  1.00 51.96  ? 3   LYS C CD  1 
ATOM   3636 C CE  . LYS C 1 4   ? 43.103  -28.148 8.768  1.00 56.26  ? 3   LYS C CE  1 
ATOM   3637 N NZ  . LYS C 1 4   ? 44.087  -29.082 8.147  1.00 62.63  ? 3   LYS C NZ  1 
ATOM   3638 N N   . GLU C 1 5   ? 41.933  -24.188 7.900  1.00 53.00  ? 4   GLU C N   1 
ATOM   3639 C CA  . GLU C 1 5   ? 41.807  -23.011 8.754  1.00 52.23  ? 4   GLU C CA  1 
ATOM   3640 C C   . GLU C 1 5   ? 43.126  -22.813 9.508  1.00 48.71  ? 4   GLU C C   1 
ATOM   3641 O O   . GLU C 1 5   ? 44.067  -22.397 8.838  1.00 85.68  ? 4   GLU C O   1 
ATOM   3642 C CB  . GLU C 1 5   ? 40.654  -23.131 9.740  1.00 59.79  ? 4   GLU C CB  1 
ATOM   3643 C CG  . GLU C 1 5   ? 39.317  -23.423 9.064  1.00 51.77  ? 4   GLU C CG  1 
ATOM   3644 C CD  . GLU C 1 5   ? 38.260  -23.730 10.113 1.00 42.96  ? 4   GLU C CD  1 
ATOM   3645 O OE1 . GLU C 1 5   ? 38.641  -24.238 11.186 1.00 50.14  ? 4   GLU C OE1 1 
ATOM   3646 O OE2 . GLU C 1 5   ? 37.081  -23.451 9.833  1.00 34.86  ? 4   GLU C OE2 1 
ATOM   3647 N N   . VAL C 1 6   ? 43.095  -23.127 10.780 1.00 43.16  ? 5   VAL C N   1 
ATOM   3648 C CA  . VAL C 1 6   ? 44.131  -23.043 11.782 1.00 57.31  ? 5   VAL C CA  1 
ATOM   3649 C C   . VAL C 1 6   ? 45.313  -22.185 11.333 1.00 62.26  ? 5   VAL C C   1 
ATOM   3650 O O   . VAL C 1 6   ? 45.552  -21.088 11.829 1.00 50.96  ? 5   VAL C O   1 
ATOM   3651 C CB  . VAL C 1 6   ? 44.686  -24.441 12.137 1.00 65.93  ? 5   VAL C CB  1 
ATOM   3652 C CG1 . VAL C 1 6   ? 45.616  -24.339 13.340 1.00 70.94  ? 5   VAL C CG1 1 
ATOM   3653 C CG2 . VAL C 1 6   ? 43.539  -25.407 12.370 1.00 65.18  ? 5   VAL C CG2 1 
ATOM   3654 N N   . CYS C 1 7   ? 45.997  -22.786 10.374 1.00 71.63  ? 6   CYS C N   1 
ATOM   3655 C CA  . CYS C 1 7   ? 47.098  -22.242 9.600  1.00 70.62  ? 6   CYS C CA  1 
ATOM   3656 C C   . CYS C 1 7   ? 46.570  -21.167 8.649  1.00 62.79  ? 6   CYS C C   1 
ATOM   3657 O O   . CYS C 1 7   ? 46.446  -21.373 7.443  1.00 74.80  ? 6   CYS C O   1 
ATOM   3658 C CB  . CYS C 1 7   ? 47.810  -23.394 8.883  1.00 75.25  ? 6   CYS C CB  1 
ATOM   3659 S SG  . CYS C 1 7   ? 48.331  -24.699 10.049 1.00 142.57 ? 6   CYS C SG  1 
ATOM   3660 N N   . SER C 1 8   ? 46.258  -20.053 9.285  1.00 49.37  ? 7   SER C N   1 
ATOM   3661 C CA  . SER C 1 8   ? 45.713  -18.817 8.774  1.00 50.84  ? 7   SER C CA  1 
ATOM   3662 C C   . SER C 1 8   ? 45.870  -17.703 9.815  1.00 51.52  ? 7   SER C C   1 
ATOM   3663 O O   . SER C 1 8   ? 45.816  -17.904 11.030 1.00 59.47  ? 7   SER C O   1 
ATOM   3664 C CB  . SER C 1 8   ? 44.249  -18.970 8.368  1.00 55.11  ? 7   SER C CB  1 
ATOM   3665 O OG  . SER C 1 8   ? 43.398  -18.013 8.969  1.00 65.39  ? 7   SER C OG  1 
ATOM   3666 N N   . VAL C 1 9   ? 46.091  -16.496 9.300  1.00 44.44  ? 8   VAL C N   1 
ATOM   3667 C CA  . VAL C 1 9   ? 46.213  -15.348 10.196 1.00 51.22  ? 8   VAL C CA  1 
ATOM   3668 C C   . VAL C 1 9   ? 44.809  -14.916 10.626 1.00 46.37  ? 8   VAL C C   1 
ATOM   3669 O O   . VAL C 1 9   ? 44.650  -14.231 11.627 1.00 41.42  ? 8   VAL C O   1 
ATOM   3670 C CB  . VAL C 1 9   ? 46.960  -14.191 9.523  1.00 54.28  ? 8   VAL C CB  1 
ATOM   3671 C CG1 . VAL C 1 9   ? 45.977  -13.130 9.056  1.00 40.79  ? 8   VAL C CG1 1 
ATOM   3672 C CG2 . VAL C 1 9   ? 47.992  -13.596 10.468 1.00 71.96  ? 8   VAL C CG2 1 
ATOM   3673 N N   . ALA C 1 10  ? 43.845  -15.352 9.830  1.00 39.71  ? 9   ALA C N   1 
ATOM   3674 C CA  . ALA C 1 10  ? 42.422  -15.173 10.008 1.00 39.60  ? 9   ALA C CA  1 
ATOM   3675 C C   . ALA C 1 10  ? 41.917  -15.990 11.197 1.00 44.50  ? 9   ALA C C   1 
ATOM   3676 O O   . ALA C 1 10  ? 41.324  -15.464 12.138 1.00 35.31  ? 9   ALA C O   1 
ATOM   3677 C CB  . ALA C 1 10  ? 41.665  -15.593 8.756  1.00 38.40  ? 9   ALA C CB  1 
ATOM   3678 N N   . PHE C 1 11  ? 42.162  -17.294 11.121 1.00 40.92  ? 10  PHE C N   1 
ATOM   3679 C CA  . PHE C 1 11  ? 41.743  -18.191 12.202 1.00 42.96  ? 10  PHE C CA  1 
ATOM   3680 C C   . PHE C 1 11  ? 42.565  -17.914 13.452 1.00 50.98  ? 10  PHE C C   1 
ATOM   3681 O O   . PHE C 1 11  ? 42.089  -18.009 14.585 1.00 56.53  ? 10  PHE C O   1 
ATOM   3682 C CB  . PHE C 1 11  ? 41.865  -19.623 11.718 1.00 44.34  ? 10  PHE C CB  1 
ATOM   3683 C CG  . PHE C 1 11  ? 41.357  -20.725 12.624 1.00 47.37  ? 10  PHE C CG  1 
ATOM   3684 C CD1 . PHE C 1 11  ? 40.107  -21.291 12.416 1.00 46.85  ? 10  PHE C CD1 1 
ATOM   3685 C CD2 . PHE C 1 11  ? 42.143  -21.189 13.668 1.00 33.83  ? 10  PHE C CD2 1 
ATOM   3686 C CE1 . PHE C 1 11  ? 39.636  -22.308 13.223 1.00 43.61  ? 10  PHE C CE1 1 
ATOM   3687 C CE2 . PHE C 1 11  ? 41.678  -22.208 14.476 1.00 24.81  ? 10  PHE C CE2 1 
ATOM   3688 C CZ  . PHE C 1 11  ? 40.435  -22.766 14.258 1.00 33.59  ? 10  PHE C CZ  1 
ATOM   3689 N N   . LEU C 1 12  ? 43.837  -17.538 13.286 1.00 44.93  ? 11  LEU C N   1 
ATOM   3690 C CA  . LEU C 1 12  ? 44.614  -17.222 14.475 1.00 43.92  ? 11  LEU C CA  1 
ATOM   3691 C C   . LEU C 1 12  ? 44.150  -15.927 15.135 1.00 50.41  ? 11  LEU C C   1 
ATOM   3692 O O   . LEU C 1 12  ? 44.264  -15.790 16.360 1.00 30.79  ? 11  LEU C O   1 
ATOM   3693 C CB  . LEU C 1 12  ? 46.100  -17.110 14.123 1.00 44.39  ? 11  LEU C CB  1 
ATOM   3694 C CG  . LEU C 1 12  ? 46.817  -15.946 14.823 1.00 39.33  ? 11  LEU C CG  1 
ATOM   3695 C CD1 . LEU C 1 12  ? 47.234  -16.341 16.229 1.00 50.17  ? 11  LEU C CD1 1 
ATOM   3696 C CD2 . LEU C 1 12  ? 48.012  -15.490 14.002 1.00 39.15  ? 11  LEU C CD2 1 
ATOM   3697 N N   . LYS C 1 13  ? 43.647  -14.972 14.352 1.00 47.83  ? 12  LYS C N   1 
ATOM   3698 C CA  . LYS C 1 13  ? 43.166  -13.708 14.915 1.00 38.78  ? 12  LYS C CA  1 
ATOM   3699 C C   . LYS C 1 13  ? 41.860  -13.944 15.672 1.00 28.67  ? 12  LYS C C   1 
ATOM   3700 O O   . LYS C 1 13  ? 41.527  -13.349 16.682 1.00 24.21  ? 12  LYS C O   1 
ATOM   3701 C CB  . LYS C 1 13  ? 42.943  -12.657 13.831 1.00 40.79  ? 12  LYS C CB  1 
ATOM   3702 C CG  . LYS C 1 13  ? 44.134  -11.794 13.450 1.00 48.03  ? 12  LYS C CG  1 
ATOM   3703 C CD  . LYS C 1 13  ? 45.365  -12.198 14.255 1.00 73.81  ? 12  LYS C CD  1 
ATOM   3704 C CE  . LYS C 1 13  ? 45.640  -11.288 15.438 1.00 77.71  ? 12  LYS C CE  1 
ATOM   3705 N NZ  . LYS C 1 13  ? 46.558  -11.881 16.454 1.00 57.02  ? 12  LYS C NZ  1 
ATOM   3706 N N   . ALA C 1 14  ? 41.067  -14.855 15.132 1.00 30.52  ? 13  ALA C N   1 
ATOM   3707 C CA  . ALA C 1 14  ? 39.751  -15.165 15.679 1.00 40.26  ? 13  ALA C CA  1 
ATOM   3708 C C   . ALA C 1 14  ? 39.908  -15.669 17.105 1.00 45.29  ? 13  ALA C C   1 
ATOM   3709 O O   . ALA C 1 14  ? 39.410  -15.101 18.070 1.00 52.41  ? 13  ALA C O   1 
ATOM   3710 C CB  . ALA C 1 14  ? 39.070  -16.200 14.799 1.00 30.51  ? 13  ALA C CB  1 
ATOM   3711 N N   . VAL C 1 15  ? 40.654  -16.772 17.177 1.00 43.57  ? 14  VAL C N   1 
ATOM   3712 C CA  . VAL C 1 15  ? 40.915  -17.428 18.448 1.00 32.56  ? 14  VAL C CA  1 
ATOM   3713 C C   . VAL C 1 15  ? 41.482  -16.439 19.450 1.00 33.41  ? 14  VAL C C   1 
ATOM   3714 O O   . VAL C 1 15  ? 41.107  -16.488 20.625 1.00 35.92  ? 14  VAL C O   1 
ATOM   3715 C CB  . VAL C 1 15  ? 41.868  -18.622 18.270 1.00 38.08  ? 14  VAL C CB  1 
ATOM   3716 C CG1 . VAL C 1 15  ? 41.952  -19.423 19.565 1.00 45.88  ? 14  VAL C CG1 1 
ATOM   3717 C CG2 . VAL C 1 15  ? 41.387  -19.490 17.121 1.00 18.72  ? 14  VAL C CG2 1 
ATOM   3718 N N   . PHE C 1 16  ? 42.374  -15.545 19.019 1.00 25.54  ? 15  PHE C N   1 
ATOM   3719 C CA  . PHE C 1 16  ? 42.877  -14.582 20.008 1.00 34.54  ? 15  PHE C CA  1 
ATOM   3720 C C   . PHE C 1 16  ? 41.744  -13.626 20.377 1.00 35.47  ? 15  PHE C C   1 
ATOM   3721 O O   . PHE C 1 16  ? 41.643  -13.115 21.496 1.00 38.11  ? 15  PHE C O   1 
ATOM   3722 C CB  . PHE C 1 16  ? 44.112  -13.846 19.506 1.00 40.05  ? 15  PHE C CB  1 
ATOM   3723 C CG  . PHE C 1 16  ? 44.467  -12.571 20.255 1.00 35.25  ? 15  PHE C CG  1 
ATOM   3724 C CD1 . PHE C 1 16  ? 45.216  -12.611 21.416 1.00 35.58  ? 15  PHE C CD1 1 
ATOM   3725 C CD2 . PHE C 1 16  ? 44.047  -11.335 19.793 1.00 33.85  ? 15  PHE C CD2 1 
ATOM   3726 C CE1 . PHE C 1 16  ? 45.539  -11.449 22.091 1.00 39.57  ? 15  PHE C CE1 1 
ATOM   3727 C CE2 . PHE C 1 16  ? 44.375  -10.170 20.455 1.00 40.97  ? 15  PHE C CE2 1 
ATOM   3728 C CZ  . PHE C 1 16  ? 45.133  -10.218 21.615 1.00 39.85  ? 15  PHE C CZ  1 
ATOM   3729 N N   . ALA C 1 17  ? 40.846  -13.403 19.413 1.00 24.43  ? 16  ALA C N   1 
ATOM   3730 C CA  . ALA C 1 17  ? 39.678  -12.593 19.762 1.00 31.67  ? 16  ALA C CA  1 
ATOM   3731 C C   . ALA C 1 17  ? 38.877  -13.220 20.903 1.00 28.88  ? 16  ALA C C   1 
ATOM   3732 O O   . ALA C 1 17  ? 38.456  -12.537 21.841 1.00 26.52  ? 16  ALA C O   1 
ATOM   3733 C CB  . ALA C 1 17  ? 38.824  -12.377 18.520 1.00 21.39  ? 16  ALA C CB  1 
ATOM   3734 N N   . GLU C 1 18  ? 38.640  -14.521 20.838 1.00 35.39  ? 17  GLU C N   1 
ATOM   3735 C CA  . GLU C 1 18  ? 37.822  -15.247 21.805 1.00 36.81  ? 17  GLU C CA  1 
ATOM   3736 C C   . GLU C 1 18  ? 38.498  -15.316 23.162 1.00 33.98  ? 17  GLU C C   1 
ATOM   3737 O O   . GLU C 1 18  ? 37.903  -15.089 24.220 1.00 35.71  ? 17  GLU C O   1 
ATOM   3738 C CB  . GLU C 1 18  ? 37.492  -16.654 21.282 1.00 33.82  ? 17  GLU C CB  1 
ATOM   3739 C CG  . GLU C 1 18  ? 36.527  -16.578 20.106 1.00 35.44  ? 17  GLU C CG  1 
ATOM   3740 C CD  . GLU C 1 18  ? 35.076  -16.345 20.484 1.00 44.15  ? 17  GLU C CD  1 
ATOM   3741 O OE1 . GLU C 1 18  ? 34.605  -16.972 21.469 1.00 27.63  ? 17  GLU C OE1 1 
ATOM   3742 O OE2 . GLU C 1 18  ? 34.411  -15.540 19.779 1.00 30.38  ? 17  GLU C OE2 1 
ATOM   3743 N N   . PHE C 1 19  ? 39.791  -15.629 23.132 1.00 34.59  ? 18  PHE C N   1 
ATOM   3744 C CA  . PHE C 1 19  ? 40.577  -15.468 24.349 1.00 27.12  ? 18  PHE C CA  1 
ATOM   3745 C C   . PHE C 1 19  ? 40.411  -14.051 24.888 1.00 33.30  ? 18  PHE C C   1 
ATOM   3746 O O   . PHE C 1 19  ? 39.966  -13.865 26.021 1.00 35.88  ? 18  PHE C O   1 
ATOM   3747 C CB  . PHE C 1 19  ? 42.051  -15.795 24.080 1.00 27.33  ? 18  PHE C CB  1 
ATOM   3748 C CG  . PHE C 1 19  ? 42.990  -15.126 25.074 1.00 38.41  ? 18  PHE C CG  1 
ATOM   3749 C CD1 . PHE C 1 19  ? 43.042  -15.566 26.386 1.00 40.78  ? 18  PHE C CD1 1 
ATOM   3750 C CD2 . PHE C 1 19  ? 43.795  -14.070 24.664 1.00 38.49  ? 18  PHE C CD2 1 
ATOM   3751 C CE1 . PHE C 1 19  ? 43.887  -14.955 27.297 1.00 40.61  ? 18  PHE C CE1 1 
ATOM   3752 C CE2 . PHE C 1 19  ? 44.626  -13.448 25.569 1.00 37.38  ? 18  PHE C CE2 1 
ATOM   3753 C CZ  . PHE C 1 19  ? 44.664  -13.889 26.880 1.00 42.19  ? 18  PHE C CZ  1 
ATOM   3754 N N   . LEU C 1 20  ? 40.745  -13.040 24.084 1.00 37.66  ? 19  LEU C N   1 
ATOM   3755 C CA  . LEU C 1 20  ? 40.745  -11.658 24.555 1.00 33.85  ? 19  LEU C CA  1 
ATOM   3756 C C   . LEU C 1 20  ? 39.383  -11.220 25.085 1.00 42.14  ? 19  LEU C C   1 
ATOM   3757 O O   . LEU C 1 20  ? 39.264  -10.609 26.154 1.00 28.81  ? 19  LEU C O   1 
ATOM   3758 C CB  . LEU C 1 20  ? 41.222  -10.732 23.427 1.00 29.15  ? 19  LEU C CB  1 
ATOM   3759 C CG  . LEU C 1 20  ? 41.146  -9.229  23.705 1.00 28.20  ? 19  LEU C CG  1 
ATOM   3760 C CD1 . LEU C 1 20  ? 41.978  -8.878  24.933 1.00 42.41  ? 19  LEU C CD1 1 
ATOM   3761 C CD2 . LEU C 1 20  ? 41.594  -8.406  22.508 1.00 24.85  ? 19  LEU C CD2 1 
ATOM   3762 N N   . ALA C 1 21  ? 38.315  -11.514 24.351 1.00 35.59  ? 20  ALA C N   1 
ATOM   3763 C CA  . ALA C 1 21  ? 36.969  -11.119 24.731 1.00 26.90  ? 20  ALA C CA  1 
ATOM   3764 C C   . ALA C 1 21  ? 36.490  -11.715 26.053 1.00 31.14  ? 20  ALA C C   1 
ATOM   3765 O O   . ALA C 1 21  ? 35.904  -11.028 26.891 1.00 25.27  ? 20  ALA C O   1 
ATOM   3766 C CB  . ALA C 1 21  ? 35.987  -11.546 23.646 1.00 29.62  ? 20  ALA C CB  1 
ATOM   3767 N N   . THR C 1 22  ? 36.724  -13.009 26.212 1.00 32.90  ? 21  THR C N   1 
ATOM   3768 C CA  . THR C 1 22  ? 36.379  -13.742 27.424 1.00 29.57  ? 21  THR C CA  1 
ATOM   3769 C C   . THR C 1 22  ? 37.084  -13.182 28.656 1.00 32.13  ? 21  THR C C   1 
ATOM   3770 O O   . THR C 1 22  ? 36.442  -13.033 29.710 1.00 28.47  ? 21  THR C O   1 
ATOM   3771 C CB  . THR C 1 22  ? 36.720  -15.231 27.249 1.00 24.20  ? 21  THR C CB  1 
ATOM   3772 O OG1 . THR C 1 22  ? 36.221  -15.655 25.972 1.00 25.69  ? 21  THR C OG1 1 
ATOM   3773 C CG2 . THR C 1 22  ? 36.027  -16.070 28.308 1.00 51.97  ? 21  THR C CG2 1 
ATOM   3774 N N   . LEU C 1 23  ? 38.370  -12.886 28.524 1.00 38.82  ? 22  LEU C N   1 
ATOM   3775 C CA  . LEU C 1 23  ? 39.158  -12.175 29.523 1.00 40.00  ? 22  LEU C CA  1 
ATOM   3776 C C   . LEU C 1 23  ? 38.385  -10.987 30.095 1.00 32.00  ? 22  LEU C C   1 
ATOM   3777 O O   . LEU C 1 23  ? 37.937  -10.931 31.236 1.00 34.77  ? 22  LEU C O   1 
ATOM   3778 C CB  . LEU C 1 23  ? 40.480  -11.641 28.938 1.00 31.35  ? 22  LEU C CB  1 
ATOM   3779 C CG  . LEU C 1 23  ? 41.553  -11.196 29.925 1.00 20.45  ? 22  LEU C CG  1 
ATOM   3780 C CD1 . LEU C 1 23  ? 42.961  -11.419 29.376 1.00 25.55  ? 22  LEU C CD1 1 
ATOM   3781 C CD2 . LEU C 1 23  ? 41.415  -9.732  30.317 1.00 26.12  ? 22  LEU C CD2 1 
ATOM   3782 N N   . ILE C 1 24  ? 38.283  -9.988  29.217 1.00 29.98  ? 23  ILE C N   1 
ATOM   3783 C CA  . ILE C 1 24  ? 37.598  -8.752  29.547 1.00 17.86  ? 23  ILE C CA  1 
ATOM   3784 C C   . ILE C 1 24  ? 36.208  -9.068  30.069 1.00 19.19  ? 23  ILE C C   1 
ATOM   3785 O O   . ILE C 1 24  ? 35.781  -8.483  31.061 1.00 29.02  ? 23  ILE C O   1 
ATOM   3786 C CB  . ILE C 1 24  ? 37.509  -7.827  28.318 1.00 22.65  ? 23  ILE C CB  1 
ATOM   3787 C CG1 . ILE C 1 24  ? 38.876  -7.338  27.831 1.00 19.40  ? 23  ILE C CG1 1 
ATOM   3788 C CG2 . ILE C 1 24  ? 36.551  -6.686  28.613 1.00 22.74  ? 23  ILE C CG2 1 
ATOM   3789 C CD1 . ILE C 1 24  ? 38.936  -7.046  26.340 1.00 31.86  ? 23  ILE C CD1 1 
ATOM   3790 N N   . PHE C 1 25  ? 35.513  -9.992  29.396 1.00 19.06  ? 24  PHE C N   1 
ATOM   3791 C CA  . PHE C 1 25  ? 34.152  -10.299 29.832 1.00 23.96  ? 24  PHE C CA  1 
ATOM   3792 C C   . PHE C 1 25  ? 34.238  -10.804 31.268 1.00 36.79  ? 24  PHE C C   1 
ATOM   3793 O O   . PHE C 1 25  ? 33.481  -10.363 32.142 1.00 51.82  ? 24  PHE C O   1 
ATOM   3794 C CB  . PHE C 1 25  ? 33.427  -11.311 28.947 1.00 30.03  ? 24  PHE C CB  1 
ATOM   3795 C CG  . PHE C 1 25  ? 32.198  -11.923 29.613 1.00 35.30  ? 24  PHE C CG  1 
ATOM   3796 C CD1 . PHE C 1 25  ? 31.172  -11.125 30.091 1.00 25.16  ? 24  PHE C CD1 1 
ATOM   3797 C CD2 . PHE C 1 25  ? 32.072  -13.297 29.760 1.00 36.69  ? 24  PHE C CD2 1 
ATOM   3798 C CE1 . PHE C 1 25  ? 30.057  -11.666 30.704 1.00 23.19  ? 24  PHE C CE1 1 
ATOM   3799 C CE2 . PHE C 1 25  ? 30.959  -13.850 30.374 1.00 35.80  ? 24  PHE C CE2 1 
ATOM   3800 C CZ  . PHE C 1 25  ? 29.945  -13.038 30.839 1.00 26.06  ? 24  PHE C CZ  1 
ATOM   3801 N N   . VAL C 1 26  ? 35.193  -11.717 31.504 1.00 40.56  ? 25  VAL C N   1 
ATOM   3802 C CA  . VAL C 1 26  ? 35.196  -12.265 32.870 1.00 44.56  ? 25  VAL C CA  1 
ATOM   3803 C C   . VAL C 1 26  ? 35.636  -11.215 33.881 1.00 35.43  ? 25  VAL C C   1 
ATOM   3804 O O   . VAL C 1 26  ? 35.062  -11.197 34.979 1.00 25.71  ? 25  VAL C O   1 
ATOM   3805 C CB  . VAL C 1 26  ? 36.040  -13.541 32.974 1.00 45.51  ? 25  VAL C CB  1 
ATOM   3806 C CG1 . VAL C 1 26  ? 36.283  -13.920 34.426 1.00 42.10  ? 25  VAL C CG1 1 
ATOM   3807 C CG2 . VAL C 1 26  ? 35.318  -14.664 32.243 1.00 30.72  ? 25  VAL C CG2 1 
ATOM   3808 N N   . PHE C 1 27  ? 36.602  -10.380 33.511 1.00 30.77  ? 26  PHE C N   1 
ATOM   3809 C CA  . PHE C 1 27  ? 37.044  -9.337  34.436 1.00 31.45  ? 26  PHE C CA  1 
ATOM   3810 C C   . PHE C 1 27  ? 35.828  -8.516  34.863 1.00 30.22  ? 26  PHE C C   1 
ATOM   3811 O O   . PHE C 1 27  ? 35.659  -8.225  36.040 1.00 29.30  ? 26  PHE C O   1 
ATOM   3812 C CB  . PHE C 1 27  ? 38.081  -8.393  33.845 1.00 35.32  ? 26  PHE C CB  1 
ATOM   3813 C CG  . PHE C 1 27  ? 38.666  -7.337  34.767 1.00 37.95  ? 26  PHE C CG  1 
ATOM   3814 C CD1 . PHE C 1 27  ? 39.902  -7.549  35.370 1.00 34.85  ? 26  PHE C CD1 1 
ATOM   3815 C CD2 . PHE C 1 27  ? 38.059  -6.124  35.053 1.00 44.20  ? 26  PHE C CD2 1 
ATOM   3816 C CE1 . PHE C 1 27  ? 40.460  -6.602  36.212 1.00 29.93  ? 26  PHE C CE1 1 
ATOM   3817 C CE2 . PHE C 1 27  ? 38.589  -5.179  35.909 1.00 30.88  ? 26  PHE C CE2 1 
ATOM   3818 C CZ  . PHE C 1 27  ? 39.821  -5.409  36.496 1.00 21.11  ? 26  PHE C CZ  1 
ATOM   3819 N N   . PHE C 1 28  ? 35.036  -8.126  33.869 1.00 25.52  ? 27  PHE C N   1 
ATOM   3820 C CA  . PHE C 1 28  ? 33.970  -7.171  34.152 1.00 28.89  ? 27  PHE C CA  1 
ATOM   3821 C C   . PHE C 1 28  ? 32.835  -7.812  34.928 1.00 29.62  ? 27  PHE C C   1 
ATOM   3822 O O   . PHE C 1 28  ? 32.296  -7.263  35.887 1.00 39.78  ? 27  PHE C O   1 
ATOM   3823 C CB  . PHE C 1 28  ? 33.473  -6.546  32.836 1.00 32.29  ? 27  PHE C CB  1 
ATOM   3824 C CG  . PHE C 1 28  ? 34.291  -5.288  32.509 1.00 31.07  ? 27  PHE C CG  1 
ATOM   3825 C CD1 . PHE C 1 28  ? 34.031  -4.094  33.169 1.00 33.07  ? 27  PHE C CD1 1 
ATOM   3826 C CD2 . PHE C 1 28  ? 35.296  -5.330  31.564 1.00 25.34  ? 27  PHE C CD2 1 
ATOM   3827 C CE1 . PHE C 1 28  ? 34.767  -2.959  32.881 1.00 30.74  ? 27  PHE C CE1 1 
ATOM   3828 C CE2 . PHE C 1 28  ? 36.045  -4.201  31.273 1.00 29.09  ? 27  PHE C CE2 1 
ATOM   3829 C CZ  . PHE C 1 28  ? 35.781  -3.015  31.944 1.00 27.79  ? 27  PHE C CZ  1 
ATOM   3830 N N   . GLY C 1 29  ? 32.468  -9.012  34.495 1.00 35.66  ? 28  GLY C N   1 
ATOM   3831 C CA  . GLY C 1 29  ? 31.424  -9.746  35.183 1.00 30.33  ? 28  GLY C CA  1 
ATOM   3832 C C   . GLY C 1 29  ? 31.742  -9.923  36.652 1.00 23.84  ? 28  GLY C C   1 
ATOM   3833 O O   . GLY C 1 29  ? 30.912  -9.604  37.493 1.00 24.61  ? 28  GLY C O   1 
ATOM   3834 N N   . LEU C 1 30  ? 32.926  -10.422 36.974 1.00 29.02  ? 29  LEU C N   1 
ATOM   3835 C CA  . LEU C 1 30  ? 33.246  -10.778 38.350 1.00 36.77  ? 29  LEU C CA  1 
ATOM   3836 C C   . LEU C 1 30  ? 33.468  -9.579  39.257 1.00 35.91  ? 29  LEU C C   1 
ATOM   3837 O O   . LEU C 1 30  ? 32.953  -9.511  40.372 1.00 28.43  ? 29  LEU C O   1 
ATOM   3838 C CB  . LEU C 1 30  ? 34.517  -11.632 38.385 1.00 32.35  ? 29  LEU C CB  1 
ATOM   3839 C CG  . LEU C 1 30  ? 34.541  -12.854 37.477 1.00 37.31  ? 29  LEU C CG  1 
ATOM   3840 C CD1 . LEU C 1 30  ? 35.727  -13.732 37.844 1.00 30.86  ? 29  LEU C CD1 1 
ATOM   3841 C CD2 . LEU C 1 30  ? 33.218  -13.593 37.577 1.00 34.98  ? 29  LEU C CD2 1 
ATOM   3842 N N   . GLY C 1 31  ? 34.271  -8.620  38.786 1.00 36.25  ? 30  GLY C N   1 
ATOM   3843 C CA  . GLY C 1 31  ? 34.489  -7.440  39.626 1.00 28.62  ? 30  GLY C CA  1 
ATOM   3844 C C   . GLY C 1 31  ? 33.189  -6.690  39.841 1.00 31.31  ? 30  GLY C C   1 
ATOM   3845 O O   . GLY C 1 31  ? 33.021  -5.957  40.816 1.00 33.18  ? 30  GLY C O   1 
ATOM   3846 N N   . SER C 1 32  ? 32.212  -6.840  38.934 1.00 37.06  ? 31  SER C N   1 
ATOM   3847 C CA  . SER C 1 32  ? 30.968  -6.076  39.114 1.00 29.62  ? 31  SER C CA  1 
ATOM   3848 C C   . SER C 1 32  ? 30.053  -6.744  40.140 1.00 27.59  ? 31  SER C C   1 
ATOM   3849 O O   . SER C 1 32  ? 29.182  -6.052  40.665 1.00 26.23  ? 31  SER C O   1 
ATOM   3850 C CB  . SER C 1 32  ? 30.261  -5.866  37.772 1.00 36.28  ? 31  SER C CB  1 
ATOM   3851 O OG  . SER C 1 32  ? 29.280  -6.843  37.501 1.00 32.98  ? 31  SER C OG  1 
ATOM   3852 N N   . ALA C 1 33  ? 30.267  -8.022  40.399 1.00 23.42  ? 32  ALA C N   1 
ATOM   3853 C CA  . ALA C 1 33  ? 29.585  -8.905  41.316 1.00 23.31  ? 32  ALA C CA  1 
ATOM   3854 C C   . ALA C 1 33  ? 30.270  -9.030  42.669 1.00 28.38  ? 32  ALA C C   1 
ATOM   3855 O O   . ALA C 1 33  ? 29.716  -9.612  43.611 1.00 38.64  ? 32  ALA C O   1 
ATOM   3856 C CB  . ALA C 1 33  ? 29.476  -10.305 40.709 1.00 21.79  ? 32  ALA C CB  1 
ATOM   3857 N N   . LEU C 1 34  ? 31.485  -8.495  42.815 1.00 32.21  ? 33  LEU C N   1 
ATOM   3858 C CA  . LEU C 1 34  ? 32.085  -8.602  44.146 1.00 27.69  ? 33  LEU C CA  1 
ATOM   3859 C C   . LEU C 1 34  ? 31.334  -7.710  45.131 1.00 33.65  ? 33  LEU C C   1 
ATOM   3860 O O   . LEU C 1 34  ? 30.686  -6.714  44.817 1.00 27.35  ? 33  LEU C O   1 
ATOM   3861 C CB  . LEU C 1 34  ? 33.554  -8.215  44.194 1.00 17.70  ? 33  LEU C CB  1 
ATOM   3862 C CG  . LEU C 1 34  ? 34.504  -9.014  43.306 1.00 20.68  ? 33  LEU C CG  1 
ATOM   3863 C CD1 . LEU C 1 34  ? 35.882  -8.374  43.310 1.00 29.13  ? 33  LEU C CD1 1 
ATOM   3864 C CD2 . LEU C 1 34  ? 34.574  -10.461 43.761 1.00 39.63  ? 33  LEU C CD2 1 
ATOM   3865 N N   . LYS C 1 35  ? 31.497  -8.154  46.371 1.00 32.41  ? 34  LYS C N   1 
ATOM   3866 C CA  . LYS C 1 35  ? 30.826  -7.531  47.495 1.00 39.28  ? 34  LYS C CA  1 
ATOM   3867 C C   . LYS C 1 35  ? 31.481  -6.220  47.888 1.00 39.85  ? 34  LYS C C   1 
ATOM   3868 O O   . LYS C 1 35  ? 32.034  -6.062  48.981 1.00 62.22  ? 34  LYS C O   1 
ATOM   3869 C CB  . LYS C 1 35  ? 30.803  -8.512  48.679 1.00 47.62  ? 34  LYS C CB  1 
ATOM   3870 C CG  . LYS C 1 35  ? 30.287  -9.899  48.331 1.00 46.72  ? 34  LYS C CG  1 
ATOM   3871 C CD  . LYS C 1 35  ? 29.173  -10.327 49.269 1.00 50.60  ? 34  LYS C CD  1 
ATOM   3872 C CE  . LYS C 1 35  ? 27.823  -10.332 48.571 1.00 46.56  ? 34  LYS C CE  1 
ATOM   3873 N NZ  . LYS C 1 35  ? 27.533  -11.641 47.928 1.00 46.21  ? 34  LYS C NZ  1 
ATOM   3874 N N   . TRP C 1 36  ? 31.425  -5.211  47.016 1.00 27.73  ? 35  TRP C N   1 
ATOM   3875 C CA  . TRP C 1 36  ? 31.958  -3.936  47.511 1.00 28.65  ? 35  TRP C CA  1 
ATOM   3876 C C   . TRP C 1 36  ? 31.176  -3.412  48.711 1.00 29.89  ? 35  TRP C C   1 
ATOM   3877 O O   . TRP C 1 36  ? 29.968  -3.235  48.792 1.00 32.31  ? 35  TRP C O   1 
ATOM   3878 C CB  . TRP C 1 36  ? 32.006  -2.927  46.381 1.00 32.76  ? 35  TRP C CB  1 
ATOM   3879 C CG  . TRP C 1 36  ? 32.705  -3.451  45.159 1.00 38.31  ? 35  TRP C CG  1 
ATOM   3880 C CD1 . TRP C 1 36  ? 32.113  -4.114  44.118 1.00 38.47  ? 35  TRP C CD1 1 
ATOM   3881 C CD2 . TRP C 1 36  ? 34.101  -3.358  44.846 1.00 36.59  ? 35  TRP C CD2 1 
ATOM   3882 N NE1 . TRP C 1 36  ? 33.062  -4.439  43.182 1.00 40.91  ? 35  TRP C NE1 1 
ATOM   3883 C CE2 . TRP C 1 36  ? 34.292  -3.989  43.599 1.00 33.94  ? 35  TRP C CE2 1 
ATOM   3884 C CE3 . TRP C 1 36  ? 35.218  -2.813  45.484 1.00 33.55  ? 35  TRP C CE3 1 
ATOM   3885 C CZ2 . TRP C 1 36  ? 35.542  -4.086  42.984 1.00 27.28  ? 35  TRP C CZ2 1 
ATOM   3886 C CZ3 . TRP C 1 36  ? 36.459  -2.908  44.878 1.00 25.41  ? 35  TRP C CZ3 1 
ATOM   3887 C CH2 . TRP C 1 36  ? 36.618  -3.540  43.638 1.00 33.86  ? 35  TRP C CH2 1 
ATOM   3888 N N   . PRO C 1 37  ? 31.957  -3.128  49.749 1.00 42.88  ? 36  PRO C N   1 
ATOM   3889 C CA  . PRO C 1 37  ? 31.444  -2.801  51.074 1.00 40.02  ? 36  PRO C CA  1 
ATOM   3890 C C   . PRO C 1 37  ? 30.885  -1.391  51.125 1.00 27.46  ? 36  PRO C C   1 
ATOM   3891 O O   . PRO C 1 37  ? 29.933  -1.103  51.850 1.00 41.45  ? 36  PRO C O   1 
ATOM   3892 C CB  . PRO C 1 37  ? 32.707  -2.877  51.939 1.00 59.25  ? 36  PRO C CB  1 
ATOM   3893 C CG  . PRO C 1 37  ? 33.777  -2.408  50.998 1.00 67.87  ? 36  PRO C CG  1 
ATOM   3894 C CD  . PRO C 1 37  ? 33.431  -3.066  49.682 1.00 61.15  ? 36  PRO C CD  1 
ATOM   3895 N N   . SER C 1 38  ? 31.491  -0.512  50.337 1.00 27.97  ? 37  SER C N   1 
ATOM   3896 C CA  . SER C 1 38  ? 30.958  0.843   50.175 1.00 33.05  ? 37  SER C CA  1 
ATOM   3897 C C   . SER C 1 38  ? 29.542  0.834   49.622 1.00 35.31  ? 37  SER C C   1 
ATOM   3898 O O   . SER C 1 38  ? 28.702  1.702   49.856 1.00 37.49  ? 37  SER C O   1 
ATOM   3899 C CB  . SER C 1 38  ? 31.902  1.599   49.232 1.00 33.92  ? 37  SER C CB  1 
ATOM   3900 O OG  . SER C 1 38  ? 32.831  0.652   48.704 1.00 51.50  ? 37  SER C OG  1 
ATOM   3901 N N   . ALA C 1 39  ? 29.251  -0.208  48.837 1.00 37.31  ? 38  ALA C N   1 
ATOM   3902 C CA  . ALA C 1 39  ? 27.980  -0.279  48.130 1.00 46.06  ? 38  ALA C CA  1 
ATOM   3903 C C   . ALA C 1 39  ? 27.763  -1.660  47.532 1.00 36.95  ? 38  ALA C C   1 
ATOM   3904 O O   . ALA C 1 39  ? 28.229  -1.875  46.408 1.00 35.03  ? 38  ALA C O   1 
ATOM   3905 C CB  . ALA C 1 39  ? 27.961  0.761   47.011 1.00 44.46  ? 38  ALA C CB  1 
ATOM   3906 N N   . LEU C 1 40  ? 27.116  -2.577  48.243 1.00 28.00  ? 39  LEU C N   1 
ATOM   3907 C CA  . LEU C 1 40  ? 26.994  -3.928  47.688 1.00 37.86  ? 39  LEU C CA  1 
ATOM   3908 C C   . LEU C 1 40  ? 26.289  -3.882  46.328 1.00 39.67  ? 39  LEU C C   1 
ATOM   3909 O O   . LEU C 1 40  ? 25.147  -3.422  46.268 1.00 28.16  ? 39  LEU C O   1 
ATOM   3910 C CB  . LEU C 1 40  ? 26.223  -4.856  48.612 1.00 36.99  ? 39  LEU C CB  1 
ATOM   3911 C CG  . LEU C 1 40  ? 26.953  -5.713  49.636 1.00 42.73  ? 39  LEU C CG  1 
ATOM   3912 C CD1 . LEU C 1 40  ? 28.448  -5.435  49.690 1.00 35.26  ? 39  LEU C CD1 1 
ATOM   3913 C CD2 . LEU C 1 40  ? 26.315  -5.503  51.011 1.00 32.44  ? 39  LEU C CD2 1 
ATOM   3914 N N   . PRO C 1 41  ? 26.976  -4.359  45.301 1.00 34.76  ? 40  PRO C N   1 
ATOM   3915 C CA  . PRO C 1 41  ? 26.380  -4.438  43.961 1.00 33.22  ? 40  PRO C CA  1 
ATOM   3916 C C   . PRO C 1 41  ? 24.986  -5.060  44.019 1.00 33.38  ? 40  PRO C C   1 
ATOM   3917 O O   . PRO C 1 41  ? 24.834  -6.136  44.601 1.00 29.11  ? 40  PRO C O   1 
ATOM   3918 C CB  . PRO C 1 41  ? 27.381  -5.335  43.231 1.00 33.15  ? 40  PRO C CB  1 
ATOM   3919 C CG  . PRO C 1 41  ? 28.689  -4.969  43.870 1.00 31.89  ? 40  PRO C CG  1 
ATOM   3920 C CD  . PRO C 1 41  ? 28.359  -4.881  45.343 1.00 32.15  ? 40  PRO C CD  1 
ATOM   3921 N N   . THR C 1 42  ? 23.990  -4.362  43.475 1.00 30.60  ? 41  THR C N   1 
ATOM   3922 C CA  . THR C 1 42  ? 22.596  -4.801  43.519 1.00 27.61  ? 41  THR C CA  1 
ATOM   3923 C C   . THR C 1 42  ? 22.353  -5.827  42.407 1.00 31.50  ? 41  THR C C   1 
ATOM   3924 O O   . THR C 1 42  ? 23.233  -6.061  41.572 1.00 29.43  ? 41  THR C O   1 
ATOM   3925 C CB  . THR C 1 42  ? 21.602  -3.636  43.397 1.00 33.81  ? 41  THR C CB  1 
ATOM   3926 O OG1 . THR C 1 42  ? 21.670  -2.976  42.110 1.00 25.48  ? 41  THR C OG1 1 
ATOM   3927 C CG2 . THR C 1 42  ? 21.933  -2.550  44.411 1.00 22.23  ? 41  THR C CG2 1 
ATOM   3928 N N   . ILE C 1 43  ? 21.175  -6.451  42.373 1.00 28.39  ? 42  ILE C N   1 
ATOM   3929 C CA  . ILE C 1 43  ? 20.882  -7.438  41.337 1.00 22.95  ? 42  ILE C CA  1 
ATOM   3930 C C   . ILE C 1 43  ? 20.833  -6.814  39.946 1.00 22.98  ? 42  ILE C C   1 
ATOM   3931 O O   . ILE C 1 43  ? 21.393  -7.362  38.991 1.00 19.86  ? 42  ILE C O   1 
ATOM   3932 C CB  . ILE C 1 43  ? 19.545  -8.147  41.617 1.00 23.79  ? 42  ILE C CB  1 
ATOM   3933 C CG1 . ILE C 1 43  ? 19.525  -8.870  42.970 1.00 31.69  ? 42  ILE C CG1 1 
ATOM   3934 C CG2 . ILE C 1 43  ? 19.192  -9.093  40.476 1.00 23.59  ? 42  ILE C CG2 1 
ATOM   3935 C CD1 . ILE C 1 43  ? 20.395  -10.114 42.963 1.00 28.22  ? 42  ILE C CD1 1 
ATOM   3936 N N   . LEU C 1 44  ? 20.161  -5.675  39.798 1.00 25.22  ? 43  LEU C N   1 
ATOM   3937 C CA  . LEU C 1 44  ? 19.967  -5.111  38.455 1.00 29.91  ? 43  LEU C CA  1 
ATOM   3938 C C   . LEU C 1 44  ? 21.299  -4.560  37.954 1.00 28.63  ? 43  LEU C C   1 
ATOM   3939 O O   . LEU C 1 44  ? 21.621  -4.670  36.776 1.00 24.09  ? 43  LEU C O   1 
ATOM   3940 C CB  . LEU C 1 44  ? 18.918  -4.008  38.435 1.00 30.61  ? 43  LEU C CB  1 
ATOM   3941 C CG  . LEU C 1 44  ? 18.700  -3.260  37.119 1.00 33.27  ? 43  LEU C CG  1 
ATOM   3942 C CD1 . LEU C 1 44  ? 17.955  -4.099  36.094 1.00 30.67  ? 43  LEU C CD1 1 
ATOM   3943 C CD2 . LEU C 1 44  ? 17.945  -1.963  37.368 1.00 29.48  ? 43  LEU C CD2 1 
ATOM   3944 N N   . GLN C 1 45  ? 22.010  -3.980  38.927 1.00 24.59  ? 44  GLN C N   1 
ATOM   3945 C CA  . GLN C 1 45  ? 23.338  -3.442  38.646 1.00 18.48  ? 44  GLN C CA  1 
ATOM   3946 C C   . GLN C 1 45  ? 24.197  -4.556  38.067 1.00 30.30  ? 44  GLN C C   1 
ATOM   3947 O O   . GLN C 1 45  ? 24.853  -4.419  37.044 1.00 21.53  ? 44  GLN C O   1 
ATOM   3948 C CB  . GLN C 1 45  ? 23.943  -2.860  39.917 1.00 25.78  ? 44  GLN C CB  1 
ATOM   3949 C CG  . GLN C 1 45  ? 25.441  -2.715  39.968 1.00 32.88  ? 44  GLN C CG  1 
ATOM   3950 C CD  . GLN C 1 45  ? 26.050  -2.125  41.219 1.00 29.13  ? 44  GLN C CD  1 
ATOM   3951 O OE1 . GLN C 1 45  ? 27.276  -2.168  41.392 1.00 19.34  ? 44  GLN C OE1 1 
ATOM   3952 N NE2 . GLN C 1 45  ? 25.246  -1.563  42.111 1.00 29.20  ? 44  GLN C NE2 1 
ATOM   3953 N N   . ILE C 1 46  ? 24.189  -5.691  38.764 1.00 29.38  ? 45  ILE C N   1 
ATOM   3954 C CA  . ILE C 1 46  ? 25.005  -6.823  38.378 1.00 16.91  ? 45  ILE C CA  1 
ATOM   3955 C C   . ILE C 1 46  ? 24.585  -7.400  37.032 1.00 26.51  ? 45  ILE C C   1 
ATOM   3956 O O   . ILE C 1 46  ? 25.430  -7.752  36.216 1.00 25.51  ? 45  ILE C O   1 
ATOM   3957 C CB  . ILE C 1 46  ? 24.917  -7.965  39.410 1.00 18.28  ? 45  ILE C CB  1 
ATOM   3958 C CG1 . ILE C 1 46  ? 25.609  -7.658  40.735 1.00 20.38  ? 45  ILE C CG1 1 
ATOM   3959 C CG2 . ILE C 1 46  ? 25.451  -9.246  38.796 1.00 22.66  ? 45  ILE C CG2 1 
ATOM   3960 C CD1 . ILE C 1 46  ? 25.414  -8.735  41.784 1.00 21.66  ? 45  ILE C CD1 1 
ATOM   3961 N N   . ALA C 1 47  ? 23.274  -7.483  36.840 1.00 24.06  ? 46  ALA C N   1 
ATOM   3962 C CA  . ALA C 1 47  ? 22.754  -8.030  35.587 1.00 30.38  ? 46  ALA C CA  1 
ATOM   3963 C C   . ALA C 1 47  ? 23.154  -7.164  34.401 1.00 30.09  ? 46  ALA C C   1 
ATOM   3964 O O   . ALA C 1 47  ? 23.360  -7.683  33.295 1.00 27.05  ? 46  ALA C O   1 
ATOM   3965 C CB  . ALA C 1 47  ? 21.245  -8.176  35.684 1.00 17.31  ? 46  ALA C CB  1 
ATOM   3966 N N   . LEU C 1 48  ? 23.270  -5.853  34.623 1.00 23.63  ? 47  LEU C N   1 
ATOM   3967 C CA  . LEU C 1 48  ? 23.599  -4.961  33.509 1.00 28.46  ? 47  LEU C CA  1 
ATOM   3968 C C   . LEU C 1 48  ? 25.089  -4.936  33.227 1.00 33.33  ? 47  LEU C C   1 
ATOM   3969 O O   . LEU C 1 48  ? 25.498  -4.685  32.092 1.00 35.23  ? 47  LEU C O   1 
ATOM   3970 C CB  . LEU C 1 48  ? 23.093  -3.533  33.757 1.00 27.11  ? 47  LEU C CB  1 
ATOM   3971 C CG  . LEU C 1 48  ? 21.598  -3.376  33.422 1.00 33.88  ? 47  LEU C CG  1 
ATOM   3972 C CD1 . LEU C 1 48  ? 20.981  -2.204  34.166 1.00 28.58  ? 47  LEU C CD1 1 
ATOM   3973 C CD2 . LEU C 1 48  ? 21.417  -3.242  31.917 1.00 28.86  ? 47  LEU C CD2 1 
ATOM   3974 N N   . ALA C 1 49  ? 25.893  -5.204  34.254 1.00 33.40  ? 48  ALA C N   1 
ATOM   3975 C CA  . ALA C 1 49  ? 27.331  -5.293  34.015 1.00 30.12  ? 48  ALA C CA  1 
ATOM   3976 C C   . ALA C 1 49  ? 27.640  -6.521  33.166 1.00 31.59  ? 48  ALA C C   1 
ATOM   3977 O O   . ALA C 1 49  ? 28.522  -6.483  32.310 1.00 27.74  ? 48  ALA C O   1 
ATOM   3978 C CB  . ALA C 1 49  ? 28.098  -5.345  35.326 1.00 28.98  ? 48  ALA C CB  1 
ATOM   3979 N N   . PHE C 1 50  ? 26.926  -7.628  33.410 1.00 24.43  ? 49  PHE C N   1 
ATOM   3980 C CA  . PHE C 1 50  ? 27.248  -8.827  32.635 1.00 23.91  ? 49  PHE C CA  1 
ATOM   3981 C C   . PHE C 1 50  ? 26.752  -8.697  31.193 1.00 25.61  ? 49  PHE C C   1 
ATOM   3982 O O   . PHE C 1 50  ? 27.446  -9.118  30.264 1.00 23.97  ? 49  PHE C O   1 
ATOM   3983 C CB  . PHE C 1 50  ? 26.629  -10.039 33.321 1.00 25.51  ? 49  PHE C CB  1 
ATOM   3984 C CG  . PHE C 1 50  ? 27.556  -10.742 34.298 1.00 29.79  ? 49  PHE C CG  1 
ATOM   3985 C CD1 . PHE C 1 50  ? 27.661  -10.297 35.607 1.00 26.08  ? 49  PHE C CD1 1 
ATOM   3986 C CD2 . PHE C 1 50  ? 28.304  -11.846 33.910 1.00 32.21  ? 49  PHE C CD2 1 
ATOM   3987 C CE1 . PHE C 1 50  ? 28.511  -10.951 36.488 1.00 30.60  ? 49  PHE C CE1 1 
ATOM   3988 C CE2 . PHE C 1 50  ? 29.161  -12.499 34.782 1.00 24.76  ? 49  PHE C CE2 1 
ATOM   3989 C CZ  . PHE C 1 50  ? 29.254  -12.051 36.089 1.00 25.68  ? 49  PHE C CZ  1 
ATOM   3990 N N   . GLY C 1 51  ? 25.565  -8.127  31.034 1.00 19.30  ? 50  GLY C N   1 
ATOM   3991 C CA  . GLY C 1 51  ? 24.817  -7.898  29.823 1.00 18.52  ? 50  GLY C CA  1 
ATOM   3992 C C   . GLY C 1 51  ? 25.504  -6.927  28.868 1.00 30.96  ? 50  GLY C C   1 
ATOM   3993 O O   . GLY C 1 51  ? 25.644  -7.172  27.660 1.00 18.88  ? 50  GLY C O   1 
ATOM   3994 N N   . LEU C 1 52  ? 25.928  -5.825  29.475 1.00 23.37  ? 51  LEU C N   1 
ATOM   3995 C CA  . LEU C 1 52  ? 26.631  -4.766  28.774 1.00 23.76  ? 51  LEU C CA  1 
ATOM   3996 C C   . LEU C 1 52  ? 28.030  -5.216  28.374 1.00 26.05  ? 51  LEU C C   1 
ATOM   3997 O O   . LEU C 1 52  ? 28.530  -4.821  27.308 1.00 39.16  ? 51  LEU C O   1 
ATOM   3998 C CB  . LEU C 1 52  ? 26.677  -3.492  29.623 1.00 23.11  ? 51  LEU C CB  1 
ATOM   3999 C CG  . LEU C 1 52  ? 25.322  -2.858  29.949 1.00 21.59  ? 51  LEU C CG  1 
ATOM   4000 C CD1 . LEU C 1 52  ? 25.516  -1.564  30.716 1.00 21.06  ? 51  LEU C CD1 1 
ATOM   4001 C CD2 . LEU C 1 52  ? 24.502  -2.624  28.688 1.00 23.45  ? 51  LEU C CD2 1 
ATOM   4002 N N   . ALA C 1 53  ? 28.693  -6.039  29.179 1.00 25.68  ? 52  ALA C N   1 
ATOM   4003 C CA  . ALA C 1 53  ? 30.021  -6.507  28.798 1.00 26.35  ? 52  ALA C CA  1 
ATOM   4004 C C   . ALA C 1 53  ? 29.933  -7.307  27.506 1.00 27.63  ? 52  ALA C C   1 
ATOM   4005 O O   . ALA C 1 53  ? 30.706  -7.196  26.563 1.00 24.13  ? 52  ALA C O   1 
ATOM   4006 C CB  . ALA C 1 53  ? 30.645  -7.343  29.905 1.00 19.58  ? 52  ALA C CB  1 
ATOM   4007 N N   . ILE C 1 54  ? 28.935  -8.181  27.452 1.00 16.83  ? 53  ILE C N   1 
ATOM   4008 C CA  . ILE C 1 54  ? 28.805  -9.004  26.256 1.00 18.31  ? 53  ILE C CA  1 
ATOM   4009 C C   . ILE C 1 54  ? 28.361  -8.147  25.064 1.00 24.05  ? 53  ILE C C   1 
ATOM   4010 O O   . ILE C 1 54  ? 28.824  -8.364  23.935 1.00 19.87  ? 53  ILE C O   1 
ATOM   4011 C CB  . ILE C 1 54  ? 27.862  -10.184 26.506 1.00 26.67  ? 53  ILE C CB  1 
ATOM   4012 C CG1 . ILE C 1 54  ? 28.468  -11.257 27.431 1.00 21.98  ? 53  ILE C CG1 1 
ATOM   4013 C CG2 . ILE C 1 54  ? 27.376  -10.836 25.211 1.00 28.85  ? 53  ILE C CG2 1 
ATOM   4014 C CD1 . ILE C 1 54  ? 29.770  -11.822 26.879 1.00 24.84  ? 53  ILE C CD1 1 
ATOM   4015 N N   . GLY C 1 55  ? 27.496  -7.176  25.300 1.00 29.40  ? 54  GLY C N   1 
ATOM   4016 C CA  . GLY C 1 55  ? 26.996  -6.266  24.285 1.00 23.46  ? 54  GLY C CA  1 
ATOM   4017 C C   . GLY C 1 55  ? 28.157  -5.550  23.606 1.00 26.14  ? 54  GLY C C   1 
ATOM   4018 O O   . GLY C 1 55  ? 28.238  -5.526  22.383 1.00 35.84  ? 54  GLY C O   1 
ATOM   4019 N N   . THR C 1 56  ? 29.047  -4.987  24.406 1.00 29.89  ? 55  THR C N   1 
ATOM   4020 C CA  . THR C 1 56  ? 30.250  -4.296  23.983 1.00 29.93  ? 55  THR C CA  1 
ATOM   4021 C C   . THR C 1 56  ? 31.269  -5.218  23.315 1.00 32.51  ? 55  THR C C   1 
ATOM   4022 O O   . THR C 1 56  ? 31.778  -4.915  22.232 1.00 42.44  ? 55  THR C O   1 
ATOM   4023 C CB  . THR C 1 56  ? 30.959  -3.627  25.179 1.00 31.09  ? 55  THR C CB  1 
ATOM   4024 O OG1 . THR C 1 56  ? 30.017  -2.877  25.959 1.00 22.91  ? 55  THR C OG1 1 
ATOM   4025 C CG2 . THR C 1 56  ? 32.012  -2.655  24.683 1.00 21.62  ? 55  THR C CG2 1 
ATOM   4026 N N   . LEU C 1 57  ? 31.593  -6.343  23.947 1.00 23.23  ? 56  LEU C N   1 
ATOM   4027 C CA  . LEU C 1 57  ? 32.627  -7.221  23.412 1.00 33.93  ? 56  LEU C CA  1 
ATOM   4028 C C   . LEU C 1 57  ? 32.226  -7.806  22.067 1.00 34.65  ? 56  LEU C C   1 
ATOM   4029 O O   . LEU C 1 57  ? 33.055  -8.013  21.189 1.00 30.66  ? 56  LEU C O   1 
ATOM   4030 C CB  . LEU C 1 57  ? 32.931  -8.368  24.385 1.00 34.78  ? 56  LEU C CB  1 
ATOM   4031 C CG  . LEU C 1 57  ? 33.569  -7.886  25.700 1.00 39.55  ? 56  LEU C CG  1 
ATOM   4032 C CD1 . LEU C 1 57  ? 33.926  -9.074  26.574 1.00 23.06  ? 56  LEU C CD1 1 
ATOM   4033 C CD2 . LEU C 1 57  ? 34.761  -7.008  25.365 1.00 25.89  ? 56  LEU C CD2 1 
ATOM   4034 N N   . ALA C 1 58  ? 30.930  -8.073  21.928 1.00 31.25  ? 57  ALA C N   1 
ATOM   4035 C CA  . ALA C 1 58  ? 30.452  -8.586  20.647 1.00 34.39  ? 57  ALA C CA  1 
ATOM   4036 C C   . ALA C 1 58  ? 30.450  -7.474  19.597 1.00 32.96  ? 57  ALA C C   1 
ATOM   4037 O O   . ALA C 1 58  ? 30.714  -7.744  18.417 1.00 35.56  ? 57  ALA C O   1 
ATOM   4038 C CB  . ALA C 1 58  ? 29.084  -9.220  20.829 1.00 40.94  ? 57  ALA C CB  1 
ATOM   4039 N N   . GLN C 1 59  ? 30.169  -6.233  19.998 1.00 26.57  ? 58  GLN C N   1 
ATOM   4040 C CA  . GLN C 1 59  ? 30.174  -5.129  19.035 1.00 30.74  ? 58  GLN C CA  1 
ATOM   4041 C C   . GLN C 1 59  ? 31.595  -4.925  18.493 1.00 28.48  ? 58  GLN C C   1 
ATOM   4042 O O   . GLN C 1 59  ? 31.757  -4.718  17.286 1.00 26.95  ? 58  GLN C O   1 
ATOM   4043 C CB  . GLN C 1 59  ? 29.672  -3.816  19.626 1.00 31.26  ? 58  GLN C CB  1 
ATOM   4044 C CG  . GLN C 1 59  ? 29.767  -2.612  18.712 1.00 38.56  ? 58  GLN C CG  1 
ATOM   4045 C CD  . GLN C 1 59  ? 28.618  -2.450  17.736 1.00 39.23  ? 58  GLN C CD  1 
ATOM   4046 O OE1 . GLN C 1 59  ? 27.910  -3.420  17.456 1.00 31.19  ? 58  GLN C OE1 1 
ATOM   4047 N NE2 . GLN C 1 59  ? 28.401  -1.246  17.204 1.00 23.26  ? 58  GLN C NE2 1 
ATOM   4048 N N   . ALA C 1 60  ? 32.522  -5.007  19.434 1.00 30.48  ? 59  ALA C N   1 
ATOM   4049 C CA  . ALA C 1 60  ? 33.930  -4.692  19.303 1.00 36.86  ? 59  ALA C CA  1 
ATOM   4050 C C   . ALA C 1 60  ? 34.785  -5.829  18.747 1.00 35.83  ? 59  ALA C C   1 
ATOM   4051 O O   . ALA C 1 60  ? 35.647  -5.509  17.926 1.00 26.43  ? 59  ALA C O   1 
ATOM   4052 C CB  . ALA C 1 60  ? 34.496  -4.267  20.653 1.00 30.50  ? 59  ALA C CB  1 
ATOM   4053 N N   . LEU C 1 61  ? 34.559  -7.063  19.178 1.00 29.87  ? 60  LEU C N   1 
ATOM   4054 C CA  . LEU C 1 61  ? 35.356  -8.209  18.754 1.00 29.98  ? 60  LEU C CA  1 
ATOM   4055 C C   . LEU C 1 61  ? 34.558  -9.176  17.881 1.00 33.45  ? 60  LEU C C   1 
ATOM   4056 O O   . LEU C 1 61  ? 35.134  -10.004 17.166 1.00 39.19  ? 60  LEU C O   1 
ATOM   4057 C CB  . LEU C 1 61  ? 35.922  -8.930  19.975 1.00 30.41  ? 60  LEU C CB  1 
ATOM   4058 C CG  . LEU C 1 61  ? 37.294  -8.564  20.537 1.00 29.15  ? 60  LEU C CG  1 
ATOM   4059 C CD1 . LEU C 1 61  ? 38.349  -8.471  19.435 1.00 46.20  ? 60  LEU C CD1 1 
ATOM   4060 C CD2 . LEU C 1 61  ? 37.276  -7.261  21.316 1.00 43.70  ? 60  LEU C CD2 1 
ATOM   4061 N N   . GLY C 1 62  ? 33.232  -9.062  17.919 1.00 23.29  ? 61  GLY C N   1 
ATOM   4062 C CA  . GLY C 1 62  ? 32.363  -9.870  17.092 1.00 30.71  ? 61  GLY C CA  1 
ATOM   4063 C C   . GLY C 1 62  ? 32.789  -10.005 15.649 1.00 40.23  ? 61  GLY C C   1 
ATOM   4064 O O   . GLY C 1 62  ? 32.731  -11.114 15.096 1.00 43.03  ? 61  GLY C O   1 
ATOM   4065 N N   . PRO C 1 63  ? 33.210  -8.959  14.951 1.00 35.67  ? 62  PRO C N   1 
ATOM   4066 C CA  . PRO C 1 63  ? 33.655  -9.140  13.559 1.00 39.62  ? 62  PRO C CA  1 
ATOM   4067 C C   . PRO C 1 63  ? 34.942  -9.936  13.394 1.00 38.10  ? 62  PRO C C   1 
ATOM   4068 O O   . PRO C 1 63  ? 35.188  -10.430 12.288 1.00 43.04  ? 62  PRO C O   1 
ATOM   4069 C CB  . PRO C 1 63  ? 33.888  -7.699  13.077 1.00 36.45  ? 62  PRO C CB  1 
ATOM   4070 C CG  . PRO C 1 63  ? 33.035  -6.881  13.999 1.00 34.39  ? 62  PRO C CG  1 
ATOM   4071 C CD  . PRO C 1 63  ? 33.261  -7.539  15.338 1.00 29.38  ? 62  PRO C CD  1 
ATOM   4072 N N   . VAL C 1 64  ? 35.771  -10.089 14.425 1.00 32.84  ? 63  VAL C N   1 
ATOM   4073 C CA  . VAL C 1 64  ? 36.987  -10.881 14.263 1.00 27.48  ? 63  VAL C CA  1 
ATOM   4074 C C   . VAL C 1 64  ? 36.732  -12.383 14.395 1.00 38.91  ? 63  VAL C C   1 
ATOM   4075 O O   . VAL C 1 64  ? 37.340  -13.187 13.675 1.00 41.42  ? 63  VAL C O   1 
ATOM   4076 C CB  . VAL C 1 64  ? 38.062  -10.489 15.295 1.00 26.63  ? 63  VAL C CB  1 
ATOM   4077 C CG1 . VAL C 1 64  ? 39.378  -11.186 14.955 1.00 34.67  ? 63  VAL C CG1 1 
ATOM   4078 C CG2 . VAL C 1 64  ? 38.279  -8.990  15.373 1.00 26.25  ? 63  VAL C CG2 1 
ATOM   4079 N N   . SER C 1 65  ? 35.852  -12.779 15.309 1.00 38.11  ? 64  SER C N   1 
ATOM   4080 C CA  . SER C 1 65  ? 35.633  -14.169 15.676 1.00 39.89  ? 64  SER C CA  1 
ATOM   4081 C C   . SER C 1 65  ? 34.200  -14.659 15.542 1.00 33.56  ? 64  SER C C   1 
ATOM   4082 O O   . SER C 1 65  ? 33.930  -15.856 15.363 1.00 25.60  ? 64  SER C O   1 
ATOM   4083 C CB  . SER C 1 65  ? 36.032  -14.357 17.155 1.00 40.45  ? 64  SER C CB  1 
ATOM   4084 O OG  . SER C 1 65  ? 35.130  -13.634 17.983 1.00 47.69  ? 64  SER C OG  1 
ATOM   4085 N N   . GLY C 1 66  ? 33.266  -13.725 15.659 1.00 32.25  ? 65  GLY C N   1 
ATOM   4086 C CA  . GLY C 1 66  ? 31.845  -14.054 15.737 1.00 34.42  ? 65  GLY C CA  1 
ATOM   4087 C C   . GLY C 1 66  ? 31.397  -13.823 17.185 1.00 29.11  ? 65  GLY C C   1 
ATOM   4088 O O   . GLY C 1 66  ? 30.222  -13.959 17.507 1.00 32.11  ? 65  GLY C O   1 
ATOM   4089 N N   . GLY C 1 67  ? 32.406  -13.473 17.975 1.00 19.15  ? 66  GLY C N   1 
ATOM   4090 C CA  . GLY C 1 67  ? 32.317  -13.243 19.389 1.00 26.76  ? 66  GLY C CA  1 
ATOM   4091 C C   . GLY C 1 67  ? 31.476  -14.276 20.107 1.00 30.64  ? 66  GLY C C   1 
ATOM   4092 O O   . GLY C 1 67  ? 30.365  -13.954 20.537 1.00 38.13  ? 66  GLY C O   1 
ATOM   4093 N N   . HIS C 1 68  ? 31.959  -15.510 20.264 1.00 22.56  ? 67  HIS C N   1 
ATOM   4094 C CA  . HIS C 1 68  ? 31.129  -16.470 21.010 1.00 35.64  ? 67  HIS C CA  1 
ATOM   4095 C C   . HIS C 1 68  ? 31.151  -16.158 22.504 1.00 35.26  ? 67  HIS C C   1 
ATOM   4096 O O   . HIS C 1 68  ? 30.143  -16.007 23.192 1.00 26.28  ? 67  HIS C O   1 
ATOM   4097 C CB  . HIS C 1 68  ? 31.579  -17.916 20.785 1.00 33.84  ? 67  HIS C CB  1 
ATOM   4098 C CG  . HIS C 1 68  ? 31.460  -18.323 19.352 1.00 39.20  ? 67  HIS C CG  1 
ATOM   4099 N ND1 . HIS C 1 68  ? 30.936  -17.457 18.413 1.00 43.04  ? 67  HIS C ND1 1 
ATOM   4100 C CD2 . HIS C 1 68  ? 31.775  -19.452 18.688 1.00 33.45  ? 67  HIS C CD2 1 
ATOM   4101 C CE1 . HIS C 1 68  ? 30.932  -18.044 17.230 1.00 36.16  ? 67  HIS C CE1 1 
ATOM   4102 N NE2 . HIS C 1 68  ? 31.439  -19.253 17.372 1.00 33.84  ? 67  HIS C NE2 1 
ATOM   4103 N N   . ILE C 1 69  ? 32.378  -16.041 23.013 1.00 31.87  ? 68  ILE C N   1 
ATOM   4104 C CA  . ILE C 1 69  ? 32.639  -15.730 24.407 1.00 30.26  ? 68  ILE C CA  1 
ATOM   4105 C C   . ILE C 1 69  ? 31.885  -16.711 25.320 1.00 38.93  ? 68  ILE C C   1 
ATOM   4106 O O   . ILE C 1 69  ? 31.519  -16.397 26.453 1.00 29.61  ? 68  ILE C O   1 
ATOM   4107 C CB  . ILE C 1 69  ? 32.296  -14.257 24.695 1.00 21.18  ? 68  ILE C CB  1 
ATOM   4108 C CG1 . ILE C 1 69  ? 32.406  -13.292 23.513 1.00 26.38  ? 68  ILE C CG1 1 
ATOM   4109 C CG2 . ILE C 1 69  ? 33.157  -13.705 25.823 1.00 17.75  ? 68  ILE C CG2 1 
ATOM   4110 C CD1 . ILE C 1 69  ? 31.906  -11.896 23.812 1.00 23.95  ? 68  ILE C CD1 1 
ATOM   4111 N N   . ASN C 1 70  ? 31.649  -17.939 24.862 1.00 31.59  ? 69  ASN C N   1 
ATOM   4112 C CA  . ASN C 1 70  ? 30.800  -18.924 25.491 1.00 30.20  ? 69  ASN C CA  1 
ATOM   4113 C C   . ASN C 1 70  ? 30.879  -20.330 24.905 1.00 39.02  ? 69  ASN C C   1 
ATOM   4114 O O   . ASN C 1 70  ? 30.302  -20.570 23.827 1.00 24.66  ? 69  ASN C O   1 
ATOM   4115 C CB  . ASN C 1 70  ? 29.336  -18.445 25.344 1.00 28.80  ? 69  ASN C CB  1 
ATOM   4116 C CG  . ASN C 1 70  ? 28.511  -19.084 26.455 1.00 41.67  ? 69  ASN C CG  1 
ATOM   4117 O OD1 . ASN C 1 70  ? 28.912  -20.142 26.950 1.00 36.13  ? 69  ASN C OD1 1 
ATOM   4118 N ND2 . ASN C 1 70  ? 27.417  -18.422 26.812 1.00 40.88  ? 69  ASN C ND2 1 
ATOM   4119 N N   . PRO C 1 71  ? 31.564  -21.266 25.565 1.00 36.55  ? 70  PRO C N   1 
ATOM   4120 C CA  . PRO C 1 71  ? 31.696  -22.646 25.061 1.00 28.54  ? 70  PRO C CA  1 
ATOM   4121 C C   . PRO C 1 71  ? 30.365  -23.303 24.741 1.00 34.55  ? 70  PRO C C   1 
ATOM   4122 O O   . PRO C 1 71  ? 30.284  -24.001 23.724 1.00 66.37  ? 70  PRO C O   1 
ATOM   4123 C CB  . PRO C 1 71  ? 32.408  -23.371 26.210 1.00 19.06  ? 70  PRO C CB  1 
ATOM   4124 C CG  . PRO C 1 71  ? 33.286  -22.265 26.734 1.00 17.43  ? 70  PRO C CG  1 
ATOM   4125 C CD  . PRO C 1 71  ? 32.313  -21.101 26.824 1.00 29.22  ? 70  PRO C CD  1 
ATOM   4126 N N   . ALA C 1 72  ? 29.322  -23.114 25.533 1.00 30.43  ? 71  ALA C N   1 
ATOM   4127 C CA  . ALA C 1 72  ? 27.971  -23.567 25.229 1.00 23.69  ? 71  ALA C CA  1 
ATOM   4128 C C   . ALA C 1 72  ? 27.409  -23.069 23.898 1.00 17.75  ? 71  ALA C C   1 
ATOM   4129 O O   . ALA C 1 72  ? 26.706  -23.793 23.179 1.00 24.24  ? 71  ALA C O   1 
ATOM   4130 C CB  . ALA C 1 72  ? 27.025  -23.104 26.342 1.00 38.88  ? 71  ALA C CB  1 
ATOM   4131 N N   . ILE C 1 73  ? 27.687  -21.820 23.535 1.00 19.96  ? 72  ILE C N   1 
ATOM   4132 C CA  . ILE C 1 73  ? 27.244  -21.319 22.233 1.00 31.07  ? 72  ILE C CA  1 
ATOM   4133 C C   . ILE C 1 73  ? 28.030  -21.960 21.091 1.00 40.28  ? 72  ILE C C   1 
ATOM   4134 O O   . ILE C 1 73  ? 27.477  -22.483 20.116 1.00 33.41  ? 72  ILE C O   1 
ATOM   4135 C CB  . ILE C 1 73  ? 27.380  -19.793 22.183 1.00 21.95  ? 72  ILE C CB  1 
ATOM   4136 C CG1 . ILE C 1 73  ? 26.592  -19.108 23.328 1.00 24.28  ? 72  ILE C CG1 1 
ATOM   4137 C CG2 . ILE C 1 73  ? 26.957  -19.216 20.840 1.00 13.08  ? 72  ILE C CG2 1 
ATOM   4138 C CD1 . ILE C 1 73  ? 25.098  -19.350 23.157 1.00 24.38  ? 72  ILE C CD1 1 
ATOM   4139 N N   . THR C 1 74  ? 29.350  -21.894 21.228 1.00 33.02  ? 73  THR C N   1 
ATOM   4140 C CA  . THR C 1 74  ? 30.284  -22.438 20.249 1.00 37.72  ? 73  THR C CA  1 
ATOM   4141 C C   . THR C 1 74  ? 29.943  -23.880 19.901 1.00 40.60  ? 73  THR C C   1 
ATOM   4142 O O   . THR C 1 74  ? 29.890  -24.292 18.744 1.00 46.20  ? 73  THR C O   1 
ATOM   4143 C CB  . THR C 1 74  ? 31.722  -22.364 20.798 1.00 47.11  ? 73  THR C CB  1 
ATOM   4144 O OG1 . THR C 1 74  ? 32.068  -20.984 21.009 1.00 51.24  ? 73  THR C OG1 1 
ATOM   4145 C CG2 . THR C 1 74  ? 32.719  -22.955 19.813 1.00 45.33  ? 73  THR C CG2 1 
ATOM   4146 N N   . LEU C 1 75  ? 29.692  -24.682 20.933 1.00 31.01  ? 74  LEU C N   1 
ATOM   4147 C CA  . LEU C 1 75  ? 29.372  -26.088 20.709 1.00 39.94  ? 74  LEU C CA  1 
ATOM   4148 C C   . LEU C 1 75  ? 28.036  -26.231 20.001 1.00 37.85  ? 74  LEU C C   1 
ATOM   4149 O O   . LEU C 1 75  ? 27.793  -27.140 19.208 1.00 41.95  ? 74  LEU C O   1 
ATOM   4150 C CB  . LEU C 1 75  ? 29.341  -26.833 22.054 1.00 40.95  ? 74  LEU C CB  1 
ATOM   4151 C CG  . LEU C 1 75  ? 30.685  -26.855 22.791 1.00 39.23  ? 74  LEU C CG  1 
ATOM   4152 C CD1 . LEU C 1 75  ? 30.583  -27.648 24.083 1.00 56.68  ? 74  LEU C CD1 1 
ATOM   4153 C CD2 . LEU C 1 75  ? 31.764  -27.434 21.886 1.00 41.65  ? 74  LEU C CD2 1 
ATOM   4154 N N   . ALA C 1 76  ? 27.164  -25.282 20.347 1.00 30.98  ? 75  ALA C N   1 
ATOM   4155 C CA  . ALA C 1 76  ? 25.826  -25.298 19.765 1.00 31.42  ? 75  ALA C CA  1 
ATOM   4156 C C   . ALA C 1 76  ? 25.925  -25.041 18.265 1.00 29.76  ? 75  ALA C C   1 
ATOM   4157 O O   . ALA C 1 76  ? 25.299  -25.683 17.427 1.00 35.82  ? 75  ALA C O   1 
ATOM   4158 C CB  . ALA C 1 76  ? 24.947  -24.270 20.462 1.00 26.33  ? 75  ALA C CB  1 
ATOM   4159 N N   . LEU C 1 77  ? 26.754  -24.050 17.933 1.00 28.64  ? 76  LEU C N   1 
ATOM   4160 C CA  . LEU C 1 77  ? 26.938  -23.682 16.533 1.00 28.52  ? 76  LEU C CA  1 
ATOM   4161 C C   . LEU C 1 77  ? 27.476  -24.863 15.739 1.00 27.86  ? 76  LEU C C   1 
ATOM   4162 O O   . LEU C 1 77  ? 27.109  -25.146 14.608 1.00 37.26  ? 76  LEU C O   1 
ATOM   4163 C CB  . LEU C 1 77  ? 27.892  -22.493 16.453 1.00 18.31  ? 76  LEU C CB  1 
ATOM   4164 C CG  . LEU C 1 77  ? 27.213  -21.159 16.804 1.00 27.59  ? 76  LEU C CG  1 
ATOM   4165 C CD1 . LEU C 1 77  ? 28.241  -20.051 16.973 1.00 37.97  ? 76  LEU C CD1 1 
ATOM   4166 C CD2 . LEU C 1 77  ? 26.168  -20.848 15.746 1.00 19.06  ? 76  LEU C CD2 1 
ATOM   4167 N N   . LEU C 1 78  ? 28.389  -25.550 16.408 1.00 30.31  ? 77  LEU C N   1 
ATOM   4168 C CA  . LEU C 1 78  ? 28.962  -26.757 15.818 1.00 30.34  ? 77  LEU C CA  1 
ATOM   4169 C C   . LEU C 1 78  ? 27.814  -27.700 15.500 1.00 35.23  ? 77  LEU C C   1 
ATOM   4170 O O   . LEU C 1 78  ? 27.634  -28.113 14.359 1.00 40.57  ? 77  LEU C O   1 
ATOM   4171 C CB  . LEU C 1 78  ? 29.970  -27.339 16.797 1.00 25.67  ? 77  LEU C CB  1 
ATOM   4172 C CG  . LEU C 1 78  ? 30.623  -28.668 16.429 1.00 36.30  ? 77  LEU C CG  1 
ATOM   4173 C CD1 . LEU C 1 78  ? 31.390  -28.533 15.120 1.00 64.48  ? 77  LEU C CD1 1 
ATOM   4174 C CD2 . LEU C 1 78  ? 31.533  -29.150 17.549 1.00 45.54  ? 77  LEU C CD2 1 
ATOM   4175 N N   . VAL C 1 79  ? 27.044  -27.987 16.552 1.00 27.50  ? 78  VAL C N   1 
ATOM   4176 C CA  . VAL C 1 79  ? 25.956  -28.950 16.443 1.00 28.45  ? 78  VAL C CA  1 
ATOM   4177 C C   . VAL C 1 79  ? 24.961  -28.508 15.385 1.00 33.70  ? 78  VAL C C   1 
ATOM   4178 O O   . VAL C 1 79  ? 24.350  -29.290 14.659 1.00 30.79  ? 78  VAL C O   1 
ATOM   4179 C CB  . VAL C 1 79  ? 25.225  -29.113 17.789 1.00 35.06  ? 78  VAL C CB  1 
ATOM   4180 C CG1 . VAL C 1 79  ? 23.880  -29.791 17.578 1.00 23.26  ? 78  VAL C CG1 1 
ATOM   4181 C CG2 . VAL C 1 79  ? 26.111  -29.873 18.769 1.00 35.48  ? 78  VAL C CG2 1 
ATOM   4182 N N   . GLY C 1 80  ? 24.806  -27.186 15.311 1.00 33.32  ? 79  GLY C N   1 
ATOM   4183 C CA  . GLY C 1 80  ? 23.885  -26.648 14.319 1.00 36.85  ? 79  GLY C CA  1 
ATOM   4184 C C   . GLY C 1 80  ? 24.543  -26.583 12.947 1.00 33.01  ? 79  GLY C C   1 
ATOM   4185 O O   . GLY C 1 80  ? 23.922  -26.019 12.049 1.00 39.57  ? 79  GLY C O   1 
ATOM   4186 N N   . ASN C 1 81  ? 25.752  -27.126 12.811 1.00 31.70  ? 80  ASN C N   1 
ATOM   4187 C CA  . ASN C 1 81  ? 26.488  -27.095 11.551 1.00 35.55  ? 80  ASN C CA  1 
ATOM   4188 C C   . ASN C 1 81  ? 26.764  -25.676 11.060 1.00 48.74  ? 80  ASN C C   1 
ATOM   4189 O O   . ASN C 1 81  ? 26.572  -25.427 9.859  1.00 62.03  ? 80  ASN C O   1 
ATOM   4190 C CB  . ASN C 1 81  ? 25.713  -27.841 10.462 1.00 38.49  ? 80  ASN C CB  1 
ATOM   4191 C CG  . ASN C 1 81  ? 26.557  -28.440 9.355  1.00 41.09  ? 80  ASN C CG  1 
ATOM   4192 O OD1 . ASN C 1 81  ? 27.785  -28.481 9.375  1.00 40.58  ? 80  ASN C OD1 1 
ATOM   4193 N ND2 . ASN C 1 81  ? 25.873  -28.948 8.336  1.00 28.88  ? 80  ASN C ND2 1 
ATOM   4194 N N   . GLN C 1 82  ? 27.190  -24.776 11.942 1.00 56.23  ? 81  GLN C N   1 
ATOM   4195 C CA  . GLN C 1 82  ? 27.469  -23.383 11.602 1.00 44.76  ? 81  GLN C CA  1 
ATOM   4196 C C   . GLN C 1 82  ? 28.959  -23.080 11.644 1.00 41.64  ? 81  GLN C C   1 
ATOM   4197 O O   . GLN C 1 82  ? 29.415  -22.038 11.170 1.00 52.51  ? 81  GLN C O   1 
ATOM   4198 C CB  . GLN C 1 82  ? 26.738  -22.411 12.540 1.00 21.13  ? 81  GLN C CB  1 
ATOM   4199 C CG  . GLN C 1 82  ? 25.242  -22.435 12.231 1.00 22.17  ? 81  GLN C CG  1 
ATOM   4200 C CD  . GLN C 1 82  ? 24.956  -21.631 10.975 1.00 29.81  ? 81  GLN C CD  1 
ATOM   4201 O OE1 . GLN C 1 82  ? 25.656  -20.654 10.719 1.00 42.19  ? 81  GLN C OE1 1 
ATOM   4202 N NE2 . GLN C 1 82  ? 23.950  -22.010 10.198 1.00 41.23  ? 81  GLN C NE2 1 
ATOM   4203 N N   . ILE C 1 83  ? 29.713  -23.999 12.234 1.00 30.50  ? 82  ILE C N   1 
ATOM   4204 C CA  . ILE C 1 83  ? 31.151  -23.857 12.371 1.00 34.33  ? 82  ILE C CA  1 
ATOM   4205 C C   . ILE C 1 83  ? 31.807  -25.245 12.345 1.00 44.08  ? 82  ILE C C   1 
ATOM   4206 O O   . ILE C 1 83  ? 31.167  -26.292 12.457 1.00 43.84  ? 82  ILE C O   1 
ATOM   4207 C CB  . ILE C 1 83  ? 31.611  -23.158 13.663 1.00 31.90  ? 82  ILE C CB  1 
ATOM   4208 C CG1 . ILE C 1 83  ? 31.322  -24.000 14.911 1.00 22.62  ? 82  ILE C CG1 1 
ATOM   4209 C CG2 . ILE C 1 83  ? 31.042  -21.765 13.828 1.00 39.35  ? 82  ILE C CG2 1 
ATOM   4210 C CD1 . ILE C 1 83  ? 31.321  -23.213 16.199 1.00 23.02  ? 82  ILE C CD1 1 
ATOM   4211 N N   . SER C 1 84  ? 33.129  -25.199 12.189 1.00 44.74  ? 83  SER C N   1 
ATOM   4212 C CA  . SER C 1 84  ? 33.884  -26.435 12.090 1.00 49.38  ? 83  SER C CA  1 
ATOM   4213 C C   . SER C 1 84  ? 34.312  -26.935 13.471 1.00 45.79  ? 83  SER C C   1 
ATOM   4214 O O   . SER C 1 84  ? 34.198  -26.166 14.427 1.00 51.69  ? 83  SER C O   1 
ATOM   4215 C CB  . SER C 1 84  ? 35.137  -26.248 11.229 1.00 40.20  ? 83  SER C CB  1 
ATOM   4216 O OG  . SER C 1 84  ? 36.202  -25.847 12.073 1.00 34.85  ? 83  SER C OG  1 
ATOM   4217 N N   . LEU C 1 85  ? 34.784  -28.164 13.495 1.00 45.30  ? 84  LEU C N   1 
ATOM   4218 C CA  . LEU C 1 85  ? 35.183  -28.962 14.645 1.00 42.22  ? 84  LEU C CA  1 
ATOM   4219 C C   . LEU C 1 85  ? 36.401  -28.398 15.370 1.00 44.21  ? 84  LEU C C   1 
ATOM   4220 O O   . LEU C 1 85  ? 36.452  -28.344 16.602 1.00 38.40  ? 84  LEU C O   1 
ATOM   4221 C CB  . LEU C 1 85  ? 35.465  -30.391 14.161 1.00 41.94  ? 84  LEU C CB  1 
ATOM   4222 C CG  . LEU C 1 85  ? 35.903  -31.381 15.240 1.00 53.94  ? 84  LEU C CG  1 
ATOM   4223 C CD1 . LEU C 1 85  ? 35.016  -31.247 16.474 1.00 51.67  ? 84  LEU C CD1 1 
ATOM   4224 C CD2 . LEU C 1 85  ? 35.899  -32.796 14.681 1.00 36.67  ? 84  LEU C CD2 1 
ATOM   4225 N N   . LEU C 1 86  ? 37.373  -27.989 14.565 1.00 40.62  ? 85  LEU C N   1 
ATOM   4226 C CA  . LEU C 1 86  ? 38.599  -27.332 14.963 1.00 37.29  ? 85  LEU C CA  1 
ATOM   4227 C C   . LEU C 1 86  ? 38.350  -25.880 15.355 1.00 38.89  ? 85  LEU C C   1 
ATOM   4228 O O   . LEU C 1 86  ? 38.976  -25.302 16.245 1.00 40.03  ? 85  LEU C O   1 
ATOM   4229 C CB  . LEU C 1 86  ? 39.588  -27.371 13.789 1.00 48.84  ? 85  LEU C CB  1 
ATOM   4230 C CG  . LEU C 1 86  ? 40.025  -28.775 13.369 1.00 58.10  ? 85  LEU C CG  1 
ATOM   4231 C CD1 . LEU C 1 86  ? 41.345  -28.734 12.618 1.00 29.39  ? 85  LEU C CD1 1 
ATOM   4232 C CD2 . LEU C 1 86  ? 40.114  -29.670 14.600 1.00 82.24  ? 85  LEU C CD2 1 
ATOM   4233 N N   . ARG C 1 87  ? 37.398  -25.280 14.625 1.00 30.08  ? 86  ARG C N   1 
ATOM   4234 C CA  . ARG C 1 87  ? 36.971  -23.939 15.000 1.00 33.24  ? 86  ARG C CA  1 
ATOM   4235 C C   . ARG C 1 87  ? 36.474  -24.003 16.444 1.00 31.52  ? 86  ARG C C   1 
ATOM   4236 O O   . ARG C 1 87  ? 36.971  -23.289 17.310 1.00 63.83  ? 86  ARG C O   1 
ATOM   4237 C CB  . ARG C 1 87  ? 35.872  -23.416 14.081 1.00 41.97  ? 86  ARG C CB  1 
ATOM   4238 C CG  . ARG C 1 87  ? 35.380  -22.033 14.489 1.00 41.05  ? 86  ARG C CG  1 
ATOM   4239 C CD  . ARG C 1 87  ? 34.807  -21.282 13.304 1.00 35.27  ? 86  ARG C CD  1 
ATOM   4240 N NE  . ARG C 1 87  ? 35.748  -21.085 12.221 1.00 34.09  ? 86  ARG C NE  1 
ATOM   4241 C CZ  . ARG C 1 87  ? 36.553  -20.055 12.015 1.00 46.77  ? 86  ARG C CZ  1 
ATOM   4242 N NH1 . ARG C 1 87  ? 36.621  -18.999 12.816 1.00 37.28  ? 86  ARG C NH1 1 
ATOM   4243 N NH2 . ARG C 1 87  ? 37.351  -20.061 10.947 1.00 45.84  ? 86  ARG C NH2 1 
ATOM   4244 N N   . ALA C 1 88  ? 35.509  -24.889 16.664 1.00 29.21  ? 87  ALA C N   1 
ATOM   4245 C CA  . ALA C 1 88  ? 34.922  -25.083 17.985 1.00 29.41  ? 87  ALA C CA  1 
ATOM   4246 C C   . ALA C 1 88  ? 35.971  -25.509 19.009 1.00 36.86  ? 87  ALA C C   1 
ATOM   4247 O O   . ALA C 1 88  ? 36.020  -24.922 20.098 1.00 31.88  ? 87  ALA C O   1 
ATOM   4248 C CB  . ALA C 1 88  ? 33.782  -26.082 17.907 1.00 17.53  ? 87  ALA C CB  1 
ATOM   4249 N N   . PHE C 1 89  ? 36.805  -26.496 18.684 1.00 44.97  ? 88  PHE C N   1 
ATOM   4250 C CA  . PHE C 1 89  ? 37.845  -26.962 19.594 1.00 38.13  ? 88  PHE C CA  1 
ATOM   4251 C C   . PHE C 1 89  ? 38.671  -25.795 20.137 1.00 43.66  ? 88  PHE C C   1 
ATOM   4252 O O   . PHE C 1 89  ? 38.642  -25.468 21.325 1.00 42.12  ? 88  PHE C O   1 
ATOM   4253 C CB  . PHE C 1 89  ? 38.776  -27.985 18.925 1.00 42.13  ? 88  PHE C CB  1 
ATOM   4254 C CG  . PHE C 1 89  ? 39.923  -28.398 19.846 1.00 47.75  ? 88  PHE C CG  1 
ATOM   4255 C CD1 . PHE C 1 89  ? 39.717  -29.315 20.862 1.00 42.83  ? 88  PHE C CD1 1 
ATOM   4256 C CD2 . PHE C 1 89  ? 41.192  -27.871 19.694 1.00 50.37  ? 88  PHE C CD2 1 
ATOM   4257 C CE1 . PHE C 1 89  ? 40.745  -29.675 21.702 1.00 43.69  ? 88  PHE C CE1 1 
ATOM   4258 C CE2 . PHE C 1 89  ? 42.228  -28.211 20.539 1.00 44.74  ? 88  PHE C CE2 1 
ATOM   4259 C CZ  . PHE C 1 89  ? 42.003  -29.120 21.550 1.00 43.89  ? 88  PHE C CZ  1 
ATOM   4260 N N   . PHE C 1 90  ? 39.401  -25.157 19.230 1.00 43.63  ? 89  PHE C N   1 
ATOM   4261 C CA  . PHE C 1 90  ? 40.298  -24.064 19.557 1.00 29.91  ? 89  PHE C CA  1 
ATOM   4262 C C   . PHE C 1 90  ? 39.606  -22.902 20.258 1.00 24.94  ? 89  PHE C C   1 
ATOM   4263 O O   . PHE C 1 90  ? 40.243  -22.317 21.143 1.00 33.58  ? 89  PHE C O   1 
ATOM   4264 C CB  . PHE C 1 90  ? 40.993  -23.596 18.265 1.00 36.66  ? 89  PHE C CB  1 
ATOM   4265 C CG  . PHE C 1 90  ? 42.218  -24.435 17.924 1.00 42.60  ? 89  PHE C CG  1 
ATOM   4266 C CD1 . PHE C 1 90  ? 43.418  -24.254 18.588 1.00 42.12  ? 89  PHE C CD1 1 
ATOM   4267 C CD2 . PHE C 1 90  ? 42.162  -25.406 16.938 1.00 53.39  ? 89  PHE C CD2 1 
ATOM   4268 C CE1 . PHE C 1 90  ? 44.531  -25.016 18.282 1.00 49.33  ? 89  PHE C CE1 1 
ATOM   4269 C CE2 . PHE C 1 90  ? 43.270  -26.174 16.621 1.00 52.68  ? 89  PHE C CE2 1 
ATOM   4270 C CZ  . PHE C 1 90  ? 44.464  -25.981 17.294 1.00 49.27  ? 89  PHE C CZ  1 
ATOM   4271 N N   . TYR C 1 91  ? 38.376  -22.525 19.930 1.00 33.69  ? 90  TYR C N   1 
ATOM   4272 C CA  . TYR C 1 91  ? 37.691  -21.407 20.582 1.00 37.59  ? 90  TYR C CA  1 
ATOM   4273 C C   . TYR C 1 91  ? 37.361  -21.694 22.054 1.00 46.33  ? 90  TYR C C   1 
ATOM   4274 O O   . TYR C 1 91  ? 37.698  -20.957 22.978 1.00 41.57  ? 90  TYR C O   1 
ATOM   4275 C CB  . TYR C 1 91  ? 36.371  -21.064 19.912 1.00 25.02  ? 90  TYR C CB  1 
ATOM   4276 C CG  . TYR C 1 91  ? 36.343  -20.232 18.670 1.00 40.29  ? 90  TYR C CG  1 
ATOM   4277 C CD1 . TYR C 1 91  ? 37.473  -20.011 17.883 1.00 39.99  ? 90  TYR C CD1 1 
ATOM   4278 C CD2 . TYR C 1 91  ? 35.139  -19.648 18.266 1.00 42.03  ? 90  TYR C CD2 1 
ATOM   4279 C CE1 . TYR C 1 91  ? 37.417  -19.235 16.738 1.00 32.30  ? 90  TYR C CE1 1 
ATOM   4280 C CE2 . TYR C 1 91  ? 35.084  -18.875 17.115 1.00 44.16  ? 90  TYR C CE2 1 
ATOM   4281 C CZ  . TYR C 1 91  ? 36.217  -18.669 16.355 1.00 40.70  ? 90  TYR C CZ  1 
ATOM   4282 O OH  . TYR C 1 91  ? 36.139  -17.897 15.213 1.00 44.11  ? 90  TYR C OH  1 
ATOM   4283 N N   . VAL C 1 92  ? 36.661  -22.810 22.264 1.00 45.22  ? 91  VAL C N   1 
ATOM   4284 C CA  . VAL C 1 92  ? 36.277  -23.243 23.604 1.00 37.33  ? 91  VAL C CA  1 
ATOM   4285 C C   . VAL C 1 92  ? 37.541  -23.336 24.444 1.00 23.04  ? 91  VAL C C   1 
ATOM   4286 O O   . VAL C 1 92  ? 37.593  -22.983 25.616 1.00 33.06  ? 91  VAL C O   1 
ATOM   4287 C CB  . VAL C 1 92  ? 35.530  -24.587 23.578 1.00 42.02  ? 91  VAL C CB  1 
ATOM   4288 C CG1 . VAL C 1 92  ? 35.368  -25.151 24.988 1.00 33.61  ? 91  VAL C CG1 1 
ATOM   4289 C CG2 . VAL C 1 92  ? 34.169  -24.454 22.901 1.00 20.01  ? 91  VAL C CG2 1 
ATOM   4290 N N   . ALA C 1 93  ? 38.577  -23.821 23.769 1.00 26.37  ? 92  ALA C N   1 
ATOM   4291 C CA  . ALA C 1 93  ? 39.919  -23.850 24.322 1.00 42.01  ? 92  ALA C CA  1 
ATOM   4292 C C   . ALA C 1 93  ? 40.298  -22.477 24.887 1.00 45.91  ? 92  ALA C C   1 
ATOM   4293 O O   . ALA C 1 93  ? 40.590  -22.380 26.080 1.00 39.45  ? 92  ALA C O   1 
ATOM   4294 C CB  . ALA C 1 93  ? 40.919  -24.277 23.257 1.00 66.62  ? 92  ALA C CB  1 
ATOM   4295 N N   . ALA C 1 94  ? 40.276  -21.502 23.993 1.00 41.22  ? 93  ALA C N   1 
ATOM   4296 C CA  . ALA C 1 94  ? 40.619  -20.107 24.187 1.00 38.18  ? 93  ALA C CA  1 
ATOM   4297 C C   . ALA C 1 94  ? 39.744  -19.397 25.214 1.00 34.98  ? 93  ALA C C   1 
ATOM   4298 O O   . ALA C 1 94  ? 40.209  -18.688 26.116 1.00 27.68  ? 93  ALA C O   1 
ATOM   4299 C CB  . ALA C 1 94  ? 40.501  -19.417 22.827 1.00 35.94  ? 93  ALA C CB  1 
ATOM   4300 N N   . GLN C 1 95  ? 38.429  -19.585 25.066 1.00 35.08  ? 94  GLN C N   1 
ATOM   4301 C CA  . GLN C 1 95  ? 37.485  -19.004 26.017 1.00 36.72  ? 94  GLN C CA  1 
ATOM   4302 C C   . GLN C 1 95  ? 37.861  -19.416 27.444 1.00 38.56  ? 94  GLN C C   1 
ATOM   4303 O O   . GLN C 1 95  ? 38.009  -18.521 28.277 1.00 38.75  ? 94  GLN C O   1 
ATOM   4304 C CB  . GLN C 1 95  ? 36.045  -19.404 25.705 1.00 28.89  ? 94  GLN C CB  1 
ATOM   4305 C CG  . GLN C 1 95  ? 35.520  -18.959 24.363 1.00 22.28  ? 94  GLN C CG  1 
ATOM   4306 C CD  . GLN C 1 95  ? 34.449  -19.776 23.696 1.00 29.94  ? 94  GLN C CD  1 
ATOM   4307 O OE1 . GLN C 1 95  ? 33.811  -19.304 22.740 1.00 33.89  ? 94  GLN C OE1 1 
ATOM   4308 N NE2 . GLN C 1 95  ? 34.210  -20.997 24.161 1.00 31.45  ? 94  GLN C NE2 1 
ATOM   4309 N N   . LEU C 1 96  ? 38.021  -20.717 27.674 1.00 48.91  ? 95  LEU C N   1 
ATOM   4310 C CA  . LEU C 1 96  ? 38.336  -21.263 28.997 1.00 54.63  ? 95  LEU C CA  1 
ATOM   4311 C C   . LEU C 1 96  ? 39.598  -20.630 29.568 1.00 49.32  ? 95  LEU C C   1 
ATOM   4312 O O   . LEU C 1 96  ? 39.653  -20.117 30.678 1.00 34.87  ? 95  LEU C O   1 
ATOM   4313 C CB  . LEU C 1 96  ? 38.503  -22.788 28.981 1.00 40.38  ? 95  LEU C CB  1 
ATOM   4314 C CG  . LEU C 1 96  ? 37.225  -23.603 28.786 1.00 37.09  ? 95  LEU C CG  1 
ATOM   4315 C CD1 . LEU C 1 96  ? 37.525  -25.099 28.768 1.00 14.25  ? 95  LEU C CD1 1 
ATOM   4316 C CD2 . LEU C 1 96  ? 36.204  -23.265 29.870 1.00 28.53  ? 95  LEU C CD2 1 
ATOM   4317 N N   . VAL C 1 97  ? 40.664  -20.656 28.767 1.00 42.53  ? 96  VAL C N   1 
ATOM   4318 C CA  . VAL C 1 97  ? 41.887  -20.055 29.275 1.00 29.88  ? 96  VAL C CA  1 
ATOM   4319 C C   . VAL C 1 97  ? 41.731  -18.552 29.399 1.00 26.09  ? 96  VAL C C   1 
ATOM   4320 O O   . VAL C 1 97  ? 42.359  -17.935 30.244 1.00 30.47  ? 96  VAL C O   1 
ATOM   4321 C CB  . VAL C 1 97  ? 43.058  -20.349 28.327 1.00 36.36  ? 96  VAL C CB  1 
ATOM   4322 C CG1 . VAL C 1 97  ? 44.349  -19.802 28.914 1.00 78.61  ? 96  VAL C CG1 1 
ATOM   4323 C CG2 . VAL C 1 97  ? 43.124  -21.843 28.050 1.00 54.24  ? 96  VAL C CG2 1 
ATOM   4324 N N   . GLY C 1 98  ? 40.896  -17.979 28.527 1.00 38.78  ? 97  GLY C N   1 
ATOM   4325 C CA  . GLY C 1 98  ? 40.714  -16.527 28.562 1.00 29.39  ? 97  GLY C CA  1 
ATOM   4326 C C   . GLY C 1 98  ? 39.992  -16.139 29.836 1.00 23.32  ? 97  GLY C C   1 
ATOM   4327 O O   . GLY C 1 98  ? 40.332  -15.142 30.461 1.00 29.55  ? 97  GLY C O   1 
ATOM   4328 N N   . ALA C 1 99  ? 39.001  -16.952 30.213 1.00 26.55  ? 98  ALA C N   1 
ATOM   4329 C CA  . ALA C 1 99  ? 38.269  -16.700 31.455 1.00 30.52  ? 98  ALA C CA  1 
ATOM   4330 C C   . ALA C 1 99  ? 39.169  -16.823 32.684 1.00 28.16  ? 98  ALA C C   1 
ATOM   4331 O O   . ALA C 1 99  ? 39.098  -15.970 33.568 1.00 32.81  ? 98  ALA C O   1 
ATOM   4332 C CB  . ALA C 1 99  ? 37.078  -17.639 31.598 1.00 22.57  ? 98  ALA C CB  1 
ATOM   4333 N N   . ILE C 1 100 ? 39.984  -17.874 32.722 1.00 36.45  ? 99  ILE C N   1 
ATOM   4334 C CA  . ILE C 1 100 ? 40.942  -18.067 33.817 1.00 43.97  ? 99  ILE C CA  1 
ATOM   4335 C C   . ILE C 1 100 ? 41.733  -16.769 33.982 1.00 38.36  ? 99  ILE C C   1 
ATOM   4336 O O   . ILE C 1 100 ? 41.750  -16.160 35.051 1.00 52.30  ? 99  ILE C O   1 
ATOM   4337 C CB  . ILE C 1 100 ? 41.906  -19.244 33.592 1.00 54.71  ? 99  ILE C CB  1 
ATOM   4338 C CG1 . ILE C 1 100 ? 41.285  -20.640 33.687 1.00 53.21  ? 99  ILE C CG1 1 
ATOM   4339 C CG2 . ILE C 1 100 ? 43.092  -19.151 34.542 1.00 50.35  ? 99  ILE C CG2 1 
ATOM   4340 C CD1 . ILE C 1 100 ? 42.083  -21.763 33.059 1.00 28.51  ? 99  ILE C CD1 1 
ATOM   4341 N N   . ALA C 1 101 ? 42.336  -16.367 32.871 1.00 33.07  ? 100 ALA C N   1 
ATOM   4342 C CA  . ALA C 1 101 ? 43.091  -15.127 32.766 1.00 30.89  ? 100 ALA C CA  1 
ATOM   4343 C C   . ALA C 1 101 ? 42.356  -13.934 33.364 1.00 37.32  ? 100 ALA C C   1 
ATOM   4344 O O   . ALA C 1 101 ? 42.936  -13.127 34.103 1.00 39.68  ? 100 ALA C O   1 
ATOM   4345 C CB  . ALA C 1 101 ? 43.402  -14.856 31.298 1.00 35.48  ? 100 ALA C CB  1 
ATOM   4346 N N   . GLY C 1 102 ? 41.068  -13.800 33.038 1.00 32.40  ? 101 GLY C N   1 
ATOM   4347 C CA  . GLY C 1 102 ? 40.320  -12.626 33.473 1.00 30.31  ? 101 GLY C CA  1 
ATOM   4348 C C   . GLY C 1 102 ? 40.059  -12.667 34.969 1.00 34.74  ? 101 GLY C C   1 
ATOM   4349 O O   . GLY C 1 102 ? 40.138  -11.656 35.678 1.00 34.91  ? 101 GLY C O   1 
ATOM   4350 N N   . ALA C 1 103 ? 39.743  -13.870 35.466 1.00 25.46  ? 102 ALA C N   1 
ATOM   4351 C CA  . ALA C 1 103 ? 39.557  -13.979 36.912 1.00 27.46  ? 102 ALA C CA  1 
ATOM   4352 C C   . ALA C 1 103 ? 40.850  -13.626 37.643 1.00 23.46  ? 102 ALA C C   1 
ATOM   4353 O O   . ALA C 1 103 ? 40.848  -12.964 38.680 1.00 35.86  ? 102 ALA C O   1 
ATOM   4354 C CB  . ALA C 1 103 ? 39.104  -15.371 37.307 1.00 25.50  ? 102 ALA C CB  1 
ATOM   4355 N N   . GLY C 1 104 ? 41.953  -14.089 37.071 1.00 26.24  ? 103 GLY C N   1 
ATOM   4356 C CA  . GLY C 1 104 ? 43.259  -13.832 37.645 1.00 22.81  ? 103 GLY C CA  1 
ATOM   4357 C C   . GLY C 1 104 ? 43.596  -12.360 37.677 1.00 29.14  ? 103 GLY C C   1 
ATOM   4358 O O   . GLY C 1 104 ? 44.059  -11.846 38.696 1.00 63.55  ? 103 GLY C O   1 
ATOM   4359 N N   . ILE C 1 105 ? 43.378  -11.654 36.565 1.00 36.66  ? 104 ILE C N   1 
ATOM   4360 C CA  . ILE C 1 105 ? 43.733  -10.229 36.568 1.00 37.01  ? 104 ILE C CA  1 
ATOM   4361 C C   . ILE C 1 105 ? 42.943  -9.510  37.644 1.00 32.59  ? 104 ILE C C   1 
ATOM   4362 O O   . ILE C 1 105 ? 43.413  -8.676  38.414 1.00 34.69  ? 104 ILE C O   1 
ATOM   4363 C CB  . ILE C 1 105 ? 43.483  -9.615  35.187 1.00 41.80  ? 104 ILE C CB  1 
ATOM   4364 C CG1 . ILE C 1 105 ? 44.277  -10.310 34.075 1.00 48.48  ? 104 ILE C CG1 1 
ATOM   4365 C CG2 . ILE C 1 105 ? 43.756  -8.123  35.165 1.00 23.62  ? 104 ILE C CG2 1 
ATOM   4366 C CD1 . ILE C 1 105 ? 43.436  -10.653 32.867 1.00 33.36  ? 104 ILE C CD1 1 
ATOM   4367 N N   . LEU C 1 106 ? 41.665  -9.881  37.727 1.00 39.61  ? 105 LEU C N   1 
ATOM   4368 C CA  . LEU C 1 106 ? 40.818  -9.304  38.760 1.00 38.59  ? 105 LEU C CA  1 
ATOM   4369 C C   . LEU C 1 106 ? 41.263  -9.704  40.161 1.00 48.61  ? 105 LEU C C   1 
ATOM   4370 O O   . LEU C 1 106 ? 41.297  -8.884  41.082 1.00 43.58  ? 105 LEU C O   1 
ATOM   4371 C CB  . LEU C 1 106 ? 39.355  -9.735  38.565 1.00 30.64  ? 105 LEU C CB  1 
ATOM   4372 C CG  . LEU C 1 106 ? 38.440  -9.308  39.713 1.00 30.09  ? 105 LEU C CG  1 
ATOM   4373 C CD1 . LEU C 1 106 ? 38.482  -7.795  39.871 1.00 45.27  ? 105 LEU C CD1 1 
ATOM   4374 C CD2 . LEU C 1 106 ? 37.021  -9.804  39.506 1.00 29.20  ? 105 LEU C CD2 1 
ATOM   4375 N N   . TYR C 1 107 ? 41.588  -10.984 40.334 1.00 53.08  ? 106 TYR C N   1 
ATOM   4376 C CA  . TYR C 1 107 ? 42.001  -11.440 41.669 1.00 60.52  ? 106 TYR C CA  1 
ATOM   4377 C C   . TYR C 1 107 ? 43.224  -10.643 42.097 1.00 54.94  ? 106 TYR C C   1 
ATOM   4378 O O   . TYR C 1 107 ? 43.392  -10.194 43.231 1.00 40.24  ? 106 TYR C O   1 
ATOM   4379 C CB  . TYR C 1 107 ? 42.241  -12.937 41.645 1.00 70.93  ? 106 TYR C CB  1 
ATOM   4380 C CG  . TYR C 1 107 ? 43.187  -13.561 42.630 1.00 78.15  ? 106 TYR C CG  1 
ATOM   4381 C CD1 . TYR C 1 107 ? 43.101  -13.334 43.997 1.00 80.91  ? 106 TYR C CD1 1 
ATOM   4382 C CD2 . TYR C 1 107 ? 44.200  -14.408 42.199 1.00 84.27  ? 106 TYR C CD2 1 
ATOM   4383 C CE1 . TYR C 1 107 ? 43.996  -13.938 44.857 1.00 86.60  ? 106 TYR C CE1 1 
ATOM   4384 C CE2 . TYR C 1 107 ? 45.100  -15.012 43.056 1.00 85.48  ? 106 TYR C CE2 1 
ATOM   4385 C CZ  . TYR C 1 107 ? 44.990  -14.765 44.408 1.00 89.46  ? 106 TYR C CZ  1 
ATOM   4386 O OH  . TYR C 1 107 ? 45.857  -15.338 45.309 1.00 98.92  ? 106 TYR C OH  1 
ATOM   4387 N N   . GLY C 1 108 ? 44.125  -10.435 41.130 1.00 52.26  ? 107 GLY C N   1 
ATOM   4388 C CA  . GLY C 1 108 ? 45.331  -9.706  41.498 1.00 51.36  ? 107 GLY C CA  1 
ATOM   4389 C C   . GLY C 1 108 ? 45.066  -8.228  41.622 1.00 45.31  ? 107 GLY C C   1 
ATOM   4390 O O   . GLY C 1 108 ? 45.969  -7.447  41.909 1.00 35.04  ? 107 GLY C O   1 
ATOM   4391 N N   . VAL C 1 109 ? 43.823  -7.797  41.394 1.00 47.59  ? 108 VAL C N   1 
ATOM   4392 C CA  . VAL C 1 109 ? 43.607  -6.347  41.374 1.00 34.73  ? 108 VAL C CA  1 
ATOM   4393 C C   . VAL C 1 109 ? 42.551  -5.901  42.367 1.00 34.08  ? 108 VAL C C   1 
ATOM   4394 O O   . VAL C 1 109 ? 42.514  -4.717  42.732 1.00 40.75  ? 108 VAL C O   1 
ATOM   4395 C CB  . VAL C 1 109 ? 43.245  -5.931  39.934 1.00 40.93  ? 108 VAL C CB  1 
ATOM   4396 C CG1 . VAL C 1 109 ? 42.620  -4.562  39.927 1.00 32.56  ? 108 VAL C CG1 1 
ATOM   4397 C CG2 . VAL C 1 109 ? 44.482  -5.944  39.040 1.00 53.45  ? 108 VAL C CG2 1 
ATOM   4398 N N   . ALA C 1 110 ? 41.688  -6.788  42.846 1.00 29.66  ? 109 ALA C N   1 
ATOM   4399 C CA  . ALA C 1 110 ? 40.624  -6.422  43.779 1.00 31.68  ? 109 ALA C CA  1 
ATOM   4400 C C   . ALA C 1 110 ? 41.129  -6.255  45.208 1.00 38.01  ? 109 ALA C C   1 
ATOM   4401 O O   . ALA C 1 110 ? 41.958  -7.075  45.628 1.00 33.16  ? 109 ALA C O   1 
ATOM   4402 C CB  . ALA C 1 110 ? 39.522  -7.475  43.763 1.00 35.52  ? 109 ALA C CB  1 
ATOM   4403 N N   . PRO C 1 111 ? 40.647  -5.249  45.930 1.00 42.57  ? 110 PRO C N   1 
ATOM   4404 C CA  . PRO C 1 111 ? 41.095  -5.017  47.312 1.00 45.19  ? 110 PRO C CA  1 
ATOM   4405 C C   . PRO C 1 111 ? 40.637  -6.189  48.183 1.00 47.00  ? 110 PRO C C   1 
ATOM   4406 O O   . PRO C 1 111 ? 39.501  -6.615  47.971 1.00 45.55  ? 110 PRO C O   1 
ATOM   4407 C CB  . PRO C 1 111 ? 40.366  -3.754  47.764 1.00 37.60  ? 110 PRO C CB  1 
ATOM   4408 C CG  . PRO C 1 111 ? 39.145  -3.758  46.903 1.00 48.40  ? 110 PRO C CG  1 
ATOM   4409 C CD  . PRO C 1 111 ? 39.631  -4.251  45.554 1.00 44.97  ? 110 PRO C CD  1 
ATOM   4410 N N   . LEU C 1 112 ? 41.504  -6.636  49.064 1.00 45.84  ? 111 LEU C N   1 
ATOM   4411 C CA  . LEU C 1 112 ? 41.313  -7.702  50.028 1.00 48.95  ? 111 LEU C CA  1 
ATOM   4412 C C   . LEU C 1 112 ? 39.884  -7.743  50.569 1.00 44.22  ? 111 LEU C C   1 
ATOM   4413 O O   . LEU C 1 112 ? 39.252  -8.803  50.558 1.00 41.92  ? 111 LEU C O   1 
ATOM   4414 C CB  . LEU C 1 112 ? 42.271  -7.529  51.208 1.00 71.34  ? 111 LEU C CB  1 
ATOM   4415 C CG  . LEU C 1 112 ? 43.774  -7.465  50.922 1.00 85.86  ? 111 LEU C CG  1 
ATOM   4416 C CD1 . LEU C 1 112 ? 44.198  -6.167  50.257 1.00 100.70 ? 111 LEU C CD1 1 
ATOM   4417 C CD2 . LEU C 1 112 ? 44.562  -7.661  52.219 1.00 104.42 ? 111 LEU C CD2 1 
ATOM   4418 N N   . ASN C 1 113 ? 39.411  -6.591  51.037 1.00 38.98  ? 112 ASN C N   1 
ATOM   4419 C CA  . ASN C 1 113 ? 38.071  -6.406  51.572 1.00 43.86  ? 112 ASN C CA  1 
ATOM   4420 C C   . ASN C 1 113 ? 36.988  -6.614  50.517 1.00 50.00  ? 112 ASN C C   1 
ATOM   4421 O O   . ASN C 1 113 ? 35.791  -6.656  50.814 1.00 34.88  ? 112 ASN C O   1 
ATOM   4422 C CB  . ASN C 1 113 ? 37.916  -5.010  52.175 1.00 43.40  ? 112 ASN C CB  1 
ATOM   4423 C CG  . ASN C 1 113 ? 37.861  -3.888  51.165 1.00 45.91  ? 112 ASN C CG  1 
ATOM   4424 O OD1 . ASN C 1 113 ? 38.095  -4.064  49.966 1.00 81.42  ? 112 ASN C OD1 1 
ATOM   4425 N ND2 . ASN C 1 113 ? 37.549  -2.688  51.655 1.00 33.35  ? 112 ASN C ND2 1 
ATOM   4426 N N   . ALA C 1 114 ? 37.378  -6.743  49.254 1.00 53.76  ? 113 ALA C N   1 
ATOM   4427 C CA  . ALA C 1 114 ? 36.421  -6.934  48.174 1.00 49.06  ? 113 ALA C CA  1 
ATOM   4428 C C   . ALA C 1 114 ? 36.462  -8.366  47.649 1.00 40.54  ? 113 ALA C C   1 
ATOM   4429 O O   . ALA C 1 114 ? 35.447  -8.872  47.171 1.00 42.13  ? 113 ALA C O   1 
ATOM   4430 C CB  . ALA C 1 114 ? 36.687  -5.950  47.041 1.00 25.45  ? 113 ALA C CB  1 
ATOM   4431 N N   . ARG C 1 115 ? 37.636  -8.977  47.748 1.00 34.44  ? 114 ARG C N   1 
ATOM   4432 C CA  . ARG C 1 115 ? 37.936  -10.198 47.022 1.00 40.06  ? 114 ARG C CA  1 
ATOM   4433 C C   . ARG C 1 115 ? 36.963  -11.341 47.313 1.00 46.26  ? 114 ARG C C   1 
ATOM   4434 O O   . ARG C 1 115 ? 36.457  -11.923 46.343 1.00 31.01  ? 114 ARG C O   1 
ATOM   4435 C CB  . ARG C 1 115 ? 39.378  -10.662 47.295 1.00 40.87  ? 114 ARG C CB  1 
ATOM   4436 C CG  . ARG C 1 115 ? 39.675  -11.988 46.600 1.00 49.81  ? 114 ARG C CG  1 
ATOM   4437 C CD  . ARG C 1 115 ? 41.041  -12.539 46.959 1.00 53.80  ? 114 ARG C CD  1 
ATOM   4438 N NE  . ARG C 1 115 ? 42.068  -11.503 46.833 1.00 69.69  ? 114 ARG C NE  1 
ATOM   4439 C CZ  . ARG C 1 115 ? 43.333  -11.707 47.181 1.00 79.70  ? 114 ARG C CZ  1 
ATOM   4440 N NH1 . ARG C 1 115 ? 43.661  -12.907 47.652 1.00 69.76  ? 114 ARG C NH1 1 
ATOM   4441 N NH2 . ARG C 1 115 ? 44.242  -10.753 47.053 1.00 95.55  ? 114 ARG C NH2 1 
ATOM   4442 N N   . GLY C 1 116 ? 36.732  -11.639 48.580 1.00 39.05  ? 115 GLY C N   1 
ATOM   4443 C CA  . GLY C 1 116 ? 35.956  -12.753 49.065 1.00 35.36  ? 115 GLY C CA  1 
ATOM   4444 C C   . GLY C 1 116 ? 36.024  -13.985 48.161 1.00 30.21  ? 115 GLY C C   1 
ATOM   4445 O O   . GLY C 1 116 ? 37.098  -14.547 47.979 1.00 28.47  ? 115 GLY C O   1 
ATOM   4446 N N   . ASN C 1 117 ? 34.889  -14.313 47.620 1.00 34.80  ? 116 ASN C N   1 
ATOM   4447 C CA  . ASN C 1 117 ? 34.291  -15.323 46.807 1.00 51.33  ? 116 ASN C CA  1 
ATOM   4448 C C   . ASN C 1 117 ? 35.250  -16.013 45.836 1.00 54.05  ? 116 ASN C C   1 
ATOM   4449 O O   . ASN C 1 117 ? 35.726  -17.092 46.247 1.00 88.64  ? 116 ASN C O   1 
ATOM   4450 C CB  . ASN C 1 117 ? 33.110  -14.748 46.002 1.00 64.17  ? 116 ASN C CB  1 
ATOM   4451 C CG  . ASN C 1 117 ? 32.869  -13.262 46.072 1.00 55.42  ? 116 ASN C CG  1 
ATOM   4452 O OD1 . ASN C 1 117 ? 33.715  -12.448 46.443 1.00 56.11  ? 116 ASN C OD1 1 
ATOM   4453 N ND2 . ASN C 1 117 ? 31.656  -12.853 45.694 1.00 45.36  ? 116 ASN C ND2 1 
ATOM   4454 N N   . LEU C 1 118 ? 35.539  -15.575 44.656 1.00 33.77  ? 117 LEU C N   1 
ATOM   4455 C CA  . LEU C 1 118 ? 35.603  -14.450 43.777 1.00 32.75  ? 117 LEU C CA  1 
ATOM   4456 C C   . LEU C 1 118 ? 34.508  -14.397 42.713 1.00 36.42  ? 117 LEU C C   1 
ATOM   4457 O O   . LEU C 1 118 ? 34.766  -14.642 41.529 1.00 31.52  ? 117 LEU C O   1 
ATOM   4458 C CB  . LEU C 1 118 ? 36.969  -14.558 43.091 1.00 31.24  ? 117 LEU C CB  1 
ATOM   4459 C CG  . LEU C 1 118 ? 37.513  -13.395 42.289 1.00 37.92  ? 117 LEU C CG  1 
ATOM   4460 C CD1 . LEU C 1 118 ? 37.925  -12.241 43.192 1.00 35.21  ? 117 LEU C CD1 1 
ATOM   4461 C CD2 . LEU C 1 118 ? 38.704  -13.848 41.446 1.00 37.01  ? 117 LEU C CD2 1 
ATOM   4462 N N   . ALA C 1 119 ? 33.270  -14.092 43.079 1.00 27.43  ? 118 ALA C N   1 
ATOM   4463 C CA  . ALA C 1 119 ? 32.119  -14.082 42.195 1.00 28.36  ? 118 ALA C CA  1 
ATOM   4464 C C   . ALA C 1 119 ? 31.889  -15.426 41.509 1.00 34.68  ? 118 ALA C C   1 
ATOM   4465 O O   . ALA C 1 119 ? 31.336  -15.458 40.403 1.00 44.58  ? 118 ALA C O   1 
ATOM   4466 C CB  . ALA C 1 119 ? 32.262  -12.998 41.135 1.00 33.07  ? 118 ALA C CB  1 
ATOM   4467 N N   . VAL C 1 120 ? 32.283  -16.523 42.142 1.00 34.34  ? 119 VAL C N   1 
ATOM   4468 C CA  . VAL C 1 120 ? 32.062  -17.878 41.646 1.00 19.64  ? 119 VAL C CA  1 
ATOM   4469 C C   . VAL C 1 120 ? 30.585  -18.207 41.593 1.00 17.58  ? 119 VAL C C   1 
ATOM   4470 O O   . VAL C 1 120 ? 29.817  -17.671 42.391 1.00 34.06  ? 119 VAL C O   1 
ATOM   4471 C CB  . VAL C 1 120 ? 32.744  -18.913 42.548 1.00 31.79  ? 119 VAL C CB  1 
ATOM   4472 C CG1 . VAL C 1 120 ? 34.255  -18.841 42.408 1.00 35.28  ? 119 VAL C CG1 1 
ATOM   4473 C CG2 . VAL C 1 120 ? 32.302  -18.661 43.985 1.00 42.67  ? 119 VAL C CG2 1 
ATOM   4474 N N   . ASN C 1 121 ? 30.176  -19.075 40.673 1.00 24.13  ? 120 ASN C N   1 
ATOM   4475 C CA  . ASN C 1 121 ? 28.758  -19.431 40.631 1.00 37.17  ? 120 ASN C CA  1 
ATOM   4476 C C   . ASN C 1 121 ? 28.407  -20.336 41.806 1.00 50.21  ? 120 ASN C C   1 
ATOM   4477 O O   . ASN C 1 121 ? 29.225  -21.153 42.245 1.00 69.93  ? 120 ASN C O   1 
ATOM   4478 C CB  . ASN C 1 121 ? 28.425  -20.093 39.293 1.00 31.25  ? 120 ASN C CB  1 
ATOM   4479 C CG  . ASN C 1 121 ? 28.145  -19.065 38.213 1.00 34.01  ? 120 ASN C CG  1 
ATOM   4480 O OD1 . ASN C 1 121 ? 28.950  -18.867 37.307 1.00 48.64  ? 120 ASN C OD1 1 
ATOM   4481 N ND2 . ASN C 1 121 ? 26.999  -18.405 38.309 1.00 39.17  ? 120 ASN C ND2 1 
ATOM   4482 N N   . ALA C 1 122 ? 27.191  -20.219 42.345 1.00 44.62  ? 121 ALA C N   1 
ATOM   4483 C CA  . ALA C 1 122 ? 26.877  -20.989 43.552 1.00 36.23  ? 121 ALA C CA  1 
ATOM   4484 C C   . ALA C 1 122 ? 25.382  -21.115 43.803 1.00 31.07  ? 121 ALA C C   1 
ATOM   4485 O O   . ALA C 1 122 ? 24.661  -20.111 43.767 1.00 46.92  ? 121 ALA C O   1 
ATOM   4486 C CB  . ALA C 1 122 ? 27.576  -20.321 44.729 1.00 40.40  ? 121 ALA C CB  1 
ATOM   4487 N N   . LEU C 1 123 ? 24.939  -22.337 44.067 1.00 30.76  ? 122 LEU C N   1 
ATOM   4488 C CA  . LEU C 1 123 ? 23.542  -22.725 44.205 1.00 32.30  ? 122 LEU C CA  1 
ATOM   4489 C C   . LEU C 1 123 ? 22.790  -22.142 45.393 1.00 35.68  ? 122 LEU C C   1 
ATOM   4490 O O   . LEU C 1 123 ? 23.357  -21.997 46.474 1.00 62.12  ? 122 LEU C O   1 
ATOM   4491 C CB  . LEU C 1 123 ? 23.465  -24.263 44.266 1.00 32.43  ? 122 LEU C CB  1 
ATOM   4492 C CG  . LEU C 1 123 ? 23.106  -24.907 42.920 1.00 40.14  ? 122 LEU C CG  1 
ATOM   4493 C CD1 . LEU C 1 123 ? 23.126  -26.420 43.009 1.00 75.03  ? 122 LEU C CD1 1 
ATOM   4494 C CD2 . LEU C 1 123 ? 21.748  -24.390 42.487 1.00 45.54  ? 122 LEU C CD2 1 
ATOM   4495 N N   . ASN C 1 124 ? 21.517  -21.829 45.170 1.00 37.50  ? 123 ASN C N   1 
ATOM   4496 C CA  . ASN C 1 124 ? 20.587  -21.134 46.033 1.00 50.18  ? 123 ASN C CA  1 
ATOM   4497 C C   . ASN C 1 124 ? 20.385  -21.773 47.395 1.00 64.40  ? 123 ASN C C   1 
ATOM   4498 O O   . ASN C 1 124 ? 19.493  -21.315 48.135 1.00 67.25  ? 123 ASN C O   1 
ATOM   4499 C CB  . ASN C 1 124 ? 19.198  -21.030 45.381 1.00 53.08  ? 123 ASN C CB  1 
ATOM   4500 C CG  . ASN C 1 124 ? 18.197  -20.166 46.122 1.00 54.46  ? 123 ASN C CG  1 
ATOM   4501 O OD1 . ASN C 1 124 ? 17.345  -19.514 45.502 1.00 44.63  ? 123 ASN C OD1 1 
ATOM   4502 N ND2 . ASN C 1 124 ? 18.229  -20.126 47.451 1.00 57.13  ? 123 ASN C ND2 1 
ATOM   4503 N N   . ASN C 1 125 ? 21.100  -22.806 47.803 1.00 61.23  ? 124 ASN C N   1 
ATOM   4504 C CA  . ASN C 1 125 ? 20.872  -23.410 49.112 1.00 63.75  ? 124 ASN C CA  1 
ATOM   4505 C C   . ASN C 1 125 ? 19.514  -24.091 49.219 1.00 57.64  ? 124 ASN C C   1 
ATOM   4506 O O   . ASN C 1 125 ? 19.436  -25.254 49.632 1.00 71.00  ? 124 ASN C O   1 
ATOM   4507 C CB  . ASN C 1 125 ? 21.011  -22.370 50.230 1.00 78.33  ? 124 ASN C CB  1 
ATOM   4508 C CG  . ASN C 1 125 ? 20.795  -23.000 51.602 1.00 89.85  ? 124 ASN C CG  1 
ATOM   4509 O OD1 . ASN C 1 125 ? 21.250  -24.127 51.861 1.00 106.25 ? 124 ASN C OD1 1 
ATOM   4510 N ND2 . ASN C 1 125 ? 20.075  -22.277 52.489 1.00 102.31 ? 124 ASN C ND2 1 
ATOM   4511 N N   . ASN C 1 126 ? 18.414  -23.438 48.883 1.00 51.08  ? 125 ASN C N   1 
ATOM   4512 C CA  . ASN C 1 126 ? 17.099  -24.066 48.842 1.00 47.87  ? 125 ASN C CA  1 
ATOM   4513 C C   . ASN C 1 126 ? 16.837  -24.564 47.428 1.00 43.80  ? 125 ASN C C   1 
ATOM   4514 O O   . ASN C 1 126 ? 15.713  -24.877 47.047 1.00 44.10  ? 125 ASN C O   1 
ATOM   4515 C CB  . ASN C 1 126 ? 16.032  -23.085 49.331 1.00 53.49  ? 125 ASN C CB  1 
ATOM   4516 C CG  . ASN C 1 126 ? 16.395  -22.483 50.681 1.00 49.91  ? 125 ASN C CG  1 
ATOM   4517 O OD1 . ASN C 1 126 ? 16.656  -21.284 50.785 1.00 49.33  ? 125 ASN C OD1 1 
ATOM   4518 N ND2 . ASN C 1 126 ? 16.420  -23.298 51.730 1.00 49.68  ? 125 ASN C ND2 1 
ATOM   4519 N N   . THR C 1 127 ? 17.931  -24.634 46.647 1.00 46.39  ? 126 THR C N   1 
ATOM   4520 C CA  . THR C 1 127 ? 17.787  -25.128 45.284 1.00 45.48  ? 126 THR C CA  1 
ATOM   4521 C C   . THR C 1 127 ? 18.622  -26.385 45.041 1.00 42.78  ? 126 THR C C   1 
ATOM   4522 O O   . THR C 1 127 ? 19.816  -26.376 45.324 1.00 50.04  ? 126 THR C O   1 
ATOM   4523 C CB  . THR C 1 127 ? 18.188  -24.090 44.219 1.00 36.86  ? 126 THR C CB  1 
ATOM   4524 O OG1 . THR C 1 127 ? 17.072  -23.242 43.954 1.00 41.43  ? 126 THR C OG1 1 
ATOM   4525 C CG2 . THR C 1 127 ? 18.507  -24.798 42.915 1.00 36.23  ? 126 THR C CG2 1 
ATOM   4526 N N   . THR C 1 128 ? 17.950  -27.401 44.513 1.00 44.40  ? 127 THR C N   1 
ATOM   4527 C CA  . THR C 1 128 ? 18.558  -28.673 44.140 1.00 34.27  ? 127 THR C CA  1 
ATOM   4528 C C   . THR C 1 128 ? 19.187  -28.569 42.747 1.00 38.26  ? 127 THR C C   1 
ATOM   4529 O O   . THR C 1 128 ? 18.887  -27.686 41.935 1.00 27.66  ? 127 THR C O   1 
ATOM   4530 C CB  . THR C 1 128 ? 17.560  -29.842 44.210 1.00 38.77  ? 127 THR C CB  1 
ATOM   4531 O OG1 . THR C 1 128 ? 16.643  -29.804 43.106 1.00 67.18  ? 127 THR C OG1 1 
ATOM   4532 C CG2 . THR C 1 128 ? 16.692  -29.783 45.469 1.00 28.64  ? 127 THR C CG2 1 
ATOM   4533 N N   . GLN C 1 129 ? 20.100  -29.492 42.481 1.00 35.69  ? 128 GLN C N   1 
ATOM   4534 C CA  . GLN C 1 129 ? 20.915  -29.454 41.271 1.00 38.12  ? 128 GLN C CA  1 
ATOM   4535 C C   . GLN C 1 129 ? 20.063  -29.694 40.041 1.00 42.15  ? 128 GLN C C   1 
ATOM   4536 O O   . GLN C 1 129 ? 20.342  -29.284 38.914 1.00 35.66  ? 128 GLN C O   1 
ATOM   4537 C CB  . GLN C 1 129 ? 22.051  -30.477 41.398 1.00 43.40  ? 128 GLN C CB  1 
ATOM   4538 C CG  . GLN C 1 129 ? 23.129  -30.104 42.407 1.00 46.47  ? 128 GLN C CG  1 
ATOM   4539 C CD  . GLN C 1 129 ? 24.254  -31.107 42.550 1.00 51.76  ? 128 GLN C CD  1 
ATOM   4540 O OE1 . GLN C 1 129 ? 24.340  -32.088 41.804 1.00 47.33  ? 128 GLN C OE1 1 
ATOM   4541 N NE2 . GLN C 1 129 ? 25.151  -30.894 43.513 1.00 40.19  ? 128 GLN C NE2 1 
ATOM   4542 N N   . GLY C 1 130 ? 18.947  -30.394 40.242 1.00 41.41  ? 129 GLY C N   1 
ATOM   4543 C CA  . GLY C 1 130 ? 18.130  -30.684 39.066 1.00 46.25  ? 129 GLY C CA  1 
ATOM   4544 C C   . GLY C 1 130 ? 17.280  -29.472 38.719 1.00 43.31  ? 129 GLY C C   1 
ATOM   4545 O O   . GLY C 1 130 ? 17.066  -29.112 37.566 1.00 39.43  ? 129 GLY C O   1 
ATOM   4546 N N   . GLN C 1 131 ? 16.798  -28.849 39.789 1.00 36.54  ? 130 GLN C N   1 
ATOM   4547 C CA  . GLN C 1 131 ? 16.071  -27.602 39.656 1.00 37.65  ? 130 GLN C CA  1 
ATOM   4548 C C   . GLN C 1 131 ? 16.886  -26.562 38.878 1.00 38.19  ? 130 GLN C C   1 
ATOM   4549 O O   . GLN C 1 131 ? 16.365  -26.010 37.907 1.00 25.35  ? 130 GLN C O   1 
ATOM   4550 C CB  . GLN C 1 131 ? 15.751  -27.062 41.050 1.00 37.15  ? 130 GLN C CB  1 
ATOM   4551 C CG  . GLN C 1 131 ? 14.882  -28.028 41.847 1.00 52.19  ? 130 GLN C CG  1 
ATOM   4552 C CD  . GLN C 1 131 ? 14.237  -27.336 43.036 1.00 44.72  ? 130 GLN C CD  1 
ATOM   4553 O OE1 . GLN C 1 131 ? 14.925  -26.953 43.981 1.00 72.26  ? 130 GLN C OE1 1 
ATOM   4554 N NE2 . GLN C 1 131 ? 12.922  -27.183 42.951 1.00 33.78  ? 130 GLN C NE2 1 
ATOM   4555 N N   . ALA C 1 132 ? 18.099  -26.356 39.355 1.00 31.56  ? 131 ALA C N   1 
ATOM   4556 C CA  . ALA C 1 132 ? 19.175  -25.518 38.874 1.00 40.49  ? 131 ALA C CA  1 
ATOM   4557 C C   . ALA C 1 132 ? 19.605  -25.835 37.440 1.00 37.90  ? 131 ALA C C   1 
ATOM   4558 O O   . ALA C 1 132 ? 19.876  -24.944 36.633 1.00 34.96  ? 131 ALA C O   1 
ATOM   4559 C CB  . ALA C 1 132 ? 20.384  -25.678 39.786 1.00 30.16  ? 131 ALA C CB  1 
ATOM   4560 N N   . MET C 1 133 ? 19.661  -27.125 37.146 1.00 31.01  ? 132 MET C N   1 
ATOM   4561 C CA  . MET C 1 133 ? 19.924  -27.645 35.820 1.00 25.84  ? 132 MET C CA  1 
ATOM   4562 C C   . MET C 1 133 ? 18.891  -27.199 34.799 1.00 25.95  ? 132 MET C C   1 
ATOM   4563 O O   . MET C 1 133 ? 19.226  -26.794 33.691 1.00 39.94  ? 132 MET C O   1 
ATOM   4564 C CB  . MET C 1 133 ? 19.925  -29.175 35.873 1.00 33.85  ? 132 MET C CB  1 
ATOM   4565 C CG  . MET C 1 133 ? 21.207  -29.752 35.281 1.00 45.25  ? 132 MET C CG  1 
ATOM   4566 S SD  . MET C 1 133 ? 21.099  -29.994 33.507 1.00 82.33  ? 132 MET C SD  1 
ATOM   4567 C CE  . MET C 1 133 ? 19.332  -30.250 33.291 1.00 79.11  ? 132 MET C CE  1 
ATOM   4568 N N   . VAL C 1 134 ? 17.623  -27.289 35.176 1.00 27.98  ? 133 VAL C N   1 
ATOM   4569 C CA  . VAL C 1 134 ? 16.555  -26.825 34.297 1.00 27.51  ? 133 VAL C CA  1 
ATOM   4570 C C   . VAL C 1 134 ? 16.626  -25.316 34.097 1.00 30.15  ? 133 VAL C C   1 
ATOM   4571 O O   . VAL C 1 134 ? 16.521  -24.822 32.963 1.00 37.56  ? 133 VAL C O   1 
ATOM   4572 C CB  . VAL C 1 134 ? 15.200  -27.270 34.873 1.00 27.09  ? 133 VAL C CB  1 
ATOM   4573 C CG1 . VAL C 1 134 ? 14.010  -26.595 34.223 1.00 36.93  ? 133 VAL C CG1 1 
ATOM   4574 C CG2 . VAL C 1 134 ? 15.055  -28.787 34.706 1.00 36.26  ? 133 VAL C CG2 1 
ATOM   4575 N N   . VAL C 1 135 ? 16.797  -24.533 35.159 1.00 19.70  ? 134 VAL C N   1 
ATOM   4576 C CA  . VAL C 1 135 ? 16.854  -23.082 35.047 1.00 20.76  ? 134 VAL C CA  1 
ATOM   4577 C C   . VAL C 1 135 ? 17.988  -22.672 34.111 1.00 26.84  ? 134 VAL C C   1 
ATOM   4578 O O   . VAL C 1 135 ? 17.764  -21.898 33.184 1.00 59.34  ? 134 VAL C O   1 
ATOM   4579 C CB  . VAL C 1 135 ? 17.074  -22.389 36.404 1.00 30.19  ? 134 VAL C CB  1 
ATOM   4580 C CG1 . VAL C 1 135 ? 17.326  -20.896 36.225 1.00 30.28  ? 134 VAL C CG1 1 
ATOM   4581 C CG2 . VAL C 1 135 ? 15.883  -22.611 37.324 1.00 29.78  ? 134 VAL C CG2 1 
ATOM   4582 N N   . GLU C 1 136 ? 19.183  -23.190 34.359 1.00 27.00  ? 135 GLU C N   1 
ATOM   4583 C CA  . GLU C 1 136 ? 20.365  -22.919 33.548 1.00 29.01  ? 135 GLU C CA  1 
ATOM   4584 C C   . GLU C 1 136 ? 20.137  -23.284 32.085 1.00 26.16  ? 135 GLU C C   1 
ATOM   4585 O O   . GLU C 1 136 ? 20.469  -22.474 31.223 1.00 27.82  ? 135 GLU C O   1 
ATOM   4586 C CB  . GLU C 1 136 ? 21.581  -23.684 34.065 1.00 28.64  ? 135 GLU C CB  1 
ATOM   4587 C CG  . GLU C 1 136 ? 22.264  -23.027 35.255 1.00 22.49  ? 135 GLU C CG  1 
ATOM   4588 C CD  . GLU C 1 136 ? 22.948  -21.748 34.827 1.00 33.35  ? 135 GLU C CD  1 
ATOM   4589 O OE1 . GLU C 1 136 ? 23.195  -20.872 35.682 1.00 30.19  ? 135 GLU C OE1 1 
ATOM   4590 O OE2 . GLU C 1 136 ? 23.216  -21.651 33.607 1.00 42.45  ? 135 GLU C OE2 1 
ATOM   4591 N N   . LEU C 1 137 ? 19.587  -24.466 31.863 1.00 24.95  ? 136 LEU C N   1 
ATOM   4592 C CA  . LEU C 1 137 ? 19.118  -24.880 30.546 1.00 38.47  ? 136 LEU C CA  1 
ATOM   4593 C C   . LEU C 1 137 ? 18.378  -23.726 29.857 1.00 38.13  ? 136 LEU C C   1 
ATOM   4594 O O   . LEU C 1 137 ? 18.761  -23.280 28.778 1.00 28.12  ? 136 LEU C O   1 
ATOM   4595 C CB  . LEU C 1 137 ? 18.172  -26.073 30.658 1.00 34.51  ? 136 LEU C CB  1 
ATOM   4596 C CG  . LEU C 1 137 ? 17.889  -26.958 29.453 1.00 33.24  ? 136 LEU C CG  1 
ATOM   4597 C CD1 . LEU C 1 137 ? 17.308  -28.288 29.919 1.00 48.31  ? 136 LEU C CD1 1 
ATOM   4598 C CD2 . LEU C 1 137 ? 16.915  -26.332 28.465 1.00 26.40  ? 136 LEU C CD2 1 
ATOM   4599 N N   . ILE C 1 138 ? 17.319  -23.298 30.538 1.00 29.19  ? 137 ILE C N   1 
ATOM   4600 C CA  . ILE C 1 138 ? 16.372  -22.316 30.049 1.00 28.32  ? 137 ILE C CA  1 
ATOM   4601 C C   . ILE C 1 138 ? 17.038  -20.963 29.814 1.00 34.54  ? 137 ILE C C   1 
ATOM   4602 O O   . ILE C 1 138 ? 16.883  -20.335 28.752 1.00 33.29  ? 137 ILE C O   1 
ATOM   4603 C CB  . ILE C 1 138 ? 15.174  -22.151 31.003 1.00 26.67  ? 137 ILE C CB  1 
ATOM   4604 C CG1 . ILE C 1 138 ? 14.267  -23.375 31.055 1.00 41.60  ? 137 ILE C CG1 1 
ATOM   4605 C CG2 . ILE C 1 138 ? 14.397  -20.899 30.608 1.00 16.42  ? 137 ILE C CG2 1 
ATOM   4606 C CD1 . ILE C 1 138 ? 13.269  -23.461 32.188 1.00 30.64  ? 137 ILE C CD1 1 
ATOM   4607 N N   . LEU C 1 139 ? 17.779  -20.540 30.832 1.00 19.99  ? 138 LEU C N   1 
ATOM   4608 C CA  . LEU C 1 139 ? 18.525  -19.296 30.721 1.00 27.27  ? 138 LEU C CA  1 
ATOM   4609 C C   . LEU C 1 139 ? 19.376  -19.279 29.452 1.00 35.63  ? 138 LEU C C   1 
ATOM   4610 O O   . LEU C 1 139 ? 19.439  -18.277 28.737 1.00 32.58  ? 138 LEU C O   1 
ATOM   4611 C CB  . LEU C 1 139 ? 19.417  -19.098 31.949 1.00 30.69  ? 138 LEU C CB  1 
ATOM   4612 C CG  . LEU C 1 139 ? 18.748  -19.222 33.321 1.00 40.84  ? 138 LEU C CG  1 
ATOM   4613 C CD1 . LEU C 1 139 ? 19.697  -18.771 34.425 1.00 24.50  ? 138 LEU C CD1 1 
ATOM   4614 C CD2 . LEU C 1 139 ? 17.449  -18.434 33.387 1.00 43.63  ? 138 LEU C CD2 1 
ATOM   4615 N N   . THR C 1 140 ? 20.048  -20.401 29.178 1.00 29.07  ? 139 THR C N   1 
ATOM   4616 C CA  . THR C 1 140 ? 20.982  -20.417 28.050 1.00 25.20  ? 139 THR C CA  1 
ATOM   4617 C C   . THR C 1 140 ? 20.245  -20.672 26.746 1.00 31.24  ? 139 THR C C   1 
ATOM   4618 O O   . THR C 1 140 ? 20.701  -20.388 25.634 1.00 24.95  ? 139 THR C O   1 
ATOM   4619 C CB  . THR C 1 140 ? 22.094  -21.449 28.286 1.00 35.13  ? 139 THR C CB  1 
ATOM   4620 O OG1 . THR C 1 140 ? 22.631  -21.289 29.614 1.00 25.89  ? 139 THR C OG1 1 
ATOM   4621 C CG2 . THR C 1 140 ? 23.256  -21.214 27.327 1.00 45.31  ? 139 THR C CG2 1 
ATOM   4622 N N   . PHE C 1 141 ? 19.031  -21.215 26.852 1.00 22.77  ? 140 PHE C N   1 
ATOM   4623 C CA  . PHE C 1 141 ? 18.249  -21.478 25.647 1.00 22.46  ? 140 PHE C CA  1 
ATOM   4624 C C   . PHE C 1 141 ? 17.745  -20.219 24.962 1.00 25.08  ? 140 PHE C C   1 
ATOM   4625 O O   . PHE C 1 141 ? 17.889  -20.091 23.744 1.00 19.83  ? 140 PHE C O   1 
ATOM   4626 C CB  . PHE C 1 141 ? 17.058  -22.344 26.033 1.00 16.60  ? 140 PHE C CB  1 
ATOM   4627 C CG  . PHE C 1 141 ? 16.188  -22.771 24.879 1.00 19.07  ? 140 PHE C CG  1 
ATOM   4628 C CD1 . PHE C 1 141 ? 16.549  -23.894 24.151 1.00 20.32  ? 140 PHE C CD1 1 
ATOM   4629 C CD2 . PHE C 1 141 ? 15.049  -22.065 24.559 1.00 17.50  ? 140 PHE C CD2 1 
ATOM   4630 C CE1 . PHE C 1 141 ? 15.740  -24.301 23.110 1.00 25.91  ? 140 PHE C CE1 1 
ATOM   4631 C CE2 . PHE C 1 141 ? 14.238  -22.474 23.516 1.00 23.60  ? 140 PHE C CE2 1 
ATOM   4632 C CZ  . PHE C 1 141 ? 14.591  -23.600 22.801 1.00 29.54  ? 140 PHE C CZ  1 
ATOM   4633 N N   . GLN C 1 142 ? 17.158  -19.319 25.748 1.00 26.20  ? 141 GLN C N   1 
ATOM   4634 C CA  . GLN C 1 142 ? 16.642  -18.065 25.198 1.00 24.76  ? 141 GLN C CA  1 
ATOM   4635 C C   . GLN C 1 142 ? 17.790  -17.237 24.623 1.00 22.28  ? 141 GLN C C   1 
ATOM   4636 O O   . GLN C 1 142 ? 17.723  -16.702 23.513 1.00 31.09  ? 141 GLN C O   1 
ATOM   4637 C CB  . GLN C 1 142 ? 15.833  -17.293 26.233 1.00 25.34  ? 141 GLN C CB  1 
ATOM   4638 C CG  . GLN C 1 142 ? 16.469  -16.914 27.554 1.00 26.78  ? 141 GLN C CG  1 
ATOM   4639 C CD  . GLN C 1 142 ? 17.296  -15.636 27.441 1.00 29.90  ? 141 GLN C CD  1 
ATOM   4640 O OE1 . GLN C 1 142 ? 16.888  -14.774 26.663 1.00 27.30  ? 141 GLN C OE1 1 
ATOM   4641 N NE2 . GLN C 1 142 ? 18.440  -15.571 28.106 1.00 15.33  ? 141 GLN C NE2 1 
ATOM   4642 N N   . LEU C 1 143 ? 18.878  -17.119 25.388 1.00 21.18  ? 142 LEU C N   1 
ATOM   4643 C CA  . LEU C 1 143 ? 20.053  -16.378 24.940 1.00 14.78  ? 142 LEU C CA  1 
ATOM   4644 C C   . LEU C 1 143 ? 20.534  -16.869 23.571 1.00 23.01  ? 142 LEU C C   1 
ATOM   4645 O O   . LEU C 1 143 ? 20.613  -16.091 22.633 1.00 27.93  ? 142 LEU C O   1 
ATOM   4646 C CB  . LEU C 1 143 ? 21.210  -16.508 25.921 1.00 8.56   ? 142 LEU C CB  1 
ATOM   4647 C CG  . LEU C 1 143 ? 22.586  -16.163 25.364 1.00 21.72  ? 142 LEU C CG  1 
ATOM   4648 C CD1 . LEU C 1 143 ? 22.629  -14.708 24.912 1.00 23.18  ? 142 LEU C CD1 1 
ATOM   4649 C CD2 . LEU C 1 143 ? 23.659  -16.422 26.399 1.00 16.95  ? 142 LEU C CD2 1 
ATOM   4650 N N   . ALA C 1 144 ? 20.866  -18.142 23.442 1.00 23.99  ? 143 ALA C N   1 
ATOM   4651 C CA  . ALA C 1 144 ? 21.326  -18.715 22.185 1.00 30.54  ? 143 ALA C CA  1 
ATOM   4652 C C   . ALA C 1 144 ? 20.393  -18.457 21.008 1.00 34.82  ? 143 ALA C C   1 
ATOM   4653 O O   . ALA C 1 144 ? 20.857  -18.112 19.910 1.00 25.85  ? 143 ALA C O   1 
ATOM   4654 C CB  . ALA C 1 144 ? 21.528  -20.221 22.357 1.00 22.91  ? 143 ALA C CB  1 
ATOM   4655 N N   . LEU C 1 145 ? 19.074  -18.629 21.194 1.00 34.19  ? 144 LEU C N   1 
ATOM   4656 C CA  . LEU C 1 145 ? 18.242  -18.404 19.994 1.00 33.10  ? 144 LEU C CA  1 
ATOM   4657 C C   . LEU C 1 145 ? 18.168  -16.894 19.768 1.00 36.08  ? 144 LEU C C   1 
ATOM   4658 O O   . LEU C 1 145 ? 17.868  -16.427 18.666 1.00 27.36  ? 144 LEU C O   1 
ATOM   4659 C CB  . LEU C 1 145 ? 16.929  -19.123 20.058 1.00 29.12  ? 144 LEU C CB  1 
ATOM   4660 C CG  . LEU C 1 145 ? 15.680  -18.821 20.831 1.00 38.20  ? 144 LEU C CG  1 
ATOM   4661 C CD1 . LEU C 1 145 ? 14.415  -19.183 20.046 1.00 32.18  ? 144 LEU C CD1 1 
ATOM   4662 C CD2 . LEU C 1 145 ? 15.646  -19.582 22.152 1.00 67.77  ? 144 LEU C CD2 1 
ATOM   4663 N N   . CYS C 1 146 ? 18.496  -16.093 20.792 1.00 25.08  ? 145 CYS C N   1 
ATOM   4664 C CA  . CYS C 1 146 ? 18.599  -14.671 20.506 1.00 18.53  ? 145 CYS C CA  1 
ATOM   4665 C C   . CYS C 1 146 ? 19.770  -14.428 19.542 1.00 32.64  ? 145 CYS C C   1 
ATOM   4666 O O   . CYS C 1 146 ? 19.613  -13.700 18.551 1.00 31.28  ? 145 CYS C O   1 
ATOM   4667 C CB  . CYS C 1 146 ? 18.772  -13.805 21.756 1.00 18.64  ? 145 CYS C CB  1 
ATOM   4668 S SG  . CYS C 1 146 ? 18.632  -12.029 21.359 1.00 22.74  ? 145 CYS C SG  1 
ATOM   4669 N N   . ILE C 1 147 ? 20.891  -15.061 19.879 1.00 20.16  ? 146 ILE C N   1 
ATOM   4670 C CA  . ILE C 1 147 ? 22.109  -15.039 19.080 1.00 24.10  ? 146 ILE C CA  1 
ATOM   4671 C C   . ILE C 1 147 ? 21.829  -15.527 17.662 1.00 21.30  ? 146 ILE C C   1 
ATOM   4672 O O   . ILE C 1 147 ? 22.041  -14.810 16.690 1.00 31.26  ? 146 ILE C O   1 
ATOM   4673 C CB  . ILE C 1 147 ? 23.199  -15.910 19.721 1.00 32.16  ? 146 ILE C CB  1 
ATOM   4674 C CG1 . ILE C 1 147 ? 23.732  -15.362 21.056 1.00 25.92  ? 146 ILE C CG1 1 
ATOM   4675 C CG2 . ILE C 1 147 ? 24.369  -16.159 18.782 1.00 26.57  ? 146 ILE C CG2 1 
ATOM   4676 C CD1 . ILE C 1 147 ? 24.561  -16.394 21.797 1.00 25.84  ? 146 ILE C CD1 1 
ATOM   4677 N N   . PHE C 1 148 ? 21.326  -16.750 17.545 1.00 23.68  ? 147 PHE C N   1 
ATOM   4678 C CA  . PHE C 1 148 ? 21.125  -17.381 16.241 1.00 22.70  ? 147 PHE C CA  1 
ATOM   4679 C C   . PHE C 1 148 ? 20.203  -16.581 15.335 1.00 31.43  ? 147 PHE C C   1 
ATOM   4680 O O   . PHE C 1 148 ? 20.477  -16.472 14.129 1.00 30.54  ? 147 PHE C O   1 
ATOM   4681 C CB  . PHE C 1 148 ? 20.581  -18.799 16.445 1.00 21.70  ? 147 PHE C CB  1 
ATOM   4682 C CG  . PHE C 1 148 ? 21.479  -19.658 17.330 1.00 27.77  ? 147 PHE C CG  1 
ATOM   4683 C CD1 . PHE C 1 148 ? 22.820  -19.364 17.487 1.00 22.83  ? 147 PHE C CD1 1 
ATOM   4684 C CD2 . PHE C 1 148 ? 20.979  -20.752 18.016 1.00 23.33  ? 147 PHE C CD2 1 
ATOM   4685 C CE1 . PHE C 1 148 ? 23.628  -20.137 18.296 1.00 24.05  ? 147 PHE C CE1 1 
ATOM   4686 C CE2 . PHE C 1 148 ? 21.792  -21.536 18.804 1.00 20.64  ? 147 PHE C CE2 1 
ATOM   4687 C CZ  . PHE C 1 148 ? 23.137  -21.244 18.955 1.00 19.71  ? 147 PHE C CZ  1 
ATOM   4688 N N   . ALA C 1 149 ? 19.124  -16.022 15.890 1.00 27.80  ? 148 ALA C N   1 
ATOM   4689 C CA  . ALA C 1 149 ? 18.231  -15.185 15.089 1.00 28.59  ? 148 ALA C CA  1 
ATOM   4690 C C   . ALA C 1 149 ? 18.859  -13.840 14.718 1.00 31.66  ? 148 ALA C C   1 
ATOM   4691 O O   . ALA C 1 149 ? 18.556  -13.306 13.642 1.00 28.74  ? 148 ALA C O   1 
ATOM   4692 C CB  . ALA C 1 149 ? 16.902  -14.957 15.801 1.00 28.61  ? 148 ALA C CB  1 
ATOM   4693 N N   . SER C 1 150 ? 19.708  -13.301 15.584 1.00 33.49  ? 149 SER C N   1 
ATOM   4694 C CA  . SER C 1 150 ? 20.318  -11.992 15.420 1.00 32.20  ? 149 SER C CA  1 
ATOM   4695 C C   . SER C 1 150 ? 21.572  -12.032 14.555 1.00 32.63  ? 149 SER C C   1 
ATOM   4696 O O   . SER C 1 150 ? 22.072  -10.998 14.103 1.00 21.40  ? 149 SER C O   1 
ATOM   4697 C CB  . SER C 1 150 ? 20.667  -11.400 16.794 1.00 27.69  ? 149 SER C CB  1 
ATOM   4698 O OG  . SER C 1 150 ? 19.496  -11.315 17.593 1.00 39.14  ? 149 SER C OG  1 
ATOM   4699 N N   . THR C 1 151 ? 22.111  -13.220 14.297 1.00 32.45  ? 150 THR C N   1 
ATOM   4700 C CA  . THR C 1 151 ? 23.241  -13.307 13.374 1.00 32.58  ? 150 THR C CA  1 
ATOM   4701 C C   . THR C 1 151 ? 22.913  -14.116 12.122 1.00 29.87  ? 150 THR C C   1 
ATOM   4702 O O   . THR C 1 151 ? 23.810  -14.554 11.399 1.00 28.32  ? 150 THR C O   1 
ATOM   4703 C CB  . THR C 1 151 ? 24.485  -13.913 14.060 1.00 40.90  ? 150 THR C CB  1 
ATOM   4704 O OG1 . THR C 1 151 ? 24.178  -15.219 14.570 1.00 44.45  ? 150 THR C OG1 1 
ATOM   4705 C CG2 . THR C 1 151 ? 24.924  -13.032 15.226 1.00 30.83  ? 150 THR C CG2 1 
ATOM   4706 N N   . ASP C 1 152 ? 21.640  -14.344 11.824 1.00 22.68  ? 151 ASP C N   1 
ATOM   4707 C CA  . ASP C 1 152 ? 21.265  -15.050 10.606 1.00 30.97  ? 151 ASP C CA  1 
ATOM   4708 C C   . ASP C 1 152 ? 21.275  -14.156 9.371  1.00 30.97  ? 151 ASP C C   1 
ATOM   4709 O O   . ASP C 1 152 ? 20.428  -13.280 9.185  1.00 30.65  ? 151 ASP C O   1 
ATOM   4710 C CB  . ASP C 1 152 ? 19.861  -15.651 10.751 1.00 31.01  ? 151 ASP C CB  1 
ATOM   4711 C CG  . ASP C 1 152 ? 19.684  -16.773 9.740  1.00 35.22  ? 151 ASP C CG  1 
ATOM   4712 O OD1 . ASP C 1 152 ? 20.328  -16.694 8.674  1.00 35.53  ? 151 ASP C OD1 1 
ATOM   4713 O OD2 . ASP C 1 152 ? 18.908  -17.700 10.028 1.00 47.31  ? 151 ASP C OD2 1 
ATOM   4714 N N   . SER C 1 153 ? 22.234  -14.377 8.469  1.00 29.65  ? 152 SER C N   1 
ATOM   4715 C CA  . SER C 1 153 ? 22.351  -13.524 7.293  1.00 35.58  ? 152 SER C CA  1 
ATOM   4716 C C   . SER C 1 153 ? 21.101  -13.604 6.427  1.00 33.79  ? 152 SER C C   1 
ATOM   4717 O O   . SER C 1 153 ? 20.897  -12.699 5.619  1.00 39.53  ? 152 SER C O   1 
ATOM   4718 C CB  . SER C 1 153 ? 23.569  -13.865 6.426  1.00 33.74  ? 152 SER C CB  1 
ATOM   4719 O OG  . SER C 1 153 ? 23.443  -15.153 5.848  1.00 44.84  ? 152 SER C OG  1 
ATOM   4720 N N   . ARG C 1 154 ? 20.293  -14.647 6.593  1.00 30.86  ? 153 ARG C N   1 
ATOM   4721 C CA  . ARG C 1 154 ? 19.071  -14.711 5.799  1.00 35.10  ? 153 ARG C CA  1 
ATOM   4722 C C   . ARG C 1 154 ? 17.998  -13.813 6.390  1.00 41.78  ? 153 ARG C C   1 
ATOM   4723 O O   . ARG C 1 154 ? 16.903  -13.704 5.834  1.00 53.80  ? 153 ARG C O   1 
ATOM   4724 C CB  . ARG C 1 154 ? 18.568  -16.155 5.686  1.00 30.91  ? 153 ARG C CB  1 
ATOM   4725 C CG  . ARG C 1 154 ? 19.687  -17.128 5.320  1.00 35.51  ? 153 ARG C CG  1 
ATOM   4726 C CD  . ARG C 1 154 ? 19.282  -18.556 5.624  1.00 43.14  ? 153 ARG C CD  1 
ATOM   4727 N NE  . ARG C 1 154 ? 18.989  -18.832 7.027  1.00 44.16  ? 153 ARG C NE  1 
ATOM   4728 C CZ  . ARG C 1 154 ? 18.679  -20.021 7.531  1.00 45.68  ? 153 ARG C CZ  1 
ATOM   4729 N NH1 . ARG C 1 154 ? 18.610  -21.102 6.766  1.00 40.72  ? 153 ARG C NH1 1 
ATOM   4730 N NH2 . ARG C 1 154 ? 18.429  -20.166 8.830  1.00 48.37  ? 153 ARG C NH2 1 
ATOM   4731 N N   . ARG C 1 155 ? 18.268  -13.164 7.524  1.00 43.35  ? 154 ARG C N   1 
ATOM   4732 C CA  . ARG C 1 155 ? 17.180  -12.386 8.123  1.00 39.71  ? 154 ARG C CA  1 
ATOM   4733 C C   . ARG C 1 155 ? 16.815  -11.142 7.314  1.00 28.36  ? 154 ARG C C   1 
ATOM   4734 O O   . ARG C 1 155 ? 17.650  -10.299 7.005  1.00 43.18  ? 154 ARG C O   1 
ATOM   4735 C CB  . ARG C 1 155 ? 17.553  -11.990 9.556  1.00 35.26  ? 154 ARG C CB  1 
ATOM   4736 C CG  . ARG C 1 155 ? 16.406  -11.366 10.347 1.00 33.76  ? 154 ARG C CG  1 
ATOM   4737 C CD  . ARG C 1 155 ? 16.866  -11.025 11.765 1.00 34.80  ? 154 ARG C CD  1 
ATOM   4738 N NE  . ARG C 1 155 ? 16.000  -10.038 12.391 1.00 35.50  ? 154 ARG C NE  1 
ATOM   4739 C CZ  . ARG C 1 155 ? 15.399  -10.173 13.568 1.00 41.48  ? 154 ARG C CZ  1 
ATOM   4740 N NH1 . ARG C 1 155 ? 15.564  -11.276 14.293 1.00 19.03  ? 154 ARG C NH1 1 
ATOM   4741 N NH2 . ARG C 1 155 ? 14.631  -9.179  14.000 1.00 35.97  ? 154 ARG C NH2 1 
ATOM   4742 N N   . THR C 1 156 ? 15.530  -10.996 6.983  1.00 18.60  ? 155 THR C N   1 
ATOM   4743 C CA  . THR C 1 156 ? 15.017  -9.811  6.322  1.00 31.43  ? 155 THR C CA  1 
ATOM   4744 C C   . THR C 1 156 ? 14.364  -8.827  7.284  1.00 33.69  ? 155 THR C C   1 
ATOM   4745 O O   . THR C 1 156 ? 14.320  -7.630  7.001  1.00 48.72  ? 155 THR C O   1 
ATOM   4746 C CB  . THR C 1 156 ? 13.953  -10.204 5.275  1.00 39.92  ? 155 THR C CB  1 
ATOM   4747 O OG1 . THR C 1 156 ? 12.907  -10.933 5.932  1.00 37.55  ? 155 THR C OG1 1 
ATOM   4748 C CG2 . THR C 1 156 ? 14.601  -11.103 4.235  1.00 35.67  ? 155 THR C CG2 1 
ATOM   4749 N N   . SER C 1 157 ? 13.840  -9.313  8.409  1.00 35.15  ? 156 SER C N   1 
ATOM   4750 C CA  . SER C 1 157 ? 13.311  -8.381  9.410  1.00 36.13  ? 156 SER C CA  1 
ATOM   4751 C C   . SER C 1 157 ? 14.455  -7.568  10.006 1.00 30.52  ? 156 SER C C   1 
ATOM   4752 O O   . SER C 1 157 ? 15.466  -8.169  10.364 1.00 48.60  ? 156 SER C O   1 
ATOM   4753 C CB  . SER C 1 157 ? 12.564  -9.136  10.508 1.00 32.15  ? 156 SER C CB  1 
ATOM   4754 O OG  . SER C 1 157 ? 11.411  -9.738  9.930  1.00 81.89  ? 156 SER C OG  1 
ATOM   4755 N N   . PRO C 1 158 ? 14.298  -6.257  10.081 1.00 39.89  ? 157 PRO C N   1 
ATOM   4756 C CA  . PRO C 1 158 ? 15.311  -5.374  10.692 1.00 27.68  ? 157 PRO C CA  1 
ATOM   4757 C C   . PRO C 1 158 ? 15.821  -5.935  12.008 1.00 16.52  ? 157 PRO C C   1 
ATOM   4758 O O   . PRO C 1 158 ? 15.023  -6.271  12.890 1.00 27.97  ? 157 PRO C O   1 
ATOM   4759 C CB  . PRO C 1 158 ? 14.520  -4.082  10.892 1.00 29.96  ? 157 PRO C CB  1 
ATOM   4760 C CG  . PRO C 1 158 ? 13.560  -4.071  9.744  1.00 42.45  ? 157 PRO C CG  1 
ATOM   4761 C CD  . PRO C 1 158 ? 13.135  -5.506  9.555  1.00 46.97  ? 157 PRO C CD  1 
ATOM   4762 N N   . VAL C 1 159 ? 17.127  -6.093  12.162 1.00 23.02  ? 158 VAL C N   1 
ATOM   4763 C CA  . VAL C 1 159 ? 17.722  -6.742  13.318 1.00 27.45  ? 158 VAL C CA  1 
ATOM   4764 C C   . VAL C 1 159 ? 18.129  -5.775  14.422 1.00 28.79  ? 158 VAL C C   1 
ATOM   4765 O O   . VAL C 1 159 ? 18.735  -6.232  15.400 1.00 24.36  ? 158 VAL C O   1 
ATOM   4766 C CB  . VAL C 1 159 ? 18.997  -7.507  12.897 1.00 30.34  ? 158 VAL C CB  1 
ATOM   4767 C CG1 . VAL C 1 159 ? 20.137  -6.514  12.732 1.00 34.98  ? 158 VAL C CG1 1 
ATOM   4768 C CG2 . VAL C 1 159 ? 19.347  -8.590  13.900 1.00 23.91  ? 158 VAL C CG2 1 
ATOM   4769 N N   . GLY C 1 160 ? 17.822  -4.502  14.229 1.00 30.92  ? 159 GLY C N   1 
ATOM   4770 C CA  . GLY C 1 160 ? 18.233  -3.425  15.139 1.00 19.98  ? 159 GLY C CA  1 
ATOM   4771 C C   . GLY C 1 160 ? 19.728  -3.546  15.382 1.00 28.62  ? 159 GLY C C   1 
ATOM   4772 O O   . GLY C 1 160 ? 20.527  -3.430  14.444 1.00 19.39  ? 159 GLY C O   1 
ATOM   4773 N N   . SER C 1 161 ? 20.058  -3.804  16.649 1.00 31.98  ? 160 SER C N   1 
ATOM   4774 C CA  . SER C 1 161 ? 21.444  -4.018  17.052 1.00 21.54  ? 160 SER C CA  1 
ATOM   4775 C C   . SER C 1 161 ? 21.666  -5.438  17.531 1.00 23.89  ? 160 SER C C   1 
ATOM   4776 O O   . SER C 1 161 ? 21.218  -5.765  18.631 1.00 31.32  ? 160 SER C O   1 
ATOM   4777 C CB  . SER C 1 161 ? 21.814  -3.037  18.162 1.00 19.21  ? 160 SER C CB  1 
ATOM   4778 O OG  . SER C 1 161 ? 23.135  -3.302  18.633 1.00 25.74  ? 160 SER C OG  1 
ATOM   4779 N N   . PRO C 1 162 ? 22.332  -6.306  16.792 1.00 20.29  ? 161 PRO C N   1 
ATOM   4780 C CA  . PRO C 1 162 ? 22.456  -7.681  17.285 1.00 25.54  ? 161 PRO C CA  1 
ATOM   4781 C C   . PRO C 1 162 ? 23.249  -7.686  18.596 1.00 31.15  ? 161 PRO C C   1 
ATOM   4782 O O   . PRO C 1 162 ? 22.910  -8.457  19.498 1.00 34.34  ? 161 PRO C O   1 
ATOM   4783 C CB  . PRO C 1 162 ? 23.204  -8.443  16.197 1.00 19.46  ? 161 PRO C CB  1 
ATOM   4784 C CG  . PRO C 1 162 ? 23.163  -7.542  15.012 1.00 30.23  ? 161 PRO C CG  1 
ATOM   4785 C CD  . PRO C 1 162 ? 23.039  -6.131  15.521 1.00 33.33  ? 161 PRO C CD  1 
ATOM   4786 N N   . ALA C 1 163 ? 24.255  -6.823  18.681 1.00 21.35  ? 162 ALA C N   1 
ATOM   4787 C CA  . ALA C 1 163 ? 25.106  -6.747  19.859 1.00 26.69  ? 162 ALA C CA  1 
ATOM   4788 C C   . ALA C 1 163 ? 24.311  -6.410  21.119 1.00 23.59  ? 162 ALA C C   1 
ATOM   4789 O O   . ALA C 1 163 ? 24.387  -7.125  22.127 1.00 28.11  ? 162 ALA C O   1 
ATOM   4790 C CB  . ALA C 1 163 ? 26.210  -5.729  19.651 1.00 20.65  ? 162 ALA C CB  1 
ATOM   4791 N N   . LEU C 1 164 ? 23.562  -5.321  21.058 1.00 19.43  ? 163 LEU C N   1 
ATOM   4792 C CA  . LEU C 1 164 ? 22.792  -4.900  22.230 1.00 24.46  ? 163 LEU C CA  1 
ATOM   4793 C C   . LEU C 1 164 ? 21.618  -5.825  22.501 1.00 33.98  ? 163 LEU C C   1 
ATOM   4794 O O   . LEU C 1 164 ? 21.221  -6.058  23.648 1.00 31.25  ? 163 LEU C O   1 
ATOM   4795 C CB  . LEU C 1 164 ? 22.281  -3.470  22.058 1.00 31.45  ? 163 LEU C CB  1 
ATOM   4796 C CG  . LEU C 1 164 ? 23.328  -2.364  22.228 1.00 26.07  ? 163 LEU C CG  1 
ATOM   4797 C CD1 . LEU C 1 164 ? 22.741  -1.051  21.746 1.00 12.48  ? 163 LEU C CD1 1 
ATOM   4798 C CD2 . LEU C 1 164 ? 23.826  -2.269  23.665 1.00 24.13  ? 163 LEU C CD2 1 
ATOM   4799 N N   . SER C 1 165 ? 21.037  -6.366  21.422 1.00 25.94  ? 164 SER C N   1 
ATOM   4800 C CA  . SER C 1 165 ? 19.944  -7.298  21.677 1.00 25.91  ? 164 SER C CA  1 
ATOM   4801 C C   . SER C 1 165 ? 20.489  -8.483  22.472 1.00 28.85  ? 164 SER C C   1 
ATOM   4802 O O   . SER C 1 165 ? 19.832  -8.966  23.388 1.00 34.67  ? 164 SER C O   1 
ATOM   4803 C CB  . SER C 1 165 ? 19.266  -7.757  20.388 1.00 18.36  ? 164 SER C CB  1 
ATOM   4804 O OG  . SER C 1 165 ? 18.057  -7.060  20.148 1.00 22.34  ? 164 SER C OG  1 
ATOM   4805 N N   . ILE C 1 166 ? 21.689  -8.899  22.085 1.00 25.94  ? 165 ILE C N   1 
ATOM   4806 C CA  . ILE C 1 166 ? 22.303  -10.112 22.644 1.00 22.28  ? 165 ILE C CA  1 
ATOM   4807 C C   . ILE C 1 166 ? 22.798  -9.806  24.045 1.00 20.58  ? 165 ILE C C   1 
ATOM   4808 O O   . ILE C 1 166 ? 22.666  -10.568 24.997 1.00 14.96  ? 165 ILE C O   1 
ATOM   4809 C CB  . ILE C 1 166 ? 23.375  -10.617 21.660 1.00 21.96  ? 165 ILE C CB  1 
ATOM   4810 C CG1 . ILE C 1 166 ? 22.823  -11.523 20.528 1.00 15.76  ? 165 ILE C CG1 1 
ATOM   4811 C CG2 . ILE C 1 166 ? 24.514  -11.344 22.339 1.00 30.20  ? 165 ILE C CG2 1 
ATOM   4812 C CD1 . ILE C 1 166 ? 23.721  -11.546 19.312 1.00 23.18  ? 165 ILE C CD1 1 
ATOM   4813 N N   . GLY C 1 167 ? 23.392  -8.629  24.247 1.00 23.51  ? 166 GLY C N   1 
ATOM   4814 C CA  . GLY C 1 167 ? 23.782  -8.248  25.597 1.00 32.31  ? 166 GLY C CA  1 
ATOM   4815 C C   . GLY C 1 167 ? 22.574  -8.169  26.505 1.00 27.32  ? 166 GLY C C   1 
ATOM   4816 O O   . GLY C 1 167 ? 22.536  -8.678  27.627 1.00 34.47  ? 166 GLY C O   1 
ATOM   4817 N N   . LEU C 1 168 ? 21.494  -7.525  26.061 1.00 19.30  ? 167 LEU C N   1 
ATOM   4818 C CA  . LEU C 1 168 ? 20.365  -7.464  27.000 1.00 18.07  ? 167 LEU C CA  1 
ATOM   4819 C C   . LEU C 1 168 ? 19.766  -8.830  27.256 1.00 18.86  ? 167 LEU C C   1 
ATOM   4820 O O   . LEU C 1 168 ? 19.084  -9.022  28.270 1.00 22.73  ? 167 LEU C O   1 
ATOM   4821 C CB  . LEU C 1 168 ? 19.351  -6.458  26.448 1.00 18.43  ? 167 LEU C CB  1 
ATOM   4822 C CG  . LEU C 1 168 ? 20.007  -5.052  26.434 1.00 15.57  ? 167 LEU C CG  1 
ATOM   4823 C CD1 . LEU C 1 168 ? 19.182  -4.093  25.607 1.00 18.52  ? 167 LEU C CD1 1 
ATOM   4824 C CD2 . LEU C 1 168 ? 20.187  -4.588  27.876 1.00 15.71  ? 167 LEU C CD2 1 
ATOM   4825 N N   . SER C 1 169 ? 20.040  -9.762  26.349 1.00 17.32  ? 168 SER C N   1 
ATOM   4826 C CA  . SER C 1 169 ? 19.588  -11.134 26.500 1.00 20.16  ? 168 SER C CA  1 
ATOM   4827 C C   . SER C 1 169 ? 20.267  -11.755 27.724 1.00 23.01  ? 168 SER C C   1 
ATOM   4828 O O   . SER C 1 169 ? 19.590  -12.355 28.544 1.00 21.06  ? 168 SER C O   1 
ATOM   4829 C CB  . SER C 1 169 ? 19.872  -11.994 25.271 1.00 17.82  ? 168 SER C CB  1 
ATOM   4830 O OG  . SER C 1 169 ? 19.319  -13.289 25.433 1.00 22.57  ? 168 SER C OG  1 
ATOM   4831 N N   . VAL C 1 170 ? 21.573  -11.592 27.812 1.00 18.70  ? 169 VAL C N   1 
ATOM   4832 C CA  . VAL C 1 170 ? 22.375  -11.949 28.968 1.00 17.04  ? 169 VAL C CA  1 
ATOM   4833 C C   . VAL C 1 170 ? 21.819  -11.343 30.256 1.00 27.52  ? 169 VAL C C   1 
ATOM   4834 O O   . VAL C 1 170 ? 21.565  -12.010 31.269 1.00 20.65  ? 169 VAL C O   1 
ATOM   4835 C CB  . VAL C 1 170 ? 23.820  -11.467 28.723 1.00 25.14  ? 169 VAL C CB  1 
ATOM   4836 C CG1 . VAL C 1 170 ? 24.688  -11.730 29.946 1.00 18.87  ? 169 VAL C CG1 1 
ATOM   4837 C CG2 . VAL C 1 170 ? 24.379  -12.129 27.461 1.00 14.45  ? 169 VAL C CG2 1 
ATOM   4838 N N   . THR C 1 171 ? 21.606  -10.031 30.227 1.00 14.26  ? 170 THR C N   1 
ATOM   4839 C CA  . THR C 1 171 ? 21.022  -9.295  31.340 1.00 20.87  ? 170 THR C CA  1 
ATOM   4840 C C   . THR C 1 171 ? 19.744  -9.963  31.837 1.00 29.26  ? 170 THR C C   1 
ATOM   4841 O O   . THR C 1 171 ? 19.628  -10.262 33.025 1.00 24.53  ? 170 THR C O   1 
ATOM   4842 C CB  . THR C 1 171 ? 20.719  -7.842  30.941 1.00 19.39  ? 170 THR C CB  1 
ATOM   4843 O OG1 . THR C 1 171 ? 21.973  -7.198  30.672 1.00 27.43  ? 170 THR C OG1 1 
ATOM   4844 C CG2 . THR C 1 171 ? 20.055  -7.086  32.081 1.00 32.51  ? 170 THR C CG2 1 
ATOM   4845 N N   . LEU C 1 172 ? 18.818  -10.220 30.927 1.00 22.44  ? 171 LEU C N   1 
ATOM   4846 C CA  . LEU C 1 172 ? 17.589  -10.927 31.232 1.00 17.88  ? 171 LEU C CA  1 
ATOM   4847 C C   . LEU C 1 172 ? 17.837  -12.233 31.978 1.00 27.10  ? 171 LEU C C   1 
ATOM   4848 O O   . LEU C 1 172 ? 17.127  -12.586 32.934 1.00 17.67  ? 171 LEU C O   1 
ATOM   4849 C CB  . LEU C 1 172 ? 16.843  -11.219 29.926 1.00 12.46  ? 171 LEU C CB  1 
ATOM   4850 C CG  . LEU C 1 172 ? 15.563  -12.038 30.055 1.00 22.42  ? 171 LEU C CG  1 
ATOM   4851 C CD1 . LEU C 1 172 ? 14.513  -11.211 30.803 1.00 17.09  ? 171 LEU C CD1 1 
ATOM   4852 C CD2 . LEU C 1 172 ? 15.061  -12.509 28.690 1.00 15.33  ? 171 LEU C CD2 1 
ATOM   4853 N N   . GLY C 1 173 ? 18.844  -12.987 31.531 1.00 24.29  ? 172 GLY C N   1 
ATOM   4854 C CA  . GLY C 1 173 ? 19.120  -14.271 32.164 1.00 29.86  ? 172 GLY C CA  1 
ATOM   4855 C C   . GLY C 1 173 ? 19.547  -14.101 33.616 1.00 28.72  ? 172 GLY C C   1 
ATOM   4856 O O   . GLY C 1 173 ? 19.252  -14.902 34.505 1.00 21.06  ? 172 GLY C O   1 
ATOM   4857 N N   . HIS C 1 174 ? 20.272  -13.019 33.874 1.00 24.62  ? 173 HIS C N   1 
ATOM   4858 C CA  . HIS C 1 174 ? 20.774  -12.743 35.219 1.00 27.68  ? 173 HIS C CA  1 
ATOM   4859 C C   . HIS C 1 174 ? 19.642  -12.362 36.158 1.00 24.66  ? 173 HIS C C   1 
ATOM   4860 O O   . HIS C 1 174 ? 19.579  -12.789 37.311 1.00 27.40  ? 173 HIS C O   1 
ATOM   4861 C CB  . HIS C 1 174 ? 21.855  -11.661 35.141 1.00 31.42  ? 173 HIS C CB  1 
ATOM   4862 C CG  . HIS C 1 174 ? 23.204  -12.209 34.775 1.00 39.09  ? 173 HIS C CG  1 
ATOM   4863 N ND1 . HIS C 1 174 ? 24.181  -12.464 35.720 1.00 40.99  ? 173 HIS C ND1 1 
ATOM   4864 C CD2 . HIS C 1 174 ? 23.741  -12.561 33.580 1.00 31.58  ? 173 HIS C CD2 1 
ATOM   4865 C CE1 . HIS C 1 174 ? 25.253  -12.942 35.120 1.00 37.44  ? 173 HIS C CE1 1 
ATOM   4866 N NE2 . HIS C 1 174 ? 25.018  -13.011 33.817 1.00 37.84  ? 173 HIS C NE2 1 
ATOM   4867 N N   . LEU C 1 175 ? 18.698  -11.565 35.678 1.00 26.73  ? 174 LEU C N   1 
ATOM   4868 C CA  . LEU C 1 175 ? 17.593  -11.058 36.475 1.00 28.99  ? 174 LEU C CA  1 
ATOM   4869 C C   . LEU C 1 175 ? 16.768  -12.206 37.055 1.00 36.09  ? 174 LEU C C   1 
ATOM   4870 O O   . LEU C 1 175 ? 16.058  -11.984 38.040 1.00 27.47  ? 174 LEU C O   1 
ATOM   4871 C CB  . LEU C 1 175 ? 16.661  -10.154 35.684 1.00 23.90  ? 174 LEU C CB  1 
ATOM   4872 C CG  . LEU C 1 175 ? 16.988  -8.682  35.502 1.00 40.78  ? 174 LEU C CG  1 
ATOM   4873 C CD1 . LEU C 1 175 ? 18.182  -8.452  34.581 1.00 73.28  ? 174 LEU C CD1 1 
ATOM   4874 C CD2 . LEU C 1 175 ? 15.822  -7.909  34.885 1.00 41.26  ? 174 LEU C CD2 1 
ATOM   4875 N N   . VAL C 1 176 ? 16.847  -13.389 36.449 1.00 29.19  ? 175 VAL C N   1 
ATOM   4876 C CA  . VAL C 1 176 ? 16.141  -14.534 37.024 1.00 19.97  ? 175 VAL C CA  1 
ATOM   4877 C C   . VAL C 1 176 ? 17.182  -15.468 37.655 1.00 31.46  ? 175 VAL C C   1 
ATOM   4878 O O   . VAL C 1 176 ? 17.037  -15.828 38.827 1.00 28.11  ? 175 VAL C O   1 
ATOM   4879 C CB  . VAL C 1 176 ? 15.269  -15.292 36.024 1.00 27.56  ? 175 VAL C CB  1 
ATOM   4880 C CG1 . VAL C 1 176 ? 14.965  -16.696 36.552 1.00 30.69  ? 175 VAL C CG1 1 
ATOM   4881 C CG2 . VAL C 1 176 ? 13.957  -14.565 35.724 1.00 14.60  ? 175 VAL C CG2 1 
ATOM   4882 N N   . GLY C 1 177 ? 18.189  -15.797 36.864 1.00 24.51  ? 176 GLY C N   1 
ATOM   4883 C CA  . GLY C 1 177 ? 19.246  -16.738 37.089 1.00 23.28  ? 176 GLY C CA  1 
ATOM   4884 C C   . GLY C 1 177 ? 20.122  -16.541 38.301 1.00 33.56  ? 176 GLY C C   1 
ATOM   4885 O O   . GLY C 1 177 ? 20.518  -17.490 38.992 1.00 19.23  ? 176 GLY C O   1 
ATOM   4886 N N   . ILE C 1 178 ? 20.470  -15.289 38.579 1.00 24.63  ? 177 ILE C N   1 
ATOM   4887 C CA  . ILE C 1 178 ? 21.285  -14.995 39.749 1.00 30.04  ? 177 ILE C CA  1 
ATOM   4888 C C   . ILE C 1 178 ? 20.661  -15.572 41.020 1.00 30.57  ? 177 ILE C C   1 
ATOM   4889 O O   . ILE C 1 178 ? 21.366  -16.017 41.925 1.00 28.23  ? 177 ILE C O   1 
ATOM   4890 C CB  . ILE C 1 178 ? 21.495  -13.479 39.903 1.00 34.71  ? 177 ILE C CB  1 
ATOM   4891 C CG1 . ILE C 1 178 ? 22.529  -12.871 38.947 1.00 28.34  ? 177 ILE C CG1 1 
ATOM   4892 C CG2 . ILE C 1 178 ? 21.849  -13.134 41.343 1.00 55.83  ? 177 ILE C CG2 1 
ATOM   4893 C CD1 . ILE C 1 178 ? 22.507  -11.354 38.947 1.00 15.47  ? 177 ILE C CD1 1 
ATOM   4894 N N   . TYR C 1 179 ? 19.342  -15.611 41.126 1.00 25.04  ? 178 TYR C N   1 
ATOM   4895 C CA  . TYR C 1 179 ? 18.675  -16.049 42.343 1.00 26.31  ? 178 TYR C CA  1 
ATOM   4896 C C   . TYR C 1 179 ? 18.778  -17.550 42.576 1.00 35.93  ? 178 TYR C C   1 
ATOM   4897 O O   . TYR C 1 179 ? 18.679  -18.012 43.725 1.00 34.43  ? 178 TYR C O   1 
ATOM   4898 C CB  . TYR C 1 179 ? 17.193  -15.648 42.297 1.00 17.20  ? 178 TYR C CB  1 
ATOM   4899 C CG  . TYR C 1 179 ? 16.961  -14.179 42.581 1.00 24.97  ? 178 TYR C CG  1 
ATOM   4900 C CD1 . TYR C 1 179 ? 16.926  -13.700 43.885 1.00 23.59  ? 178 TYR C CD1 1 
ATOM   4901 C CD2 . TYR C 1 179 ? 16.767  -13.271 41.545 1.00 27.89  ? 178 TYR C CD2 1 
ATOM   4902 C CE1 . TYR C 1 179 ? 16.711  -12.362 44.154 1.00 24.02  ? 178 TYR C CE1 1 
ATOM   4903 C CE2 . TYR C 1 179 ? 16.554  -11.932 41.804 1.00 28.47  ? 178 TYR C CE2 1 
ATOM   4904 C CZ  . TYR C 1 179 ? 16.525  -11.485 43.110 1.00 30.51  ? 178 TYR C CZ  1 
ATOM   4905 O OH  . TYR C 1 179 ? 16.315  -10.151 43.379 1.00 25.66  ? 178 TYR C OH  1 
ATOM   4906 N N   . PHE C 1 180 ? 18.966  -18.325 41.515 1.00 26.17  ? 179 PHE C N   1 
ATOM   4907 C CA  . PHE C 1 180 ? 19.077  -19.773 41.607 1.00 15.89  ? 179 PHE C CA  1 
ATOM   4908 C C   . PHE C 1 180 ? 20.498  -20.291 41.737 1.00 30.34  ? 179 PHE C C   1 
ATOM   4909 O O   . PHE C 1 180 ? 20.745  -21.224 42.493 1.00 52.20  ? 179 PHE C O   1 
ATOM   4910 C CB  . PHE C 1 180 ? 18.517  -20.389 40.320 1.00 20.67  ? 179 PHE C CB  1 
ATOM   4911 C CG  . PHE C 1 180 ? 16.997  -20.391 40.322 1.00 35.74  ? 179 PHE C CG  1 
ATOM   4912 C CD1 . PHE C 1 180 ? 16.323  -21.447 40.920 1.00 31.91  ? 179 PHE C CD1 1 
ATOM   4913 C CD2 . PHE C 1 180 ? 16.285  -19.362 39.735 1.00 31.19  ? 179 PHE C CD2 1 
ATOM   4914 C CE1 . PHE C 1 180 ? 14.944  -21.492 40.917 1.00 20.38  ? 179 PHE C CE1 1 
ATOM   4915 C CE2 . PHE C 1 180 ? 14.902  -19.419 39.728 1.00 32.96  ? 179 PHE C CE2 1 
ATOM   4916 C CZ  . PHE C 1 180 ? 14.229  -20.486 40.309 1.00 24.52  ? 179 PHE C CZ  1 
ATOM   4917 N N   . THR C 1 181 ? 21.414  -19.716 40.978 1.00 35.39  ? 180 THR C N   1 
ATOM   4918 C CA  . THR C 1 181 ? 22.732  -20.287 40.711 1.00 25.41  ? 180 THR C CA  1 
ATOM   4919 C C   . THR C 1 181 ? 23.813  -19.232 40.658 1.00 31.30  ? 180 THR C C   1 
ATOM   4920 O O   . THR C 1 181 ? 25.026  -19.437 40.591 1.00 31.12  ? 180 THR C O   1 
ATOM   4921 C CB  . THR C 1 181 ? 22.623  -21.029 39.359 1.00 23.56  ? 180 THR C CB  1 
ATOM   4922 O OG1 . THR C 1 181 ? 22.876  -22.425 39.555 1.00 37.07  ? 180 THR C OG1 1 
ATOM   4923 C CG2 . THR C 1 181 ? 23.650  -20.482 38.401 1.00 60.07  ? 180 THR C CG2 1 
ATOM   4924 N N   . GLY C 1 182 ? 23.357  -17.977 40.708 1.00 34.12  ? 181 GLY C N   1 
ATOM   4925 C CA  . GLY C 1 182 ? 24.280  -16.850 40.616 1.00 31.25  ? 181 GLY C CA  1 
ATOM   4926 C C   . GLY C 1 182 ? 24.360  -16.477 39.128 1.00 29.95  ? 181 GLY C C   1 
ATOM   4927 O O   . GLY C 1 182 ? 24.995  -15.485 38.791 1.00 25.90  ? 181 GLY C O   1 
ATOM   4928 N N   . CYS C 1 183 ? 23.695  -17.310 38.344 1.00 30.54  ? 182 CYS C N   1 
ATOM   4929 C CA  . CYS C 1 183 ? 23.607  -17.235 36.900 1.00 42.04  ? 182 CYS C CA  1 
ATOM   4930 C C   . CYS C 1 183 ? 24.931  -17.502 36.191 1.00 39.34  ? 182 CYS C C   1 
ATOM   4931 O O   . CYS C 1 183 ? 25.801  -16.641 36.059 1.00 50.78  ? 182 CYS C O   1 
ATOM   4932 C CB  . CYS C 1 183 ? 23.113  -15.862 36.413 1.00 35.35  ? 182 CYS C CB  1 
ATOM   4933 S SG  . CYS C 1 183 ? 22.570  -15.960 34.675 1.00 36.27  ? 182 CYS C SG  1 
ATOM   4934 N N   . SER C 1 184 ? 25.105  -18.718 35.673 1.00 30.85  ? 183 SER C N   1 
ATOM   4935 C CA  . SER C 1 184 ? 26.297  -18.911 34.850 1.00 31.10  ? 183 SER C CA  1 
ATOM   4936 C C   . SER C 1 184 ? 26.025  -18.679 33.367 1.00 27.41  ? 183 SER C C   1 
ATOM   4937 O O   . SER C 1 184 ? 26.570  -17.790 32.708 1.00 32.07  ? 183 SER C O   1 
ATOM   4938 C CB  . SER C 1 184 ? 26.819  -20.330 35.071 1.00 37.20  ? 183 SER C CB  1 
ATOM   4939 O OG  . SER C 1 184 ? 27.580  -20.745 33.956 1.00 32.34  ? 183 SER C OG  1 
ATOM   4940 N N   . MET C 1 185 ? 25.185  -19.513 32.762 1.00 25.72  ? 184 MET C N   1 
ATOM   4941 C CA  . MET C 1 185 ? 24.869  -19.451 31.345 1.00 28.55  ? 184 MET C CA  1 
ATOM   4942 C C   . MET C 1 185 ? 26.037  -19.772 30.416 1.00 33.13  ? 184 MET C C   1 
ATOM   4943 O O   . MET C 1 185 ? 25.856  -19.802 29.196 1.00 41.66  ? 184 MET C O   1 
ATOM   4944 C CB  . MET C 1 185 ? 24.353  -18.038 31.018 1.00 31.34  ? 184 MET C CB  1 
ATOM   4945 C CG  . MET C 1 185 ? 22.896  -17.859 31.415 1.00 21.11  ? 184 MET C CG  1 
ATOM   4946 S SD  . MET C 1 185 ? 22.314  -16.158 31.256 1.00 29.00  ? 184 MET C SD  1 
ATOM   4947 C CE  . MET C 1 185 ? 21.172  -16.404 29.885 1.00 21.56  ? 184 MET C CE  1 
ATOM   4948 N N   . ASN C 1 186 ? 27.206  -20.006 30.970 1.00 25.06  ? 185 ASN C N   1 
ATOM   4949 C CA  . ASN C 1 186 ? 28.538  -19.960 30.440 1.00 20.14  ? 185 ASN C CA  1 
ATOM   4950 C C   . ASN C 1 186 ? 29.516  -20.747 31.300 1.00 25.62  ? 185 ASN C C   1 
ATOM   4951 O O   . ASN C 1 186 ? 29.938  -20.241 32.346 1.00 30.34  ? 185 ASN C O   1 
ATOM   4952 C CB  . ASN C 1 186 ? 28.960  -18.488 30.389 1.00 26.80  ? 185 ASN C CB  1 
ATOM   4953 C CG  . ASN C 1 186 ? 30.151  -18.259 29.489 1.00 27.76  ? 185 ASN C CG  1 
ATOM   4954 O OD1 . ASN C 1 186 ? 31.067  -19.073 29.447 1.00 36.30  ? 185 ASN C OD1 1 
ATOM   4955 N ND2 . ASN C 1 186 ? 30.117  -17.141 28.774 1.00 31.14  ? 185 ASN C ND2 1 
ATOM   4956 N N   . PRO C 1 187 ? 29.867  -21.956 30.877 1.00 27.60  ? 186 PRO C N   1 
ATOM   4957 C CA  . PRO C 1 187 ? 30.813  -22.791 31.627 1.00 34.91  ? 186 PRO C CA  1 
ATOM   4958 C C   . PRO C 1 187 ? 32.157  -22.122 31.892 1.00 42.38  ? 186 PRO C C   1 
ATOM   4959 O O   . PRO C 1 187 ? 32.778  -22.286 32.948 1.00 24.52  ? 186 PRO C O   1 
ATOM   4960 C CB  . PRO C 1 187 ? 31.028  -23.994 30.689 1.00 35.36  ? 186 PRO C CB  1 
ATOM   4961 C CG  . PRO C 1 187 ? 29.785  -24.058 29.856 1.00 37.99  ? 186 PRO C CG  1 
ATOM   4962 C CD  . PRO C 1 187 ? 29.374  -22.624 29.660 1.00 33.78  ? 186 PRO C CD  1 
ATOM   4963 N N   . ALA C 1 188 ? 32.645  -21.366 30.902 1.00 44.95  ? 187 ALA C N   1 
ATOM   4964 C CA  . ALA C 1 188 ? 33.901  -20.642 31.036 1.00 26.70  ? 187 ALA C CA  1 
ATOM   4965 C C   . ALA C 1 188 ? 33.813  -19.621 32.169 1.00 34.25  ? 187 ALA C C   1 
ATOM   4966 O O   . ALA C 1 188 ? 34.701  -19.512 33.011 1.00 45.49  ? 187 ALA C O   1 
ATOM   4967 C CB  . ALA C 1 188 ? 34.254  -19.940 29.739 1.00 25.22  ? 187 ALA C CB  1 
ATOM   4968 N N   . ARG C 1 189 ? 32.718  -18.867 32.178 1.00 37.21  ? 188 ARG C N   1 
ATOM   4969 C CA  . ARG C 1 189 ? 32.436  -17.909 33.241 1.00 37.05  ? 188 ARG C CA  1 
ATOM   4970 C C   . ARG C 1 189 ? 32.535  -18.578 34.611 1.00 37.89  ? 188 ARG C C   1 
ATOM   4971 O O   . ARG C 1 189 ? 33.142  -18.070 35.555 1.00 30.54  ? 188 ARG C O   1 
ATOM   4972 C CB  . ARG C 1 189 ? 31.046  -17.303 33.036 1.00 32.59  ? 188 ARG C CB  1 
ATOM   4973 C CG  . ARG C 1 189 ? 30.571  -16.375 34.136 1.00 25.63  ? 188 ARG C CG  1 
ATOM   4974 C CD  . ARG C 1 189 ? 29.631  -17.097 35.102 1.00 27.79  ? 188 ARG C CD  1 
ATOM   4975 N NE  . ARG C 1 189 ? 29.325  -16.249 36.241 1.00 28.25  ? 188 ARG C NE  1 
ATOM   4976 C CZ  . ARG C 1 189 ? 29.938  -16.124 37.399 1.00 32.81  ? 188 ARG C CZ  1 
ATOM   4977 N NH1 . ARG C 1 189 ? 31.023  -16.831 37.700 1.00 27.06  ? 188 ARG C NH1 1 
ATOM   4978 N NH2 . ARG C 1 189 ? 29.457  -15.262 38.298 1.00 31.66  ? 188 ARG C NH2 1 
ATOM   4979 N N   . SER C 1 190 ? 31.911  -19.747 34.719 1.00 31.09  ? 189 SER C N   1 
ATOM   4980 C CA  . SER C 1 190 ? 31.899  -20.468 35.982 1.00 32.58  ? 189 SER C CA  1 
ATOM   4981 C C   . SER C 1 190 ? 33.188  -21.240 36.225 1.00 40.74  ? 189 SER C C   1 
ATOM   4982 O O   . SER C 1 190 ? 33.551  -21.473 37.376 1.00 46.84  ? 189 SER C O   1 
ATOM   4983 C CB  . SER C 1 190 ? 30.708  -21.437 36.025 1.00 35.82  ? 189 SER C CB  1 
ATOM   4984 O OG  . SER C 1 190 ? 30.582  -21.898 37.366 1.00 76.78  ? 189 SER C OG  1 
ATOM   4985 N N   . PHE C 1 191 ? 33.878  -21.624 35.163 1.00 50.15  ? 190 PHE C N   1 
ATOM   4986 C CA  . PHE C 1 191 ? 35.110  -22.400 35.237 1.00 42.97  ? 190 PHE C CA  1 
ATOM   4987 C C   . PHE C 1 191 ? 36.302  -21.595 35.738 1.00 29.92  ? 190 PHE C C   1 
ATOM   4988 O O   . PHE C 1 191 ? 37.115  -22.049 36.549 1.00 38.82  ? 190 PHE C O   1 
ATOM   4989 C CB  . PHE C 1 191 ? 35.392  -22.975 33.840 1.00 38.55  ? 190 PHE C CB  1 
ATOM   4990 C CG  . PHE C 1 191 ? 36.653  -23.824 33.790 1.00 49.89  ? 190 PHE C CG  1 
ATOM   4991 C CD1 . PHE C 1 191 ? 36.725  -25.039 34.458 1.00 43.78  ? 190 PHE C CD1 1 
ATOM   4992 C CD2 . PHE C 1 191 ? 37.755  -23.395 33.064 1.00 54.25  ? 190 PHE C CD2 1 
ATOM   4993 C CE1 . PHE C 1 191 ? 37.877  -25.797 34.386 1.00 41.96  ? 190 PHE C CE1 1 
ATOM   4994 C CE2 . PHE C 1 191 ? 38.916  -24.143 32.985 1.00 43.82  ? 190 PHE C CE2 1 
ATOM   4995 C CZ  . PHE C 1 191 ? 38.967  -25.357 33.649 1.00 40.33  ? 190 PHE C CZ  1 
ATOM   4996 N N   . GLY C 1 192 ? 36.402  -20.376 35.234 1.00 29.78  ? 191 GLY C N   1 
ATOM   4997 C CA  . GLY C 1 192 ? 37.444  -19.422 35.456 1.00 28.76  ? 191 GLY C CA  1 
ATOM   4998 C C   . GLY C 1 192 ? 37.706  -19.092 36.910 1.00 41.16  ? 191 GLY C C   1 
ATOM   4999 O O   . GLY C 1 192 ? 38.796  -19.371 37.422 1.00 44.20  ? 191 GLY C O   1 
ATOM   5000 N N   . PRO C 1 193 ? 36.760  -18.472 37.608 1.00 35.61  ? 192 PRO C N   1 
ATOM   5001 C CA  . PRO C 1 193 ? 36.978  -18.154 39.021 1.00 35.95  ? 192 PRO C CA  1 
ATOM   5002 C C   . PRO C 1 193 ? 37.253  -19.410 39.846 1.00 43.87  ? 192 PRO C C   1 
ATOM   5003 O O   . PRO C 1 193 ? 37.961  -19.301 40.851 1.00 64.73  ? 192 PRO C O   1 
ATOM   5004 C CB  . PRO C 1 193 ? 35.659  -17.533 39.483 1.00 36.26  ? 192 PRO C CB  1 
ATOM   5005 C CG  . PRO C 1 193 ? 34.664  -17.900 38.428 1.00 30.49  ? 192 PRO C CG  1 
ATOM   5006 C CD  . PRO C 1 193 ? 35.446  -18.009 37.139 1.00 29.88  ? 192 PRO C CD  1 
ATOM   5007 N N   . ALA C 1 194 ? 36.698  -20.536 39.417 1.00 38.01  ? 193 ALA C N   1 
ATOM   5008 C CA  . ALA C 1 194 ? 36.793  -21.804 40.134 1.00 30.33  ? 193 ALA C CA  1 
ATOM   5009 C C   . ALA C 1 194 ? 38.218  -22.329 40.065 1.00 34.05  ? 193 ALA C C   1 
ATOM   5010 O O   . ALA C 1 194 ? 38.775  -22.857 41.026 1.00 33.10  ? 193 ALA C O   1 
ATOM   5011 C CB  . ALA C 1 194 ? 35.849  -22.860 39.583 1.00 27.59  ? 193 ALA C CB  1 
ATOM   5012 N N   . VAL C 1 195 ? 38.786  -22.155 38.875 1.00 33.10  ? 194 VAL C N   1 
ATOM   5013 C CA  . VAL C 1 195 ? 40.180  -22.581 38.736 1.00 41.30  ? 194 VAL C CA  1 
ATOM   5014 C C   . VAL C 1 195 ? 41.072  -21.679 39.583 1.00 32.95  ? 194 VAL C C   1 
ATOM   5015 O O   . VAL C 1 195 ? 41.924  -22.122 40.346 1.00 44.33  ? 194 VAL C O   1 
ATOM   5016 C CB  . VAL C 1 195 ? 40.637  -22.538 37.269 1.00 44.56  ? 194 VAL C CB  1 
ATOM   5017 C CG1 . VAL C 1 195 ? 42.151  -22.376 37.192 1.00 61.18  ? 194 VAL C CG1 1 
ATOM   5018 C CG2 . VAL C 1 195 ? 40.190  -23.787 36.529 1.00 39.38  ? 194 VAL C CG2 1 
ATOM   5019 N N   . VAL C 1 196 ? 40.840  -20.388 39.416 1.00 28.65  ? 195 VAL C N   1 
ATOM   5020 C CA  . VAL C 1 196 ? 41.583  -19.333 40.082 1.00 42.29  ? 195 VAL C CA  1 
ATOM   5021 C C   . VAL C 1 196 ? 41.545  -19.474 41.587 1.00 54.57  ? 195 VAL C C   1 
ATOM   5022 O O   . VAL C 1 196 ? 42.460  -19.177 42.366 1.00 57.36  ? 195 VAL C O   1 
ATOM   5023 C CB  . VAL C 1 196 ? 40.987  -17.977 39.649 1.00 47.44  ? 195 VAL C CB  1 
ATOM   5024 C CG1 . VAL C 1 196 ? 41.683  -16.808 40.305 1.00 34.40  ? 195 VAL C CG1 1 
ATOM   5025 C CG2 . VAL C 1 196 ? 41.060  -17.893 38.129 1.00 64.90  ? 195 VAL C CG2 1 
ATOM   5026 N N   . MET C 1 197 ? 40.403  -19.963 42.086 1.00 56.96  ? 196 MET C N   1 
ATOM   5027 C CA  . MET C 1 197 ? 40.347  -20.042 43.551 1.00 59.55  ? 196 MET C CA  1 
ATOM   5028 C C   . MET C 1 197 ? 40.039  -21.462 43.993 1.00 61.99  ? 196 MET C C   1 
ATOM   5029 O O   . MET C 1 197 ? 39.265  -21.670 44.924 1.00 71.65  ? 196 MET C O   1 
ATOM   5030 C CB  . MET C 1 197 ? 39.325  -19.013 44.040 1.00 62.76  ? 196 MET C CB  1 
ATOM   5031 C CG  . MET C 1 197 ? 39.658  -17.609 43.542 1.00 60.55  ? 196 MET C CG  1 
ATOM   5032 S SD  . MET C 1 197 ? 39.410  -16.329 44.778 1.00 49.57  ? 196 MET C SD  1 
ATOM   5033 C CE  . MET C 1 197 ? 41.067  -15.713 45.021 1.00 46.45  ? 196 MET C CE  1 
ATOM   5034 N N   . ASN C 1 198 ? 40.662  -22.417 43.310 1.00 63.10  ? 197 ASN C N   1 
ATOM   5035 C CA  . ASN C 1 198 ? 40.468  -23.834 43.580 1.00 78.51  ? 197 ASN C CA  1 
ATOM   5036 C C   . ASN C 1 198 ? 38.976  -24.185 43.635 1.00 77.92  ? 197 ASN C C   1 
ATOM   5037 O O   . ASN C 1 198 ? 38.408  -24.487 42.592 1.00 88.59  ? 197 ASN C O   1 
ATOM   5038 C CB  . ASN C 1 198 ? 41.146  -24.229 44.889 1.00 95.78  ? 197 ASN C CB  1 
ATOM   5039 C CG  . ASN C 1 198 ? 42.487  -24.900 44.695 1.00 106.84 ? 197 ASN C CG  1 
ATOM   5040 O OD1 . ASN C 1 198 ? 42.854  -25.779 45.496 1.00 126.65 ? 197 ASN C OD1 1 
ATOM   5041 N ND2 . ASN C 1 198 ? 43.230  -24.474 43.685 1.00 115.48 ? 197 ASN C ND2 1 
ATOM   5042 N N   . ARG C 1 199 ? 38.415  -24.133 44.818 1.00 77.36  ? 198 ARG C N   1 
ATOM   5043 C CA  . ARG C 1 199 ? 37.042  -24.266 45.241 1.00 81.52  ? 198 ARG C CA  1 
ATOM   5044 C C   . ARG C 1 199 ? 36.073  -24.579 44.113 1.00 65.23  ? 198 ARG C C   1 
ATOM   5045 O O   . ARG C 1 199 ? 35.343  -23.734 43.602 1.00 61.40  ? 198 ARG C O   1 
ATOM   5046 C CB  . ARG C 1 199 ? 36.613  -22.963 45.934 1.00 104.86 ? 198 ARG C CB  1 
ATOM   5047 C CG  . ARG C 1 199 ? 35.123  -22.848 46.225 1.00 129.23 ? 198 ARG C CG  1 
ATOM   5048 C CD  . ARG C 1 199 ? 34.752  -21.407 46.600 1.00 147.26 ? 198 ARG C CD  1 
ATOM   5049 N NE  . ARG C 1 199 ? 33.649  -21.338 47.550 1.00 157.91 ? 198 ARG C NE  1 
ATOM   5050 C CZ  . ARG C 1 199 ? 33.793  -21.030 48.840 1.00 157.91 ? 198 ARG C CZ  1 
ATOM   5051 N NH1 . ARG C 1 199 ? 32.732  -20.988 49.627 1.00 157.91 ? 198 ARG C NH1 1 
ATOM   5052 N NH2 . ARG C 1 199 ? 35.005  -20.759 49.354 1.00 157.91 ? 198 ARG C NH2 1 
ATOM   5053 N N   . PHE C 1 200 ? 36.068  -25.841 43.695 1.00 58.59  ? 199 PHE C N   1 
ATOM   5054 C CA  . PHE C 1 200 ? 35.073  -26.276 42.714 1.00 49.00  ? 199 PHE C CA  1 
ATOM   5055 C C   . PHE C 1 200 ? 33.838  -26.738 43.484 1.00 56.08  ? 199 PHE C C   1 
ATOM   5056 O O   . PHE C 1 200 ? 33.977  -27.488 44.452 1.00 75.36  ? 199 PHE C O   1 
ATOM   5057 C CB  . PHE C 1 200 ? 35.628  -27.379 41.821 1.00 46.88  ? 199 PHE C CB  1 
ATOM   5058 C CG  . PHE C 1 200 ? 36.330  -26.907 40.565 1.00 52.04  ? 199 PHE C CG  1 
ATOM   5059 C CD1 . PHE C 1 200 ? 35.766  -27.109 39.314 1.00 52.80  ? 199 PHE C CD1 1 
ATOM   5060 C CD2 . PHE C 1 200 ? 37.558  -26.272 40.626 1.00 52.89  ? 199 PHE C CD2 1 
ATOM   5061 C CE1 . PHE C 1 200 ? 36.401  -26.684 38.166 1.00 49.39  ? 199 PHE C CE1 1 
ATOM   5062 C CE2 . PHE C 1 200 ? 38.196  -25.830 39.486 1.00 54.06  ? 199 PHE C CE2 1 
ATOM   5063 C CZ  . PHE C 1 200 ? 37.619  -26.043 38.247 1.00 52.89  ? 199 PHE C CZ  1 
ATOM   5064 N N   . SER C 1 201 ? 32.657  -26.299 43.085 1.00 66.92  ? 200 SER C N   1 
ATOM   5065 C CA  . SER C 1 201 ? 31.413  -26.632 43.790 1.00 70.16  ? 200 SER C CA  1 
ATOM   5066 C C   . SER C 1 201 ? 30.974  -28.058 43.501 1.00 63.99  ? 200 SER C C   1 
ATOM   5067 O O   . SER C 1 201 ? 31.310  -28.646 42.462 1.00 58.17  ? 200 SER C O   1 
ATOM   5068 C CB  . SER C 1 201 ? 30.346  -25.602 43.391 1.00 72.87  ? 200 SER C CB  1 
ATOM   5069 O OG  . SER C 1 201 ? 29.043  -25.958 43.814 1.00 75.34  ? 200 SER C OG  1 
ATOM   5070 N N   . PRO C 1 202 ? 30.214  -28.688 44.394 1.00 59.30  ? 201 PRO C N   1 
ATOM   5071 C CA  . PRO C 1 202 ? 29.689  -30.025 44.077 1.00 52.04  ? 201 PRO C CA  1 
ATOM   5072 C C   . PRO C 1 202 ? 28.577  -29.944 43.037 1.00 44.22  ? 201 PRO C C   1 
ATOM   5073 O O   . PRO C 1 202 ? 28.105  -30.943 42.496 1.00 50.52  ? 201 PRO C O   1 
ATOM   5074 C CB  . PRO C 1 202 ? 29.170  -30.530 45.424 1.00 53.22  ? 201 PRO C CB  1 
ATOM   5075 C CG  . PRO C 1 202 ? 28.924  -29.316 46.248 1.00 54.34  ? 201 PRO C CG  1 
ATOM   5076 C CD  . PRO C 1 202 ? 29.818  -28.233 45.732 1.00 59.97  ? 201 PRO C CD  1 
ATOM   5077 N N   . ALA C 1 203 ? 28.154  -28.721 42.741 1.00 35.37  ? 202 ALA C N   1 
ATOM   5078 C CA  . ALA C 1 203 ? 27.160  -28.474 41.715 1.00 40.59  ? 202 ALA C CA  1 
ATOM   5079 C C   . ALA C 1 203 ? 27.769  -28.004 40.396 1.00 38.03  ? 202 ALA C C   1 
ATOM   5080 O O   . ALA C 1 203 ? 27.020  -27.750 39.445 1.00 53.54  ? 202 ALA C O   1 
ATOM   5081 C CB  . ALA C 1 203 ? 26.168  -27.433 42.231 1.00 43.98  ? 202 ALA C CB  1 
ATOM   5082 N N   . HIS C 1 204 ? 29.086  -27.889 40.314 1.00 31.90  ? 203 HIS C N   1 
ATOM   5083 C CA  . HIS C 1 204 ? 29.761  -27.322 39.152 1.00 37.49  ? 203 HIS C CA  1 
ATOM   5084 C C   . HIS C 1 204 ? 29.285  -27.873 37.814 1.00 35.24  ? 203 HIS C C   1 
ATOM   5085 O O   . HIS C 1 204 ? 29.132  -27.104 36.852 1.00 40.12  ? 203 HIS C O   1 
ATOM   5086 C CB  . HIS C 1 204 ? 31.279  -27.516 39.284 1.00 43.81  ? 203 HIS C CB  1 
ATOM   5087 C CG  . HIS C 1 204 ? 32.108  -26.647 38.386 1.00 44.48  ? 203 HIS C CG  1 
ATOM   5088 N ND1 . HIS C 1 204 ? 32.336  -25.311 38.619 1.00 36.76  ? 203 HIS C ND1 1 
ATOM   5089 C CD2 . HIS C 1 204 ? 32.784  -26.934 37.244 1.00 50.19  ? 203 HIS C CD2 1 
ATOM   5090 C CE1 . HIS C 1 204 ? 33.105  -24.814 37.666 1.00 32.72  ? 203 HIS C CE1 1 
ATOM   5091 N NE2 . HIS C 1 204 ? 33.394  -25.779 36.813 1.00 43.06  ? 203 HIS C NE2 1 
ATOM   5092 N N   . TRP C 1 205 ? 29.045  -29.177 37.717 1.00 25.34  ? 204 TRP C N   1 
ATOM   5093 C CA  . TRP C 1 205 ? 28.594  -29.762 36.464 1.00 32.66  ? 204 TRP C CA  1 
ATOM   5094 C C   . TRP C 1 205 ? 27.361  -29.051 35.909 1.00 37.10  ? 204 TRP C C   1 
ATOM   5095 O O   . TRP C 1 205 ? 27.276  -28.925 34.690 1.00 31.87  ? 204 TRP C O   1 
ATOM   5096 C CB  . TRP C 1 205 ? 28.289  -31.253 36.624 1.00 30.71  ? 204 TRP C CB  1 
ATOM   5097 C CG  . TRP C 1 205 ? 27.141  -31.534 37.537 1.00 32.23  ? 204 TRP C CG  1 
ATOM   5098 C CD1 . TRP C 1 205 ? 27.181  -31.717 38.894 1.00 35.64  ? 204 TRP C CD1 1 
ATOM   5099 C CD2 . TRP C 1 205 ? 25.775  -31.662 37.145 1.00 28.00  ? 204 TRP C CD2 1 
ATOM   5100 N NE1 . TRP C 1 205 ? 25.908  -31.951 39.359 1.00 33.87  ? 204 TRP C NE1 1 
ATOM   5101 C CE2 . TRP C 1 205 ? 25.030  -31.922 38.312 1.00 37.41  ? 204 TRP C CE2 1 
ATOM   5102 C CE3 . TRP C 1 205 ? 25.123  -31.574 35.914 1.00 26.94  ? 204 TRP C CE3 1 
ATOM   5103 C CZ2 . TRP C 1 205 ? 23.646  -32.099 38.276 1.00 45.85  ? 204 TRP C CZ2 1 
ATOM   5104 C CZ3 . TRP C 1 205 ? 23.760  -31.751 35.884 1.00 26.64  ? 204 TRP C CZ3 1 
ATOM   5105 C CH2 . TRP C 1 205 ? 23.033  -32.011 37.053 1.00 42.37  ? 204 TRP C CH2 1 
ATOM   5106 N N   . VAL C 1 206 ? 26.465  -28.631 36.788 1.00 20.00  ? 205 VAL C N   1 
ATOM   5107 C CA  . VAL C 1 206 ? 25.297  -27.854 36.391 1.00 20.00  ? 205 VAL C CA  1 
ATOM   5108 C C   . VAL C 1 206 ? 25.677  -26.751 35.409 1.00 20.00  ? 205 VAL C C   1 
ATOM   5109 O O   . VAL C 1 206 ? 24.992  -26.519 34.417 1.00 40.73  ? 205 VAL C O   1 
ATOM   5110 C CB  . VAL C 1 206 ? 24.597  -27.224 37.609 1.00 20.00  ? 205 VAL C CB  1 
ATOM   5111 C CG1 . VAL C 1 206 ? 23.458  -26.322 37.161 1.00 20.00  ? 205 VAL C CG1 1 
ATOM   5112 C CG2 . VAL C 1 206 ? 24.090  -28.307 38.551 1.00 20.00  ? 205 VAL C CG2 1 
ATOM   5113 N N   . PHE C 1 207 ? 26.780  -26.112 35.779 1.00 31.62  ? 206 PHE C N   1 
ATOM   5114 C CA  . PHE C 1 207 ? 27.285  -24.919 35.106 1.00 34.47  ? 206 PHE C CA  1 
ATOM   5115 C C   . PHE C 1 207 ? 27.970  -25.262 33.793 1.00 38.50  ? 206 PHE C C   1 
ATOM   5116 O O   . PHE C 1 207 ? 28.516  -24.429 33.065 1.00 43.30  ? 206 PHE C O   1 
ATOM   5117 C CB  . PHE C 1 207 ? 28.202  -24.174 36.086 1.00 25.92  ? 206 PHE C CB  1 
ATOM   5118 C CG  . PHE C 1 207 ? 27.550  -23.957 37.449 1.00 32.05  ? 206 PHE C CG  1 
ATOM   5119 C CD1 . PHE C 1 207 ? 26.195  -23.696 37.556 1.00 35.63  ? 206 PHE C CD1 1 
ATOM   5120 C CD2 . PHE C 1 207 ? 28.301  -24.011 38.614 1.00 36.75  ? 206 PHE C CD2 1 
ATOM   5121 C CE1 . PHE C 1 207 ? 25.596  -23.504 38.793 1.00 23.99  ? 206 PHE C CE1 1 
ATOM   5122 C CE2 . PHE C 1 207 ? 27.720  -23.834 39.860 1.00 28.99  ? 206 PHE C CE2 1 
ATOM   5123 C CZ  . PHE C 1 207 ? 26.361  -23.582 39.936 1.00 23.14  ? 206 PHE C CZ  1 
ATOM   5124 N N   . TRP C 1 208 ? 27.955  -26.542 33.417 1.00 33.67  ? 207 TRP C N   1 
ATOM   5125 C CA  . TRP C 1 208 ? 28.452  -26.902 32.097 1.00 33.99  ? 207 TRP C CA  1 
ATOM   5126 C C   . TRP C 1 208 ? 27.300  -27.469 31.269 1.00 36.48  ? 207 TRP C C   1 
ATOM   5127 O O   . TRP C 1 208 ? 27.005  -27.116 30.130 1.00 32.33  ? 207 TRP C O   1 
ATOM   5128 C CB  . TRP C 1 208 ? 29.586  -27.920 32.221 1.00 41.97  ? 207 TRP C CB  1 
ATOM   5129 C CG  . TRP C 1 208 ? 30.853  -27.338 32.759 1.00 40.44  ? 207 TRP C CG  1 
ATOM   5130 C CD1 . TRP C 1 208 ? 31.106  -27.031 34.065 1.00 38.87  ? 207 TRP C CD1 1 
ATOM   5131 C CD2 . TRP C 1 208 ? 32.032  -26.999 32.024 1.00 40.25  ? 207 TRP C CD2 1 
ATOM   5132 N NE1 . TRP C 1 208 ? 32.373  -26.519 34.181 1.00 34.03  ? 207 TRP C NE1 1 
ATOM   5133 C CE2 . TRP C 1 208 ? 32.964  -26.485 32.947 1.00 33.69  ? 207 TRP C CE2 1 
ATOM   5134 C CE3 . TRP C 1 208 ? 32.413  -27.064 30.678 1.00 45.89  ? 207 TRP C CE3 1 
ATOM   5135 C CZ2 . TRP C 1 208 ? 34.231  -26.053 32.556 1.00 36.00  ? 207 TRP C CZ2 1 
ATOM   5136 C CZ3 . TRP C 1 208 ? 33.672  -26.634 30.291 1.00 41.81  ? 207 TRP C CZ3 1 
ATOM   5137 C CH2 . TRP C 1 208 ? 34.580  -26.128 31.236 1.00 37.35  ? 207 TRP C CH2 1 
ATOM   5138 N N   . VAL C 1 209 ? 26.638  -28.407 31.940 1.00 33.46  ? 208 VAL C N   1 
ATOM   5139 C CA  . VAL C 1 209 ? 25.625  -29.254 31.331 1.00 34.10  ? 208 VAL C CA  1 
ATOM   5140 C C   . VAL C 1 209 ? 24.347  -28.493 31.045 1.00 33.65  ? 208 VAL C C   1 
ATOM   5141 O O   . VAL C 1 209 ? 23.695  -28.686 30.018 1.00 35.29  ? 208 VAL C O   1 
ATOM   5142 C CB  . VAL C 1 209 ? 25.375  -30.459 32.264 1.00 33.04  ? 208 VAL C CB  1 
ATOM   5143 C CG1 . VAL C 1 209 ? 24.406  -31.449 31.663 1.00 26.06  ? 208 VAL C CG1 1 
ATOM   5144 C CG2 . VAL C 1 209 ? 26.718  -31.120 32.564 1.00 26.07  ? 208 VAL C CG2 1 
ATOM   5145 N N   . GLY C 1 210 ? 23.992  -27.621 31.981 1.00 33.24  ? 209 GLY C N   1 
ATOM   5146 C CA  . GLY C 1 210 ? 22.799  -26.808 31.861 1.00 30.15  ? 209 GLY C CA  1 
ATOM   5147 C C   . GLY C 1 210 ? 22.846  -25.832 30.707 1.00 34.54  ? 209 GLY C C   1 
ATOM   5148 O O   . GLY C 1 210 ? 21.972  -25.833 29.842 1.00 23.69  ? 209 GLY C O   1 
ATOM   5149 N N   . PRO C 1 211 ? 23.852  -24.967 30.701 1.00 33.64  ? 210 PRO C N   1 
ATOM   5150 C CA  . PRO C 1 211 ? 24.075  -24.068 29.570 1.00 31.90  ? 210 PRO C CA  1 
ATOM   5151 C C   . PRO C 1 211 ? 24.335  -24.782 28.250 1.00 29.88  ? 210 PRO C C   1 
ATOM   5152 O O   . PRO C 1 211 ? 23.999  -24.263 27.178 1.00 30.31  ? 210 PRO C O   1 
ATOM   5153 C CB  . PRO C 1 211 ? 25.356  -23.324 29.970 1.00 26.30  ? 210 PRO C CB  1 
ATOM   5154 C CG  . PRO C 1 211 ? 25.427  -23.428 31.456 1.00 25.19  ? 210 PRO C CG  1 
ATOM   5155 C CD  . PRO C 1 211 ? 24.819  -24.757 31.793 1.00 25.68  ? 210 PRO C CD  1 
ATOM   5156 N N   . ILE C 1 212 ? 24.960  -25.963 28.256 1.00 33.04  ? 211 ILE C N   1 
ATOM   5157 C CA  . ILE C 1 212 ? 25.288  -26.546 26.941 1.00 33.14  ? 211 ILE C CA  1 
ATOM   5158 C C   . ILE C 1 212 ? 24.063  -27.185 26.296 1.00 39.86  ? 211 ILE C C   1 
ATOM   5159 O O   . ILE C 1 212 ? 23.695  -26.906 25.153 1.00 61.35  ? 211 ILE C O   1 
ATOM   5160 C CB  . ILE C 1 212 ? 26.447  -27.545 27.047 1.00 34.12  ? 211 ILE C CB  1 
ATOM   5161 C CG1 . ILE C 1 212 ? 27.824  -26.887 27.001 1.00 29.26  ? 211 ILE C CG1 1 
ATOM   5162 C CG2 . ILE C 1 212 ? 26.341  -28.624 25.975 1.00 59.48  ? 211 ILE C CG2 1 
ATOM   5163 C CD1 . ILE C 1 212 ? 28.850  -27.441 27.952 1.00 27.70  ? 211 ILE C CD1 1 
ATOM   5164 N N   . VAL C 1 213 ? 23.402  -28.059 27.033 1.00 31.53  ? 212 VAL C N   1 
ATOM   5165 C CA  . VAL C 1 213 ? 22.146  -28.664 26.646 1.00 28.41  ? 212 VAL C CA  1 
ATOM   5166 C C   . VAL C 1 213 ? 21.130  -27.653 26.157 1.00 25.10  ? 212 VAL C C   1 
ATOM   5167 O O   . VAL C 1 213 ? 20.399  -27.883 25.192 1.00 35.56  ? 212 VAL C O   1 
ATOM   5168 C CB  . VAL C 1 213 ? 21.556  -29.408 27.866 1.00 38.08  ? 212 VAL C CB  1 
ATOM   5169 C CG1 . VAL C 1 213 ? 20.154  -29.886 27.563 1.00 28.44  ? 212 VAL C CG1 1 
ATOM   5170 C CG2 . VAL C 1 213 ? 22.469  -30.565 28.262 1.00 45.80  ? 212 VAL C CG2 1 
ATOM   5171 N N   . GLY C 1 214 ? 21.058  -26.508 26.837 1.00 18.68  ? 213 GLY C N   1 
ATOM   5172 C CA  . GLY C 1 214 ? 20.027  -25.532 26.512 1.00 16.10  ? 213 GLY C CA  1 
ATOM   5173 C C   . GLY C 1 214 ? 20.302  -24.806 25.208 1.00 22.71  ? 213 GLY C C   1 
ATOM   5174 O O   . GLY C 1 214 ? 19.418  -24.524 24.395 1.00 33.51  ? 213 GLY C O   1 
ATOM   5175 N N   . ALA C 1 215 ? 21.578  -24.509 25.010 1.00 21.68  ? 214 ALA C N   1 
ATOM   5176 C CA  . ALA C 1 215 ? 22.068  -23.891 23.790 1.00 22.32  ? 214 ALA C CA  1 
ATOM   5177 C C   . ALA C 1 215 ? 21.910  -24.864 22.621 1.00 36.32  ? 214 ALA C C   1 
ATOM   5178 O O   . ALA C 1 215 ? 21.410  -24.538 21.538 1.00 27.62  ? 214 ALA C O   1 
ATOM   5179 C CB  . ALA C 1 215 ? 23.513  -23.482 23.987 1.00 22.89  ? 214 ALA C CB  1 
ATOM   5180 N N   . VAL C 1 216 ? 22.341  -26.104 22.866 1.00 22.09  ? 215 VAL C N   1 
ATOM   5181 C CA  . VAL C 1 216 ? 22.286  -27.106 21.797 1.00 18.02  ? 215 VAL C CA  1 
ATOM   5182 C C   . VAL C 1 216 ? 20.852  -27.345 21.373 1.00 27.24  ? 215 VAL C C   1 
ATOM   5183 O O   . VAL C 1 216 ? 20.535  -27.431 20.188 1.00 39.31  ? 215 VAL C O   1 
ATOM   5184 C CB  . VAL C 1 216 ? 22.976  -28.392 22.281 1.00 24.61  ? 215 VAL C CB  1 
ATOM   5185 C CG1 . VAL C 1 216 ? 22.642  -29.565 21.385 1.00 32.90  ? 215 VAL C CG1 1 
ATOM   5186 C CG2 . VAL C 1 216 ? 24.478  -28.135 22.338 1.00 27.83  ? 215 VAL C CG2 1 
ATOM   5187 N N   . LEU C 1 217 ? 19.954  -27.431 22.348 1.00 29.58  ? 216 LEU C N   1 
ATOM   5188 C CA  . LEU C 1 217 ? 18.531  -27.549 22.049 1.00 28.48  ? 216 LEU C CA  1 
ATOM   5189 C C   . LEU C 1 217 ? 18.089  -26.434 21.105 1.00 29.38  ? 216 LEU C C   1 
ATOM   5190 O O   . LEU C 1 217 ? 17.321  -26.656 20.171 1.00 31.41  ? 216 LEU C O   1 
ATOM   5191 C CB  . LEU C 1 217 ? 17.740  -27.501 23.353 1.00 24.53  ? 216 LEU C CB  1 
ATOM   5192 C CG  . LEU C 1 217 ? 17.132  -28.785 23.911 1.00 36.46  ? 216 LEU C CG  1 
ATOM   5193 C CD1 . LEU C 1 217 ? 17.835  -30.023 23.387 1.00 32.51  ? 216 LEU C CD1 1 
ATOM   5194 C CD2 . LEU C 1 217 ? 17.131  -28.758 25.439 1.00 31.94  ? 216 LEU C CD2 1 
ATOM   5195 N N   . ALA C 1 218 ? 18.588  -25.225 21.348 1.00 33.21  ? 217 ALA C N   1 
ATOM   5196 C CA  . ALA C 1 218 ? 18.202  -24.038 20.589 1.00 38.25  ? 217 ALA C CA  1 
ATOM   5197 C C   . ALA C 1 218 ? 18.779  -24.079 19.171 1.00 34.91  ? 217 ALA C C   1 
ATOM   5198 O O   . ALA C 1 218 ? 18.098  -23.690 18.213 1.00 29.43  ? 217 ALA C O   1 
ATOM   5199 C CB  . ALA C 1 218 ? 18.635  -22.756 21.287 1.00 29.62  ? 217 ALA C CB  1 
ATOM   5200 N N   . ALA C 1 219 ? 20.020  -24.551 19.114 1.00 25.84  ? 218 ALA C N   1 
ATOM   5201 C CA  . ALA C 1 219 ? 20.694  -24.792 17.834 1.00 26.63  ? 218 ALA C CA  1 
ATOM   5202 C C   . ALA C 1 219 ? 19.873  -25.760 17.001 1.00 26.60  ? 218 ALA C C   1 
ATOM   5203 O O   . ALA C 1 219 ? 19.529  -25.567 15.835 1.00 35.93  ? 218 ALA C O   1 
ATOM   5204 C CB  . ALA C 1 219 ? 22.110  -25.274 18.094 1.00 21.30  ? 218 ALA C CB  1 
ATOM   5205 N N   . ILE C 1 220 ? 19.477  -26.893 17.584 1.00 24.05  ? 219 ILE C N   1 
ATOM   5206 C CA  . ILE C 1 220 ? 18.732  -27.846 16.776 1.00 28.40  ? 219 ILE C CA  1 
ATOM   5207 C C   . ILE C 1 220 ? 17.365  -27.282 16.425 1.00 30.71  ? 219 ILE C C   1 
ATOM   5208 O O   . ILE C 1 220 ? 16.862  -27.534 15.332 1.00 36.67  ? 219 ILE C O   1 
ATOM   5209 C CB  . ILE C 1 220 ? 18.544  -29.193 17.501 1.00 29.57  ? 219 ILE C CB  1 
ATOM   5210 C CG1 . ILE C 1 220 ? 19.856  -29.868 17.873 1.00 21.97  ? 219 ILE C CG1 1 
ATOM   5211 C CG2 . ILE C 1 220 ? 17.645  -30.097 16.674 1.00 47.06  ? 219 ILE C CG2 1 
ATOM   5212 C CD1 . ILE C 1 220 ? 19.783  -30.821 19.045 1.00 26.28  ? 219 ILE C CD1 1 
ATOM   5213 N N   . LEU C 1 221 ? 16.769  -26.534 17.358 1.00 38.71  ? 220 LEU C N   1 
ATOM   5214 C CA  . LEU C 1 221 ? 15.460  -25.962 17.075 1.00 33.85  ? 220 LEU C CA  1 
ATOM   5215 C C   . LEU C 1 221 ? 15.517  -25.025 15.864 1.00 34.04  ? 220 LEU C C   1 
ATOM   5216 O O   . LEU C 1 221 ? 14.689  -25.112 14.957 1.00 53.46  ? 220 LEU C O   1 
ATOM   5217 C CB  . LEU C 1 221 ? 14.884  -25.145 18.239 1.00 23.15  ? 220 LEU C CB  1 
ATOM   5218 C CG  . LEU C 1 221 ? 13.527  -24.512 17.929 1.00 16.16  ? 220 LEU C CG  1 
ATOM   5219 C CD1 . LEU C 1 221 ? 12.526  -25.584 17.560 1.00 23.00  ? 220 LEU C CD1 1 
ATOM   5220 C CD2 . LEU C 1 221 ? 12.981  -23.704 19.103 1.00 31.00  ? 220 LEU C CD2 1 
ATOM   5221 N N   . TYR C 1 222 ? 16.495  -24.122 15.913 1.00 26.68  ? 221 TYR C N   1 
ATOM   5222 C CA  . TYR C 1 222 ? 16.542  -23.025 14.959 1.00 29.29  ? 221 TYR C CA  1 
ATOM   5223 C C   . TYR C 1 222 ? 17.154  -23.441 13.628 1.00 28.66  ? 221 TYR C C   1 
ATOM   5224 O O   . TYR C 1 222 ? 16.590  -23.110 12.587 1.00 27.74  ? 221 TYR C O   1 
ATOM   5225 C CB  . TYR C 1 222 ? 17.324  -21.855 15.552 1.00 35.78  ? 221 TYR C CB  1 
ATOM   5226 C CG  . TYR C 1 222 ? 17.395  -20.591 14.729 1.00 36.10  ? 221 TYR C CG  1 
ATOM   5227 C CD1 . TYR C 1 222 ? 16.485  -19.558 14.896 1.00 30.61  ? 221 TYR C CD1 1 
ATOM   5228 C CD2 . TYR C 1 222 ? 18.381  -20.390 13.769 1.00 35.43  ? 221 TYR C CD2 1 
ATOM   5229 C CE1 . TYR C 1 222 ? 16.542  -18.394 14.151 1.00 33.14  ? 221 TYR C CE1 1 
ATOM   5230 C CE2 . TYR C 1 222 ? 18.453  -19.234 13.021 1.00 32.14  ? 221 TYR C CE2 1 
ATOM   5231 C CZ  . TYR C 1 222 ? 17.530  -18.229 13.208 1.00 31.35  ? 221 TYR C CZ  1 
ATOM   5232 O OH  . TYR C 1 222 ? 17.621  -17.080 12.452 1.00 26.97  ? 221 TYR C OH  1 
ATOM   5233 N N   . PHE C 1 223 ? 18.295  -24.109 13.656 1.00 31.10  ? 222 PHE C N   1 
ATOM   5234 C CA  . PHE C 1 223 ? 18.982  -24.480 12.419 1.00 37.95  ? 222 PHE C CA  1 
ATOM   5235 C C   . PHE C 1 223 ? 18.368  -25.690 11.735 1.00 43.59  ? 222 PHE C C   1 
ATOM   5236 O O   . PHE C 1 223 ? 18.447  -25.851 10.516 1.00 44.57  ? 222 PHE C O   1 
ATOM   5237 C CB  . PHE C 1 223 ? 20.467  -24.729 12.727 1.00 33.65  ? 222 PHE C CB  1 
ATOM   5238 C CG  . PHE C 1 223 ? 21.137  -23.452 13.232 1.00 38.08  ? 222 PHE C CG  1 
ATOM   5239 C CD1 . PHE C 1 223 ? 21.365  -22.405 12.353 1.00 25.62  ? 222 PHE C CD1 1 
ATOM   5240 C CD2 . PHE C 1 223 ? 21.502  -23.332 14.565 1.00 34.43  ? 222 PHE C CD2 1 
ATOM   5241 C CE1 . PHE C 1 223 ? 21.950  -21.252 12.834 1.00 24.58  ? 222 PHE C CE1 1 
ATOM   5242 C CE2 . PHE C 1 223 ? 22.103  -22.184 15.043 1.00 24.73  ? 222 PHE C CE2 1 
ATOM   5243 C CZ  . PHE C 1 223 ? 22.330  -21.146 14.157 1.00 32.24  ? 222 PHE C CZ  1 
ATOM   5244 N N   . TYR C 1 224 ? 17.727  -26.593 12.481 1.00 37.70  ? 223 TYR C N   1 
ATOM   5245 C CA  . TYR C 1 224 ? 17.222  -27.792 11.825 1.00 37.54  ? 223 TYR C CA  1 
ATOM   5246 C C   . TYR C 1 224 ? 15.719  -27.776 11.605 1.00 42.49  ? 223 TYR C C   1 
ATOM   5247 O O   . TYR C 1 224 ? 15.240  -28.146 10.531 1.00 44.36  ? 223 TYR C O   1 
ATOM   5248 C CB  . TYR C 1 224 ? 17.642  -29.007 12.673 1.00 40.77  ? 223 TYR C CB  1 
ATOM   5249 C CG  . TYR C 1 224 ? 19.154  -29.144 12.596 1.00 35.21  ? 223 TYR C CG  1 
ATOM   5250 C CD1 . TYR C 1 224 ? 19.757  -28.851 11.373 1.00 25.25  ? 223 TYR C CD1 1 
ATOM   5251 C CD2 . TYR C 1 224 ? 19.939  -29.531 13.663 1.00 28.27  ? 223 TYR C CD2 1 
ATOM   5252 C CE1 . TYR C 1 224 ? 21.121  -28.957 11.250 1.00 21.49  ? 223 TYR C CE1 1 
ATOM   5253 C CE2 . TYR C 1 224 ? 21.314  -29.637 13.535 1.00 37.05  ? 223 TYR C CE2 1 
ATOM   5254 C CZ  . TYR C 1 224 ? 21.897  -29.345 12.315 1.00 33.41  ? 223 TYR C CZ  1 
ATOM   5255 O OH  . TYR C 1 224 ? 23.264  -29.438 12.143 1.00 36.34  ? 223 TYR C OH  1 
ATOM   5256 N N   . LEU C 1 225 ? 15.002  -27.346 12.625 1.00 37.74  ? 224 LEU C N   1 
ATOM   5257 C CA  . LEU C 1 225 ? 13.556  -27.339 12.686 1.00 29.74  ? 224 LEU C CA  1 
ATOM   5258 C C   . LEU C 1 225 ? 12.951  -26.026 12.217 1.00 26.96  ? 224 LEU C C   1 
ATOM   5259 O O   . LEU C 1 225 ? 11.954  -26.053 11.497 1.00 45.35  ? 224 LEU C O   1 
ATOM   5260 C CB  . LEU C 1 225 ? 13.114  -27.578 14.140 1.00 41.56  ? 224 LEU C CB  1 
ATOM   5261 C CG  . LEU C 1 225 ? 13.107  -29.031 14.609 1.00 41.61  ? 224 LEU C CG  1 
ATOM   5262 C CD1 . LEU C 1 225 ? 13.814  -29.921 13.602 1.00 59.75  ? 224 LEU C CD1 1 
ATOM   5263 C CD2 . LEU C 1 225 ? 13.727  -29.150 15.991 1.00 47.44  ? 224 LEU C CD2 1 
ATOM   5264 N N   . LEU C 1 226 ? 13.533  -24.909 12.640 1.00 27.83  ? 225 LEU C N   1 
ATOM   5265 C CA  . LEU C 1 226 ? 12.998  -23.580 12.355 1.00 33.11  ? 225 LEU C CA  1 
ATOM   5266 C C   . LEU C 1 226 ? 13.465  -23.001 11.028 1.00 31.29  ? 225 LEU C C   1 
ATOM   5267 O O   . LEU C 1 226 ? 12.724  -22.738 10.075 1.00 27.07  ? 225 LEU C O   1 
ATOM   5268 C CB  . LEU C 1 226 ? 13.375  -22.616 13.495 1.00 25.66  ? 225 LEU C CB  1 
ATOM   5269 C CG  . LEU C 1 226 ? 12.563  -22.802 14.784 1.00 24.31  ? 225 LEU C CG  1 
ATOM   5270 C CD1 . LEU C 1 226 ? 12.645  -21.541 15.629 1.00 16.66  ? 225 LEU C CD1 1 
ATOM   5271 C CD2 . LEU C 1 226 ? 11.126  -23.148 14.448 1.00 15.48  ? 225 LEU C CD2 1 
ATOM   5272 N N   . PHE C 1 227 ? 14.769  -22.773 10.924 1.00 32.68  ? 226 PHE C N   1 
ATOM   5273 C CA  . PHE C 1 227 ? 15.341  -22.171 9.728  1.00 34.45  ? 226 PHE C CA  1 
ATOM   5274 C C   . PHE C 1 227 ? 16.510  -22.953 9.150  1.00 37.38  ? 226 PHE C C   1 
ATOM   5275 O O   . PHE C 1 227 ? 17.661  -22.506 9.152  1.00 32.22  ? 226 PHE C O   1 
ATOM   5276 C CB  . PHE C 1 227 ? 15.774  -20.746 10.104 1.00 35.16  ? 226 PHE C CB  1 
ATOM   5277 C CG  . PHE C 1 227 ? 14.548  -19.932 10.513 1.00 36.58  ? 226 PHE C CG  1 
ATOM   5278 C CD1 . PHE C 1 227 ? 13.493  -19.797 9.631  1.00 39.12  ? 226 PHE C CD1 1 
ATOM   5279 C CD2 . PHE C 1 227 ? 14.485  -19.325 11.751 1.00 46.81  ? 226 PHE C CD2 1 
ATOM   5280 C CE1 . PHE C 1 227 ? 12.387  -19.052 9.987  1.00 43.42  ? 226 PHE C CE1 1 
ATOM   5281 C CE2 . PHE C 1 227 ? 13.381  -18.586 12.125 1.00 44.44  ? 226 PHE C CE2 1 
ATOM   5282 C CZ  . PHE C 1 227 ? 12.334  -18.459 11.235 1.00 44.83  ? 226 PHE C CZ  1 
ATOM   5283 N N   . PRO C 1 228 ? 16.201  -24.141 8.634  1.00 42.15  ? 227 PRO C N   1 
ATOM   5284 C CA  . PRO C 1 228 ? 17.212  -24.962 7.962  1.00 46.52  ? 227 PRO C CA  1 
ATOM   5285 C C   . PRO C 1 228 ? 17.594  -24.396 6.587  1.00 42.95  ? 227 PRO C C   1 
ATOM   5286 O O   . PRO C 1 228 ? 16.813  -23.641 6.008  1.00 29.89  ? 227 PRO C O   1 
ATOM   5287 C CB  . PRO C 1 228 ? 16.530  -26.314 7.772  1.00 40.68  ? 227 PRO C CB  1 
ATOM   5288 C CG  . PRO C 1 228 ? 15.072  -26.047 7.867  1.00 44.10  ? 227 PRO C CG  1 
ATOM   5289 C CD  . PRO C 1 228 ? 14.877  -24.781 8.647  1.00 35.63  ? 227 PRO C CD  1 
ATOM   5290 N N   . ASN C 1 229 ? 18.777  -24.788 6.147  1.00 50.24  ? 228 ASN C N   1 
ATOM   5291 C CA  . ASN C 1 229 ? 19.370  -24.541 4.845  1.00 55.55  ? 228 ASN C CA  1 
ATOM   5292 C C   . ASN C 1 229 ? 19.356  -25.846 4.040  1.00 58.31  ? 228 ASN C C   1 
ATOM   5293 O O   . ASN C 1 229 ? 18.934  -26.861 4.605  1.00 53.73  ? 228 ASN C O   1 
ATOM   5294 C CB  . ASN C 1 229 ? 20.798  -24.016 4.940  1.00 55.33  ? 228 ASN C CB  1 
ATOM   5295 C CG  . ASN C 1 229 ? 21.732  -24.976 5.652  1.00 59.94  ? 228 ASN C CG  1 
ATOM   5296 O OD1 . ASN C 1 229 ? 21.372  -26.116 5.958  1.00 65.75  ? 228 ASN C OD1 1 
ATOM   5297 N ND2 . ASN C 1 229 ? 22.951  -24.518 5.924  1.00 57.57  ? 228 ASN C ND2 1 
ATOM   5298 N N   . SER C 1 230 ? 19.808  -25.800 2.796  1.00 61.94  ? 229 SER C N   1 
ATOM   5299 C CA  . SER C 1 230 ? 19.728  -26.924 1.878  1.00 58.42  ? 229 SER C CA  1 
ATOM   5300 C C   . SER C 1 230 ? 20.957  -27.835 1.888  1.00 53.94  ? 229 SER C C   1 
ATOM   5301 O O   . SER C 1 230 ? 20.818  -28.994 1.491  1.00 74.05  ? 229 SER C O   1 
ATOM   5302 C CB  . SER C 1 230 ? 19.574  -26.418 0.434  1.00 66.90  ? 229 SER C CB  1 
ATOM   5303 O OG  . SER C 1 230 ? 20.708  -26.818 -0.327 1.00 71.71  ? 229 SER C OG  1 
ATOM   5304 N N   . LEU C 1 231 ? 22.057  -27.295 2.324  1.00 46.07  ? 230 LEU C N   1 
ATOM   5305 C CA  . LEU C 1 231 ? 23.451  -27.575 2.426  1.00 54.55  ? 230 LEU C CA  1 
ATOM   5306 C C   . LEU C 1 231 ? 23.947  -28.964 2.046  1.00 64.67  ? 230 LEU C C   1 
ATOM   5307 O O   . LEU C 1 231 ? 25.170  -29.165 2.123  1.00 77.66  ? 230 LEU C O   1 
ATOM   5308 C CB  . LEU C 1 231 ? 23.901  -27.314 3.888  1.00 52.61  ? 230 LEU C CB  1 
ATOM   5309 C CG  . LEU C 1 231 ? 24.968  -26.216 3.972  1.00 44.13  ? 230 LEU C CG  1 
ATOM   5310 C CD1 . LEU C 1 231 ? 26.304  -26.810 4.370  1.00 67.33  ? 230 LEU C CD1 1 
ATOM   5311 C CD2 . LEU C 1 231 ? 25.027  -25.491 2.633  1.00 45.32  ? 230 LEU C CD2 1 
ATOM   5312 N N   . SER C 1 232 ? 23.134  -29.918 1.642  1.00 60.11  ? 231 SER C N   1 
ATOM   5313 C CA  . SER C 1 232 ? 23.619  -31.180 1.094  1.00 57.97  ? 231 SER C CA  1 
ATOM   5314 C C   . SER C 1 232 ? 24.567  -31.947 2.011  1.00 51.93  ? 231 SER C C   1 
ATOM   5315 O O   . SER C 1 232 ? 25.481  -31.387 2.621  1.00 28.61  ? 231 SER C O   1 
ATOM   5316 C CB  . SER C 1 232 ? 24.331  -30.917 -0.240 1.00 69.13  ? 231 SER C CB  1 
ATOM   5317 O OG  . SER C 1 232 ? 25.603  -31.549 -0.243 1.00 78.78  ? 231 SER C OG  1 
ATOM   5318 N N   . LEU C 1 233 ? 24.331  -33.256 2.084  1.00 38.82  ? 232 LEU C N   1 
ATOM   5319 C CA  . LEU C 1 233 ? 25.031  -34.148 3.000  1.00 40.44  ? 232 LEU C CA  1 
ATOM   5320 C C   . LEU C 1 233 ? 26.540  -33.938 3.005  1.00 49.91  ? 232 LEU C C   1 
ATOM   5321 O O   . LEU C 1 233 ? 27.146  -33.581 4.018  1.00 45.94  ? 232 LEU C O   1 
ATOM   5322 C CB  . LEU C 1 233 ? 24.697  -35.593 2.625  1.00 48.39  ? 232 LEU C CB  1 
ATOM   5323 C CG  . LEU C 1 233 ? 24.917  -36.642 3.713  1.00 63.65  ? 232 LEU C CG  1 
ATOM   5324 C CD1 . LEU C 1 233 ? 23.818  -36.581 4.761  1.00 51.36  ? 232 LEU C CD1 1 
ATOM   5325 C CD2 . LEU C 1 233 ? 25.000  -38.028 3.086  1.00 96.02  ? 232 LEU C CD2 1 
ATOM   5326 N N   . SER C 1 234 ? 27.153  -34.147 1.844  1.00 56.90  ? 233 SER C N   1 
ATOM   5327 C CA  . SER C 1 234 ? 28.579  -33.931 1.664  1.00 47.37  ? 233 SER C CA  1 
ATOM   5328 C C   . SER C 1 234 ? 28.970  -32.494 1.963  1.00 39.07  ? 233 SER C C   1 
ATOM   5329 O O   . SER C 1 234 ? 30.105  -32.293 2.402  1.00 40.96  ? 233 SER C O   1 
ATOM   5330 C CB  . SER C 1 234 ? 29.003  -34.273 0.231  1.00 58.09  ? 233 SER C CB  1 
ATOM   5331 O OG  . SER C 1 234 ? 28.412  -35.486 -0.204 1.00 77.73  ? 233 SER C OG  1 
ATOM   5332 N N   . GLU C 1 235 ? 28.087  -31.520 1.718  1.00 39.53  ? 234 GLU C N   1 
ATOM   5333 C CA  . GLU C 1 235 ? 28.523  -30.143 1.962  1.00 50.57  ? 234 GLU C CA  1 
ATOM   5334 C C   . GLU C 1 235 ? 28.349  -29.829 3.450  1.00 46.18  ? 234 GLU C C   1 
ATOM   5335 O O   . GLU C 1 235 ? 28.833  -28.832 3.970  1.00 42.49  ? 234 GLU C O   1 
ATOM   5336 C CB  . GLU C 1 235 ? 27.806  -29.047 1.205  1.00 59.34  ? 234 GLU C CB  1 
ATOM   5337 C CG  . GLU C 1 235 ? 27.161  -29.228 -0.136 1.00 58.43  ? 234 GLU C CG  1 
ATOM   5338 C CD  . GLU C 1 235 ? 26.343  -28.003 -0.540 1.00 57.04  ? 234 GLU C CD  1 
ATOM   5339 O OE1 . GLU C 1 235 ? 25.095  -28.065 -0.533 1.00 46.82  ? 234 GLU C OE1 1 
ATOM   5340 O OE2 . GLU C 1 235 ? 26.960  -26.967 -0.859 1.00 47.43  ? 234 GLU C OE2 1 
ATOM   5341 N N   . ARG C 1 236 ? 27.621  -30.706 4.145  1.00 48.04  ? 235 ARG C N   1 
ATOM   5342 C CA  . ARG C 1 236 ? 27.475  -30.362 5.571  1.00 42.30  ? 235 ARG C CA  1 
ATOM   5343 C C   . ARG C 1 236 ? 28.736  -30.829 6.272  1.00 36.62  ? 235 ARG C C   1 
ATOM   5344 O O   . ARG C 1 236 ? 29.275  -30.146 7.143  1.00 40.77  ? 235 ARG C O   1 
ATOM   5345 C CB  . ARG C 1 236 ? 26.158  -30.926 6.098  1.00 42.76  ? 235 ARG C CB  1 
ATOM   5346 C CG  . ARG C 1 236 ? 24.975  -30.077 5.632  1.00 43.43  ? 235 ARG C CG  1 
ATOM   5347 C CD  . ARG C 1 236 ? 23.608  -30.621 6.004  1.00 57.76  ? 235 ARG C CD  1 
ATOM   5348 N NE  . ARG C 1 236 ? 22.917  -29.810 6.992  1.00 67.75  ? 235 ARG C NE  1 
ATOM   5349 C CZ  . ARG C 1 236 ? 21.803  -29.112 6.877  1.00 65.85  ? 235 ARG C CZ  1 
ATOM   5350 N NH1 . ARG C 1 236 ? 21.118  -29.054 5.744  1.00 59.14  ? 235 ARG C NH1 1 
ATOM   5351 N NH2 . ARG C 1 236 ? 21.339  -28.437 7.933  1.00 77.87  ? 235 ARG C NH2 1 
ATOM   5352 N N   . VAL C 1 237 ? 29.222  -31.983 5.844  1.00 35.60  ? 236 VAL C N   1 
ATOM   5353 C CA  . VAL C 1 237 ? 30.454  -32.572 6.357  1.00 43.64  ? 236 VAL C CA  1 
ATOM   5354 C C   . VAL C 1 237 ? 31.669  -31.702 6.087  1.00 45.33  ? 236 VAL C C   1 
ATOM   5355 O O   . VAL C 1 237 ? 32.648  -31.692 6.839  1.00 42.88  ? 236 VAL C O   1 
ATOM   5356 C CB  . VAL C 1 237 ? 30.662  -33.962 5.731  1.00 61.04  ? 236 VAL C CB  1 
ATOM   5357 C CG1 . VAL C 1 237 ? 29.301  -34.602 5.479  1.00 79.90  ? 236 VAL C CG1 1 
ATOM   5358 C CG2 . VAL C 1 237 ? 31.463  -33.869 4.443  1.00 83.06  ? 236 VAL C CG2 1 
ATOM   5359 N N   . ALA C 1 238 ? 31.634  -30.933 5.000  1.00 43.24  ? 237 ALA C N   1 
ATOM   5360 C CA  . ALA C 1 238 ? 32.732  -29.999 4.739  1.00 41.76  ? 237 ALA C CA  1 
ATOM   5361 C C   . ALA C 1 238 ? 32.676  -28.805 5.688  1.00 42.22  ? 237 ALA C C   1 
ATOM   5362 O O   . ALA C 1 238 ? 33.676  -28.128 5.937  1.00 36.32  ? 237 ALA C O   1 
ATOM   5363 C CB  . ALA C 1 238 ? 32.702  -29.553 3.285  1.00 56.55  ? 237 ALA C CB  1 
ATOM   5364 N N   . ILE C 1 239 ? 31.487  -28.551 6.230  1.00 42.40  ? 238 ILE C N   1 
ATOM   5365 C CA  . ILE C 1 239 ? 31.333  -27.587 7.305  1.00 40.89  ? 238 ILE C CA  1 
ATOM   5366 C C   . ILE C 1 239 ? 32.207  -27.970 8.499  1.00 32.43  ? 238 ILE C C   1 
ATOM   5367 O O   . ILE C 1 239 ? 32.903  -27.127 9.064  1.00 48.56  ? 238 ILE C O   1 
ATOM   5368 C CB  . ILE C 1 239 ? 29.873  -27.491 7.796  1.00 39.44  ? 238 ILE C CB  1 
ATOM   5369 C CG1 . ILE C 1 239 ? 28.858  -27.071 6.744  1.00 32.04  ? 238 ILE C CG1 1 
ATOM   5370 C CG2 . ILE C 1 239 ? 29.816  -26.588 9.021  1.00 38.52  ? 238 ILE C CG2 1 
ATOM   5371 C CD1 . ILE C 1 239 ? 28.949  -25.635 6.296  1.00 30.77  ? 238 ILE C CD1 1 
ATOM   5372 N N   . ILE C 1 240 ? 32.165  -29.234 8.893  1.00 39.44  ? 239 ILE C N   1 
ATOM   5373 C CA  . ILE C 1 240 ? 32.865  -29.794 10.041 1.00 33.98  ? 239 ILE C CA  1 
ATOM   5374 C C   . ILE C 1 240 ? 34.366  -29.971 9.861  1.00 38.34  ? 239 ILE C C   1 
ATOM   5375 O O   . ILE C 1 240 ? 35.157  -29.878 10.801 1.00 33.02  ? 239 ILE C O   1 
ATOM   5376 C CB  . ILE C 1 240 ? 32.308  -31.199 10.368 1.00 36.74  ? 239 ILE C CB  1 
ATOM   5377 C CG1 . ILE C 1 240 ? 30.942  -31.163 11.049 1.00 42.29  ? 239 ILE C CG1 1 
ATOM   5378 C CG2 . ILE C 1 240 ? 33.330  -31.962 11.184 1.00 33.38  ? 239 ILE C CG2 1 
ATOM   5379 C CD1 . ILE C 1 240 ? 29.801  -30.910 10.087 1.00 37.86  ? 239 ILE C CD1 1 
ATOM   5380 N N   . LYS C 1 241 ? 34.749  -30.248 8.617  1.00 36.79  ? 240 LYS C N   1 
ATOM   5381 C CA  . LYS C 1 241 ? 36.148  -30.406 8.257  1.00 50.74  ? 240 LYS C CA  1 
ATOM   5382 C C   . LYS C 1 241 ? 36.805  -29.068 7.948  1.00 42.73  ? 240 LYS C C   1 
ATOM   5383 O O   . LYS C 1 241 ? 37.978  -29.015 7.581  1.00 56.72  ? 240 LYS C O   1 
ATOM   5384 C CB  . LYS C 1 241 ? 36.291  -31.343 7.053  1.00 58.97  ? 240 LYS C CB  1 
ATOM   5385 C CG  . LYS C 1 241 ? 36.160  -32.818 7.392  1.00 59.78  ? 240 LYS C CG  1 
ATOM   5386 C CD  . LYS C 1 241 ? 36.104  -33.680 6.138  1.00 63.66  ? 240 LYS C CD  1 
ATOM   5387 C CE  . LYS C 1 241 ? 37.475  -34.248 5.793  1.00 70.11  ? 240 LYS C CE  1 
ATOM   5388 N NZ  . LYS C 1 241 ? 37.516  -35.734 5.927  1.00 73.84  ? 240 LYS C NZ  1 
ATOM   5389 N N   . GLY C 1 242 ? 36.072  -27.972 8.094  1.00 35.60  ? 241 GLY C N   1 
ATOM   5390 C CA  . GLY C 1 242 ? 36.657  -26.656 7.905  1.00 38.00  ? 241 GLY C CA  1 
ATOM   5391 C C   . GLY C 1 242 ? 37.204  -26.426 6.507  1.00 46.20  ? 241 GLY C C   1 
ATOM   5392 O O   . GLY C 1 242 ? 38.307  -25.889 6.370  1.00 43.84  ? 241 GLY C O   1 
ATOM   5393 N N   . THR C 1 243 ? 36.451  -26.831 5.488  1.00 49.85  ? 242 THR C N   1 
ATOM   5394 C CA  . THR C 1 243 ? 36.809  -26.683 4.088  1.00 46.12  ? 242 THR C CA  1 
ATOM   5395 C C   . THR C 1 243 ? 35.602  -26.273 3.239  1.00 57.29  ? 242 THR C C   1 
ATOM   5396 O O   . THR C 1 243 ? 35.711  -26.209 2.011  1.00 64.36  ? 242 THR C O   1 
ATOM   5397 C CB  . THR C 1 243 ? 37.383  -27.965 3.453  1.00 31.10  ? 242 THR C CB  1 
ATOM   5398 O OG1 . THR C 1 243 ? 36.297  -28.866 3.166  1.00 41.43  ? 242 THR C OG1 1 
ATOM   5399 C CG2 . THR C 1 243 ? 38.312  -28.700 4.395  1.00 41.97  ? 242 THR C CG2 1 
ATOM   5400 N N   . TYR C 1 244 ? 34.455  -26.013 3.866  1.00 50.98  ? 243 TYR C N   1 
ATOM   5401 C CA  . TYR C 1 244 ? 33.295  -25.586 3.076  1.00 32.18  ? 243 TYR C CA  1 
ATOM   5402 C C   . TYR C 1 244 ? 33.542  -24.189 2.544  1.00 36.68  ? 243 TYR C C   1 
ATOM   5403 O O   . TYR C 1 244 ? 33.900  -23.264 3.284  1.00 45.18  ? 243 TYR C O   1 
ATOM   5404 C CB  . TYR C 1 244 ? 32.031  -25.637 3.930  1.00 36.57  ? 243 TYR C CB  1 
ATOM   5405 C CG  . TYR C 1 244 ? 30.820  -24.967 3.328  1.00 35.76  ? 243 TYR C CG  1 
ATOM   5406 C CD1 . TYR C 1 244 ? 29.997  -25.668 2.456  1.00 42.33  ? 243 TYR C CD1 1 
ATOM   5407 C CD2 . TYR C 1 244 ? 30.481  -23.649 3.621  1.00 45.22  ? 243 TYR C CD2 1 
ATOM   5408 C CE1 . TYR C 1 244 ? 28.877  -25.072 1.892  1.00 50.87  ? 243 TYR C CE1 1 
ATOM   5409 C CE2 . TYR C 1 244 ? 29.369  -23.040 3.065  1.00 45.96  ? 243 TYR C CE2 1 
ATOM   5410 C CZ  . TYR C 1 244 ? 28.567  -23.760 2.197  1.00 52.62  ? 243 TYR C CZ  1 
ATOM   5411 O OH  . TYR C 1 244 ? 27.452  -23.172 1.634  1.00 53.77  ? 243 TYR C OH  1 
ATOM   5412 N N   . GLU C 1 245 ? 33.354  -23.952 1.240  1.00 48.37  ? 244 GLU C N   1 
ATOM   5413 C CA  . GLU C 1 245 ? 33.686  -22.557 0.867  1.00 61.46  ? 244 GLU C CA  1 
ATOM   5414 C C   . GLU C 1 245 ? 32.498  -21.656 1.125  1.00 64.75  ? 244 GLU C C   1 
ATOM   5415 O O   . GLU C 1 245 ? 32.547  -20.947 2.164  1.00 76.07  ? 244 GLU C O   1 
ATOM   5416 C CB  . GLU C 1 245 ? 34.270  -22.551 -0.543 1.00 61.21  ? 244 GLU C CB  1 
ATOM   5417 C CG  . GLU C 1 245 ? 35.312  -21.472 -0.777 1.00 69.87  ? 244 GLU C CG  1 
ATOM   5418 C CD  . GLU C 1 245 ? 36.650  -21.938 -1.310 1.00 74.30  ? 244 GLU C CD  1 
ATOM   5419 O OE1 . GLU C 1 245 ? 36.861  -23.146 -1.541 1.00 85.28  ? 244 GLU C OE1 1 
ATOM   5420 O OE2 . GLU C 1 245 ? 37.521  -21.061 -1.503 1.00 83.16  ? 244 GLU C OE2 1 
ATOM   5421 N N   . PRO C 1 246 ? 31.401  -21.542 0.400  1.00 64.35  ? 245 PRO C N   1 
ATOM   5422 C CA  . PRO C 1 246 ? 31.012  -22.207 -0.839 1.00 79.35  ? 245 PRO C CA  1 
ATOM   5423 C C   . PRO C 1 246 ? 31.374  -21.395 -2.085 1.00 89.83  ? 245 PRO C C   1 
ATOM   5424 O O   . PRO C 1 246 ? 30.799  -20.314 -2.309 1.00 100.81 ? 245 PRO C O   1 
ATOM   5425 C CB  . PRO C 1 246 ? 29.481  -22.248 -0.716 1.00 76.90  ? 245 PRO C CB  1 
ATOM   5426 C CG  . PRO C 1 246 ? 29.181  -20.919 -0.111 1.00 69.98  ? 245 PRO C CG  1 
ATOM   5427 C CD  . PRO C 1 246 ? 30.316  -20.635 0.842  1.00 66.04  ? 245 PRO C CD  1 
ATOM   5428 N N   . SER D 1 2   ? -0.953  27.286  3.501  1.00 48.22  ? 1   SER D N   1 
ATOM   5429 C CA  . SER D 1 2   ? -1.272  27.575  4.896  1.00 55.25  ? 1   SER D CA  1 
ATOM   5430 C C   . SER D 1 2   ? -2.726  27.248  5.197  1.00 52.68  ? 1   SER D C   1 
ATOM   5431 O O   . SER D 1 2   ? -3.023  26.475  6.111  0.35 41.65  ? 1   SER D O   1 
ATOM   5432 C CB  . SER D 1 2   ? -0.978  29.039  5.248  1.00 56.00  ? 1   SER D CB  1 
ATOM   5433 O OG  . SER D 1 2   ? -1.526  29.326  6.527  1.00 66.25  ? 1   SER D OG  1 
ATOM   5434 N N   . LYS D 1 3   ? -3.642  27.836  4.423  1.00 60.30  ? 2   LYS D N   1 
ATOM   5435 C CA  . LYS D 1 3   ? -5.037  27.414  4.579  1.00 56.64  ? 2   LYS D CA  1 
ATOM   5436 C C   . LYS D 1 3   ? -5.098  25.961  4.113  1.00 47.31  ? 2   LYS D C   1 
ATOM   5437 O O   . LYS D 1 3   ? -5.847  25.125  4.600  1.00 52.35  ? 2   LYS D O   1 
ATOM   5438 C CB  . LYS D 1 3   ? -6.014  28.278  3.809  1.00 64.06  ? 2   LYS D CB  1 
ATOM   5439 C CG  . LYS D 1 3   ? -5.389  29.303  2.867  1.00 76.40  ? 2   LYS D CG  1 
ATOM   5440 C CD  . LYS D 1 3   ? -5.886  29.072  1.441  1.00 80.81  ? 2   LYS D CD  1 
ATOM   5441 C CE  . LYS D 1 3   ? -6.182  30.385  0.729  1.00 77.18  ? 2   LYS D CE  1 
ATOM   5442 N NZ  . LYS D 1 3   ? -7.487  30.339  0.008  1.00 57.78  ? 2   LYS D NZ  1 
ATOM   5443 N N   . LYS D 1 4   ? -4.238  25.690  3.136  1.00 40.38  ? 3   LYS D N   1 
ATOM   5444 C CA  . LYS D 1 4   ? -4.139  24.324  2.648  1.00 49.59  ? 3   LYS D CA  1 
ATOM   5445 C C   . LYS D 1 4   ? -3.427  23.473  3.691  1.00 51.95  ? 3   LYS D C   1 
ATOM   5446 O O   . LYS D 1 4   ? -3.822  22.330  3.915  0.16 49.08  ? 3   LYS D O   1 
ATOM   5447 C CB  . LYS D 1 4   ? -3.399  24.276  1.313  1.00 59.79  ? 3   LYS D CB  1 
ATOM   5448 C CG  . LYS D 1 4   ? -3.826  25.364  0.341  1.00 69.75  ? 3   LYS D CG  1 
ATOM   5449 C CD  . LYS D 1 4   ? -5.346  25.459  0.267  1.00 79.04  ? 3   LYS D CD  1 
ATOM   5450 C CE  . LYS D 1 4   ? -5.768  26.539  -0.726 1.00 83.52  ? 3   LYS D CE  1 
ATOM   5451 N NZ  . LYS D 1 4   ? -7.241  26.779  -0.722 1.00 85.79  ? 3   LYS D NZ  1 
ATOM   5452 N N   . GLU D 1 5   ? -2.380  24.039  4.311  1.00 48.96  ? 4   GLU D N   1 
ATOM   5453 C CA  . GLU D 1 5   ? -1.647  23.243  5.296  1.00 35.82  ? 4   GLU D CA  1 
ATOM   5454 C C   . GLU D 1 5   ? -2.619  22.803  6.393  1.00 32.54  ? 4   GLU D C   1 
ATOM   5455 O O   . GLU D 1 5   ? -2.861  21.615  6.549  1.00 44.85  ? 4   GLU D O   1 
ATOM   5456 C CB  . GLU D 1 5   ? -0.451  23.958  5.936  1.00 27.78  ? 4   GLU D CB  1 
ATOM   5457 C CG  . GLU D 1 5   ? 0.338   23.008  6.832  1.00 31.58  ? 4   GLU D CG  1 
ATOM   5458 C CD  . GLU D 1 5   ? 1.468   23.613  7.626  1.00 44.98  ? 4   GLU D CD  1 
ATOM   5459 O OE1 . GLU D 1 5   ? 1.268   24.650  8.289  1.00 44.38  ? 4   GLU D OE1 1 
ATOM   5460 O OE2 . GLU D 1 5   ? 2.594   23.059  7.620  1.00 42.01  ? 4   GLU D OE2 1 
ATOM   5461 N N   . VAL D 1 6   ? -3.140  23.785  7.102  1.00 38.20  ? 5   VAL D N   1 
ATOM   5462 C CA  . VAL D 1 6   ? -3.932  23.644  8.309  1.00 38.06  ? 5   VAL D CA  1 
ATOM   5463 C C   . VAL D 1 6   ? -5.219  22.875  8.066  1.00 38.46  ? 5   VAL D C   1 
ATOM   5464 O O   . VAL D 1 6   ? -5.841  22.324  8.969  1.00 44.50  ? 5   VAL D O   1 
ATOM   5465 C CB  . VAL D 1 6   ? -4.251  25.048  8.862  1.00 35.18  ? 5   VAL D CB  1 
ATOM   5466 C CG1 . VAL D 1 6   ? -5.302  24.963  9.949  1.00 50.93  ? 5   VAL D CG1 1 
ATOM   5467 C CG2 . VAL D 1 6   ? -2.966  25.695  9.369  1.00 31.32  ? 5   VAL D CG2 1 
ATOM   5468 N N   . CYS D 1 7   ? -5.591  22.869  6.793  1.00 42.51  ? 6   CYS D N   1 
ATOM   5469 C CA  . CYS D 1 7   ? -6.834  22.237  6.386  1.00 55.38  ? 6   CYS D CA  1 
ATOM   5470 C C   . CYS D 1 7   ? -6.557  20.931  5.653  1.00 64.03  ? 6   CYS D C   1 
ATOM   5471 O O   . CYS D 1 7   ? -7.203  20.639  4.647  1.00 74.83  ? 6   CYS D O   1 
ATOM   5472 C CB  . CYS D 1 7   ? -7.650  23.191  5.512  1.00 65.71  ? 6   CYS D CB  1 
ATOM   5473 S SG  . CYS D 1 7   ? -8.219  24.684  6.373  1.00 90.75  ? 6   CYS D SG  1 
ATOM   5474 N N   . SER D 1 8   ? -5.597  20.187  6.194  1.00 70.06  ? 7   SER D N   1 
ATOM   5475 C CA  . SER D 1 8   ? -5.303  18.822  5.782  1.00 59.92  ? 7   SER D CA  1 
ATOM   5476 C C   . SER D 1 8   ? -5.864  17.851  6.831  1.00 33.59  ? 7   SER D C   1 
ATOM   5477 O O   . SER D 1 8   ? -6.016  18.211  7.994  1.00 29.12  ? 7   SER D O   1 
ATOM   5478 C CB  . SER D 1 8   ? -3.823  18.496  5.604  1.00 58.71  ? 7   SER D CB  1 
ATOM   5479 O OG  . SER D 1 8   ? -2.982  19.609  5.399  1.00 67.38  ? 7   SER D OG  1 
ATOM   5480 N N   . VAL D 1 9   ? -6.161  16.639  6.395  1.00 30.31  ? 8   VAL D N   1 
ATOM   5481 C CA  . VAL D 1 9   ? -6.439  15.553  7.321  1.00 32.36  ? 8   VAL D CA  1 
ATOM   5482 C C   . VAL D 1 9   ? -5.090  15.187  7.931  1.00 32.39  ? 8   VAL D C   1 
ATOM   5483 O O   . VAL D 1 9   ? -4.930  14.731  9.048  1.00 51.97  ? 8   VAL D O   1 
ATOM   5484 C CB  . VAL D 1 9   ? -7.045  14.313  6.655  1.00 42.12  ? 8   VAL D CB  1 
ATOM   5485 C CG1 . VAL D 1 9   ? -6.058  13.661  5.696  1.00 51.89  ? 8   VAL D CG1 1 
ATOM   5486 C CG2 . VAL D 1 9   ? -7.491  13.298  7.703  1.00 59.48  ? 8   VAL D CG2 1 
ATOM   5487 N N   . ALA D 1 10  ? -4.084  15.437  7.081  1.00 31.09  ? 9   ALA D N   1 
ATOM   5488 C CA  . ALA D 1 10  ? -2.734  15.127  7.525  1.00 31.29  ? 9   ALA D CA  1 
ATOM   5489 C C   . ALA D 1 10  ? -2.411  15.981  8.751  1.00 28.89  ? 9   ALA D C   1 
ATOM   5490 O O   . ALA D 1 10  ? -1.848  15.455  9.708  1.00 34.95  ? 9   ALA D O   1 
ATOM   5491 C CB  . ALA D 1 10  ? -1.732  15.342  6.413  1.00 25.92  ? 9   ALA D CB  1 
ATOM   5492 N N   . PHE D 1 11  ? -2.774  17.251  8.669  1.00 27.97  ? 10  PHE D N   1 
ATOM   5493 C CA  . PHE D 1 11  ? -2.527  18.252  9.698  1.00 39.31  ? 10  PHE D CA  1 
ATOM   5494 C C   . PHE D 1 11  ? -3.405  17.961  10.915 1.00 42.10  ? 10  PHE D C   1 
ATOM   5495 O O   . PHE D 1 11  ? -2.938  17.898  12.050 1.00 50.34  ? 10  PHE D O   1 
ATOM   5496 C CB  . PHE D 1 11  ? -2.778  19.665  9.173  1.00 37.77  ? 10  PHE D CB  1 
ATOM   5497 C CG  . PHE D 1 11  ? -2.256  20.789  10.048 1.00 37.09  ? 10  PHE D CG  1 
ATOM   5498 C CD1 . PHE D 1 11  ? -0.921  21.166  10.001 1.00 39.00  ? 10  PHE D CD1 1 
ATOM   5499 C CD2 . PHE D 1 11  ? -3.108  21.455  10.916 1.00 30.56  ? 10  PHE D CD2 1 
ATOM   5500 C CE1 . PHE D 1 11  ? -0.440  22.185  10.808 1.00 31.87  ? 10  PHE D CE1 1 
ATOM   5501 C CE2 . PHE D 1 11  ? -2.629  22.477  11.719 1.00 21.67  ? 10  PHE D CE2 1 
ATOM   5502 C CZ  . PHE D 1 11  ? -1.295  22.845  11.670 1.00 19.63  ? 10  PHE D CZ  1 
ATOM   5503 N N   . LEU D 1 12  ? -4.688  17.774  10.630 1.00 31.12  ? 11  LEU D N   1 
ATOM   5504 C CA  . LEU D 1 12  ? -5.635  17.411  11.682 1.00 39.23  ? 11  LEU D CA  1 
ATOM   5505 C C   . LEU D 1 12  ? -5.149  16.182  12.438 1.00 37.10  ? 11  LEU D C   1 
ATOM   5506 O O   . LEU D 1 12  ? -5.358  16.044  13.637 1.00 29.91  ? 11  LEU D O   1 
ATOM   5507 C CB  . LEU D 1 12  ? -6.996  17.199  11.021 1.00 45.68  ? 11  LEU D CB  1 
ATOM   5508 C CG  . LEU D 1 12  ? -8.042  16.376  11.759 1.00 40.59  ? 11  LEU D CG  1 
ATOM   5509 C CD1 . LEU D 1 12  ? -8.345  17.012  13.102 1.00 38.11  ? 11  LEU D CD1 1 
ATOM   5510 C CD2 . LEU D 1 12  ? -9.293  16.250  10.905 1.00 42.38  ? 11  LEU D CD2 1 
ATOM   5511 N N   . LYS D 1 13  ? -4.486  15.260  11.752 1.00 32.40  ? 12  LYS D N   1 
ATOM   5512 C CA  . LYS D 1 13  ? -3.953  14.044  12.333 1.00 27.69  ? 12  LYS D CA  1 
ATOM   5513 C C   . LYS D 1 13  ? -2.715  14.317  13.193 1.00 31.03  ? 12  LYS D C   1 
ATOM   5514 O O   . LYS D 1 13  ? -2.577  13.769  14.285 1.00 37.34  ? 12  LYS D O   1 
ATOM   5515 C CB  . LYS D 1 13  ? -3.580  13.069  11.216 1.00 23.66  ? 12  LYS D CB  1 
ATOM   5516 C CG  . LYS D 1 13  ? -4.755  12.297  10.645 1.00 25.28  ? 12  LYS D CG  1 
ATOM   5517 C CD  . LYS D 1 13  ? -4.262  11.265  9.641  1.00 29.69  ? 12  LYS D CD  1 
ATOM   5518 C CE  . LYS D 1 13  ? -5.109  11.225  8.377  1.00 38.37  ? 12  LYS D CE  1 
ATOM   5519 N NZ  . LYS D 1 13  ? -4.988  9.900   7.699  1.00 50.84  ? 12  LYS D NZ  1 
ATOM   5520 N N   . ALA D 1 14  ? -1.857  15.161  12.648 1.00 26.18  ? 13  ALA D N   1 
ATOM   5521 C CA  . ALA D 1 14  ? -0.604  15.622  13.195 1.00 27.25  ? 13  ALA D CA  1 
ATOM   5522 C C   . ALA D 1 14  ? -0.853  16.420  14.476 1.00 34.29  ? 13  ALA D C   1 
ATOM   5523 O O   . ALA D 1 14  ? -0.073  16.332  15.419 1.00 42.00  ? 13  ALA D O   1 
ATOM   5524 C CB  . ALA D 1 14  ? 0.157   16.520  12.239 1.00 36.28  ? 13  ALA D CB  1 
ATOM   5525 N N   . VAL D 1 15  ? -1.955  17.168  14.428 1.00 30.56  ? 14  VAL D N   1 
ATOM   5526 C CA  . VAL D 1 15  ? -2.331  17.946  15.614 1.00 33.87  ? 14  VAL D CA  1 
ATOM   5527 C C   . VAL D 1 15  ? -2.874  16.971  16.646 1.00 34.21  ? 14  VAL D C   1 
ATOM   5528 O O   . VAL D 1 15  ? -2.579  17.055  17.831 1.00 23.16  ? 14  VAL D O   1 
ATOM   5529 C CB  . VAL D 1 15  ? -3.323  19.058  15.246 1.00 43.82  ? 14  VAL D CB  1 
ATOM   5530 C CG1 . VAL D 1 15  ? -4.609  18.990  16.050 1.00 38.71  ? 14  VAL D CG1 1 
ATOM   5531 C CG2 . VAL D 1 15  ? -2.686  20.430  15.439 1.00 50.87  ? 14  VAL D CG2 1 
ATOM   5532 N N   . PHE D 1 16  ? -3.670  15.998  16.203 1.00 33.59  ? 15  PHE D N   1 
ATOM   5533 C CA  . PHE D 1 16  ? -4.206  15.026  17.145 1.00 34.69  ? 15  PHE D CA  1 
ATOM   5534 C C   . PHE D 1 16  ? -3.097  14.161  17.740 1.00 32.65  ? 15  PHE D C   1 
ATOM   5535 O O   . PHE D 1 16  ? -3.148  13.848  18.936 1.00 47.26  ? 15  PHE D O   1 
ATOM   5536 C CB  . PHE D 1 16  ? -5.253  14.146  16.471 1.00 33.02  ? 15  PHE D CB  1 
ATOM   5537 C CG  . PHE D 1 16  ? -5.669  12.926  17.277 1.00 41.20  ? 15  PHE D CG  1 
ATOM   5538 C CD1 . PHE D 1 16  ? -6.614  13.038  18.285 1.00 37.97  ? 15  PHE D CD1 1 
ATOM   5539 C CD2 . PHE D 1 16  ? -5.132  11.673  17.026 1.00 38.20  ? 15  PHE D CD2 1 
ATOM   5540 C CE1 . PHE D 1 16  ? -7.006  11.923  19.005 1.00 39.22  ? 15  PHE D CE1 1 
ATOM   5541 C CE2 . PHE D 1 16  ? -5.518  10.558  17.742 1.00 28.94  ? 15  PHE D CE2 1 
ATOM   5542 C CZ  . PHE D 1 16  ? -6.466  10.674  18.739 1.00 31.52  ? 15  PHE D CZ  1 
ATOM   5543 N N   . ALA D 1 17  ? -2.123  13.765  16.928 1.00 33.06  ? 16  ALA D N   1 
ATOM   5544 C CA  . ALA D 1 17  ? -1.022  12.939  17.433 1.00 28.64  ? 16  ALA D CA  1 
ATOM   5545 C C   . ALA D 1 17  ? -0.305  13.621  18.596 1.00 25.31  ? 16  ALA D C   1 
ATOM   5546 O O   . ALA D 1 17  ? 0.095   12.975  19.558 1.00 32.86  ? 16  ALA D O   1 
ATOM   5547 C CB  . ALA D 1 17  ? 0.007   12.624  16.350 1.00 12.42  ? 16  ALA D CB  1 
ATOM   5548 N N   . GLU D 1 18  ? -0.107  14.935  18.521 1.00 29.95  ? 17  GLU D N   1 
ATOM   5549 C CA  . GLU D 1 18  ? 0.641   15.633  19.572 1.00 25.90  ? 17  GLU D CA  1 
ATOM   5550 C C   . GLU D 1 18  ? -0.160  15.702  20.861 1.00 20.18  ? 17  GLU D C   1 
ATOM   5551 O O   . GLU D 1 18  ? 0.347   15.517  21.957 1.00 33.89  ? 17  GLU D O   1 
ATOM   5552 C CB  . GLU D 1 18  ? 1.007   17.038  19.090 1.00 21.62  ? 17  GLU D CB  1 
ATOM   5553 C CG  . GLU D 1 18  ? 1.964   17.044  17.903 1.00 22.31  ? 17  GLU D CG  1 
ATOM   5554 C CD  . GLU D 1 18  ? 3.386   16.785  18.368 1.00 22.44  ? 17  GLU D CD  1 
ATOM   5555 O OE1 . GLU D 1 18  ? 3.757   17.332  19.428 1.00 28.99  ? 17  GLU D OE1 1 
ATOM   5556 O OE2 . GLU D 1 18  ? 4.145   16.050  17.712 1.00 23.99  ? 17  GLU D OE2 1 
ATOM   5557 N N   . PHE D 1 19  ? -1.450  15.985  20.742 1.00 22.40  ? 18  PHE D N   1 
ATOM   5558 C CA  . PHE D 1 19  ? -2.327  16.015  21.905 1.00 27.08  ? 18  PHE D CA  1 
ATOM   5559 C C   . PHE D 1 19  ? -2.264  14.699  22.671 1.00 29.81  ? 18  PHE D C   1 
ATOM   5560 O O   . PHE D 1 19  ? -1.975  14.697  23.860 1.00 26.52  ? 18  PHE D O   1 
ATOM   5561 C CB  . PHE D 1 19  ? -3.768  16.285  21.459 1.00 25.71  ? 18  PHE D CB  1 
ATOM   5562 C CG  . PHE D 1 19  ? -4.831  15.902  22.475 1.00 29.10  ? 18  PHE D CG  1 
ATOM   5563 C CD1 . PHE D 1 19  ? -5.026  16.669  23.611 1.00 24.27  ? 18  PHE D CD1 1 
ATOM   5564 C CD2 . PHE D 1 19  ? -5.624  14.784  22.278 1.00 34.49  ? 18  PHE D CD2 1 
ATOM   5565 C CE1 . PHE D 1 19  ? -5.992  16.322  24.539 1.00 33.48  ? 18  PHE D CE1 1 
ATOM   5566 C CE2 . PHE D 1 19  ? -6.583  14.424  23.202 1.00 42.61  ? 18  PHE D CE2 1 
ATOM   5567 C CZ  . PHE D 1 19  ? -6.768  15.197  24.339 1.00 44.45  ? 18  PHE D CZ  1 
ATOM   5568 N N   . LEU D 1 20  ? -2.543  13.601  21.981 1.00 27.80  ? 19  LEU D N   1 
ATOM   5569 C CA  . LEU D 1 20  ? -2.535  12.246  22.500 1.00 24.64  ? 19  LEU D CA  1 
ATOM   5570 C C   . LEU D 1 20  ? -1.154  11.815  22.966 1.00 23.81  ? 19  LEU D C   1 
ATOM   5571 O O   . LEU D 1 20  ? -1.000  11.005  23.881 1.00 36.70  ? 19  LEU D O   1 
ATOM   5572 C CB  . LEU D 1 20  ? -3.027  11.249  21.429 1.00 29.96  ? 19  LEU D CB  1 
ATOM   5573 C CG  . LEU D 1 20  ? -3.150  9.794   21.884 1.00 33.38  ? 19  LEU D CG  1 
ATOM   5574 C CD1 . LEU D 1 20  ? -4.323  9.610   22.845 1.00 23.56  ? 19  LEU D CD1 1 
ATOM   5575 C CD2 . LEU D 1 20  ? -3.304  8.835   20.712 1.00 33.79  ? 19  LEU D CD2 1 
ATOM   5576 N N   . ALA D 1 21  ? -0.111  12.338  22.327 1.00 20.93  ? 20  ALA D N   1 
ATOM   5577 C CA  . ALA D 1 21  ? 1.235   11.945  22.745 1.00 29.24  ? 20  ALA D CA  1 
ATOM   5578 C C   . ALA D 1 21  ? 1.558   12.620  24.073 1.00 24.31  ? 20  ALA D C   1 
ATOM   5579 O O   . ALA D 1 21  ? 2.025   12.010  25.027 1.00 20.70  ? 20  ALA D O   1 
ATOM   5580 C CB  . ALA D 1 21  ? 2.249   12.313  21.684 1.00 19.34  ? 20  ALA D CB  1 
ATOM   5581 N N   . THR D 1 22  ? 1.280   13.928  24.110 1.00 22.53  ? 21  THR D N   1 
ATOM   5582 C CA  . THR D 1 22  ? 1.554   14.650  25.361 1.00 23.61  ? 21  THR D CA  1 
ATOM   5583 C C   . THR D 1 22  ? 0.649   14.173  26.488 1.00 19.08  ? 21  THR D C   1 
ATOM   5584 O O   . THR D 1 22  ? 1.125   14.133  27.626 1.00 26.03  ? 21  THR D O   1 
ATOM   5585 C CB  . THR D 1 22  ? 1.396   16.161  25.180 1.00 21.80  ? 21  THR D CB  1 
ATOM   5586 O OG1 . THR D 1 22  ? 1.911   16.495  23.884 1.00 28.29  ? 21  THR D OG1 1 
ATOM   5587 C CG2 . THR D 1 22  ? 2.203   16.909  26.234 1.00 17.49  ? 21  THR D CG2 1 
ATOM   5588 N N   . LEU D 1 23  ? -0.585  13.805  26.162 1.00 23.01  ? 22  LEU D N   1 
ATOM   5589 C CA  . LEU D 1 23  ? -1.474  13.154  27.137 1.00 24.14  ? 22  LEU D CA  1 
ATOM   5590 C C   . LEU D 1 23  ? -0.803  11.932  27.743 1.00 34.81  ? 22  LEU D C   1 
ATOM   5591 O O   . LEU D 1 23  ? -0.622  11.749  28.954 1.00 23.43  ? 22  LEU D O   1 
ATOM   5592 C CB  . LEU D 1 23  ? -2.782  12.760  26.464 1.00 21.27  ? 22  LEU D CB  1 
ATOM   5593 C CG  . LEU D 1 23  ? -3.912  12.129  27.256 1.00 21.43  ? 22  LEU D CG  1 
ATOM   5594 C CD1 . LEU D 1 23  ? -5.255  12.462  26.608 1.00 23.10  ? 22  LEU D CD1 1 
ATOM   5595 C CD2 . LEU D 1 23  ? -3.786  10.618  27.364 1.00 19.61  ? 22  LEU D CD2 1 
ATOM   5596 N N   . ILE D 1 24  ? -0.444  11.019  26.825 1.00 29.32  ? 23  ILE D N   1 
ATOM   5597 C CA  . ILE D 1 24  ? 0.085   9.751   27.325 1.00 21.15  ? 23  ILE D CA  1 
ATOM   5598 C C   . ILE D 1 24  ? 1.382   10.000  28.085 1.00 24.44  ? 23  ILE D C   1 
ATOM   5599 O O   . ILE D 1 24  ? 1.591   9.375   29.134 1.00 22.12  ? 23  ILE D O   1 
ATOM   5600 C CB  . ILE D 1 24  ? 0.265   8.745   26.174 1.00 18.39  ? 23  ILE D CB  1 
ATOM   5601 C CG1 . ILE D 1 24  ? -1.062  8.300   25.557 1.00 21.28  ? 23  ILE D CG1 1 
ATOM   5602 C CG2 . ILE D 1 24  ? 1.067   7.535   26.612 1.00 17.90  ? 23  ILE D CG2 1 
ATOM   5603 C CD1 . ILE D 1 24  ? -0.884  7.527   24.260 1.00 46.49  ? 23  ILE D CD1 1 
ATOM   5604 N N   . PHE D 1 25  ? 2.216   10.901  27.566 1.00 21.30  ? 24  PHE D N   1 
ATOM   5605 C CA  . PHE D 1 25  ? 3.529   11.185  28.135 1.00 16.50  ? 24  PHE D CA  1 
ATOM   5606 C C   . PHE D 1 25  ? 3.400   11.690  29.572 1.00 26.09  ? 24  PHE D C   1 
ATOM   5607 O O   . PHE D 1 25  ? 4.172   11.289  30.444 1.00 28.37  ? 24  PHE D O   1 
ATOM   5608 C CB  . PHE D 1 25  ? 4.304   12.210  27.303 1.00 17.98  ? 24  PHE D CB  1 
ATOM   5609 C CG  . PHE D 1 25  ? 5.477   12.896  27.982 1.00 19.25  ? 24  PHE D CG  1 
ATOM   5610 C CD1 . PHE D 1 25  ? 5.546   14.284  28.003 1.00 23.33  ? 24  PHE D CD1 1 
ATOM   5611 C CD2 . PHE D 1 25  ? 6.503   12.193  28.578 1.00 17.86  ? 24  PHE D CD2 1 
ATOM   5612 C CE1 . PHE D 1 25  ? 6.599   14.923  28.615 1.00 19.98  ? 24  PHE D CE1 1 
ATOM   5613 C CE2 . PHE D 1 25  ? 7.554   12.824  29.216 1.00 18.92  ? 24  PHE D CE2 1 
ATOM   5614 C CZ  . PHE D 1 25  ? 7.601   14.206  29.227 1.00 16.23  ? 24  PHE D CZ  1 
ATOM   5615 N N   . VAL D 1 26  ? 2.447   12.574  29.816 1.00 26.10  ? 25  VAL D N   1 
ATOM   5616 C CA  . VAL D 1 26  ? 2.307   13.199  31.137 1.00 28.15  ? 25  VAL D CA  1 
ATOM   5617 C C   . VAL D 1 26  ? 1.751   12.206  32.149 1.00 12.85  ? 25  VAL D C   1 
ATOM   5618 O O   . VAL D 1 26  ? 2.184   12.119  33.292 1.00 28.46  ? 25  VAL D O   1 
ATOM   5619 C CB  . VAL D 1 26  ? 1.400   14.444  31.035 1.00 27.49  ? 25  VAL D CB  1 
ATOM   5620 C CG1 . VAL D 1 26  ? 1.068   14.972  32.414 1.00 23.76  ? 25  VAL D CG1 1 
ATOM   5621 C CG2 . VAL D 1 26  ? 2.049   15.531  30.188 1.00 17.04  ? 25  VAL D CG2 1 
ATOM   5622 N N   . PHE D 1 27  ? 0.786   11.406  31.723 1.00 30.93  ? 26  PHE D N   1 
ATOM   5623 C CA  . PHE D 1 27  ? 0.219   10.315  32.496 1.00 33.60  ? 26  PHE D CA  1 
ATOM   5624 C C   . PHE D 1 27  ? 1.338   9.458   33.078 1.00 33.74  ? 26  PHE D C   1 
ATOM   5625 O O   . PHE D 1 27  ? 1.414   9.220   34.281 1.00 26.13  ? 26  PHE D O   1 
ATOM   5626 C CB  . PHE D 1 27  ? -0.719  9.441   31.635 1.00 26.82  ? 26  PHE D CB  1 
ATOM   5627 C CG  . PHE D 1 27  ? -1.362  8.329   32.452 1.00 23.73  ? 26  PHE D CG  1 
ATOM   5628 C CD1 . PHE D 1 27  ? -2.498  8.589   33.206 1.00 25.66  ? 26  PHE D CD1 1 
ATOM   5629 C CD2 . PHE D 1 27  ? -0.828  7.056   32.471 1.00 25.05  ? 26  PHE D CD2 1 
ATOM   5630 C CE1 . PHE D 1 27  ? -3.088  7.617   33.989 1.00 26.92  ? 26  PHE D CE1 1 
ATOM   5631 C CE2 . PHE D 1 27  ? -1.411  6.079   33.256 1.00 27.23  ? 26  PHE D CE2 1 
ATOM   5632 C CZ  . PHE D 1 27  ? -2.537  6.352   34.010 1.00 26.47  ? 26  PHE D CZ  1 
ATOM   5633 N N   . PHE D 1 28  ? 2.189   9.002   32.157 1.00 19.74  ? 27  PHE D N   1 
ATOM   5634 C CA  . PHE D 1 28  ? 3.210   8.020   32.493 1.00 20.68  ? 27  PHE D CA  1 
ATOM   5635 C C   . PHE D 1 28  ? 4.313   8.653   33.330 1.00 19.39  ? 27  PHE D C   1 
ATOM   5636 O O   . PHE D 1 28  ? 4.782   8.040   34.280 1.00 27.42  ? 27  PHE D O   1 
ATOM   5637 C CB  . PHE D 1 28  ? 3.812   7.402   31.218 1.00 26.71  ? 27  PHE D CB  1 
ATOM   5638 C CG  . PHE D 1 28  ? 3.092   6.121   30.813 1.00 21.12  ? 27  PHE D CG  1 
ATOM   5639 C CD1 . PHE D 1 28  ? 3.246   4.967   31.570 1.00 25.87  ? 27  PHE D CD1 1 
ATOM   5640 C CD2 . PHE D 1 28  ? 2.290   6.104   29.693 1.00 18.87  ? 27  PHE D CD2 1 
ATOM   5641 C CE1 . PHE D 1 28  ? 2.610   3.785   31.224 1.00 30.11  ? 27  PHE D CE1 1 
ATOM   5642 C CE2 . PHE D 1 28  ? 1.645   4.929   29.333 1.00 21.87  ? 27  PHE D CE2 1 
ATOM   5643 C CZ  . PHE D 1 28  ? 1.815   3.780   30.085 1.00 27.42  ? 27  PHE D CZ  1 
ATOM   5644 N N   . GLY D 1 29  ? 4.704   9.865   32.956 1.00 17.71  ? 28  GLY D N   1 
ATOM   5645 C CA  . GLY D 1 29  ? 5.810   10.534  33.620 1.00 17.78  ? 28  GLY D CA  1 
ATOM   5646 C C   . GLY D 1 29  ? 5.384   10.880  35.041 1.00 24.03  ? 28  GLY D C   1 
ATOM   5647 O O   . GLY D 1 29  ? 6.078   10.560  36.013 1.00 23.00  ? 28  GLY D O   1 
ATOM   5648 N N   . LEU D 1 30  ? 4.214   11.523  35.157 1.00 19.02  ? 29  LEU D N   1 
ATOM   5649 C CA  . LEU D 1 30  ? 3.765   11.847  36.519 1.00 25.42  ? 29  LEU D CA  1 
ATOM   5650 C C   . LEU D 1 30  ? 3.479   10.577  37.313 1.00 24.86  ? 29  LEU D C   1 
ATOM   5651 O O   . LEU D 1 30  ? 3.885   10.426  38.462 1.00 16.25  ? 29  LEU D O   1 
ATOM   5652 C CB  . LEU D 1 30  ? 2.514   12.719  36.497 1.00 19.28  ? 29  LEU D CB  1 
ATOM   5653 C CG  . LEU D 1 30  ? 2.583   13.971  35.613 1.00 26.16  ? 29  LEU D CG  1 
ATOM   5654 C CD1 . LEU D 1 30  ? 1.267   14.731  35.693 1.00 26.65  ? 29  LEU D CD1 1 
ATOM   5655 C CD2 . LEU D 1 30  ? 3.756   14.826  36.030 1.00 16.72  ? 29  LEU D CD2 1 
ATOM   5656 N N   . GLY D 1 31  ? 2.749   9.650   36.686 1.00 21.29  ? 30  GLY D N   1 
ATOM   5657 C CA  . GLY D 1 31  ? 2.422   8.424   37.393 1.00 37.29  ? 30  GLY D CA  1 
ATOM   5658 C C   . GLY D 1 31  ? 3.598   7.691   38.010 1.00 29.90  ? 30  GLY D C   1 
ATOM   5659 O O   . GLY D 1 31  ? 3.452   7.066   39.060 1.00 27.34  ? 30  GLY D O   1 
ATOM   5660 N N   . SER D 1 32  ? 4.756   7.752   37.370 1.00 27.40  ? 31  SER D N   1 
ATOM   5661 C CA  . SER D 1 32  ? 5.944   7.019   37.750 1.00 18.75  ? 31  SER D CA  1 
ATOM   5662 C C   . SER D 1 32  ? 6.673   7.685   38.905 1.00 15.53  ? 31  SER D C   1 
ATOM   5663 O O   . SER D 1 32  ? 7.532   7.027   39.480 1.00 26.71  ? 31  SER D O   1 
ATOM   5664 C CB  . SER D 1 32  ? 6.936   6.951   36.576 1.00 19.18  ? 31  SER D CB  1 
ATOM   5665 O OG  . SER D 1 32  ? 7.524   8.243   36.362 1.00 22.51  ? 31  SER D OG  1 
ATOM   5666 N N   . ALA D 1 33  ? 6.350   8.939   39.184 1.00 23.10  ? 32  ALA D N   1 
ATOM   5667 C CA  . ALA D 1 33  ? 7.016   9.763   40.180 1.00 22.36  ? 32  ALA D CA  1 
ATOM   5668 C C   . ALA D 1 33  ? 6.204   10.001  41.444 1.00 28.22  ? 32  ALA D C   1 
ATOM   5669 O O   . ALA D 1 33  ? 6.683   10.577  42.431 1.00 27.44  ? 32  ALA D O   1 
ATOM   5670 C CB  . ALA D 1 33  ? 7.345   11.109  39.521 1.00 13.68  ? 32  ALA D CB  1 
ATOM   5671 N N   . LEU D 1 34  ? 4.938   9.601   41.481 1.00 24.90  ? 33  LEU D N   1 
ATOM   5672 C CA  . LEU D 1 34  ? 4.163   9.719   42.712 1.00 25.14  ? 33  LEU D CA  1 
ATOM   5673 C C   . LEU D 1 34  ? 4.862   8.981   43.844 1.00 31.27  ? 33  LEU D C   1 
ATOM   5674 O O   . LEU D 1 34  ? 5.601   8.015   43.651 1.00 28.15  ? 33  LEU D O   1 
ATOM   5675 C CB  . LEU D 1 34  ? 2.746   9.162   42.539 1.00 20.50  ? 33  LEU D CB  1 
ATOM   5676 C CG  . LEU D 1 34  ? 1.946   9.809   41.412 1.00 18.85  ? 33  LEU D CG  1 
ATOM   5677 C CD1 . LEU D 1 34  ? 0.567   9.193   41.297 1.00 12.77  ? 33  LEU D CD1 1 
ATOM   5678 C CD2 . LEU D 1 34  ? 1.870   11.307  41.662 1.00 25.90  ? 33  LEU D CD2 1 
ATOM   5679 N N   . LYS D 1 35  ? 4.637   9.438   45.074 1.00 31.64  ? 34  LYS D N   1 
ATOM   5680 C CA  . LYS D 1 35  ? 5.275   8.727   46.180 1.00 33.36  ? 34  LYS D CA  1 
ATOM   5681 C C   . LYS D 1 35  ? 4.480   7.493   46.585 1.00 32.53  ? 34  LYS D C   1 
ATOM   5682 O O   . LYS D 1 35  ? 3.949   7.410   47.686 1.00 30.70  ? 34  LYS D O   1 
ATOM   5683 C CB  . LYS D 1 35  ? 5.429   9.636   47.394 1.00 31.52  ? 34  LYS D CB  1 
ATOM   5684 C CG  . LYS D 1 35  ? 6.041   10.984  47.103 1.00 33.44  ? 34  LYS D CG  1 
ATOM   5685 C CD  . LYS D 1 35  ? 7.435   10.854  46.505 1.00 30.81  ? 34  LYS D CD  1 
ATOM   5686 C CE  . LYS D 1 35  ? 8.080   12.240  46.583 1.00 40.80  ? 34  LYS D CE  1 
ATOM   5687 N NZ  . LYS D 1 35  ? 7.091   13.215  47.134 1.00 59.93  ? 34  LYS D NZ  1 
ATOM   5688 N N   . TRP D 1 36  ? 4.395   6.519   45.695 1.00 26.84  ? 35  TRP D N   1 
ATOM   5689 C CA  . TRP D 1 36  ? 3.848   5.224   46.042 1.00 26.68  ? 35  TRP D CA  1 
ATOM   5690 C C   . TRP D 1 36  ? 4.450   4.684   47.338 1.00 14.17  ? 35  TRP D C   1 
ATOM   5691 O O   . TRP D 1 36  ? 5.639   4.382   47.423 1.00 26.82  ? 35  TRP D O   1 
ATOM   5692 C CB  . TRP D 1 36  ? 4.108   4.232   44.904 1.00 22.21  ? 35  TRP D CB  1 
ATOM   5693 C CG  . TRP D 1 36  ? 3.368   4.636   43.658 1.00 31.14  ? 35  TRP D CG  1 
ATOM   5694 C CD1 . TRP D 1 36  ? 3.928   5.317   42.606 1.00 29.81  ? 35  TRP D CD1 1 
ATOM   5695 C CD2 . TRP D 1 36  ? 1.994   4.413   43.317 1.00 21.56  ? 35  TRP D CD2 1 
ATOM   5696 N NE1 . TRP D 1 36  ? 2.979   5.524   41.637 1.00 32.05  ? 35  TRP D NE1 1 
ATOM   5697 C CE2 . TRP D 1 36  ? 1.786   4.981   42.046 1.00 27.63  ? 35  TRP D CE2 1 
ATOM   5698 C CE3 . TRP D 1 36  ? 0.914   3.795   43.944 1.00 23.21  ? 35  TRP D CE3 1 
ATOM   5699 C CZ2 . TRP D 1 36  ? 0.558   4.958   41.384 1.00 27.90  ? 35  TRP D CZ2 1 
ATOM   5700 C CZ3 . TRP D 1 36  ? -0.300  3.770   43.292 1.00 29.34  ? 35  TRP D CZ3 1 
ATOM   5701 C CH2 . TRP D 1 36  ? -0.485  4.342   42.028 1.00 29.54  ? 35  TRP D CH2 1 
ATOM   5702 N N   . PRO D 1 37  ? 3.561   4.554   48.313 1.00 18.82  ? 36  PRO D N   1 
ATOM   5703 C CA  . PRO D 1 37  ? 3.973   4.180   49.676 1.00 26.72  ? 36  PRO D CA  1 
ATOM   5704 C C   . PRO D 1 37  ? 4.570   2.773   49.629 1.00 27.54  ? 36  PRO D C   1 
ATOM   5705 O O   . PRO D 1 37  ? 5.674   2.524   50.097 1.00 47.42  ? 36  PRO D O   1 
ATOM   5706 C CB  . PRO D 1 37  ? 2.685   4.229   50.479 1.00 32.46  ? 36  PRO D CB  1 
ATOM   5707 C CG  . PRO D 1 37  ? 1.568   4.513   49.543 1.00 29.07  ? 36  PRO D CG  1 
ATOM   5708 C CD  . PRO D 1 37  ? 2.109   4.728   48.161 1.00 21.01  ? 36  PRO D CD  1 
ATOM   5709 N N   . SER D 1 38  ? 3.790   1.916   49.013 1.00 29.03  ? 37  SER D N   1 
ATOM   5710 C CA  . SER D 1 38  ? 4.094   0.646   48.392 1.00 40.03  ? 37  SER D CA  1 
ATOM   5711 C C   . SER D 1 38  ? 5.596   0.501   48.164 1.00 41.12  ? 37  SER D C   1 
ATOM   5712 O O   . SER D 1 38  ? 6.319   -0.220  48.855 1.00 29.49  ? 37  SER D O   1 
ATOM   5713 C CB  . SER D 1 38  ? 3.290   0.556   47.079 1.00 43.41  ? 37  SER D CB  1 
ATOM   5714 O OG  . SER D 1 38  ? 2.189   1.478   47.049 1.00 35.19  ? 37  SER D OG  1 
ATOM   5715 N N   . ALA D 1 39  ? 6.105   1.215   47.164 1.00 35.75  ? 38  ALA D N   1 
ATOM   5716 C CA  . ALA D 1 39  ? 7.525   1.284   46.848 1.00 25.10  ? 38  ALA D CA  1 
ATOM   5717 C C   . ALA D 1 39  ? 7.816   2.698   46.372 1.00 29.93  ? 38  ALA D C   1 
ATOM   5718 O O   . ALA D 1 39  ? 7.157   3.186   45.457 1.00 29.36  ? 38  ALA D O   1 
ATOM   5719 C CB  . ALA D 1 39  ? 7.935   0.261   45.802 1.00 21.28  ? 38  ALA D CB  1 
ATOM   5720 N N   . LEU D 1 40  ? 8.757   3.406   46.998 1.00 31.74  ? 39  LEU D N   1 
ATOM   5721 C CA  . LEU D 1 40  ? 8.845   4.815   46.598 1.00 32.14  ? 39  LEU D CA  1 
ATOM   5722 C C   . LEU D 1 40  ? 9.815   4.965   45.437 1.00 27.81  ? 39  LEU D C   1 
ATOM   5723 O O   . LEU D 1 40  ? 10.963  4.540   45.555 1.00 22.05  ? 39  LEU D O   1 
ATOM   5724 C CB  . LEU D 1 40  ? 9.247   5.685   47.786 1.00 32.60  ? 39  LEU D CB  1 
ATOM   5725 C CG  . LEU D 1 40  ? 8.004   6.297   48.464 1.00 44.59  ? 39  LEU D CG  1 
ATOM   5726 C CD1 . LEU D 1 40  ? 7.923   5.875   49.917 1.00 64.01  ? 39  LEU D CD1 1 
ATOM   5727 C CD2 . LEU D 1 40  ? 8.014   7.812   48.316 1.00 43.13  ? 39  LEU D CD2 1 
ATOM   5728 N N   . PRO D 1 41  ? 9.338   5.560   44.355 1.00 24.57  ? 40  PRO D N   1 
ATOM   5729 C CA  . PRO D 1 41  ? 10.163  5.577   43.133 1.00 32.78  ? 40  PRO D CA  1 
ATOM   5730 C C   . PRO D 1 41  ? 11.502  6.251   43.415 1.00 29.04  ? 40  PRO D C   1 
ATOM   5731 O O   . PRO D 1 41  ? 11.592  7.217   44.174 1.00 29.54  ? 40  PRO D O   1 
ATOM   5732 C CB  . PRO D 1 41  ? 9.329   6.345   42.120 1.00 21.29  ? 40  PRO D CB  1 
ATOM   5733 C CG  . PRO D 1 41  ? 7.933   6.285   42.651 1.00 21.55  ? 40  PRO D CG  1 
ATOM   5734 C CD  . PRO D 1 41  ? 8.055   6.248   44.159 1.00 20.73  ? 40  PRO D CD  1 
ATOM   5735 N N   . THR D 1 42  ? 12.494  5.648   42.777 1.00 25.00  ? 41  THR D N   1 
ATOM   5736 C CA  . THR D 1 42  ? 13.881  6.085   42.851 1.00 23.80  ? 41  THR D CA  1 
ATOM   5737 C C   . THR D 1 42  ? 14.223  7.007   41.682 1.00 25.08  ? 41  THR D C   1 
ATOM   5738 O O   . THR D 1 42  ? 13.448  7.077   40.732 1.00 31.62  ? 41  THR D O   1 
ATOM   5739 C CB  . THR D 1 42  ? 14.806  4.861   42.862 1.00 29.96  ? 41  THR D CB  1 
ATOM   5740 O OG1 . THR D 1 42  ? 14.963  4.377   41.525 1.00 31.82  ? 41  THR D OG1 1 
ATOM   5741 C CG2 . THR D 1 42  ? 14.168  3.748   43.700 1.00 35.18  ? 41  THR D CG2 1 
ATOM   5742 N N   . ILE D 1 43  ? 15.355  7.697   41.759 1.00 26.07  ? 42  ILE D N   1 
ATOM   5743 C CA  . ILE D 1 43  ? 15.772  8.643   40.738 1.00 30.86  ? 42  ILE D CA  1 
ATOM   5744 C C   . ILE D 1 43  ? 15.835  7.965   39.370 1.00 22.38  ? 42  ILE D C   1 
ATOM   5745 O O   . ILE D 1 43  ? 15.283  8.491   38.415 1.00 24.86  ? 42  ILE D O   1 
ATOM   5746 C CB  . ILE D 1 43  ? 17.146  9.274   41.015 1.00 29.79  ? 42  ILE D CB  1 
ATOM   5747 C CG1 . ILE D 1 43  ? 17.172  10.166  42.254 1.00 23.33  ? 42  ILE D CG1 1 
ATOM   5748 C CG2 . ILE D 1 43  ? 17.607  10.036  39.778 1.00 30.38  ? 42  ILE D CG2 1 
ATOM   5749 C CD1 . ILE D 1 43  ? 16.009  11.136  42.293 1.00 21.02  ? 42  ILE D CD1 1 
ATOM   5750 N N   . LEU D 1 44  ? 16.512  6.827   39.346 1.00 20.71  ? 43  LEU D N   1 
ATOM   5751 C CA  . LEU D 1 44  ? 16.729  6.084   38.110 1.00 27.87  ? 43  LEU D CA  1 
ATOM   5752 C C   . LEU D 1 44  ? 15.412  5.565   37.547 1.00 36.00  ? 43  LEU D C   1 
ATOM   5753 O O   . LEU D 1 44  ? 15.161  5.542   36.340 1.00 26.63  ? 43  LEU D O   1 
ATOM   5754 C CB  . LEU D 1 44  ? 17.694  4.925   38.324 1.00 23.43  ? 43  LEU D CB  1 
ATOM   5755 C CG  . LEU D 1 44  ? 18.111  4.173   37.055 1.00 25.82  ? 43  LEU D CG  1 
ATOM   5756 C CD1 . LEU D 1 44  ? 18.214  5.111   35.868 1.00 21.24  ? 43  LEU D CD1 1 
ATOM   5757 C CD2 . LEU D 1 44  ? 19.436  3.464   37.290 1.00 37.15  ? 43  LEU D CD2 1 
ATOM   5758 N N   . GLN D 1 45  ? 14.560  5.144   38.488 1.00 27.58  ? 44  GLN D N   1 
ATOM   5759 C CA  . GLN D 1 45  ? 13.281  4.573   38.053 1.00 28.02  ? 44  GLN D CA  1 
ATOM   5760 C C   . GLN D 1 45  ? 12.454  5.596   37.278 1.00 24.17  ? 44  GLN D C   1 
ATOM   5761 O O   . GLN D 1 45  ? 11.982  5.308   36.175 1.00 18.67  ? 44  GLN D O   1 
ATOM   5762 C CB  . GLN D 1 45  ? 12.561  4.050   39.288 1.00 33.11  ? 44  GLN D CB  1 
ATOM   5763 C CG  . GLN D 1 45  ? 11.179  3.485   39.091 1.00 22.49  ? 44  GLN D CG  1 
ATOM   5764 C CD  . GLN D 1 45  ? 10.590  3.024   40.422 1.00 18.10  ? 44  GLN D CD  1 
ATOM   5765 O OE1 . GLN D 1 45  ? 11.295  2.628   41.339 1.00 13.66  ? 44  GLN D OE1 1 
ATOM   5766 N NE2 . GLN D 1 45  ? 9.279   3.079   40.482 1.00 19.26  ? 44  GLN D NE2 1 
ATOM   5767 N N   . ILE D 1 46  ? 12.305  6.755   37.897 1.00 15.61  ? 45  ILE D N   1 
ATOM   5768 C CA  . ILE D 1 46  ? 11.641  7.937   37.410 1.00 15.71  ? 45  ILE D CA  1 
ATOM   5769 C C   . ILE D 1 46  ? 12.270  8.467   36.110 1.00 18.69  ? 45  ILE D C   1 
ATOM   5770 O O   . ILE D 1 46  ? 11.505  8.684   35.174 1.00 21.41  ? 45  ILE D O   1 
ATOM   5771 C CB  . ILE D 1 46  ? 11.677  9.088   38.428 1.00 12.39  ? 45  ILE D CB  1 
ATOM   5772 C CG1 . ILE D 1 46  ? 10.941  8.792   39.735 1.00 24.78  ? 45  ILE D CG1 1 
ATOM   5773 C CG2 . ILE D 1 46  ? 11.108  10.329  37.784 1.00 18.21  ? 45  ILE D CG2 1 
ATOM   5774 C CD1 . ILE D 1 46  ? 11.012  9.958   40.706 1.00 29.40  ? 45  ILE D CD1 1 
ATOM   5775 N N   . ALA D 1 47  ? 13.586  8.650   36.074 1.00 14.95  ? 46  ALA D N   1 
ATOM   5776 C CA  . ALA D 1 47  ? 14.310  9.078   34.874 1.00 18.72  ? 46  ALA D CA  1 
ATOM   5777 C C   . ALA D 1 47  ? 14.131  8.129   33.690 1.00 16.72  ? 46  ALA D C   1 
ATOM   5778 O O   . ALA D 1 47  ? 13.993  8.564   32.548 1.00 22.86  ? 46  ALA D O   1 
ATOM   5779 C CB  . ALA D 1 47  ? 15.773  9.242   35.251 1.00 6.87   ? 46  ALA D CB  1 
ATOM   5780 N N   . LEU D 1 48  ? 14.093  6.804   33.871 1.00 14.61  ? 47  LEU D N   1 
ATOM   5781 C CA  . LEU D 1 48  ? 13.864  5.894   32.754 1.00 15.65  ? 47  LEU D CA  1 
ATOM   5782 C C   . LEU D 1 48  ? 12.393  5.861   32.385 1.00 22.14  ? 47  LEU D C   1 
ATOM   5783 O O   . LEU D 1 48  ? 11.988  5.621   31.256 1.00 19.89  ? 47  LEU D O   1 
ATOM   5784 C CB  . LEU D 1 48  ? 14.343  4.480   33.096 1.00 19.50  ? 47  LEU D CB  1 
ATOM   5785 C CG  . LEU D 1 48  ? 15.826  4.228   32.797 1.00 19.92  ? 47  LEU D CG  1 
ATOM   5786 C CD1 . LEU D 1 48  ? 16.371  3.057   33.591 1.00 21.22  ? 47  LEU D CD1 1 
ATOM   5787 C CD2 . LEU D 1 48  ? 16.015  3.979   31.313 1.00 29.85  ? 47  LEU D CD2 1 
ATOM   5788 N N   . ALA D 1 49  ? 11.535  6.104   33.381 1.00 29.09  ? 48  ALA D N   1 
ATOM   5789 C CA  . ALA D 1 49  ? 10.114  6.207   33.064 1.00 25.52  ? 48  ALA D CA  1 
ATOM   5790 C C   . ALA D 1 49  ? 9.858   7.396   32.142 1.00 25.46  ? 48  ALA D C   1 
ATOM   5791 O O   . ALA D 1 49  ? 9.150   7.293   31.137 1.00 21.06  ? 48  ALA D O   1 
ATOM   5792 C CB  . ALA D 1 49  ? 9.272   6.329   34.333 1.00 23.14  ? 48  ALA D CB  1 
ATOM   5793 N N   . PHE D 1 50  ? 10.398  8.577   32.472 1.00 19.81  ? 49  PHE D N   1 
ATOM   5794 C CA  . PHE D 1 50  ? 10.073  9.692   31.573 1.00 20.52  ? 49  PHE D CA  1 
ATOM   5795 C C   . PHE D 1 50  ? 10.655  9.450   30.185 1.00 16.97  ? 49  PHE D C   1 
ATOM   5796 O O   . PHE D 1 50  ? 9.963   9.716   29.203 1.00 20.90  ? 49  PHE D O   1 
ATOM   5797 C CB  . PHE D 1 50  ? 10.608  11.004  32.137 1.00 30.24  ? 49  PHE D CB  1 
ATOM   5798 C CG  . PHE D 1 50  ? 9.681   11.658  33.158 1.00 18.68  ? 49  PHE D CG  1 
ATOM   5799 C CD1 . PHE D 1 50  ? 9.661   11.207  34.459 1.00 19.94  ? 49  PHE D CD1 1 
ATOM   5800 C CD2 . PHE D 1 50  ? 8.861   12.705  32.779 1.00 23.95  ? 49  PHE D CD2 1 
ATOM   5801 C CE1 . PHE D 1 50  ? 8.815   11.832  35.354 1.00 26.63  ? 49  PHE D CE1 1 
ATOM   5802 C CE2 . PHE D 1 50  ? 8.007   13.345  33.657 1.00 25.20  ? 49  PHE D CE2 1 
ATOM   5803 C CZ  . PHE D 1 50  ? 8.003   12.881  34.960 1.00 30.42  ? 49  PHE D CZ  1 
ATOM   5804 N N   . GLY D 1 51  ? 11.887  8.960   30.115 1.00 16.58  ? 50  GLY D N   1 
ATOM   5805 C CA  . GLY D 1 51  ? 12.612  8.721   28.887 1.00 21.30  ? 50  GLY D CA  1 
ATOM   5806 C C   . GLY D 1 51  ? 12.017  7.677   27.960 1.00 28.78  ? 50  GLY D C   1 
ATOM   5807 O O   . GLY D 1 51  ? 12.057  7.858   26.735 1.00 18.27  ? 50  GLY D O   1 
ATOM   5808 N N   . LEU D 1 52  ? 11.490  6.592   28.532 1.00 26.32  ? 51  LEU D N   1 
ATOM   5809 C CA  . LEU D 1 52  ? 10.926  5.476   27.778 1.00 21.02  ? 51  LEU D CA  1 
ATOM   5810 C C   . LEU D 1 52  ? 9.566   5.885   27.233 1.00 16.70  ? 51  LEU D C   1 
ATOM   5811 O O   . LEU D 1 52  ? 9.052   5.437   26.210 1.00 21.36  ? 51  LEU D O   1 
ATOM   5812 C CB  . LEU D 1 52  ? 10.832  4.228   28.661 1.00 16.49  ? 51  LEU D CB  1 
ATOM   5813 C CG  . LEU D 1 52  ? 12.188  3.628   29.041 1.00 22.45  ? 51  LEU D CG  1 
ATOM   5814 C CD1 . LEU D 1 52  ? 12.001  2.347   29.829 1.00 19.68  ? 51  LEU D CD1 1 
ATOM   5815 C CD2 . LEU D 1 52  ? 13.051  3.370   27.811 1.00 23.14  ? 51  LEU D CD2 1 
ATOM   5816 N N   . ALA D 1 53  ? 8.975   6.806   27.985 1.00 13.80  ? 52  ALA D N   1 
ATOM   5817 C CA  . ALA D 1 53  ? 7.741   7.450   27.561 1.00 20.08  ? 52  ALA D CA  1 
ATOM   5818 C C   . ALA D 1 53  ? 8.030   8.181   26.253 1.00 20.27  ? 52  ALA D C   1 
ATOM   5819 O O   . ALA D 1 53  ? 7.367   8.021   25.240 1.00 29.58  ? 52  ALA D O   1 
ATOM   5820 C CB  . ALA D 1 53  ? 7.221   8.395   28.648 1.00 10.33  ? 52  ALA D CB  1 
ATOM   5821 N N   . ILE D 1 54  ? 9.065   9.026   26.276 1.00 26.47  ? 53  ILE D N   1 
ATOM   5822 C CA  . ILE D 1 54  ? 9.383   9.807   25.087 1.00 31.19  ? 53  ILE D CA  1 
ATOM   5823 C C   . ILE D 1 54  ? 9.916   8.895   23.977 1.00 27.79  ? 53  ILE D C   1 
ATOM   5824 O O   . ILE D 1 54  ? 9.478   9.082   22.850 1.00 21.45  ? 53  ILE D O   1 
ATOM   5825 C CB  . ILE D 1 54  ? 10.390  10.936  25.342 1.00 25.23  ? 53  ILE D CB  1 
ATOM   5826 C CG1 . ILE D 1 54  ? 9.876   12.043  26.253 1.00 24.02  ? 53  ILE D CG1 1 
ATOM   5827 C CG2 . ILE D 1 54  ? 10.825  11.524  23.999 1.00 13.93  ? 53  ILE D CG2 1 
ATOM   5828 C CD1 . ILE D 1 54  ? 8.618   12.701  25.688 1.00 20.04  ? 53  ILE D CD1 1 
ATOM   5829 N N   . GLY D 1 55  ? 10.807  7.955   24.268 1.00 17.87  ? 54  GLY D N   1 
ATOM   5830 C CA  . GLY D 1 55  ? 11.277  7.012   23.262 1.00 23.75  ? 54  GLY D CA  1 
ATOM   5831 C C   . GLY D 1 55  ? 10.109  6.265   22.650 1.00 25.03  ? 54  GLY D C   1 
ATOM   5832 O O   . GLY D 1 55  ? 9.930   6.188   21.438 1.00 28.57  ? 54  GLY D O   1 
ATOM   5833 N N   . THR D 1 56  ? 9.237   5.681   23.460 1.00 27.24  ? 55  THR D N   1 
ATOM   5834 C CA  . THR D 1 56  ? 8.066   4.982   22.953 1.00 15.90  ? 55  THR D CA  1 
ATOM   5835 C C   . THR D 1 56  ? 7.098   5.844   22.160 1.00 19.43  ? 55  THR D C   1 
ATOM   5836 O O   . THR D 1 56  ? 6.465   5.387   21.203 1.00 21.71  ? 55  THR D O   1 
ATOM   5837 C CB  . THR D 1 56  ? 7.323   4.332   24.147 1.00 19.13  ? 55  THR D CB  1 
ATOM   5838 O OG1 . THR D 1 56  ? 8.251   3.457   24.794 1.00 12.79  ? 55  THR D OG1 1 
ATOM   5839 C CG2 . THR D 1 56  ? 6.140   3.528   23.648 1.00 17.98  ? 55  THR D CG2 1 
ATOM   5840 N N   . LEU D 1 57  ? 6.884   7.117   22.457 1.00 26.55  ? 56  LEU D N   1 
ATOM   5841 C CA  . LEU D 1 57  ? 5.883   7.895   21.718 1.00 28.38  ? 56  LEU D CA  1 
ATOM   5842 C C   . LEU D 1 57  ? 6.469   8.524   20.461 1.00 23.12  ? 56  LEU D C   1 
ATOM   5843 O O   . LEU D 1 57  ? 5.797   8.726   19.444 1.00 21.40  ? 56  LEU D O   1 
ATOM   5844 C CB  . LEU D 1 57  ? 5.304   8.965   22.644 1.00 32.50  ? 56  LEU D CB  1 
ATOM   5845 C CG  . LEU D 1 57  ? 4.313   8.510   23.713 1.00 22.74  ? 56  LEU D CG  1 
ATOM   5846 C CD1 . LEU D 1 57  ? 4.205   9.534   24.842 1.00 23.05  ? 56  LEU D CD1 1 
ATOM   5847 C CD2 . LEU D 1 57  ? 2.969   8.260   23.050 1.00 17.46  ? 56  LEU D CD2 1 
ATOM   5848 N N   . ALA D 1 58  ? 7.761   8.846   20.526 1.00 18.69  ? 57  ALA D N   1 
ATOM   5849 C CA  . ALA D 1 58  ? 8.511   9.270   19.353 1.00 19.39  ? 57  ALA D CA  1 
ATOM   5850 C C   . ALA D 1 58  ? 8.458   8.169   18.294 1.00 25.62  ? 57  ALA D C   1 
ATOM   5851 O O   . ALA D 1 58  ? 8.172   8.404   17.127 1.00 22.34  ? 57  ALA D O   1 
ATOM   5852 C CB  . ALA D 1 58  ? 9.962   9.560   19.697 1.00 18.66  ? 57  ALA D CB  1 
ATOM   5853 N N   . GLN D 1 59  ? 8.740   6.950   18.769 1.00 20.26  ? 58  GLN D N   1 
ATOM   5854 C CA  . GLN D 1 59  ? 8.635   5.792   17.883 1.00 13.21  ? 58  GLN D CA  1 
ATOM   5855 C C   . GLN D 1 59  ? 7.231   5.622   17.340 1.00 13.73  ? 58  GLN D C   1 
ATOM   5856 O O   . GLN D 1 59  ? 7.101   5.425   16.141 1.00 21.01  ? 58  GLN D O   1 
ATOM   5857 C CB  . GLN D 1 59  ? 9.083   4.506   18.591 1.00 14.14  ? 58  GLN D CB  1 
ATOM   5858 C CG  . GLN D 1 59  ? 8.933   3.225   17.792 1.00 15.61  ? 58  GLN D CG  1 
ATOM   5859 C CD  . GLN D 1 59  ? 10.119  2.898   16.905 1.00 33.67  ? 58  GLN D CD  1 
ATOM   5860 O OE1 . GLN D 1 59  ? 10.191  1.846   16.243 1.00 28.65  ? 58  GLN D OE1 1 
ATOM   5861 N NE2 . GLN D 1 59  ? 11.063  3.837   16.911 1.00 16.79  ? 58  GLN D NE2 1 
ATOM   5862 N N   . ALA D 1 60  ? 6.192   5.643   18.158 1.00 18.68  ? 59  ALA D N   1 
ATOM   5863 C CA  . ALA D 1 60  ? 4.858   5.229   17.767 1.00 17.56  ? 59  ALA D CA  1 
ATOM   5864 C C   . ALA D 1 60  ? 4.124   6.297   16.971 1.00 26.16  ? 59  ALA D C   1 
ATOM   5865 O O   . ALA D 1 60  ? 3.333   5.973   16.092 1.00 23.25  ? 59  ALA D O   1 
ATOM   5866 C CB  . ALA D 1 60  ? 4.058   4.867   19.014 1.00 12.63  ? 59  ALA D CB  1 
ATOM   5867 N N   . LEU D 1 61  ? 4.371   7.563   17.283 1.00 23.81  ? 60  LEU D N   1 
ATOM   5868 C CA  . LEU D 1 61  ? 3.602   8.657   16.729 1.00 21.77  ? 60  LEU D CA  1 
ATOM   5869 C C   . LEU D 1 61  ? 4.454   9.688   16.007 1.00 19.27  ? 60  LEU D C   1 
ATOM   5870 O O   . LEU D 1 61  ? 3.891   10.528  15.305 1.00 21.44  ? 60  LEU D O   1 
ATOM   5871 C CB  . LEU D 1 61  ? 2.846   9.370   17.857 1.00 19.45  ? 60  LEU D CB  1 
ATOM   5872 C CG  . LEU D 1 61  ? 1.509   8.762   18.271 1.00 21.37  ? 60  LEU D CG  1 
ATOM   5873 C CD1 . LEU D 1 61  ? 0.863   9.633   19.335 1.00 26.16  ? 60  LEU D CD1 1 
ATOM   5874 C CD2 . LEU D 1 61  ? 0.569   8.596   17.087 1.00 20.90  ? 60  LEU D CD2 1 
ATOM   5875 N N   . GLY D 1 62  ? 5.757   9.635   16.230 1.00 20.28  ? 61  GLY D N   1 
ATOM   5876 C CA  . GLY D 1 62  ? 6.727   10.424  15.501 1.00 18.65  ? 61  GLY D CA  1 
ATOM   5877 C C   . GLY D 1 62  ? 6.364   10.458  14.016 1.00 31.88  ? 61  GLY D C   1 
ATOM   5878 O O   . GLY D 1 62  ? 6.252   11.514  13.395 1.00 24.08  ? 61  GLY D O   1 
ATOM   5879 N N   . PRO D 1 63  ? 6.169   9.318   13.370 1.00 23.80  ? 62  PRO D N   1 
ATOM   5880 C CA  . PRO D 1 63  ? 5.653   9.282   12.002 1.00 35.59  ? 62  PRO D CA  1 
ATOM   5881 C C   . PRO D 1 63  ? 4.479   10.193  11.682 1.00 43.46  ? 62  PRO D C   1 
ATOM   5882 O O   . PRO D 1 63  ? 4.256   10.567  10.514 1.00 48.84  ? 62  PRO D O   1 
ATOM   5883 C CB  . PRO D 1 63  ? 5.163   7.820   11.927 1.00 39.33  ? 62  PRO D CB  1 
ATOM   5884 C CG  . PRO D 1 63  ? 6.236   7.092   12.686 1.00 30.29  ? 62  PRO D CG  1 
ATOM   5885 C CD  . PRO D 1 63  ? 6.493   7.966   13.870 1.00 28.86  ? 62  PRO D CD  1 
ATOM   5886 N N   . VAL D 1 64  ? 3.680   10.569  12.684 1.00 29.39  ? 63  VAL D N   1 
ATOM   5887 C CA  . VAL D 1 64  ? 2.484   11.330  12.345 1.00 31.14  ? 63  VAL D CA  1 
ATOM   5888 C C   . VAL D 1 64  ? 2.640   12.841  12.453 1.00 40.70  ? 63  VAL D C   1 
ATOM   5889 O O   . VAL D 1 64  ? 1.858   13.537  11.785 1.00 42.83  ? 63  VAL D O   1 
ATOM   5890 C CB  . VAL D 1 64  ? 1.303   10.915  13.244 1.00 29.54  ? 63  VAL D CB  1 
ATOM   5891 C CG1 . VAL D 1 64  ? 0.047   11.691  12.848 1.00 19.24  ? 63  VAL D CG1 1 
ATOM   5892 C CG2 . VAL D 1 64  ? 1.081   9.415   13.161 1.00 33.55  ? 63  VAL D CG2 1 
ATOM   5893 N N   . SER D 1 65  ? 3.566   13.355  13.251 1.00 27.60  ? 64  SER D N   1 
ATOM   5894 C CA  . SER D 1 65  ? 3.616   14.773  13.598 1.00 27.50  ? 64  SER D CA  1 
ATOM   5895 C C   . SER D 1 65  ? 4.997   15.382  13.701 1.00 28.71  ? 64  SER D C   1 
ATOM   5896 O O   . SER D 1 65  ? 5.242   16.594  13.639 1.00 27.71  ? 64  SER D O   1 
ATOM   5897 C CB  . SER D 1 65  ? 2.927   14.945  14.982 1.00 24.47  ? 64  SER D CB  1 
ATOM   5898 O OG  . SER D 1 65  ? 3.774   14.382  15.981 1.00 24.20  ? 64  SER D OG  1 
ATOM   5899 N N   . GLY D 1 66  ? 6.037   14.572  13.901 1.00 28.24  ? 65  GLY D N   1 
ATOM   5900 C CA  . GLY D 1 66  ? 7.305   15.176  14.315 1.00 30.33  ? 65  GLY D CA  1 
ATOM   5901 C C   . GLY D 1 66  ? 7.678   14.613  15.692 1.00 21.24  ? 65  GLY D C   1 
ATOM   5902 O O   . GLY D 1 66  ? 8.866   14.527  15.965 1.00 22.28  ? 65  GLY D O   1 
ATOM   5903 N N   . GLY D 1 67  ? 6.641   14.242  16.432 1.00 19.66  ? 66  GLY D N   1 
ATOM   5904 C CA  . GLY D 1 67  ? 6.731   13.635  17.753 1.00 22.64  ? 66  GLY D CA  1 
ATOM   5905 C C   . GLY D 1 67  ? 7.420   14.632  18.666 1.00 16.22  ? 66  GLY D C   1 
ATOM   5906 O O   . GLY D 1 67  ? 8.461   14.362  19.252 1.00 26.90  ? 66  GLY D O   1 
ATOM   5907 N N   . HIS D 1 68  ? 6.823   15.827  18.713 1.00 19.72  ? 67  HIS D N   1 
ATOM   5908 C CA  . HIS D 1 68  ? 7.511   16.903  19.432 1.00 26.91  ? 67  HIS D CA  1 
ATOM   5909 C C   . HIS D 1 68  ? 7.177   16.812  20.918 1.00 28.95  ? 67  HIS D C   1 
ATOM   5910 O O   . HIS D 1 68  ? 8.080   16.911  21.751 1.00 33.23  ? 67  HIS D O   1 
ATOM   5911 C CB  . HIS D 1 68  ? 7.154   18.281  18.913 1.00 27.66  ? 67  HIS D CB  1 
ATOM   5912 C CG  . HIS D 1 68  ? 7.395   18.585  17.472 1.00 29.83  ? 67  HIS D CG  1 
ATOM   5913 N ND1 . HIS D 1 68  ? 7.075   19.821  16.945 1.00 28.89  ? 67  HIS D ND1 1 
ATOM   5914 C CD2 . HIS D 1 68  ? 7.903   17.870  16.448 1.00 20.27  ? 67  HIS D CD2 1 
ATOM   5915 C CE1 . HIS D 1 68  ? 7.379   19.851  15.661 1.00 32.46  ? 67  HIS D CE1 1 
ATOM   5916 N NE2 . HIS D 1 68  ? 7.888   18.679  15.344 1.00 23.98  ? 67  HIS D NE2 1 
ATOM   5917 N N   . ILE D 1 69  ? 5.903   16.633  21.259 1.00 31.04  ? 68  ILE D N   1 
ATOM   5918 C CA  . ILE D 1 69  ? 5.505   16.364  22.649 1.00 26.60  ? 68  ILE D CA  1 
ATOM   5919 C C   . ILE D 1 69  ? 6.087   17.329  23.667 1.00 26.29  ? 68  ILE D C   1 
ATOM   5920 O O   . ILE D 1 69  ? 6.212   16.974  24.839 1.00 35.95  ? 68  ILE D O   1 
ATOM   5921 C CB  . ILE D 1 69  ? 5.946   14.922  22.967 1.00 14.27  ? 68  ILE D CB  1 
ATOM   5922 C CG1 . ILE D 1 69  ? 5.629   13.985  21.791 1.00 23.05  ? 68  ILE D CG1 1 
ATOM   5923 C CG2 . ILE D 1 69  ? 5.364   14.375  24.251 1.00 16.20  ? 68  ILE D CG2 1 
ATOM   5924 C CD1 . ILE D 1 69  ? 6.127   12.574  22.021 1.00 24.51  ? 68  ILE D CD1 1 
ATOM   5925 N N   . ASN D 1 70  ? 6.455   18.536  23.250 1.00 27.93  ? 69  ASN D N   1 
ATOM   5926 C CA  . ASN D 1 70  ? 7.191   19.525  24.012 1.00 26.49  ? 69  ASN D CA  1 
ATOM   5927 C C   . ASN D 1 70  ? 7.170   20.904  23.350 1.00 36.26  ? 69  ASN D C   1 
ATOM   5928 O O   . ASN D 1 70  ? 7.806   21.065  22.296 1.00 23.14  ? 69  ASN D O   1 
ATOM   5929 C CB  . ASN D 1 70  ? 8.643   19.067  24.175 1.00 26.70  ? 69  ASN D CB  1 
ATOM   5930 C CG  . ASN D 1 70  ? 9.461   19.957  25.084 1.00 22.84  ? 69  ASN D CG  1 
ATOM   5931 O OD1 . ASN D 1 70  ? 9.107   21.106  25.361 1.00 27.60  ? 69  ASN D OD1 1 
ATOM   5932 N ND2 . ASN D 1 70  ? 10.577  19.421  25.561 1.00 18.79  ? 69  ASN D ND2 1 
ATOM   5933 N N   . PRO D 1 71  ? 6.462   21.841  23.981 1.00 40.33  ? 70  PRO D N   1 
ATOM   5934 C CA  . PRO D 1 71  ? 6.353   23.210  23.469 1.00 36.45  ? 70  PRO D CA  1 
ATOM   5935 C C   . PRO D 1 71  ? 7.712   23.853  23.230 1.00 35.29  ? 70  PRO D C   1 
ATOM   5936 O O   . PRO D 1 71  ? 7.861   24.684  22.326 1.00 44.54  ? 70  PRO D O   1 
ATOM   5937 C CB  . PRO D 1 71  ? 5.632   23.979  24.579 1.00 28.93  ? 70  PRO D CB  1 
ATOM   5938 C CG  . PRO D 1 71  ? 4.869   22.928  25.316 1.00 27.41  ? 70  PRO D CG  1 
ATOM   5939 C CD  . PRO D 1 71  ? 5.703   21.676  25.240 1.00 27.39  ? 70  PRO D CD  1 
ATOM   5940 N N   . ALA D 1 72  ? 8.720   23.488  24.020 1.00 27.76  ? 71  ALA D N   1 
ATOM   5941 C CA  . ALA D 1 72  ? 10.013  24.142  23.805 1.00 26.08  ? 71  ALA D CA  1 
ATOM   5942 C C   . ALA D 1 72  ? 10.638  23.651  22.509 1.00 27.75  ? 71  ALA D C   1 
ATOM   5943 O O   . ALA D 1 72  ? 11.326  24.379  21.787 1.00 23.06  ? 71  ALA D O   1 
ATOM   5944 C CB  . ALA D 1 72  ? 10.924  23.920  25.004 1.00 22.95  ? 71  ALA D CB  1 
ATOM   5945 N N   . ILE D 1 73  ? 10.402  22.376  22.172 1.00 27.18  ? 72  ILE D N   1 
ATOM   5946 C CA  . ILE D 1 73  ? 11.081  21.891  20.968 1.00 26.26  ? 72  ILE D CA  1 
ATOM   5947 C C   . ILE D 1 73  ? 10.341  22.344  19.714 1.00 34.12  ? 72  ILE D C   1 
ATOM   5948 O O   . ILE D 1 73  ? 10.941  22.629  18.671 1.00 37.80  ? 72  ILE D O   1 
ATOM   5949 C CB  . ILE D 1 73  ? 11.250  20.369  21.022 1.00 27.50  ? 72  ILE D CB  1 
ATOM   5950 C CG1 . ILE D 1 73  ? 12.360  19.910  21.979 1.00 20.86  ? 72  ILE D CG1 1 
ATOM   5951 C CG2 . ILE D 1 73  ? 11.498  19.856  19.616 1.00 24.17  ? 72  ILE D CG2 1 
ATOM   5952 C CD1 . ILE D 1 73  ? 11.983  18.694  22.789 1.00 54.04  ? 72  ILE D CD1 1 
ATOM   5953 N N   . THR D 1 74  ? 9.022   22.440  19.812 1.00 23.23  ? 73  THR D N   1 
ATOM   5954 C CA  . THR D 1 74  ? 8.189   23.016  18.781 1.00 19.83  ? 73  THR D CA  1 
ATOM   5955 C C   . THR D 1 74  ? 8.564   24.484  18.556 1.00 37.01  ? 73  THR D C   1 
ATOM   5956 O O   . THR D 1 74  ? 8.722   24.901  17.402 1.00 41.10  ? 73  THR D O   1 
ATOM   5957 C CB  . THR D 1 74  ? 6.690   22.926  19.119 1.00 26.82  ? 73  THR D CB  1 
ATOM   5958 O OG1 . THR D 1 74  ? 6.218   21.571  19.076 1.00 24.49  ? 73  THR D OG1 1 
ATOM   5959 C CG2 . THR D 1 74  ? 5.864   23.694  18.086 1.00 26.35  ? 73  THR D CG2 1 
ATOM   5960 N N   . LEU D 1 75  ? 8.723   25.306  19.601 1.00 27.41  ? 74  LEU D N   1 
ATOM   5961 C CA  . LEU D 1 75  ? 9.045   26.714  19.330 1.00 15.15  ? 74  LEU D CA  1 
ATOM   5962 C C   . LEU D 1 75  ? 10.430  26.807  18.696 1.00 27.83  ? 74  LEU D C   1 
ATOM   5963 O O   . LEU D 1 75  ? 10.707  27.604  17.791 1.00 31.34  ? 74  LEU D O   1 
ATOM   5964 C CB  . LEU D 1 75  ? 8.991   27.561  20.584 1.00 21.02  ? 74  LEU D CB  1 
ATOM   5965 C CG  . LEU D 1 75  ? 7.782   27.616  21.506 1.00 30.99  ? 74  LEU D CG  1 
ATOM   5966 C CD1 . LEU D 1 75  ? 7.979   28.651  22.621 1.00 18.14  ? 74  LEU D CD1 1 
ATOM   5967 C CD2 . LEU D 1 75  ? 6.514   27.932  20.734 1.00 39.36  ? 74  LEU D CD2 1 
ATOM   5968 N N   . ALA D 1 76  ? 11.327  25.951  19.186 1.00 20.49  ? 75  ALA D N   1 
ATOM   5969 C CA  . ALA D 1 76  ? 12.668  25.869  18.636 1.00 20.73  ? 75  ALA D CA  1 
ATOM   5970 C C   . ALA D 1 76  ? 12.640  25.536  17.147 1.00 27.05  ? 75  ALA D C   1 
ATOM   5971 O O   . ALA D 1 76  ? 13.330  26.150  16.349 1.00 33.50  ? 75  ALA D O   1 
ATOM   5972 C CB  . ALA D 1 76  ? 13.498  24.797  19.335 1.00 24.32  ? 75  ALA D CB  1 
ATOM   5973 N N   . LEU D 1 77  ? 11.841  24.531  16.803 1.00 22.04  ? 76  LEU D N   1 
ATOM   5974 C CA  . LEU D 1 77  ? 11.827  24.088  15.416 1.00 27.16  ? 76  LEU D CA  1 
ATOM   5975 C C   . LEU D 1 77  ? 11.222  25.220  14.588 1.00 36.48  ? 76  LEU D C   1 
ATOM   5976 O O   . LEU D 1 77  ? 11.522  25.360  13.406 1.00 28.62  ? 76  LEU D O   1 
ATOM   5977 C CB  . LEU D 1 77  ? 11.058  22.794  15.217 1.00 14.74  ? 76  LEU D CB  1 
ATOM   5978 C CG  . LEU D 1 77  ? 11.792  21.492  15.544 1.00 19.62  ? 76  LEU D CG  1 
ATOM   5979 C CD1 . LEU D 1 77  ? 10.775  20.385  15.780 1.00 18.13  ? 76  LEU D CD1 1 
ATOM   5980 C CD2 . LEU D 1 77  ? 12.762  21.100  14.449 1.00 23.24  ? 76  LEU D CD2 1 
ATOM   5981 N N   . LEU D 1 78  ? 10.382  26.025  15.238 1.00 33.08  ? 77  LEU D N   1 
ATOM   5982 C CA  . LEU D 1 78  ? 9.866   27.195  14.523 1.00 27.21  ? 77  LEU D CA  1 
ATOM   5983 C C   . LEU D 1 78  ? 11.039  28.130  14.256 1.00 33.42  ? 77  LEU D C   1 
ATOM   5984 O O   . LEU D 1 78  ? 11.276  28.564  13.125 1.00 31.46  ? 77  LEU D O   1 
ATOM   5985 C CB  . LEU D 1 78  ? 8.767   27.897  15.296 1.00 29.28  ? 77  LEU D CB  1 
ATOM   5986 C CG  . LEU D 1 78  ? 8.121   29.125  14.646 1.00 36.88  ? 77  LEU D CG  1 
ATOM   5987 C CD1 . LEU D 1 78  ? 7.525   28.794  13.279 1.00 18.47  ? 77  LEU D CD1 1 
ATOM   5988 C CD2 . LEU D 1 78  ? 7.068   29.686  15.586 1.00 42.85  ? 77  LEU D CD2 1 
ATOM   5989 N N   . VAL D 1 79  ? 11.789  28.420  15.321 1.00 33.18  ? 78  VAL D N   1 
ATOM   5990 C CA  . VAL D 1 79  ? 12.922  29.328  15.122 1.00 29.33  ? 78  VAL D CA  1 
ATOM   5991 C C   . VAL D 1 79  ? 13.892  28.806  14.081 1.00 39.58  ? 78  VAL D C   1 
ATOM   5992 O O   . VAL D 1 79  ? 14.428  29.565  13.257 1.00 30.25  ? 78  VAL D O   1 
ATOM   5993 C CB  . VAL D 1 79  ? 13.618  29.581  16.465 1.00 29.48  ? 78  VAL D CB  1 
ATOM   5994 C CG1 . VAL D 1 79  ? 14.970  30.242  16.297 1.00 30.33  ? 78  VAL D CG1 1 
ATOM   5995 C CG2 . VAL D 1 79  ? 12.701  30.455  17.316 1.00 22.55  ? 78  VAL D CG2 1 
ATOM   5996 N N   . GLY D 1 80  ? 14.139  27.498  14.052 1.00 38.81  ? 79  GLY D N   1 
ATOM   5997 C CA  . GLY D 1 80  ? 15.077  26.967  13.077 1.00 33.91  ? 79  GLY D CA  1 
ATOM   5998 C C   . GLY D 1 80  ? 14.553  26.870  11.662 1.00 33.95  ? 79  GLY D C   1 
ATOM   5999 O O   . GLY D 1 80  ? 15.196  26.229  10.817 1.00 33.61  ? 79  GLY D O   1 
ATOM   6000 N N   . ASN D 1 81  ? 13.401  27.472  11.372 1.00 31.99  ? 80  ASN D N   1 
ATOM   6001 C CA  . ASN D 1 81  ? 12.822  27.415  10.025 1.00 35.61  ? 80  ASN D CA  1 
ATOM   6002 C C   . ASN D 1 81  ? 12.503  26.005  9.570  1.00 32.97  ? 80  ASN D C   1 
ATOM   6003 O O   . ASN D 1 81  ? 12.806  25.609  8.442  1.00 37.03  ? 80  ASN D O   1 
ATOM   6004 C CB  . ASN D 1 81  ? 13.803  28.085  9.045  1.00 32.11  ? 80  ASN D CB  1 
ATOM   6005 C CG  . ASN D 1 81  ? 13.106  28.749  7.872  1.00 39.79  ? 80  ASN D CG  1 
ATOM   6006 O OD1 . ASN D 1 81  ? 12.009  29.295  7.997  1.00 30.66  ? 80  ASN D OD1 1 
ATOM   6007 N ND2 . ASN D 1 81  ? 13.745  28.701  6.699  1.00 37.99  ? 80  ASN D ND2 1 
ATOM   6008 N N   . GLN D 1 82  ? 11.886  25.182  10.418 1.00 34.16  ? 81  GLN D N   1 
ATOM   6009 C CA  . GLN D 1 82  ? 11.574  23.808  10.047 1.00 24.45  ? 81  GLN D CA  1 
ATOM   6010 C C   . GLN D 1 82  ? 10.068  23.590  9.901  1.00 24.41  ? 81  GLN D C   1 
ATOM   6011 O O   . GLN D 1 82  ? 9.686   22.596  9.280  1.00 41.85  ? 81  GLN D O   1 
ATOM   6012 C CB  . GLN D 1 82  ? 12.096  22.782  11.062 1.00 16.57  ? 81  GLN D CB  1 
ATOM   6013 C CG  . GLN D 1 82  ? 13.589  22.897  11.317 1.00 30.50  ? 81  GLN D CG  1 
ATOM   6014 C CD  . GLN D 1 82  ? 14.428  22.464  10.128 1.00 30.66  ? 81  GLN D CD  1 
ATOM   6015 O OE1 . GLN D 1 82  ? 15.280  23.204  9.636  1.00 47.52  ? 81  GLN D OE1 1 
ATOM   6016 N NE2 . GLN D 1 82  ? 14.191  21.244  9.680  1.00 27.10  ? 81  GLN D NE2 1 
ATOM   6017 N N   . ILE D 1 83  ? 9.263   24.474  10.461 1.00 31.08  ? 82  ILE D N   1 
ATOM   6018 C CA  . ILE D 1 83  ? 7.810   24.334  10.503 1.00 38.88  ? 82  ILE D CA  1 
ATOM   6019 C C   . ILE D 1 83  ? 7.089   25.660  10.315 1.00 29.86  ? 82  ILE D C   1 
ATOM   6020 O O   . ILE D 1 83  ? 7.654   26.743  10.481 1.00 26.19  ? 82  ILE D O   1 
ATOM   6021 C CB  . ILE D 1 83  ? 7.352   23.711  11.848 1.00 43.44  ? 82  ILE D CB  1 
ATOM   6022 C CG1 . ILE D 1 83  ? 7.712   24.525  13.099 1.00 32.02  ? 82  ILE D CG1 1 
ATOM   6023 C CG2 . ILE D 1 83  ? 7.853   22.275  11.959 1.00 25.33  ? 82  ILE D CG2 1 
ATOM   6024 C CD1 . ILE D 1 83  ? 6.784   24.299  14.281 1.00 30.05  ? 82  ILE D CD1 1 
ATOM   6025 N N   . SER D 1 84  ? 5.798   25.608  9.977  1.00 32.69  ? 83  SER D N   1 
ATOM   6026 C CA  . SER D 1 84  ? 5.086   26.866  9.746  1.00 28.37  ? 83  SER D CA  1 
ATOM   6027 C C   . SER D 1 84  ? 4.612   27.479  11.053 1.00 33.57  ? 83  SER D C   1 
ATOM   6028 O O   . SER D 1 84  ? 4.493   26.815  12.084 1.00 37.02  ? 83  SER D O   1 
ATOM   6029 C CB  . SER D 1 84  ? 3.898   26.642  8.805  1.00 31.21  ? 83  SER D CB  1 
ATOM   6030 O OG  . SER D 1 84  ? 2.812   26.030  9.493  1.00 27.07  ? 83  SER D OG  1 
ATOM   6031 N N   . LEU D 1 85  ? 4.333   28.783  11.024 1.00 27.80  ? 84  LEU D N   1 
ATOM   6032 C CA  . LEU D 1 85  ? 3.791   29.435  12.212 1.00 28.44  ? 84  LEU D CA  1 
ATOM   6033 C C   . LEU D 1 85  ? 2.557   28.721  12.741 1.00 39.65  ? 84  LEU D C   1 
ATOM   6034 O O   . LEU D 1 85  ? 2.431   28.467  13.944 1.00 42.86  ? 84  LEU D O   1 
ATOM   6035 C CB  . LEU D 1 85  ? 3.458   30.890  11.898 1.00 33.15  ? 84  LEU D CB  1 
ATOM   6036 C CG  . LEU D 1 85  ? 3.040   31.767  13.079 1.00 44.20  ? 84  LEU D CG  1 
ATOM   6037 C CD1 . LEU D 1 85  ? 4.215   32.015  14.018 1.00 48.16  ? 84  LEU D CD1 1 
ATOM   6038 C CD2 . LEU D 1 85  ? 2.462   33.089  12.592 1.00 53.66  ? 84  LEU D CD2 1 
ATOM   6039 N N   . LEU D 1 86  ? 1.628   28.389  11.840 1.00 42.55  ? 85  LEU D N   1 
ATOM   6040 C CA  . LEU D 1 86  ? 0.396   27.746  12.304 1.00 41.04  ? 85  LEU D CA  1 
ATOM   6041 C C   . LEU D 1 86  ? 0.648   26.346  12.850 1.00 37.61  ? 85  LEU D C   1 
ATOM   6042 O O   . LEU D 1 86  ? -0.051  25.920  13.773 1.00 40.55  ? 85  LEU D O   1 
ATOM   6043 C CB  . LEU D 1 86  ? -0.641  27.702  11.183 1.00 46.90  ? 85  LEU D CB  1 
ATOM   6044 C CG  . LEU D 1 86  ? -1.124  29.066  10.685 1.00 61.00  ? 85  LEU D CG  1 
ATOM   6045 C CD1 . LEU D 1 86  ? -1.465  29.963  11.865 1.00 64.91  ? 85  LEU D CD1 1 
ATOM   6046 C CD2 . LEU D 1 86  ? -0.086  29.708  9.775  1.00 79.70  ? 85  LEU D CD2 1 
ATOM   6047 N N   . ARG D 1 87  ? 1.621   25.606  12.316 1.00 30.43  ? 86  ARG D N   1 
ATOM   6048 C CA  . ARG D 1 87  ? 1.909   24.301  12.900 1.00 32.84  ? 86  ARG D CA  1 
ATOM   6049 C C   . ARG D 1 87  ? 2.396   24.471  14.342 1.00 30.53  ? 86  ARG D C   1 
ATOM   6050 O O   . ARG D 1 87  ? 1.935   23.760  15.233 1.00 38.72  ? 86  ARG D O   1 
ATOM   6051 C CB  . ARG D 1 87  ? 2.956   23.525  12.101 1.00 29.56  ? 86  ARG D CB  1 
ATOM   6052 C CG  . ARG D 1 87  ? 3.296   22.179  12.712 1.00 28.97  ? 86  ARG D CG  1 
ATOM   6053 C CD  . ARG D 1 87  ? 4.261   21.382  11.838 1.00 39.61  ? 86  ARG D CD  1 
ATOM   6054 N NE  . ARG D 1 87  ? 3.749   21.330  10.476 1.00 41.46  ? 86  ARG D NE  1 
ATOM   6055 C CZ  . ARG D 1 87  ? 2.969   20.398  9.957  1.00 43.37  ? 86  ARG D CZ  1 
ATOM   6056 N NH1 . ARG D 1 87  ? 2.562   19.357  10.672 1.00 41.95  ? 86  ARG D NH1 1 
ATOM   6057 N NH2 . ARG D 1 87  ? 2.599   20.535  8.686  1.00 29.61  ? 86  ARG D NH2 1 
ATOM   6058 N N   . ALA D 1 88  ? 3.326   25.399  14.551 1.00 25.02  ? 87  ALA D N   1 
ATOM   6059 C CA  . ALA D 1 88  ? 3.866   25.636  15.884 1.00 26.96  ? 87  ALA D CA  1 
ATOM   6060 C C   . ALA D 1 88  ? 2.728   25.924  16.852 1.00 35.13  ? 87  ALA D C   1 
ATOM   6061 O O   . ALA D 1 88  ? 2.551   25.280  17.886 1.00 48.45  ? 87  ALA D O   1 
ATOM   6062 C CB  . ALA D 1 88  ? 4.863   26.777  15.894 1.00 28.87  ? 87  ALA D CB  1 
ATOM   6063 N N   . PHE D 1 89  ? 1.920   26.916  16.497 1.00 39.20  ? 88  PHE D N   1 
ATOM   6064 C CA  . PHE D 1 89  ? 0.819   27.349  17.364 1.00 29.47  ? 88  PHE D CA  1 
ATOM   6065 C C   . PHE D 1 89  ? -0.130  26.223  17.696 1.00 26.76  ? 88  PHE D C   1 
ATOM   6066 O O   . PHE D 1 89  ? -0.496  25.959  18.836 1.00 25.74  ? 88  PHE D O   1 
ATOM   6067 C CB  . PHE D 1 89  ? 0.081   28.482  16.656 1.00 33.29  ? 88  PHE D CB  1 
ATOM   6068 C CG  . PHE D 1 89  ? -1.322  28.769  17.125 1.00 35.86  ? 88  PHE D CG  1 
ATOM   6069 C CD1 . PHE D 1 89  ? -1.558  29.234  18.407 1.00 40.95  ? 88  PHE D CD1 1 
ATOM   6070 C CD2 . PHE D 1 89  ? -2.395  28.578  16.272 1.00 48.04  ? 88  PHE D CD2 1 
ATOM   6071 C CE1 . PHE D 1 89  ? -2.853  29.498  18.810 1.00 44.37  ? 88  PHE D CE1 1 
ATOM   6072 C CE2 . PHE D 1 89  ? -3.690  28.844  16.674 1.00 50.17  ? 88  PHE D CE2 1 
ATOM   6073 C CZ  . PHE D 1 89  ? -3.919  29.311  17.953 1.00 46.69  ? 88  PHE D CZ  1 
ATOM   6074 N N   . PHE D 1 90  ? -0.609  25.503  16.674 1.00 32.35  ? 89  PHE D N   1 
ATOM   6075 C CA  . PHE D 1 90  ? -1.583  24.469  17.037 1.00 27.92  ? 89  PHE D CA  1 
ATOM   6076 C C   . PHE D 1 90  ? -0.899  23.376  17.834 1.00 25.05  ? 89  PHE D C   1 
ATOM   6077 O O   . PHE D 1 90  ? -1.515  22.716  18.659 1.00 26.39  ? 89  PHE D O   1 
ATOM   6078 C CB  . PHE D 1 90  ? -2.238  23.914  15.779 1.00 25.79  ? 89  PHE D CB  1 
ATOM   6079 C CG  . PHE D 1 90  ? -3.436  24.757  15.370 1.00 33.16  ? 89  PHE D CG  1 
ATOM   6080 C CD1 . PHE D 1 90  ? -4.649  24.597  16.013 1.00 40.64  ? 89  PHE D CD1 1 
ATOM   6081 C CD2 . PHE D 1 90  ? -3.314  25.693  14.357 1.00 41.78  ? 89  PHE D CD2 1 
ATOM   6082 C CE1 . PHE D 1 90  ? -5.748  25.360  15.655 1.00 56.18  ? 89  PHE D CE1 1 
ATOM   6083 C CE2 . PHE D 1 90  ? -4.412  26.456  13.986 1.00 52.89  ? 89  PHE D CE2 1 
ATOM   6084 C CZ  . PHE D 1 90  ? -5.627  26.287  14.630 1.00 60.95  ? 89  PHE D CZ  1 
ATOM   6085 N N   . TYR D 1 91  ? 0.397   23.189  17.573 1.00 29.04  ? 90  TYR D N   1 
ATOM   6086 C CA  . TYR D 1 91  ? 1.059   22.085  18.265 1.00 28.32  ? 90  TYR D CA  1 
ATOM   6087 C C   . TYR D 1 91  ? 1.158   22.419  19.748 1.00 25.19  ? 90  TYR D C   1 
ATOM   6088 O O   . TYR D 1 91  ? 0.946   21.585  20.627 1.00 29.18  ? 90  TYR D O   1 
ATOM   6089 C CB  . TYR D 1 91  ? 2.436   21.809  17.693 1.00 26.48  ? 90  TYR D CB  1 
ATOM   6090 C CG  . TYR D 1 91  ? 2.489   20.814  16.558 1.00 32.30  ? 90  TYR D CG  1 
ATOM   6091 C CD1 . TYR D 1 91  ? 1.384   20.524  15.770 1.00 35.57  ? 90  TYR D CD1 1 
ATOM   6092 C CD2 . TYR D 1 91  ? 3.685   20.155  16.284 1.00 32.10  ? 90  TYR D CD2 1 
ATOM   6093 C CE1 . TYR D 1 91  ? 1.486   19.600  14.740 1.00 39.01  ? 90  TYR D CE1 1 
ATOM   6094 C CE2 . TYR D 1 91  ? 3.791   19.240  15.260 1.00 30.80  ? 90  TYR D CE2 1 
ATOM   6095 C CZ  . TYR D 1 91  ? 2.681   18.964  14.486 1.00 36.25  ? 90  TYR D CZ  1 
ATOM   6096 O OH  . TYR D 1 91  ? 2.787   18.046  13.457 1.00 31.84  ? 90  TYR D OH  1 
ATOM   6097 N N   . VAL D 1 92  ? 1.500   23.680  20.007 1.00 25.27  ? 91  VAL D N   1 
ATOM   6098 C CA  . VAL D 1 92  ? 1.697   24.043  21.409 1.00 22.52  ? 91  VAL D CA  1 
ATOM   6099 C C   . VAL D 1 92  ? 0.383   23.912  22.161 1.00 31.85  ? 91  VAL D C   1 
ATOM   6100 O O   . VAL D 1 92  ? 0.378   23.349  23.258 1.00 27.14  ? 91  VAL D O   1 
ATOM   6101 C CB  . VAL D 1 92  ? 2.253   25.455  21.521 1.00 25.37  ? 91  VAL D CB  1 
ATOM   6102 C CG1 . VAL D 1 92  ? 2.384   25.892  22.971 1.00 20.36  ? 91  VAL D CG1 1 
ATOM   6103 C CG2 . VAL D 1 92  ? 3.609   25.444  20.825 1.00 16.27  ? 91  VAL D CG2 1 
ATOM   6104 N N   . ALA D 1 93  ? -0.675  24.413  21.522 1.00 27.47  ? 92  ALA D N   1 
ATOM   6105 C CA  . ALA D 1 93  ? -1.999  24.277  22.131 1.00 34.97  ? 92  ALA D CA  1 
ATOM   6106 C C   . ALA D 1 93  ? -2.260  22.817  22.505 1.00 33.58  ? 92  ALA D C   1 
ATOM   6107 O O   . ALA D 1 93  ? -2.524  22.467  23.647 1.00 41.28  ? 92  ALA D O   1 
ATOM   6108 C CB  . ALA D 1 93  ? -3.087  24.771  21.197 1.00 32.20  ? 92  ALA D CB  1 
ATOM   6109 N N   . ALA D 1 94  ? -2.168  21.983  21.482 1.00 30.71  ? 93  ALA D N   1 
ATOM   6110 C CA  . ALA D 1 94  ? -2.327  20.547  21.576 1.00 35.63  ? 93  ALA D CA  1 
ATOM   6111 C C   . ALA D 1 94  ? -1.510  19.969  22.720 1.00 28.60  ? 93  ALA D C   1 
ATOM   6112 O O   . ALA D 1 94  ? -1.992  19.183  23.538 1.00 22.15  ? 93  ALA D O   1 
ATOM   6113 C CB  . ALA D 1 94  ? -1.921  19.932  20.237 1.00 26.14  ? 93  ALA D CB  1 
ATOM   6114 N N   . GLN D 1 95  ? -0.235  20.348  22.785 1.00 28.02  ? 94  GLN D N   1 
ATOM   6115 C CA  . GLN D 1 95  ? 0.620   19.812  23.832 1.00 26.44  ? 94  GLN D CA  1 
ATOM   6116 C C   . GLN D 1 95  ? 0.185   20.244  25.228 1.00 30.09  ? 94  GLN D C   1 
ATOM   6117 O O   . GLN D 1 95  ? 0.287   19.444  26.162 1.00 30.61  ? 94  GLN D O   1 
ATOM   6118 C CB  . GLN D 1 95  ? 2.082   20.239  23.602 1.00 21.04  ? 94  GLN D CB  1 
ATOM   6119 C CG  . GLN D 1 95  ? 2.527   19.761  22.225 1.00 23.10  ? 94  GLN D CG  1 
ATOM   6120 C CD  . GLN D 1 95  ? 3.706   20.528  21.675 1.00 33.58  ? 94  GLN D CD  1 
ATOM   6121 O OE1 . GLN D 1 95  ? 4.080   21.597  22.167 1.00 32.94  ? 94  GLN D OE1 1 
ATOM   6122 N NE2 . GLN D 1 95  ? 4.308   19.955  20.636 1.00 26.75  ? 94  GLN D NE2 1 
ATOM   6123 N N   . LEU D 1 96  ? -0.266  21.490  25.333 1.00 30.35  ? 95  LEU D N   1 
ATOM   6124 C CA  . LEU D 1 96  ? -0.768  22.028  26.593 1.00 25.54  ? 95  LEU D CA  1 
ATOM   6125 C C   . LEU D 1 96  ? -2.101  21.360  26.925 1.00 22.46  ? 95  LEU D C   1 
ATOM   6126 O O   . LEU D 1 96  ? -2.251  20.805  28.012 1.00 36.07  ? 95  LEU D O   1 
ATOM   6127 C CB  . LEU D 1 96  ? -0.867  23.549  26.554 1.00 33.04  ? 95  LEU D CB  1 
ATOM   6128 C CG  . LEU D 1 96  ? 0.427   24.363  26.528 1.00 37.42  ? 95  LEU D CG  1 
ATOM   6129 C CD1 . LEU D 1 96  ? 0.126   25.858  26.472 1.00 27.38  ? 95  LEU D CD1 1 
ATOM   6130 C CD2 . LEU D 1 96  ? 1.314   24.061  27.724 1.00 29.31  ? 95  LEU D CD2 1 
ATOM   6131 N N   . VAL D 1 97  ? -3.081  21.349  26.039 1.00 22.10  ? 96  VAL D N   1 
ATOM   6132 C CA  . VAL D 1 97  ? -4.339  20.646  26.278 1.00 21.94  ? 96  VAL D CA  1 
ATOM   6133 C C   . VAL D 1 97  ? -4.081  19.174  26.591 1.00 40.74  ? 96  VAL D C   1 
ATOM   6134 O O   . VAL D 1 97  ? -4.749  18.559  27.429 1.00 31.06  ? 96  VAL D O   1 
ATOM   6135 C CB  . VAL D 1 97  ? -5.286  20.741  25.067 1.00 25.73  ? 96  VAL D CB  1 
ATOM   6136 C CG1 . VAL D 1 97  ? -6.624  20.087  25.370 1.00 39.54  ? 96  VAL D CG1 1 
ATOM   6137 C CG2 . VAL D 1 97  ? -5.484  22.197  24.658 1.00 29.77  ? 96  VAL D CG2 1 
ATOM   6138 N N   . GLY D 1 98  ? -3.091  18.623  25.882 1.00 48.14  ? 97  GLY D N   1 
ATOM   6139 C CA  . GLY D 1 98  ? -2.696  17.234  26.067 1.00 38.85  ? 97  GLY D CA  1 
ATOM   6140 C C   . GLY D 1 98  ? -2.196  17.020  27.489 1.00 24.27  ? 97  GLY D C   1 
ATOM   6141 O O   . GLY D 1 98  ? -2.704  16.177  28.215 1.00 19.56  ? 97  GLY D O   1 
ATOM   6142 N N   . ALA D 1 99  ? -1.193  17.805  27.854 1.00 27.84  ? 98  ALA D N   1 
ATOM   6143 C CA  . ALA D 1 99  ? -0.611  17.756  29.193 1.00 20.92  ? 98  ALA D CA  1 
ATOM   6144 C C   . ALA D 1 99  ? -1.694  17.810  30.260 1.00 24.54  ? 98  ALA D C   1 
ATOM   6145 O O   . ALA D 1 99  ? -1.648  17.052  31.231 1.00 31.44  ? 98  ALA D O   1 
ATOM   6146 C CB  . ALA D 1 99  ? 0.380   18.894  29.334 1.00 20.91  ? 98  ALA D CB  1 
ATOM   6147 N N   . ILE D 1 100 ? -2.684  18.685  30.111 1.00 27.43  ? 99  ILE D N   1 
ATOM   6148 C CA  . ILE D 1 100 ? -3.732  18.804  31.130 1.00 25.46  ? 99  ILE D CA  1 
ATOM   6149 C C   . ILE D 1 100 ? -4.616  17.576  31.121 1.00 25.66  ? 99  ILE D C   1 
ATOM   6150 O O   . ILE D 1 100 ? -4.935  17.063  32.197 1.00 25.52  ? 99  ILE D O   1 
ATOM   6151 C CB  . ILE D 1 100 ? -4.595  20.060  30.929 1.00 25.59  ? 99  ILE D CB  1 
ATOM   6152 C CG1 . ILE D 1 100 ? -3.823  21.376  31.081 1.00 32.93  ? 99  ILE D CG1 1 
ATOM   6153 C CG2 . ILE D 1 100 ? -5.808  20.037  31.852 1.00 16.79  ? 99  ILE D CG2 1 
ATOM   6154 C CD1 . ILE D 1 100 ? -4.536  22.564  30.461 1.00 29.65  ? 99  ILE D CD1 1 
ATOM   6155 N N   . ALA D 1 101 ? -5.021  17.083  29.932 1.00 21.54  ? 100 ALA D N   1 
ATOM   6156 C CA  . ALA D 1 101 ? -5.883  15.895  30.007 1.00 25.00  ? 100 ALA D CA  1 
ATOM   6157 C C   . ALA D 1 101 ? -5.135  14.729  30.644 1.00 29.29  ? 100 ALA D C   1 
ATOM   6158 O O   . ALA D 1 101 ? -5.749  13.972  31.391 1.00 29.83  ? 100 ALA D O   1 
ATOM   6159 C CB  . ALA D 1 101 ? -6.412  15.444  28.664 1.00 18.14  ? 100 ALA D CB  1 
ATOM   6160 N N   . GLY D 1 102 ? -3.842  14.571  30.348 1.00 25.33  ? 101 GLY D N   1 
ATOM   6161 C CA  . GLY D 1 102 ? -3.150  13.397  30.871 1.00 29.81  ? 101 GLY D CA  1 
ATOM   6162 C C   . GLY D 1 102 ? -3.055  13.433  32.385 1.00 31.09  ? 101 GLY D C   1 
ATOM   6163 O O   . GLY D 1 102 ? -3.198  12.441  33.101 1.00 25.32  ? 101 GLY D O   1 
ATOM   6164 N N   . ALA D 1 103 ? -2.789  14.635  32.884 1.00 34.26  ? 102 ALA D N   1 
ATOM   6165 C CA  . ALA D 1 103 ? -2.653  14.837  34.328 1.00 33.41  ? 102 ALA D CA  1 
ATOM   6166 C C   . ALA D 1 103 ? -4.012  14.574  34.989 1.00 37.31  ? 102 ALA D C   1 
ATOM   6167 O O   . ALA D 1 103 ? -4.103  14.115  36.130 1.00 21.72  ? 102 ALA D O   1 
ATOM   6168 C CB  . ALA D 1 103 ? -2.136  16.229  34.593 1.00 16.46  ? 102 ALA D CB  1 
ATOM   6169 N N   . GLY D 1 104 ? -5.007  14.897  34.165 1.00 33.06  ? 103 GLY D N   1 
ATOM   6170 C CA  . GLY D 1 104 ? -6.415  14.787  34.453 1.00 26.74  ? 103 GLY D CA  1 
ATOM   6171 C C   . GLY D 1 104 ? -6.801  13.344  34.713 1.00 35.93  ? 103 GLY D C   1 
ATOM   6172 O O   . GLY D 1 104 ? -7.477  12.996  35.674 1.00 42.06  ? 103 GLY D O   1 
ATOM   6173 N N   . ILE D 1 105 ? -6.338  12.477  33.818 1.00 31.96  ? 104 ILE D N   1 
ATOM   6174 C CA  . ILE D 1 105 ? -6.677  11.067  33.942 1.00 28.26  ? 104 ILE D CA  1 
ATOM   6175 C C   . ILE D 1 105 ? -5.938  10.430  35.099 1.00 20.48  ? 104 ILE D C   1 
ATOM   6176 O O   . ILE D 1 105 ? -6.505  9.586   35.792 1.00 31.51  ? 104 ILE D O   1 
ATOM   6177 C CB  . ILE D 1 105 ? -6.346  10.341  32.621 1.00 30.29  ? 104 ILE D CB  1 
ATOM   6178 C CG1 . ILE D 1 105 ? -7.276  10.795  31.496 1.00 29.16  ? 104 ILE D CG1 1 
ATOM   6179 C CG2 . ILE D 1 105 ? -6.332  8.839   32.825 1.00 29.65  ? 104 ILE D CG2 1 
ATOM   6180 C CD1 . ILE D 1 105 ? -6.603  10.883  30.143 1.00 36.88  ? 104 ILE D CD1 1 
ATOM   6181 N N   . LEU D 1 106 ? -4.684  10.839  35.297 1.00 15.03  ? 105 LEU D N   1 
ATOM   6182 C CA  . LEU D 1 106 ? -3.934  10.284  36.420 1.00 21.73  ? 105 LEU D CA  1 
ATOM   6183 C C   . LEU D 1 106 ? -4.601  10.648  37.752 1.00 35.40  ? 105 LEU D C   1 
ATOM   6184 O O   . LEU D 1 106 ? -4.814  9.739   38.562 1.00 34.12  ? 105 LEU D O   1 
ATOM   6185 C CB  . LEU D 1 106 ? -2.500  10.786  36.425 1.00 22.22  ? 105 LEU D CB  1 
ATOM   6186 C CG  . LEU D 1 106 ? -1.628  10.270  37.570 1.00 30.75  ? 105 LEU D CG  1 
ATOM   6187 C CD1 . LEU D 1 106 ? -1.506  8.755   37.497 1.00 32.07  ? 105 LEU D CD1 1 
ATOM   6188 C CD2 . LEU D 1 106 ? -0.271  10.957  37.534 1.00 31.66  ? 105 LEU D CD2 1 
ATOM   6189 N N   . TYR D 1 107 ? -4.897  11.936  37.925 1.00 30.81  ? 106 TYR D N   1 
ATOM   6190 C CA  . TYR D 1 107 ? -5.606  12.421  39.107 1.00 35.10  ? 106 TYR D CA  1 
ATOM   6191 C C   . TYR D 1 107 ? -6.811  11.512  39.352 1.00 33.87  ? 106 TYR D C   1 
ATOM   6192 O O   . TYR D 1 107 ? -7.074  11.087  40.465 1.00 45.74  ? 106 TYR D O   1 
ATOM   6193 C CB  . TYR D 1 107 ? -6.087  13.858  38.956 1.00 40.52  ? 106 TYR D CB  1 
ATOM   6194 C CG  . TYR D 1 107 ? -6.726  14.492  40.172 1.00 36.77  ? 106 TYR D CG  1 
ATOM   6195 C CD1 . TYR D 1 107 ? -5.977  15.294  41.025 1.00 49.63  ? 106 TYR D CD1 1 
ATOM   6196 C CD2 . TYR D 1 107 ? -8.060  14.326  40.500 1.00 28.23  ? 106 TYR D CD2 1 
ATOM   6197 C CE1 . TYR D 1 107 ? -6.543  15.885  42.139 1.00 53.04  ? 106 TYR D CE1 1 
ATOM   6198 C CE2 . TYR D 1 107 ? -8.649  14.902  41.605 1.00 38.25  ? 106 TYR D CE2 1 
ATOM   6199 C CZ  . TYR D 1 107 ? -7.874  15.690  42.430 1.00 45.70  ? 106 TYR D CZ  1 
ATOM   6200 O OH  . TYR D 1 107 ? -8.433  16.279  43.536 1.00 54.86  ? 106 TYR D OH  1 
ATOM   6201 N N   . GLY D 1 108 ? -7.495  11.265  38.239 1.00 30.50  ? 107 GLY D N   1 
ATOM   6202 C CA  . GLY D 1 108 ? -8.653  10.409  38.223 1.00 39.04  ? 107 GLY D CA  1 
ATOM   6203 C C   . GLY D 1 108 ? -8.374  8.985   38.630 1.00 44.81  ? 107 GLY D C   1 
ATOM   6204 O O   . GLY D 1 108 ? -9.280  8.300   39.117 1.00 42.69  ? 107 GLY D O   1 
ATOM   6205 N N   . VAL D 1 109 ? -7.156  8.452   38.459 1.00 38.00  ? 108 VAL D N   1 
ATOM   6206 C CA  . VAL D 1 109 ? -7.072  7.015   38.719 1.00 28.96  ? 108 VAL D CA  1 
ATOM   6207 C C   . VAL D 1 109 ? -6.148  6.659   39.870 1.00 20.51  ? 108 VAL D C   1 
ATOM   6208 O O   . VAL D 1 109 ? -6.245  5.501   40.294 1.00 37.21  ? 108 VAL D O   1 
ATOM   6209 C CB  . VAL D 1 109 ? -6.634  6.222   37.461 1.00 30.47  ? 108 VAL D CB  1 
ATOM   6210 C CG1 . VAL D 1 109 ? -7.673  6.399   36.359 1.00 16.68  ? 108 VAL D CG1 1 
ATOM   6211 C CG2 . VAL D 1 109 ? -5.245  6.632   36.997 1.00 24.97  ? 108 VAL D CG2 1 
ATOM   6212 N N   . ALA D 1 110 ? -5.302  7.547   40.350 1.00 22.90  ? 109 ALA D N   1 
ATOM   6213 C CA  . ALA D 1 110 ? -4.368  7.239   41.434 1.00 23.19  ? 109 ALA D CA  1 
ATOM   6214 C C   . ALA D 1 110 ? -5.069  7.210   42.782 1.00 18.00  ? 109 ALA D C   1 
ATOM   6215 O O   . ALA D 1 110 ? -5.956  8.060   42.960 1.00 35.01  ? 109 ALA D O   1 
ATOM   6216 C CB  . ALA D 1 110 ? -3.244  8.269   41.514 1.00 24.39  ? 109 ALA D CB  1 
ATOM   6217 N N   . PRO D 1 111 ? -4.709  6.313   43.685 1.00 24.55  ? 110 PRO D N   1 
ATOM   6218 C CA  . PRO D 1 111 ? -5.336  6.304   45.017 1.00 32.04  ? 110 PRO D CA  1 
ATOM   6219 C C   . PRO D 1 111 ? -5.018  7.577   45.802 1.00 45.20  ? 110 PRO D C   1 
ATOM   6220 O O   . PRO D 1 111 ? -3.942  8.139   45.548 1.00 45.43  ? 110 PRO D O   1 
ATOM   6221 C CB  . PRO D 1 111 ? -4.662  5.122   45.716 1.00 31.06  ? 110 PRO D CB  1 
ATOM   6222 C CG  . PRO D 1 111 ? -3.349  4.981   45.018 1.00 31.64  ? 110 PRO D CG  1 
ATOM   6223 C CD  . PRO D 1 111 ? -3.698  5.251   43.565 1.00 29.70  ? 110 PRO D CD  1 
ATOM   6224 N N   . LEU D 1 112 ? -5.898  7.984   46.706 1.00 46.72  ? 111 LEU D N   1 
ATOM   6225 C CA  . LEU D 1 112 ? -5.762  9.120   47.617 1.00 46.11  ? 111 LEU D CA  1 
ATOM   6226 C C   . LEU D 1 112 ? -4.336  9.226   48.182 1.00 28.51  ? 111 LEU D C   1 
ATOM   6227 O O   . LEU D 1 112 ? -3.714  10.280  48.178 1.00 39.56  ? 111 LEU D O   1 
ATOM   6228 C CB  . LEU D 1 112 ? -6.709  9.020   48.808 1.00 53.57  ? 111 LEU D CB  1 
ATOM   6229 C CG  . LEU D 1 112 ? -7.835  10.015  49.057 1.00 52.65  ? 111 LEU D CG  1 
ATOM   6230 C CD1 . LEU D 1 112 ? -7.447  11.014  50.146 1.00 55.14  ? 111 LEU D CD1 1 
ATOM   6231 C CD2 . LEU D 1 112 ? -8.236  10.743  47.783 1.00 45.35  ? 111 LEU D CD2 1 
ATOM   6232 N N   . ASN D 1 113 ? -3.909  8.096   48.662 1.00 21.81  ? 112 ASN D N   1 
ATOM   6233 C CA  . ASN D 1 113 ? -2.659  7.552   49.099 1.00 42.01  ? 112 ASN D CA  1 
ATOM   6234 C C   . ASN D 1 113 ? -1.456  8.049   48.303 1.00 50.00  ? 112 ASN D C   1 
ATOM   6235 O O   . ASN D 1 113 ? -0.407  8.386   48.855 1.00 48.95  ? 112 ASN D O   1 
ATOM   6236 C CB  . ASN D 1 113 ? -2.778  6.021   48.924 1.00 58.34  ? 112 ASN D CB  1 
ATOM   6237 C CG  . ASN D 1 113 ? -1.699  5.218   49.620 1.00 70.10  ? 112 ASN D CG  1 
ATOM   6238 O OD1 . ASN D 1 113 ? -1.459  4.059   49.267 1.00 81.96  ? 112 ASN D OD1 1 
ATOM   6239 N ND2 . ASN D 1 113 ? -1.041  5.826   50.616 1.00 71.93  ? 112 ASN D ND2 1 
ATOM   6240 N N   . ALA D 1 114 ? -1.597  8.074   46.976 1.00 42.84  ? 113 ALA D N   1 
ATOM   6241 C CA  . ALA D 1 114 ? -0.469  8.307   46.090 1.00 41.50  ? 113 ALA D CA  1 
ATOM   6242 C C   . ALA D 1 114 ? -0.598  9.588   45.290 1.00 32.29  ? 113 ALA D C   1 
ATOM   6243 O O   . ALA D 1 114 ? 0.343   9.964   44.586 1.00 42.56  ? 113 ALA D O   1 
ATOM   6244 C CB  . ALA D 1 114 ? -0.333  7.129   45.123 1.00 26.00  ? 113 ALA D CB  1 
ATOM   6245 N N   . ARG D 1 115 ? -1.752  10.244  45.384 1.00 26.26  ? 114 ARG D N   1 
ATOM   6246 C CA  . ARG D 1 115 ? -1.967  11.414  44.528 1.00 32.00  ? 114 ARG D CA  1 
ATOM   6247 C C   . ARG D 1 115 ? -0.981  12.538  44.817 1.00 29.20  ? 114 ARG D C   1 
ATOM   6248 O O   . ARG D 1 115 ? -0.484  13.198  43.902 1.00 35.93  ? 114 ARG D O   1 
ATOM   6249 C CB  . ARG D 1 115 ? -3.414  11.894  44.666 1.00 34.21  ? 114 ARG D CB  1 
ATOM   6250 C CG  . ARG D 1 115 ? -3.573  13.384  44.449 1.00 39.68  ? 114 ARG D CG  1 
ATOM   6251 C CD  . ARG D 1 115 ? -4.991  13.820  44.186 1.00 40.04  ? 114 ARG D CD  1 
ATOM   6252 N NE  . ARG D 1 115 ? -5.978  12.760  44.039 1.00 43.04  ? 114 ARG D NE  1 
ATOM   6253 C CZ  . ARG D 1 115 ? -7.239  12.908  44.443 1.00 45.94  ? 114 ARG D CZ  1 
ATOM   6254 N NH1 . ARG D 1 115 ? -7.608  14.058  45.006 1.00 73.10  ? 114 ARG D NH1 1 
ATOM   6255 N NH2 . ARG D 1 115 ? -8.147  11.954  44.314 1.00 35.99  ? 114 ARG D NH2 1 
ATOM   6256 N N   . GLY D 1 116 ? -0.648  12.792  46.072 1.00 28.83  ? 115 GLY D N   1 
ATOM   6257 C CA  . GLY D 1 116 ? 0.307   13.817  46.466 1.00 26.20  ? 115 GLY D CA  1 
ATOM   6258 C C   . GLY D 1 116 ? 0.028   15.158  45.827 1.00 22.08  ? 115 GLY D C   1 
ATOM   6259 O O   . GLY D 1 116 ? -1.117  15.605  45.794 1.00 23.18  ? 115 GLY D O   1 
ATOM   6260 N N   . ASN D 1 117 ? 1.046   15.834  45.278 1.00 28.62  ? 116 ASN D N   1 
ATOM   6261 C CA  . ASN D 1 117 ? 0.697   17.049  44.533 1.00 34.24  ? 116 ASN D CA  1 
ATOM   6262 C C   . ASN D 1 117 ? 0.765   16.766  43.032 1.00 25.93  ? 116 ASN D C   1 
ATOM   6263 O O   . ASN D 1 117 ? 0.923   17.706  42.266 1.00 24.91  ? 116 ASN D O   1 
ATOM   6264 C CB  . ASN D 1 117 ? 1.594   18.234  44.862 1.00 31.96  ? 116 ASN D CB  1 
ATOM   6265 C CG  . ASN D 1 117 ? 3.062   17.883  44.725 1.00 44.49  ? 116 ASN D CG  1 
ATOM   6266 O OD1 . ASN D 1 117 ? 3.398   17.004  43.929 1.00 50.64  ? 116 ASN D OD1 1 
ATOM   6267 N ND2 . ASN D 1 117 ? 3.902   18.568  45.496 1.00 48.11  ? 116 ASN D ND2 1 
ATOM   6268 N N   . LEU D 1 118 ? 0.653   15.494  42.691 1.00 20.93  ? 117 LEU D N   1 
ATOM   6269 C CA  . LEU D 1 118 ? 0.612   15.057  41.312 1.00 26.23  ? 117 LEU D CA  1 
ATOM   6270 C C   . LEU D 1 118 ? 1.916   15.342  40.571 1.00 23.95  ? 117 LEU D C   1 
ATOM   6271 O O   . LEU D 1 118 ? 1.840   15.703  39.395 1.00 28.85  ? 117 LEU D O   1 
ATOM   6272 C CB  . LEU D 1 118 ? -0.561  15.720  40.569 1.00 39.05  ? 117 LEU D CB  1 
ATOM   6273 C CG  . LEU D 1 118 ? -1.291  14.838  39.548 1.00 40.49  ? 117 LEU D CG  1 
ATOM   6274 C CD1 . LEU D 1 118 ? -2.067  13.738  40.261 1.00 26.86  ? 117 LEU D CD1 1 
ATOM   6275 C CD2 . LEU D 1 118 ? -2.208  15.666  38.655 1.00 26.65  ? 117 LEU D CD2 1 
ATOM   6276 N N   . ALA D 1 119 ? 3.064   15.173  41.204 1.00 28.33  ? 118 ALA D N   1 
ATOM   6277 C CA  . ALA D 1 119 ? 4.378   15.308  40.592 1.00 35.98  ? 118 ALA D CA  1 
ATOM   6278 C C   . ALA D 1 119 ? 4.599   16.644  39.879 1.00 38.67  ? 118 ALA D C   1 
ATOM   6279 O O   . ALA D 1 119 ? 5.361   16.704  38.901 1.00 24.12  ? 118 ALA D O   1 
ATOM   6280 C CB  . ALA D 1 119 ? 4.664   14.150  39.619 1.00 9.95   ? 118 ALA D CB  1 
ATOM   6281 N N   . VAL D 1 120 ? 3.991   17.724  40.355 1.00 26.16  ? 119 VAL D N   1 
ATOM   6282 C CA  . VAL D 1 120 ? 4.300   19.071  39.863 1.00 17.65  ? 119 VAL D CA  1 
ATOM   6283 C C   . VAL D 1 120 ? 5.802   19.299  39.921 1.00 23.65  ? 119 VAL D C   1 
ATOM   6284 O O   . VAL D 1 120 ? 6.428   18.747  40.820 1.00 24.87  ? 119 VAL D O   1 
ATOM   6285 C CB  . VAL D 1 120 ? 3.543   20.137  40.670 1.00 30.80  ? 119 VAL D CB  1 
ATOM   6286 C CG1 . VAL D 1 120 ? 2.087   20.157  40.214 1.00 20.76  ? 119 VAL D CG1 1 
ATOM   6287 C CG2 . VAL D 1 120 ? 3.609   19.909  42.180 1.00 27.73  ? 119 VAL D CG2 1 
ATOM   6288 N N   . ASN D 1 121 ? 6.419   20.061  39.008 1.00 19.82  ? 120 ASN D N   1 
ATOM   6289 C CA  . ASN D 1 121 ? 7.836   20.385  39.184 1.00 18.61  ? 120 ASN D CA  1 
ATOM   6290 C C   . ASN D 1 121 ? 8.027   21.270  40.411 1.00 28.79  ? 120 ASN D C   1 
ATOM   6291 O O   . ASN D 1 121 ? 7.124   21.923  40.938 1.00 29.53  ? 120 ASN D O   1 
ATOM   6292 C CB  . ASN D 1 121 ? 8.426   21.094  37.957 1.00 15.31  ? 120 ASN D CB  1 
ATOM   6293 C CG  . ASN D 1 121 ? 8.734   20.114  36.831 1.00 21.47  ? 120 ASN D CG  1 
ATOM   6294 O OD1 . ASN D 1 121 ? 9.667   19.318  36.913 1.00 33.60  ? 120 ASN D OD1 1 
ATOM   6295 N ND2 . ASN D 1 121 ? 7.943   20.158  35.768 1.00 22.71  ? 120 ASN D ND2 1 
ATOM   6296 N N   . ALA D 1 122 ? 9.250   21.338  40.939 1.00 20.46  ? 121 ALA D N   1 
ATOM   6297 C CA  . ALA D 1 122 ? 9.386   22.183  42.120 1.00 25.20  ? 121 ALA D CA  1 
ATOM   6298 C C   . ALA D 1 122 ? 10.866  22.344  42.427 1.00 22.48  ? 121 ALA D C   1 
ATOM   6299 O O   . ALA D 1 122 ? 11.623  21.414  42.155 1.00 30.64  ? 121 ALA D O   1 
ATOM   6300 C CB  . ALA D 1 122 ? 8.639   21.584  43.305 1.00 24.89  ? 121 ALA D CB  1 
ATOM   6301 N N   . LEU D 1 123 ? 11.237  23.493  42.976 1.00 26.86  ? 122 LEU D N   1 
ATOM   6302 C CA  . LEU D 1 123 ? 12.645  23.716  43.272 1.00 31.22  ? 122 LEU D CA  1 
ATOM   6303 C C   . LEU D 1 123 ? 13.130  22.939  44.486 1.00 38.08  ? 122 LEU D C   1 
ATOM   6304 O O   . LEU D 1 123 ? 12.369  22.616  45.393 1.00 53.63  ? 122 LEU D O   1 
ATOM   6305 C CB  . LEU D 1 123 ? 12.884  25.212  43.523 1.00 44.66  ? 122 LEU D CB  1 
ATOM   6306 C CG  . LEU D 1 123 ? 13.202  25.998  42.244 1.00 49.19  ? 122 LEU D CG  1 
ATOM   6307 C CD1 . LEU D 1 123 ? 13.705  27.385  42.594 1.00 42.91  ? 122 LEU D CD1 1 
ATOM   6308 C CD2 . LEU D 1 123 ? 14.197  25.197  41.422 1.00 69.07  ? 122 LEU D CD2 1 
ATOM   6309 N N   . ASN D 1 124 ? 14.428  22.695  44.475 1.00 45.31  ? 123 ASN D N   1 
ATOM   6310 C CA  . ASN D 1 124 ? 15.225  22.186  45.570 1.00 49.76  ? 123 ASN D CA  1 
ATOM   6311 C C   . ASN D 1 124 ? 15.133  23.061  46.816 1.00 55.21  ? 123 ASN D C   1 
ATOM   6312 O O   . ASN D 1 124 ? 15.586  22.608  47.871 1.00 65.64  ? 123 ASN D O   1 
ATOM   6313 C CB  . ASN D 1 124 ? 16.685  22.108  45.125 1.00 56.75  ? 123 ASN D CB  1 
ATOM   6314 C CG  . ASN D 1 124 ? 17.692  21.809  46.208 1.00 74.52  ? 123 ASN D CG  1 
ATOM   6315 O OD1 . ASN D 1 124 ? 17.848  22.528  47.201 1.00 97.40  ? 123 ASN D OD1 1 
ATOM   6316 N ND2 . ASN D 1 124 ? 18.439  20.716  46.025 1.00 90.25  ? 123 ASN D ND2 1 
ATOM   6317 N N   . ASN D 1 125 ? 14.604  24.271  46.726 1.00 57.83  ? 124 ASN D N   1 
ATOM   6318 C CA  . ASN D 1 125 ? 14.470  25.159  47.877 1.00 64.33  ? 124 ASN D CA  1 
ATOM   6319 C C   . ASN D 1 125 ? 15.826  25.751  48.238 1.00 65.72  ? 124 ASN D C   1 
ATOM   6320 O O   . ASN D 1 125 ? 15.977  26.973  48.315 1.00 88.78  ? 124 ASN D O   1 
ATOM   6321 C CB  . ASN D 1 125 ? 13.866  24.443  49.079 1.00 69.09  ? 124 ASN D CB  1 
ATOM   6322 C CG  . ASN D 1 125 ? 12.360  24.283  49.025 1.00 72.23  ? 124 ASN D CG  1 
ATOM   6323 O OD1 . ASN D 1 125 ? 11.720  24.425  47.979 1.00 85.90  ? 124 ASN D OD1 1 
ATOM   6324 N ND2 . ASN D 1 125 ? 11.778  23.980  50.181 1.00 38.54  ? 124 ASN D ND2 1 
ATOM   6325 N N   . ASN D 1 126 ? 16.844  24.914  48.441 1.00 56.99  ? 125 ASN D N   1 
ATOM   6326 C CA  . ASN D 1 126 ? 18.181  25.499  48.616 1.00 59.15  ? 125 ASN D CA  1 
ATOM   6327 C C   . ASN D 1 126 ? 18.816  25.759  47.245 1.00 59.07  ? 125 ASN D C   1 
ATOM   6328 O O   . ASN D 1 126 ? 20.009  26.053  47.135 1.00 60.10  ? 125 ASN D O   1 
ATOM   6329 C CB  . ASN D 1 126 ? 19.073  24.622  49.486 1.00 63.72  ? 125 ASN D CB  1 
ATOM   6330 C CG  . ASN D 1 126 ? 18.645  24.546  50.939 1.00 71.01  ? 125 ASN D CG  1 
ATOM   6331 O OD1 . ASN D 1 126 ? 18.669  25.513  51.706 1.00 80.65  ? 125 ASN D OD1 1 
ATOM   6332 N ND2 . ASN D 1 126 ? 18.239  23.349  51.350 1.00 73.61  ? 125 ASN D ND2 1 
ATOM   6333 N N   . THR D 1 127 ? 18.012  25.656  46.191 1.00 48.40  ? 126 THR D N   1 
ATOM   6334 C CA  . THR D 1 127 ? 18.407  25.966  44.825 1.00 43.17  ? 126 THR D CA  1 
ATOM   6335 C C   . THR D 1 127 ? 17.740  27.266  44.409 1.00 41.71  ? 126 THR D C   1 
ATOM   6336 O O   . THR D 1 127 ? 16.529  27.399  44.596 1.00 47.49  ? 126 THR D O   1 
ATOM   6337 C CB  . THR D 1 127 ? 18.003  24.846  43.851 1.00 42.57  ? 126 THR D CB  1 
ATOM   6338 O OG1 . THR D 1 127 ? 18.907  23.740  43.978 1.00 34.55  ? 126 THR D OG1 1 
ATOM   6339 C CG2 . THR D 1 127 ? 18.082  25.317  42.406 1.00 37.59  ? 126 THR D CG2 1 
ATOM   6340 N N   . THR D 1 128 ? 18.460  28.235  43.863 1.00 50.69  ? 127 THR D N   1 
ATOM   6341 C CA  . THR D 1 128 ? 17.817  29.480  43.460 1.00 51.53  ? 127 THR D CA  1 
ATOM   6342 C C   . THR D 1 128 ? 17.168  29.394  42.077 1.00 49.70  ? 127 THR D C   1 
ATOM   6343 O O   . THR D 1 128 ? 17.538  28.536  41.278 1.00 38.85  ? 127 THR D O   1 
ATOM   6344 C CB  . THR D 1 128 ? 18.815  30.650  43.405 1.00 59.77  ? 127 THR D CB  1 
ATOM   6345 O OG1 . THR D 1 128 ? 18.089  31.879  43.286 1.00 97.46  ? 127 THR D OG1 1 
ATOM   6346 C CG2 . THR D 1 128 ? 19.674  30.542  42.157 1.00 33.61  ? 127 THR D CG2 1 
ATOM   6347 N N   . GLN D 1 129 ? 16.237  30.311  41.853 1.00 47.77  ? 128 GLN D N   1 
ATOM   6348 C CA  . GLN D 1 129 ? 15.482  30.494  40.627 1.00 48.12  ? 128 GLN D CA  1 
ATOM   6349 C C   . GLN D 1 129 ? 16.393  30.611  39.403 1.00 46.00  ? 128 GLN D C   1 
ATOM   6350 O O   . GLN D 1 129 ? 16.185  29.938  38.392 1.00 32.07  ? 128 GLN D O   1 
ATOM   6351 C CB  . GLN D 1 129 ? 14.592  31.738  40.718 1.00 34.79  ? 128 GLN D CB  1 
ATOM   6352 C CG  . GLN D 1 129 ? 13.483  31.602  41.741 1.00 24.12  ? 128 GLN D CG  1 
ATOM   6353 C CD  . GLN D 1 129 ? 12.199  32.300  41.344 1.00 33.54  ? 128 GLN D CD  1 
ATOM   6354 O OE1 . GLN D 1 129 ? 11.181  32.196  42.039 1.00 36.74  ? 128 GLN D OE1 1 
ATOM   6355 N NE2 . GLN D 1 129 ? 12.250  33.012  40.229 1.00 51.96  ? 128 GLN D NE2 1 
ATOM   6356 N N   . GLY D 1 130 ? 17.400  31.465  39.525 1.00 36.54  ? 129 GLY D N   1 
ATOM   6357 C CA  . GLY D 1 130 ? 18.393  31.667  38.484 1.00 35.27  ? 129 GLY D CA  1 
ATOM   6358 C C   . GLY D 1 130 ? 19.108  30.363  38.172 1.00 35.54  ? 129 GLY D C   1 
ATOM   6359 O O   . GLY D 1 130 ? 19.231  29.960  37.016 1.00 50.84  ? 129 GLY D O   1 
ATOM   6360 N N   . GLN D 1 131 ? 19.567  29.721  39.239 1.00 28.19  ? 130 GLN D N   1 
ATOM   6361 C CA  . GLN D 1 131 ? 20.188  28.409  39.115 1.00 36.46  ? 130 GLN D CA  1 
ATOM   6362 C C   . GLN D 1 131 ? 19.258  27.493  38.323 1.00 27.81  ? 130 GLN D C   1 
ATOM   6363 O O   . GLN D 1 131 ? 19.662  26.979  37.293 1.00 26.88  ? 130 GLN D O   1 
ATOM   6364 C CB  . GLN D 1 131 ? 20.468  27.810  40.492 1.00 50.31  ? 130 GLN D CB  1 
ATOM   6365 C CG  . GLN D 1 131 ? 21.785  28.244  41.104 1.00 57.83  ? 130 GLN D CG  1 
ATOM   6366 C CD  . GLN D 1 131 ? 21.870  28.125  42.612 1.00 57.51  ? 130 GLN D CD  1 
ATOM   6367 O OE1 . GLN D 1 131 ? 20.899  28.062  43.362 1.00 53.95  ? 130 GLN D OE1 1 
ATOM   6368 N NE2 . GLN D 1 131 ? 23.116  28.091  43.087 1.00 43.11  ? 130 GLN D NE2 1 
ATOM   6369 N N   . ALA D 1 132 ? 18.044  27.351  38.843 1.00 26.12  ? 131 ALA D N   1 
ATOM   6370 C CA  . ALA D 1 132 ? 17.000  26.526  38.261 1.00 28.32  ? 131 ALA D CA  1 
ATOM   6371 C C   . ALA D 1 132 ? 16.926  26.810  36.755 1.00 28.95  ? 131 ALA D C   1 
ATOM   6372 O O   . ALA D 1 132 ? 16.995  25.884  35.952 1.00 34.43  ? 131 ALA D O   1 
ATOM   6373 C CB  . ALA D 1 132 ? 15.665  26.772  38.929 1.00 21.41  ? 131 ALA D CB  1 
ATOM   6374 N N   . MET D 1 133 ? 16.811  28.087  36.467 1.00 26.45  ? 132 MET D N   1 
ATOM   6375 C CA  . MET D 1 133 ? 16.822  28.704  35.162 1.00 28.20  ? 132 MET D CA  1 
ATOM   6376 C C   . MET D 1 133 ? 17.973  28.239  34.289 1.00 31.91  ? 132 MET D C   1 
ATOM   6377 O O   . MET D 1 133 ? 17.822  27.866  33.121 1.00 57.29  ? 132 MET D O   1 
ATOM   6378 C CB  . MET D 1 133 ? 16.922  30.228  35.304 1.00 30.77  ? 132 MET D CB  1 
ATOM   6379 C CG  . MET D 1 133 ? 17.040  30.912  33.954 1.00 41.85  ? 132 MET D CG  1 
ATOM   6380 S SD  . MET D 1 133 ? 15.575  30.750  32.911 1.00 123.33 ? 132 MET D SD  1 
ATOM   6381 C CE  . MET D 1 133 ? 16.316  30.994  31.275 1.00 157.91 ? 132 MET D CE  1 
ATOM   6382 N N   . VAL D 1 134 ? 19.185  28.253  34.835 1.00 27.37  ? 133 VAL D N   1 
ATOM   6383 C CA  . VAL D 1 134 ? 20.299  27.838  33.976 1.00 23.22  ? 133 VAL D CA  1 
ATOM   6384 C C   . VAL D 1 134 ? 20.425  26.332  33.837 1.00 23.74  ? 133 VAL D C   1 
ATOM   6385 O O   . VAL D 1 134 ? 20.792  25.805  32.777 1.00 32.65  ? 133 VAL D O   1 
ATOM   6386 C CB  . VAL D 1 134 ? 21.593  28.430  34.560 1.00 30.26  ? 133 VAL D CB  1 
ATOM   6387 C CG1 . VAL D 1 134 ? 22.828  27.800  33.945 1.00 30.98  ? 133 VAL D CG1 1 
ATOM   6388 C CG2 . VAL D 1 134 ? 21.557  29.939  34.353 1.00 37.96  ? 133 VAL D CG2 1 
ATOM   6389 N N   . VAL D 1 135 ? 20.128  25.591  34.899 1.00 20.54  ? 134 VAL D N   1 
ATOM   6390 C CA  . VAL D 1 135 ? 20.125  24.124  34.811 1.00 21.58  ? 134 VAL D CA  1 
ATOM   6391 C C   . VAL D 1 135 ? 19.170  23.694  33.700 1.00 25.07  ? 134 VAL D C   1 
ATOM   6392 O O   . VAL D 1 135 ? 19.510  22.915  32.819 1.00 38.61  ? 134 VAL D O   1 
ATOM   6393 C CB  . VAL D 1 135 ? 19.725  23.469  36.142 1.00 23.81  ? 134 VAL D CB  1 
ATOM   6394 C CG1 . VAL D 1 135 ? 19.319  22.006  35.968 1.00 18.54  ? 134 VAL D CG1 1 
ATOM   6395 C CG2 . VAL D 1 135 ? 20.860  23.552  37.156 1.00 27.10  ? 134 VAL D CG2 1 
ATOM   6396 N N   . GLU D 1 136 ? 17.943  24.222  33.732 1.00 30.40  ? 135 GLU D N   1 
ATOM   6397 C CA  . GLU D 1 136 ? 16.924  23.878  32.749 1.00 28.84  ? 135 GLU D CA  1 
ATOM   6398 C C   . GLU D 1 136 ? 17.357  24.263  31.338 1.00 27.47  ? 135 GLU D C   1 
ATOM   6399 O O   . GLU D 1 136 ? 17.052  23.504  30.415 1.00 37.90  ? 135 GLU D O   1 
ATOM   6400 C CB  . GLU D 1 136 ? 15.578  24.523  33.082 1.00 33.18  ? 135 GLU D CB  1 
ATOM   6401 C CG  . GLU D 1 136 ? 14.826  23.829  34.209 1.00 39.11  ? 135 GLU D CG  1 
ATOM   6402 C CD  . GLU D 1 136 ? 14.187  22.520  33.793 1.00 39.93  ? 135 GLU D CD  1 
ATOM   6403 O OE1 . GLU D 1 136 ? 13.933  22.283  32.594 1.00 34.58  ? 135 GLU D OE1 1 
ATOM   6404 O OE2 . GLU D 1 136 ? 13.930  21.706  34.703 1.00 29.93  ? 135 GLU D OE2 1 
ATOM   6405 N N   . LEU D 1 137 ? 18.047  25.386  31.177 1.00 33.00  ? 136 LEU D N   1 
ATOM   6406 C CA  . LEU D 1 137 ? 18.563  25.770  29.856 1.00 28.85  ? 136 LEU D CA  1 
ATOM   6407 C C   . LEU D 1 137 ? 19.409  24.625  29.311 1.00 25.88  ? 136 LEU D C   1 
ATOM   6408 O O   . LEU D 1 137 ? 19.228  24.159  28.188 1.00 27.31  ? 136 LEU D O   1 
ATOM   6409 C CB  . LEU D 1 137 ? 19.373  27.053  29.932 1.00 30.87  ? 136 LEU D CB  1 
ATOM   6410 C CG  . LEU D 1 137 ? 19.637  27.917  28.708 1.00 28.04  ? 136 LEU D CG  1 
ATOM   6411 C CD1 . LEU D 1 137 ? 20.199  29.284  29.110 1.00 17.55  ? 136 LEU D CD1 1 
ATOM   6412 C CD2 . LEU D 1 137 ? 20.604  27.257  27.737 1.00 36.96  ? 136 LEU D CD2 1 
ATOM   6413 N N   . ILE D 1 138 ? 20.345  24.182  30.140 1.00 22.94  ? 137 ILE D N   1 
ATOM   6414 C CA  . ILE D 1 138 ? 21.268  23.130  29.764 1.00 20.06  ? 137 ILE D CA  1 
ATOM   6415 C C   . ILE D 1 138 ? 20.621  21.770  29.576 1.00 23.59  ? 137 ILE D C   1 
ATOM   6416 O O   . ILE D 1 138 ? 20.988  20.983  28.691 1.00 23.65  ? 137 ILE D O   1 
ATOM   6417 C CB  . ILE D 1 138 ? 22.365  23.012  30.854 1.00 27.46  ? 137 ILE D CB  1 
ATOM   6418 C CG1 . ILE D 1 138 ? 23.120  24.309  31.143 1.00 34.64  ? 137 ILE D CG1 1 
ATOM   6419 C CG2 . ILE D 1 138 ? 23.308  21.887  30.476 1.00 15.87  ? 137 ILE D CG2 1 
ATOM   6420 C CD1 . ILE D 1 138 ? 24.153  24.204  32.258 1.00 24.44  ? 137 ILE D CD1 1 
ATOM   6421 N N   . LEU D 1 139 ? 19.638  21.422  30.406 1.00 23.77  ? 138 LEU D N   1 
ATOM   6422 C CA  . LEU D 1 139 ? 18.976  20.136  30.259 1.00 20.58  ? 138 LEU D CA  1 
ATOM   6423 C C   . LEU D 1 139 ? 18.296  20.004  28.893 1.00 30.73  ? 138 LEU D C   1 
ATOM   6424 O O   . LEU D 1 139 ? 18.235  18.925  28.306 1.00 29.64  ? 138 LEU D O   1 
ATOM   6425 C CB  . LEU D 1 139 ? 17.856  19.949  31.283 1.00 24.67  ? 138 LEU D CB  1 
ATOM   6426 C CG  . LEU D 1 139 ? 18.155  19.919  32.769 1.00 34.33  ? 138 LEU D CG  1 
ATOM   6427 C CD1 . LEU D 1 139 ? 16.887  19.481  33.499 1.00 40.74  ? 138 LEU D CD1 1 
ATOM   6428 C CD2 . LEU D 1 139 ? 19.337  19.018  33.113 1.00 17.98  ? 138 LEU D CD2 1 
ATOM   6429 N N   . THR D 1 140 ? 17.741  21.136  28.473 1.00 28.06  ? 139 THR D N   1 
ATOM   6430 C CA  . THR D 1 140 ? 16.904  21.205  27.276 1.00 35.20  ? 139 THR D CA  1 
ATOM   6431 C C   . THR D 1 140 ? 17.792  21.388  26.055 1.00 30.84  ? 139 THR D C   1 
ATOM   6432 O O   . THR D 1 140 ? 17.573  20.756  25.023 1.00 49.04  ? 139 THR D O   1 
ATOM   6433 C CB  . THR D 1 140 ? 15.853  22.311  27.446 1.00 34.10  ? 139 THR D CB  1 
ATOM   6434 O OG1 . THR D 1 140 ? 15.242  22.106  28.732 1.00 18.26  ? 139 THR D OG1 1 
ATOM   6435 C CG2 . THR D 1 140 ? 14.715  22.217  26.450 1.00 24.31  ? 139 THR D CG2 1 
ATOM   6436 N N   . PHE D 1 141 ? 18.816  22.217  26.170 1.00 29.13  ? 140 PHE D N   1 
ATOM   6437 C CA  . PHE D 1 141 ? 19.814  22.357  25.125 1.00 26.96  ? 140 PHE D CA  1 
ATOM   6438 C C   . PHE D 1 141 ? 20.336  21.006  24.645 1.00 22.56  ? 140 PHE D C   1 
ATOM   6439 O O   . PHE D 1 141 ? 20.408  20.771  23.437 1.00 17.86  ? 140 PHE D O   1 
ATOM   6440 C CB  . PHE D 1 141 ? 21.003  23.204  25.606 1.00 21.02  ? 140 PHE D CB  1 
ATOM   6441 C CG  . PHE D 1 141 ? 22.009  23.485  24.496 1.00 28.04  ? 140 PHE D CG  1 
ATOM   6442 C CD1 . PHE D 1 141 ? 21.810  24.563  23.642 1.00 29.42  ? 140 PHE D CD1 1 
ATOM   6443 C CD2 . PHE D 1 141 ? 23.133  22.708  24.300 1.00 33.17  ? 140 PHE D CD2 1 
ATOM   6444 C CE1 . PHE D 1 141 ? 22.705  24.855  22.629 1.00 21.03  ? 140 PHE D CE1 1 
ATOM   6445 C CE2 . PHE D 1 141 ? 24.038  22.980  23.282 1.00 28.40  ? 140 PHE D CE2 1 
ATOM   6446 C CZ  . PHE D 1 141 ? 23.817  24.060  22.448 1.00 19.20  ? 140 PHE D CZ  1 
ATOM   6447 N N   . GLN D 1 142 ? 20.735  20.121  25.556 1.00 25.85  ? 141 GLN D N   1 
ATOM   6448 C CA  . GLN D 1 142 ? 21.349  18.876  25.069 1.00 25.65  ? 141 GLN D CA  1 
ATOM   6449 C C   . GLN D 1 142 ? 20.277  18.017  24.412 1.00 22.98  ? 141 GLN D C   1 
ATOM   6450 O O   . GLN D 1 142 ? 20.485  17.273  23.457 1.00 24.16  ? 141 GLN D O   1 
ATOM   6451 C CB  . GLN D 1 142 ? 22.094  18.157  26.185 1.00 13.66  ? 141 GLN D CB  1 
ATOM   6452 C CG  . GLN D 1 142 ? 21.273  17.689  27.373 1.00 22.57  ? 141 GLN D CG  1 
ATOM   6453 C CD  . GLN D 1 142 ? 20.616  16.331  27.218 1.00 30.46  ? 141 GLN D CD  1 
ATOM   6454 O OE1 . GLN D 1 142 ? 21.119  15.415  26.567 1.00 27.29  ? 141 GLN D OE1 1 
ATOM   6455 N NE2 . GLN D 1 142 ? 19.430  16.161  27.800 1.00 25.74  ? 141 GLN D NE2 1 
ATOM   6456 N N   . LEU D 1 143 ? 19.048  18.103  24.933 1.00 22.08  ? 142 LEU D N   1 
ATOM   6457 C CA  . LEU D 1 143 ? 17.995  17.282  24.333 1.00 21.25  ? 142 LEU D CA  1 
ATOM   6458 C C   . LEU D 1 143 ? 17.738  17.753  22.910 1.00 25.77  ? 142 LEU D C   1 
ATOM   6459 O O   . LEU D 1 143 ? 17.695  16.937  21.980 1.00 33.86  ? 142 LEU D O   1 
ATOM   6460 C CB  . LEU D 1 143 ? 16.741  17.326  25.206 1.00 14.52  ? 142 LEU D CB  1 
ATOM   6461 C CG  . LEU D 1 143 ? 15.412  16.931  24.568 1.00 20.10  ? 142 LEU D CG  1 
ATOM   6462 C CD1 . LEU D 1 143 ? 15.424  15.452  24.185 1.00 30.02  ? 142 LEU D CD1 1 
ATOM   6463 C CD2 . LEU D 1 143 ? 14.207  17.217  25.464 1.00 12.38  ? 142 LEU D CD2 1 
ATOM   6464 N N   . ALA D 1 144 ? 17.555  19.060  22.714 1.00 20.23  ? 143 ALA D N   1 
ATOM   6465 C CA  . ALA D 1 144 ? 17.209  19.559  21.372 1.00 25.98  ? 143 ALA D CA  1 
ATOM   6466 C C   . ALA D 1 144 ? 18.240  19.170  20.315 1.00 22.57  ? 143 ALA D C   1 
ATOM   6467 O O   . ALA D 1 144 ? 17.951  18.656  19.233 1.00 17.35  ? 143 ALA D O   1 
ATOM   6468 C CB  . ALA D 1 144 ? 17.029  21.070  21.438 1.00 16.59  ? 143 ALA D CB  1 
ATOM   6469 N N   . LEU D 1 145 ? 19.499  19.423  20.652 1.00 21.57  ? 144 LEU D N   1 
ATOM   6470 C CA  . LEU D 1 145 ? 20.655  19.067  19.853 1.00 19.74  ? 144 LEU D CA  1 
ATOM   6471 C C   . LEU D 1 145 ? 20.586  17.613  19.409 1.00 26.59  ? 144 LEU D C   1 
ATOM   6472 O O   . LEU D 1 145 ? 20.612  17.308  18.219 1.00 34.65  ? 144 LEU D O   1 
ATOM   6473 C CB  . LEU D 1 145 ? 21.901  19.354  20.687 1.00 25.61  ? 144 LEU D CB  1 
ATOM   6474 C CG  . LEU D 1 145 ? 23.061  20.092  20.023 1.00 29.50  ? 144 LEU D CG  1 
ATOM   6475 C CD1 . LEU D 1 145 ? 22.585  21.280  19.194 1.00 14.85  ? 144 LEU D CD1 1 
ATOM   6476 C CD2 . LEU D 1 145 ? 24.071  20.541  21.061 1.00 25.23  ? 144 LEU D CD2 1 
ATOM   6477 N N   . CYS D 1 146 ? 20.476  16.697  20.368 1.00 21.52  ? 145 CYS D N   1 
ATOM   6478 C CA  . CYS D 1 146 ? 20.277  15.286  20.086 1.00 25.78  ? 145 CYS D CA  1 
ATOM   6479 C C   . CYS D 1 146 ? 19.087  15.123  19.146 1.00 35.85  ? 145 CYS D C   1 
ATOM   6480 O O   . CYS D 1 146 ? 19.122  14.305  18.224 1.00 38.93  ? 145 CYS D O   1 
ATOM   6481 C CB  . CYS D 1 146 ? 20.041  14.459  21.355 1.00 28.06  ? 145 CYS D CB  1 
ATOM   6482 S SG  . CYS D 1 146 ? 19.806  12.678  21.085 1.00 25.59  ? 145 CYS D SG  1 
ATOM   6483 N N   . ILE D 1 147 ? 18.048  15.928  19.402 1.00 30.83  ? 146 ILE D N   1 
ATOM   6484 C CA  . ILE D 1 147 ? 16.855  15.765  18.579 1.00 25.32  ? 146 ILE D CA  1 
ATOM   6485 C C   . ILE D 1 147 ? 17.126  16.161  17.127 1.00 27.60  ? 146 ILE D C   1 
ATOM   6486 O O   . ILE D 1 147 ? 16.740  15.434  16.208 1.00 27.67  ? 146 ILE D O   1 
ATOM   6487 C CB  . ILE D 1 147 ? 15.663  16.572  19.114 1.00 31.38  ? 146 ILE D CB  1 
ATOM   6488 C CG1 . ILE D 1 147 ? 14.995  15.965  20.348 1.00 26.36  ? 146 ILE D CG1 1 
ATOM   6489 C CG2 . ILE D 1 147 ? 14.637  16.772  18.008 1.00 22.54  ? 146 ILE D CG2 1 
ATOM   6490 C CD1 . ILE D 1 147 ? 13.813  16.766  20.845 1.00 36.95  ? 146 ILE D CD1 1 
ATOM   6491 N N   . PHE D 1 148 ? 17.769  17.302  16.940 1.00 22.03  ? 147 PHE D N   1 
ATOM   6492 C CA  . PHE D 1 148 ? 17.927  17.861  15.586 1.00 18.72  ? 147 PHE D CA  1 
ATOM   6493 C C   . PHE D 1 148 ? 18.855  16.940  14.830 1.00 24.27  ? 147 PHE D C   1 
ATOM   6494 O O   . PHE D 1 148 ? 18.694  16.630  13.656 1.00 19.29  ? 147 PHE D O   1 
ATOM   6495 C CB  . PHE D 1 148 ? 18.451  19.292  15.655 1.00 18.08  ? 147 PHE D CB  1 
ATOM   6496 C CG  . PHE D 1 148 ? 17.553  20.191  16.491 1.00 15.07  ? 147 PHE D CG  1 
ATOM   6497 C CD1 . PHE D 1 148 ? 16.174  20.020  16.445 1.00 20.88  ? 147 PHE D CD1 1 
ATOM   6498 C CD2 . PHE D 1 148 ? 18.053  21.176  17.320 1.00 24.31  ? 147 PHE D CD2 1 
ATOM   6499 C CE1 . PHE D 1 148 ? 15.311  20.811  17.196 1.00 23.52  ? 147 PHE D CE1 1 
ATOM   6500 C CE2 . PHE D 1 148 ? 17.197  21.981  18.056 1.00 25.29  ? 147 PHE D CE2 1 
ATOM   6501 C CZ  . PHE D 1 148 ? 15.825  21.804  18.004 1.00 18.34  ? 147 PHE D CZ  1 
ATOM   6502 N N   . ALA D 1 149 ? 19.850  16.466  15.601 1.00 27.37  ? 148 ALA D N   1 
ATOM   6503 C CA  . ALA D 1 149 ? 20.827  15.593  14.953 1.00 25.69  ? 148 ALA D CA  1 
ATOM   6504 C C   . ALA D 1 149 ? 20.203  14.252  14.591 1.00 37.48  ? 148 ALA D C   1 
ATOM   6505 O O   . ALA D 1 149 ? 20.489  13.645  13.548 1.00 28.81  ? 148 ALA D O   1 
ATOM   6506 C CB  . ALA D 1 149 ? 22.049  15.490  15.854 1.00 16.15  ? 148 ALA D CB  1 
ATOM   6507 N N   . SER D 1 150 ? 19.306  13.739  15.435 1.00 36.50  ? 149 SER D N   1 
ATOM   6508 C CA  . SER D 1 150 ? 18.762  12.404  15.213 1.00 22.84  ? 149 SER D CA  1 
ATOM   6509 C C   . SER D 1 150 ? 17.709  12.365  14.124 1.00 26.58  ? 149 SER D C   1 
ATOM   6510 O O   . SER D 1 150 ? 17.381  11.269  13.676 1.00 30.30  ? 149 SER D O   1 
ATOM   6511 C CB  . SER D 1 150 ? 18.144  11.892  16.519 1.00 19.84  ? 149 SER D CB  1 
ATOM   6512 O OG  . SER D 1 150 ? 19.175  11.321  17.306 1.00 18.04  ? 149 SER D OG  1 
ATOM   6513 N N   . THR D 1 151 ? 17.169  13.516  13.722 1.00 22.03  ? 150 THR D N   1 
ATOM   6514 C CA  . THR D 1 151 ? 16.128  13.495  12.691 1.00 25.86  ? 150 THR D CA  1 
ATOM   6515 C C   . THR D 1 151 ? 16.528  14.241  11.424 1.00 21.66  ? 150 THR D C   1 
ATOM   6516 O O   . THR D 1 151 ? 15.749  14.394  10.473 1.00 31.34  ? 150 THR D O   1 
ATOM   6517 C CB  . THR D 1 151 ? 14.832  14.080  13.284 1.00 24.97  ? 150 THR D CB  1 
ATOM   6518 O OG1 . THR D 1 151 ? 15.136  15.312  13.955 1.00 23.42  ? 150 THR D OG1 1 
ATOM   6519 C CG2 . THR D 1 151 ? 14.242  13.149  14.329 1.00 23.44  ? 150 THR D CG2 1 
ATOM   6520 N N   . ASP D 1 152 ? 17.761  14.733  11.343 1.00 33.25  ? 151 ASP D N   1 
ATOM   6521 C CA  . ASP D 1 152 ? 18.198  15.453  10.140 1.00 28.90  ? 151 ASP D CA  1 
ATOM   6522 C C   . ASP D 1 152 ? 18.206  14.501  8.949  1.00 33.78  ? 151 ASP D C   1 
ATOM   6523 O O   . ASP D 1 152 ? 18.949  13.511  8.914  1.00 24.81  ? 151 ASP D O   1 
ATOM   6524 C CB  . ASP D 1 152 ? 19.570  16.071  10.363 1.00 25.28  ? 151 ASP D CB  1 
ATOM   6525 C CG  . ASP D 1 152 ? 20.018  17.106  9.349  1.00 31.08  ? 151 ASP D CG  1 
ATOM   6526 O OD1 . ASP D 1 152 ? 19.601  17.036  8.172  1.00 33.17  ? 151 ASP D OD1 1 
ATOM   6527 O OD2 . ASP D 1 152 ? 20.814  18.007  9.709  1.00 26.10  ? 151 ASP D OD2 1 
ATOM   6528 N N   . SER D 1 153 ? 17.372  14.798  7.943  1.00 21.96  ? 152 SER D N   1 
ATOM   6529 C CA  . SER D 1 153 ? 17.369  13.981  6.739  1.00 24.89  ? 152 SER D CA  1 
ATOM   6530 C C   . SER D 1 153 ? 18.723  13.928  6.051  1.00 25.62  ? 152 SER D C   1 
ATOM   6531 O O   . SER D 1 153 ? 18.946  13.038  5.228  1.00 43.27  ? 152 SER D O   1 
ATOM   6532 C CB  . SER D 1 153 ? 16.342  14.526  5.722  1.00 31.66  ? 152 SER D CB  1 
ATOM   6533 O OG  . SER D 1 153 ? 15.102  14.647  6.420  1.00 86.74  ? 152 SER D OG  1 
ATOM   6534 N N   . ARG D 1 154 ? 19.638  14.850  6.347  1.00 22.91  ? 153 ARG D N   1 
ATOM   6535 C CA  . ARG D 1 154 ? 20.913  14.829  5.643  1.00 21.99  ? 153 ARG D CA  1 
ATOM   6536 C C   . ARG D 1 154 ? 21.951  13.988  6.366  1.00 32.06  ? 153 ARG D C   1 
ATOM   6537 O O   . ARG D 1 154 ? 23.049  13.786  5.852  1.00 41.50  ? 153 ARG D O   1 
ATOM   6538 C CB  . ARG D 1 154 ? 21.479  16.244  5.480  1.00 31.39  ? 153 ARG D CB  1 
ATOM   6539 C CG  . ARG D 1 154 ? 20.526  17.251  4.875  1.00 35.83  ? 153 ARG D CG  1 
ATOM   6540 C CD  . ARG D 1 154 ? 21.001  18.671  5.117  1.00 38.21  ? 153 ARG D CD  1 
ATOM   6541 N NE  . ARG D 1 154 ? 20.901  19.063  6.514  1.00 42.40  ? 153 ARG D NE  1 
ATOM   6542 C CZ  . ARG D 1 154 ? 21.077  20.295  6.981  1.00 51.81  ? 153 ARG D CZ  1 
ATOM   6543 N NH1 . ARG D 1 154 ? 21.361  21.291  6.148  1.00 25.34  ? 153 ARG D NH1 1 
ATOM   6544 N NH2 . ARG D 1 154 ? 20.968  20.535  8.286  1.00 52.58  ? 153 ARG D NH2 1 
ATOM   6545 N N   . ARG D 1 155 ? 21.637  13.507  7.564  1.00 40.18  ? 154 ARG D N   1 
ATOM   6546 C CA  . ARG D 1 155 ? 22.680  12.869  8.366  1.00 33.87  ? 154 ARG D CA  1 
ATOM   6547 C C   . ARG D 1 155 ? 23.303  11.673  7.664  1.00 28.68  ? 154 ARG D C   1 
ATOM   6548 O O   . ARG D 1 155 ? 22.581  10.872  7.072  1.00 29.72  ? 154 ARG D O   1 
ATOM   6549 C CB  . ARG D 1 155 ? 22.075  12.457  9.711  1.00 39.04  ? 154 ARG D CB  1 
ATOM   6550 C CG  . ARG D 1 155 ? 23.166  12.109  10.725 1.00 34.21  ? 154 ARG D CG  1 
ATOM   6551 C CD  . ARG D 1 155 ? 22.552  11.246  11.806 1.00 28.21  ? 154 ARG D CD  1 
ATOM   6552 N NE  . ARG D 1 155 ? 23.527  10.342  12.403 1.00 37.32  ? 154 ARG D NE  1 
ATOM   6553 C CZ  . ARG D 1 155 ? 23.986  10.538  13.642 1.00 34.05  ? 154 ARG D CZ  1 
ATOM   6554 N NH1 . ARG D 1 155 ? 23.534  11.586  14.327 1.00 23.33  ? 154 ARG D NH1 1 
ATOM   6555 N NH2 . ARG D 1 155 ? 24.867  9.681   14.135 1.00 23.00  ? 154 ARG D NH2 1 
ATOM   6556 N N   . THR D 1 156 ? 24.626  11.549  7.721  1.00 35.61  ? 155 THR D N   1 
ATOM   6557 C CA  . THR D 1 156 ? 25.295  10.528  6.910  1.00 40.90  ? 155 THR D CA  1 
ATOM   6558 C C   . THR D 1 156 ? 25.713  9.317   7.723  1.00 42.85  ? 155 THR D C   1 
ATOM   6559 O O   . THR D 1 156 ? 25.623  8.159   7.308  1.00 32.31  ? 155 THR D O   1 
ATOM   6560 C CB  . THR D 1 156 ? 26.509  11.162  6.191  1.00 44.30  ? 155 THR D CB  1 
ATOM   6561 O OG1 . THR D 1 156 ? 26.369  10.894  4.786  1.00 56.72  ? 155 THR D OG1 1 
ATOM   6562 C CG2 . THR D 1 156 ? 27.831  10.563  6.639  1.00 47.32  ? 155 THR D CG2 1 
ATOM   6563 N N   . SER D 1 157 ? 26.177  9.578   8.935  1.00 49.46  ? 156 SER D N   1 
ATOM   6564 C CA  . SER D 1 157 ? 26.498  8.522   9.877  1.00 51.83  ? 156 SER D CA  1 
ATOM   6565 C C   . SER D 1 157 ? 25.255  7.759   10.318 1.00 39.22  ? 156 SER D C   1 
ATOM   6566 O O   . SER D 1 157 ? 24.176  8.338   10.401 1.00 36.13  ? 156 SER D O   1 
ATOM   6567 C CB  . SER D 1 157 ? 27.148  9.133   11.125 1.00 65.41  ? 156 SER D CB  1 
ATOM   6568 O OG  . SER D 1 157 ? 26.251  10.115  11.667 1.00 79.36  ? 156 SER D OG  1 
ATOM   6569 N N   . PRO D 1 158 ? 25.435  6.476   10.605 1.00 35.72  ? 157 PRO D N   1 
ATOM   6570 C CA  . PRO D 1 158 ? 24.377  5.635   11.164 1.00 25.69  ? 157 PRO D CA  1 
ATOM   6571 C C   . PRO D 1 158 ? 23.713  6.334   12.346 1.00 22.76  ? 157 PRO D C   1 
ATOM   6572 O O   . PRO D 1 158 ? 24.404  6.728   13.280 1.00 26.18  ? 157 PRO D O   1 
ATOM   6573 C CB  . PRO D 1 158 ? 25.111  4.393   11.649 1.00 29.05  ? 157 PRO D CB  1 
ATOM   6574 C CG  . PRO D 1 158 ? 26.369  4.337   10.851 1.00 38.13  ? 157 PRO D CG  1 
ATOM   6575 C CD  . PRO D 1 158 ? 26.689  5.731   10.393 1.00 40.80  ? 157 PRO D CD  1 
ATOM   6576 N N   . VAL D 1 159 ? 22.405  6.477   12.230 1.00 28.14  ? 158 VAL D N   1 
ATOM   6577 C CA  . VAL D 1 159 ? 21.567  7.200   13.153 1.00 29.58  ? 158 VAL D CA  1 
ATOM   6578 C C   . VAL D 1 159 ? 21.187  6.334   14.359 1.00 42.66  ? 158 VAL D C   1 
ATOM   6579 O O   . VAL D 1 159 ? 20.951  6.906   15.428 1.00 38.03  ? 158 VAL D O   1 
ATOM   6580 C CB  . VAL D 1 159 ? 20.251  7.671   12.507 1.00 23.37  ? 158 VAL D CB  1 
ATOM   6581 C CG1 . VAL D 1 159 ? 19.485  6.470   11.986 1.00 12.00  ? 158 VAL D CG1 1 
ATOM   6582 C CG2 . VAL D 1 159 ? 19.445  8.464   13.513 1.00 25.68  ? 158 VAL D CG2 1 
ATOM   6583 N N   . GLY D 1 160 ? 21.144  5.029   14.126 1.00 39.22  ? 159 GLY D N   1 
ATOM   6584 C CA  . GLY D 1 160 ? 20.744  4.059   15.148 1.00 27.32  ? 159 GLY D CA  1 
ATOM   6585 C C   . GLY D 1 160 ? 19.243  4.100   15.340 1.00 20.23  ? 159 GLY D C   1 
ATOM   6586 O O   . GLY D 1 160 ? 18.440  3.929   14.425 1.00 25.22  ? 159 GLY D O   1 
ATOM   6587 N N   . SER D 1 161 ? 18.804  4.372   16.564 1.00 17.31  ? 160 SER D N   1 
ATOM   6588 C CA  . SER D 1 161 ? 17.366  4.543   16.767 1.00 19.14  ? 160 SER D CA  1 
ATOM   6589 C C   . SER D 1 161 ? 17.109  5.990   17.140 1.00 28.34  ? 160 SER D C   1 
ATOM   6590 O O   . SER D 1 161 ? 17.519  6.388   18.238 1.00 36.36  ? 160 SER D O   1 
ATOM   6591 C CB  . SER D 1 161 ? 16.901  3.595   17.869 1.00 15.18  ? 160 SER D CB  1 
ATOM   6592 O OG  . SER D 1 161 ? 15.609  3.967   18.307 1.00 15.04  ? 160 SER D OG  1 
ATOM   6593 N N   . PRO D 1 162 ? 16.519  6.835   16.309 1.00 27.67  ? 161 PRO D N   1 
ATOM   6594 C CA  . PRO D 1 162 ? 16.300  8.221   16.752 1.00 20.00  ? 161 PRO D CA  1 
ATOM   6595 C C   . PRO D 1 162 ? 15.451  8.260   18.025 1.00 19.06  ? 161 PRO D C   1 
ATOM   6596 O O   . PRO D 1 162 ? 15.767  8.983   18.967 1.00 22.85  ? 161 PRO D O   1 
ATOM   6597 C CB  . PRO D 1 162 ? 15.585  8.872   15.565 1.00 21.01  ? 161 PRO D CB  1 
ATOM   6598 C CG  . PRO D 1 162 ? 16.006  8.024   14.399 1.00 24.14  ? 161 PRO D CG  1 
ATOM   6599 C CD  . PRO D 1 162 ? 16.068  6.611   14.924 1.00 29.16  ? 161 PRO D CD  1 
ATOM   6600 N N   . ALA D 1 163 ? 14.391  7.472   18.062 1.00 23.02  ? 162 ALA D N   1 
ATOM   6601 C CA  . ALA D 1 163 ? 13.477  7.341   19.183 1.00 30.36  ? 162 ALA D CA  1 
ATOM   6602 C C   . ALA D 1 163 ? 14.176  7.038   20.506 1.00 24.01  ? 162 ALA D C   1 
ATOM   6603 O O   . ALA D 1 163 ? 13.966  7.761   21.477 1.00 24.94  ? 162 ALA D O   1 
ATOM   6604 C CB  . ALA D 1 163 ? 12.462  6.239   18.881 1.00 20.70  ? 162 ALA D CB  1 
ATOM   6605 N N   . LEU D 1 164 ? 14.993  5.991   20.575 1.00 18.79  ? 163 LEU D N   1 
ATOM   6606 C CA  . LEU D 1 164 ? 15.627  5.600   21.826 1.00 25.89  ? 163 LEU D CA  1 
ATOM   6607 C C   . LEU D 1 164 ? 16.765  6.542   22.180 1.00 35.06  ? 163 LEU D C   1 
ATOM   6608 O O   . LEU D 1 164 ? 16.970  6.810   23.376 1.00 23.79  ? 163 LEU D O   1 
ATOM   6609 C CB  . LEU D 1 164 ? 16.144  4.159   21.785 1.00 28.67  ? 163 LEU D CB  1 
ATOM   6610 C CG  . LEU D 1 164 ? 15.112  3.044   21.590 1.00 19.62  ? 163 LEU D CG  1 
ATOM   6611 C CD1 . LEU D 1 164 ? 15.756  1.682   21.356 1.00 12.48  ? 163 LEU D CD1 1 
ATOM   6612 C CD2 . LEU D 1 164 ? 14.182  3.026   22.797 1.00 19.89  ? 163 LEU D CD2 1 
ATOM   6613 N N   . SER D 1 165 ? 17.502  7.035   21.168 1.00 15.10  ? 164 SER D N   1 
ATOM   6614 C CA  . SER D 1 165 ? 18.547  7.987   21.565 1.00 16.29  ? 164 SER D CA  1 
ATOM   6615 C C   . SER D 1 165 ? 17.935  9.214   22.244 1.00 10.24  ? 164 SER D C   1 
ATOM   6616 O O   . SER D 1 165 ? 18.484  9.779   23.180 1.00 16.86  ? 164 SER D O   1 
ATOM   6617 C CB  . SER D 1 165 ? 19.382  8.418   20.364 1.00 22.31  ? 164 SER D CB  1 
ATOM   6618 O OG  . SER D 1 165 ? 20.468  7.567   20.054 1.00 14.36  ? 164 SER D OG  1 
ATOM   6619 N N   . ILE D 1 166 ? 16.801  9.654   21.716 1.00 17.54  ? 165 ILE D N   1 
ATOM   6620 C CA  . ILE D 1 166 ? 16.065  10.849  22.087 1.00 22.15  ? 165 ILE D CA  1 
ATOM   6621 C C   . ILE D 1 166 ? 15.412  10.621  23.448 1.00 32.45  ? 165 ILE D C   1 
ATOM   6622 O O   . ILE D 1 166 ? 15.563  11.404  24.396 1.00 22.16  ? 165 ILE D O   1 
ATOM   6623 C CB  . ILE D 1 166 ? 15.037  11.217  20.996 1.00 29.48  ? 165 ILE D CB  1 
ATOM   6624 C CG1 . ILE D 1 166 ? 15.631  11.811  19.709 1.00 32.17  ? 165 ILE D CG1 1 
ATOM   6625 C CG2 . ILE D 1 166 ? 13.954  12.144  21.552 1.00 14.65  ? 165 ILE D CG2 1 
ATOM   6626 C CD1 . ILE D 1 166 ? 14.642  12.039  18.571 1.00 19.93  ? 165 ILE D CD1 1 
ATOM   6627 N N   . GLY D 1 167 ? 14.677  9.508   23.570 1.00 16.29  ? 166 GLY D N   1 
ATOM   6628 C CA  . GLY D 1 167 ? 14.148  9.208   24.904 1.00 34.34  ? 166 GLY D CA  1 
ATOM   6629 C C   . GLY D 1 167 ? 15.250  9.091   25.941 1.00 31.65  ? 166 GLY D C   1 
ATOM   6630 O O   . GLY D 1 167 ? 15.243  9.751   26.991 1.00 20.87  ? 166 GLY D O   1 
ATOM   6631 N N   . LEU D 1 168 ? 16.275  8.261   25.696 1.00 23.95  ? 167 LEU D N   1 
ATOM   6632 C CA  . LEU D 1 168 ? 17.350  8.145   26.692 1.00 18.10  ? 167 LEU D CA  1 
ATOM   6633 C C   . LEU D 1 168 ? 18.028  9.492   26.905 1.00 26.24  ? 167 LEU D C   1 
ATOM   6634 O O   . LEU D 1 168 ? 18.643  9.772   27.940 1.00 27.57  ? 167 LEU D O   1 
ATOM   6635 C CB  . LEU D 1 168 ? 18.389  7.100   26.308 1.00 17.27  ? 167 LEU D CB  1 
ATOM   6636 C CG  . LEU D 1 168 ? 17.929  5.640   26.346 1.00 15.91  ? 167 LEU D CG  1 
ATOM   6637 C CD1 . LEU D 1 168 ? 18.916  4.745   25.615 1.00 15.67  ? 167 LEU D CD1 1 
ATOM   6638 C CD2 . LEU D 1 168 ? 17.734  5.196   27.788 1.00 16.71  ? 167 LEU D CD2 1 
ATOM   6639 N N   . SER D 1 169 ? 17.941  10.387  25.912 1.00 23.58  ? 168 SER D N   1 
ATOM   6640 C CA  . SER D 1 169 ? 18.474  11.718  26.208 1.00 16.04  ? 168 SER D CA  1 
ATOM   6641 C C   . SER D 1 169 ? 17.595  12.347  27.276 1.00 24.78  ? 168 SER D C   1 
ATOM   6642 O O   . SER D 1 169 ? 18.017  13.036  28.199 1.00 14.24  ? 168 SER D O   1 
ATOM   6643 C CB  . SER D 1 169 ? 18.518  12.564  24.950 1.00 21.37  ? 168 SER D CB  1 
ATOM   6644 O OG  . SER D 1 169 ? 18.919  13.880  25.291 1.00 19.59  ? 168 SER D OG  1 
ATOM   6645 N N   . VAL D 1 170 ? 16.269  12.112  27.207 1.00 21.54  ? 169 VAL D N   1 
ATOM   6646 C CA  . VAL D 1 170 ? 15.548  12.772  28.298 1.00 27.71  ? 169 VAL D CA  1 
ATOM   6647 C C   . VAL D 1 170 ? 15.798  12.065  29.628 1.00 25.63  ? 169 VAL D C   1 
ATOM   6648 O O   . VAL D 1 170 ? 15.848  12.748  30.663 1.00 15.02  ? 169 VAL D O   1 
ATOM   6649 C CB  . VAL D 1 170 ? 14.050  12.928  28.001 1.00 33.09  ? 169 VAL D CB  1 
ATOM   6650 C CG1 . VAL D 1 170 ? 13.706  12.781  26.524 1.00 26.97  ? 169 VAL D CG1 1 
ATOM   6651 C CG2 . VAL D 1 170 ? 13.256  11.947  28.838 1.00 19.54  ? 169 VAL D CG2 1 
ATOM   6652 N N   . THR D 1 171 ? 15.987  10.744  29.706 1.00 19.26  ? 170 THR D N   1 
ATOM   6653 C CA  . THR D 1 171 ? 16.353  10.163  30.991 1.00 17.00  ? 170 THR D CA  1 
ATOM   6654 C C   . THR D 1 171 ? 17.645  10.790  31.531 1.00 25.27  ? 170 THR D C   1 
ATOM   6655 O O   . THR D 1 171 ? 17.732  11.043  32.732 1.00 30.27  ? 170 THR D O   1 
ATOM   6656 C CB  . THR D 1 171 ? 16.565  8.632   31.024 1.00 12.78  ? 170 THR D CB  1 
ATOM   6657 O OG1 . THR D 1 171 ? 17.861  8.323   30.516 1.00 64.19  ? 170 THR D OG1 1 
ATOM   6658 C CG2 . THR D 1 171 ? 15.542  7.932   30.178 1.00 4.82   ? 170 THR D CG2 1 
ATOM   6659 N N   . LEU D 1 172 ? 18.631  11.049  30.694 1.00 27.65  ? 171 LEU D N   1 
ATOM   6660 C CA  . LEU D 1 172 ? 19.852  11.715  31.128 1.00 23.84  ? 171 LEU D CA  1 
ATOM   6661 C C   . LEU D 1 172 ? 19.540  13.065  31.771 1.00 28.58  ? 171 LEU D C   1 
ATOM   6662 O O   . LEU D 1 172 ? 20.171  13.495  32.741 1.00 18.21  ? 171 LEU D O   1 
ATOM   6663 C CB  . LEU D 1 172 ? 20.810  11.902  29.944 1.00 17.66  ? 171 LEU D CB  1 
ATOM   6664 C CG  . LEU D 1 172 ? 22.063  12.733  30.222 1.00 25.25  ? 171 LEU D CG  1 
ATOM   6665 C CD1 . LEU D 1 172 ? 23.073  11.888  30.995 1.00 17.24  ? 171 LEU D CD1 1 
ATOM   6666 C CD2 . LEU D 1 172 ? 22.704  13.294  28.957 1.00 18.01  ? 171 LEU D CD2 1 
ATOM   6667 N N   . GLY D 1 173 ? 18.548  13.754  31.213 1.00 30.73  ? 172 GLY D N   1 
ATOM   6668 C CA  . GLY D 1 173 ? 18.165  15.074  31.704 1.00 25.32  ? 172 GLY D CA  1 
ATOM   6669 C C   . GLY D 1 173 ? 17.618  14.975  33.119 1.00 23.78  ? 172 GLY D C   1 
ATOM   6670 O O   . GLY D 1 173 ? 17.951  15.764  33.999 1.00 28.05  ? 172 GLY D O   1 
ATOM   6671 N N   . HIS D 1 174 ? 16.767  13.984  33.340 1.00 19.08  ? 173 HIS D N   1 
ATOM   6672 C CA  . HIS D 1 174 ? 16.232  13.744  34.669 1.00 25.26  ? 173 HIS D CA  1 
ATOM   6673 C C   . HIS D 1 174 ? 17.258  13.370  35.729 1.00 26.76  ? 173 HIS D C   1 
ATOM   6674 O O   . HIS D 1 174 ? 17.001  13.674  36.893 1.00 34.40  ? 173 HIS D O   1 
ATOM   6675 C CB  . HIS D 1 174 ? 15.197  12.600  34.603 1.00 19.25  ? 173 HIS D CB  1 
ATOM   6676 C CG  . HIS D 1 174 ? 13.939  13.133  33.999 1.00 21.16  ? 173 HIS D CG  1 
ATOM   6677 N ND1 . HIS D 1 174 ? 12.855  13.532  34.734 1.00 31.91  ? 173 HIS D ND1 1 
ATOM   6678 C CD2 . HIS D 1 174 ? 13.635  13.352  32.700 1.00 18.15  ? 173 HIS D CD2 1 
ATOM   6679 C CE1 . HIS D 1 174 ? 11.915  13.964  33.906 1.00 24.08  ? 173 HIS D CE1 1 
ATOM   6680 N NE2 . HIS D 1 174 ? 12.360  13.866  32.675 1.00 17.36  ? 173 HIS D NE2 1 
ATOM   6681 N N   . LEU D 1 175 ? 18.338  12.721  35.341 1.00 18.19  ? 174 LEU D N   1 
ATOM   6682 C CA  . LEU D 1 175 ? 19.352  12.175  36.232 1.00 26.65  ? 174 LEU D CA  1 
ATOM   6683 C C   . LEU D 1 175 ? 20.138  13.262  36.953 1.00 19.39  ? 174 LEU D C   1 
ATOM   6684 O O   . LEU D 1 175 ? 20.829  13.059  37.950 1.00 26.77  ? 174 LEU D O   1 
ATOM   6685 C CB  . LEU D 1 175 ? 20.300  11.292  35.415 1.00 31.78  ? 174 LEU D CB  1 
ATOM   6686 C CG  . LEU D 1 175 ? 20.065  9.784   35.469 1.00 31.05  ? 174 LEU D CG  1 
ATOM   6687 C CD1 . LEU D 1 175 ? 18.863  9.472   36.348 1.00 37.80  ? 174 LEU D CD1 1 
ATOM   6688 C CD2 . LEU D 1 175 ? 19.906  9.207   34.078 1.00 26.37  ? 174 LEU D CD2 1 
ATOM   6689 N N   . VAL D 1 176 ? 20.033  14.467  36.413 1.00 19.90  ? 175 VAL D N   1 
ATOM   6690 C CA  . VAL D 1 176 ? 20.530  15.687  37.035 1.00 33.36  ? 175 VAL D CA  1 
ATOM   6691 C C   . VAL D 1 176 ? 19.339  16.605  37.321 1.00 31.38  ? 175 VAL D C   1 
ATOM   6692 O O   . VAL D 1 176 ? 19.210  17.084  38.452 1.00 38.67  ? 175 VAL D O   1 
ATOM   6693 C CB  . VAL D 1 176 ? 21.622  16.340  36.174 1.00 34.57  ? 175 VAL D CB  1 
ATOM   6694 C CG1 . VAL D 1 176 ? 22.087  17.699  36.674 1.00 29.62  ? 175 VAL D CG1 1 
ATOM   6695 C CG2 . VAL D 1 176 ? 22.853  15.441  36.122 1.00 24.55  ? 175 VAL D CG2 1 
ATOM   6696 N N   . GLY D 1 177 ? 18.449  16.863  36.368 1.00 18.73  ? 176 GLY D N   1 
ATOM   6697 C CA  . GLY D 1 177 ? 17.374  17.822  36.521 1.00 13.42  ? 176 GLY D CA  1 
ATOM   6698 C C   . GLY D 1 177 ? 16.545  17.595  37.771 1.00 30.14  ? 176 GLY D C   1 
ATOM   6699 O O   . GLY D 1 177 ? 16.159  18.565  38.438 1.00 21.60  ? 176 GLY D O   1 
ATOM   6700 N N   . ILE D 1 178 ? 16.258  16.325  38.077 1.00 25.64  ? 177 ILE D N   1 
ATOM   6701 C CA  . ILE D 1 178 ? 15.372  16.012  39.203 1.00 31.19  ? 177 ILE D CA  1 
ATOM   6702 C C   . ILE D 1 178 ? 15.900  16.675  40.480 1.00 28.90  ? 177 ILE D C   1 
ATOM   6703 O O   . ILE D 1 178 ? 15.147  17.253  41.255 1.00 24.07  ? 177 ILE D O   1 
ATOM   6704 C CB  . ILE D 1 178 ? 15.162  14.506  39.438 1.00 27.44  ? 177 ILE D CB  1 
ATOM   6705 C CG1 . ILE D 1 178 ? 14.529  13.756  38.259 1.00 24.14  ? 177 ILE D CG1 1 
ATOM   6706 C CG2 . ILE D 1 178 ? 14.338  14.267  40.705 1.00 19.77  ? 177 ILE D CG2 1 
ATOM   6707 C CD1 . ILE D 1 178 ? 14.159  12.314  38.540 1.00 13.82  ? 177 ILE D CD1 1 
ATOM   6708 N N   . TYR D 1 179 ? 17.201  16.655  40.715 1.00 18.43  ? 178 TYR D N   1 
ATOM   6709 C CA  . TYR D 1 179 ? 17.731  17.259  41.927 1.00 20.20  ? 178 TYR D CA  1 
ATOM   6710 C C   . TYR D 1 179 ? 17.572  18.768  41.974 1.00 31.16  ? 178 TYR D C   1 
ATOM   6711 O O   . TYR D 1 179 ? 17.541  19.362  43.068 1.00 47.95  ? 178 TYR D O   1 
ATOM   6712 C CB  . TYR D 1 179 ? 19.197  16.837  42.004 1.00 14.68  ? 178 TYR D CB  1 
ATOM   6713 C CG  . TYR D 1 179 ? 19.410  15.383  42.362 1.00 25.89  ? 178 TYR D CG  1 
ATOM   6714 C CD1 . TYR D 1 179 ? 20.099  14.581  41.461 1.00 19.22  ? 178 TYR D CD1 1 
ATOM   6715 C CD2 . TYR D 1 179 ? 18.970  14.786  43.538 1.00 27.52  ? 178 TYR D CD2 1 
ATOM   6716 C CE1 . TYR D 1 179 ? 20.338  13.253  41.703 1.00 19.97  ? 178 TYR D CE1 1 
ATOM   6717 C CE2 . TYR D 1 179 ? 19.207  13.441  43.814 1.00 20.13  ? 178 TYR D CE2 1 
ATOM   6718 C CZ  . TYR D 1 179 ? 19.894  12.690  42.884 1.00 26.18  ? 178 TYR D CZ  1 
ATOM   6719 O OH  . TYR D 1 179 ? 20.172  11.357  43.068 1.00 18.31  ? 178 TYR D OH  1 
ATOM   6720 N N   . PHE D 1 180 ? 17.461  19.452  40.835 1.00 20.77  ? 179 PHE D N   1 
ATOM   6721 C CA  . PHE D 1 180 ? 17.305  20.910  40.874 1.00 23.29  ? 179 PHE D CA  1 
ATOM   6722 C C   . PHE D 1 180 ? 15.847  21.355  40.898 1.00 31.65  ? 179 PHE D C   1 
ATOM   6723 O O   . PHE D 1 180 ? 15.412  22.206  41.687 1.00 25.28  ? 179 PHE D O   1 
ATOM   6724 C CB  . PHE D 1 180 ? 18.037  21.536  39.668 1.00 27.77  ? 179 PHE D CB  1 
ATOM   6725 C CG  . PHE D 1 180 ? 19.559  21.498  39.755 1.00 35.61  ? 179 PHE D CG  1 
ATOM   6726 C CD1 . PHE D 1 180 ? 20.267  22.488  40.414 1.00 32.11  ? 179 PHE D CD1 1 
ATOM   6727 C CD2 . PHE D 1 180 ? 20.282  20.466  39.182 1.00 41.59  ? 179 PHE D CD2 1 
ATOM   6728 C CE1 . PHE D 1 180 ? 21.645  22.467  40.518 1.00 25.96  ? 179 PHE D CE1 1 
ATOM   6729 C CE2 . PHE D 1 180 ? 21.661  20.420  39.289 1.00 42.20  ? 179 PHE D CE2 1 
ATOM   6730 C CZ  . PHE D 1 180 ? 22.343  21.414  39.962 1.00 35.74  ? 179 PHE D CZ  1 
ATOM   6731 N N   . THR D 1 181 ? 15.021  20.800  40.014 1.00 39.33  ? 180 THR D N   1 
ATOM   6732 C CA  . THR D 1 181 ? 13.676  21.271  39.730 1.00 24.45  ? 180 THR D CA  1 
ATOM   6733 C C   . THR D 1 181 ? 12.594  20.214  39.662 1.00 19.47  ? 180 THR D C   1 
ATOM   6734 O O   . THR D 1 181 ? 11.419  20.529  39.431 1.00 31.05  ? 180 THR D O   1 
ATOM   6735 C CB  . THR D 1 181 ? 13.705  21.940  38.326 1.00 25.97  ? 180 THR D CB  1 
ATOM   6736 O OG1 . THR D 1 181 ? 14.222  20.972  37.407 1.00 35.57  ? 180 THR D OG1 1 
ATOM   6737 C CG2 . THR D 1 181 ? 14.651  23.117  38.335 1.00 22.03  ? 180 THR D CG2 1 
ATOM   6738 N N   . GLY D 1 182 ? 12.950  18.940  39.806 1.00 27.76  ? 181 GLY D N   1 
ATOM   6739 C CA  . GLY D 1 182 ? 12.008  17.860  39.502 1.00 18.20  ? 181 GLY D CA  1 
ATOM   6740 C C   . GLY D 1 182 ? 12.166  17.425  38.045 1.00 22.69  ? 181 GLY D C   1 
ATOM   6741 O O   . GLY D 1 182 ? 11.736  16.342  37.661 1.00 18.89  ? 181 GLY D O   1 
ATOM   6742 N N   . CYS D 1 183 ? 12.796  18.293  37.276 1.00 30.76  ? 182 CYS D N   1 
ATOM   6743 C CA  . CYS D 1 183 ? 13.106  18.195  35.866 1.00 35.75  ? 182 CYS D CA  1 
ATOM   6744 C C   . CYS D 1 183 ? 11.870  18.467  35.008 1.00 26.68  ? 182 CYS D C   1 
ATOM   6745 O O   . CYS D 1 183 ? 10.902  17.717  34.982 1.00 24.88  ? 182 CYS D O   1 
ATOM   6746 C CB  . CYS D 1 183 ? 13.708  16.836  35.485 1.00 42.81  ? 182 CYS D CB  1 
ATOM   6747 S SG  . CYS D 1 183 ? 14.396  16.854  33.804 1.00 29.37  ? 182 CYS D SG  1 
ATOM   6748 N N   . SER D 1 184 ? 11.908  19.599  34.315 1.00 33.60  ? 183 SER D N   1 
ATOM   6749 C CA  . SER D 1 184 ? 10.855  19.988  33.384 1.00 31.32  ? 183 SER D CA  1 
ATOM   6750 C C   . SER D 1 184 ? 11.335  19.692  31.964 1.00 31.59  ? 183 SER D C   1 
ATOM   6751 O O   . SER D 1 184 ? 10.896  18.703  31.373 1.00 21.15  ? 183 SER D O   1 
ATOM   6752 C CB  . SER D 1 184 ? 10.442  21.449  33.514 1.00 22.11  ? 183 SER D CB  1 
ATOM   6753 O OG  . SER D 1 184 ? 9.740   21.902  32.367 1.00 30.00  ? 183 SER D OG  1 
ATOM   6754 N N   . MET D 1 185 ? 12.208  20.517  31.395 1.00 23.98  ? 184 MET D N   1 
ATOM   6755 C CA  . MET D 1 185 ? 12.630  20.290  30.010 1.00 31.05  ? 184 MET D CA  1 
ATOM   6756 C C   . MET D 1 185 ? 11.477  20.423  29.017 1.00 32.30  ? 184 MET D C   1 
ATOM   6757 O O   . MET D 1 185 ? 11.612  20.046  27.847 1.00 30.61  ? 184 MET D O   1 
ATOM   6758 C CB  . MET D 1 185 ? 13.254  18.897  29.857 1.00 21.75  ? 184 MET D CB  1 
ATOM   6759 C CG  . MET D 1 185 ? 14.519  18.716  30.683 1.00 33.29  ? 184 MET D CG  1 
ATOM   6760 S SD  . MET D 1 185 ? 15.318  17.117  30.436 1.00 45.53  ? 184 MET D SD  1 
ATOM   6761 C CE  . MET D 1 185 ? 13.947  15.996  30.681 1.00 31.39  ? 184 MET D CE  1 
ATOM   6762 N N   . ASN D 1 186 ? 10.344  20.958  29.453 1.00 22.00  ? 185 ASN D N   1 
ATOM   6763 C CA  . ASN D 1 186 ? 9.066   20.841  28.784 1.00 20.51  ? 185 ASN D CA  1 
ATOM   6764 C C   . ASN D 1 186 ? 7.990   21.594  29.552 1.00 23.73  ? 185 ASN D C   1 
ATOM   6765 O O   . ASN D 1 186 ? 7.512   21.074  30.554 1.00 16.81  ? 185 ASN D O   1 
ATOM   6766 C CB  . ASN D 1 186 ? 8.709   19.355  28.676 1.00 17.48  ? 185 ASN D CB  1 
ATOM   6767 C CG  . ASN D 1 186 ? 7.514   19.062  27.804 1.00 24.17  ? 185 ASN D CG  1 
ATOM   6768 O OD1 . ASN D 1 186 ? 6.584   19.845  27.666 1.00 25.02  ? 185 ASN D OD1 1 
ATOM   6769 N ND2 . ASN D 1 186 ? 7.502   17.883  27.183 1.00 36.58  ? 185 ASN D ND2 1 
ATOM   6770 N N   . PRO D 1 187 ? 7.673   22.785  29.066 1.00 25.35  ? 186 PRO D N   1 
ATOM   6771 C CA  . PRO D 1 187 ? 6.564   23.624  29.519 1.00 22.28  ? 186 PRO D CA  1 
ATOM   6772 C C   . PRO D 1 187 ? 5.220   22.932  29.671 1.00 24.14  ? 186 PRO D C   1 
ATOM   6773 O O   . PRO D 1 187 ? 4.371   23.301  30.492 1.00 31.56  ? 186 PRO D O   1 
ATOM   6774 C CB  . PRO D 1 187 ? 6.467   24.640  28.353 1.00 22.54  ? 186 PRO D CB  1 
ATOM   6775 C CG  . PRO D 1 187 ? 7.902   24.824  27.962 1.00 21.37  ? 186 PRO D CG  1 
ATOM   6776 C CD  . PRO D 1 187 ? 8.469   23.432  27.998 1.00 23.43  ? 186 PRO D CD  1 
ATOM   6777 N N   . ALA D 1 188 ? 4.944   21.895  28.879 1.00 24.62  ? 187 ALA D N   1 
ATOM   6778 C CA  . ALA D 1 188 ? 3.632   21.265  28.982 1.00 24.73  ? 187 ALA D CA  1 
ATOM   6779 C C   . ALA D 1 188 ? 3.607   20.278  30.147 1.00 27.24  ? 187 ALA D C   1 
ATOM   6780 O O   . ALA D 1 188 ? 2.593   20.145  30.844 1.00 23.63  ? 187 ALA D O   1 
ATOM   6781 C CB  . ALA D 1 188 ? 3.281   20.615  27.649 1.00 17.90  ? 187 ALA D CB  1 
ATOM   6782 N N   . ARG D 1 189 ? 4.721   19.589  30.363 1.00 22.07  ? 188 ARG D N   1 
ATOM   6783 C CA  . ARG D 1 189 ? 4.896   18.673  31.491 1.00 25.95  ? 188 ARG D CA  1 
ATOM   6784 C C   . ARG D 1 189 ? 4.694   19.388  32.829 1.00 29.21  ? 188 ARG D C   1 
ATOM   6785 O O   . ARG D 1 189 ? 4.228   18.792  33.807 1.00 22.90  ? 188 ARG D O   1 
ATOM   6786 C CB  . ARG D 1 189 ? 6.297   18.045  31.479 1.00 23.66  ? 188 ARG D CB  1 
ATOM   6787 C CG  . ARG D 1 189 ? 6.617   17.154  32.669 1.00 32.67  ? 188 ARG D CG  1 
ATOM   6788 C CD  . ARG D 1 189 ? 7.506   17.824  33.703 1.00 30.50  ? 188 ARG D CD  1 
ATOM   6789 N NE  . ARG D 1 189 ? 7.577   17.117  34.968 1.00 32.72  ? 188 ARG D NE  1 
ATOM   6790 C CZ  . ARG D 1 189 ? 6.772   17.070  36.012 1.00 27.52  ? 188 ARG D CZ  1 
ATOM   6791 N NH1 . ARG D 1 189 ? 5.620   17.721  36.126 1.00 20.57  ? 188 ARG D NH1 1 
ATOM   6792 N NH2 . ARG D 1 189 ? 7.127   16.309  37.048 1.00 32.24  ? 188 ARG D NH2 1 
ATOM   6793 N N   . SER D 1 190 ? 5.087   20.660  32.819 1.00 24.34  ? 189 SER D N   1 
ATOM   6794 C CA  . SER D 1 190 ? 4.979   21.549  33.976 1.00 23.79  ? 189 SER D CA  1 
ATOM   6795 C C   . SER D 1 190 ? 3.571   22.109  34.122 1.00 23.89  ? 189 SER D C   1 
ATOM   6796 O O   . SER D 1 190 ? 2.936   22.052  35.178 1.00 33.38  ? 189 SER D O   1 
ATOM   6797 C CB  . SER D 1 190 ? 6.005   22.685  33.856 1.00 21.51  ? 189 SER D CB  1 
ATOM   6798 O OG  . SER D 1 190 ? 7.305   22.262  34.231 1.00 24.44  ? 189 SER D OG  1 
ATOM   6799 N N   . PHE D 1 191 ? 3.037   22.668  33.040 1.00 26.86  ? 190 PHE D N   1 
ATOM   6800 C CA  . PHE D 1 191 ? 1.712   23.239  33.004 1.00 25.90  ? 190 PHE D CA  1 
ATOM   6801 C C   . PHE D 1 191 ? 0.581   22.308  33.448 1.00 37.40  ? 190 PHE D C   1 
ATOM   6802 O O   . PHE D 1 191 ? -0.298  22.757  34.188 1.00 31.92  ? 190 PHE D O   1 
ATOM   6803 C CB  . PHE D 1 191 ? 1.364   23.675  31.567 1.00 33.17  ? 190 PHE D CB  1 
ATOM   6804 C CG  . PHE D 1 191 ? 0.318   24.787  31.621 1.00 28.17  ? 190 PHE D CG  1 
ATOM   6805 C CD1 . PHE D 1 191 ? 0.411   25.740  32.622 1.00 31.08  ? 190 PHE D CD1 1 
ATOM   6806 C CD2 . PHE D 1 191 ? -0.708  24.854  30.711 1.00 29.61  ? 190 PHE D CD2 1 
ATOM   6807 C CE1 . PHE D 1 191 ? -0.523  26.749  32.678 1.00 33.37  ? 190 PHE D CE1 1 
ATOM   6808 C CE2 . PHE D 1 191 ? -1.634  25.876  30.756 1.00 27.05  ? 190 PHE D CE2 1 
ATOM   6809 C CZ  . PHE D 1 191 ? -1.534  26.831  31.748 1.00 26.78  ? 190 PHE D CZ  1 
ATOM   6810 N N   . GLY D 1 192 ? 0.600   21.070  32.974 1.00 41.83  ? 191 GLY D N   1 
ATOM   6811 C CA  . GLY D 1 192 ? -0.365  20.022  33.181 1.00 43.63  ? 191 GLY D CA  1 
ATOM   6812 C C   . GLY D 1 192 ? -0.778  19.731  34.613 1.00 42.33  ? 191 GLY D C   1 
ATOM   6813 O O   . GLY D 1 192 ? -1.978  19.860  34.921 1.00 33.67  ? 191 GLY D O   1 
ATOM   6814 N N   . PRO D 1 193 ? 0.162   19.331  35.467 1.00 22.86  ? 192 PRO D N   1 
ATOM   6815 C CA  . PRO D 1 193 ? -0.110  19.077  36.880 1.00 29.78  ? 192 PRO D CA  1 
ATOM   6816 C C   . PRO D 1 193 ? -0.555  20.343  37.621 1.00 44.69  ? 192 PRO D C   1 
ATOM   6817 O O   . PRO D 1 193 ? -1.449  20.251  38.468 1.00 32.60  ? 192 PRO D O   1 
ATOM   6818 C CB  . PRO D 1 193 ? 1.243   18.617  37.430 1.00 31.23  ? 192 PRO D CB  1 
ATOM   6819 C CG  . PRO D 1 193 ? 2.278   19.083  36.454 1.00 18.62  ? 192 PRO D CG  1 
ATOM   6820 C CD  . PRO D 1 193 ? 1.572   19.059  35.136 1.00 24.42  ? 192 PRO D CD  1 
ATOM   6821 N N   . ALA D 1 194 ? 0.080   21.457  37.295 1.00 41.14  ? 193 ALA D N   1 
ATOM   6822 C CA  . ALA D 1 194 ? -0.126  22.791  37.833 1.00 33.97  ? 193 ALA D CA  1 
ATOM   6823 C C   . ALA D 1 194 ? -1.566  23.234  37.599 1.00 30.95  ? 193 ALA D C   1 
ATOM   6824 O O   . ALA D 1 194 ? -2.214  23.645  38.554 1.00 35.15  ? 193 ALA D O   1 
ATOM   6825 C CB  . ALA D 1 194 ? 0.847   23.791  37.230 1.00 24.22  ? 193 ALA D CB  1 
ATOM   6826 N N   . VAL D 1 195 ? -2.060  23.134  36.373 1.00 26.83  ? 194 VAL D N   1 
ATOM   6827 C CA  . VAL D 1 195 ? -3.492  23.052  36.088 1.00 35.72  ? 194 VAL D CA  1 
ATOM   6828 C C   . VAL D 1 195 ? -4.013  21.726  36.627 1.00 47.16  ? 194 VAL D C   1 
ATOM   6829 O O   . VAL D 1 195 ? -3.248  21.023  37.301 1.00 71.63  ? 194 VAL D O   1 
ATOM   6830 C CB  . VAL D 1 195 ? -3.761  23.192  34.586 1.00 33.50  ? 194 VAL D CB  1 
ATOM   6831 C CG1 . VAL D 1 195 ? -5.253  23.287  34.310 1.00 23.42  ? 194 VAL D CG1 1 
ATOM   6832 C CG2 . VAL D 1 195 ? -3.063  24.414  34.010 1.00 34.20  ? 194 VAL D CG2 1 
ATOM   6833 N N   . VAL D 1 196 ? -5.224  21.221  36.480 1.00 51.16  ? 195 VAL D N   1 
ATOM   6834 C CA  . VAL D 1 196 ? -5.618  19.999  37.206 1.00 42.53  ? 195 VAL D CA  1 
ATOM   6835 C C   . VAL D 1 196 ? -5.541  20.256  38.710 1.00 35.55  ? 195 VAL D C   1 
ATOM   6836 O O   . VAL D 1 196 ? -6.559  20.617  39.298 1.00 32.87  ? 195 VAL D O   1 
ATOM   6837 C CB  . VAL D 1 196 ? -4.809  18.747  36.858 1.00 29.24  ? 195 VAL D CB  1 
ATOM   6838 C CG1 . VAL D 1 196 ? -5.340  17.538  37.606 1.00 25.60  ? 195 VAL D CG1 1 
ATOM   6839 C CG2 . VAL D 1 196 ? -4.889  18.480  35.359 1.00 31.11  ? 195 VAL D CG2 1 
ATOM   6840 N N   . MET D 1 197 ? -4.376  20.095  39.327 1.00 26.87  ? 196 MET D N   1 
ATOM   6841 C CA  . MET D 1 197 ? -4.195  20.644  40.662 1.00 37.36  ? 196 MET D CA  1 
ATOM   6842 C C   . MET D 1 197 ? -4.271  22.151  40.419 1.00 51.00  ? 196 MET D C   1 
ATOM   6843 O O   . MET D 1 197 ? -4.131  22.601  39.274 1.00 69.53  ? 196 MET D O   1 
ATOM   6844 C CB  . MET D 1 197 ? -2.894  20.297  41.351 1.00 38.73  ? 196 MET D CB  1 
ATOM   6845 C CG  . MET D 1 197 ? -2.437  18.867  41.416 1.00 45.44  ? 196 MET D CG  1 
ATOM   6846 S SD  . MET D 1 197 ? -3.603  17.722  42.187 1.00 46.29  ? 196 MET D SD  1 
ATOM   6847 C CE  . MET D 1 197 ? -3.196  17.953  43.925 1.00 157.91 ? 196 MET D CE  1 
ATOM   6848 N N   . ASN D 1 198 ? -4.489  22.991  41.418 1.00 46.03  ? 197 ASN D N   1 
ATOM   6849 C CA  . ASN D 1 198 ? -4.444  24.409  40.958 1.00 40.96  ? 197 ASN D CA  1 
ATOM   6850 C C   . ASN D 1 198 ? -3.307  25.046  41.758 1.00 45.20  ? 197 ASN D C   1 
ATOM   6851 O O   . ASN D 1 198 ? -3.463  25.932  42.594 1.00 33.76  ? 197 ASN D O   1 
ATOM   6852 C CB  . ASN D 1 198 ? -5.829  24.989  41.061 1.00 38.60  ? 197 ASN D CB  1 
ATOM   6853 C CG  . ASN D 1 198 ? -5.975  26.433  41.462 1.00 47.79  ? 197 ASN D CG  1 
ATOM   6854 O OD1 . ASN D 1 198 ? -5.176  27.310  41.117 1.00 40.44  ? 197 ASN D OD1 1 
ATOM   6855 N ND2 . ASN D 1 198 ? -7.046  26.730  42.208 1.00 80.00  ? 197 ASN D ND2 1 
ATOM   6856 N N   . ARG D 1 199 ? -2.136  24.499  41.452 1.00 33.89  ? 198 ARG D N   1 
ATOM   6857 C CA  . ARG D 1 199 ? -0.833  24.688  42.050 1.00 33.92  ? 198 ARG D CA  1 
ATOM   6858 C C   . ARG D 1 199 ? 0.144   25.324  41.065 1.00 42.44  ? 198 ARG D C   1 
ATOM   6859 O O   . ARG D 1 199 ? 0.564   24.699  40.091 1.00 72.02  ? 198 ARG D O   1 
ATOM   6860 C CB  . ARG D 1 199 ? -0.301  23.337  42.522 1.00 37.19  ? 198 ARG D CB  1 
ATOM   6861 C CG  . ARG D 1 199 ? 0.865   23.297  43.482 1.00 48.03  ? 198 ARG D CG  1 
ATOM   6862 C CD  . ARG D 1 199 ? 0.684   22.148  44.476 1.00 50.17  ? 198 ARG D CD  1 
ATOM   6863 N NE  . ARG D 1 199 ? 1.718   22.033  45.494 1.00 47.89  ? 198 ARG D NE  1 
ATOM   6864 C CZ  . ARG D 1 199 ? 1.564   21.331  46.607 1.00 44.56  ? 198 ARG D CZ  1 
ATOM   6865 N NH1 . ARG D 1 199 ? 0.424   20.686  46.827 1.00 45.46  ? 198 ARG D NH1 1 
ATOM   6866 N NH2 . ARG D 1 199 ? 2.530   21.260  47.511 1.00 50.05  ? 198 ARG D NH2 1 
ATOM   6867 N N   . PHE D 1 200 ? 0.491   26.576  41.329 1.00 35.37  ? 199 PHE D N   1 
ATOM   6868 C CA  . PHE D 1 200 ? 1.475   27.312  40.554 1.00 29.10  ? 199 PHE D CA  1 
ATOM   6869 C C   . PHE D 1 200 ? 2.429   28.014  41.516 1.00 34.25  ? 199 PHE D C   1 
ATOM   6870 O O   . PHE D 1 200 ? 2.026   28.882  42.291 1.00 61.09  ? 199 PHE D O   1 
ATOM   6871 C CB  . PHE D 1 200 ? 0.813   28.332  39.641 1.00 37.85  ? 199 PHE D CB  1 
ATOM   6872 C CG  . PHE D 1 200 ? 0.220   27.808  38.346 1.00 45.20  ? 199 PHE D CG  1 
ATOM   6873 C CD1 . PHE D 1 200 ? 1.005   27.691  37.206 1.00 40.53  ? 199 PHE D CD1 1 
ATOM   6874 C CD2 . PHE D 1 200 ? -1.116  27.439  38.281 1.00 48.87  ? 199 PHE D CD2 1 
ATOM   6875 C CE1 . PHE D 1 200 ? 0.462   27.214  36.024 1.00 44.80  ? 199 PHE D CE1 1 
ATOM   6876 C CE2 . PHE D 1 200 ? -1.672  26.973  37.105 1.00 42.79  ? 199 PHE D CE2 1 
ATOM   6877 C CZ  . PHE D 1 200 ? -0.876  26.864  35.975 1.00 43.24  ? 199 PHE D CZ  1 
ATOM   6878 N N   . SER D 1 201 ? 3.695   27.640  41.480 1.00 27.51  ? 200 SER D N   1 
ATOM   6879 C CA  . SER D 1 201 ? 4.703   28.264  42.314 1.00 30.50  ? 200 SER D CA  1 
ATOM   6880 C C   . SER D 1 201 ? 5.265   29.520  41.658 1.00 45.79  ? 200 SER D C   1 
ATOM   6881 O O   . SER D 1 201 ? 5.184   29.731  40.449 1.00 46.00  ? 200 SER D O   1 
ATOM   6882 C CB  . SER D 1 201 ? 5.821   27.266  42.616 1.00 24.73  ? 200 SER D CB  1 
ATOM   6883 O OG  . SER D 1 201 ? 6.789   27.210  41.584 1.00 54.77  ? 200 SER D OG  1 
ATOM   6884 N N   . PRO D 1 202 ? 5.859   30.390  42.471 1.00 58.85  ? 201 PRO D N   1 
ATOM   6885 C CA  . PRO D 1 202 ? 6.472   31.607  41.939 1.00 55.54  ? 201 PRO D CA  1 
ATOM   6886 C C   . PRO D 1 202 ? 7.557   31.301  40.913 1.00 42.81  ? 201 PRO D C   1 
ATOM   6887 O O   . PRO D 1 202 ? 7.874   32.125  40.056 1.00 55.47  ? 201 PRO D O   1 
ATOM   6888 C CB  . PRO D 1 202 ? 7.122   32.236  43.174 1.00 61.93  ? 201 PRO D CB  1 
ATOM   6889 C CG  . PRO D 1 202 ? 6.395   31.664  44.343 1.00 67.04  ? 201 PRO D CG  1 
ATOM   6890 C CD  . PRO D 1 202 ? 5.985   30.280  43.936 1.00 66.59  ? 201 PRO D CD  1 
ATOM   6891 N N   . ALA D 1 203 ? 8.134   30.108  41.021 1.00 30.84  ? 202 ALA D N   1 
ATOM   6892 C CA  . ALA D 1 203 ? 9.235   29.735  40.144 1.00 32.20  ? 202 ALA D CA  1 
ATOM   6893 C C   . ALA D 1 203 ? 8.739   29.137  38.831 1.00 28.13  ? 202 ALA D C   1 
ATOM   6894 O O   . ALA D 1 203 ? 9.560   29.009  37.924 1.00 30.17  ? 202 ALA D O   1 
ATOM   6895 C CB  . ALA D 1 203 ? 10.162  28.777  40.883 1.00 31.72  ? 202 ALA D CB  1 
ATOM   6896 N N   . HIS D 1 204 ? 7.457   28.814  38.730 1.00 23.80  ? 203 HIS D N   1 
ATOM   6897 C CA  . HIS D 1 204 ? 6.840   28.145  37.596 1.00 29.70  ? 203 HIS D CA  1 
ATOM   6898 C C   . HIS D 1 204 ? 7.310   28.735  36.269 1.00 41.30  ? 203 HIS D C   1 
ATOM   6899 O O   . HIS D 1 204 ? 7.468   28.052  35.262 1.00 24.14  ? 203 HIS D O   1 
ATOM   6900 C CB  . HIS D 1 204 ? 5.314   28.217  37.671 1.00 29.74  ? 203 HIS D CB  1 
ATOM   6901 C CG  . HIS D 1 204 ? 4.562   27.582  36.537 1.00 44.90  ? 203 HIS D CG  1 
ATOM   6902 N ND1 . HIS D 1 204 ? 4.394   26.221  36.380 1.00 41.19  ? 203 HIS D ND1 1 
ATOM   6903 C CD2 . HIS D 1 204 ? 3.906   28.119  35.477 1.00 47.02  ? 203 HIS D CD2 1 
ATOM   6904 C CE1 . HIS D 1 204 ? 3.687   25.956  35.298 1.00 34.57  ? 203 HIS D CE1 1 
ATOM   6905 N NE2 . HIS D 1 204 ? 3.373   27.100  34.724 1.00 39.03  ? 203 HIS D NE2 1 
ATOM   6906 N N   . TRP D 1 205 ? 7.548   30.040  36.225 1.00 38.74  ? 204 TRP D N   1 
ATOM   6907 C CA  . TRP D 1 205 ? 8.018   30.676  35.010 1.00 26.69  ? 204 TRP D CA  1 
ATOM   6908 C C   . TRP D 1 205 ? 9.307   30.029  34.528 1.00 34.34  ? 204 TRP D C   1 
ATOM   6909 O O   . TRP D 1 205 ? 9.628   29.969  33.344 1.00 38.34  ? 204 TRP D O   1 
ATOM   6910 C CB  . TRP D 1 205 ? 8.257   32.163  35.276 1.00 28.08  ? 204 TRP D CB  1 
ATOM   6911 C CG  . TRP D 1 205 ? 9.433   32.427  36.168 1.00 34.30  ? 204 TRP D CG  1 
ATOM   6912 C CD1 . TRP D 1 205 ? 9.397   32.480  37.536 1.00 42.08  ? 204 TRP D CD1 1 
ATOM   6913 C CD2 . TRP D 1 205 ? 10.793  32.679  35.793 1.00 39.94  ? 204 TRP D CD2 1 
ATOM   6914 N NE1 . TRP D 1 205 ? 10.656  32.746  38.027 1.00 42.11  ? 204 TRP D NE1 1 
ATOM   6915 C CE2 . TRP D 1 205 ? 11.529  32.872  36.981 1.00 42.97  ? 204 TRP D CE2 1 
ATOM   6916 C CE3 . TRP D 1 205 ? 11.467  32.759  34.565 1.00 43.49  ? 204 TRP D CE3 1 
ATOM   6917 C CZ2 . TRP D 1 205 ? 12.900  33.139  36.967 1.00 47.25  ? 204 TRP D CZ2 1 
ATOM   6918 C CZ3 . TRP D 1 205 ? 12.823  33.022  34.548 1.00 36.82  ? 204 TRP D CZ3 1 
ATOM   6919 C CH2 . TRP D 1 205 ? 13.527  33.208  35.749 1.00 45.38  ? 204 TRP D CH2 1 
ATOM   6920 N N   . VAL D 1 206 ? 10.110  29.552  35.485 1.00 26.13  ? 205 VAL D N   1 
ATOM   6921 C CA  . VAL D 1 206 ? 11.395  29.022  35.049 1.00 20.17  ? 205 VAL D CA  1 
ATOM   6922 C C   . VAL D 1 206 ? 11.190  27.798  34.160 1.00 39.48  ? 205 VAL D C   1 
ATOM   6923 O O   . VAL D 1 206 ? 12.015  27.481  33.300 1.00 52.15  ? 205 VAL D O   1 
ATOM   6924 C CB  . VAL D 1 206 ? 12.290  28.604  36.222 1.00 28.01  ? 205 VAL D CB  1 
ATOM   6925 C CG1 . VAL D 1 206 ? 13.587  28.004  35.694 1.00 50.09  ? 205 VAL D CG1 1 
ATOM   6926 C CG2 . VAL D 1 206 ? 12.592  29.765  37.154 1.00 27.68  ? 205 VAL D CG2 1 
ATOM   6927 N N   . PHE D 1 207 ? 10.079  27.098  34.388 1.00 43.24  ? 206 PHE D N   1 
ATOM   6928 C CA  . PHE D 1 207 ? 9.856   25.831  33.683 1.00 40.27  ? 206 PHE D CA  1 
ATOM   6929 C C   . PHE D 1 207 ? 9.424   26.057  32.235 1.00 35.64  ? 206 PHE D C   1 
ATOM   6930 O O   . PHE D 1 207 ? 9.395   25.106  31.445 1.00 24.45  ? 206 PHE D O   1 
ATOM   6931 C CB  . PHE D 1 207 ? 8.849   24.985  34.468 1.00 32.74  ? 206 PHE D CB  1 
ATOM   6932 C CG  . PHE D 1 207 ? 9.235   24.809  35.938 1.00 28.36  ? 206 PHE D CG  1 
ATOM   6933 C CD1 . PHE D 1 207 ? 10.556  24.624  36.300 1.00 22.79  ? 206 PHE D CD1 1 
ATOM   6934 C CD2 . PHE D 1 207 ? 8.279   24.835  36.942 1.00 31.30  ? 206 PHE D CD2 1 
ATOM   6935 C CE1 . PHE D 1 207 ? 10.895  24.479  37.632 1.00 24.83  ? 206 PHE D CE1 1 
ATOM   6936 C CE2 . PHE D 1 207 ? 8.612   24.672  38.275 1.00 22.65  ? 206 PHE D CE2 1 
ATOM   6937 C CZ  . PHE D 1 207 ? 9.939   24.472  38.629 1.00 26.12  ? 206 PHE D CZ  1 
ATOM   6938 N N   . TRP D 1 208 ? 9.103   27.303  31.906 1.00 28.92  ? 207 TRP D N   1 
ATOM   6939 C CA  . TRP D 1 208 ? 8.770   27.751  30.566 1.00 31.19  ? 207 TRP D CA  1 
ATOM   6940 C C   . TRP D 1 208 ? 9.997   28.381  29.900 1.00 33.13  ? 207 TRP D C   1 
ATOM   6941 O O   . TRP D 1 208 ? 10.210  28.113  28.719 1.00 28.98  ? 207 TRP D O   1 
ATOM   6942 C CB  . TRP D 1 208 ? 7.649   28.789  30.515 1.00 28.96  ? 207 TRP D CB  1 
ATOM   6943 C CG  . TRP D 1 208 ? 6.305   28.253  30.893 1.00 33.01  ? 207 TRP D CG  1 
ATOM   6944 C CD1 . TRP D 1 208 ? 5.879   27.988  32.163 1.00 33.63  ? 207 TRP D CD1 1 
ATOM   6945 C CD2 . TRP D 1 208 ? 5.215   27.919  30.025 1.00 41.52  ? 207 TRP D CD2 1 
ATOM   6946 N NE1 . TRP D 1 208 ? 4.590   27.510  32.142 1.00 44.89  ? 207 TRP D NE1 1 
ATOM   6947 C CE2 . TRP D 1 208 ? 4.158   27.454  30.841 1.00 47.84  ? 207 TRP D CE2 1 
ATOM   6948 C CE3 . TRP D 1 208 ? 5.009   27.959  28.639 1.00 38.01  ? 207 TRP D CE3 1 
ATOM   6949 C CZ2 . TRP D 1 208 ? 2.931   27.039  30.317 1.00 45.57  ? 207 TRP D CZ2 1 
ATOM   6950 C CZ3 . TRP D 1 208 ? 3.788   27.542  28.125 1.00 31.11  ? 207 TRP D CZ3 1 
ATOM   6951 C CH2 . TRP D 1 208 ? 2.760   27.086  28.959 1.00 36.26  ? 207 TRP D CH2 1 
ATOM   6952 N N   . VAL D 1 209 ? 10.736  29.172  30.660 1.00 27.89  ? 208 VAL D N   1 
ATOM   6953 C CA  . VAL D 1 209 ? 11.808  30.007  30.151 1.00 29.49  ? 208 VAL D CA  1 
ATOM   6954 C C   . VAL D 1 209 ? 13.070  29.224  29.832 1.00 31.99  ? 208 VAL D C   1 
ATOM   6955 O O   . VAL D 1 209 ? 13.576  29.305  28.713 1.00 32.48  ? 208 VAL D O   1 
ATOM   6956 C CB  . VAL D 1 209 ? 12.172  31.107  31.171 1.00 41.13  ? 208 VAL D CB  1 
ATOM   6957 C CG1 . VAL D 1 209 ? 13.368  31.922  30.709 1.00 23.55  ? 208 VAL D CG1 1 
ATOM   6958 C CG2 . VAL D 1 209 ? 10.964  32.005  31.394 1.00 63.54  ? 208 VAL D CG2 1 
ATOM   6959 N N   . GLY D 1 210 ? 13.559  28.507  30.837 1.00 36.22  ? 209 GLY D N   1 
ATOM   6960 C CA  . GLY D 1 210 ? 14.740  27.672  30.715 1.00 39.89  ? 209 GLY D CA  1 
ATOM   6961 C C   . GLY D 1 210 ? 14.630  26.648  29.600 1.00 45.93  ? 209 GLY D C   1 
ATOM   6962 O O   . GLY D 1 210 ? 15.501  26.545  28.737 1.00 30.45  ? 209 GLY D O   1 
ATOM   6963 N N   . PRO D 1 211 ? 13.579  25.836  29.568 1.00 51.67  ? 210 PRO D N   1 
ATOM   6964 C CA  . PRO D 1 211 ? 13.381  24.923  28.430 1.00 48.89  ? 210 PRO D CA  1 
ATOM   6965 C C   . PRO D 1 211 ? 13.367  25.637  27.079 1.00 44.70  ? 210 PRO D C   1 
ATOM   6966 O O   . PRO D 1 211 ? 14.174  25.346  26.191 1.00 26.17  ? 210 PRO D O   1 
ATOM   6967 C CB  . PRO D 1 211 ? 12.010  24.301  28.725 1.00 44.24  ? 210 PRO D CB  1 
ATOM   6968 C CG  . PRO D 1 211 ? 11.810  24.445  30.197 1.00 43.33  ? 210 PRO D CG  1 
ATOM   6969 C CD  . PRO D 1 211 ? 12.533  25.699  30.598 1.00 48.34  ? 210 PRO D CD  1 
ATOM   6970 N N   . ILE D 1 212 ? 12.465  26.590  26.853 1.00 32.54  ? 211 ILE D N   1 
ATOM   6971 C CA  . ILE D 1 212 ? 12.384  27.251  25.557 1.00 28.69  ? 211 ILE D CA  1 
ATOM   6972 C C   . ILE D 1 212 ? 13.675  27.935  25.148 1.00 32.52  ? 211 ILE D C   1 
ATOM   6973 O O   . ILE D 1 212 ? 14.132  27.853  24.011 1.00 28.03  ? 211 ILE D O   1 
ATOM   6974 C CB  . ILE D 1 212 ? 11.270  28.316  25.554 1.00 25.85  ? 211 ILE D CB  1 
ATOM   6975 C CG1 . ILE D 1 212 ? 9.876   27.712  25.721 1.00 25.79  ? 211 ILE D CG1 1 
ATOM   6976 C CG2 . ILE D 1 212 ? 11.393  29.190  24.309 1.00 26.69  ? 211 ILE D CG2 1 
ATOM   6977 C CD1 . ILE D 1 212 ? 8.844   28.628  26.331 1.00 20.74  ? 211 ILE D CD1 1 
ATOM   6978 N N   . VAL D 1 213 ? 14.303  28.655  26.076 1.00 24.98  ? 212 VAL D N   1 
ATOM   6979 C CA  . VAL D 1 213 ? 15.525  29.348  25.676 1.00 27.58  ? 212 VAL D CA  1 
ATOM   6980 C C   . VAL D 1 213 ? 16.617  28.372  25.260 1.00 32.33  ? 212 VAL D C   1 
ATOM   6981 O O   . VAL D 1 213 ? 17.364  28.670  24.318 1.00 30.98  ? 212 VAL D O   1 
ATOM   6982 C CB  . VAL D 1 213 ? 15.981  30.254  26.838 1.00 39.61  ? 212 VAL D CB  1 
ATOM   6983 C CG1 . VAL D 1 213 ? 17.463  30.570  26.774 1.00 28.61  ? 212 VAL D CG1 1 
ATOM   6984 C CG2 . VAL D 1 213 ? 15.138  31.526  26.819 1.00 22.19  ? 212 VAL D CG2 1 
ATOM   6985 N N   . GLY D 1 214 ? 16.689  27.243  25.954 1.00 32.59  ? 213 GLY D N   1 
ATOM   6986 C CA  . GLY D 1 214 ? 17.634  26.156  25.790 1.00 32.20  ? 213 GLY D CA  1 
ATOM   6987 C C   . GLY D 1 214 ? 17.495  25.436  24.458 1.00 27.87  ? 213 GLY D C   1 
ATOM   6988 O O   . GLY D 1 214 ? 18.463  25.287  23.709 1.00 21.36  ? 213 GLY D O   1 
ATOM   6989 N N   . ALA D 1 215 ? 16.275  25.006  24.168 1.00 24.77  ? 214 ALA D N   1 
ATOM   6990 C CA  . ALA D 1 215 ? 15.881  24.510  22.858 1.00 30.30  ? 214 ALA D CA  1 
ATOM   6991 C C   . ALA D 1 215 ? 16.195  25.499  21.740 1.00 26.72  ? 214 ALA D C   1 
ATOM   6992 O O   . ALA D 1 215 ? 16.817  25.185  20.730 1.00 29.64  ? 214 ALA D O   1 
ATOM   6993 C CB  . ALA D 1 215 ? 14.386  24.186  22.826 1.00 17.80  ? 214 ALA D CB  1 
ATOM   6994 N N   . VAL D 1 216 ? 15.769  26.745  21.874 1.00 24.81  ? 215 VAL D N   1 
ATOM   6995 C CA  . VAL D 1 216 ? 15.954  27.705  20.796 1.00 24.44  ? 215 VAL D CA  1 
ATOM   6996 C C   . VAL D 1 216 ? 17.427  28.019  20.578 1.00 32.42  ? 215 VAL D C   1 
ATOM   6997 O O   . VAL D 1 216 ? 17.883  28.204  19.437 1.00 32.26  ? 215 VAL D O   1 
ATOM   6998 C CB  . VAL D 1 216 ? 15.149  28.983  21.075 1.00 31.52  ? 215 VAL D CB  1 
ATOM   6999 C CG1 . VAL D 1 216 ? 15.483  30.062  20.049 1.00 37.92  ? 215 VAL D CG1 1 
ATOM   7000 C CG2 . VAL D 1 216 ? 13.660  28.662  21.068 1.00 22.84  ? 215 VAL D CG2 1 
ATOM   7001 N N   . LEU D 1 217 ? 18.179  28.064  21.683 1.00 28.17  ? 216 LEU D N   1 
ATOM   7002 C CA  . LEU D 1 217 ? 19.620  28.214  21.488 1.00 29.03  ? 216 LEU D CA  1 
ATOM   7003 C C   . LEU D 1 217 ? 20.107  27.022  20.657 1.00 35.58  ? 216 LEU D C   1 
ATOM   7004 O O   . LEU D 1 217 ? 20.920  27.234  19.755 1.00 44.71  ? 216 LEU D O   1 
ATOM   7005 C CB  . LEU D 1 217 ? 20.398  28.322  22.795 1.00 17.26  ? 216 LEU D CB  1 
ATOM   7006 C CG  . LEU D 1 217 ? 20.302  29.659  23.533 1.00 22.43  ? 216 LEU D CG  1 
ATOM   7007 C CD1 . LEU D 1 217 ? 21.056  29.597  24.850 1.00 15.57  ? 216 LEU D CD1 1 
ATOM   7008 C CD2 . LEU D 1 217 ? 20.848  30.794  22.672 1.00 29.78  ? 216 LEU D CD2 1 
ATOM   7009 N N   . ALA D 1 218 ? 19.605  25.815  20.946 1.00 23.72  ? 217 ALA D N   1 
ATOM   7010 C CA  . ALA D 1 218 ? 20.066  24.638  20.203 1.00 19.64  ? 217 ALA D CA  1 
ATOM   7011 C C   . ALA D 1 218 ? 19.686  24.745  18.727 1.00 17.66  ? 217 ALA D C   1 
ATOM   7012 O O   . ALA D 1 218 ? 20.501  24.426  17.858 1.00 26.61  ? 217 ALA D O   1 
ATOM   7013 C CB  . ALA D 1 218 ? 19.564  23.347  20.818 1.00 17.22  ? 217 ALA D CB  1 
ATOM   7014 N N   . ALA D 1 219 ? 18.485  25.208  18.448 1.00 22.83  ? 218 ALA D N   1 
ATOM   7015 C CA  . ALA D 1 219 ? 17.957  25.392  17.103 1.00 29.25  ? 218 ALA D CA  1 
ATOM   7016 C C   . ALA D 1 219 ? 18.759  26.409  16.308 1.00 25.58  ? 218 ALA D C   1 
ATOM   7017 O O   . ALA D 1 219 ? 19.019  26.306  15.114 1.00 34.98  ? 218 ALA D O   1 
ATOM   7018 C CB  . ALA D 1 219 ? 16.496  25.822  17.224 1.00 25.15  ? 218 ALA D CB  1 
ATOM   7019 N N   . ILE D 1 220 ? 19.184  27.466  16.992 1.00 25.21  ? 219 ILE D N   1 
ATOM   7020 C CA  . ILE D 1 220 ? 19.991  28.461  16.304 1.00 38.13  ? 219 ILE D CA  1 
ATOM   7021 C C   . ILE D 1 220 ? 21.394  27.934  16.061 1.00 38.40  ? 219 ILE D C   1 
ATOM   7022 O O   . ILE D 1 220 ? 22.025  28.264  15.057 1.00 32.30  ? 219 ILE D O   1 
ATOM   7023 C CB  . ILE D 1 220 ? 20.054  29.757  17.136 1.00 41.36  ? 219 ILE D CB  1 
ATOM   7024 C CG1 . ILE D 1 220 ? 18.711  30.480  17.174 1.00 31.15  ? 219 ILE D CG1 1 
ATOM   7025 C CG2 . ILE D 1 220 ? 21.174  30.656  16.648 1.00 38.29  ? 219 ILE D CG2 1 
ATOM   7026 C CD1 . ILE D 1 220 ? 18.385  31.131  18.492 1.00 25.23  ? 219 ILE D CD1 1 
ATOM   7027 N N   . LEU D 1 221 ? 21.897  27.115  16.989 1.00 32.38  ? 220 LEU D N   1 
ATOM   7028 C CA  . LEU D 1 221 ? 23.276  26.662  16.830 1.00 26.97  ? 220 LEU D CA  1 
ATOM   7029 C C   . LEU D 1 221 ? 23.363  25.682  15.666 1.00 23.86  ? 220 LEU D C   1 
ATOM   7030 O O   . LEU D 1 221 ? 24.077  25.911  14.695 1.00 28.45  ? 220 LEU D O   1 
ATOM   7031 C CB  . LEU D 1 221 ? 23.845  26.006  18.093 1.00 28.03  ? 220 LEU D CB  1 
ATOM   7032 C CG  . LEU D 1 221 ? 25.086  25.143  17.846 1.00 28.60  ? 220 LEU D CG  1 
ATOM   7033 C CD1 . LEU D 1 221 ? 26.218  26.012  17.311 1.00 30.24  ? 220 LEU D CD1 1 
ATOM   7034 C CD2 . LEU D 1 221 ? 25.512  24.392  19.099 1.00 21.00  ? 220 LEU D CD2 1 
ATOM   7035 N N   . TYR D 1 222 ? 22.618  24.602  15.791 1.00 24.72  ? 221 TYR D N   1 
ATOM   7036 C CA  . TYR D 1 222 ? 22.529  23.561  14.792 1.00 29.67  ? 221 TYR D CA  1 
ATOM   7037 C C   . TYR D 1 222 ? 22.138  24.028  13.393 1.00 26.11  ? 221 TYR D C   1 
ATOM   7038 O O   . TYR D 1 222 ? 22.891  23.861  12.434 1.00 37.41  ? 221 TYR D O   1 
ATOM   7039 C CB  . TYR D 1 222 ? 21.466  22.536  15.218 1.00 23.67  ? 221 TYR D CB  1 
ATOM   7040 C CG  . TYR D 1 222 ? 21.469  21.278  14.388 1.00 24.72  ? 221 TYR D CG  1 
ATOM   7041 C CD1 . TYR D 1 222 ? 22.390  20.277  14.640 1.00 28.05  ? 221 TYR D CD1 1 
ATOM   7042 C CD2 . TYR D 1 222 ? 20.546  21.087  13.356 1.00 29.77  ? 221 TYR D CD2 1 
ATOM   7043 C CE1 . TYR D 1 222 ? 22.400  19.116  13.880 1.00 28.56  ? 221 TYR D CE1 1 
ATOM   7044 C CE2 . TYR D 1 222 ? 20.552  19.925  12.598 1.00 29.32  ? 221 TYR D CE2 1 
ATOM   7045 C CZ  . TYR D 1 222 ? 21.481  18.944  12.867 1.00 26.20  ? 221 TYR D CZ  1 
ATOM   7046 O OH  . TYR D 1 222 ? 21.516  17.779  12.135 1.00 32.76  ? 221 TYR D OH  1 
ATOM   7047 N N   . PHE D 1 223 ? 20.932  24.560  13.278 1.00 24.03  ? 222 PHE D N   1 
ATOM   7048 C CA  . PHE D 1 223 ? 20.353  24.879  11.986 1.00 32.78  ? 222 PHE D CA  1 
ATOM   7049 C C   . PHE D 1 223 ? 20.989  26.094  11.313 1.00 37.38  ? 222 PHE D C   1 
ATOM   7050 O O   . PHE D 1 223 ? 20.799  26.286  10.106 1.00 41.30  ? 222 PHE D O   1 
ATOM   7051 C CB  . PHE D 1 223 ? 18.842  25.072  12.154 1.00 29.10  ? 222 PHE D CB  1 
ATOM   7052 C CG  . PHE D 1 223 ? 18.068  23.792  12.421 1.00 44.64  ? 222 PHE D CG  1 
ATOM   7053 C CD1 . PHE D 1 223 ? 17.381  23.642  13.622 1.00 48.68  ? 222 PHE D CD1 1 
ATOM   7054 C CD2 . PHE D 1 223 ? 18.012  22.759  11.500 1.00 41.24  ? 222 PHE D CD2 1 
ATOM   7055 C CE1 . PHE D 1 223 ? 16.664  22.493  13.895 1.00 38.16  ? 222 PHE D CE1 1 
ATOM   7056 C CE2 . PHE D 1 223 ? 17.305  21.602  11.769 1.00 35.63  ? 222 PHE D CE2 1 
ATOM   7057 C CZ  . PHE D 1 223 ? 16.623  21.473  12.967 1.00 28.44  ? 222 PHE D CZ  1 
ATOM   7058 N N   . TYR D 1 224 ? 21.746  26.934  12.006 1.00 25.60  ? 223 TYR D N   1 
ATOM   7059 C CA  . TYR D 1 224 ? 22.269  28.147  11.405 1.00 29.11  ? 223 TYR D CA  1 
ATOM   7060 C C   . TYR D 1 224 ? 23.762  28.329  11.656 1.00 37.93  ? 223 TYR D C   1 
ATOM   7061 O O   . TYR D 1 224 ? 24.355  29.268  11.117 1.00 37.75  ? 223 TYR D O   1 
ATOM   7062 C CB  . TYR D 1 224 ? 21.555  29.388  11.945 1.00 30.85  ? 223 TYR D CB  1 
ATOM   7063 C CG  . TYR D 1 224 ? 20.067  29.453  11.698 1.00 36.38  ? 223 TYR D CG  1 
ATOM   7064 C CD1 . TYR D 1 224 ? 19.518  29.207  10.441 1.00 34.85  ? 223 TYR D CD1 1 
ATOM   7065 C CD2 . TYR D 1 224 ? 19.199  29.775  12.741 1.00 28.53  ? 223 TYR D CD2 1 
ATOM   7066 C CE1 . TYR D 1 224 ? 18.154  29.268  10.215 1.00 34.14  ? 223 TYR D CE1 1 
ATOM   7067 C CE2 . TYR D 1 224 ? 17.839  29.832  12.513 1.00 30.34  ? 223 TYR D CE2 1 
ATOM   7068 C CZ  . TYR D 1 224 ? 17.311  29.585  11.268 1.00 24.87  ? 223 TYR D CZ  1 
ATOM   7069 O OH  . TYR D 1 224 ? 15.947  29.653  11.058 1.00 25.50  ? 223 TYR D OH  1 
ATOM   7070 N N   . LEU D 1 225 ? 24.366  27.470  12.458 1.00 44.70  ? 224 LEU D N   1 
ATOM   7071 C CA  . LEU D 1 225 ? 25.794  27.572  12.751 1.00 49.96  ? 224 LEU D CA  1 
ATOM   7072 C C   . LEU D 1 225 ? 26.534  26.294  12.358 1.00 53.81  ? 224 LEU D C   1 
ATOM   7073 O O   . LEU D 1 225 ? 27.594  26.338  11.730 1.00 67.24  ? 224 LEU D O   1 
ATOM   7074 C CB  . LEU D 1 225 ? 26.048  27.842  14.227 1.00 48.33  ? 224 LEU D CB  1 
ATOM   7075 C CG  . LEU D 1 225 ? 25.811  29.218  14.838 1.00 54.02  ? 224 LEU D CG  1 
ATOM   7076 C CD1 . LEU D 1 225 ? 27.023  29.636  15.675 1.00 40.99  ? 224 LEU D CD1 1 
ATOM   7077 C CD2 . LEU D 1 225 ? 25.496  30.270  13.793 1.00 59.09  ? 224 LEU D CD2 1 
ATOM   7078 N N   . LEU D 1 226 ? 26.001  25.129  12.727 1.00 46.21  ? 225 LEU D N   1 
ATOM   7079 C CA  . LEU D 1 226 ? 26.669  23.877  12.373 1.00 39.92  ? 225 LEU D CA  1 
ATOM   7080 C C   . LEU D 1 226 ? 26.193  23.389  11.009 1.00 39.58  ? 225 LEU D C   1 
ATOM   7081 O O   . LEU D 1 226 ? 27.014  23.138  10.118 1.00 35.32  ? 225 LEU D O   1 
ATOM   7082 C CB  . LEU D 1 226 ? 26.459  22.794  13.441 1.00 27.26  ? 225 LEU D CB  1 
ATOM   7083 C CG  . LEU D 1 226 ? 26.694  23.169  14.903 1.00 33.92  ? 225 LEU D CG  1 
ATOM   7084 C CD1 . LEU D 1 226 ? 26.423  22.000  15.852 1.00 27.46  ? 225 LEU D CD1 1 
ATOM   7085 C CD2 . LEU D 1 226 ? 28.109  23.680  15.133 1.00 32.68  ? 225 LEU D CD2 1 
ATOM   7086 N N   . PHE D 1 227 ? 24.875  23.208  10.828 1.00 27.67  ? 226 PHE D N   1 
ATOM   7087 C CA  . PHE D 1 227 ? 24.371  22.616  9.592  1.00 38.35  ? 226 PHE D CA  1 
ATOM   7088 C C   . PHE D 1 227 ? 23.282  23.434  8.924  1.00 39.53  ? 226 PHE D C   1 
ATOM   7089 O O   . PHE D 1 227 ? 22.132  23.024  8.771  1.00 32.81  ? 226 PHE D O   1 
ATOM   7090 C CB  . PHE D 1 227 ? 23.861  21.176  9.842  1.00 42.17  ? 226 PHE D CB  1 
ATOM   7091 C CG  . PHE D 1 227 ? 25.022  20.379  10.435 1.00 51.60  ? 226 PHE D CG  1 
ATOM   7092 C CD1 . PHE D 1 227 ? 26.034  19.905  9.626  1.00 59.19  ? 226 PHE D CD1 1 
ATOM   7093 C CD2 . PHE D 1 227 ? 25.078  20.167  11.800 1.00 53.29  ? 226 PHE D CD2 1 
ATOM   7094 C CE1 . PHE D 1 227 ? 27.101  19.219  10.180 1.00 66.22  ? 226 PHE D CE1 1 
ATOM   7095 C CE2 . PHE D 1 227 ? 26.134  19.474  12.353 1.00 56.14  ? 226 PHE D CE2 1 
ATOM   7096 C CZ  . PHE D 1 227 ? 27.155  19.006  11.547 1.00 63.66  ? 226 PHE D CZ  1 
ATOM   7097 N N   . PRO D 1 228 ? 23.654  24.628  8.469  1.00 40.38  ? 227 PRO D N   1 
ATOM   7098 C CA  . PRO D 1 228 ? 22.667  25.461  7.767  1.00 30.16  ? 227 PRO D CA  1 
ATOM   7099 C C   . PRO D 1 228 ? 22.445  24.859  6.381  1.00 27.77  ? 227 PRO D C   1 
ATOM   7100 O O   . PRO D 1 228 ? 23.329  24.161  5.880  1.00 30.25  ? 227 PRO D O   1 
ATOM   7101 C CB  . PRO D 1 228 ? 23.358  26.818  7.705  1.00 30.28  ? 227 PRO D CB  1 
ATOM   7102 C CG  . PRO D 1 228 ? 24.820  26.491  7.700  1.00 38.08  ? 227 PRO D CG  1 
ATOM   7103 C CD  . PRO D 1 228 ? 24.976  25.259  8.552  1.00 38.65  ? 227 PRO D CD  1 
ATOM   7104 N N   . ASN D 1 229 ? 21.300  25.100  5.786  1.00 25.25  ? 228 ASN D N   1 
ATOM   7105 C CA  . ASN D 1 229 ? 21.002  24.695  4.427  1.00 38.09  ? 228 ASN D CA  1 
ATOM   7106 C C   . ASN D 1 229 ? 20.910  25.970  3.582  1.00 41.89  ? 228 ASN D C   1 
ATOM   7107 O O   . ASN D 1 229 ? 21.008  27.054  4.164  1.00 40.83  ? 228 ASN D O   1 
ATOM   7108 C CB  . ASN D 1 229 ? 19.699  23.918  4.350  1.00 36.18  ? 228 ASN D CB  1 
ATOM   7109 C CG  . ASN D 1 229 ? 18.564  24.736  4.944  1.00 53.53  ? 228 ASN D CG  1 
ATOM   7110 O OD1 . ASN D 1 229 ? 18.757  25.880  5.356  1.00 91.11  ? 228 ASN D OD1 1 
ATOM   7111 N ND2 . ASN D 1 229 ? 17.369  24.160  5.009  1.00 83.32  ? 228 ASN D ND2 1 
ATOM   7112 N N   . SER D 1 230 ? 20.713  25.795  2.292  1.00 39.10  ? 229 SER D N   1 
ATOM   7113 C CA  . SER D 1 230 ? 20.629  26.902  1.354  1.00 45.44  ? 229 SER D CA  1 
ATOM   7114 C C   . SER D 1 230 ? 19.258  26.953  0.687  1.00 52.73  ? 229 SER D C   1 
ATOM   7115 O O   . SER D 1 230 ? 18.955  26.142  -0.184 1.00 69.17  ? 229 SER D O   1 
ATOM   7116 C CB  . SER D 1 230 ? 21.713  26.780  0.282  1.00 44.37  ? 229 SER D CB  1 
ATOM   7117 O OG  . SER D 1 230 ? 22.332  25.507  0.401  1.00 63.20  ? 229 SER D OG  1 
ATOM   7118 N N   . LEU D 1 231 ? 18.485  27.927  1.131  1.00 55.63  ? 230 LEU D N   1 
ATOM   7119 C CA  . LEU D 1 231 ? 17.175  28.248  0.609  1.00 63.50  ? 230 LEU D CA  1 
ATOM   7120 C C   . LEU D 1 231 ? 17.039  29.764  0.438  1.00 63.95  ? 230 LEU D C   1 
ATOM   7121 O O   . LEU D 1 231 ? 17.807  30.540  1.001  1.00 70.57  ? 230 LEU D O   1 
ATOM   7122 C CB  . LEU D 1 231 ? 16.072  27.730  1.533  1.00 72.27  ? 230 LEU D CB  1 
ATOM   7123 C CG  . LEU D 1 231 ? 15.684  26.254  1.501  1.00 78.12  ? 230 LEU D CG  1 
ATOM   7124 C CD1 . LEU D 1 231 ? 15.695  25.687  0.088  1.00 67.10  ? 230 LEU D CD1 1 
ATOM   7125 C CD2 . LEU D 1 231 ? 16.623  25.443  2.400  1.00 93.36  ? 230 LEU D CD2 1 
ATOM   7126 N N   . SER D 1 232 ? 16.047  30.173  -0.343 1.00 65.08  ? 231 SER D N   1 
ATOM   7127 C CA  . SER D 1 232 ? 15.713  31.569  -0.565 1.00 57.81  ? 231 SER D CA  1 
ATOM   7128 C C   . SER D 1 232 ? 14.870  32.130  0.574  1.00 59.76  ? 231 SER D C   1 
ATOM   7129 O O   . SER D 1 232 ? 14.147  31.424  1.269  1.00 56.49  ? 231 SER D O   1 
ATOM   7130 C CB  . SER D 1 232 ? 14.937  31.729  -1.880 1.00 50.63  ? 231 SER D CB  1 
ATOM   7131 O OG  . SER D 1 232 ? 13.575  31.365  -1.720 1.00 43.09  ? 231 SER D OG  1 
ATOM   7132 N N   . LEU D 1 233 ? 14.932  33.442  0.768  1.00 58.96  ? 232 LEU D N   1 
ATOM   7133 C CA  . LEU D 1 233 ? 14.049  34.098  1.720  1.00 53.38  ? 232 LEU D CA  1 
ATOM   7134 C C   . LEU D 1 233 ? 12.590  33.809  1.392  1.00 49.07  ? 232 LEU D C   1 
ATOM   7135 O O   . LEU D 1 233 ? 11.764  33.764  2.300  1.00 46.52  ? 232 LEU D O   1 
ATOM   7136 C CB  . LEU D 1 233 ? 14.285  35.608  1.708  1.00 55.98  ? 232 LEU D CB  1 
ATOM   7137 C CG  . LEU D 1 233 ? 15.698  36.030  2.128  1.00 57.48  ? 232 LEU D CG  1 
ATOM   7138 C CD1 . LEU D 1 233 ? 15.736  37.528  2.391  1.00 64.11  ? 232 LEU D CD1 1 
ATOM   7139 C CD2 . LEU D 1 233 ? 16.150  35.231  3.343  1.00 42.58  ? 232 LEU D CD2 1 
ATOM   7140 N N   . SER D 1 234 ? 12.320  33.633  0.107  1.00 51.46  ? 233 SER D N   1 
ATOM   7141 C CA  . SER D 1 234 ? 11.007  33.258  -0.392 1.00 56.64  ? 233 SER D CA  1 
ATOM   7142 C C   . SER D 1 234 ? 10.648  31.870  0.140  1.00 50.45  ? 233 SER D C   1 
ATOM   7143 O O   . SER D 1 234 ? 9.555   31.663  0.659  1.00 40.02  ? 233 SER D O   1 
ATOM   7144 C CB  . SER D 1 234 ? 10.919  33.238  -1.917 1.00 64.27  ? 233 SER D CB  1 
ATOM   7145 O OG  . SER D 1 234 ? 11.968  33.950  -2.550 1.00 87.66  ? 233 SER D OG  1 
ATOM   7146 N N   . GLU D 1 235 ? 11.606  30.959  -0.014 1.00 49.97  ? 234 GLU D N   1 
ATOM   7147 C CA  . GLU D 1 235 ? 11.449  29.603  0.512  1.00 54.56  ? 234 GLU D CA  1 
ATOM   7148 C C   . GLU D 1 235 ? 11.440  29.607  2.032  1.00 52.91  ? 234 GLU D C   1 
ATOM   7149 O O   . GLU D 1 235 ? 10.687  28.888  2.690  1.00 57.89  ? 234 GLU D O   1 
ATOM   7150 C CB  . GLU D 1 235 ? 12.576  28.726  -0.032 1.00 60.85  ? 234 GLU D CB  1 
ATOM   7151 C CG  . GLU D 1 235 ? 12.605  28.746  -1.558 1.00 73.44  ? 234 GLU D CG  1 
ATOM   7152 C CD  . GLU D 1 235 ? 13.709  27.879  -2.116 1.00 79.25  ? 234 GLU D CD  1 
ATOM   7153 O OE1 . GLU D 1 235 ? 14.820  28.417  -2.311 1.00 81.07  ? 234 GLU D OE1 1 
ATOM   7154 O OE2 . GLU D 1 235 ? 13.441  26.679  -2.340 1.00 86.05  ? 234 GLU D OE2 1 
ATOM   7155 N N   . ARG D 1 236 ? 12.289  30.447  2.622  1.00 47.39  ? 235 ARG D N   1 
ATOM   7156 C CA  . ARG D 1 236 ? 12.261  30.603  4.072  1.00 46.18  ? 235 ARG D CA  1 
ATOM   7157 C C   . ARG D 1 236 ? 10.907  31.170  4.481  1.00 53.68  ? 235 ARG D C   1 
ATOM   7158 O O   . ARG D 1 236 ? 10.251  30.747  5.438  1.00 57.13  ? 235 ARG D O   1 
ATOM   7159 C CB  . ARG D 1 236 ? 13.410  31.490  4.525  1.00 38.95  ? 235 ARG D CB  1 
ATOM   7160 C CG  . ARG D 1 236 ? 14.749  30.759  4.589  1.00 44.45  ? 235 ARG D CG  1 
ATOM   7161 C CD  . ARG D 1 236 ? 15.649  31.414  5.621  1.00 53.33  ? 235 ARG D CD  1 
ATOM   7162 N NE  . ARG D 1 236 ? 17.026  30.966  5.661  1.00 51.17  ? 235 ARG D NE  1 
ATOM   7163 C CZ  . ARG D 1 236 ? 17.499  29.785  6.024  1.00 53.14  ? 235 ARG D CZ  1 
ATOM   7164 N NH1 . ARG D 1 236 ? 16.695  28.802  6.418  1.00 39.73  ? 235 ARG D NH1 1 
ATOM   7165 N NH2 . ARG D 1 236 ? 18.810  29.564  5.998  1.00 72.06  ? 235 ARG D NH2 1 
ATOM   7166 N N   . VAL D 1 237 ? 10.465  32.156  3.696  1.00 39.92  ? 236 VAL D N   1 
ATOM   7167 C CA  . VAL D 1 237 ? 9.183   32.776  4.020  1.00 36.42  ? 236 VAL D CA  1 
ATOM   7168 C C   . VAL D 1 237 ? 8.072   31.739  3.920  1.00 29.85  ? 236 VAL D C   1 
ATOM   7169 O O   . VAL D 1 237 ? 7.224   31.660  4.808  1.00 42.83  ? 236 VAL D O   1 
ATOM   7170 C CB  . VAL D 1 237 ? 8.887   33.980  3.114  1.00 36.88  ? 236 VAL D CB  1 
ATOM   7171 C CG1 . VAL D 1 237 ? 7.401   34.288  3.095  1.00 28.80  ? 236 VAL D CG1 1 
ATOM   7172 C CG2 . VAL D 1 237 ? 9.671   35.192  3.607  1.00 37.86  ? 236 VAL D CG2 1 
ATOM   7173 N N   . ALA D 1 238 ? 8.123   30.960  2.850  1.00 31.18  ? 237 ALA D N   1 
ATOM   7174 C CA  . ALA D 1 238 ? 7.182   29.889  2.555  1.00 39.87  ? 237 ALA D CA  1 
ATOM   7175 C C   . ALA D 1 238 ? 7.064   28.882  3.696  1.00 33.98  ? 237 ALA D C   1 
ATOM   7176 O O   . ALA D 1 238 ? 5.954   28.462  4.042  1.00 29.61  ? 237 ALA D O   1 
ATOM   7177 C CB  . ALA D 1 238 ? 7.576   29.189  1.258  1.00 39.33  ? 237 ALA D CB  1 
ATOM   7178 N N   . ILE D 1 239 ? 8.194   28.499  4.286  1.00 31.04  ? 238 ILE D N   1 
ATOM   7179 C CA  . ILE D 1 239 ? 8.140   27.638  5.461  1.00 29.49  ? 238 ILE D CA  1 
ATOM   7180 C C   . ILE D 1 239 ? 7.224   28.235  6.534  1.00 32.98  ? 238 ILE D C   1 
ATOM   7181 O O   . ILE D 1 239 ? 6.294   27.553  6.963  1.00 34.13  ? 238 ILE D O   1 
ATOM   7182 C CB  . ILE D 1 239 ? 9.523   27.445  6.109  1.00 39.43  ? 238 ILE D CB  1 
ATOM   7183 C CG1 . ILE D 1 239 ? 10.712  27.580  5.163  1.00 43.16  ? 238 ILE D CG1 1 
ATOM   7184 C CG2 . ILE D 1 239 ? 9.554   26.108  6.839  1.00 58.42  ? 238 ILE D CG2 1 
ATOM   7185 C CD1 . ILE D 1 239 ? 11.470  26.297  4.915  1.00 38.29  ? 238 ILE D CD1 1 
ATOM   7186 N N   . ILE D 1 240 ? 7.525   29.471  6.938  1.00 27.43  ? 239 ILE D N   1 
ATOM   7187 C CA  . ILE D 1 240 ? 6.820   30.152  8.011  1.00 38.89  ? 239 ILE D CA  1 
ATOM   7188 C C   . ILE D 1 240 ? 5.345   30.382  7.683  1.00 42.79  ? 239 ILE D C   1 
ATOM   7189 O O   . ILE D 1 240 ? 4.508   30.338  8.587  1.00 35.37  ? 239 ILE D O   1 
ATOM   7190 C CB  . ILE D 1 240 ? 7.415   31.531  8.364  1.00 36.77  ? 239 ILE D CB  1 
ATOM   7191 C CG1 . ILE D 1 240 ? 8.901   31.483  8.696  1.00 36.96  ? 239 ILE D CG1 1 
ATOM   7192 C CG2 . ILE D 1 240 ? 6.616   32.185  9.494  1.00 27.54  ? 239 ILE D CG2 1 
ATOM   7193 C CD1 . ILE D 1 240 ? 9.732   32.621  8.154  1.00 42.60  ? 239 ILE D CD1 1 
ATOM   7194 N N   . LYS D 1 241 ? 5.063   30.627  6.406  1.00 39.23  ? 240 LYS D N   1 
ATOM   7195 C CA  . LYS D 1 241 ? 3.669   30.877  6.029  1.00 48.98  ? 240 LYS D CA  1 
ATOM   7196 C C   . LYS D 1 241 ? 3.011   29.556  5.633  1.00 43.22  ? 240 LYS D C   1 
ATOM   7197 O O   . LYS D 1 241 ? 1.814   29.484  5.348  1.00 36.89  ? 240 LYS D O   1 
ATOM   7198 C CB  . LYS D 1 241 ? 3.571   31.924  4.927  1.00 58.43  ? 240 LYS D CB  1 
ATOM   7199 C CG  . LYS D 1 241 ? 4.721   32.902  4.821  1.00 74.39  ? 240 LYS D CG  1 
ATOM   7200 C CD  . LYS D 1 241 ? 4.868   33.842  6.000  1.00 86.69  ? 240 LYS D CD  1 
ATOM   7201 C CE  . LYS D 1 241 ? 6.307   34.291  6.205  1.00 88.14  ? 240 LYS D CE  1 
ATOM   7202 N NZ  . LYS D 1 241 ? 6.417   35.541  7.014  1.00 81.23  ? 240 LYS D NZ  1 
ATOM   7203 N N   . GLY D 1 242 ? 3.856   28.529  5.645  1.00 36.03  ? 241 GLY D N   1 
ATOM   7204 C CA  . GLY D 1 242 ? 3.449   27.150  5.466  1.00 33.42  ? 241 GLY D CA  1 
ATOM   7205 C C   . GLY D 1 242 ? 3.047   26.869  4.036  1.00 35.12  ? 241 GLY D C   1 
ATOM   7206 O O   . GLY D 1 242 ? 2.210   26.035  3.711  1.00 43.54  ? 241 GLY D O   1 
ATOM   7207 N N   . THR D 1 243 ? 3.684   27.616  3.150  1.00 32.56  ? 242 THR D N   1 
ATOM   7208 C CA  . THR D 1 243 ? 3.336   27.558  1.735  1.00 47.10  ? 242 THR D CA  1 
ATOM   7209 C C   . THR D 1 243 ? 4.336   26.721  0.947  1.00 59.08  ? 242 THR D C   1 
ATOM   7210 O O   . THR D 1 243 ? 3.968   26.113  -0.064 1.00 77.39  ? 242 THR D O   1 
ATOM   7211 C CB  . THR D 1 243 ? 3.258   29.013  1.225  1.00 47.20  ? 242 THR D CB  1 
ATOM   7212 O OG1 . THR D 1 243 ? 1.869   29.353  1.122  1.00 47.50  ? 242 THR D OG1 1 
ATOM   7213 C CG2 . THR D 1 243 ? 3.905   29.175  -0.138 1.00 67.14  ? 242 THR D CG2 1 
ATOM   7214 N N   . TYR D 1 244 ? 5.566   26.701  1.438  1.00 63.76  ? 243 TYR D N   1 
ATOM   7215 C CA  . TYR D 1 244 ? 6.714   26.036  0.856  1.00 68.38  ? 243 TYR D CA  1 
ATOM   7216 C C   . TYR D 1 244 ? 6.341   24.677  0.263  1.00 80.70  ? 243 TYR D C   1 
ATOM   7217 O O   . TYR D 1 244 ? 6.824   24.363  -0.831 1.00 109.53 ? 243 TYR D O   1 
ATOM   7218 C CB  . TYR D 1 244 ? 7.824   25.893  1.897  1.00 67.86  ? 243 TYR D CB  1 
ATOM   7219 C CG  . TYR D 1 244 ? 9.152   25.387  1.381  1.00 79.05  ? 243 TYR D CG  1 
ATOM   7220 C CD1 . TYR D 1 244 ? 10.028  26.196  0.653  1.00 82.75  ? 243 TYR D CD1 1 
ATOM   7221 C CD2 . TYR D 1 244 ? 9.554   24.075  1.614  1.00 88.19  ? 243 TYR D CD2 1 
ATOM   7222 C CE1 . TYR D 1 244 ? 11.240  25.723  0.187  1.00 86.10  ? 243 TYR D CE1 1 
ATOM   7223 C CE2 . TYR D 1 244 ? 10.767  23.594  1.152  1.00 94.02  ? 243 TYR D CE2 1 
ATOM   7224 C CZ  . TYR D 1 244 ? 11.616  24.421  0.439  1.00 89.64  ? 243 TYR D CZ  1 
ATOM   7225 O OH  . TYR D 1 244 ? 12.822  23.943  -0.019 1.00 75.33  ? 243 TYR D OH  1 
ATOM   7226 N N   . GLU D 1 245 ? 5.497   23.942  0.963  1.00 86.29  ? 244 GLU D N   1 
ATOM   7227 C CA  . GLU D 1 245 ? 4.958   22.652  0.554  1.00 99.68  ? 244 GLU D CA  1 
ATOM   7228 C C   . GLU D 1 245 ? 4.408   21.928  1.782  1.00 105.26 ? 244 GLU D C   1 
ATOM   7229 O O   . GLU D 1 245 ? 4.787   22.269  2.906  1.00 96.70  ? 244 GLU D O   1 
ATOM   7230 C CB  . GLU D 1 245 ? 6.001   21.784  -0.143 1.00 107.19 ? 244 GLU D CB  1 
ATOM   7231 C CG  . GLU D 1 245 ? 5.677   21.163  -1.484 1.00 109.55 ? 244 GLU D CG  1 
ATOM   7232 C CD  . GLU D 1 245 ? 4.903   22.024  -2.456 1.00 110.44 ? 244 GLU D CD  1 
ATOM   7233 O OE1 . GLU D 1 245 ? 3.896   21.555  -3.033 1.00 101.54 ? 244 GLU D OE1 1 
ATOM   7234 O OE2 . GLU D 1 245 ? 5.284   23.192  -2.674 1.00 120.68 ? 244 GLU D OE2 1 
ATOM   7235 N N   . PRO D 1 246 ? 3.526   20.961  1.543  1.00 111.50 ? 245 PRO D N   1 
ATOM   7236 C CA  . PRO D 1 246 ? 3.029   20.049  2.571  1.00 112.00 ? 245 PRO D CA  1 
ATOM   7237 C C   . PRO D 1 246 ? 4.100   19.162  3.180  1.00 100.56 ? 245 PRO D C   1 
ATOM   7238 O O   . PRO D 1 246 ? 5.308   19.303  2.975  0.71 61.54  ? 245 PRO D O   1 
ATOM   7239 C CB  . PRO D 1 246 ? 2.037   19.151  1.814  1.00 115.85 ? 245 PRO D CB  1 
ATOM   7240 C CG  . PRO D 1 246 ? 1.698   19.898  0.576  1.00 115.72 ? 245 PRO D CG  1 
ATOM   7241 C CD  . PRO D 1 246 ? 2.904   20.718  0.226  1.00 112.32 ? 245 PRO D CD  1 
HETATM 7242 O O2  . PS6 E 2 .   ? 20.465  1.154   11.098 1.00 102.93 ? 266 PS6 D O2  1 
HETATM 7243 O O1  . PS6 E 2 .   ? 19.839  2.338   8.928  1.00 125.15 ? 266 PS6 D O1  1 
HETATM 7244 P P   . PS6 E 2 .   ? 20.320  0.939   9.528  1.00 121.12 ? 266 PS6 D P   1 
HETATM 7245 O O4  . PS6 E 2 .   ? 21.560  0.480   8.889  1.00 154.18 ? 266 PS6 D O4  1 
HETATM 7246 O O3  . PS6 E 2 .   ? 19.113  -0.076  9.300  1.00 114.51 ? 266 PS6 D O3  1 
HETATM 7247 C C2  . PS6 E 2 .   ? 20.177  0.167   12.090 1.00 84.11  ? 266 PS6 D C2  1 
HETATM 7248 C C3  . PS6 E 2 .   ? 19.646  0.816   13.356 1.00 68.44  ? 266 PS6 D C3  1 
HETATM 7249 O O11 . PS6 E 2 .   ? 18.220  0.786   13.428 1.00 75.56  ? 266 PS6 D O11 1 
HETATM 7250 O O12 . PS6 E 2 .   ? 17.633  2.378   11.940 1.00 38.77  ? 266 PS6 D O12 1 
HETATM 7251 C C1  . PS6 E 2 .   ? 17.631  1.189   12.276 1.00 85.89  ? 266 PS6 D C1  1 
HETATM 7252 C C4  . PS6 E 2 .   ? 20.105  0.120   14.640 1.00 55.97  ? 266 PS6 D C4  1 
HETATM 7253 C C5  . PS6 E 2 .   ? 19.425  0.056   16.847 1.00 33.46  ? 266 PS6 D C5  1 
HETATM 7254 O O51 . PS6 E 2 .   ? 20.068  -0.995  16.870 1.00 74.71  ? 266 PS6 D O51 1 
HETATM 7255 O O52 . PS6 E 2 .   ? 19.192  0.624   15.641 1.00 53.81  ? 266 PS6 D O52 1 
HETATM 7256 C C13 . PS6 E 2 .   ? 16.944  0.106   11.433 1.00 100.05 ? 266 PS6 D C13 1 
HETATM 7257 C C14 . PS6 E 2 .   ? 17.224  -1.288  12.023 1.00 103.90 ? 266 PS6 D C14 1 
HETATM 7258 C C15 . PS6 E 2 .   ? 17.311  -2.325  10.906 1.00 114.37 ? 266 PS6 D C15 1 
HETATM 7259 N N   . PS6 E 2 .   ? 23.023  3.705   7.865  1.00 114.43 ? 266 PS6 D N   1 
HETATM 7260 C CA  . PS6 E 2 .   ? 21.807  3.812   8.686  1.00 113.78 ? 266 PS6 D CA  1 
HETATM 7261 C CB  . PS6 E 2 .   ? 20.643  3.097   8.005  1.00 121.59 ? 266 PS6 D CB  1 
HETATM 7262 C C   . PS6 E 2 .   ? 21.480  5.281   8.956  1.00 99.85  ? 266 PS6 D C   1 
HETATM 7263 O O   . PS6 E 2 .   ? 22.444  6.053   9.186  1.00 52.16  ? 266 PS6 D O   1 
HETATM 7264 O OXT . PS6 E 2 .   ? 20.272  5.616   8.933  1.00 73.81  ? 266 PS6 D OXT 1 
HETATM 7265 C C16 . PS6 E 2 .   ? 18.263  -3.467  11.280 1.00 122.91 ? 266 PS6 D C16 1 
HETATM 7266 C C17 . PS6 E 2 .   ? 18.415  -4.441  10.086 1.00 138.58 ? 266 PS6 D C17 1 
HETATM 7267 C C6  . PS6 E 2 .   ? 18.891  0.714   18.114 1.00 26.86  ? 266 PS6 D C6  1 
HETATM 7268 C C7  . PS6 E 2 .   ? 19.497  0.085   19.374 1.00 30.93  ? 266 PS6 D C7  1 
HETATM 7269 C C8  . PS6 E 2 .   ? 18.758  0.527   20.627 1.00 29.92  ? 266 PS6 D C8  1 
HETATM 7270 C C9  . PS6 E 2 .   ? 19.255  -0.149  21.894 1.00 27.66  ? 266 PS6 D C9  1 
HETATM 7271 C C10 . PS6 E 2 .   ? 19.425  0.835   23.046 1.00 32.35  ? 266 PS6 D C10 1 
HETATM 7272 C C18 . PS6 E 2 .   ? 19.458  0.146   24.409 1.00 31.87  ? 266 PS6 D C18 1 
HETATM 7273 C C19 . PS6 E 2 .   ? 18.622  0.956   25.406 1.00 35.57  ? 266 PS6 D C19 1 
HETATM 7274 C C20 . PS6 E 2 .   ? 18.203  0.123   26.608 1.00 41.37  ? 266 PS6 D C20 1 
HETATM 7275 C C21 . PS6 E 2 .   ? 18.539  0.823   27.930 1.00 50.79  ? 266 PS6 D C21 1 
HETATM 7276 C C22 . PS6 E 2 .   ? 18.090  -0.015  29.127 1.00 54.50  ? 266 PS6 D C22 1 
HETATM 7277 C C23 . PS6 E 2 .   ? 18.008  0.796   30.424 1.00 57.96  ? 266 PS6 D C23 1 
HETATM 7278 C C24 . PS6 E 2 .   ? 18.358  -0.064  31.637 1.00 62.26  ? 266 PS6 D C24 1 
HETATM 7279 C C25 . PS6 E 2 .   ? 19.171  0.699   32.690 1.00 70.21  ? 266 PS6 D C25 1 
HETATM 7280 O O   . HOH F 3 .   ? 2.864   -7.439  31.856 1.00 53.09  ? 266 HOH A O   1 
HETATM 7281 O O   . HOH F 3 .   ? 3.447   -8.712  27.779 1.00 36.22  ? 267 HOH A O   1 
HETATM 7282 O O   . HOH F 3 .   ? 3.491   -8.089  24.790 1.00 24.31  ? 268 HOH A O   1 
HETATM 7283 O O   . HOH F 3 .   ? 3.629   -8.251  22.079 1.00 44.59  ? 269 HOH A O   1 
HETATM 7284 O O   . HOH F 3 .   ? 3.903   -8.305  35.717 1.00 45.98  ? 270 HOH A O   1 
HETATM 7285 O O   . HOH F 3 .   ? 4.560   -7.537  39.495 1.00 68.34  ? 271 HOH A O   1 
HETATM 7286 O O   . HOH F 3 .   ? 7.927   -8.872  43.948 1.00 19.37  ? 272 HOH A O   1 
HETATM 7287 O O   . HOH F 3 .   ? 14.306  -10.176 39.083 1.00 27.69  ? 273 HOH A O   1 
HETATM 7288 O O   . HOH F 3 .   ? 5.960   -7.967  18.840 1.00 37.25  ? 274 HOH A O   1 
HETATM 7289 O O   . HOH F 3 .   ? 7.236   -7.812  16.909 1.00 36.67  ? 275 HOH A O   1 
HETATM 7290 O O   . HOH F 3 .   ? 13.915  1.435   17.788 1.00 13.33  ? 276 HOH A O   1 
HETATM 7291 O O   . HOH F 3 .   ? 11.067  3.132   21.628 1.00 35.94  ? 277 HOH A O   1 
HETATM 7292 O O   . HOH F 3 .   ? -6.224  -20.596 7.816  1.00 49.06  ? 278 HOH A O   1 
HETATM 7293 O O   . HOH F 3 .   ? -2.113  -16.428 4.818  1.00 46.88  ? 279 HOH A O   1 
HETATM 7294 O O   . HOH F 3 .   ? -3.307  -14.049 8.930  1.00 32.12  ? 280 HOH A O   1 
HETATM 7295 O O   . HOH F 3 .   ? -5.344  -14.095 6.640  1.00 64.58  ? 281 HOH A O   1 
HETATM 7296 O O   . HOH F 3 .   ? -9.324  -17.285 8.723  1.00 35.20  ? 282 HOH A O   1 
HETATM 7297 O O   . HOH F 3 .   ? 6.759   -14.929 45.563 1.00 32.61  ? 283 HOH A O   1 
HETATM 7298 O O   . HOH F 3 .   ? 17.305  -17.307 50.895 1.00 88.22  ? 284 HOH A O   1 
HETATM 7299 O O   . HOH F 3 .   ? 1.235   -11.582 43.319 1.00 33.86  ? 285 HOH A O   1 
HETATM 7300 O O   . HOH F 3 .   ? 9.137   -9.599  13.345 1.00 54.21  ? 286 HOH A O   1 
HETATM 7301 O O   . HOH F 3 .   ? 10.405  -5.948  12.608 1.00 70.91  ? 287 HOH A O   1 
HETATM 7302 O O   . HOH F 3 .   ? 5.079   -7.789  41.756 1.00 50.60  ? 288 HOH A O   1 
HETATM 7303 O O   . HOH F 3 .   ? 6.331   -7.170  43.658 1.00 63.90  ? 289 HOH A O   1 
HETATM 7304 O O   . HOH F 3 .   ? 3.824   -7.926  46.033 1.00 78.00  ? 290 HOH A O   1 
HETATM 7305 O O   . HOH F 3 .   ? 9.769   -7.892  45.094 1.00 32.93  ? 291 HOH A O   1 
HETATM 7306 O O   . HOH G 3 .   ? 27.922  25.494  44.214 1.00 45.32  ? 266 HOH B O   1 
HETATM 7307 O O   . HOH G 3 .   ? 32.393  9.717   42.661 1.00 89.86  ? 267 HOH B O   1 
HETATM 7308 O O   . HOH G 3 .   ? 33.723  8.404   28.410 1.00 53.74  ? 268 HOH B O   1 
HETATM 7309 O O   . HOH G 3 .   ? 34.479  8.964   26.103 1.00 54.97  ? 269 HOH B O   1 
HETATM 7310 O O   . HOH G 3 .   ? 33.985  9.200   23.579 1.00 33.27  ? 270 HOH B O   1 
HETATM 7311 O O   . HOH G 3 .   ? 32.861  8.592   20.069 1.00 47.12  ? 271 HOH B O   1 
HETATM 7312 O O   . HOH G 3 .   ? 33.584  13.908  11.383 1.00 38.80  ? 272 HOH B O   1 
HETATM 7313 O O   . HOH G 3 .   ? 27.233  -2.806  22.046 1.00 27.18  ? 273 HOH B O   1 
HETATM 7314 O O   . HOH G 3 .   ? 22.561  11.165  39.270 1.00 44.95  ? 274 HOH B O   1 
HETATM 7315 O O   . HOH G 3 .   ? 41.024  13.489  8.615  1.00 79.41  ? 275 HOH B O   1 
HETATM 7316 O O   . HOH G 3 .   ? 37.641  4.014   35.500 1.00 139.86 ? 276 HOH B O   1 
HETATM 7317 O O   . HOH G 3 .   ? 34.837  9.117   33.571 1.00 51.49  ? 277 HOH B O   1 
HETATM 7318 O O   . HOH G 3 .   ? 34.908  -4.073  12.958 1.00 48.64  ? 278 HOH B O   1 
HETATM 7319 O O   . HOH G 3 .   ? 40.813  -4.628  51.693 1.00 42.38  ? 279 HOH B O   1 
HETATM 7320 O O   . HOH G 3 .   ? 25.178  -1.301  18.560 1.00 31.52  ? 280 HOH B O   1 
HETATM 7321 O O   . HOH G 3 .   ? 32.089  10.753  45.145 1.00 44.99  ? 281 HOH B O   1 
HETATM 7322 O O   . HOH G 3 .   ? 29.948  13.810  44.795 1.00 54.35  ? 282 HOH B O   1 
HETATM 7323 O O   . HOH G 3 .   ? 42.147  16.165  7.104  1.00 96.18  ? 283 HOH B O   1 
HETATM 7324 O O   . HOH G 3 .   ? 39.872  15.420  5.076  1.00 99.85  ? 284 HOH B O   1 
HETATM 7325 O O   . HOH G 3 .   ? 42.525  14.736  10.414 1.00 30.00  ? 285 HOH B O   1 
HETATM 7326 O O   . HOH G 3 .   ? 41.731  11.522  7.376  1.00 57.94  ? 286 HOH B O   1 
HETATM 7327 O O   . HOH G 3 .   ? 43.353  17.384  1.910  1.00 89.51  ? 287 HOH B O   1 
HETATM 7328 O O   . HOH G 3 .   ? 48.991  17.674  11.005 1.00 35.84  ? 288 HOH B O   1 
HETATM 7329 O O   . HOH G 3 .   ? 41.603  -5.250  7.663  1.00 60.61  ? 289 HOH B O   1 
HETATM 7330 O O   . HOH G 3 .   ? 37.487  -4.549  7.558  1.00 46.49  ? 290 HOH B O   1 
HETATM 7331 O O   . HOH G 3 .   ? 34.767  -4.568  10.536 1.00 33.57  ? 291 HOH B O   1 
HETATM 7332 O O   . HOH G 3 .   ? 32.490  9.912   50.967 1.00 151.46 ? 292 HOH B O   1 
HETATM 7333 O O   . HOH H 3 .   ? 28.742  -3.223  39.888 1.00 29.72  ? 266 HOH C O   1 
HETATM 7334 O O   . HOH H 3 .   ? 28.080  -10.679 16.231 1.00 74.24  ? 267 HOH C O   1 
HETATM 7335 O O   . HOH H 3 .   ? 28.109  -14.490 23.121 1.00 54.72  ? 268 HOH C O   1 
HETATM 7336 O O   . HOH H 3 .   ? 28.020  -14.902 28.501 1.00 40.54  ? 269 HOH C O   1 
HETATM 7337 O O   . HOH H 3 .   ? 27.153  -15.103 33.988 1.00 36.76  ? 270 HOH C O   1 
HETATM 7338 O O   . HOH H 3 .   ? 27.026  -14.248 36.842 1.00 29.61  ? 271 HOH C O   1 
HETATM 7339 O O   . HOH H 3 .   ? 27.530  -16.171 14.847 1.00 48.08  ? 272 HOH C O   1 
HETATM 7340 O O   . HOH H 3 .   ? 28.958  -7.095  16.565 1.00 42.87  ? 273 HOH C O   1 
HETATM 7341 O O   . HOH H 3 .   ? 26.413  -12.781 39.636 1.00 61.93  ? 274 HOH C O   1 
HETATM 7342 O O   . HOH H 3 .   ? 25.279  -12.251 43.348 1.00 36.57  ? 275 HOH C O   1 
HETATM 7343 O O   . HOH H 3 .   ? 16.219  -7.571  21.430 1.00 28.90  ? 276 HOH C O   1 
HETATM 7344 O O   . HOH H 3 .   ? 26.162  -14.637 31.971 1.00 76.72  ? 277 HOH C O   1 
HETATM 7345 O O   . HOH H 3 .   ? 21.751  -13.822 46.025 1.00 41.84  ? 278 HOH C O   1 
HETATM 7346 O O   . HOH H 3 .   ? 20.732  -0.575  41.812 1.00 26.03  ? 279 HOH C O   1 
HETATM 7347 O O   . HOH H 3 .   ? 27.852  -14.525 26.172 1.00 50.48  ? 280 HOH C O   1 
HETATM 7348 O O   . HOH H 3 .   ? 29.360  -28.354 12.110 1.00 26.52  ? 281 HOH C O   1 
HETATM 7349 O O   . HOH H 3 .   ? 38.413  -14.508 10.149 1.00 79.61  ? 282 HOH C O   1 
HETATM 7350 O O   . HOH H 3 .   ? 44.020  -17.018 47.477 1.00 53.04  ? 283 HOH C O   1 
HETATM 7351 O O   . HOH H 3 .   ? 41.172  -9.192  45.240 1.00 68.32  ? 284 HOH C O   1 
HETATM 7352 O O   . HOH H 3 .   ? 27.473  -16.479 41.889 1.00 33.56  ? 285 HOH C O   1 
HETATM 7353 O O   . HOH H 3 .   ? 24.491  -16.501 9.004  1.00 36.48  ? 286 HOH C O   1 
HETATM 7354 O O   . HOH H 3 .   ? 18.615  -21.535 2.879  1.00 69.77  ? 287 HOH C O   1 
HETATM 7355 O O   . HOH H 3 .   ? 24.629  -13.449 46.180 1.00 98.16  ? 288 HOH C O   1 
HETATM 7356 O O   . HOH H 3 .   ? 21.878  -22.170 8.530  1.00 46.62  ? 289 HOH C O   1 
HETATM 7357 O O   . HOH H 3 .   ? 24.269  -19.195 48.119 1.00 90.46  ? 290 HOH C O   1 
HETATM 7358 O O   . HOH H 3 .   ? 16.675  -14.223 12.700 1.00 42.37  ? 291 HOH C O   1 
HETATM 7359 O O   . HOH H 3 .   ? 17.443  -8.327  24.076 1.00 20.12  ? 292 HOH C O   1 
HETATM 7360 O O   . HOH H 3 .   ? 32.734  -25.511 47.203 1.00 59.25  ? 293 HOH C O   1 
HETATM 7361 O O   . HOH H 3 .   ? 32.014  -21.041 39.432 1.00 36.54  ? 294 HOH C O   1 
HETATM 7362 O O   . HOH H 3 .   ? 32.397  -23.517 41.235 1.00 43.65  ? 295 HOH C O   1 
HETATM 7363 O O   . HOH H 3 .   ? 15.413  -17.688 7.779  1.00 126.26 ? 296 HOH C O   1 
HETATM 7364 O O   . HOH H 3 .   ? 27.811  -12.786 19.930 1.00 67.91  ? 297 HOH C O   1 
HETATM 7365 O O   . HOH I 3 .   ? 10.923  12.236  16.835 1.00 48.84  ? 267 HOH D O   1 
HETATM 7366 O O   . HOH I 3 .   ? 10.741  14.289  19.528 1.00 33.35  ? 268 HOH D O   1 
HETATM 7367 O O   . HOH I 3 .   ? 10.264  15.018  21.887 1.00 43.94  ? 269 HOH D O   1 
HETATM 7368 O O   . HOH I 3 .   ? 10.312  15.713  24.953 1.00 40.58  ? 270 HOH D O   1 
HETATM 7369 O O   . HOH I 3 .   ? 10.098  15.722  27.371 1.00 40.86  ? 271 HOH D O   1 
HETATM 7370 O O   . HOH I 3 .   ? 8.749   9.396   12.789 1.00 36.30  ? 272 HOH D O   1 
HETATM 7371 O O   . HOH I 3 .   ? 24.161  15.308  9.613  1.00 82.73  ? 273 HOH D O   1 
HETATM 7372 O O   . HOH I 3 .   ? 9.316   12.399  15.214 1.00 118.26 ? 274 HOH D O   1 
HETATM 7373 O O   . HOH I 3 .   ? 22.250  8.672   21.327 1.00 38.69  ? 275 HOH D O   1 
HETATM 7374 O O   . HOH I 3 .   ? 10.615  18.957  42.859 1.00 62.41  ? 276 HOH D O   1 
HETATM 7375 O O   . HOH I 3 .   ? 8.915   17.664  40.766 1.00 35.26  ? 277 HOH D O   1 
HETATM 7376 O O   . HOH I 3 .   ? 10.095  15.359  36.097 1.00 30.37  ? 278 HOH D O   1 
HETATM 7377 O O   . HOH I 3 .   ? 3.792   22.998  5.207  1.00 78.81  ? 279 HOH D O   1 
HETATM 7378 O O   . HOH I 3 .   ? 10.040  2.302   23.590 1.00 18.14  ? 280 HOH D O   1 
HETATM 7379 O O   . HOH I 3 .   ? 13.523  18.388  45.658 1.00 44.60  ? 281 HOH D O   1 
HETATM 7380 O O   . HOH I 3 .   ? 6.130   13.025  43.022 1.00 39.67  ? 282 HOH D O   1 
HETATM 7381 O O   . HOH I 3 .   ? 19.501  23.882  8.524  1.00 55.33  ? 283 HOH D O   1 
HETATM 7382 O O   . HOH I 3 .   ? 17.564  21.835  7.988  1.00 38.02  ? 284 HOH D O   1 
HETATM 7383 O O   . HOH I 3 .   ? 16.816  19.000  9.393  1.00 54.11  ? 285 HOH D O   1 
HETATM 7384 O O   . HOH I 3 .   ? 24.526  18.909  6.263  1.00 51.24  ? 286 HOH D O   1 
HETATM 7385 O O   . HOH I 3 .   ? 26.499  10.265  15.987 1.00 42.41  ? 287 HOH D O   1 
HETATM 7386 O O   . HOH I 3 .   ? 11.115  15.897  30.471 1.00 59.81  ? 288 HOH D O   1 
HETATM 7387 O O   . HOH I 3 .   ? 9.697   14.701  38.885 1.00 45.86  ? 289 HOH D O   1 
HETATM 7388 O O   . HOH I 3 .   ? 2.690   11.554  45.416 1.00 31.62  ? 290 HOH D O   1 
HETATM 7389 O O   . HOH I 3 .   ? 3.486   14.065  44.658 1.00 44.23  ? 291 HOH D O   1 
HETATM 7390 O O   . HOH I 3 .   ? 6.164   17.411  43.044 1.00 40.98  ? 292 HOH D O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   0   ?   ?   ?   A . n 
A 1 2   SER 2   1   1   SER SER A . n 
A 1 3   LYS 3   2   2   LYS LYS A . n 
A 1 4   LYS 4   3   3   LYS LYS A . n 
A 1 5   GLU 5   4   4   GLU GLU A . n 
A 1 6   VAL 6   5   5   VAL VAL A . n 
A 1 7   CYS 7   6   6   CYS CYS A . n 
A 1 8   SER 8   7   7   SER SER A . n 
A 1 9   VAL 9   8   8   VAL VAL A . n 
A 1 10  ALA 10  9   9   ALA ALA A . n 
A 1 11  PHE 11  10  10  PHE PHE A . n 
A 1 12  LEU 12  11  11  LEU LEU A . n 
A 1 13  LYS 13  12  12  LYS LYS A . n 
A 1 14  ALA 14  13  13  ALA ALA A . n 
A 1 15  VAL 15  14  14  VAL VAL A . n 
A 1 16  PHE 16  15  15  PHE PHE A . n 
A 1 17  ALA 17  16  16  ALA ALA A . n 
A 1 18  GLU 18  17  17  GLU GLU A . n 
A 1 19  PHE 19  18  18  PHE PHE A . n 
A 1 20  LEU 20  19  19  LEU LEU A . n 
A 1 21  ALA 21  20  20  ALA ALA A . n 
A 1 22  THR 22  21  21  THR THR A . n 
A 1 23  LEU 23  22  22  LEU LEU A . n 
A 1 24  ILE 24  23  23  ILE ILE A . n 
A 1 25  PHE 25  24  24  PHE PHE A . n 
A 1 26  VAL 26  25  25  VAL VAL A . n 
A 1 27  PHE 27  26  26  PHE PHE A . n 
A 1 28  PHE 28  27  27  PHE PHE A . n 
A 1 29  GLY 29  28  28  GLY GLY A . n 
A 1 30  LEU 30  29  29  LEU LEU A . n 
A 1 31  GLY 31  30  30  GLY GLY A . n 
A 1 32  SER 32  31  31  SER SER A . n 
A 1 33  ALA 33  32  32  ALA ALA A . n 
A 1 34  LEU 34  33  33  LEU LEU A . n 
A 1 35  LYS 35  34  34  LYS LYS A . n 
A 1 36  TRP 36  35  35  TRP TRP A . n 
A 1 37  PRO 37  36  36  PRO PRO A . n 
A 1 38  SER 38  37  37  SER SER A . n 
A 1 39  ALA 39  38  38  ALA ALA A . n 
A 1 40  LEU 40  39  39  LEU LEU A . n 
A 1 41  PRO 41  40  40  PRO PRO A . n 
A 1 42  THR 42  41  41  THR THR A . n 
A 1 43  ILE 43  42  42  ILE ILE A . n 
A 1 44  LEU 44  43  43  LEU LEU A . n 
A 1 45  GLN 45  44  44  GLN GLN A . n 
A 1 46  ILE 46  45  45  ILE ILE A . n 
A 1 47  ALA 47  46  46  ALA ALA A . n 
A 1 48  LEU 48  47  47  LEU LEU A . n 
A 1 49  ALA 49  48  48  ALA ALA A . n 
A 1 50  PHE 50  49  49  PHE PHE A . n 
A 1 51  GLY 51  50  50  GLY GLY A . n 
A 1 52  LEU 52  51  51  LEU LEU A . n 
A 1 53  ALA 53  52  52  ALA ALA A . n 
A 1 54  ILE 54  53  53  ILE ILE A . n 
A 1 55  GLY 55  54  54  GLY GLY A . n 
A 1 56  THR 56  55  55  THR THR A . n 
A 1 57  LEU 57  56  56  LEU LEU A . n 
A 1 58  ALA 58  57  57  ALA ALA A . n 
A 1 59  GLN 59  58  58  GLN GLN A . n 
A 1 60  ALA 60  59  59  ALA ALA A . n 
A 1 61  LEU 61  60  60  LEU LEU A . n 
A 1 62  GLY 62  61  61  GLY GLY A . n 
A 1 63  PRO 63  62  62  PRO PRO A . n 
A 1 64  VAL 64  63  63  VAL VAL A . n 
A 1 65  SER 65  64  64  SER SER A . n 
A 1 66  GLY 66  65  65  GLY GLY A . n 
A 1 67  GLY 67  66  66  GLY GLY A . n 
A 1 68  HIS 68  67  67  HIS HIS A . n 
A 1 69  ILE 69  68  68  ILE ILE A . n 
A 1 70  ASN 70  69  69  ASN ASN A . n 
A 1 71  PRO 71  70  70  PRO PRO A . n 
A 1 72  ALA 72  71  71  ALA ALA A . n 
A 1 73  ILE 73  72  72  ILE ILE A . n 
A 1 74  THR 74  73  73  THR THR A . n 
A 1 75  LEU 75  74  74  LEU LEU A . n 
A 1 76  ALA 76  75  75  ALA ALA A . n 
A 1 77  LEU 77  76  76  LEU LEU A . n 
A 1 78  LEU 78  77  77  LEU LEU A . n 
A 1 79  VAL 79  78  78  VAL VAL A . n 
A 1 80  GLY 80  79  79  GLY GLY A . n 
A 1 81  ASN 81  80  80  ASN ASN A . n 
A 1 82  GLN 82  81  81  GLN GLN A . n 
A 1 83  ILE 83  82  82  ILE ILE A . n 
A 1 84  SER 84  83  83  SER SER A . n 
A 1 85  LEU 85  84  84  LEU LEU A . n 
A 1 86  LEU 86  85  85  LEU LEU A . n 
A 1 87  ARG 87  86  86  ARG ARG A . n 
A 1 88  ALA 88  87  87  ALA ALA A . n 
A 1 89  PHE 89  88  88  PHE PHE A . n 
A 1 90  PHE 90  89  89  PHE PHE A . n 
A 1 91  TYR 91  90  90  TYR TYR A . n 
A 1 92  VAL 92  91  91  VAL VAL A . n 
A 1 93  ALA 93  92  92  ALA ALA A . n 
A 1 94  ALA 94  93  93  ALA ALA A . n 
A 1 95  GLN 95  94  94  GLN GLN A . n 
A 1 96  LEU 96  95  95  LEU LEU A . n 
A 1 97  VAL 97  96  96  VAL VAL A . n 
A 1 98  GLY 98  97  97  GLY GLY A . n 
A 1 99  ALA 99  98  98  ALA ALA A . n 
A 1 100 ILE 100 99  99  ILE ILE A . n 
A 1 101 ALA 101 100 100 ALA ALA A . n 
A 1 102 GLY 102 101 101 GLY GLY A . n 
A 1 103 ALA 103 102 102 ALA ALA A . n 
A 1 104 GLY 104 103 103 GLY GLY A . n 
A 1 105 ILE 105 104 104 ILE ILE A . n 
A 1 106 LEU 106 105 105 LEU LEU A . n 
A 1 107 TYR 107 106 106 TYR TYR A . n 
A 1 108 GLY 108 107 107 GLY GLY A . n 
A 1 109 VAL 109 108 108 VAL VAL A . n 
A 1 110 ALA 110 109 109 ALA ALA A . n 
A 1 111 PRO 111 110 110 PRO PRO A . n 
A 1 112 LEU 112 111 111 LEU LEU A . n 
A 1 113 ASN 113 112 112 ASN ASN A . n 
A 1 114 ALA 114 113 113 ALA ALA A . n 
A 1 115 ARG 115 114 114 ARG ARG A . n 
A 1 116 GLY 116 115 115 GLY GLY A . n 
A 1 117 ASN 117 116 116 ASN ASN A . n 
A 1 118 LEU 118 117 117 LEU LEU A . n 
A 1 119 ALA 119 118 118 ALA ALA A . n 
A 1 120 VAL 120 119 119 VAL VAL A . n 
A 1 121 ASN 121 120 120 ASN ASN A . n 
A 1 122 ALA 122 121 121 ALA ALA A . n 
A 1 123 LEU 123 122 122 LEU LEU A . n 
A 1 124 ASN 124 123 123 ASN ASN A . n 
A 1 125 ASN 125 124 124 ASN ASN A . n 
A 1 126 ASN 126 125 125 ASN ASN A . n 
A 1 127 THR 127 126 126 THR THR A . n 
A 1 128 THR 128 127 127 THR THR A . n 
A 1 129 GLN 129 128 128 GLN GLN A . n 
A 1 130 GLY 130 129 129 GLY GLY A . n 
A 1 131 GLN 131 130 130 GLN GLN A . n 
A 1 132 ALA 132 131 131 ALA ALA A . n 
A 1 133 MET 133 132 132 MET MET A . n 
A 1 134 VAL 134 133 133 VAL VAL A . n 
A 1 135 VAL 135 134 134 VAL VAL A . n 
A 1 136 GLU 136 135 135 GLU GLU A . n 
A 1 137 LEU 137 136 136 LEU LEU A . n 
A 1 138 ILE 138 137 137 ILE ILE A . n 
A 1 139 LEU 139 138 138 LEU LEU A . n 
A 1 140 THR 140 139 139 THR THR A . n 
A 1 141 PHE 141 140 140 PHE PHE A . n 
A 1 142 GLN 142 141 141 GLN GLN A . n 
A 1 143 LEU 143 142 142 LEU LEU A . n 
A 1 144 ALA 144 143 143 ALA ALA A . n 
A 1 145 LEU 145 144 144 LEU LEU A . n 
A 1 146 CYS 146 145 145 CYS CYS A . n 
A 1 147 ILE 147 146 146 ILE ILE A . n 
A 1 148 PHE 148 147 147 PHE PHE A . n 
A 1 149 ALA 149 148 148 ALA ALA A . n 
A 1 150 SER 150 149 149 SER SER A . n 
A 1 151 THR 151 150 150 THR THR A . n 
A 1 152 ASP 152 151 151 ASP ASP A . n 
A 1 153 SER 153 152 152 SER SER A . n 
A 1 154 ARG 154 153 153 ARG ARG A . n 
A 1 155 ARG 155 154 154 ARG ARG A . n 
A 1 156 THR 156 155 155 THR THR A . n 
A 1 157 SER 157 156 156 SER SER A . n 
A 1 158 PRO 158 157 157 PRO PRO A . n 
A 1 159 VAL 159 158 158 VAL VAL A . n 
A 1 160 GLY 160 159 159 GLY GLY A . n 
A 1 161 SER 161 160 160 SER SER A . n 
A 1 162 PRO 162 161 161 PRO PRO A . n 
A 1 163 ALA 163 162 162 ALA ALA A . n 
A 1 164 LEU 164 163 163 LEU LEU A . n 
A 1 165 SER 165 164 164 SER SER A . n 
A 1 166 ILE 166 165 165 ILE ILE A . n 
A 1 167 GLY 167 166 166 GLY GLY A . n 
A 1 168 LEU 168 167 167 LEU LEU A . n 
A 1 169 SER 169 168 168 SER SER A . n 
A 1 170 VAL 170 169 169 VAL VAL A . n 
A 1 171 THR 171 170 170 THR THR A . n 
A 1 172 LEU 172 171 171 LEU LEU A . n 
A 1 173 GLY 173 172 172 GLY GLY A . n 
A 1 174 HIS 174 173 173 HIS HIS A . n 
A 1 175 LEU 175 174 174 LEU LEU A . n 
A 1 176 VAL 176 175 175 VAL VAL A . n 
A 1 177 GLY 177 176 176 GLY GLY A . n 
A 1 178 ILE 178 177 177 ILE ILE A . n 
A 1 179 TYR 179 178 178 TYR TYR A . n 
A 1 180 PHE 180 179 179 PHE PHE A . n 
A 1 181 THR 181 180 180 THR THR A . n 
A 1 182 GLY 182 181 181 GLY GLY A . n 
A 1 183 CYS 183 182 182 CYS CYS A . n 
A 1 184 SER 184 183 183 SER SER A . n 
A 1 185 MET 185 184 184 MET MET A . n 
A 1 186 ASN 186 185 185 ASN ASN A . n 
A 1 187 PRO 187 186 186 PRO PRO A . n 
A 1 188 ALA 188 187 187 ALA ALA A . n 
A 1 189 ARG 189 188 188 ARG ARG A . n 
A 1 190 SER 190 189 189 SER SER A . n 
A 1 191 PHE 191 190 190 PHE PHE A . n 
A 1 192 GLY 192 191 191 GLY GLY A . n 
A 1 193 PRO 193 192 192 PRO PRO A . n 
A 1 194 ALA 194 193 193 ALA ALA A . n 
A 1 195 VAL 195 194 194 VAL VAL A . n 
A 1 196 VAL 196 195 195 VAL VAL A . n 
A 1 197 MET 197 196 196 MET MET A . n 
A 1 198 ASN 198 197 197 ASN ASN A . n 
A 1 199 ARG 199 198 198 ARG ARG A . n 
A 1 200 PHE 200 199 199 PHE PHE A . n 
A 1 201 SER 201 200 200 SER SER A . n 
A 1 202 PRO 202 201 201 PRO PRO A . n 
A 1 203 ALA 203 202 202 ALA ALA A . n 
A 1 204 HIS 204 203 203 HIS HIS A . n 
A 1 205 TRP 205 204 204 TRP TRP A . n 
A 1 206 VAL 206 205 205 VAL VAL A . n 
A 1 207 PHE 207 206 206 PHE PHE A . n 
A 1 208 TRP 208 207 207 TRP TRP A . n 
A 1 209 VAL 209 208 208 VAL VAL A . n 
A 1 210 GLY 210 209 209 GLY GLY A . n 
A 1 211 PRO 211 210 210 PRO PRO A . n 
A 1 212 ILE 212 211 211 ILE ILE A . n 
A 1 213 VAL 213 212 212 VAL VAL A . n 
A 1 214 GLY 214 213 213 GLY GLY A . n 
A 1 215 ALA 215 214 214 ALA ALA A . n 
A 1 216 VAL 216 215 215 VAL VAL A . n 
A 1 217 LEU 217 216 216 LEU LEU A . n 
A 1 218 ALA 218 217 217 ALA ALA A . n 
A 1 219 ALA 219 218 218 ALA ALA A . n 
A 1 220 ILE 220 219 219 ILE ILE A . n 
A 1 221 LEU 221 220 220 LEU LEU A . n 
A 1 222 TYR 222 221 221 TYR TYR A . n 
A 1 223 PHE 223 222 222 PHE PHE A . n 
A 1 224 TYR 224 223 223 TYR TYR A . n 
A 1 225 LEU 225 224 224 LEU LEU A . n 
A 1 226 LEU 226 225 225 LEU LEU A . n 
A 1 227 PHE 227 226 226 PHE PHE A . n 
A 1 228 PRO 228 227 227 PRO PRO A . n 
A 1 229 ASN 229 228 228 ASN ASN A . n 
A 1 230 SER 230 229 229 SER SER A . n 
A 1 231 LEU 231 230 230 LEU LEU A . n 
A 1 232 SER 232 231 231 SER SER A . n 
A 1 233 LEU 233 232 232 LEU LEU A . n 
A 1 234 SER 234 233 233 SER SER A . n 
A 1 235 GLU 235 234 234 GLU GLU A . n 
A 1 236 ARG 236 235 235 ARG ARG A . n 
A 1 237 VAL 237 236 236 VAL VAL A . n 
A 1 238 ALA 238 237 237 ALA ALA A . n 
A 1 239 ILE 239 238 238 ILE ILE A . n 
A 1 240 ILE 240 239 239 ILE ILE A . n 
A 1 241 LYS 241 240 240 LYS LYS A . n 
A 1 242 GLY 242 241 241 GLY GLY A . n 
A 1 243 THR 243 242 242 THR THR A . n 
A 1 244 TYR 244 243 243 TYR TYR A . n 
A 1 245 GLU 245 244 244 GLU GLU A . n 
A 1 246 PRO 246 245 245 PRO PRO A . n 
A 1 247 ASP 247 246 ?   ?   ?   A . n 
A 1 248 GLU 248 247 ?   ?   ?   A . n 
A 1 249 ASP 249 248 ?   ?   ?   A . n 
A 1 250 TRP 250 249 ?   ?   ?   A . n 
A 1 251 GLU 251 250 ?   ?   ?   A . n 
A 1 252 GLU 252 251 ?   ?   ?   A . n 
A 1 253 GLN 253 252 ?   ?   ?   A . n 
A 1 254 ARG 254 253 ?   ?   ?   A . n 
A 1 255 GLU 255 254 ?   ?   ?   A . n 
A 1 256 GLU 256 255 ?   ?   ?   A . n 
A 1 257 ARG 257 256 ?   ?   ?   A . n 
A 1 258 LYS 258 257 ?   ?   ?   A . n 
A 1 259 LYS 259 258 ?   ?   ?   A . n 
A 1 260 THR 260 259 ?   ?   ?   A . n 
A 1 261 MET 261 260 ?   ?   ?   A . n 
A 1 262 GLU 262 261 ?   ?   ?   A . n 
A 1 263 LEU 263 262 ?   ?   ?   A . n 
A 1 264 THR 264 263 ?   ?   ?   A . n 
A 1 265 THR 265 264 ?   ?   ?   A . n 
A 1 266 ARG 266 265 ?   ?   ?   A . n 
B 1 1   MET 1   0   ?   ?   ?   B . n 
B 1 2   SER 2   1   1   SER SER B . n 
B 1 3   LYS 3   2   2   LYS LYS B . n 
B 1 4   LYS 4   3   3   LYS LYS B . n 
B 1 5   GLU 5   4   4   GLU GLU B . n 
B 1 6   VAL 6   5   5   VAL VAL B . n 
B 1 7   CYS 7   6   6   CYS CYS B . n 
B 1 8   SER 8   7   7   SER SER B . n 
B 1 9   VAL 9   8   8   VAL VAL B . n 
B 1 10  ALA 10  9   9   ALA ALA B . n 
B 1 11  PHE 11  10  10  PHE PHE B . n 
B 1 12  LEU 12  11  11  LEU LEU B . n 
B 1 13  LYS 13  12  12  LYS LYS B . n 
B 1 14  ALA 14  13  13  ALA ALA B . n 
B 1 15  VAL 15  14  14  VAL VAL B . n 
B 1 16  PHE 16  15  15  PHE PHE B . n 
B 1 17  ALA 17  16  16  ALA ALA B . n 
B 1 18  GLU 18  17  17  GLU GLU B . n 
B 1 19  PHE 19  18  18  PHE PHE B . n 
B 1 20  LEU 20  19  19  LEU LEU B . n 
B 1 21  ALA 21  20  20  ALA ALA B . n 
B 1 22  THR 22  21  21  THR THR B . n 
B 1 23  LEU 23  22  22  LEU LEU B . n 
B 1 24  ILE 24  23  23  ILE ILE B . n 
B 1 25  PHE 25  24  24  PHE PHE B . n 
B 1 26  VAL 26  25  25  VAL VAL B . n 
B 1 27  PHE 27  26  26  PHE PHE B . n 
B 1 28  PHE 28  27  27  PHE PHE B . n 
B 1 29  GLY 29  28  28  GLY GLY B . n 
B 1 30  LEU 30  29  29  LEU LEU B . n 
B 1 31  GLY 31  30  30  GLY GLY B . n 
B 1 32  SER 32  31  31  SER SER B . n 
B 1 33  ALA 33  32  32  ALA ALA B . n 
B 1 34  LEU 34  33  33  LEU LEU B . n 
B 1 35  LYS 35  34  34  LYS LYS B . n 
B 1 36  TRP 36  35  35  TRP TRP B . n 
B 1 37  PRO 37  36  36  PRO PRO B . n 
B 1 38  SER 38  37  37  SER SER B . n 
B 1 39  ALA 39  38  38  ALA ALA B . n 
B 1 40  LEU 40  39  39  LEU LEU B . n 
B 1 41  PRO 41  40  40  PRO PRO B . n 
B 1 42  THR 42  41  41  THR THR B . n 
B 1 43  ILE 43  42  42  ILE ILE B . n 
B 1 44  LEU 44  43  43  LEU LEU B . n 
B 1 45  GLN 45  44  44  GLN GLN B . n 
B 1 46  ILE 46  45  45  ILE ILE B . n 
B 1 47  ALA 47  46  46  ALA ALA B . n 
B 1 48  LEU 48  47  47  LEU LEU B . n 
B 1 49  ALA 49  48  48  ALA ALA B . n 
B 1 50  PHE 50  49  49  PHE PHE B . n 
B 1 51  GLY 51  50  50  GLY GLY B . n 
B 1 52  LEU 52  51  51  LEU LEU B . n 
B 1 53  ALA 53  52  52  ALA ALA B . n 
B 1 54  ILE 54  53  53  ILE ILE B . n 
B 1 55  GLY 55  54  54  GLY GLY B . n 
B 1 56  THR 56  55  55  THR THR B . n 
B 1 57  LEU 57  56  56  LEU LEU B . n 
B 1 58  ALA 58  57  57  ALA ALA B . n 
B 1 59  GLN 59  58  58  GLN GLN B . n 
B 1 60  ALA 60  59  59  ALA ALA B . n 
B 1 61  LEU 61  60  60  LEU LEU B . n 
B 1 62  GLY 62  61  61  GLY GLY B . n 
B 1 63  PRO 63  62  62  PRO PRO B . n 
B 1 64  VAL 64  63  63  VAL VAL B . n 
B 1 65  SER 65  64  64  SER SER B . n 
B 1 66  GLY 66  65  65  GLY GLY B . n 
B 1 67  GLY 67  66  66  GLY GLY B . n 
B 1 68  HIS 68  67  67  HIS HIS B . n 
B 1 69  ILE 69  68  68  ILE ILE B . n 
B 1 70  ASN 70  69  69  ASN ASN B . n 
B 1 71  PRO 71  70  70  PRO PRO B . n 
B 1 72  ALA 72  71  71  ALA ALA B . n 
B 1 73  ILE 73  72  72  ILE ILE B . n 
B 1 74  THR 74  73  73  THR THR B . n 
B 1 75  LEU 75  74  74  LEU LEU B . n 
B 1 76  ALA 76  75  75  ALA ALA B . n 
B 1 77  LEU 77  76  76  LEU LEU B . n 
B 1 78  LEU 78  77  77  LEU LEU B . n 
B 1 79  VAL 79  78  78  VAL VAL B . n 
B 1 80  GLY 80  79  79  GLY GLY B . n 
B 1 81  ASN 81  80  80  ASN ASN B . n 
B 1 82  GLN 82  81  81  GLN GLN B . n 
B 1 83  ILE 83  82  82  ILE ILE B . n 
B 1 84  SER 84  83  83  SER SER B . n 
B 1 85  LEU 85  84  84  LEU LEU B . n 
B 1 86  LEU 86  85  85  LEU LEU B . n 
B 1 87  ARG 87  86  86  ARG ARG B . n 
B 1 88  ALA 88  87  87  ALA ALA B . n 
B 1 89  PHE 89  88  88  PHE PHE B . n 
B 1 90  PHE 90  89  89  PHE PHE B . n 
B 1 91  TYR 91  90  90  TYR TYR B . n 
B 1 92  VAL 92  91  91  VAL VAL B . n 
B 1 93  ALA 93  92  92  ALA ALA B . n 
B 1 94  ALA 94  93  93  ALA ALA B . n 
B 1 95  GLN 95  94  94  GLN GLN B . n 
B 1 96  LEU 96  95  95  LEU LEU B . n 
B 1 97  VAL 97  96  96  VAL VAL B . n 
B 1 98  GLY 98  97  97  GLY GLY B . n 
B 1 99  ALA 99  98  98  ALA ALA B . n 
B 1 100 ILE 100 99  99  ILE ILE B . n 
B 1 101 ALA 101 100 100 ALA ALA B . n 
B 1 102 GLY 102 101 101 GLY GLY B . n 
B 1 103 ALA 103 102 102 ALA ALA B . n 
B 1 104 GLY 104 103 103 GLY GLY B . n 
B 1 105 ILE 105 104 104 ILE ILE B . n 
B 1 106 LEU 106 105 105 LEU LEU B . n 
B 1 107 TYR 107 106 106 TYR TYR B . n 
B 1 108 GLY 108 107 107 GLY GLY B . n 
B 1 109 VAL 109 108 108 VAL VAL B . n 
B 1 110 ALA 110 109 109 ALA ALA B . n 
B 1 111 PRO 111 110 110 PRO PRO B . n 
B 1 112 LEU 112 111 111 LEU LEU B . n 
B 1 113 ASN 113 112 112 ASN ASN B . n 
B 1 114 ALA 114 113 113 ALA ALA B . n 
B 1 115 ARG 115 114 114 ARG ARG B . n 
B 1 116 GLY 116 115 115 GLY GLY B . n 
B 1 117 ASN 117 116 116 ASN ASN B . n 
B 1 118 LEU 118 117 117 LEU LEU B . n 
B 1 119 ALA 119 118 118 ALA ALA B . n 
B 1 120 VAL 120 119 119 VAL VAL B . n 
B 1 121 ASN 121 120 120 ASN ASN B . n 
B 1 122 ALA 122 121 121 ALA ALA B . n 
B 1 123 LEU 123 122 122 LEU LEU B . n 
B 1 124 ASN 124 123 123 ASN ASN B . n 
B 1 125 ASN 125 124 124 ASN ASN B . n 
B 1 126 ASN 126 125 125 ASN ASN B . n 
B 1 127 THR 127 126 126 THR THR B . n 
B 1 128 THR 128 127 127 THR THR B . n 
B 1 129 GLN 129 128 128 GLN GLN B . n 
B 1 130 GLY 130 129 129 GLY GLY B . n 
B 1 131 GLN 131 130 130 GLN GLN B . n 
B 1 132 ALA 132 131 131 ALA ALA B . n 
B 1 133 MET 133 132 132 MET MET B . n 
B 1 134 VAL 134 133 133 VAL VAL B . n 
B 1 135 VAL 135 134 134 VAL VAL B . n 
B 1 136 GLU 136 135 135 GLU GLU B . n 
B 1 137 LEU 137 136 136 LEU LEU B . n 
B 1 138 ILE 138 137 137 ILE ILE B . n 
B 1 139 LEU 139 138 138 LEU LEU B . n 
B 1 140 THR 140 139 139 THR THR B . n 
B 1 141 PHE 141 140 140 PHE PHE B . n 
B 1 142 GLN 142 141 141 GLN GLN B . n 
B 1 143 LEU 143 142 142 LEU LEU B . n 
B 1 144 ALA 144 143 143 ALA ALA B . n 
B 1 145 LEU 145 144 144 LEU LEU B . n 
B 1 146 CYS 146 145 145 CYS CYS B . n 
B 1 147 ILE 147 146 146 ILE ILE B . n 
B 1 148 PHE 148 147 147 PHE PHE B . n 
B 1 149 ALA 149 148 148 ALA ALA B . n 
B 1 150 SER 150 149 149 SER SER B . n 
B 1 151 THR 151 150 150 THR THR B . n 
B 1 152 ASP 152 151 151 ASP ASP B . n 
B 1 153 SER 153 152 152 SER SER B . n 
B 1 154 ARG 154 153 153 ARG ARG B . n 
B 1 155 ARG 155 154 154 ARG ARG B . n 
B 1 156 THR 156 155 155 THR THR B . n 
B 1 157 SER 157 156 156 SER SER B . n 
B 1 158 PRO 158 157 157 PRO PRO B . n 
B 1 159 VAL 159 158 158 VAL VAL B . n 
B 1 160 GLY 160 159 159 GLY GLY B . n 
B 1 161 SER 161 160 160 SER SER B . n 
B 1 162 PRO 162 161 161 PRO PRO B . n 
B 1 163 ALA 163 162 162 ALA ALA B . n 
B 1 164 LEU 164 163 163 LEU LEU B . n 
B 1 165 SER 165 164 164 SER SER B . n 
B 1 166 ILE 166 165 165 ILE ILE B . n 
B 1 167 GLY 167 166 166 GLY GLY B . n 
B 1 168 LEU 168 167 167 LEU LEU B . n 
B 1 169 SER 169 168 168 SER SER B . n 
B 1 170 VAL 170 169 169 VAL VAL B . n 
B 1 171 THR 171 170 170 THR THR B . n 
B 1 172 LEU 172 171 171 LEU LEU B . n 
B 1 173 GLY 173 172 172 GLY GLY B . n 
B 1 174 HIS 174 173 173 HIS HIS B . n 
B 1 175 LEU 175 174 174 LEU LEU B . n 
B 1 176 VAL 176 175 175 VAL VAL B . n 
B 1 177 GLY 177 176 176 GLY GLY B . n 
B 1 178 ILE 178 177 177 ILE ILE B . n 
B 1 179 TYR 179 178 178 TYR TYR B . n 
B 1 180 PHE 180 179 179 PHE PHE B . n 
B 1 181 THR 181 180 180 THR THR B . n 
B 1 182 GLY 182 181 181 GLY GLY B . n 
B 1 183 CYS 183 182 182 CYS CYS B . n 
B 1 184 SER 184 183 183 SER SER B . n 
B 1 185 MET 185 184 184 MET MET B . n 
B 1 186 ASN 186 185 185 ASN ASN B . n 
B 1 187 PRO 187 186 186 PRO PRO B . n 
B 1 188 ALA 188 187 187 ALA ALA B . n 
B 1 189 ARG 189 188 188 ARG ARG B . n 
B 1 190 SER 190 189 189 SER SER B . n 
B 1 191 PHE 191 190 190 PHE PHE B . n 
B 1 192 GLY 192 191 191 GLY GLY B . n 
B 1 193 PRO 193 192 192 PRO PRO B . n 
B 1 194 ALA 194 193 193 ALA ALA B . n 
B 1 195 VAL 195 194 194 VAL VAL B . n 
B 1 196 VAL 196 195 195 VAL VAL B . n 
B 1 197 MET 197 196 196 MET MET B . n 
B 1 198 ASN 198 197 197 ASN ASN B . n 
B 1 199 ARG 199 198 198 ARG ARG B . n 
B 1 200 PHE 200 199 199 PHE PHE B . n 
B 1 201 SER 201 200 200 SER SER B . n 
B 1 202 PRO 202 201 201 PRO PRO B . n 
B 1 203 ALA 203 202 202 ALA ALA B . n 
B 1 204 HIS 204 203 203 HIS HIS B . n 
B 1 205 TRP 205 204 204 TRP TRP B . n 
B 1 206 VAL 206 205 205 VAL VAL B . n 
B 1 207 PHE 207 206 206 PHE PHE B . n 
B 1 208 TRP 208 207 207 TRP TRP B . n 
B 1 209 VAL 209 208 208 VAL VAL B . n 
B 1 210 GLY 210 209 209 GLY GLY B . n 
B 1 211 PRO 211 210 210 PRO PRO B . n 
B 1 212 ILE 212 211 211 ILE ILE B . n 
B 1 213 VAL 213 212 212 VAL VAL B . n 
B 1 214 GLY 214 213 213 GLY GLY B . n 
B 1 215 ALA 215 214 214 ALA ALA B . n 
B 1 216 VAL 216 215 215 VAL VAL B . n 
B 1 217 LEU 217 216 216 LEU LEU B . n 
B 1 218 ALA 218 217 217 ALA ALA B . n 
B 1 219 ALA 219 218 218 ALA ALA B . n 
B 1 220 ILE 220 219 219 ILE ILE B . n 
B 1 221 LEU 221 220 220 LEU LEU B . n 
B 1 222 TYR 222 221 221 TYR TYR B . n 
B 1 223 PHE 223 222 222 PHE PHE B . n 
B 1 224 TYR 224 223 223 TYR TYR B . n 
B 1 225 LEU 225 224 224 LEU LEU B . n 
B 1 226 LEU 226 225 225 LEU LEU B . n 
B 1 227 PHE 227 226 226 PHE PHE B . n 
B 1 228 PRO 228 227 227 PRO PRO B . n 
B 1 229 ASN 229 228 228 ASN ASN B . n 
B 1 230 SER 230 229 229 SER SER B . n 
B 1 231 LEU 231 230 230 LEU LEU B . n 
B 1 232 SER 232 231 231 SER SER B . n 
B 1 233 LEU 233 232 232 LEU LEU B . n 
B 1 234 SER 234 233 233 SER SER B . n 
B 1 235 GLU 235 234 234 GLU GLU B . n 
B 1 236 ARG 236 235 235 ARG ARG B . n 
B 1 237 VAL 237 236 236 VAL VAL B . n 
B 1 238 ALA 238 237 237 ALA ALA B . n 
B 1 239 ILE 239 238 238 ILE ILE B . n 
B 1 240 ILE 240 239 239 ILE ILE B . n 
B 1 241 LYS 241 240 240 LYS LYS B . n 
B 1 242 GLY 242 241 241 GLY GLY B . n 
B 1 243 THR 243 242 242 THR THR B . n 
B 1 244 TYR 244 243 243 TYR TYR B . n 
B 1 245 GLU 245 244 244 GLU GLU B . n 
B 1 246 PRO 246 245 245 PRO PRO B . n 
B 1 247 ASP 247 246 ?   ?   ?   B . n 
B 1 248 GLU 248 247 ?   ?   ?   B . n 
B 1 249 ASP 249 248 ?   ?   ?   B . n 
B 1 250 TRP 250 249 ?   ?   ?   B . n 
B 1 251 GLU 251 250 ?   ?   ?   B . n 
B 1 252 GLU 252 251 ?   ?   ?   B . n 
B 1 253 GLN 253 252 ?   ?   ?   B . n 
B 1 254 ARG 254 253 ?   ?   ?   B . n 
B 1 255 GLU 255 254 ?   ?   ?   B . n 
B 1 256 GLU 256 255 ?   ?   ?   B . n 
B 1 257 ARG 257 256 ?   ?   ?   B . n 
B 1 258 LYS 258 257 ?   ?   ?   B . n 
B 1 259 LYS 259 258 ?   ?   ?   B . n 
B 1 260 THR 260 259 ?   ?   ?   B . n 
B 1 261 MET 261 260 ?   ?   ?   B . n 
B 1 262 GLU 262 261 ?   ?   ?   B . n 
B 1 263 LEU 263 262 ?   ?   ?   B . n 
B 1 264 THR 264 263 ?   ?   ?   B . n 
B 1 265 THR 265 264 ?   ?   ?   B . n 
B 1 266 ARG 266 265 ?   ?   ?   B . n 
C 1 1   MET 1   0   ?   ?   ?   C . n 
C 1 2   SER 2   1   ?   ?   ?   C . n 
C 1 3   LYS 3   2   ?   ?   ?   C . n 
C 1 4   LYS 4   3   3   LYS LYS C . n 
C 1 5   GLU 5   4   4   GLU GLU C . n 
C 1 6   VAL 6   5   5   VAL VAL C . n 
C 1 7   CYS 7   6   6   CYS CYS C . n 
C 1 8   SER 8   7   7   SER SER C . n 
C 1 9   VAL 9   8   8   VAL VAL C . n 
C 1 10  ALA 10  9   9   ALA ALA C . n 
C 1 11  PHE 11  10  10  PHE PHE C . n 
C 1 12  LEU 12  11  11  LEU LEU C . n 
C 1 13  LYS 13  12  12  LYS LYS C . n 
C 1 14  ALA 14  13  13  ALA ALA C . n 
C 1 15  VAL 15  14  14  VAL VAL C . n 
C 1 16  PHE 16  15  15  PHE PHE C . n 
C 1 17  ALA 17  16  16  ALA ALA C . n 
C 1 18  GLU 18  17  17  GLU GLU C . n 
C 1 19  PHE 19  18  18  PHE PHE C . n 
C 1 20  LEU 20  19  19  LEU LEU C . n 
C 1 21  ALA 21  20  20  ALA ALA C . n 
C 1 22  THR 22  21  21  THR THR C . n 
C 1 23  LEU 23  22  22  LEU LEU C . n 
C 1 24  ILE 24  23  23  ILE ILE C . n 
C 1 25  PHE 25  24  24  PHE PHE C . n 
C 1 26  VAL 26  25  25  VAL VAL C . n 
C 1 27  PHE 27  26  26  PHE PHE C . n 
C 1 28  PHE 28  27  27  PHE PHE C . n 
C 1 29  GLY 29  28  28  GLY GLY C . n 
C 1 30  LEU 30  29  29  LEU LEU C . n 
C 1 31  GLY 31  30  30  GLY GLY C . n 
C 1 32  SER 32  31  31  SER SER C . n 
C 1 33  ALA 33  32  32  ALA ALA C . n 
C 1 34  LEU 34  33  33  LEU LEU C . n 
C 1 35  LYS 35  34  34  LYS LYS C . n 
C 1 36  TRP 36  35  35  TRP TRP C . n 
C 1 37  PRO 37  36  36  PRO PRO C . n 
C 1 38  SER 38  37  37  SER SER C . n 
C 1 39  ALA 39  38  38  ALA ALA C . n 
C 1 40  LEU 40  39  39  LEU LEU C . n 
C 1 41  PRO 41  40  40  PRO PRO C . n 
C 1 42  THR 42  41  41  THR THR C . n 
C 1 43  ILE 43  42  42  ILE ILE C . n 
C 1 44  LEU 44  43  43  LEU LEU C . n 
C 1 45  GLN 45  44  44  GLN GLN C . n 
C 1 46  ILE 46  45  45  ILE ILE C . n 
C 1 47  ALA 47  46  46  ALA ALA C . n 
C 1 48  LEU 48  47  47  LEU LEU C . n 
C 1 49  ALA 49  48  48  ALA ALA C . n 
C 1 50  PHE 50  49  49  PHE PHE C . n 
C 1 51  GLY 51  50  50  GLY GLY C . n 
C 1 52  LEU 52  51  51  LEU LEU C . n 
C 1 53  ALA 53  52  52  ALA ALA C . n 
C 1 54  ILE 54  53  53  ILE ILE C . n 
C 1 55  GLY 55  54  54  GLY GLY C . n 
C 1 56  THR 56  55  55  THR THR C . n 
C 1 57  LEU 57  56  56  LEU LEU C . n 
C 1 58  ALA 58  57  57  ALA ALA C . n 
C 1 59  GLN 59  58  58  GLN GLN C . n 
C 1 60  ALA 60  59  59  ALA ALA C . n 
C 1 61  LEU 61  60  60  LEU LEU C . n 
C 1 62  GLY 62  61  61  GLY GLY C . n 
C 1 63  PRO 63  62  62  PRO PRO C . n 
C 1 64  VAL 64  63  63  VAL VAL C . n 
C 1 65  SER 65  64  64  SER SER C . n 
C 1 66  GLY 66  65  65  GLY GLY C . n 
C 1 67  GLY 67  66  66  GLY GLY C . n 
C 1 68  HIS 68  67  67  HIS HIS C . n 
C 1 69  ILE 69  68  68  ILE ILE C . n 
C 1 70  ASN 70  69  69  ASN ASN C . n 
C 1 71  PRO 71  70  70  PRO PRO C . n 
C 1 72  ALA 72  71  71  ALA ALA C . n 
C 1 73  ILE 73  72  72  ILE ILE C . n 
C 1 74  THR 74  73  73  THR THR C . n 
C 1 75  LEU 75  74  74  LEU LEU C . n 
C 1 76  ALA 76  75  75  ALA ALA C . n 
C 1 77  LEU 77  76  76  LEU LEU C . n 
C 1 78  LEU 78  77  77  LEU LEU C . n 
C 1 79  VAL 79  78  78  VAL VAL C . n 
C 1 80  GLY 80  79  79  GLY GLY C . n 
C 1 81  ASN 81  80  80  ASN ASN C . n 
C 1 82  GLN 82  81  81  GLN GLN C . n 
C 1 83  ILE 83  82  82  ILE ILE C . n 
C 1 84  SER 84  83  83  SER SER C . n 
C 1 85  LEU 85  84  84  LEU LEU C . n 
C 1 86  LEU 86  85  85  LEU LEU C . n 
C 1 87  ARG 87  86  86  ARG ARG C . n 
C 1 88  ALA 88  87  87  ALA ALA C . n 
C 1 89  PHE 89  88  88  PHE PHE C . n 
C 1 90  PHE 90  89  89  PHE PHE C . n 
C 1 91  TYR 91  90  90  TYR TYR C . n 
C 1 92  VAL 92  91  91  VAL VAL C . n 
C 1 93  ALA 93  92  92  ALA ALA C . n 
C 1 94  ALA 94  93  93  ALA ALA C . n 
C 1 95  GLN 95  94  94  GLN GLN C . n 
C 1 96  LEU 96  95  95  LEU LEU C . n 
C 1 97  VAL 97  96  96  VAL VAL C . n 
C 1 98  GLY 98  97  97  GLY GLY C . n 
C 1 99  ALA 99  98  98  ALA ALA C . n 
C 1 100 ILE 100 99  99  ILE ILE C . n 
C 1 101 ALA 101 100 100 ALA ALA C . n 
C 1 102 GLY 102 101 101 GLY GLY C . n 
C 1 103 ALA 103 102 102 ALA ALA C . n 
C 1 104 GLY 104 103 103 GLY GLY C . n 
C 1 105 ILE 105 104 104 ILE ILE C . n 
C 1 106 LEU 106 105 105 LEU LEU C . n 
C 1 107 TYR 107 106 106 TYR TYR C . n 
C 1 108 GLY 108 107 107 GLY GLY C . n 
C 1 109 VAL 109 108 108 VAL VAL C . n 
C 1 110 ALA 110 109 109 ALA ALA C . n 
C 1 111 PRO 111 110 110 PRO PRO C . n 
C 1 112 LEU 112 111 111 LEU LEU C . n 
C 1 113 ASN 113 112 112 ASN ASN C . n 
C 1 114 ALA 114 113 113 ALA ALA C . n 
C 1 115 ARG 115 114 114 ARG ARG C . n 
C 1 116 GLY 116 115 115 GLY GLY C . n 
C 1 117 ASN 117 116 116 ASN ASN C . n 
C 1 118 LEU 118 117 117 LEU LEU C . n 
C 1 119 ALA 119 118 118 ALA ALA C . n 
C 1 120 VAL 120 119 119 VAL VAL C . n 
C 1 121 ASN 121 120 120 ASN ASN C . n 
C 1 122 ALA 122 121 121 ALA ALA C . n 
C 1 123 LEU 123 122 122 LEU LEU C . n 
C 1 124 ASN 124 123 123 ASN ASN C . n 
C 1 125 ASN 125 124 124 ASN ASN C . n 
C 1 126 ASN 126 125 125 ASN ASN C . n 
C 1 127 THR 127 126 126 THR THR C . n 
C 1 128 THR 128 127 127 THR THR C . n 
C 1 129 GLN 129 128 128 GLN GLN C . n 
C 1 130 GLY 130 129 129 GLY GLY C . n 
C 1 131 GLN 131 130 130 GLN GLN C . n 
C 1 132 ALA 132 131 131 ALA ALA C . n 
C 1 133 MET 133 132 132 MET MET C . n 
C 1 134 VAL 134 133 133 VAL VAL C . n 
C 1 135 VAL 135 134 134 VAL VAL C . n 
C 1 136 GLU 136 135 135 GLU GLU C . n 
C 1 137 LEU 137 136 136 LEU LEU C . n 
C 1 138 ILE 138 137 137 ILE ILE C . n 
C 1 139 LEU 139 138 138 LEU LEU C . n 
C 1 140 THR 140 139 139 THR THR C . n 
C 1 141 PHE 141 140 140 PHE PHE C . n 
C 1 142 GLN 142 141 141 GLN GLN C . n 
C 1 143 LEU 143 142 142 LEU LEU C . n 
C 1 144 ALA 144 143 143 ALA ALA C . n 
C 1 145 LEU 145 144 144 LEU LEU C . n 
C 1 146 CYS 146 145 145 CYS CYS C . n 
C 1 147 ILE 147 146 146 ILE ILE C . n 
C 1 148 PHE 148 147 147 PHE PHE C . n 
C 1 149 ALA 149 148 148 ALA ALA C . n 
C 1 150 SER 150 149 149 SER SER C . n 
C 1 151 THR 151 150 150 THR THR C . n 
C 1 152 ASP 152 151 151 ASP ASP C . n 
C 1 153 SER 153 152 152 SER SER C . n 
C 1 154 ARG 154 153 153 ARG ARG C . n 
C 1 155 ARG 155 154 154 ARG ARG C . n 
C 1 156 THR 156 155 155 THR THR C . n 
C 1 157 SER 157 156 156 SER SER C . n 
C 1 158 PRO 158 157 157 PRO PRO C . n 
C 1 159 VAL 159 158 158 VAL VAL C . n 
C 1 160 GLY 160 159 159 GLY GLY C . n 
C 1 161 SER 161 160 160 SER SER C . n 
C 1 162 PRO 162 161 161 PRO PRO C . n 
C 1 163 ALA 163 162 162 ALA ALA C . n 
C 1 164 LEU 164 163 163 LEU LEU C . n 
C 1 165 SER 165 164 164 SER SER C . n 
C 1 166 ILE 166 165 165 ILE ILE C . n 
C 1 167 GLY 167 166 166 GLY GLY C . n 
C 1 168 LEU 168 167 167 LEU LEU C . n 
C 1 169 SER 169 168 168 SER SER C . n 
C 1 170 VAL 170 169 169 VAL VAL C . n 
C 1 171 THR 171 170 170 THR THR C . n 
C 1 172 LEU 172 171 171 LEU LEU C . n 
C 1 173 GLY 173 172 172 GLY GLY C . n 
C 1 174 HIS 174 173 173 HIS HIS C . n 
C 1 175 LEU 175 174 174 LEU LEU C . n 
C 1 176 VAL 176 175 175 VAL VAL C . n 
C 1 177 GLY 177 176 176 GLY GLY C . n 
C 1 178 ILE 178 177 177 ILE ILE C . n 
C 1 179 TYR 179 178 178 TYR TYR C . n 
C 1 180 PHE 180 179 179 PHE PHE C . n 
C 1 181 THR 181 180 180 THR THR C . n 
C 1 182 GLY 182 181 181 GLY GLY C . n 
C 1 183 CYS 183 182 182 CYS CYS C . n 
C 1 184 SER 184 183 183 SER SER C . n 
C 1 185 MET 185 184 184 MET MET C . n 
C 1 186 ASN 186 185 185 ASN ASN C . n 
C 1 187 PRO 187 186 186 PRO PRO C . n 
C 1 188 ALA 188 187 187 ALA ALA C . n 
C 1 189 ARG 189 188 188 ARG ARG C . n 
C 1 190 SER 190 189 189 SER SER C . n 
C 1 191 PHE 191 190 190 PHE PHE C . n 
C 1 192 GLY 192 191 191 GLY GLY C . n 
C 1 193 PRO 193 192 192 PRO PRO C . n 
C 1 194 ALA 194 193 193 ALA ALA C . n 
C 1 195 VAL 195 194 194 VAL VAL C . n 
C 1 196 VAL 196 195 195 VAL VAL C . n 
C 1 197 MET 197 196 196 MET MET C . n 
C 1 198 ASN 198 197 197 ASN ASN C . n 
C 1 199 ARG 199 198 198 ARG ARG C . n 
C 1 200 PHE 200 199 199 PHE PHE C . n 
C 1 201 SER 201 200 200 SER SER C . n 
C 1 202 PRO 202 201 201 PRO PRO C . n 
C 1 203 ALA 203 202 202 ALA ALA C . n 
C 1 204 HIS 204 203 203 HIS HIS C . n 
C 1 205 TRP 205 204 204 TRP TRP C . n 
C 1 206 VAL 206 205 205 VAL VAL C . n 
C 1 207 PHE 207 206 206 PHE PHE C . n 
C 1 208 TRP 208 207 207 TRP TRP C . n 
C 1 209 VAL 209 208 208 VAL VAL C . n 
C 1 210 GLY 210 209 209 GLY GLY C . n 
C 1 211 PRO 211 210 210 PRO PRO C . n 
C 1 212 ILE 212 211 211 ILE ILE C . n 
C 1 213 VAL 213 212 212 VAL VAL C . n 
C 1 214 GLY 214 213 213 GLY GLY C . n 
C 1 215 ALA 215 214 214 ALA ALA C . n 
C 1 216 VAL 216 215 215 VAL VAL C . n 
C 1 217 LEU 217 216 216 LEU LEU C . n 
C 1 218 ALA 218 217 217 ALA ALA C . n 
C 1 219 ALA 219 218 218 ALA ALA C . n 
C 1 220 ILE 220 219 219 ILE ILE C . n 
C 1 221 LEU 221 220 220 LEU LEU C . n 
C 1 222 TYR 222 221 221 TYR TYR C . n 
C 1 223 PHE 223 222 222 PHE PHE C . n 
C 1 224 TYR 224 223 223 TYR TYR C . n 
C 1 225 LEU 225 224 224 LEU LEU C . n 
C 1 226 LEU 226 225 225 LEU LEU C . n 
C 1 227 PHE 227 226 226 PHE PHE C . n 
C 1 228 PRO 228 227 227 PRO PRO C . n 
C 1 229 ASN 229 228 228 ASN ASN C . n 
C 1 230 SER 230 229 229 SER SER C . n 
C 1 231 LEU 231 230 230 LEU LEU C . n 
C 1 232 SER 232 231 231 SER SER C . n 
C 1 233 LEU 233 232 232 LEU LEU C . n 
C 1 234 SER 234 233 233 SER SER C . n 
C 1 235 GLU 235 234 234 GLU GLU C . n 
C 1 236 ARG 236 235 235 ARG ARG C . n 
C 1 237 VAL 237 236 236 VAL VAL C . n 
C 1 238 ALA 238 237 237 ALA ALA C . n 
C 1 239 ILE 239 238 238 ILE ILE C . n 
C 1 240 ILE 240 239 239 ILE ILE C . n 
C 1 241 LYS 241 240 240 LYS LYS C . n 
C 1 242 GLY 242 241 241 GLY GLY C . n 
C 1 243 THR 243 242 242 THR THR C . n 
C 1 244 TYR 244 243 243 TYR TYR C . n 
C 1 245 GLU 245 244 244 GLU GLU C . n 
C 1 246 PRO 246 245 245 PRO PRO C . n 
C 1 247 ASP 247 246 ?   ?   ?   C . n 
C 1 248 GLU 248 247 ?   ?   ?   C . n 
C 1 249 ASP 249 248 ?   ?   ?   C . n 
C 1 250 TRP 250 249 ?   ?   ?   C . n 
C 1 251 GLU 251 250 ?   ?   ?   C . n 
C 1 252 GLU 252 251 ?   ?   ?   C . n 
C 1 253 GLN 253 252 ?   ?   ?   C . n 
C 1 254 ARG 254 253 ?   ?   ?   C . n 
C 1 255 GLU 255 254 ?   ?   ?   C . n 
C 1 256 GLU 256 255 ?   ?   ?   C . n 
C 1 257 ARG 257 256 ?   ?   ?   C . n 
C 1 258 LYS 258 257 ?   ?   ?   C . n 
C 1 259 LYS 259 258 ?   ?   ?   C . n 
C 1 260 THR 260 259 ?   ?   ?   C . n 
C 1 261 MET 261 260 ?   ?   ?   C . n 
C 1 262 GLU 262 261 ?   ?   ?   C . n 
C 1 263 LEU 263 262 ?   ?   ?   C . n 
C 1 264 THR 264 263 ?   ?   ?   C . n 
C 1 265 THR 265 264 ?   ?   ?   C . n 
C 1 266 ARG 266 265 ?   ?   ?   C . n 
D 1 1   MET 1   0   ?   ?   ?   D . n 
D 1 2   SER 2   1   1   SER SER D . n 
D 1 3   LYS 3   2   2   LYS LYS D . n 
D 1 4   LYS 4   3   3   LYS LYS D . n 
D 1 5   GLU 5   4   4   GLU GLU D . n 
D 1 6   VAL 6   5   5   VAL VAL D . n 
D 1 7   CYS 7   6   6   CYS CYS D . n 
D 1 8   SER 8   7   7   SER SER D . n 
D 1 9   VAL 9   8   8   VAL VAL D . n 
D 1 10  ALA 10  9   9   ALA ALA D . n 
D 1 11  PHE 11  10  10  PHE PHE D . n 
D 1 12  LEU 12  11  11  LEU LEU D . n 
D 1 13  LYS 13  12  12  LYS LYS D . n 
D 1 14  ALA 14  13  13  ALA ALA D . n 
D 1 15  VAL 15  14  14  VAL VAL D . n 
D 1 16  PHE 16  15  15  PHE PHE D . n 
D 1 17  ALA 17  16  16  ALA ALA D . n 
D 1 18  GLU 18  17  17  GLU GLU D . n 
D 1 19  PHE 19  18  18  PHE PHE D . n 
D 1 20  LEU 20  19  19  LEU LEU D . n 
D 1 21  ALA 21  20  20  ALA ALA D . n 
D 1 22  THR 22  21  21  THR THR D . n 
D 1 23  LEU 23  22  22  LEU LEU D . n 
D 1 24  ILE 24  23  23  ILE ILE D . n 
D 1 25  PHE 25  24  24  PHE PHE D . n 
D 1 26  VAL 26  25  25  VAL VAL D . n 
D 1 27  PHE 27  26  26  PHE PHE D . n 
D 1 28  PHE 28  27  27  PHE PHE D . n 
D 1 29  GLY 29  28  28  GLY GLY D . n 
D 1 30  LEU 30  29  29  LEU LEU D . n 
D 1 31  GLY 31  30  30  GLY GLY D . n 
D 1 32  SER 32  31  31  SER SER D . n 
D 1 33  ALA 33  32  32  ALA ALA D . n 
D 1 34  LEU 34  33  33  LEU LEU D . n 
D 1 35  LYS 35  34  34  LYS LYS D . n 
D 1 36  TRP 36  35  35  TRP TRP D . n 
D 1 37  PRO 37  36  36  PRO PRO D . n 
D 1 38  SER 38  37  37  SER SER D . n 
D 1 39  ALA 39  38  38  ALA ALA D . n 
D 1 40  LEU 40  39  39  LEU LEU D . n 
D 1 41  PRO 41  40  40  PRO PRO D . n 
D 1 42  THR 42  41  41  THR THR D . n 
D 1 43  ILE 43  42  42  ILE ILE D . n 
D 1 44  LEU 44  43  43  LEU LEU D . n 
D 1 45  GLN 45  44  44  GLN GLN D . n 
D 1 46  ILE 46  45  45  ILE ILE D . n 
D 1 47  ALA 47  46  46  ALA ALA D . n 
D 1 48  LEU 48  47  47  LEU LEU D . n 
D 1 49  ALA 49  48  48  ALA ALA D . n 
D 1 50  PHE 50  49  49  PHE PHE D . n 
D 1 51  GLY 51  50  50  GLY GLY D . n 
D 1 52  LEU 52  51  51  LEU LEU D . n 
D 1 53  ALA 53  52  52  ALA ALA D . n 
D 1 54  ILE 54  53  53  ILE ILE D . n 
D 1 55  GLY 55  54  54  GLY GLY D . n 
D 1 56  THR 56  55  55  THR THR D . n 
D 1 57  LEU 57  56  56  LEU LEU D . n 
D 1 58  ALA 58  57  57  ALA ALA D . n 
D 1 59  GLN 59  58  58  GLN GLN D . n 
D 1 60  ALA 60  59  59  ALA ALA D . n 
D 1 61  LEU 61  60  60  LEU LEU D . n 
D 1 62  GLY 62  61  61  GLY GLY D . n 
D 1 63  PRO 63  62  62  PRO PRO D . n 
D 1 64  VAL 64  63  63  VAL VAL D . n 
D 1 65  SER 65  64  64  SER SER D . n 
D 1 66  GLY 66  65  65  GLY GLY D . n 
D 1 67  GLY 67  66  66  GLY GLY D . n 
D 1 68  HIS 68  67  67  HIS HIS D . n 
D 1 69  ILE 69  68  68  ILE ILE D . n 
D 1 70  ASN 70  69  69  ASN ASN D . n 
D 1 71  PRO 71  70  70  PRO PRO D . n 
D 1 72  ALA 72  71  71  ALA ALA D . n 
D 1 73  ILE 73  72  72  ILE ILE D . n 
D 1 74  THR 74  73  73  THR THR D . n 
D 1 75  LEU 75  74  74  LEU LEU D . n 
D 1 76  ALA 76  75  75  ALA ALA D . n 
D 1 77  LEU 77  76  76  LEU LEU D . n 
D 1 78  LEU 78  77  77  LEU LEU D . n 
D 1 79  VAL 79  78  78  VAL VAL D . n 
D 1 80  GLY 80  79  79  GLY GLY D . n 
D 1 81  ASN 81  80  80  ASN ASN D . n 
D 1 82  GLN 82  81  81  GLN GLN D . n 
D 1 83  ILE 83  82  82  ILE ILE D . n 
D 1 84  SER 84  83  83  SER SER D . n 
D 1 85  LEU 85  84  84  LEU LEU D . n 
D 1 86  LEU 86  85  85  LEU LEU D . n 
D 1 87  ARG 87  86  86  ARG ARG D . n 
D 1 88  ALA 88  87  87  ALA ALA D . n 
D 1 89  PHE 89  88  88  PHE PHE D . n 
D 1 90  PHE 90  89  89  PHE PHE D . n 
D 1 91  TYR 91  90  90  TYR TYR D . n 
D 1 92  VAL 92  91  91  VAL VAL D . n 
D 1 93  ALA 93  92  92  ALA ALA D . n 
D 1 94  ALA 94  93  93  ALA ALA D . n 
D 1 95  GLN 95  94  94  GLN GLN D . n 
D 1 96  LEU 96  95  95  LEU LEU D . n 
D 1 97  VAL 97  96  96  VAL VAL D . n 
D 1 98  GLY 98  97  97  GLY GLY D . n 
D 1 99  ALA 99  98  98  ALA ALA D . n 
D 1 100 ILE 100 99  99  ILE ILE D . n 
D 1 101 ALA 101 100 100 ALA ALA D . n 
D 1 102 GLY 102 101 101 GLY GLY D . n 
D 1 103 ALA 103 102 102 ALA ALA D . n 
D 1 104 GLY 104 103 103 GLY GLY D . n 
D 1 105 ILE 105 104 104 ILE ILE D . n 
D 1 106 LEU 106 105 105 LEU LEU D . n 
D 1 107 TYR 107 106 106 TYR TYR D . n 
D 1 108 GLY 108 107 107 GLY GLY D . n 
D 1 109 VAL 109 108 108 VAL VAL D . n 
D 1 110 ALA 110 109 109 ALA ALA D . n 
D 1 111 PRO 111 110 110 PRO PRO D . n 
D 1 112 LEU 112 111 111 LEU LEU D . n 
D 1 113 ASN 113 112 112 ASN ASN D . n 
D 1 114 ALA 114 113 113 ALA ALA D . n 
D 1 115 ARG 115 114 114 ARG ARG D . n 
D 1 116 GLY 116 115 115 GLY GLY D . n 
D 1 117 ASN 117 116 116 ASN ASN D . n 
D 1 118 LEU 118 117 117 LEU LEU D . n 
D 1 119 ALA 119 118 118 ALA ALA D . n 
D 1 120 VAL 120 119 119 VAL VAL D . n 
D 1 121 ASN 121 120 120 ASN ASN D . n 
D 1 122 ALA 122 121 121 ALA ALA D . n 
D 1 123 LEU 123 122 122 LEU LEU D . n 
D 1 124 ASN 124 123 123 ASN ASN D . n 
D 1 125 ASN 125 124 124 ASN ASN D . n 
D 1 126 ASN 126 125 125 ASN ASN D . n 
D 1 127 THR 127 126 126 THR THR D . n 
D 1 128 THR 128 127 127 THR THR D . n 
D 1 129 GLN 129 128 128 GLN GLN D . n 
D 1 130 GLY 130 129 129 GLY GLY D . n 
D 1 131 GLN 131 130 130 GLN GLN D . n 
D 1 132 ALA 132 131 131 ALA ALA D . n 
D 1 133 MET 133 132 132 MET MET D . n 
D 1 134 VAL 134 133 133 VAL VAL D . n 
D 1 135 VAL 135 134 134 VAL VAL D . n 
D 1 136 GLU 136 135 135 GLU GLU D . n 
D 1 137 LEU 137 136 136 LEU LEU D . n 
D 1 138 ILE 138 137 137 ILE ILE D . n 
D 1 139 LEU 139 138 138 LEU LEU D . n 
D 1 140 THR 140 139 139 THR THR D . n 
D 1 141 PHE 141 140 140 PHE PHE D . n 
D 1 142 GLN 142 141 141 GLN GLN D . n 
D 1 143 LEU 143 142 142 LEU LEU D . n 
D 1 144 ALA 144 143 143 ALA ALA D . n 
D 1 145 LEU 145 144 144 LEU LEU D . n 
D 1 146 CYS 146 145 145 CYS CYS D . n 
D 1 147 ILE 147 146 146 ILE ILE D . n 
D 1 148 PHE 148 147 147 PHE PHE D . n 
D 1 149 ALA 149 148 148 ALA ALA D . n 
D 1 150 SER 150 149 149 SER SER D . n 
D 1 151 THR 151 150 150 THR THR D . n 
D 1 152 ASP 152 151 151 ASP ASP D . n 
D 1 153 SER 153 152 152 SER SER D . n 
D 1 154 ARG 154 153 153 ARG ARG D . n 
D 1 155 ARG 155 154 154 ARG ARG D . n 
D 1 156 THR 156 155 155 THR THR D . n 
D 1 157 SER 157 156 156 SER SER D . n 
D 1 158 PRO 158 157 157 PRO PRO D . n 
D 1 159 VAL 159 158 158 VAL VAL D . n 
D 1 160 GLY 160 159 159 GLY GLY D . n 
D 1 161 SER 161 160 160 SER SER D . n 
D 1 162 PRO 162 161 161 PRO PRO D . n 
D 1 163 ALA 163 162 162 ALA ALA D . n 
D 1 164 LEU 164 163 163 LEU LEU D . n 
D 1 165 SER 165 164 164 SER SER D . n 
D 1 166 ILE 166 165 165 ILE ILE D . n 
D 1 167 GLY 167 166 166 GLY GLY D . n 
D 1 168 LEU 168 167 167 LEU LEU D . n 
D 1 169 SER 169 168 168 SER SER D . n 
D 1 170 VAL 170 169 169 VAL VAL D . n 
D 1 171 THR 171 170 170 THR THR D . n 
D 1 172 LEU 172 171 171 LEU LEU D . n 
D 1 173 GLY 173 172 172 GLY GLY D . n 
D 1 174 HIS 174 173 173 HIS HIS D . n 
D 1 175 LEU 175 174 174 LEU LEU D . n 
D 1 176 VAL 176 175 175 VAL VAL D . n 
D 1 177 GLY 177 176 176 GLY GLY D . n 
D 1 178 ILE 178 177 177 ILE ILE D . n 
D 1 179 TYR 179 178 178 TYR TYR D . n 
D 1 180 PHE 180 179 179 PHE PHE D . n 
D 1 181 THR 181 180 180 THR THR D . n 
D 1 182 GLY 182 181 181 GLY GLY D . n 
D 1 183 CYS 183 182 182 CYS CYS D . n 
D 1 184 SER 184 183 183 SER SER D . n 
D 1 185 MET 185 184 184 MET MET D . n 
D 1 186 ASN 186 185 185 ASN ASN D . n 
D 1 187 PRO 187 186 186 PRO PRO D . n 
D 1 188 ALA 188 187 187 ALA ALA D . n 
D 1 189 ARG 189 188 188 ARG ARG D . n 
D 1 190 SER 190 189 189 SER SER D . n 
D 1 191 PHE 191 190 190 PHE PHE D . n 
D 1 192 GLY 192 191 191 GLY GLY D . n 
D 1 193 PRO 193 192 192 PRO PRO D . n 
D 1 194 ALA 194 193 193 ALA ALA D . n 
D 1 195 VAL 195 194 194 VAL VAL D . n 
D 1 196 VAL 196 195 195 VAL VAL D . n 
D 1 197 MET 197 196 196 MET MET D . n 
D 1 198 ASN 198 197 197 ASN ASN D . n 
D 1 199 ARG 199 198 198 ARG ARG D . n 
D 1 200 PHE 200 199 199 PHE PHE D . n 
D 1 201 SER 201 200 200 SER SER D . n 
D 1 202 PRO 202 201 201 PRO PRO D . n 
D 1 203 ALA 203 202 202 ALA ALA D . n 
D 1 204 HIS 204 203 203 HIS HIS D . n 
D 1 205 TRP 205 204 204 TRP TRP D . n 
D 1 206 VAL 206 205 205 VAL VAL D . n 
D 1 207 PHE 207 206 206 PHE PHE D . n 
D 1 208 TRP 208 207 207 TRP TRP D . n 
D 1 209 VAL 209 208 208 VAL VAL D . n 
D 1 210 GLY 210 209 209 GLY GLY D . n 
D 1 211 PRO 211 210 210 PRO PRO D . n 
D 1 212 ILE 212 211 211 ILE ILE D . n 
D 1 213 VAL 213 212 212 VAL VAL D . n 
D 1 214 GLY 214 213 213 GLY GLY D . n 
D 1 215 ALA 215 214 214 ALA ALA D . n 
D 1 216 VAL 216 215 215 VAL VAL D . n 
D 1 217 LEU 217 216 216 LEU LEU D . n 
D 1 218 ALA 218 217 217 ALA ALA D . n 
D 1 219 ALA 219 218 218 ALA ALA D . n 
D 1 220 ILE 220 219 219 ILE ILE D . n 
D 1 221 LEU 221 220 220 LEU LEU D . n 
D 1 222 TYR 222 221 221 TYR TYR D . n 
D 1 223 PHE 223 222 222 PHE PHE D . n 
D 1 224 TYR 224 223 223 TYR TYR D . n 
D 1 225 LEU 225 224 224 LEU LEU D . n 
D 1 226 LEU 226 225 225 LEU LEU D . n 
D 1 227 PHE 227 226 226 PHE PHE D . n 
D 1 228 PRO 228 227 227 PRO PRO D . n 
D 1 229 ASN 229 228 228 ASN ASN D . n 
D 1 230 SER 230 229 229 SER SER D . n 
D 1 231 LEU 231 230 230 LEU LEU D . n 
D 1 232 SER 232 231 231 SER SER D . n 
D 1 233 LEU 233 232 232 LEU LEU D . n 
D 1 234 SER 234 233 233 SER SER D . n 
D 1 235 GLU 235 234 234 GLU GLU D . n 
D 1 236 ARG 236 235 235 ARG ARG D . n 
D 1 237 VAL 237 236 236 VAL VAL D . n 
D 1 238 ALA 238 237 237 ALA ALA D . n 
D 1 239 ILE 239 238 238 ILE ILE D . n 
D 1 240 ILE 240 239 239 ILE ILE D . n 
D 1 241 LYS 241 240 240 LYS LYS D . n 
D 1 242 GLY 242 241 241 GLY GLY D . n 
D 1 243 THR 243 242 242 THR THR D . n 
D 1 244 TYR 244 243 243 TYR TYR D . n 
D 1 245 GLU 245 244 244 GLU GLU D . n 
D 1 246 PRO 246 245 245 PRO PRO D . n 
D 1 247 ASP 247 246 ?   ?   ?   D . n 
D 1 248 GLU 248 247 ?   ?   ?   D . n 
D 1 249 ASP 249 248 ?   ?   ?   D . n 
D 1 250 TRP 250 249 ?   ?   ?   D . n 
D 1 251 GLU 251 250 ?   ?   ?   D . n 
D 1 252 GLU 252 251 ?   ?   ?   D . n 
D 1 253 GLN 253 252 ?   ?   ?   D . n 
D 1 254 ARG 254 253 ?   ?   ?   D . n 
D 1 255 GLU 255 254 ?   ?   ?   D . n 
D 1 256 GLU 256 255 ?   ?   ?   D . n 
D 1 257 ARG 257 256 ?   ?   ?   D . n 
D 1 258 LYS 258 257 ?   ?   ?   D . n 
D 1 259 LYS 259 258 ?   ?   ?   D . n 
D 1 260 THR 260 259 ?   ?   ?   D . n 
D 1 261 MET 261 260 ?   ?   ?   D . n 
D 1 262 GLU 262 261 ?   ?   ?   D . n 
D 1 263 LEU 263 262 ?   ?   ?   D . n 
D 1 264 THR 264 263 ?   ?   ?   D . n 
D 1 265 THR 265 264 ?   ?   ?   D . n 
D 1 266 ARG 266 265 ?   ?   ?   D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 2 PS6 1  266 1   PS6 PS6 D . 
F 3 HOH 1  266 13  HOH HOH A . 
F 3 HOH 2  267 14  HOH HOH A . 
F 3 HOH 3  268 15  HOH HOH A . 
F 3 HOH 4  269 16  HOH HOH A . 
F 3 HOH 5  270 17  HOH HOH A . 
F 3 HOH 6  271 18  HOH HOH A . 
F 3 HOH 7  272 19  HOH HOH A . 
F 3 HOH 8  273 28  HOH HOH A . 
F 3 HOH 9  274 29  HOH HOH A . 
F 3 HOH 10 275 30  HOH HOH A . 
F 3 HOH 11 276 39  HOH HOH A . 
F 3 HOH 12 277 46  HOH HOH A . 
F 3 HOH 13 278 48  HOH HOH A . 
F 3 HOH 14 279 50  HOH HOH A . 
F 3 HOH 15 280 51  HOH HOH A . 
F 3 HOH 16 281 91  HOH HOH A . 
F 3 HOH 17 282 92  HOH HOH A . 
F 3 HOH 18 283 93  HOH HOH A . 
F 3 HOH 19 284 99  HOH HOH A . 
F 3 HOH 20 285 100 HOH HOH A . 
F 3 HOH 21 286 112 HOH HOH A . 
F 3 HOH 22 287 113 HOH HOH A . 
F 3 HOH 23 288 114 HOH HOH A . 
F 3 HOH 24 289 115 HOH HOH A . 
F 3 HOH 25 290 116 HOH HOH A . 
F 3 HOH 26 291 117 HOH HOH A . 
G 3 HOH 1  266 7   HOH HOH B . 
G 3 HOH 2  267 8   HOH HOH B . 
G 3 HOH 3  268 9   HOH HOH B . 
G 3 HOH 4  269 10  HOH HOH B . 
G 3 HOH 5  270 11  HOH HOH B . 
G 3 HOH 6  271 12  HOH HOH B . 
G 3 HOH 7  272 31  HOH HOH B . 
G 3 HOH 8  273 49  HOH HOH B . 
G 3 HOH 9  274 52  HOH HOH B . 
G 3 HOH 10 275 53  HOH HOH B . 
G 3 HOH 11 276 54  HOH HOH B . 
G 3 HOH 12 277 55  HOH HOH B . 
G 3 HOH 13 278 58  HOH HOH B . 
G 3 HOH 14 279 68  HOH HOH B . 
G 3 HOH 15 280 72  HOH HOH B . 
G 3 HOH 16 281 74  HOH HOH B . 
G 3 HOH 17 282 75  HOH HOH B . 
G 3 HOH 18 283 81  HOH HOH B . 
G 3 HOH 19 284 82  HOH HOH B . 
G 3 HOH 20 285 83  HOH HOH B . 
G 3 HOH 21 286 84  HOH HOH B . 
G 3 HOH 22 287 85  HOH HOH B . 
G 3 HOH 23 288 86  HOH HOH B . 
G 3 HOH 24 289 87  HOH HOH B . 
G 3 HOH 25 290 88  HOH HOH B . 
G 3 HOH 26 291 89  HOH HOH B . 
G 3 HOH 27 292 110 HOH HOH B . 
H 3 HOH 1  266 20  HOH HOH C . 
H 3 HOH 2  267 21  HOH HOH C . 
H 3 HOH 3  268 23  HOH HOH C . 
H 3 HOH 4  269 24  HOH HOH C . 
H 3 HOH 5  270 25  HOH HOH C . 
H 3 HOH 6  271 26  HOH HOH C . 
H 3 HOH 7  272 27  HOH HOH C . 
H 3 HOH 8  273 34  HOH HOH C . 
H 3 HOH 9  274 35  HOH HOH C . 
H 3 HOH 10 275 36  HOH HOH C . 
H 3 HOH 11 276 45  HOH HOH C . 
H 3 HOH 12 277 59  HOH HOH C . 
H 3 HOH 13 278 60  HOH HOH C . 
H 3 HOH 14 279 61  HOH HOH C . 
H 3 HOH 15 280 62  HOH HOH C . 
H 3 HOH 16 281 63  HOH HOH C . 
H 3 HOH 17 282 64  HOH HOH C . 
H 3 HOH 18 283 65  HOH HOH C . 
H 3 HOH 19 284 66  HOH HOH C . 
H 3 HOH 20 285 69  HOH HOH C . 
H 3 HOH 21 286 70  HOH HOH C . 
H 3 HOH 22 287 71  HOH HOH C . 
H 3 HOH 23 288 76  HOH HOH C . 
H 3 HOH 24 289 77  HOH HOH C . 
H 3 HOH 25 290 78  HOH HOH C . 
H 3 HOH 26 291 79  HOH HOH C . 
H 3 HOH 27 292 80  HOH HOH C . 
H 3 HOH 28 293 101 HOH HOH C . 
H 3 HOH 29 294 102 HOH HOH C . 
H 3 HOH 30 295 103 HOH HOH C . 
H 3 HOH 31 296 104 HOH HOH C . 
H 3 HOH 32 297 111 HOH HOH C . 
I 3 HOH 1  267 1   HOH HOH D . 
I 3 HOH 2  268 2   HOH HOH D . 
I 3 HOH 3  269 3   HOH HOH D . 
I 3 HOH 4  270 4   HOH HOH D . 
I 3 HOH 5  271 5   HOH HOH D . 
I 3 HOH 6  272 6   HOH HOH D . 
I 3 HOH 7  273 32  HOH HOH D . 
I 3 HOH 8  274 37  HOH HOH D . 
I 3 HOH 9  275 40  HOH HOH D . 
I 3 HOH 10 276 41  HOH HOH D . 
I 3 HOH 11 277 42  HOH HOH D . 
I 3 HOH 12 278 43  HOH HOH D . 
I 3 HOH 13 279 44  HOH HOH D . 
I 3 HOH 14 280 47  HOH HOH D . 
I 3 HOH 15 281 56  HOH HOH D . 
I 3 HOH 16 282 57  HOH HOH D . 
I 3 HOH 17 283 94  HOH HOH D . 
I 3 HOH 18 284 95  HOH HOH D . 
I 3 HOH 19 285 96  HOH HOH D . 
I 3 HOH 20 286 97  HOH HOH D . 
I 3 HOH 21 287 98  HOH HOH D . 
I 3 HOH 22 288 105 HOH HOH D . 
I 3 HOH 23 289 106 HOH HOH D . 
I 3 HOH 24 290 107 HOH HOH D . 
I 3 HOH 25 291 108 HOH HOH D . 
I 3 HOH 26 292 109 HOH HOH D . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 13190 ? 
1 MORE         -132  ? 
1 'SSA (A^2)'  32430 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2008-08-26 
2 'Structure model' 1 1 2011-07-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Version format compliance' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
SHELX     'model building'  . ? 1 
SHELXL-97 refinement        . ? 2 
MxCuBE    'data collection' . ? 3 
MOSFLM    'data reduction'  . ? 4 
SCALA     'data scaling'    . ? 5 
AMoRE     phasing           . ? 6 
# 
_pdbx_entry_details.entry_id             3D9S 
_pdbx_entry_details.compound_details     ? 
_pdbx_entry_details.source_details       ? 
_pdbx_entry_details.nonpolymer_details   'PS6 IS A MODIFIED FORM OF PHOSPHATIDYLSERINE (PSF).' 
_pdbx_entry_details.sequence_details     ? 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 C  A GLY 115 ? ? N  A ASN 116 ? ? CA  A ASN 116 ? ? 149.53 121.70 27.83 2.50 Y 
2  1 CA B LEU 22  ? ? CB B LEU 22  ? ? CG  B LEU 22  ? ? 139.98 115.30 24.68 2.30 N 
3  1 CA B LEU 230 ? ? CB B LEU 230 ? ? CG  B LEU 230 ? ? 131.67 115.30 16.37 2.30 N 
4  1 NE C ARG 86  ? ? CZ C ARG 86  ? ? NH1 C ARG 86  ? ? 123.81 120.30 3.51  0.50 N 
5  1 C  C GLY 115 ? ? N  C ASN 116 ? ? CA  C ASN 116 ? ? 141.39 121.70 19.69 2.50 Y 
6  1 C  C ASN 116 ? ? N  C LEU 117 ? ? CA  C LEU 117 ? ? 147.04 121.70 25.34 2.50 Y 
7  1 CA C LEU 144 ? ? CB C LEU 144 ? ? CG  C LEU 144 ? ? 130.94 115.30 15.64 2.30 N 
8  1 CB C TYR 223 ? ? CG C TYR 223 ? ? CD1 C TYR 223 ? ? 117.10 121.00 -3.90 0.60 N 
9  1 C  C SER 229 ? ? N  C LEU 230 ? ? CA  C LEU 230 ? ? 140.31 121.70 18.61 2.50 Y 
10 1 C  D LEU 111 ? ? N  D ASN 112 ? ? CA  D ASN 112 ? ? 136.88 121.70 15.18 2.50 Y 
11 1 CB D TYR 178 ? ? CG D TYR 178 ? ? CD2 D TYR 178 ? ? 124.64 121.00 3.64  0.60 N 
12 1 CD D ARG 188 ? ? NE D ARG 188 ? ? CZ  D ARG 188 ? ? 132.65 123.60 9.05  1.40 N 
13 1 NE D ARG 188 ? ? CZ D ARG 188 ? ? NH1 D ARG 188 ? ? 125.44 120.30 5.14  0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LEU A 33  ? ? -48.36  152.32  
2  1 TRP A 35  ? ? 57.27   104.09  
3  1 ALA A 38  ? ? -162.66 100.34  
4  1 ILE A 68  ? ? 48.89   23.95   
5  1 ASN A 69  ? ? -163.93 110.99  
6  1 ASN A 80  ? ? 62.89   167.81  
7  1 GLN A 81  ? ? 102.74  4.94    
8  1 ASN A 116 ? ? 105.68  -49.48  
9  1 PHE A 179 ? ? -107.70 -62.51  
10 1 CYS A 182 ? ? 68.34   106.68  
11 1 SER A 183 ? ? -90.83  -86.45  
12 1 ASN A 185 ? ? -169.24 98.71   
13 1 SER A 200 ? ? -39.39  142.72  
14 1 SER A 231 ? ? 57.50   137.21  
15 1 LEU A 232 ? ? -89.45  -119.01 
16 1 SER A 233 ? ? -40.77  16.48   
17 1 LYS B 34  ? ? -69.07  69.31   
18 1 ALA B 38  ? ? -174.00 101.15  
19 1 ASN B 69  ? ? -177.20 114.79  
20 1 ALA B 121 ? ? 178.75  103.76  
21 1 ARG B 154 ? ? -20.92  126.22  
22 1 THR B 180 ? ? -141.68 -6.34   
23 1 CYS B 182 ? ? 54.49   104.83  
24 1 SER B 183 ? ? -93.40  -80.09  
25 1 ASN B 185 ? ? -175.79 110.58  
26 1 ARG B 198 ? ? -146.08 58.27   
27 1 SER B 200 ? ? 78.38   163.27  
28 1 ALA B 202 ? ? 73.97   -5.82   
29 1 GLU C 4   ? ? -82.42  -106.33 
30 1 VAL C 5   ? ? 14.56   -69.92  
31 1 LEU C 22  ? ? -43.40  -72.30  
32 1 ALA C 38  ? ? -168.76 91.69   
33 1 ASN C 69  ? ? -169.90 103.45  
34 1 ASN C 116 ? ? -28.91  -86.12  
35 1 LEU C 117 ? ? -105.58 72.68   
36 1 ASN C 123 ? ? -56.95  6.25    
37 1 ASN C 124 ? ? 66.79   -51.40  
38 1 THR C 180 ? ? -142.42 -7.30   
39 1 CYS C 182 ? ? 67.20   100.59  
40 1 SER C 183 ? ? -93.15  -64.61  
41 1 MET C 184 ? ? 66.09   -3.10   
42 1 ASN C 185 ? ? -160.71 101.40  
43 1 ASN C 197 ? ? 49.98   -91.91  
44 1 ARG C 198 ? ? 2.81    77.58   
45 1 LEU C 230 ? ? -7.17   -0.79   
46 1 SER C 231 ? ? 56.20   136.26  
47 1 GLU C 244 ? ? -84.69  -76.39  
48 1 CYS D 6   ? ? -106.97 41.80   
49 1 SER D 37  ? ? -15.90  -74.59  
50 1 SER D 64  ? ? -142.21 -21.10  
51 1 ILE D 68  ? ? 49.98   23.93   
52 1 ASN D 69  ? ? -167.05 110.60  
53 1 ASN D 124 ? ? 75.31   -53.49  
54 1 CYS D 182 ? ? 76.64   111.11  
55 1 SER D 183 ? ? -101.47 -76.94  
56 1 ASN D 185 ? ? -179.15 100.73  
57 1 VAL D 194 ? ? -67.22  -174.14 
58 1 VAL D 195 ? ? 61.47   -85.50  
59 1 ASN D 197 ? ? -119.49 64.52   
60 1 GLU D 244 ? ? 161.65  159.59  
# 
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 0   ? A MET 1   
2  1 Y 1 A ASP 246 ? A ASP 247 
3  1 Y 1 A GLU 247 ? A GLU 248 
4  1 Y 1 A ASP 248 ? A ASP 249 
5  1 Y 1 A TRP 249 ? A TRP 250 
6  1 Y 1 A GLU 250 ? A GLU 251 
7  1 Y 1 A GLU 251 ? A GLU 252 
8  1 Y 1 A GLN 252 ? A GLN 253 
9  1 Y 1 A ARG 253 ? A ARG 254 
10 1 Y 1 A GLU 254 ? A GLU 255 
11 1 Y 1 A GLU 255 ? A GLU 256 
12 1 Y 1 A ARG 256 ? A ARG 257 
13 1 Y 1 A LYS 257 ? A LYS 258 
14 1 Y 1 A LYS 258 ? A LYS 259 
15 1 Y 1 A THR 259 ? A THR 260 
16 1 Y 1 A MET 260 ? A MET 261 
17 1 Y 1 A GLU 261 ? A GLU 262 
18 1 Y 1 A LEU 262 ? A LEU 263 
19 1 Y 1 A THR 263 ? A THR 264 
20 1 Y 1 A THR 264 ? A THR 265 
21 1 Y 1 A ARG 265 ? A ARG 266 
22 1 Y 1 B MET 0   ? B MET 1   
23 1 Y 1 B ASP 246 ? B ASP 247 
24 1 Y 1 B GLU 247 ? B GLU 248 
25 1 Y 1 B ASP 248 ? B ASP 249 
26 1 Y 1 B TRP 249 ? B TRP 250 
27 1 Y 1 B GLU 250 ? B GLU 251 
28 1 Y 1 B GLU 251 ? B GLU 252 
29 1 Y 1 B GLN 252 ? B GLN 253 
30 1 Y 1 B ARG 253 ? B ARG 254 
31 1 Y 1 B GLU 254 ? B GLU 255 
32 1 Y 1 B GLU 255 ? B GLU 256 
33 1 Y 1 B ARG 256 ? B ARG 257 
34 1 Y 1 B LYS 257 ? B LYS 258 
35 1 Y 1 B LYS 258 ? B LYS 259 
36 1 Y 1 B THR 259 ? B THR 260 
37 1 Y 1 B MET 260 ? B MET 261 
38 1 Y 1 B GLU 261 ? B GLU 262 
39 1 Y 1 B LEU 262 ? B LEU 263 
40 1 Y 1 B THR 263 ? B THR 264 
41 1 Y 1 B THR 264 ? B THR 265 
42 1 Y 1 B ARG 265 ? B ARG 266 
43 1 Y 1 C MET 0   ? C MET 1   
44 1 Y 1 C SER 1   ? C SER 2   
45 1 Y 1 C LYS 2   ? C LYS 3   
46 1 Y 1 C ASP 246 ? C ASP 247 
47 1 Y 1 C GLU 247 ? C GLU 248 
48 1 Y 1 C ASP 248 ? C ASP 249 
49 1 Y 1 C TRP 249 ? C TRP 250 
50 1 Y 1 C GLU 250 ? C GLU 251 
51 1 Y 1 C GLU 251 ? C GLU 252 
52 1 Y 1 C GLN 252 ? C GLN 253 
53 1 Y 1 C ARG 253 ? C ARG 254 
54 1 Y 1 C GLU 254 ? C GLU 255 
55 1 Y 1 C GLU 255 ? C GLU 256 
56 1 Y 1 C ARG 256 ? C ARG 257 
57 1 Y 1 C LYS 257 ? C LYS 258 
58 1 Y 1 C LYS 258 ? C LYS 259 
59 1 Y 1 C THR 259 ? C THR 260 
60 1 Y 1 C MET 260 ? C MET 261 
61 1 Y 1 C GLU 261 ? C GLU 262 
62 1 Y 1 C LEU 262 ? C LEU 263 
63 1 Y 1 C THR 263 ? C THR 264 
64 1 Y 1 C THR 264 ? C THR 265 
65 1 Y 1 C ARG 265 ? C ARG 266 
66 1 Y 1 D MET 0   ? D MET 1   
67 1 Y 1 D ASP 246 ? D ASP 247 
68 1 Y 1 D GLU 247 ? D GLU 248 
69 1 Y 1 D ASP 248 ? D ASP 249 
70 1 Y 1 D TRP 249 ? D TRP 250 
71 1 Y 1 D GLU 250 ? D GLU 251 
72 1 Y 1 D GLU 251 ? D GLU 252 
73 1 Y 1 D GLN 252 ? D GLN 253 
74 1 Y 1 D ARG 253 ? D ARG 254 
75 1 Y 1 D GLU 254 ? D GLU 255 
76 1 Y 1 D GLU 255 ? D GLU 256 
77 1 Y 1 D ARG 256 ? D ARG 257 
78 1 Y 1 D LYS 257 ? D LYS 258 
79 1 Y 1 D LYS 258 ? D LYS 259 
80 1 Y 1 D THR 259 ? D THR 260 
81 1 Y 1 D MET 260 ? D MET 261 
82 1 Y 1 D GLU 261 ? D GLU 262 
83 1 Y 1 D LEU 262 ? D LEU 263 
84 1 Y 1 D THR 263 ? D THR 264 
85 1 Y 1 D THR 264 ? D THR 265 
86 1 Y 1 D ARG 265 ? D ARG 266 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'O-[(S)-{[(2S)-2-(hexanoyloxy)-3-(tetradecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-D-serine' PS6 
3 water                                                                                        HOH 
# 


A second structure was input as follows:


HEADER    TRANSPORT PROTEIN                       08-JUN-10   3NE2              
TITLE     ARCHAEOGLOBUS FULGIDUS AQUAPORIN                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROBABLE AQUAPORIN AQPM;                                   
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;                         
SOURCE   3 ORGANISM_TAXID: 2234;                                                
SOURCE   4 GENE: AQPM, AF_1426;                                                 
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET28B                                    
KEYWDS    TRANSMEMBRANE HELICES, WATER CHANNEL, STRUCTURAL GENOMICS, PSI-2,     
KEYWDS   2 PROTEIN STRUCTURE INITIATIVE, CENTER FOR STRUCTURES OF MEMBRANE      
KEYWDS   3 PROTEINS, CSMP, TRANSPORT PROTEIN                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.K.LEE,J.S.FINER-MOORE,R.M.STROUD,CENTER FOR STRUCTURES OF MEMBRANE  
AUTHOR   2 PROTEINS (CSMP)                                                      
REVDAT   2   08-NOV-17 3NE2    1       REMARK                                   
REVDAT   1   22-SEP-10 3NE2    0                                                
JRNL        AUTH   J.K.LEE,J.S.FINER-MOORE,R.M.STROUD                           
JRNL        TITL   ARCHAEOGLOBUS FULGIDUS AQUAPORIN                             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.07                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 61.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 33177                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.246                           
REMARK   3   R VALUE            (WORKING SET) : 0.245                           
REMARK   3   FREE R VALUE                     : 0.274                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1693                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.07                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 923                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 24.65                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3670                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 48                           
REMARK   3   BIN FREE R VALUE                    : 0.4910                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 14029                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 180                                     
REMARK   3   SOLVENT ATOMS            : 29                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 141.8                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.48000                                             
REMARK   3    B22 (A**2) : 0.36000                                              
REMARK   3    B33 (A**2) : 0.72000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.64000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.659         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.453         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 55.475        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.918                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.841                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 14569 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  9291 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 19928 ; 1.165 ; 1.977       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 22794 ; 0.953 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1947 ; 5.030 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   420 ;30.864 ;22.762       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1934 ;17.354 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    40 ;25.910 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2392 ; 0.058 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 16285 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  3027 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  9583 ; 0.240 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4086 ; 0.080 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15241 ; 0.392 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4986 ; 0.553 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4687 ; 0.919 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D E F G H                 
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      3       A     245      1                      
REMARK   3           1     B      3       B     245      1                      
REMARK   3           1     C      3       C     245      1                      
REMARK   3           1     D      3       D     245      1                      
REMARK   3           1     E      3       E     245      1                      
REMARK   3           1     F      3       F     245      1                      
REMARK   3           1     G      3       G     245      1                      
REMARK   3           1     H      3       H     245      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   2831 ; 0.040 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    B    (A):   2831 ; 0.030 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    C    (A):   2831 ; 0.040 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    D    (A):   2831 ; 0.030 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    E    (A):   2831 ; 0.030 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    F    (A):   2831 ; 0.040 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    G    (A):   2831 ; 0.030 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    H    (A):   2831 ; 0.030 ; 0.050           
REMARK   3   TIGHT THERMAL      1    A (A**2):   2831 ; 0.070 ; 0.500           
REMARK   3   TIGHT THERMAL      1    B (A**2):   2831 ; 0.050 ; 0.500           
REMARK   3   TIGHT THERMAL      1    C (A**2):   2831 ; 0.060 ; 0.500           
REMARK   3   TIGHT THERMAL      1    D (A**2):   2831 ; 0.050 ; 0.500           
REMARK   3   TIGHT THERMAL      1    E (A**2):   2831 ; 0.040 ; 0.500           
REMARK   3   TIGHT THERMAL      1    F (A**2):   2831 ; 0.070 ; 0.500           
REMARK   3   TIGHT THERMAL      1    G (A**2):   2831 ; 0.040 ; 0.500           
REMARK   3   TIGHT THERMAL      1    H (A**2):   2831 ; 0.050 ; 0.500           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   -10        A  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.3080  33.7130  -2.5150              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4480 T22:   0.2591                                     
REMARK   3      T33:   0.0311 T12:  -0.0339                                     
REMARK   3      T13:  -0.0560 T23:   0.0114                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7737 L22:  10.2455                                     
REMARK   3      L33:   2.3161 L12:  -0.2457                                     
REMARK   3      L13:   0.5358 L23:  -1.3573                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1575 S12:   0.1538 S13:  -0.0022                       
REMARK   3      S21:  -1.2827 S22:  -0.0153 S23:   0.3543                       
REMARK   3      S31:  -0.3559 S32:  -0.0301 S33:  -0.1422                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   -10        B  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.9550  40.1580  21.9780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4763 T22:   0.3333                                     
REMARK   3      T33:   0.4858 T12:   0.1492                                     
REMARK   3      T13:   0.4816 T23:   0.0317                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4144 L22:   8.6351                                     
REMARK   3      L33:   3.6375 L12:   0.3997                                     
REMARK   3      L13:   0.0585 L23:  -0.6567                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0345 S12:  -0.1839 S13:   0.3487                       
REMARK   3      S21:   2.5711 S22:   0.2549 S23:   1.9123                       
REMARK   3      S31:  -0.9776 S32:  -0.5051 S33:  -0.2894                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   -10        C  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.2070  24.1310   9.6500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1050 T22:   0.3964                                     
REMARK   3      T33:   1.0750 T12:  -0.1104                                     
REMARK   3      T13:  -0.2282 T23:   0.1018                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4410 L22:  10.4593                                     
REMARK   3      L33:   4.6190 L12:  -0.9217                                     
REMARK   3      L13:  -0.5481 L23:  -1.6148                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0541 S12:   0.0829 S13:   0.0878                       
REMARK   3      S21:   0.4925 S22:  -0.4207 S23:  -3.0232                       
REMARK   3      S31:  -0.3520 S32:   0.5569 S33:   0.3666                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   -10        D  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.9890  30.9470  34.2030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.0298 T22:   0.2558                                     
REMARK   3      T33:   0.5328 T12:  -0.1092                                     
REMARK   3      T13:  -0.7933 T23:  -0.0453                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0739 L22:   8.1923                                     
REMARK   3      L33:   2.4683 L12:  -0.7752                                     
REMARK   3      L13:   0.6656 L23:  -0.9685                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1126 S12:  -0.4107 S13:   0.1869                       
REMARK   3      S21:   3.3698 S22:   0.0847 S23:  -2.0413                       
REMARK   3      S31:  -0.9848 S32:  -0.1199 S33:   0.0279                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   -10        E  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.0480 -11.2950  24.0240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5527 T22:   0.5946                                     
REMARK   3      T33:   1.6161 T12:  -0.0478                                     
REMARK   3      T13:   0.6744 T23:   0.1000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5801 L22:   8.6599                                     
REMARK   3      L33:   4.0553 L12:  -1.4117                                     
REMARK   3      L13:   0.5220 L23:   0.0275                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2446 S12:  -0.2432 S13:  -0.0445                       
REMARK   3      S21:   1.9408 S22:   0.2701 S23:   3.4497                       
REMARK   3      S31:   0.1003 S32:  -0.5992 S33:  -0.0255                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   -10        F  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.3330 -19.5060   9.0240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3396 T22:   0.2448                                     
REMARK   3      T33:   0.0797 T12:  -0.0788                                     
REMARK   3      T13:  -0.1327 T23:  -0.0219                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7415 L22:  10.0849                                     
REMARK   3      L33:   2.7120 L12:  -1.0109                                     
REMARK   3      L13:  -0.3322 L23:  -0.6189                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2203 S12:   0.0210 S13:   0.0241                       
REMARK   3      S21:  -1.1308 S22:  -0.0485 S23:   0.3497                       
REMARK   3      S31:   0.3996 S32:  -0.0737 S33:  -0.1718                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G   -10        G  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.0780 -16.9970  47.0660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.4852 T22:   0.6306                                     
REMARK   3      T33:   0.2654 T12:  -0.0317                                     
REMARK   3      T13:   0.5683 T23:   0.1402                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1688 L22:   7.6312                                     
REMARK   3      L33:   2.3485 L12:   0.2905                                     
REMARK   3      L13:  -0.3070 L23:   0.2463                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0936 S12:  -0.6312 S13:  -0.3146                       
REMARK   3      S21:   4.4635 S22:   0.2338 S23:   1.1470                       
REMARK   3      S31:  -0.0137 S32:  -0.3041 S33:  -0.1401                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   -10        H  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.4600 -24.9650  31.8580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4078 T22:   0.4410                                     
REMARK   3      T33:   0.4072 T12:  -0.0178                                     
REMARK   3      T13:  -0.6724 T23:   0.0118                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5371 L22:   9.9300                                     
REMARK   3      L33:   2.6829 L12:  -0.2100                                     
REMARK   3      L13:   0.5779 L23:  -0.6094                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0731 S12:  -0.3318 S13:  -0.0243                       
REMARK   3      S21:   2.2618 S22:  -0.0643 S23:  -1.7921                       
REMARK   3      S31:   0.5535 S32:   0.2914 S33:  -0.0088                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES      :   
REMARK   3  RESIDUAL ONLY                                                       
REMARK   3  TLS REFINEMENT - EACH CHAIN A SEPARATE GROUP, STRICT NCS            
REMARK   3  RESTRAINTS FOR ALL CHAINS                                           
REMARK   4                                                                      
REMARK   4 3NE2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUN-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000059712.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-APR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 103.0                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1159                             
REMARK 200  MONOCHROMATOR                  : KHOZU DOUBLE FLAT CRYSTAL          
REMARK 200  OPTICS                         : MONOCHROMETER                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35301                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 54.6                               
REMARK 200  DATA REDUNDANCY                : 2.300                              
REMARK 200  R MERGE                    (I) : 0.07700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 7.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 12.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.20000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ACCESSION CODE 2F2B                              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       99.93050            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL UNIT IS A TETRAMER. THERE ARE TWO TETRAMERS   
REMARK 300 IN THE ASYMMETRIC UNIT. CHAINS A,B,C, AND D COMPRISE ONE TETRAMER    
REMARK 300 AND CHAINS E,F,G, AND H COMPRISE THE SECOND.                         
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17430 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 29150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -144.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 15760 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 27630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -159.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLU A   246                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B   246                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLU D   246                                                      
REMARK 465     GLU E   246                                                      
REMARK 465     MET F     1                                                      
REMARK 465     GLU F   246                                                      
REMARK 465     MET G     1                                                      
REMARK 465     GLU G   246                                                      
REMARK 465     MET H     1                                                      
REMARK 465     GLU H   246                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  99    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  39    CG   CD   CE   NZ                                   
REMARK 470     LYS C  39    CG   CD   CE   NZ                                   
REMARK 470     GLU C 169    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 245    CG   CD   CE   NZ                                   
REMARK 470     LYS D  39    CG   CD   CE   NZ                                   
REMARK 470     GLU D 169    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 170    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 245    CG   CD   CE   NZ                                   
REMARK 470     LYS E  39    CG   CD   CE   NZ                                   
REMARK 470     GLU E 169    CG   CD   OE1  OE2                                  
REMARK 470     ARG E 170    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS F  39    CG   CD   CE   NZ                                   
REMARK 470     ARG F  99    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG F 170    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS G  39    CG   CD   CE   NZ                                   
REMARK 470     ARG G  76    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG G  99    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU G 169    CG   CD   OE1  OE2                                  
REMARK 470     ARG G 170    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS G 245    CG   CD   CE   NZ                                   
REMARK 470     LYS H  39    CG   CD   CE   NZ                                   
REMARK 470     GLU H 169    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU F 169   CG    GLU F 169   CD      0.096                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LYS C 245   N   -  CA  -  C   ANGL. DEV. =  20.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  38      109.78    -58.72                                   
REMARK 500    ILE A  77      -62.43    -98.09                                   
REMARK 500    ILE A  82       30.92     37.49                                   
REMARK 500    LEU A 133       26.64     49.77                                   
REMARK 500    ALA A 166      -51.04   -134.00                                   
REMARK 500    SER A 197       68.19     39.16                                   
REMARK 500    ASN A 200      112.64   -166.95                                   
REMARK 500    ILE B  77      -61.34    -97.81                                   
REMARK 500    ILE B  82       25.42     38.34                                   
REMARK 500    ASN B  83      119.78   -165.51                                   
REMARK 500    ALA B 166      -54.21   -134.99                                   
REMARK 500    ALA B 176      -66.26    -29.34                                   
REMARK 500    SER B 197       73.14     39.15                                   
REMARK 500    ASN B 200      108.97   -167.65                                   
REMARK 500    ILE C  77      -61.42    -99.98                                   
REMARK 500    ILE C  82       26.19     40.46                                   
REMARK 500    LEU C 133       25.66     49.06                                   
REMARK 500    ALA C 166      -54.04   -132.09                                   
REMARK 500    SER C 197       70.90     41.42                                   
REMARK 500    ASN C 200      110.23   -167.42                                   
REMARK 500    ILE D  77      -61.64    -95.43                                   
REMARK 500    ILE D  82       27.41     37.67                                   
REMARK 500    LEU D 133       27.76     49.11                                   
REMARK 500    ALA D 166      -53.45   -136.34                                   
REMARK 500    SER D 197       71.64     41.17                                   
REMARK 500    ASN D 200      109.10   -165.58                                   
REMARK 500    ILE E  77      -60.75    -99.15                                   
REMARK 500    ILE E  82       25.66     39.23                                   
REMARK 500    LEU E 133       26.59     48.62                                   
REMARK 500    ALA E 166      -52.91   -132.17                                   
REMARK 500    SER E 197       72.11     42.84                                   
REMARK 500    ASN E 200      110.47   -166.96                                   
REMARK 500    ILE F  82       22.77     38.37                                   
REMARK 500    ALA F 166      -51.25   -134.75                                   
REMARK 500    SER F 197       70.26     42.97                                   
REMARK 500    ASN F 200      113.90   -164.75                                   
REMARK 500    ASP G  38      109.85    -59.75                                   
REMARK 500    ILE G  77      -62.50    -97.67                                   
REMARK 500    ILE G  82       26.50     36.70                                   
REMARK 500    ALA G 166      -50.47   -136.91                                   
REMARK 500    SER G 197       71.63     40.04                                   
REMARK 500    ASN G 200      110.43   -166.65                                   
REMARK 500    ILE H  77      -62.71    -97.86                                   
REMARK 500    ILE H  82       26.16     37.84                                   
REMARK 500    LEU H 133       26.17     47.77                                   
REMARK 500    ALA H 166      -51.98   -134.95                                   
REMARK 500    SER H 197       72.18     39.38                                   
REMARK 500    ASN H 200      110.27   -166.71                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 MET E    1     THR E    2                  140.98                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG H 247                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG D 247                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG H 248                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG D 248                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 247                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 248                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 249                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG H 249                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG F 247                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2F2B   RELATED DB: PDB                                   
REMARK 900 ARCHAEL AQUAPORIN AQPM, A HOMOLOGUE OF THE A. FULGIDUS AQUAPORIN     
DBREF  3NE2 A    1   246  UNP    O28846   AQPM_ARCFU       1    246             
DBREF  3NE2 B    1   246  UNP    O28846   AQPM_ARCFU       1    246             
DBREF  3NE2 C    1   246  UNP    O28846   AQPM_ARCFU       1    246             
DBREF  3NE2 D    1   246  UNP    O28846   AQPM_ARCFU       1    246             
DBREF  3NE2 E    1   246  UNP    O28846   AQPM_ARCFU       1    246             
DBREF  3NE2 F    1   246  UNP    O28846   AQPM_ARCFU       1    246             
DBREF  3NE2 G    1   246  UNP    O28846   AQPM_ARCFU       1    246             
DBREF  3NE2 H    1   246  UNP    O28846   AQPM_ARCFU       1    246             
SEQRES   1 A  246  MET THR MET THR LEU ALA LYS ARG PHE THR ALA GLU VAL          
SEQRES   2 A  246  VAL GLY THR PHE ILE LEU VAL PHE PHE GLY PRO GLY ALA          
SEQRES   3 A  246  ALA VAL ILE THR LEU MET ILE ALA ASN GLY ALA ASP LYS          
SEQRES   4 A  246  PRO ASN GLU PHE ASN ILE GLY ILE GLY ALA LEU GLY GLY          
SEQRES   5 A  246  LEU GLY ASP TRP PHE ALA ILE GLY MET ALA PHE ALA LEU          
SEQRES   6 A  246  ALA ILE ALA ALA VAL ILE TYR SER LEU GLY ARG ILE SER          
SEQRES   7 A  246  GLY ALA HIS ILE ASN PRO ALA VAL THR ILE ALA LEU TRP          
SEQRES   8 A  246  SER ILE GLY ARG PHE PRO GLY ARG GLU VAL VAL PRO TYR          
SEQRES   9 A  246  ILE VAL ALA GLN PHE ILE GLY ALA ALA LEU GLY SER LEU          
SEQRES  10 A  246  LEU PHE LEU ALA CYS VAL GLY PRO ALA ALA ALA THR VAL          
SEQRES  11 A  246  GLY GLY LEU GLY ALA THR ALA PRO PHE PRO GLY ILE GLY          
SEQRES  12 A  246  TYR GLY GLN ALA ILE LEU THR GLU ALA ILE GLY THR PHE          
SEQRES  13 A  246  LEU LEU MET LEU VAL ILE MET GLY VAL ALA VAL ASP GLU          
SEQRES  14 A  246  ARG ALA PRO PRO GLY PHE ALA GLY LEU VAL ILE GLY LEU          
SEQRES  15 A  246  THR VAL GLY GLY ILE ILE THR THR ILE GLY ASN ILE THR          
SEQRES  16 A  246  GLY SER SER LEU ASN PRO ALA ARG THR PHE GLY PRO TYR          
SEQRES  17 A  246  LEU GLY ASP SER LEU MET GLY ILE ASN LEU TRP GLN TYR          
SEQRES  18 A  246  PHE PRO ILE TYR VAL ILE GLY PRO ILE VAL GLY ALA VAL          
SEQRES  19 A  246  ALA ALA ALA TRP LEU TYR ASN TYR LEU ALA LYS GLU              
SEQRES   1 B  246  MET THR MET THR LEU ALA LYS ARG PHE THR ALA GLU VAL          
SEQRES   2 B  246  VAL GLY THR PHE ILE LEU VAL PHE PHE GLY PRO GLY ALA          
SEQRES   3 B  246  ALA VAL ILE THR LEU MET ILE ALA ASN GLY ALA ASP LYS          
SEQRES   4 B  246  PRO ASN GLU PHE ASN ILE GLY ILE GLY ALA LEU GLY GLY          
SEQRES   5 B  246  LEU GLY ASP TRP PHE ALA ILE GLY MET ALA PHE ALA LEU          
SEQRES   6 B  246  ALA ILE ALA ALA VAL ILE TYR SER LEU GLY ARG ILE SER          
SEQRES   7 B  246  GLY ALA HIS ILE ASN PRO ALA VAL THR ILE ALA LEU TRP          
SEQRES   8 B  246  SER ILE GLY ARG PHE PRO GLY ARG GLU VAL VAL PRO TYR          
SEQRES   9 B  246  ILE VAL ALA GLN PHE ILE GLY ALA ALA LEU GLY SER LEU          
SEQRES  10 B  246  LEU PHE LEU ALA CYS VAL GLY PRO ALA ALA ALA THR VAL          
SEQRES  11 B  246  GLY GLY LEU GLY ALA THR ALA PRO PHE PRO GLY ILE GLY          
SEQRES  12 B  246  TYR GLY GLN ALA ILE LEU THR GLU ALA ILE GLY THR PHE          
SEQRES  13 B  246  LEU LEU MET LEU VAL ILE MET GLY VAL ALA VAL ASP GLU          
SEQRES  14 B  246  ARG ALA PRO PRO GLY PHE ALA GLY LEU VAL ILE GLY LEU          
SEQRES  15 B  246  THR VAL GLY GLY ILE ILE THR THR ILE GLY ASN ILE THR          
SEQRES  16 B  246  GLY SER SER LEU ASN PRO ALA ARG THR PHE GLY PRO TYR          
SEQRES  17 B  246  LEU GLY ASP SER LEU MET GLY ILE ASN LEU TRP GLN TYR          
SEQRES  18 B  246  PHE PRO ILE TYR VAL ILE GLY PRO ILE VAL GLY ALA VAL          
SEQRES  19 B  246  ALA ALA ALA TRP LEU TYR ASN TYR LEU ALA LYS GLU              
SEQRES   1 C  246  MET THR MET THR LEU ALA LYS ARG PHE THR ALA GLU VAL          
SEQRES   2 C  246  VAL GLY THR PHE ILE LEU VAL PHE PHE GLY PRO GLY ALA          
SEQRES   3 C  246  ALA VAL ILE THR LEU MET ILE ALA ASN GLY ALA ASP LYS          
SEQRES   4 C  246  PRO ASN GLU PHE ASN ILE GLY ILE GLY ALA LEU GLY GLY          
SEQRES   5 C  246  LEU GLY ASP TRP PHE ALA ILE GLY MET ALA PHE ALA LEU          
SEQRES   6 C  246  ALA ILE ALA ALA VAL ILE TYR SER LEU GLY ARG ILE SER          
SEQRES   7 C  246  GLY ALA HIS ILE ASN PRO ALA VAL THR ILE ALA LEU TRP          
SEQRES   8 C  246  SER ILE GLY ARG PHE PRO GLY ARG GLU VAL VAL PRO TYR          
SEQRES   9 C  246  ILE VAL ALA GLN PHE ILE GLY ALA ALA LEU GLY SER LEU          
SEQRES  10 C  246  LEU PHE LEU ALA CYS VAL GLY PRO ALA ALA ALA THR VAL          
SEQRES  11 C  246  GLY GLY LEU GLY ALA THR ALA PRO PHE PRO GLY ILE GLY          
SEQRES  12 C  246  TYR GLY GLN ALA ILE LEU THR GLU ALA ILE GLY THR PHE          
SEQRES  13 C  246  LEU LEU MET LEU VAL ILE MET GLY VAL ALA VAL ASP GLU          
SEQRES  14 C  246  ARG ALA PRO PRO GLY PHE ALA GLY LEU VAL ILE GLY LEU          
SEQRES  15 C  246  THR VAL GLY GLY ILE ILE THR THR ILE GLY ASN ILE THR          
SEQRES  16 C  246  GLY SER SER LEU ASN PRO ALA ARG THR PHE GLY PRO TYR          
SEQRES  17 C  246  LEU GLY ASP SER LEU MET GLY ILE ASN LEU TRP GLN TYR          
SEQRES  18 C  246  PHE PRO ILE TYR VAL ILE GLY PRO ILE VAL GLY ALA VAL          
SEQRES  19 C  246  ALA ALA ALA TRP LEU TYR ASN TYR LEU ALA LYS GLU              
SEQRES   1 D  246  MET THR MET THR LEU ALA LYS ARG PHE THR ALA GLU VAL          
SEQRES   2 D  246  VAL GLY THR PHE ILE LEU VAL PHE PHE GLY PRO GLY ALA          
SEQRES   3 D  246  ALA VAL ILE THR LEU MET ILE ALA ASN GLY ALA ASP LYS          
SEQRES   4 D  246  PRO ASN GLU PHE ASN ILE GLY ILE GLY ALA LEU GLY GLY          
SEQRES   5 D  246  LEU GLY ASP TRP PHE ALA ILE GLY MET ALA PHE ALA LEU          
SEQRES   6 D  246  ALA ILE ALA ALA VAL ILE TYR SER LEU GLY ARG ILE SER          
SEQRES   7 D  246  GLY ALA HIS ILE ASN PRO ALA VAL THR ILE ALA LEU TRP          
SEQRES   8 D  246  SER ILE GLY ARG PHE PRO GLY ARG GLU VAL VAL PRO TYR          
SEQRES   9 D  246  ILE VAL ALA GLN PHE ILE GLY ALA ALA LEU GLY SER LEU          
SEQRES  10 D  246  LEU PHE LEU ALA CYS VAL GLY PRO ALA ALA ALA THR VAL          
SEQRES  11 D  246  GLY GLY LEU GLY ALA THR ALA PRO PHE PRO GLY ILE GLY          
SEQRES  12 D  246  TYR GLY GLN ALA ILE LEU THR GLU ALA ILE GLY THR PHE          
SEQRES  13 D  246  LEU LEU MET LEU VAL ILE MET GLY VAL ALA VAL ASP GLU          
SEQRES  14 D  246  ARG ALA PRO PRO GLY PHE ALA GLY LEU VAL ILE GLY LEU          
SEQRES  15 D  246  THR VAL GLY GLY ILE ILE THR THR ILE GLY ASN ILE THR          
SEQRES  16 D  246  GLY SER SER LEU ASN PRO ALA ARG THR PHE GLY PRO TYR          
SEQRES  17 D  246  LEU GLY ASP SER LEU MET GLY ILE ASN LEU TRP GLN TYR          
SEQRES  18 D  246  PHE PRO ILE TYR VAL ILE GLY PRO ILE VAL GLY ALA VAL          
SEQRES  19 D  246  ALA ALA ALA TRP LEU TYR ASN TYR LEU ALA LYS GLU              
SEQRES   1 E  246  MET THR MET THR LEU ALA LYS ARG PHE THR ALA GLU VAL          
SEQRES   2 E  246  VAL GLY THR PHE ILE LEU VAL PHE PHE GLY PRO GLY ALA          
SEQRES   3 E  246  ALA VAL ILE THR LEU MET ILE ALA ASN GLY ALA ASP LYS          
SEQRES   4 E  246  PRO ASN GLU PHE ASN ILE GLY ILE GLY ALA LEU GLY GLY          
SEQRES   5 E  246  LEU GLY ASP TRP PHE ALA ILE GLY MET ALA PHE ALA LEU          
SEQRES   6 E  246  ALA ILE ALA ALA VAL ILE TYR SER LEU GLY ARG ILE SER          
SEQRES   7 E  246  GLY ALA HIS ILE ASN PRO ALA VAL THR ILE ALA LEU TRP          
SEQRES   8 E  246  SER ILE GLY ARG PHE PRO GLY ARG GLU VAL VAL PRO TYR          
SEQRES   9 E  246  ILE VAL ALA GLN PHE ILE GLY ALA ALA LEU GLY SER LEU          
SEQRES  10 E  246  LEU PHE LEU ALA CYS VAL GLY PRO ALA ALA ALA THR VAL          
SEQRES  11 E  246  GLY GLY LEU GLY ALA THR ALA PRO PHE PRO GLY ILE GLY          
SEQRES  12 E  246  TYR GLY GLN ALA ILE LEU THR GLU ALA ILE GLY THR PHE          
SEQRES  13 E  246  LEU LEU MET LEU VAL ILE MET GLY VAL ALA VAL ASP GLU          
SEQRES  14 E  246  ARG ALA PRO PRO GLY PHE ALA GLY LEU VAL ILE GLY LEU          
SEQRES  15 E  246  THR VAL GLY GLY ILE ILE THR THR ILE GLY ASN ILE THR          
SEQRES  16 E  246  GLY SER SER LEU ASN PRO ALA ARG THR PHE GLY PRO TYR          
SEQRES  17 E  246  LEU GLY ASP SER LEU MET GLY ILE ASN LEU TRP GLN TYR          
SEQRES  18 E  246  PHE PRO ILE TYR VAL ILE GLY PRO ILE VAL GLY ALA VAL          
SEQRES  19 E  246  ALA ALA ALA TRP LEU TYR ASN TYR LEU ALA LYS GLU              
SEQRES   1 F  246  MET THR MET THR LEU ALA LYS ARG PHE THR ALA GLU VAL          
SEQRES   2 F  246  VAL GLY THR PHE ILE LEU VAL PHE PHE GLY PRO GLY ALA          
SEQRES   3 F  246  ALA VAL ILE THR LEU MET ILE ALA ASN GLY ALA ASP LYS          
SEQRES   4 F  246  PRO ASN GLU PHE ASN ILE GLY ILE GLY ALA LEU GLY GLY          
SEQRES   5 F  246  LEU GLY ASP TRP PHE ALA ILE GLY MET ALA PHE ALA LEU          
SEQRES   6 F  246  ALA ILE ALA ALA VAL ILE TYR SER LEU GLY ARG ILE SER          
SEQRES   7 F  246  GLY ALA HIS ILE ASN PRO ALA VAL THR ILE ALA LEU TRP          
SEQRES   8 F  246  SER ILE GLY ARG PHE PRO GLY ARG GLU VAL VAL PRO TYR          
SEQRES   9 F  246  ILE VAL ALA GLN PHE ILE GLY ALA ALA LEU GLY SER LEU          
SEQRES  10 F  246  LEU PHE LEU ALA CYS VAL GLY PRO ALA ALA ALA THR VAL          
SEQRES  11 F  246  GLY GLY LEU GLY ALA THR ALA PRO PHE PRO GLY ILE GLY          
SEQRES  12 F  246  TYR GLY GLN ALA ILE LEU THR GLU ALA ILE GLY THR PHE          
SEQRES  13 F  246  LEU LEU MET LEU VAL ILE MET GLY VAL ALA VAL ASP GLU          
SEQRES  14 F  246  ARG ALA PRO PRO GLY PHE ALA GLY LEU VAL ILE GLY LEU          
SEQRES  15 F  246  THR VAL GLY GLY ILE ILE THR THR ILE GLY ASN ILE THR          
SEQRES  16 F  246  GLY SER SER LEU ASN PRO ALA ARG THR PHE GLY PRO TYR          
SEQRES  17 F  246  LEU GLY ASP SER LEU MET GLY ILE ASN LEU TRP GLN TYR          
SEQRES  18 F  246  PHE PRO ILE TYR VAL ILE GLY PRO ILE VAL GLY ALA VAL          
SEQRES  19 F  246  ALA ALA ALA TRP LEU TYR ASN TYR LEU ALA LYS GLU              
SEQRES   1 G  246  MET THR MET THR LEU ALA LYS ARG PHE THR ALA GLU VAL          
SEQRES   2 G  246  VAL GLY THR PHE ILE LEU VAL PHE PHE GLY PRO GLY ALA          
SEQRES   3 G  246  ALA VAL ILE THR LEU MET ILE ALA ASN GLY ALA ASP LYS          
SEQRES   4 G  246  PRO ASN GLU PHE ASN ILE GLY ILE GLY ALA LEU GLY GLY          
SEQRES   5 G  246  LEU GLY ASP TRP PHE ALA ILE GLY MET ALA PHE ALA LEU          
SEQRES   6 G  246  ALA ILE ALA ALA VAL ILE TYR SER LEU GLY ARG ILE SER          
SEQRES   7 G  246  GLY ALA HIS ILE ASN PRO ALA VAL THR ILE ALA LEU TRP          
SEQRES   8 G  246  SER ILE GLY ARG PHE PRO GLY ARG GLU VAL VAL PRO TYR          
SEQRES   9 G  246  ILE VAL ALA GLN PHE ILE GLY ALA ALA LEU GLY SER LEU          
SEQRES  10 G  246  LEU PHE LEU ALA CYS VAL GLY PRO ALA ALA ALA THR VAL          
SEQRES  11 G  246  GLY GLY LEU GLY ALA THR ALA PRO PHE PRO GLY ILE GLY          
SEQRES  12 G  246  TYR GLY GLN ALA ILE LEU THR GLU ALA ILE GLY THR PHE          
SEQRES  13 G  246  LEU LEU MET LEU VAL ILE MET GLY VAL ALA VAL ASP GLU          
SEQRES  14 G  246  ARG ALA PRO PRO GLY PHE ALA GLY LEU VAL ILE GLY LEU          
SEQRES  15 G  246  THR VAL GLY GLY ILE ILE THR THR ILE GLY ASN ILE THR          
SEQRES  16 G  246  GLY SER SER LEU ASN PRO ALA ARG THR PHE GLY PRO TYR          
SEQRES  17 G  246  LEU GLY ASP SER LEU MET GLY ILE ASN LEU TRP GLN TYR          
SEQRES  18 G  246  PHE PRO ILE TYR VAL ILE GLY PRO ILE VAL GLY ALA VAL          
SEQRES  19 G  246  ALA ALA ALA TRP LEU TYR ASN TYR LEU ALA LYS GLU              
SEQRES   1 H  246  MET THR MET THR LEU ALA LYS ARG PHE THR ALA GLU VAL          
SEQRES   2 H  246  VAL GLY THR PHE ILE LEU VAL PHE PHE GLY PRO GLY ALA          
SEQRES   3 H  246  ALA VAL ILE THR LEU MET ILE ALA ASN GLY ALA ASP LYS          
SEQRES   4 H  246  PRO ASN GLU PHE ASN ILE GLY ILE GLY ALA LEU GLY GLY          
SEQRES   5 H  246  LEU GLY ASP TRP PHE ALA ILE GLY MET ALA PHE ALA LEU          
SEQRES   6 H  246  ALA ILE ALA ALA VAL ILE TYR SER LEU GLY ARG ILE SER          
SEQRES   7 H  246  GLY ALA HIS ILE ASN PRO ALA VAL THR ILE ALA LEU TRP          
SEQRES   8 H  246  SER ILE GLY ARG PHE PRO GLY ARG GLU VAL VAL PRO TYR          
SEQRES   9 H  246  ILE VAL ALA GLN PHE ILE GLY ALA ALA LEU GLY SER LEU          
SEQRES  10 H  246  LEU PHE LEU ALA CYS VAL GLY PRO ALA ALA ALA THR VAL          
SEQRES  11 H  246  GLY GLY LEU GLY ALA THR ALA PRO PHE PRO GLY ILE GLY          
SEQRES  12 H  246  TYR GLY GLN ALA ILE LEU THR GLU ALA ILE GLY THR PHE          
SEQRES  13 H  246  LEU LEU MET LEU VAL ILE MET GLY VAL ALA VAL ASP GLU          
SEQRES  14 H  246  ARG ALA PRO PRO GLY PHE ALA GLY LEU VAL ILE GLY LEU          
SEQRES  15 H  246  THR VAL GLY GLY ILE ILE THR THR ILE GLY ASN ILE THR          
SEQRES  16 H  246  GLY SER SER LEU ASN PRO ALA ARG THR PHE GLY PRO TYR          
SEQRES  17 H  246  LEU GLY ASP SER LEU MET GLY ILE ASN LEU TRP GLN TYR          
SEQRES  18 H  246  PHE PRO ILE TYR VAL ILE GLY PRO ILE VAL GLY ALA VAL          
SEQRES  19 H  246  ALA ALA ALA TRP LEU TYR ASN TYR LEU ALA LYS GLU              
HET    BOG  A 247      20                                                       
HET    BOG  A 248      20                                                       
HET    BOG  A 249      20                                                       
HET    BOG  D 247      20                                                       
HET    BOG  D 248      20                                                       
HET    BOG  F 247      20                                                       
HET    BOG  H 247      20                                                       
HET    BOG  H 248      20                                                       
HET    BOG  H 249      20                                                       
HETNAM     BOG B-OCTYLGLUCOSIDE                                                 
FORMUL   9  BOG    9(C14 H28 O6)                                                
FORMUL  18  HOH   *29(H2 O)                                                     
HELIX    1   1 THR A    4  ASN A   35  1                                  32    
HELIX    2   2 GLY A   52  GLY A   79  1                                  28    
HELIX    3   3 ASN A   83  SER A   92  1                                  10    
HELIX    4   4 PRO A   97  ARG A   99  5                                   3    
HELIX    5   5 GLU A  100  GLY A  124  1                                  25    
HELIX    6   6 PRO A  125  VAL A  130  1                                   6    
HELIX    7   7 GLY A  131  ALA A  135  5                                   5    
HELIX    8   8 GLY A  143  ALA A  166  1                                  24    
HELIX    9   9 PHE A  175  GLY A  196  1                                  22    
HELIX   10  10 ASN A  200  MET A  214  1                                  15    
HELIX   11  11 LEU A  218  PHE A  222  5                                   5    
HELIX   12  12 PRO A  223  ALA A  244  1                                  22    
HELIX   13  13 THR B    4  ASN B   35  1                                  32    
HELIX   14  14 GLY B   52  GLY B   79  1                                  28    
HELIX   15  15 ASN B   83  SER B   92  1                                  10    
HELIX   16  16 PRO B   97  ARG B   99  5                                   3    
HELIX   17  17 GLU B  100  GLY B  124  1                                  25    
HELIX   18  18 PRO B  125  VAL B  130  1                                   6    
HELIX   19  19 GLY B  131  ALA B  135  5                                   5    
HELIX   20  20 GLY B  143  ALA B  166  1                                  24    
HELIX   21  21 PHE B  175  GLY B  196  1                                  22    
HELIX   22  22 ASN B  200  MET B  214  1                                  15    
HELIX   23  23 LEU B  218  PHE B  222  5                                   5    
HELIX   24  24 PRO B  223  ALA B  244  1                                  22    
HELIX   25  25 THR C    4  ASN C   35  1                                  32    
HELIX   26  26 GLY C   52  GLY C   79  1                                  28    
HELIX   27  27 ASN C   83  SER C   92  1                                  10    
HELIX   28  28 PRO C   97  ARG C   99  5                                   3    
HELIX   29  29 GLU C  100  GLY C  124  1                                  25    
HELIX   30  30 PRO C  125  VAL C  130  1                                   6    
HELIX   31  31 GLY C  131  ALA C  135  5                                   5    
HELIX   32  32 GLY C  143  ALA C  166  1                                  24    
HELIX   33  33 PHE C  175  GLY C  196  1                                  22    
HELIX   34  34 ASN C  200  MET C  214  1                                  15    
HELIX   35  35 LEU C  218  PHE C  222  5                                   5    
HELIX   36  36 PRO C  223  ALA C  244  1                                  22    
HELIX   37  37 THR D    4  ASN D   35  1                                  32    
HELIX   38  38 GLY D   52  GLY D   79  1                                  28    
HELIX   39  39 ASN D   83  SER D   92  1                                  10    
HELIX   40  40 PRO D   97  ARG D   99  5                                   3    
HELIX   41  41 GLU D  100  GLY D  124  1                                  25    
HELIX   42  42 PRO D  125  VAL D  130  1                                   6    
HELIX   43  43 GLY D  131  ALA D  135  5                                   5    
HELIX   44  44 GLY D  143  ALA D  166  1                                  24    
HELIX   45  45 PHE D  175  GLY D  196  1                                  22    
HELIX   46  46 ASN D  200  MET D  214  1                                  15    
HELIX   47  47 LEU D  218  PHE D  222  5                                   5    
HELIX   48  48 PRO D  223  ALA D  244  1                                  22    
HELIX   49  49 THR E    4  ASN E   35  1                                  32    
HELIX   50  50 GLY E   52  GLY E   79  1                                  28    
HELIX   51  51 ASN E   83  SER E   92  1                                  10    
HELIX   52  52 PRO E   97  ARG E   99  5                                   3    
HELIX   53  53 GLU E  100  GLY E  124  1                                  25    
HELIX   54  54 PRO E  125  VAL E  130  1                                   6    
HELIX   55  55 GLY E  131  ALA E  135  5                                   5    
HELIX   56  56 GLY E  143  ALA E  166  1                                  24    
HELIX   57  57 PHE E  175  GLY E  196  1                                  22    
HELIX   58  58 ASN E  200  MET E  214  1                                  15    
HELIX   59  59 LEU E  218  PHE E  222  5                                   5    
HELIX   60  60 PRO E  223  ALA E  244  1                                  22    
HELIX   61  61 THR F    4  ASN F   35  1                                  32    
HELIX   62  62 GLY F   52  GLY F   79  1                                  28    
HELIX   63  63 ASN F   83  SER F   92  1                                  10    
HELIX   64  64 PRO F   97  ARG F   99  5                                   3    
HELIX   65  65 GLU F  100  GLY F  124  1                                  25    
HELIX   66  66 PRO F  125  VAL F  130  1                                   6    
HELIX   67  67 GLY F  131  ALA F  135  5                                   5    
HELIX   68  68 GLY F  143  ALA F  166  1                                  24    
HELIX   69  69 PHE F  175  GLY F  196  1                                  22    
HELIX   70  70 ASN F  200  MET F  214  1                                  15    
HELIX   71  71 LEU F  218  PHE F  222  5                                   5    
HELIX   72  72 PRO F  223  ALA F  244  1                                  22    
HELIX   73  73 THR G    4  ASN G   35  1                                  32    
HELIX   74  74 GLY G   52  GLY G   79  1                                  28    
HELIX   75  75 ASN G   83  SER G   92  1                                  10    
HELIX   76  76 PRO G   97  ARG G   99  5                                   3    
HELIX   77  77 GLU G  100  GLY G  124  1                                  25    
HELIX   78  78 PRO G  125  VAL G  130  1                                   6    
HELIX   79  79 GLY G  131  ALA G  135  5                                   5    
HELIX   80  80 GLY G  143  ALA G  166  1                                  24    
HELIX   81  81 PHE G  175  GLY G  196  1                                  22    
HELIX   82  82 ASN G  200  MET G  214  1                                  15    
HELIX   83  83 LEU G  218  PHE G  222  5                                   5    
HELIX   84  84 PRO G  223  ALA G  244  1                                  22    
HELIX   85  85 THR H    4  ASN H   35  1                                  32    
HELIX   86  86 GLY H   52  GLY H   79  1                                  28    
HELIX   87  87 ASN H   83  SER H   92  1                                  10    
HELIX   88  88 PRO H   97  ARG H   99  5                                   3    
HELIX   89  89 GLU H  100  GLY H  124  1                                  25    
HELIX   90  90 PRO H  125  VAL H  130  1                                   6    
HELIX   91  91 GLY H  131  ALA H  135  5                                   5    
HELIX   92  92 GLY H  143  ALA H  166  1                                  24    
HELIX   93  93 PHE H  175  GLY H  196  1                                  22    
HELIX   94  94 ASN H  200  MET H  214  1                                  15    
HELIX   95  95 LEU H  218  PHE H  222  5                                   5    
HELIX   96  96 PRO H  223  ALA H  244  1                                  22    
SITE     1 AC1  3 PHE F  17  ILE H 153  PHE H 156                               
SITE     1 AC2 10 THR D   2  ARG D   8  GLY D  75  ARG D  76                    
SITE     2 AC2 10 ILE D  77  SER D  78  GLY D  79  HIS D  81                    
SITE     3 AC2 10 ARG D  99  BOG D 248                                          
SITE     1 AC3  2 SER H 212  ASN H 217                                          
SITE     1 AC4  3 GLY D  94  ARG D  95  BOG D 247                               
SITE     1 AC5  1 PHE A  17                                                     
SITE     1 AC6  5 LEU A 120  PRO A 125  LEU A 213  MET A 214                    
SITE     2 AC6  5 BOG A 249                                                     
SITE     1 AC7  1 BOG A 248                                                     
SITE     1 AC8 12 GLU C 246  PRO G 172  ILE H  71  ARG H  76                    
SITE     2 AC8 12 VAL H 165  ALA H 166  ALA H 171  PRO H 172                    
SITE     3 AC8 12 PRO H 173  GLY H 174  ALA H 176  GLY H 177                    
SITE     1 AC9  1 PHE F 156                                                     
CRYST1   84.899  199.861   90.567  90.00 117.51  90.00 P 1 21 1     16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011779  0.000000  0.006134        0.00000                         
SCALE2      0.000000  0.005003  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012449        0.00000                         
ATOM      1  N   THR A   2     -20.452  14.325  -0.824  1.00132.00           N  
ANISOU    1  N   THR A   2    11866  13490  24800  -1839  -6869   2341       N  
ATOM      2  CA  THR A   2     -19.811  15.681  -0.699  1.00128.33           C  
ANISOU    2  CA  THR A   2    11693  13371  23694  -1605  -6370   2203       C  
ATOM      3  C   THR A   2     -20.832  16.826  -0.937  1.00131.74           C  
ANISOU    3  C   THR A   2    11653  13623  24778  -1503  -6564   2375       C  
ATOM      4  O   THR A   2     -21.995  16.544  -1.287  1.00137.82           O  
ANISOU    4  O   THR A   2    11883  13986  26497  -1615  -7154   2594       O  
ATOM      5  CB  THR A   2     -18.565  15.840  -1.657  1.00124.71           C  
ANISOU    5  CB  THR A   2    12205  13059  22120  -1526  -6628   1845       C  
ATOM      6  OG1 THR A   2     -18.983  15.706  -3.027  1.00128.95           O  
ANISOU    6  OG1 THR A   2    13072  13207  22716  -1588  -7625   1776       O  
ATOM      7  CG2 THR A   2     -17.407  14.808  -1.306  1.00120.24           C  
ANISOU    7  CG2 THR A   2    12078  12705  20901  -1578  -6295   1670       C  
ATOM      8  N   MET A   3     -20.423  18.093  -0.718  1.00128.07           N  
ANISOU    8  N   MET A   3    11351  13429  23882  -1296  -6085   2294       N  
ATOM      9  CA  MET A   3     -21.339  19.228  -0.906  1.00131.13           C  
ANISOU    9  CA  MET A   3    11309  13645  24870  -1169  -6221   2452       C  
ATOM     10  C   MET A   3     -21.424  19.613  -2.380  1.00132.57           C  
ANISOU   10  C   MET A   3    11962  13566  24844  -1161  -7204   2329       C  
ATOM     11  O   MET A   3     -20.434  19.518  -3.109  1.00129.32           O  
ANISOU   11  O   MET A   3    12379  13264  23493  -1156  -7433   2058       O  
ATOM     12  CB  MET A   3     -20.917  20.453  -0.080  1.00127.83           C  
ANISOU   12  CB  MET A   3    10907  13573  24092   -949  -5341   2418       C  
ATOM     13  CG  MET A   3     -21.047  20.306   1.464  1.00127.44           C  
ANISOU   13  CG  MET A   3    10387  13709  24323   -921  -4331   2583       C  
ATOM     14  SD  MET A   3     -22.703  19.859   2.159  1.00136.09           S  
ANISOU   14  SD  MET A   3    10356  14428  26924   -991  -4155   3019       S  
ATOM     15  CE  MET A   3     -23.874  20.551   0.973  1.00140.54           C  
ANISOU   15  CE  MET A   3    10490  14540  28369   -948  -5105   3159       C  
ATOM     16  N   THR A   4     -22.614  20.040  -2.804  1.00137.72           N  
ANISOU   16  N   THR A   4    12091  13839  26396  -1153  -7768   2545       N  
ATOM     17  CA  THR A   4     -22.862  20.440  -4.198  1.00140.52           C  
ANISOU   17  CA  THR A   4    12881  13863  26646  -1149  -8803   2474       C  
ATOM     18  C   THR A   4     -21.782  21.441  -4.678  1.00135.48           C  
ANISOU   18  C   THR A   4    13098  13506  24871   -975  -8606   2204       C  
ATOM     19  O   THR A   4     -21.277  22.231  -3.879  1.00131.43           O  
ANISOU   19  O   THR A   4    12534  13361  24042   -821  -7740   2165       O  
ATOM     20  CB  THR A   4     -24.351  20.997  -4.406  1.00147.73           C  
ANISOU   20  CB  THR A   4    12972  14332  28828  -1123  -9354   2793       C  
ATOM     21  OG1 THR A   4     -24.426  21.870  -5.549  1.00149.63           O  
ANISOU   21  OG1 THR A   4    13706  14353  28792  -1030 -10119   2717       O  
ATOM     22  CG2 THR A   4     -24.870  21.750  -3.174  1.00147.69           C  
ANISOU   22  CG2 THR A   4    12123  14488  29502   -958  -8391   3016       C  
ATOM     23  N   LEU A   5     -21.431  21.384  -5.969  1.00136.14           N  
ANISOU   23  N   LEU A   5    13996  13387  24344  -1009  -9398   2024       N  
ATOM     24  CA  LEU A   5     -20.465  22.328  -6.594  1.00132.43           C  
ANISOU   24  CA  LEU A   5    14377  13103  22837   -859  -9283   1795       C  
ATOM     25  C   LEU A   5     -20.835  23.814  -6.386  1.00132.51           C  
ANISOU   25  C   LEU A   5    14095  13164  23089   -664  -9036   1908       C  
ATOM     26  O   LEU A   5     -19.967  24.678  -6.227  1.00127.78           O  
ANISOU   26  O   LEU A   5    13893  12881  21775   -526  -8456   1765       O  
ATOM     27  CB  LEU A   5     -20.342  22.052  -8.108  1.00135.63           C  
ANISOU   27  CB  LEU A   5    15679  13138  22717   -926 -10288   1649       C  
ATOM     28  CG  LEU A   5     -19.479  23.011  -8.956  1.00133.35           C  
ANISOU   28  CG  LEU A   5    16334  12926  21408   -785 -10281   1449       C  
ATOM     29  CD1 LEU A   5     -18.006  22.801  -8.666  1.00127.04           C  
ANISOU   29  CD1 LEU A   5    16081  12560  19629   -746  -9453   1199       C  
ATOM     30  CD2 LEU A   5     -19.750  22.830 -10.437  1.00138.54           C  
ANISOU   30  CD2 LEU A   5    17793  13082  21766   -844 -11395   1386       C  
ATOM     31  N   ALA A   6     -22.130  24.096  -6.429  1.00138.12           N  
ANISOU   31  N   ALA A   6    14107  13522  24851   -655  -9517   2171       N  
ATOM     32  CA  ALA A   6     -22.649  25.427  -6.159  1.00139.34           C  
ANISOU   32  CA  ALA A   6    13853  13664  25428   -457  -9289   2313       C  
ATOM     33  C   ALA A   6     -22.159  25.935  -4.804  1.00134.36           C  
ANISOU   33  C   ALA A   6    12898  13495  24656   -324  -8049   2296       C  
ATOM     34  O   ALA A   6     -21.812  27.106  -4.655  1.00132.03           O  
ANISOU   34  O   ALA A   6    12786  13369  24012   -146  -7640   2240       O  
ATOM     35  CB  ALA A   6     -24.186  25.397  -6.197  1.00146.80           C  
ANISOU   35  CB  ALA A   6    13879  14139  27760   -481  -9896   2642       C  
ATOM     36  N   LYS A   7     -22.144  25.038  -3.822  1.00133.05           N  
ANISOU   36  N   LYS A   7    12300  13498  24756   -419  -7488   2350       N  
ATOM     37  CA  LYS A   7     -21.719  25.377  -2.469  1.00129.16           C  
ANISOU   37  CA  LYS A   7    11559  13394  24123   -313  -6350   2345       C  
ATOM     38  C   LYS A   7     -20.197  25.362  -2.300  1.00122.37           C  
ANISOU   38  C   LYS A   7    11478  12962  22055   -315  -5850   2054       C  
ATOM     39  O   LYS A   7     -19.669  26.031  -1.416  1.00119.06           O  
ANISOU   39  O   LYS A   7    11087  12845  21308   -197  -5048   2000       O  
ATOM     40  CB  LYS A   7     -22.350  24.430  -1.456  1.00131.21           C  
ANISOU   40  CB  LYS A   7    11075  13619  25158   -414  -5936   2551       C  
ATOM     41  CG  LYS A   7     -23.741  24.834  -1.015  1.00137.70           C  
ANISOU   41  CG  LYS A   7    10941  14138  27242   -324  -5846   2876       C  
ATOM     42  CD  LYS A   7     -24.295  23.812  -0.027  1.00140.64           C  
ANISOU   42  CD  LYS A   7    10634  14464  28340   -443  -5368   3090       C  
ATOM     43  CE  LYS A   7     -25.752  24.077   0.366  1.00147.99           C  
ANISOU   43  CE  LYS A   7    10519  15024  30685   -368  -5265   3455       C  
ATOM     44  NZ  LYS A   7     -26.249  23.049   1.349  1.00150.84           N  
ANISOU   44  NZ  LYS A   7    10253  15330  31731   -496  -4709   3682       N  
ATOM     45  N   ARG A   8     -19.492  24.580  -3.114  1.00120.85           N  
ANISOU   45  N   ARG A   8    11912  12767  21239   -447  -6313   1872       N  
ATOM     46  CA  ARG A   8     -18.026  24.580  -3.094  1.00115.04           C  
ANISOU   46  CA  ARG A   8    11892  12385  19432   -439  -5890   1608       C  
ATOM     47  C   ARG A   8     -17.497  25.821  -3.798  1.00113.84           C  
ANISOU   47  C   ARG A   8    12302  12274  18680   -306  -5962   1482       C  
ATOM     48  O   ARG A   8     -16.447  26.354  -3.431  1.00109.50           O  
ANISOU   48  O   ARG A   8    12102  12038  17464   -241  -5378   1334       O  
ATOM     49  CB  ARG A   8     -17.473  23.301  -3.725  1.00114.39           C  
ANISOU   49  CB  ARG A   8    12275  12245  18943   -600  -6291   1464       C  
ATOM     50  CG  ARG A   8     -17.794  22.094  -2.877  1.00115.14           C  
ANISOU   50  CG  ARG A   8    11863  12355  19530   -734  -6083   1576       C  
ATOM     51  CD  ARG A   8     -17.254  20.799  -3.435  1.00114.91           C  
ANISOU   51  CD  ARG A   8    12280  12250  19130   -882  -6453   1432       C  
ATOM     52  NE  ARG A   8     -18.063  20.309  -4.552  1.00119.65           N  
ANISOU   52  NE  ARG A   8    12977  12395  20089   -985  -7446   1479       N  
ATOM     53  CZ  ARG A   8     -17.633  20.165  -5.806  1.00120.63           C  
ANISOU   53  CZ  ARG A   8    13898  12328  19606   -999  -8051   1292       C  
ATOM     54  NH1 ARG A   8     -16.371  20.457  -6.151  1.00116.88           N  
ANISOU   54  NH1 ARG A   8    14161  12086  18162   -910  -7708   1053       N  
ATOM     55  NH2 ARG A   8     -18.477  19.715  -6.729  1.00126.16           N  
ANISOU   55  NH2 ARG A   8    14679  12564  20690  -1104  -9012   1355       N  
ATOM     56  N   PHE A   9     -18.243  26.289  -4.794  1.00118.14           N  
ANISOU   56  N   PHE A   9    12920  12468  19499   -272  -6708   1560       N  
ATOM     57  CA  PHE A   9     -17.956  27.563  -5.440  1.00117.97           C  
ANISOU   57  CA  PHE A   9    13364  12422  19038   -137  -6808   1496       C  
ATOM     58  C   PHE A   9     -18.008  28.701  -4.415  1.00116.00           C  
ANISOU   58  C   PHE A   9    12710  12385  18979     26  -6063   1563       C  
ATOM     59  O   PHE A   9     -17.035  29.433  -4.222  1.00111.89           O  
ANISOU   59  O   PHE A   9    12600  12128  17785     95  -5562   1420       O  
ATOM     60  CB  PHE A   9     -18.973  27.826  -6.564  1.00124.13           C  
ANISOU   60  CB  PHE A   9    14187  12723  20255   -129  -7810   1623       C  
ATOM     61  CG  PHE A   9     -18.694  29.071  -7.359  1.00124.39           C  
ANISOU   61  CG  PHE A   9    14797  12673  19791     -1  -8009   1570       C  
ATOM     62  CD1 PHE A   9     -17.897  29.015  -8.497  1.00123.81           C  
ANISOU   62  CD1 PHE A   9    15704  12522  18815    -40  -8366   1392       C  
ATOM     63  CD2 PHE A   9     -19.223  30.296  -6.969  1.00125.32           C  
ANISOU   63  CD2 PHE A   9    14513  12765  20336    168  -7799   1702       C  
ATOM     64  CE1 PHE A   9     -17.634  30.169  -9.242  1.00124.75           C  
ANISOU   64  CE1 PHE A   9    16401  12541  18457     70  -8521   1363       C  
ATOM     65  CE2 PHE A   9     -18.956  31.448  -7.696  1.00125.82           C  
ANISOU   65  CE2 PHE A   9    15128  12737  19942    281  -7986   1663       C  
ATOM     66  CZ  PHE A   9     -18.162  31.386  -8.840  1.00125.54           C  
ANISOU   66  CZ  PHE A   9    16077  12626  18996    223  -8355   1502       C  
ATOM     67  N   THR A  10     -19.153  28.824  -3.749  1.00119.19           N  
ANISOU   67  N   THR A  10    12307  12643  20336     85  -5979   1787       N  
ATOM     68  CA  THR A  10     -19.372  29.900  -2.798  1.00118.67           C  
ANISOU   68  CA  THR A  10    11863  12697  20529    266  -5290   1864       C  
ATOM     69  C   THR A  10     -18.426  29.733  -1.606  1.00113.60           C  
ANISOU   69  C   THR A  10    11309  12468  19387    254  -4363   1741       C  
ATOM     70  O   THR A  10     -18.024  30.705  -0.985  1.00111.68           O  
ANISOU   70  O   THR A  10    11165  12397  18870    383  -3786   1685       O  
ATOM     71  CB  THR A  10     -20.852  29.987  -2.342  1.00124.16           C  
ANISOU   71  CB  THR A  10    11637  13097  22440    349  -5337   2151       C  
ATOM     72  OG1 THR A  10     -21.204  28.816  -1.606  1.00125.26           O  
ANISOU   72  OG1 THR A  10    11275  13260  23057    224  -5088   2257       O  
ATOM     73  CG2 THR A  10     -21.796  30.123  -3.543  1.00129.53           C  
ANISOU   73  CG2 THR A  10    12209  13320  23688    347  -6383   2291       C  
ATOM     74  N   ALA A  11     -18.041  28.499  -1.306  1.00111.94           N  
ANISOU   74  N   ALA A  11    11111  12386  19035     95  -4273   1694       N  
ATOM     75  CA  ALA A  11     -17.003  28.260  -0.307  1.00107.21           C  
ANISOU   75  CA  ALA A  11    10713  12152  17870     64  -3534   1565       C  
ATOM     76  C   ALA A  11     -15.664  28.803  -0.787  1.00103.21           C  
ANISOU   76  C   ALA A  11    10946  11856  16414     68  -3474   1332       C  
ATOM     77  O   ALA A  11     -14.962  29.457  -0.028  1.00100.34           O  
ANISOU   77  O   ALA A  11    10733  11723  15669    130  -2888   1251       O  
ATOM     78  CB  ALA A  11     -16.887  26.810  -0.002  1.00106.60           C  
ANISOU   78  CB  ALA A  11    10515  12122  17864   -104  -3541   1577       C  
ATOM     79  N   GLU A  12     -15.320  28.558  -2.047  1.00103.61           N  
ANISOU   79  N   GLU A  12    11476  11792  16098      4  -4073   1234       N  
ATOM     80  CA  GLU A  12     -14.071  29.092  -2.621  1.00100.56           C  
ANISOU   80  CA  GLU A  12    11790  11557  14862     12  -3987   1039       C  
ATOM     81  C   GLU A  12     -14.043  30.630  -2.752  1.00100.66           C  
ANISOU   81  C   GLU A  12    11957  11551  14739    155  -3860   1042       C  
ATOM     82  O   GLU A  12     -12.968  31.257  -2.741  1.00 97.67           O  
ANISOU   82  O   GLU A  12    12004  11355  13752    167  -3524    910       O  
ATOM     83  CB  GLU A  12     -13.804  28.468  -3.995  1.00101.93           C  
ANISOU   83  CB  GLU A  12    12509  11546  14672    -70  -4622    946       C  
ATOM     84  CG  GLU A  12     -13.192  27.066  -3.927  1.00100.61           C  
ANISOU   84  CG  GLU A  12    12470  11476  14283   -203  -4585    848       C  
ATOM     85  CD  GLU A  12     -11.823  27.029  -3.217  1.00 95.62           C  
ANISOU   85  CD  GLU A  12    12029  11193  13109   -218  -3904    708       C  
ATOM     86  OE1 GLU A  12     -11.046  28.031  -3.287  1.00 93.09           O  
ANISOU   86  OE1 GLU A  12    12018  10998  12352   -155  -3604    630       O  
ATOM     87  OE2 GLU A  12     -11.535  25.979  -2.591  1.00 93.90           O  
ANISOU   87  OE2 GLU A  12    11638  11095  12945   -302  -3708    691       O  
ATOM     88  N   VAL A  13     -15.210  31.241  -2.901  1.00104.22           N  
ANISOU   88  N   VAL A  13    12050  11753  15797    260  -4146   1201       N  
ATOM     89  CA  VAL A  13     -15.273  32.690  -2.922  1.00104.55           C  
ANISOU   89  CA  VAL A  13    12186  11752  15787    412  -4004   1219       C  
ATOM     90  C   VAL A  13     -14.919  33.209  -1.533  1.00101.85           C  
ANISOU   90  C   VAL A  13    11627  11659  15410    481  -3184   1192       C  
ATOM     91  O   VAL A  13     -13.941  33.929  -1.383  1.00 98.63           O  
ANISOU   91  O   VAL A  13    11622  11423  14430    492  -2850   1065       O  
ATOM     92  CB  VAL A  13     -16.667  33.185  -3.334  1.00109.86           C  
ANISOU   92  CB  VAL A  13    12448  12064  17228    529  -4504   1417       C  
ATOM     93  CG1 VAL A  13     -16.776  34.677  -3.108  1.00110.20           C  
ANISOU   93  CG1 VAL A  13    12502  12070  17298    711  -4235   1443       C  
ATOM     94  CG2 VAL A  13     -16.963  32.818  -4.786  1.00112.77           C  
ANISOU   94  CG2 VAL A  13    13182  12131  17535    459  -5422   1434       C  
ATOM     95  N   VAL A  14     -15.699  32.790  -0.526  1.00103.36           N  
ANISOU   95  N   VAL A  14    11220  11842  16210    515  -2869   1318       N  
ATOM     96  CA  VAL A  14     -15.551  33.245   0.868  1.00101.93           C  
ANISOU   96  CA  VAL A  14    10870  11826  16032    599  -2087   1312       C  
ATOM     97  C   VAL A  14     -14.149  32.969   1.399  1.00 97.37           C  
ANISOU   97  C   VAL A  14    10731  11564  14701    484  -1701   1131       C  
ATOM     98  O   VAL A  14     -13.633  33.704   2.233  1.00 96.01           O  
ANISOU   98  O   VAL A  14    10721  11515  14241    541  -1200   1061       O  
ATOM     99  CB  VAL A  14     -16.606  32.606   1.805  1.00104.68           C  
ANISOU   99  CB  VAL A  14    10555  12083  17135    635  -1781   1495       C  
ATOM    100  CG1 VAL A  14     -16.429  33.077   3.245  1.00103.56           C  
ANISOU  100  CG1 VAL A  14    10386  12073  16890    734   -942   1480       C  
ATOM    101  CG2 VAL A  14     -17.995  32.953   1.352  1.00109.67           C  
ANISOU  101  CG2 VAL A  14    10657  12371  18644    761  -2134   1701       C  
ATOM    102  N   GLY A  15     -13.514  31.931   0.893  1.00 95.57           N  
ANISOU  102  N   GLY A  15    10713  11432  14167    324  -1967   1053       N  
ATOM    103  CA  GLY A  15     -12.138  31.638   1.286  1.00 91.76           C  
ANISOU  103  CA  GLY A  15    10609  11213  13042    218  -1667    895       C  
ATOM    104  C   GLY A  15     -11.132  32.621   0.689  1.00 89.73           C  
ANISOU  104  C   GLY A  15    10863  11015  12215    225  -1680    763       C  
ATOM    105  O   GLY A  15     -10.301  33.214   1.373  1.00 87.60           O  
ANISOU  105  O   GLY A  15    10784  10893  11605    221  -1285    680       O  
ATOM    106  N   THR A  16     -11.194  32.802  -0.613  1.00 90.84           N  
ANISOU  106  N   THR A  16    11263  11007  12246    227  -2154    751       N  
ATOM    107  CA  THR A  16     -10.199  33.634  -1.281  1.00 89.38           C  
ANISOU  107  CA  THR A  16    11596  10852  11511    217  -2139    646       C  
ATOM    108  C   THR A  16     -10.408  35.100  -0.903  1.00 90.03           C  
ANISOU  108  C   THR A  16    11680  10882  11647    340  -1920    674       C  
ATOM    109  O   THR A  16      -9.492  35.925  -0.967  1.00 88.41           O  
ANISOU  109  O   THR A  16    11820  10741  11032    322  -1721    594       O  
ATOM    110  CB  THR A  16     -10.250  33.443  -2.800  1.00 91.05           C  
ANISOU  110  CB  THR A  16    12192  10871  11531    196  -2683    637       C  
ATOM    111  OG1 THR A  16     -10.520  32.060  -3.105  1.00 91.53           O  
ANISOU  111  OG1 THR A  16    12163  10889  11724    114  -2983    640       O  
ATOM    112  CG2 THR A  16      -8.909  33.862  -3.403  1.00 88.78           C  
ANISOU  112  CG2 THR A  16    12471  10659  10603    141  -2515    519       C  
ATOM    113  N   PHE A  17     -11.633  35.409  -0.506  1.00 92.68           N  
ANISOU  113  N   PHE A  17    11603  11070  12540    469  -1946    798       N  
ATOM    114  CA  PHE A  17     -11.962  36.718  -0.015  1.00 93.75           C  
ANISOU  114  CA  PHE A  17    11691  11126  12806    616  -1690    828       C  
ATOM    115  C   PHE A  17     -11.129  36.991   1.227  1.00 90.96           C  
ANISOU  115  C   PHE A  17    11434  10977  12151    585  -1102    728       C  
ATOM    116  O   PHE A  17     -10.467  38.006   1.347  1.00 89.56           O  
ANISOU  116  O   PHE A  17    11565  10816  11648    598   -923    653       O  
ATOM    117  CB  PHE A  17     -13.472  36.795   0.267  1.00 97.69           C  
ANISOU  117  CB  PHE A  17    11640  11409  14069    773  -1761    997       C  
ATOM    118  CG  PHE A  17     -13.844  37.874   1.227  1.00 99.32           C  
ANISOU  118  CG  PHE A  17    11706  11556  14475    947  -1278   1020       C  
ATOM    119  CD1 PHE A  17     -13.977  37.592   2.574  1.00 99.32           C  
ANISOU  119  CD1 PHE A  17    11478  11651  14609    980   -703   1026       C  
ATOM    120  CD2 PHE A  17     -14.028  39.186   0.793  1.00101.15           C  
ANISOU  120  CD2 PHE A  17    12107  11611  14713   1083  -1378   1033       C  
ATOM    121  CE1 PHE A  17     -14.299  38.593   3.486  1.00101.39           C  
ANISOU  121  CE1 PHE A  17    11710  11821  14991   1157   -208   1029       C  
ATOM    122  CE2 PHE A  17     -14.362  40.206   1.687  1.00102.99           C  
ANISOU  122  CE2 PHE A  17    12257  11757  15117   1262   -910   1039       C  
ATOM    123  CZ  PHE A  17     -14.491  39.911   3.041  1.00103.24           C  
ANISOU  123  CZ  PHE A  17    12093  11875  15258   1303   -308   1028       C  
ATOM    124  N   ILE A  18     -11.162  36.058   2.155  1.00 90.40           N  
ANISOU  124  N   ILE A  18    11126  11033  12189    532   -840    736       N  
ATOM    125  CA  ILE A  18     -10.454  36.244   3.416  1.00 88.87           C  
ANISOU  125  CA  ILE A  18    11067  10987  11712    502   -341    654       C  
ATOM    126  C   ILE A  18      -8.972  36.229   3.151  1.00 86.00           C  
ANISOU  126  C   ILE A  18    11108  10785  10783    342   -380    520       C  
ATOM    127  O   ILE A  18      -8.246  37.002   3.759  1.00 85.44           O  
ANISOU  127  O   ILE A  18    11286  10752  10424    324   -133    441       O  
ATOM    128  CB  ILE A  18     -10.858  35.179   4.494  1.00 89.35           C  
ANISOU  128  CB  ILE A  18    10831  11116  12002    480    -52    716       C  
ATOM    129  CG1 ILE A  18     -12.177  35.607   5.183  1.00 92.94           C  
ANISOU  129  CG1 ILE A  18    10931  11386  12997    673    261    847       C  
ATOM    130  CG2 ILE A  18      -9.704  34.950   5.530  1.00 86.18           C  
ANISOU  130  CG2 ILE A  18    10726  10896  11123    364    264    608       C  
ATOM    131  CD1 ILE A  18     -13.098  34.454   5.632  1.00 94.77           C  
ANISOU  131  CD1 ILE A  18    10693  11574  13740    670    372    998       C  
ATOM    132  N   LEU A  19      -8.523  35.372   2.243  1.00 85.06           N  
ANISOU  132  N   LEU A  19    11059  10725  10535    231   -684    499       N  
ATOM    133  CA  LEU A  19      -7.120  35.353   1.886  1.00 83.18           C  
ANISOU  133  CA  LEU A  19    11158  10603   9844     97   -675    393       C  
ATOM    134  C   LEU A  19      -6.660  36.755   1.464  1.00 83.87           C  
ANISOU  134  C   LEU A  19    11553  10608   9707    124   -645    358       C  
ATOM    135  O   LEU A  19      -5.626  37.244   1.966  1.00 83.02           O  
ANISOU  135  O   LEU A  19    11630  10572   9341     41   -430    287       O  
ATOM    136  CB  LEU A  19      -6.829  34.344   0.769  1.00 82.98           C  
ANISOU  136  CB  LEU A  19    11223  10584   9721     19   -982    377       C  
ATOM    137  CG  LEU A  19      -5.428  34.459   0.120  1.00 81.52           C  
ANISOU  137  CG  LEU A  19    11400  10456   9118    -84   -931    289       C  
ATOM    138  CD1 LEU A  19      -4.350  34.225   1.196  1.00 79.65           C  
ANISOU  138  CD1 LEU A  19    11116  10387   8761   -188   -628    230       C  
ATOM    139  CD2 LEU A  19      -5.255  33.492  -1.090  1.00 80.81           C  
ANISOU  139  CD2 LEU A  19    11491  10311   8903   -120  -1195    268       C  
ATOM    140  N   VAL A  20      -7.411  37.408   0.565  1.00 86.04           N  
ANISOU  140  N   VAL A  20    11885  10704  10104    229   -893    419       N  
ATOM    141  CA  VAL A  20      -6.981  38.749   0.033  1.00 86.92           C  
ANISOU  141  CA  VAL A  20    12333  10703   9988    250   -891    404       C  
ATOM    142  C   VAL A  20      -7.369  39.947   0.935  1.00 87.58           C  
ANISOU  142  C   VAL A  20    12376  10703  10198    363   -648    407       C  
ATOM    143  O   VAL A  20      -6.875  41.052   0.772  1.00 88.17           O  
ANISOU  143  O   VAL A  20    12725  10698  10079    358   -585    380       O  
ATOM    144  CB  VAL A  20      -7.461  39.039  -1.477  1.00 89.05           C  
ANISOU  144  CB  VAL A  20    12833  10770  10230    307  -1310    472       C  
ATOM    145  CG1 VAL A  20      -6.902  37.999  -2.489  1.00 88.19           C  
ANISOU  145  CG1 VAL A  20    12953  10692   9862    200  -1513    443       C  
ATOM    146  CG2 VAL A  20      -8.976  39.118  -1.565  1.00 92.13           C  
ANISOU  146  CG2 VAL A  20    12920  10981  11103    469  -1588    582       C  
ATOM    147  N   PHE A  21      -8.284  39.745   1.857  1.00 88.35           N  
ANISOU  147  N   PHE A  21    12152  10785  10631    474   -489    445       N  
ATOM    148  CA  PHE A  21      -8.681  40.852   2.671  1.00 89.71           C  
ANISOU  148  CA  PHE A  21    12344  10838  10905    610   -216    438       C  
ATOM    149  C   PHE A  21      -7.558  41.071   3.675  1.00 87.95           C  
ANISOU  149  C   PHE A  21    12372  10729  10317    489     84    322       C  
ATOM    150  O   PHE A  21      -7.066  42.199   3.840  1.00 88.15           O  
ANISOU  150  O   PHE A  21    12683  10662  10147    486    174    265       O  
ATOM    151  CB  PHE A  21     -10.018  40.591   3.401  1.00 92.13           C  
ANISOU  151  CB  PHE A  21    12242  11052  11711    788    -36    528       C  
ATOM    152  CG  PHE A  21     -10.484  41.764   4.235  1.00 94.12           C  
ANISOU  152  CG  PHE A  21    12553  11134  12073    970    316    516       C  
ATOM    153  CD1 PHE A  21      -9.913  42.034   5.477  1.00 93.14           C  
ANISOU  153  CD1 PHE A  21    12678  11055  11657    944    723    412       C  
ATOM    154  CD2 PHE A  21     -11.455  42.643   3.742  1.00 97.59           C  
ANISOU  154  CD2 PHE A  21    12858  11330  12891   1172    207    604       C  
ATOM    155  CE1 PHE A  21     -10.319  43.143   6.227  1.00 96.05           C  
ANISOU  155  CE1 PHE A  21    13198  11226  12072   1124   1060    381       C  
ATOM    156  CE2 PHE A  21     -11.865  43.776   4.483  1.00 99.65           C  
ANISOU  156  CE2 PHE A  21    13205  11401  13258   1365    563    583       C  
ATOM    157  CZ  PHE A  21     -11.302  44.012   5.732  1.00 98.94           C  
ANISOU  157  CZ  PHE A  21    13401  11356  12837   1344   1012    463       C  
ATOM    158  N   PHE A  22      -7.190  39.986   4.359  1.00 86.37           N  
ANISOU  158  N   PHE A  22    12071  10695  10051    385    194    295       N  
ATOM    159  CA  PHE A  22      -6.322  40.061   5.529  1.00 85.39           C  
ANISOU  159  CA  PHE A  22    12159  10637   9647    286    433    205       C  
ATOM    160  C   PHE A  22      -4.872  39.953   5.133  1.00 83.45           C  
ANISOU  160  C   PHE A  22    12108  10495   9103     76    285    142       C  
ATOM    161  O   PHE A  22      -4.045  40.661   5.690  1.00 83.38           O  
ANISOU  161  O   PHE A  22    12355  10442   8883     -9    356     73       O  
ATOM    162  CB  PHE A  22      -6.660  38.950   6.511  1.00 85.43           C  
ANISOU  162  CB  PHE A  22    11986  10733   9739    284    617    230       C  
ATOM    163  CG  PHE A  22      -7.933  39.172   7.246  1.00 88.07           C  
ANISOU  163  CG  PHE A  22    12171  10931  10362    488    925    294       C  
ATOM    164  CD1 PHE A  22      -7.915  39.656   8.550  1.00 89.73           C  
ANISOU  164  CD1 PHE A  22    12652  11048  10392    547   1293    240       C  
ATOM    165  CD2 PHE A  22      -9.164  38.884   6.646  1.00 89.22           C  
ANISOU  165  CD2 PHE A  22    11916  11001  10984    624    853    417       C  
ATOM    166  CE1 PHE A  22      -9.109  39.865   9.265  1.00 92.73           C  
ANISOU  166  CE1 PHE A  22    12914  11267  11050    763   1694    307       C  
ATOM    167  CE2 PHE A  22     -10.360  39.093   7.335  1.00 92.47           C  
ANISOU  167  CE2 PHE A  22    12111  11254  11770    826   1201    502       C  
ATOM    168  CZ  PHE A  22     -10.336  39.585   8.660  1.00 93.93           C  
ANISOU  168  CZ  PHE A  22    12576  11351  11760    907   1680    447       C  
ATOM    169  N   GLY A  23      -4.561  39.054   4.195  1.00 82.20           N  
ANISOU  169  N   GLY A  23    11831  10443   8957     -6     86    170       N  
ATOM    170  CA  GLY A  23      -3.175  38.842   3.769  1.00 80.65           C  
ANISOU  170  CA  GLY A  23    11766  10327   8552   -187     18    129       C  
ATOM    171  C   GLY A  23      -2.545  40.135   3.241  1.00 81.34           C  
ANISOU  171  C   GLY A  23    12114  10291   8500   -231     15    115       C  
ATOM    172  O   GLY A  23      -1.661  40.716   3.878  1.00 81.63           O  
ANISOU  172  O   GLY A  23    12294  10295   8429   -343     90     69       O  
ATOM    173  N   PRO A  24      -2.974  40.584   2.052  1.00 81.81           N  
ANISOU  173  N   PRO A  24    12264  10253   8568   -158   -107    166       N  
ATOM    174  CA  PRO A  24      -2.414  41.828   1.522  1.00 82.68           C  
ANISOU  174  CA  PRO A  24    12648  10220   8545   -202    -89    175       C  
ATOM    175  C   PRO A  24      -2.837  43.071   2.322  1.00 84.12           C  
ANISOU  175  C   PRO A  24    12943  10258   8761   -118     -1    148       C  
ATOM    176  O   PRO A  24      -2.243  44.157   2.177  1.00 84.78           O  
ANISOU  176  O   PRO A  24    13260  10210   8743   -184     30    143       O  
ATOM    177  CB  PRO A  24      -2.969  41.869   0.081  1.00 83.94           C  
ANISOU  177  CB  PRO A  24    12930  10284   8680   -118   -279    249       C  
ATOM    178  CG  PRO A  24      -3.284  40.401  -0.265  1.00 82.78           C  
ANISOU  178  CG  PRO A  24    12601  10260   8593   -109   -404    255       C  
ATOM    179  CD  PRO A  24      -3.723  39.810   1.035  1.00 82.03           C  
ANISOU  179  CD  PRO A  24    12201  10281   8684    -80   -311    222       C  
ATOM    180  N   GLY A  25      -3.875  42.912   3.144  1.00 84.77           N  
ANISOU  180  N   GLY A  25    12871  10336   9004     34     70    138       N  
ATOM    181  CA  GLY A  25      -4.358  44.004   4.016  1.00 86.32           C  
ANISOU  181  CA  GLY A  25    13202  10367   9229    153    228     99       C  
ATOM    182  C   GLY A  25      -3.320  44.436   5.045  1.00 85.97           C  
ANISOU  182  C   GLY A  25    13397  10297   8971      4    334      4       C  
ATOM    183  O   GLY A  25      -3.192  45.622   5.332  1.00 87.43           O  
ANISOU  183  O   GLY A  25    13843  10297   9080     22    379    -37       O  
ATOM    184  N   ALA A  26      -2.571  43.461   5.573  1.00 84.30           N  
ANISOU  184  N   ALA A  26    13109  10243   8680   -147    323    -25       N  
ATOM    185  CA  ALA A  26      -1.414  43.703   6.432  1.00 84.19           C  
ANISOU  185  CA  ALA A  26    13300  10191   8498   -333    296    -96       C  
ATOM    186  C   ALA A  26      -0.332  44.491   5.725  1.00 84.38           C  
ANISOU  186  C   ALA A  26    13442  10125   8495   -503    181    -80       C  
ATOM    187  O   ALA A  26       0.231  45.422   6.316  1.00 85.55           O  
ANISOU  187  O   ALA A  26    13844  10101   8560   -596    143   -132       O  
ATOM    188  CB  ALA A  26      -0.824  42.401   6.909  1.00 82.99           C  
ANISOU  188  CB  ALA A  26    12987  10213   8332   -456    241    -98       C  
ATOM    189  N   ALA A  27      -0.042  44.124   4.469  1.00 83.36           N  
ANISOU  189  N   ALA A  27    13164  10078   8431   -548    138     -3       N  
ATOM    190  CA  ALA A  27       0.935  44.855   3.643  1.00 83.90           C  
ANISOU  190  CA  ALA A  27    13342  10040   8498   -699    117     46       C  
ATOM    191  C   ALA A  27       0.581  46.359   3.504  1.00 85.88           C  
ANISOU  191  C   ALA A  27    13870  10058   8705   -636    125     48       C  
ATOM    192  O   ALA A  27       1.444  47.264   3.626  1.00 86.93           O  
ANISOU  192  O   ALA A  27    14166  10026   8836   -793    101     49       O  
ATOM    193  CB  ALA A  27       1.028  44.214   2.313  1.00 83.06           C  
ANISOU  193  CB  ALA A  27    13134  10021   8403   -694    139    126       C  
ATOM    194  N   VAL A  28      -0.704  46.614   3.270  1.00 86.54           N  
ANISOU  194  N   VAL A  28    13981  10098   8801   -406    139     58       N  
ATOM    195  CA  VAL A  28      -1.211  47.979   3.175  1.00 88.53           C  
ANISOU  195  CA  VAL A  28    14478  10114   9046   -297    144     60       C  
ATOM    196  C   VAL A  28      -0.980  48.729   4.476  1.00 89.97           C  
ANISOU  196  C   VAL A  28    14876  10146   9164   -328    193    -48       C  
ATOM    197  O   VAL A  28      -0.409  49.823   4.464  1.00 91.38           O  
ANISOU  197  O   VAL A  28    15301  10119   9300   -429    152    -56       O  
ATOM    198  CB  VAL A  28      -2.729  48.006   2.869  1.00 89.30           C  
ANISOU  198  CB  VAL A  28    14486  10171   9271    -16    134     96       C  
ATOM    199  CG1 VAL A  28      -3.303  49.414   3.109  1.00 91.29           C  
ANISOU  199  CG1 VAL A  28    14974  10151   9560    133    174     78       C  
ATOM    200  CG2 VAL A  28      -2.997  47.541   1.439  1.00 88.97           C  
ANISOU  200  CG2 VAL A  28    14373  10179   9253     13    -18    207       C  
ATOM    201  N   ILE A  29      -1.430  48.133   5.587  1.00 89.68           N  
ANISOU  201  N   ILE A  29    14792  10182   9103   -244    279   -126       N  
ATOM    202  CA  ILE A  29      -1.350  48.770   6.887  1.00 91.26           C  
ANISOU  202  CA  ILE A  29    15307  10203   9166   -238    339   -243       C  
ATOM    203  C   ILE A  29       0.097  48.962   7.329  1.00 91.78           C  
ANISOU  203  C   ILE A  29    15534  10201   9137   -534    149   -282       C  
ATOM    204  O   ILE A  29       0.391  49.967   7.963  1.00 94.09           O  
ANISOU  204  O   ILE A  29    16183  10242   9324   -583     90   -360       O  
ATOM    205  CB  ILE A  29      -2.129  47.996   7.938  1.00 91.32           C  
ANISOU  205  CB  ILE A  29    15281  10285   9130    -85    521   -297       C  
ATOM    206  CG1 ILE A  29      -3.626  48.158   7.673  1.00 92.07           C  
ANISOU  206  CG1 ILE A  29    15230  10333   9420    225    731   -253       C  
ATOM    207  CG2 ILE A  29      -1.757  48.464   9.341  1.00 93.04           C  
ANISOU  207  CG2 ILE A  29    15944  10309   9098   -132    552   -426       C  
ATOM    208  CD1 ILE A  29      -4.191  49.467   8.108  1.00 94.03           C  
ANISOU  208  CD1 ILE A  29    15799  10280   9649    407    889   -316       C  
ATOM    209  N   THR A  30       1.000  48.033   6.986  1.00 90.15           N  
ANISOU  209  N   THR A  30    15064  10180   9008   -728     36   -225       N  
ATOM    210  CA  THR A  30       2.444  48.256   7.204  1.00 91.02           C  
ANISOU  210  CA  THR A  30    15217  10193   9172  -1023   -173   -219       C  
ATOM    211  C   THR A  30       2.885  49.515   6.498  1.00 92.65           C  
ANISOU  211  C   THR A  30    15562  10183   9457  -1119   -205   -168       C  
ATOM    212  O   THR A  30       3.412  50.426   7.136  1.00 95.45           O  
ANISOU  212  O   THR A  30    16196  10285   9787  -1247   -357   -223       O  
ATOM    213  CB  THR A  30       3.324  47.153   6.655  1.00 89.35           C  
ANISOU  213  CB  THR A  30    14629  10185   9134  -1183   -223   -132       C  
ATOM    214  OG1 THR A  30       2.914  45.903   7.211  1.00 88.19           O  
ANISOU  214  OG1 THR A  30    14335  10242   8930  -1099   -201   -162       O  
ATOM    215  CG2 THR A  30       4.782  47.422   7.000  1.00 90.71           C  
ANISOU  215  CG2 THR A  30    14782  10207   9475  -1480   -449   -108       C  
ATOM    216  N   LEU A  31       2.638  49.591   5.196  1.00 91.62           N  
ANISOU  216  N   LEU A  31    15295  10116   9401  -1057    -81    -62       N  
ATOM    217  CA  LEU A  31       3.011  50.787   4.419  1.00 93.29           C  
ANISOU  217  CA  LEU A  31    15671  10105   9670  -1142    -75     15       C  
ATOM    218  C   LEU A  31       2.378  52.118   4.939  1.00 95.36           C  
ANISOU  218  C   LEU A  31    16317  10088   9826  -1023   -105    -66       C  
ATOM    219  O   LEU A  31       3.041  53.173   5.006  1.00 97.21           O  
ANISOU  219  O   LEU A  31    16765  10062  10109  -1185   -202    -56       O  
ATOM    220  CB  LEU A  31       2.644  50.586   2.948  1.00 92.42           C  
ANISOU  220  CB  LEU A  31    15463  10088   9566  -1048     62    141       C  
ATOM    221  CG  LEU A  31       3.575  49.683   2.137  1.00 91.67           C  
ANISOU  221  CG  LEU A  31    15112  10143   9576  -1205    153    244       C  
ATOM    222  CD1 LEU A  31       3.002  49.348   0.735  1.00 90.69           C  
ANISOU  222  CD1 LEU A  31    15021  10092   9346  -1065    271    341       C  
ATOM    223  CD2 LEU A  31       4.976  50.320   2.041  1.00 92.72           C  
ANISOU  223  CD2 LEU A  31    15233  10088   9910  -1495    165    326       C  
ATOM    224  N   MET A  32       1.099  52.055   5.304  1.00 95.02           N  
ANISOU  224  N   MET A  32    16345  10075   9683   -737     -5   -137       N  
ATOM    225  CA  MET A  32       0.388  53.223   5.792  1.00 97.20           C  
ANISOU  225  CA  MET A  32    16968  10079   9886   -568     35   -217       C  
ATOM    226  C   MET A  32       0.958  53.721   7.106  1.00 99.22           C  
ANISOU  226  C   MET A  32    17567  10120  10011   -691    -77   -357       C  
ATOM    227  O   MET A  32       1.203  54.903   7.228  1.00101.79           O  
ANISOU  227  O   MET A  32    18215  10146  10314   -746   -158   -390       O  
ATOM    228  CB  MET A  32      -1.106  52.944   5.935  1.00 97.00           C  
ANISOU  228  CB  MET A  32    16866  10115   9876   -221    219   -244       C  
ATOM    229  CG  MET A  32      -1.868  53.026   4.632  1.00 96.55           C  
ANISOU  229  CG  MET A  32    16633  10091   9961    -62    224   -112       C  
ATOM    230  SD  MET A  32      -3.659  52.865   4.883  1.00 97.76           S  
ANISOU  230  SD  MET A  32    16630  10226  10290    346    397   -120       S  
ATOM    231  CE  MET A  32      -4.086  54.365   5.731  1.00101.02           C  
ANISOU  231  CE  MET A  32    17465  10247  10671    522    537   -232       C  
ATOM    232  N   ILE A  33       1.194  52.847   8.077  1.00 98.67           N  
ANISOU  232  N   ILE A  33    17483  10168   9840   -746   -118   -435       N  
ATOM    233  CA  ILE A  33       1.693  53.315   9.379  1.00101.50           C  
ANISOU  233  CA  ILE A  33    18283  10272  10010   -857   -286   -575       C  
ATOM    234  C   ILE A  33       3.188  53.708   9.310  1.00102.76           C  
ANISOU  234  C   ILE A  33    18455  10279  10311  -1233   -637   -531       C  
ATOM    235  O   ILE A  33       3.656  54.575  10.063  1.00105.32           O  
ANISOU  235  O   ILE A  33    19203  10274  10542  -1359   -863   -625       O  
ATOM    236  CB  ILE A  33       1.417  52.298  10.544  1.00101.28           C  
ANISOU  236  CB  ILE A  33    18349  10360   9774   -785   -236   -667       C  
ATOM    237  CG1 ILE A  33       2.325  51.065  10.479  1.00 99.50           C  
ANISOU  237  CG1 ILE A  33    17756  10387   9662  -1011   -430   -592       C  
ATOM    238  CG2 ILE A  33      -0.045  51.879  10.566  1.00100.50           C  
ANISOU  238  CG2 ILE A  33    18149  10393   9644   -431    155   -674       C  
ATOM    239  CD1 ILE A  33       2.325  50.273  11.789  1.00100.64           C  
ANISOU  239  CD1 ILE A  33    18139  10541   9560  -1009   -491   -682       C  
ATOM    240  N   ALA A  34       3.920  53.073   8.394  1.00100.96           N  
ANISOU  240  N   ALA A  34    17764  10259  10338  -1407   -671   -384       N  
ATOM    241  CA  ALA A  34       5.333  53.371   8.175  1.00102.60           C  
ANISOU  241  CA  ALA A  34    17845  10323  10813  -1757   -927   -294       C  
ATOM    242  C   ALA A  34       5.533  54.554   7.241  1.00104.29           C  
ANISOU  242  C   ALA A  34    18123  10327  11175  -1827   -869   -197       C  
ATOM    243  O   ALA A  34       6.655  55.042   7.095  1.00106.76           O  
ANISOU  243  O   ALA A  34    18367  10442  11755  -2122  -1054   -111       O  
ATOM    244  CB  ALA A  34       6.045  52.153   7.604  1.00100.47           C  
ANISOU  244  CB  ALA A  34    17050  10335  10788  -1887   -901   -169       C  
ATOM    245  N   ASN A  35       4.455  55.023   6.614  1.00103.74           N  
ANISOU  245  N   ASN A  35    18172  10271  10974  -1564   -627   -191       N  
ATOM    246  CA  ASN A  35       4.536  56.113   5.642  1.00105.04           C  
ANISOU  246  CA  ASN A  35    18436  10234  11242  -1603   -560    -79       C  
ATOM    247  C   ASN A  35       5.099  57.394   6.249  1.00108.41           C  
ANISOU  247  C   ASN A  35    19238  10245  11709  -1783   -795   -135       C  
ATOM    248  O   ASN A  35       4.468  58.022   7.109  1.00109.56           O  
ANISOU  248  O   ASN A  35    19803  10186  11640  -1630   -855   -296       O  
ATOM    249  CB  ASN A  35       3.165  56.393   5.026  1.00104.31           C  
ANISOU  249  CB  ASN A  35    18446  10184  11003  -1259   -346    -74       C  
ATOM    250  CG  ASN A  35       3.207  57.513   3.995  1.00106.16           C  
ANISOU  250  CG  ASN A  35    18839  10188  11309  -1286   -304     56       C  
ATOM    251  OD1 ASN A  35       4.263  57.823   3.411  1.00107.23           O  
ANISOU  251  OD1 ASN A  35    18905  10219  11618  -1562   -327    191       O  
ATOM    252  ND2 ASN A  35       2.052  58.129   3.763  1.00106.98           N  
ANISOU  252  ND2 ASN A  35    19148  10185  11315   -995   -228     34       N  
ATOM    253  N   GLY A  36       6.287  57.763   5.775  1.00110.00           N  
ANISOU  253  N   GLY A  36    19288  10296  12209  -2107   -903      7       N  
ATOM    254  CA  GLY A  36       6.979  58.951   6.246  1.00113.83           C  
ANISOU  254  CA  GLY A  36    20070  10356  12824  -2343  -1179    -12       C  
ATOM    255  C   GLY A  36       8.330  58.629   6.857  1.00115.63           C  
ANISOU  255  C   GLY A  36    20087  10478  13369  -2710  -1519     20       C  
ATOM    256  O   GLY A  36       9.209  59.493   6.906  1.00119.12           O  
ANISOU  256  O   GLY A  36    20592  10571  14099  -3001  -1754     90       O  
ATOM    257  N   ALA A  37       8.509  57.397   7.326  1.00113.48           N  
ANISOU  257  N   ALA A  37    19550  10474  13092  -2708  -1581    -18       N  
ATOM    258  CA  ALA A  37       9.750  57.029   7.995  1.00115.60           C  
ANISOU  258  CA  ALA A  37    19610  10620  13694  -3037  -1979     14       C  
ATOM    259  C   ALA A  37      10.928  56.956   7.020  1.00116.80           C  
ANISOU  259  C   ALA A  37    19208  10745  14425  -3324  -1880    269       C  
ATOM    260  O   ALA A  37      10.726  56.735   5.819  1.00115.00           O  
ANISOU  260  O   ALA A  37    18737  10721  14238  -3221  -1431    408       O  
ATOM    261  CB  ALA A  37       9.576  55.716   8.703  1.00113.31           C  
ANISOU  261  CB  ALA A  37    19197  10613  13241  -2935  -2054    -76       C  
ATOM    262  N   ASP A  38      12.141  57.150   7.554  1.00120.27           N  
ANISOU  262  N   ASP A  38    19480  10896  15320  -3678  -2303    335       N  
ATOM    263  CA  ASP A  38      13.389  57.051   6.784  1.00122.37           C  
ANISOU  263  CA  ASP A  38    19148  11079  16270  -3976  -2209    597       C  
ATOM    264  C   ASP A  38      13.581  55.675   6.134  1.00118.89           C  
ANISOU  264  C   ASP A  38    18158  11032  15981  -3883  -1844    705       C  
ATOM    265  O   ASP A  38      13.824  54.689   6.822  1.00118.41           O  
ANISOU  265  O   ASP A  38    17903  11110  15976  -3889  -2084    646       O  
ATOM    266  CB  ASP A  38      14.606  57.291   7.686  1.00127.30           C  
ANISOU  266  CB  ASP A  38    19626  11321  17420  -4359  -2838    637       C  
ATOM    267  CG  ASP A  38      14.774  58.747   8.097  1.00132.87           C  
ANISOU  267  CG  ASP A  38    20778  11535  18170  -4555  -3207    597       C  
ATOM    268  OD1 ASP A  38      14.388  59.663   7.329  1.00134.42           O  
ANISOU  268  OD1 ASP A  38    21167  11638  18270  -4498  -2877    654       O  
ATOM    269  OD2 ASP A  38      15.329  58.988   9.196  1.00137.97           O  
ANISOU  269  OD2 ASP A  38    21616  11850  18958  -4779  -3873    514       O  
ATOM    270  N   LYS A  39      13.470  55.615   4.809  1.00116.41           N  
ANISOU  270  N   LYS A  39    17655  10868  15707  -3792  -1272    861       N  
ATOM    271  CA  LYS A  39      13.815  54.415   4.032  1.00113.78           C  
ANISOU  271  CA  LYS A  39    16829  10829  15574  -3732   -872    987       C  
ATOM    272  C   LYS A  39      15.290  54.503   3.615  1.00118.83           C  
ANISOU  272  C   LYS A  39    16915  11223  17013  -4065   -781   1244       C  
ATOM    273  O   LYS A  39      15.625  55.204   2.668  1.00121.78           O  
ANISOU  273  O   LYS A  39    17254  11423  17596  -4163   -405   1430       O  
ATOM    274  CB  LYS A  39      12.905  54.298   2.798  1.00107.76           C  
ANISOU  274  CB  LYS A  39    16251  10305  14387  -3451   -313   1019       C  
ATOM    275  CG  LYS A  39      11.385  54.350   3.115  1.00106.94           C  
ANISOU  275  CG  LYS A  39    16637  10390  13606  -3119   -386    801       C  
ATOM    276  CD  LYS A  39      10.516  54.200   1.845  1.00105.49           C  
ANISOU  276  CD  LYS A  39    16611  10398  13071  -2860     66    856       C  
ATOM    277  CE  LYS A  39      10.730  55.329   0.805  1.00108.38           C  
ANISOU  277  CE  LYS A  39    17175  10500  13505  -2949    331   1035       C  
ATOM    278  NZ  LYS A  39       9.724  55.253  -0.308  1.00106.56           N  
ANISOU  278  NZ  LYS A  39    17236  10412  12841  -2674    638   1065       N  
ATOM    279  N   PRO A  40      16.172  53.763   4.299  1.00121.94           N  
ANISOU  279  N   PRO A  40    16858  11582  17890  -4232  -1101   1276       N  
ATOM    280  CA  PRO A  40      17.622  53.969   4.245  1.00127.63           C  
ANISOU  280  CA  PRO A  40    17008  11972  19514  -4589  -1196   1513       C  
ATOM    281  C   PRO A  40      18.305  53.450   2.985  1.00129.15           C  
ANISOU  281  C   PRO A  40    16671  12227  20172  -4597   -481   1767       C  
ATOM    282  O   PRO A  40      19.521  53.589   2.862  1.00134.02           O  
ANISOU  282  O   PRO A  40    16734  12554  21633  -4878   -457   1996       O  
ATOM    283  CB  PRO A  40      18.116  53.154   5.433  1.00128.50           C  
ANISOU  283  CB  PRO A  40    16864  12071  19888  -4686  -1815   1435       C  
ATOM    284  CG  PRO A  40      17.209  51.971   5.423  1.00123.43           C  
ANISOU  284  CG  PRO A  40    16352  11891  18656  -4342  -1606   1273       C  
ATOM    285  CD  PRO A  40      15.851  52.475   4.937  1.00119.24           C  
ANISOU  285  CD  PRO A  40    16427  11551  17327  -4061  -1277   1132       C  
ATOM    286  N   ASN A  41      17.550  52.816   2.090  1.00125.60           N  
ANISOU  286  N   ASN A  41    16391  12122  19210  -4290     85   1729       N  
ATOM    287  CA  ASN A  41      18.004  52.631   0.713  1.00127.59           C  
ANISOU  287  CA  ASN A  41    16410  12369  19698  -4264    867   1957       C  
ATOM    288  C   ASN A  41      16.834  52.375  -0.232  1.00123.80           C  
ANISOU  288  C   ASN A  41    16442  12187  18408  -3923   1326   1866       C  
ATOM    289  O   ASN A  41      15.688  52.393   0.200  1.00119.76           O  
ANISOU  289  O   ASN A  41    16378  11875  17252  -3721   1030   1644       O  
ATOM    290  CB  ASN A  41      19.096  51.556   0.599  1.00129.89           C  
ANISOU  290  CB  ASN A  41    15983  12664  20705  -4340   1084   2110       C  
ATOM    291  CG  ASN A  41      18.552  50.132   0.692  1.00125.28           C  
ANISOU  291  CG  ASN A  41    15383  12481  19737  -4053   1128   1947       C  
ATOM    292  OD1 ASN A  41      17.653  49.836   1.482  1.00121.66           O  
ANISOU  292  OD1 ASN A  41    15252  12245  18729  -3906    674   1709       O  
ATOM    293  ND2 ASN A  41      19.123  49.237  -0.108  1.00125.93           N  
ANISOU  293  ND2 ASN A  41    15083  12625  20139  -3975   1707   2084       N  
ATOM    294  N   GLU A  42      17.133  52.192  -1.521  1.00125.87           N  
ANISOU  294  N   GLU A  42    16666  12432  18728  -3867   2044   2051       N  
ATOM    295  CA  GLU A  42      16.110  52.026  -2.553  1.00123.42           C  
ANISOU  295  CA  GLU A  42    16901  12321  17670  -3572   2450   1999       C  
ATOM    296  C   GLU A  42      15.363  50.720  -2.365  1.00118.77           C  
ANISOU  296  C   GLU A  42    16348  12120  16657  -3296   2347   1798       C  
ATOM    297  O   GLU A  42      14.146  50.643  -2.571  1.00115.34           O  
ANISOU  297  O   GLU A  42    16390  11887  15548  -3052   2260   1646       O  
ATOM    298  CB  GLU A  42      16.754  52.048  -3.934  1.00127.50           C  
ANISOU  298  CB  GLU A  42    17413  12674  18357  -3593   3256   2255       C  
ATOM    299  CG  GLU A  42      15.769  51.914  -5.098  1.00126.47           C  
ANISOU  299  CG  GLU A  42    17944  12677  17431  -3309   3641   2223       C  
ATOM    300  CD  GLU A  42      16.384  52.320  -6.452  1.00132.59           C  
ANISOU  300  CD  GLU A  42    18917  13178  18283  -3364   4433   2499       C  
ATOM    301  OE1 GLU A  42      17.568  52.770  -6.499  1.00137.64           O  
ANISOU  301  OE1 GLU A  42    19129  13519  19650  -3630   4740   2733       O  
ATOM    302  OE2 GLU A  42      15.664  52.199  -7.479  1.00132.60           O  
ANISOU  302  OE2 GLU A  42    19534  13233  17617  -3143   4743   2494       O  
ATOM    303  N   PHE A  43      16.099  49.692  -1.961  1.00119.01           N  
ANISOU  303  N   PHE A  43    15846  12231  17143  -3341   2333   1809       N  
ATOM    304  CA  PHE A  43      15.543  48.354  -1.856  1.00115.31           C  
ANISOU  304  CA  PHE A  43    15359  12098  16355  -3099   2295   1650       C  
ATOM    305  C   PHE A  43      14.435  48.316  -0.826  1.00111.21           C  
ANISOU  305  C   PHE A  43    15109  11786  15358  -2981   1686   1405       C  
ATOM    306  O   PHE A  43      13.528  47.474  -0.942  1.00107.79           O  
ANISOU  306  O   PHE A  43    14869  11632  14455  -2735   1681   1264       O  
ATOM    307  CB  PHE A  43      16.652  47.352  -1.507  1.00117.17           C  
ANISOU  307  CB  PHE A  43    14931  12320  17268  -3193   2345   1728       C  
ATOM    308  CG  PHE A  43      16.279  45.895  -1.737  1.00114.27           C  
ANISOU  308  CG  PHE A  43    14529  12245  16642  -2943   2500   1619       C  
ATOM    309  CD1 PHE A  43      16.430  44.949  -0.718  1.00111.67           C  
ANISOU  309  CD1 PHE A  43    13847  12058  16526  -2939   2070   1517       C  
ATOM    310  CD2 PHE A  43      15.812  45.463  -2.983  1.00113.86           C  
ANISOU  310  CD2 PHE A  43    14840  12286  16134  -2722   3056   1626       C  
ATOM    311  CE1 PHE A  43      16.110  43.611  -0.930  1.00108.99           C  
ANISOU  311  CE1 PHE A  43    13473  11961  15979  -2720   2209   1425       C  
ATOM    312  CE2 PHE A  43      15.485  44.118  -3.200  1.00111.14           C  
ANISOU  312  CE2 PHE A  43    14490  12173  15565  -2503   3167   1519       C  
ATOM    313  CZ  PHE A  43      15.638  43.194  -2.168  1.00108.69           C  
ANISOU  313  CZ  PHE A  43    13778  12012  15507  -2505   2754   1421       C  
ATOM    314  N   ASN A  44      14.533  49.198   0.185  1.00111.94           N  
ANISOU  314  N   ASN A  44    15222  11712  15597  -3157   1192   1360       N  
ATOM    315  CA  ASN A  44      13.517  49.326   1.237  1.00108.76           C  
ANISOU  315  CA  ASN A  44    15141  11436  14746  -3048    673   1135       C  
ATOM    316  C   ASN A  44      12.447  50.272   0.763  1.00107.48           C  
ANISOU  316  C   ASN A  44    15524  11252  14060  -2902    751   1082       C  
ATOM    317  O   ASN A  44      12.711  51.439   0.584  1.00110.26           O  
ANISOU  317  O   ASN A  44    16028  11336  14529  -3046    760   1169       O  
ATOM    318  CB  ASN A  44      14.135  49.837   2.551  1.00110.84           C  
ANISOU  318  CB  ASN A  44    15278  11475  15362  -3294     97   1099       C  
ATOM    319  CG  ASN A  44      13.195  49.684   3.751  1.00108.48           C  
ANISOU  319  CG  ASN A  44    15314  11305  14597  -3162   -375    863       C  
ATOM    320  OD1 ASN A  44      12.040  50.096   3.695  1.00106.17           O  
ANISOU  320  OD1 ASN A  44    15462  11101  13775  -2960   -336    742       O  
ATOM    321  ND2 ASN A  44      13.699  49.093   4.846  1.00109.84           N  
ANISOU  321  ND2 ASN A  44    15288  11456  14992  -3272   -813    811       N  
ATOM    322  N   ILE A  45      11.237  49.763   0.555  1.00104.10           N  
ANISOU  322  N   ILE A  45    15369  11081  13103  -2619    786    952       N  
ATOM    323  CA  ILE A  45      10.140  50.594   0.081  1.00103.22           C  
ANISOU  323  CA  ILE A  45    15739  10936  12542  -2449    822    913       C  
ATOM    324  C   ILE A  45       9.105  50.865   1.162  1.00101.46           C  
ANISOU  324  C   ILE A  45    15756  10770  12024  -2312    435    716       C  
ATOM    325  O   ILE A  45       7.954  51.125   0.832  1.00100.36           O  
ANISOU  325  O   ILE A  45    15924  10688  11518  -2086    459    657       O  
ATOM    326  CB  ILE A  45       9.402  49.955  -1.103  1.00101.52           C  
ANISOU  326  CB  ILE A  45    15706  10900  11967  -2212   1136    936       C  
ATOM    327  CG1 ILE A  45       8.644  48.722  -0.641  1.00 97.67           C  
ANISOU  327  CG1 ILE A  45    15113  10719  11277  -2017    981    785       C  
ATOM    328  CG2 ILE A  45      10.390  49.627  -2.266  1.00104.04           C  
ANISOU  328  CG2 ILE A  45    15894  11138  12497  -2308   1630   1128       C  
ATOM    329  CD1 ILE A  45       7.230  48.697  -1.144  1.00 95.25           C  
ANISOU  329  CD1 ILE A  45    15144  10518  10527  -1748    944    718       C  
ATOM    330  N   GLY A  46       9.498  50.784   2.440  1.00101.90           N  
ANISOU  330  N   GLY A  46    15692  10781  12244  -2436     86    622       N  
ATOM    331  CA  GLY A  46       8.633  51.202   3.558  1.00100.94           C  
ANISOU  331  CA  GLY A  46    15890  10629  11834  -2323   -226    439       C  
ATOM    332  C   GLY A  46       8.294  50.067   4.472  1.00 98.68           C  
ANISOU  332  C   GLY A  46    15497  10569  11427  -2222   -388    313       C  
ATOM    333  O   GLY A  46       8.154  50.271   5.690  1.00 99.40           O  
ANISOU  333  O   GLY A  46    15793  10564  11409  -2241   -688    186       O  
ATOM    334  N   ILE A  47       8.149  48.879   3.877  1.00 96.47           N  
ANISOU  334  N   ILE A  47    14959  10560  11136  -2113   -182    349       N  
ATOM    335  CA  ILE A  47       8.054  47.615   4.629  1.00 94.52           C  
ANISOU  335  CA  ILE A  47    14528  10527  10859  -2057   -310    271       C  
ATOM    336  C   ILE A  47       9.455  47.249   5.090  1.00 96.58           C  
ANISOU  336  C   ILE A  47    14460  10687  11548  -2321   -505    341       C  
ATOM    337  O   ILE A  47      10.372  47.089   4.261  1.00 98.20           O  
ANISOU  337  O   ILE A  47    14348  10852  12110  -2446   -302    487       O  
ATOM    338  CB  ILE A  47       7.463  46.501   3.764  1.00 91.91           C  
ANISOU  338  CB  ILE A  47    14041  10474  10405  -1864    -49    292       C  
ATOM    339  CG1 ILE A  47       5.981  46.792   3.507  1.00 90.01           C  
ANISOU  339  CG1 ILE A  47    14085  10305   9811  -1603     26    223       C  
ATOM    340  CG2 ILE A  47       7.659  45.149   4.444  1.00 90.66           C  
ANISOU  340  CG2 ILE A  47    13629  10501  10315  -1861   -169    248       C  
ATOM    341  CD1 ILE A  47       5.383  45.988   2.425  1.00 88.50           C  
ANISOU  341  CD1 ILE A  47    13820  10296   9509  -1438    223    264       C  
ATOM    342  N   GLY A  48       9.628  47.164   6.409  1.00 97.31           N  
ANISOU  342  N   GLY A  48    14655  10697  11623  -2403   -895    249       N  
ATOM    343  CA  GLY A  48      10.959  47.018   7.020  1.00100.07           C  
ANISOU  343  CA  GLY A  48    14739  10861  12421  -2679  -1237    319       C  
ATOM    344  C   GLY A  48      11.496  48.331   7.589  1.00103.64           C  
ANISOU  344  C   GLY A  48    15428  10941  13008  -2900  -1575    315       C  
ATOM    345  O   GLY A  48      12.427  48.333   8.397  1.00106.61           O  
ANISOU  345  O   GLY A  48    15709  11101  13699  -3131  -2022    340       O  
ATOM    346  N   ALA A  49      10.911  49.449   7.169  1.00103.54           N  
ANISOU  346  N   ALA A  49    15738  10822  12779  -2834  -1409    289       N  
ATOM    347  CA  ALA A  49      11.364  50.758   7.586  1.00107.08           C  
ANISOU  347  CA  ALA A  49    16444  10894  13347  -3037  -1698    285       C  
ATOM    348  C   ALA A  49      11.389  50.912   9.107  1.00109.09           C  
ANISOU  348  C   ALA A  49    17094  10945  13410  -3111  -2240    131       C  
ATOM    349  O   ALA A  49      12.371  51.402   9.699  1.00112.88           O  
ANISOU  349  O   ALA A  49    17578  11092  14218  -3398  -2704    167       O  
ATOM    350  CB  ALA A  49      10.470  51.804   6.980  1.00106.62           C  
ANISOU  350  CB  ALA A  49    16745  10784  12983  -2880  -1424    252       C  
ATOM    351  N   LEU A  50      10.300  50.493   9.735  1.00106.90           N  
ANISOU  351  N   LEU A  50    17175  10834  12606  -2856  -2183    -30       N  
ATOM    352  CA  LEU A  50      10.156  50.623  11.182  1.00108.87           C  
ANISOU  352  CA  LEU A  50    17953  10880  12534  -2874  -2604   -190       C  
ATOM    353  C   LEU A  50      10.486  49.322  11.941  1.00108.29           C  
ANISOU  353  C   LEU A  50    17745  10936  12465  -2905  -2858   -194       C  
ATOM    354  O   LEU A  50      11.167  49.352  12.970  1.00111.67           O  
ANISOU  354  O   LEU A  50    18404  11094  12930  -3099  -3408   -228       O  
ATOM    355  CB  LEU A  50       8.743  51.125  11.517  1.00107.87           C  
ANISOU  355  CB  LEU A  50    18387  10770  11829  -2567  -2334   -358       C  
ATOM    356  CG  LEU A  50       8.509  52.610  11.164  1.00109.31           C  
ANISOU  356  CG  LEU A  50    18876  10682  11974  -2564  -2262   -387       C  
ATOM    357  CD1 LEU A  50       7.041  53.028  11.269  1.00107.78           C  
ANISOU  357  CD1 LEU A  50    19097  10532  11322  -2209  -1895   -520       C  
ATOM    358  CD2 LEU A  50       9.353  53.485  12.061  1.00113.59           C  
ANISOU  358  CD2 LEU A  50    19810  10767  12580  -2837  -2813   -445       C  
ATOM    359  N   GLY A  51      10.026  48.189  11.426  1.00104.41           N  
ANISOU  359  N   GLY A  51    16907  10821  11942  -2723  -2506   -153       N  
ATOM    360  CA  GLY A  51      10.203  46.907  12.113  1.00103.78           C  
ANISOU  360  CA  GLY A  51    16723  10877  11832  -2718  -2700   -154       C  
ATOM    361  C   GLY A  51      11.124  45.911  11.434  1.00102.92           C  
ANISOU  361  C   GLY A  51    15919  10927  12258  -2831  -2686      9       C  
ATOM    362  O   GLY A  51      11.100  44.728  11.769  1.00101.48           O  
ANISOU  362  O   GLY A  51    15592  10918  12047  -2770  -2735     17       O  
ATOM    363  N   GLY A  52      11.929  46.385  10.481  1.00104.03           N  
ANISOU  363  N   GLY A  52    15646  10986  12896  -2986  -2578    146       N  
ATOM    364  CA  GLY A  52      12.879  45.535   9.749  1.00104.05           C  
ANISOU  364  CA  GLY A  52    14975  11087  13473  -3081  -2467    314       C  
ATOM    365  C   GLY A  52      12.208  44.337   9.115  1.00100.06           C  
ANISOU  365  C   GLY A  52    14264  10963  12789  -2834  -2036    309       C  
ATOM    366  O   GLY A  52      11.069  44.437   8.697  1.00 97.41           O  
ANISOU  366  O   GLY A  52    14171  10816  12023  -2609  -1692    229       O  
ATOM    367  N   LEU A  53      12.903  43.201   9.054  1.00100.08           N  
ANISOU  367  N   LEU A  53    13818  11051  13157  -2873  -2084    397       N  
ATOM    368  CA  LEU A  53      12.344  41.979   8.480  1.00 96.66           C  
ANISOU  368  CA  LEU A  53    13200  10945  12580  -2653  -1722    389       C  
ATOM    369  C   LEU A  53      11.159  41.478   9.309  1.00 94.46           C  
ANISOU  369  C   LEU A  53    13336  10833  11722  -2467  -1800    245       C  
ATOM    370  O   LEU A  53      10.297  40.725   8.814  1.00 91.25           O  
ANISOU  370  O   LEU A  53    12904  10691  11077  -2257  -1474    212       O  
ATOM    371  CB  LEU A  53      13.414  40.888   8.399  1.00 97.89           C  
ANISOU  371  CB  LEU A  53    12812  11098  13284  -2738  -1808    510       C  
ATOM    372  CG  LEU A  53      13.080  39.720   7.477  1.00 94.76           C  
ANISOU  372  CG  LEU A  53    12165  10980  12858  -2534  -1355    525       C  
ATOM    373  CD1 LEU A  53      13.312  40.116   6.015  1.00 94.15           C  
ANISOU  373  CD1 LEU A  53    11901  10907  12964  -2503   -812    613       C  
ATOM    374  CD2 LEU A  53      13.892  38.493   7.862  1.00 95.97           C  
ANISOU  374  CD2 LEU A  53    11914  11126  13425  -2574  -1563    597       C  
ATOM    375  N   GLY A  54      11.125  41.882  10.581  1.00 96.57           N  
ANISOU  375  N   GLY A  54    14008  10912  11773  -2550  -2230    168       N  
ATOM    376  CA  GLY A  54       9.969  41.617  11.440  1.00 95.42           C  
ANISOU  376  CA  GLY A  54    14345  10859  11051  -2373  -2224     39       C  
ATOM    377  C   GLY A  54       8.651  42.103  10.827  1.00 93.00           C  
ANISOU  377  C   GLY A  54    14239  10711  10387  -2139  -1758    -34       C  
ATOM    378  O   GLY A  54       7.587  41.503  11.035  1.00 91.00           O  
ANISOU  378  O   GLY A  54    14122  10637   9816  -1937  -1549    -89       O  
ATOM    379  N   ASP A  55       8.719  43.200  10.075  1.00 93.65           N  
ANISOU  379  N   ASP A  55    14323  10695  10562  -2171  -1610    -17       N  
ATOM    380  CA  ASP A  55       7.559  43.671   9.316  1.00 91.94           C  
ANISOU  380  CA  ASP A  55    14232  10601  10099  -1954  -1212    -56       C  
ATOM    381  C   ASP A  55       7.130  42.572   8.304  1.00 89.11           C  
ANISOU  381  C   ASP A  55    13517  10540   9800  -1804   -897     -1       C  
ATOM    382  O   ASP A  55       5.950  42.215   8.213  1.00 87.36           O  
ANISOU  382  O   ASP A  55    13387  10476   9332  -1591   -698    -47       O  
ATOM    383  CB  ASP A  55       7.849  45.023   8.607  1.00 93.36           C  
ANISOU  383  CB  ASP A  55    14477  10594  10402  -2038  -1140    -21       C  
ATOM    384  CG  ASP A  55       7.801  46.221   9.550  1.00 96.38           C  
ANISOU  384  CG  ASP A  55    15343  10678  10597  -2106  -1390   -116       C  
ATOM    385  OD1 ASP A  55       8.493  47.215   9.259  1.00 98.66           O  
ANISOU  385  OD1 ASP A  55    15645  10738  11102  -2280  -1497    -68       O  
ATOM    386  OD2 ASP A  55       7.087  46.177  10.573  1.00 97.17           O  
ANISOU  386  OD2 ASP A  55    15838  10743  10338  -1988  -1457   -234       O  
ATOM    387  N   TRP A  56       8.091  42.023   7.564  1.00 89.11           N  
ANISOU  387  N   TRP A  56    13119  10583  10158  -1913   -853    102       N  
ATOM    388  CA  TRP A  56       7.773  40.982   6.616  1.00 86.82           C  
ANISOU  388  CA  TRP A  56    12572  10521   9894  -1778   -579    140       C  
ATOM    389  C   TRP A  56       7.208  39.749   7.295  1.00 84.98           C  
ANISOU  389  C   TRP A  56    12313  10460   9516  -1672   -655     92       C  
ATOM    390  O   TRP A  56       6.298  39.143   6.749  1.00 82.93           O  
ANISOU  390  O   TRP A  56    12026  10372   9110  -1499   -456     77       O  
ATOM    391  CB  TRP A  56       8.989  40.616   5.767  1.00 88.16           C  
ANISOU  391  CB  TRP A  56    12357  10656  10483  -1902   -458    256       C  
ATOM    392  CG  TRP A  56       9.128  41.413   4.525  1.00 88.98           C  
ANISOU  392  CG  TRP A  56    12483  10685  10639  -1904   -148    326       C  
ATOM    393  CD1 TRP A  56      10.213  42.139   4.156  1.00 92.43           C  
ANISOU  393  CD1 TRP A  56    12773  10917  11430  -2089    -85    434       C  
ATOM    394  CD2 TRP A  56       8.164  41.562   3.470  1.00 87.28           C  
ANISOU  394  CD2 TRP A  56    12469  10564  10130  -1722    129    313       C  
ATOM    395  NE1 TRP A  56       9.997  42.744   2.936  1.00 93.13           N  
ANISOU  395  NE1 TRP A  56    12999  10969  11416  -2031    265    491       N  
ATOM    396  CE2 TRP A  56       8.744  42.404   2.494  1.00 89.84           C  
ANISOU  396  CE2 TRP A  56    12822  10730  10583  -1804    366    414       C  
ATOM    397  CE3 TRP A  56       6.876  41.076   3.256  1.00 84.68           C  
ANISOU  397  CE3 TRP A  56    12295  10404   9477  -1509    171    243       C  
ATOM    398  CZ2 TRP A  56       8.069  42.774   1.309  1.00 89.31           C  
ANISOU  398  CZ2 TRP A  56    13012  10666  10256  -1669    619    439       C  
ATOM    399  CZ3 TRP A  56       6.208  41.424   2.081  1.00 84.65           C  
ANISOU  399  CZ3 TRP A  56    12485  10399   9280  -1382    369    267       C  
ATOM    400  CH2 TRP A  56       6.807  42.262   1.119  1.00 86.91           C  
ANISOU  400  CH2 TRP A  56    12872  10523   9627  -1459    579    361       C  
ATOM    401  N   PHE A  57       7.739  39.360   8.457  1.00 86.16           N  
ANISOU  401  N   PHE A  57    12488  10535   9715  -1782   -968     82       N  
ATOM    402  CA  PHE A  57       7.206  38.168   9.179  1.00 85.02           C  
ANISOU  402  CA  PHE A  57    12366  10529   9410  -1689  -1033     55       C  
ATOM    403  C   PHE A  57       5.784  38.430   9.703  1.00 84.07           C  
ANISOU  403  C   PHE A  57    12604  10455   8886  -1512   -892    -25       C  
ATOM    404  O   PHE A  57       4.896  37.553   9.618  1.00 82.23           O  
ANISOU  404  O   PHE A  57    12302  10390   8551  -1363   -727    -26       O  
ATOM    405  CB  PHE A  57       8.131  37.729  10.325  1.00 87.03           C  
ANISOU  405  CB  PHE A  57    12636  10647   9786  -1852  -1447     79       C  
ATOM    406  CG  PHE A  57       7.613  36.538  11.109  1.00 86.13           C  
ANISOU  406  CG  PHE A  57    12606  10641   9478  -1768  -1512     69       C  
ATOM    407  CD1 PHE A  57       7.565  35.276  10.540  1.00 84.02           C  
ANISOU  407  CD1 PHE A  57    11998  10559   9367  -1692  -1376    116       C  
ATOM    408  CD2 PHE A  57       7.176  36.691  12.426  1.00 87.42           C  
ANISOU  408  CD2 PHE A  57    13247  10689   9281  -1764  -1689     15       C  
ATOM    409  CE1 PHE A  57       7.091  34.186  11.271  1.00 83.34           C  
ANISOU  409  CE1 PHE A  57    11994  10550   9122  -1628  -1438    122       C  
ATOM    410  CE2 PHE A  57       6.702  35.611  13.156  1.00 86.62           C  
ANISOU  410  CE2 PHE A  57    13261  10661   8989  -1693  -1707     29       C  
ATOM    411  CZ  PHE A  57       6.657  34.356  12.582  1.00 84.36           C  
ANISOU  411  CZ  PHE A  57    12583  10570   8902  -1633  -1592     89       C  
ATOM    412  N   ALA A  58       5.589  39.646  10.222  1.00 85.50           N  
ANISOU  412  N   ALA A  58    13146  10455   8885  -1528   -943    -85       N  
ATOM    413  CA  ALA A  58       4.264  40.136  10.615  1.00 85.20           C  
ANISOU  413  CA  ALA A  58    13435  10407   8530  -1336   -726   -156       C  
ATOM    414  C   ALA A  58       3.292  39.881   9.474  1.00 82.84           C  
ANISOU  414  C   ALA A  58    12891  10292   8293  -1154   -422   -125       C  
ATOM    415  O   ALA A  58       2.249  39.272   9.644  1.00 81.94           O  
ANISOU  415  O   ALA A  58    12755  10285   8095   -995   -254   -124       O  
ATOM    416  CB  ALA A  58       4.332  41.647  10.955  1.00 87.18           C  
ANISOU  416  CB  ALA A  58    14067  10407   8649  -1373   -788   -223       C  
ATOM    417  N   ILE A  59       3.675  40.355   8.291  1.00 82.57           N  
ANISOU  417  N   ILE A  59    12687  10260   8424  -1191   -372    -85       N  
ATOM    418  CA  ILE A  59       2.847  40.246   7.086  1.00 80.89           C  
ANISOU  418  CA  ILE A  59    12330  10162   8243  -1037   -168    -52       C  
ATOM    419  C   ILE A  59       2.636  38.804   6.727  1.00 79.14           C  
ANISOU  419  C   ILE A  59    11838  10131   8101   -988   -137    -18       C  
ATOM    420  O   ILE A  59       1.516  38.382   6.496  1.00 78.79           O  
ANISOU  420  O   ILE A  59    11741  10170   8025   -830    -42    -12       O  
ATOM    421  CB  ILE A  59       3.467  41.017   5.886  1.00 81.15           C  
ANISOU  421  CB  ILE A  59    12330  10119   8385  -1110   -119     -3       C  
ATOM    422  CG1 ILE A  59       3.381  42.544   6.126  1.00 82.88           C  
ANISOU  422  CG1 ILE A  59    12844  10129   8518  -1124   -134    -34       C  
ATOM    423  CG2 ILE A  59       2.755  40.652   4.595  1.00 79.52           C  
ANISOU  423  CG2 ILE A  59    12034  10012   8170   -969     19     39       C  
ATOM    424  CD1 ILE A  59       4.147  43.389   5.049  1.00 83.99           C  
ANISOU  424  CD1 ILE A  59    12984  10149   8780  -1236    -78     39       C  
ATOM    425  N   GLY A  60       3.712  38.043   6.706  1.00 78.94           N  
ANISOU  425  N   GLY A  60    11622  10146   8224  -1122   -234     12       N  
ATOM    426  CA  GLY A  60       3.615  36.615   6.393  1.00 77.78           C  
ANISOU  426  CA  GLY A  60    11239  10155   8160  -1079   -216     37       C  
ATOM    427  C   GLY A  60       2.666  35.887   7.341  1.00 77.30           C  
ANISOU  427  C   GLY A  60    11218  10167   7988   -987   -229     22       C  
ATOM    428  O   GLY A  60       1.958  34.947   6.962  1.00 75.68           O  
ANISOU  428  O   GLY A  60    10865  10072   7818   -891   -172     43       O  
ATOM    429  N   MET A  61       2.660  36.327   8.592  1.00 78.63           N  
ANISOU  429  N   MET A  61    11622  10239   8014  -1022   -299     -7       N  
ATOM    430  CA  MET A  61       1.844  35.673   9.597  1.00 78.91           C  
ANISOU  430  CA  MET A  61    11761  10304   7918   -943   -244     -4       C  
ATOM    431  C   MET A  61       0.382  36.073   9.449  1.00 79.07           C  
ANISOU  431  C   MET A  61    11824  10326   7893   -751      4     -5       C  
ATOM    432  O   MET A  61      -0.511  35.241   9.685  1.00 79.20           O  
ANISOU  432  O   MET A  61    11730  10411   7952   -655    127     39       O  
ATOM    433  CB  MET A  61       2.381  35.966  11.011  1.00 80.71           C  
ANISOU  433  CB  MET A  61    12335  10381   7951  -1043   -403    -34       C  
ATOM    434  CG  MET A  61       3.694  35.272  11.279  1.00 80.48           C  
ANISOU  434  CG  MET A  61    12189  10336   8055  -1220   -711     -1       C  
ATOM    435  SD  MET A  61       3.562  33.495  10.912  1.00 78.60           S  
ANISOU  435  SD  MET A  61    11586  10289   7990  -1180   -685     69       S  
ATOM    436  CE  MET A  61       2.759  32.958  12.433  1.00 79.68           C  
ANISOU  436  CE  MET A  61    12078  10372   7824  -1127   -642     88       C  
ATOM    437  N   ALA A  62       0.146  37.328   9.080  1.00 79.52           N  
ANISOU  437  N   ALA A  62    12016  10283   7916   -698     71    -38       N  
ATOM    438  CA  ALA A  62      -1.189  37.779   8.724  1.00 80.18           C  
ANISOU  438  CA  ALA A  62    12065  10340   8059   -504    269    -22       C  
ATOM    439  C   ALA A  62      -1.767  36.840   7.665  1.00 78.69           C  
ANISOU  439  C   ALA A  62    11534  10283   8080   -442    242     42       C  
ATOM    440  O   ALA A  62      -2.900  36.376   7.757  1.00 79.18           O  
ANISOU  440  O   ALA A  62    11445  10361   8281   -315    354     93       O  
ATOM    441  CB  ALA A  62      -1.134  39.240   8.194  1.00 80.98           C  
ANISOU  441  CB  ALA A  62    12333  10306   8130   -476    274    -57       C  
ATOM    442  N   PHE A  63      -0.964  36.577   6.654  1.00 77.42           N  
ANISOU  442  N   PHE A  63    11273  10183   7959   -536     98     45       N  
ATOM    443  CA  PHE A  63      -1.326  35.623   5.633  1.00 76.98           C  
ANISOU  443  CA  PHE A  63    10998  10216   8034   -498     27     85       C  
ATOM    444  C   PHE A  63      -1.547  34.203   6.223  1.00 76.61           C  
ANISOU  444  C   PHE A  63    10773  10269   8068   -512     15    114       C  
ATOM    445  O   PHE A  63      -2.601  33.581   6.037  1.00 76.76           O  
ANISOU  445  O   PHE A  63    10623  10304   8239   -420     18    164       O  
ATOM    446  CB  PHE A  63      -0.200  35.554   4.560  1.00 76.68           C  
ANISOU  446  CB  PHE A  63    10973  10191   7971   -600    -47     74       C  
ATOM    447  CG  PHE A  63      -0.397  36.461   3.377  1.00 77.19           C  
ANISOU  447  CG  PHE A  63    11176  10163   7989   -546    -50     86       C  
ATOM    448  CD1 PHE A  63      -1.157  36.048   2.295  1.00 76.73           C  
ANISOU  448  CD1 PHE A  63    11106  10090   7957   -451   -148    115       C  
ATOM    449  CD2 PHE A  63       0.198  37.721   3.349  1.00 77.76           C  
ANISOU  449  CD2 PHE A  63    11430  10130   7985   -603      5     76       C  
ATOM    450  CE1 PHE A  63      -1.348  36.887   1.212  1.00 77.87           C  
ANISOU  450  CE1 PHE A  63    11456  10115   8016   -401   -193    138       C  
ATOM    451  CE2 PHE A  63       0.033  38.543   2.266  1.00 78.67           C  
ANISOU  451  CE2 PHE A  63    11713  10140   8038   -559      6    104       C  
ATOM    452  CZ  PHE A  63      -0.745  38.125   1.187  1.00 78.44           C  
ANISOU  452  CZ  PHE A  63    11710  10095   7996   -452    -94    137       C  
ATOM    453  N   ALA A  64      -0.509  33.699   6.896  1.00 76.38           N  
ANISOU  453  N   ALA A  64    10770  10278   7974   -637    -34     97       N  
ATOM    454  CA  ALA A  64      -0.431  32.304   7.303  1.00 75.72           C  
ANISOU  454  CA  ALA A  64    10538  10273   7957   -674    -87    130       C  
ATOM    455  C   ALA A  64      -1.602  31.951   8.195  1.00 76.37           C  
ANISOU  455  C   ALA A  64    10607  10345   8064   -589     49    183       C  
ATOM    456  O   ALA A  64      -2.282  30.978   7.973  1.00 76.49           O  
ANISOU  456  O   ALA A  64    10422  10402   8237   -550     44    237       O  
ATOM    457  CB  ALA A  64       0.886  32.053   8.037  1.00 76.01           C  
ANISOU  457  CB  ALA A  64    10638  10301   7940   -818   -202    116       C  
ATOM    458  N   LEU A  65      -1.844  32.761   9.202  1.00 77.39           N  
ANISOU  458  N   LEU A  65    10969  10387   8047   -557    196    172       N  
ATOM    459  CA  LEU A  65      -2.881  32.445  10.146  1.00 78.90           C  
ANISOU  459  CA  LEU A  65    11192  10534   8253   -468    427    235       C  
ATOM    460  C   LEU A  65      -4.290  32.537   9.508  1.00 79.58           C  
ANISOU  460  C   LEU A  65    11012  10595   8628   -314    567    299       C  
ATOM    461  O   LEU A  65      -5.211  31.815   9.914  1.00 80.62           O  
ANISOU  461  O   LEU A  65    10975  10710   8946   -256    731    393       O  
ATOM    462  CB  LEU A  65      -2.712  33.318  11.401  1.00 80.72           C  
ANISOU  462  CB  LEU A  65    11846  10629   8194   -461    577    193       C  
ATOM    463  CG  LEU A  65      -1.342  33.110  12.077  1.00 80.75           C  
ANISOU  463  CG  LEU A  65    12099  10612   7970   -633    325    152       C  
ATOM    464  CD1 LEU A  65      -1.015  34.266  13.031  1.00 83.10           C  
ANISOU  464  CD1 LEU A  65    12887  10728   7962   -648    346     79       C  
ATOM    465  CD2 LEU A  65      -1.257  31.734  12.839  1.00 79.70           C  
ANISOU  465  CD2 LEU A  65    11968  10512   7802   -691    290    229       C  
ATOM    466  N   ALA A  66      -4.441  33.427   8.522  1.00 79.20           N  
ANISOU  466  N   ALA A  66    10924  10516   8652   -256    484    265       N  
ATOM    467  CA  ALA A  66      -5.683  33.567   7.774  1.00 80.16           C  
ANISOU  467  CA  ALA A  66    10788  10579   9092   -120    492    333       C  
ATOM    468  C   ALA A  66      -5.875  32.306   6.922  1.00 79.56           C  
ANISOU  468  C   ALA A  66    10436  10574   9221   -169    253    382       C  
ATOM    469  O   ALA A  66      -6.930  31.637   6.946  1.00 81.02           O  
ANISOU  469  O   ALA A  66    10340  10715   9728   -114    277    482       O  
ATOM    470  CB  ALA A  66      -5.659  34.842   6.904  1.00 79.84           C  
ANISOU  470  CB  ALA A  66    10853  10462   9022    -59    397    288       C  
ATOM    471  N   ILE A  67      -4.849  31.968   6.164  1.00 77.72           N  
ANISOU  471  N   ILE A  67    10284  10418   8827   -275     33    316       N  
ATOM    472  CA  ILE A  67      -4.905  30.781   5.337  1.00 77.13           C  
ANISOU  472  CA  ILE A  67    10049  10379   8879   -317   -192    334       C  
ATOM    473  C   ILE A  67      -5.288  29.580   6.177  1.00 77.33           C  
ANISOU  473  C   ILE A  67     9892  10435   9054   -351   -119    407       C  
ATOM    474  O   ILE A  67      -6.148  28.794   5.773  1.00 78.20           O  
ANISOU  474  O   ILE A  67     9770  10499   9445   -331   -244    478       O  
ATOM    475  CB  ILE A  67      -3.552  30.495   4.665  1.00 75.91           C  
ANISOU  475  CB  ILE A  67    10048  10287   8506   -417   -313    250       C  
ATOM    476  CG1 ILE A  67      -3.273  31.505   3.552  1.00 76.30           C  
ANISOU  476  CG1 ILE A  67    10285  10274   8432   -387   -384    205       C  
ATOM    477  CG2 ILE A  67      -3.499  29.044   4.127  1.00 75.13           C  
ANISOU  477  CG2 ILE A  67     9834  10210   8502   -457   -484    255       C  
ATOM    478  CD1 ILE A  67      -1.738  31.675   3.243  1.00 75.89           C  
ANISOU  478  CD1 ILE A  67    10398  10258   8178   -487   -331    138       C  
ATOM    479  N   ALA A  68      -4.631  29.433   7.329  1.00 76.65           N  
ANISOU  479  N   ALA A  68     9940  10400   8784   -413     45    397       N  
ATOM    480  CA  ALA A  68      -4.869  28.303   8.213  1.00 76.95           C  
ANISOU  480  CA  ALA A  68     9885  10451   8901   -456    131    478       C  
ATOM    481  C   ALA A  68      -6.330  28.316   8.674  1.00 78.97           C  
ANISOU  481  C   ALA A  68     9943  10610   9451   -357    365    601       C  
ATOM    482  O   ALA A  68      -7.030  27.327   8.577  1.00 79.48           O  
ANISOU  482  O   ALA A  68     9748  10645   9807   -371    327    699       O  
ATOM    483  CB  ALA A  68      -3.904  28.331   9.379  1.00 76.86           C  
ANISOU  483  CB  ALA A  68    10146  10462   8594   -534    219    451       C  
ATOM    484  N   ALA A  69      -6.786  29.454   9.153  1.00 80.51           N  
ANISOU  484  N   ALA A  69    10245  10730   9613   -253    618    604       N  
ATOM    485  CA  ALA A  69      -8.175  29.612   9.571  1.00 83.54           C  
ANISOU  485  CA  ALA A  69    10407  10987  10348   -126    919    731       C  
ATOM    486  C   ALA A  69      -9.176  29.100   8.514  1.00 84.38           C  
ANISOU  486  C   ALA A  69    10067  11031  10961    -96    681    824       C  
ATOM    487  O   ALA A  69     -10.176  28.422   8.857  1.00 86.31           O  
ANISOU  487  O   ALA A  69     9995  11185  11616    -74    834    975       O  
ATOM    488  CB  ALA A  69      -8.457  31.113   9.914  1.00 84.90           C  
ANISOU  488  CB  ALA A  69    10769  11059  10432     16   1182    690       C  
ATOM    489  N   VAL A  70      -8.904  29.467   7.252  1.00 83.05           N  
ANISOU  489  N   VAL A  70     9908  10879  10768   -101    305    743       N  
ATOM    490  CA  VAL A  70      -9.751  29.111   6.095  1.00 84.38           C  
ANISOU  490  CA  VAL A  70     9775  10945  11342    -81    -55    807       C  
ATOM    491  C   VAL A  70      -9.805  27.584   5.840  1.00 84.30           C  
ANISOU  491  C   VAL A  70     9592  10944  11495   -201   -289    854       C  
ATOM    492  O   VAL A  70     -10.875  26.972   5.751  1.00 86.42           O  
ANISOU  492  O   VAL A  70     9495  11082  12259   -197   -374    992       O  
ATOM    493  CB  VAL A  70      -9.243  29.844   4.801  1.00 83.27           C  
ANISOU  493  CB  VAL A  70     9860  10799  10981    -70   -405    696       C  
ATOM    494  CG1 VAL A  70      -9.888  29.260   3.545  1.00 84.54           C  
ANISOU  494  CG1 VAL A  70     9864  10831  11425    -83   -886    738       C  
ATOM    495  CG2 VAL A  70      -9.515  31.333   4.873  1.00 84.34           C  
ANISOU  495  CG2 VAL A  70    10085  10859  11100     61   -249    685       C  
ATOM    496  N   ILE A  71      -8.628  26.976   5.745  1.00 82.01           N  
ANISOU  496  N   ILE A  71     9548  10783  10827   -307   -390    746       N  
ATOM    497  CA  ILE A  71      -8.539  25.529   5.619  1.00 81.86           C  
ANISOU  497  CA  ILE A  71     9425  10765  10911   -412   -572    774       C  
ATOM    498  C   ILE A  71      -9.342  24.883   6.757  1.00 83.58           C  
ANISOU  498  C   ILE A  71     9379  10932  11445   -428   -282    939       C  
ATOM    499  O   ILE A  71     -10.286  24.159   6.480  1.00 85.71           O  
ANISOU  499  O   ILE A  71     9326  11073  12168   -454   -432   1058       O  
ATOM    500  CB  ILE A  71      -7.071  25.005   5.637  1.00 79.35           C  
ANISOU  500  CB  ILE A  71     9392  10583  10174   -499   -613    649       C  
ATOM    501  CG1 ILE A  71      -6.256  25.590   4.466  1.00 77.85           C  
ANISOU  501  CG1 ILE A  71     9459  10414   9706   -482   -814    507       C  
ATOM    502  CG2 ILE A  71      -7.070  23.502   5.584  1.00 79.05           C  
ANISOU  502  CG2 ILE A  71     9243  10516  10278   -587   -778    686       C  
ATOM    503  CD1 ILE A  71      -4.814  25.099   4.416  1.00 76.04           C  
ANISOU  503  CD1 ILE A  71     9433  10279   9179   -550   -810    404       C  
ATOM    504  N   TYR A  72      -9.004  25.181   8.014  1.00 83.11           N  
ANISOU  504  N   TYR A  72     9485  10936  11158   -415    128    958       N  
ATOM    505  CA  TYR A  72      -9.680  24.553   9.168  1.00 85.39           C  
ANISOU  505  CA  TYR A  72     9629  11154  11660   -429    488   1124       C  
ATOM    506  C   TYR A  72     -11.187  24.761   9.211  1.00 88.87           C  
ANISOU  506  C   TYR A  72     9651  11419  12696   -339    683   1299       C  
ATOM    507  O   TYR A  72     -11.903  23.983   9.866  1.00 91.22           O  
ANISOU  507  O   TYR A  72     9714  11617  13329   -372    928   1474       O  
ATOM    508  CB  TYR A  72      -9.102  25.026  10.509  1.00 85.36           C  
ANISOU  508  CB  TYR A  72    10006  11196  11232   -409    896   1107       C  
ATOM    509  CG  TYR A  72      -7.803  24.380  10.848  1.00 83.52           C  
ANISOU  509  CG  TYR A  72    10078  11071  10583   -526    733   1025       C  
ATOM    510  CD1 TYR A  72      -7.734  23.013  11.063  1.00 84.21           C  
ANISOU  510  CD1 TYR A  72    10077  11148  10770   -629    642   1108       C  
ATOM    511  CD2 TYR A  72      -6.623  25.125  10.941  1.00 82.69           C  
ANISOU  511  CD2 TYR A  72    10322  11054  10042   -539    642    876       C  
ATOM    512  CE1 TYR A  72      -6.509  22.398  11.353  1.00 82.75           C  
ANISOU  512  CE1 TYR A  72    10144  11038  10258   -723    458   1040       C  
ATOM    513  CE2 TYR A  72      -5.412  24.528  11.249  1.00 81.25           C  
ANISOU  513  CE2 TYR A  72    10354  10938   9579   -644    456    820       C  
ATOM    514  CZ  TYR A  72      -5.366  23.178  11.456  1.00 81.34           C  
ANISOU  514  CZ  TYR A  72    10271  10937   9696   -725    366    902       C  
ATOM    515  OH  TYR A  72      -4.167  22.627  11.758  1.00 81.63           O  
ANISOU  515  OH  TYR A  72    10496  11014   9507   -811    163    856       O  
ATOM    516  N   SER A  73     -11.674  25.810   8.558  1.00 89.58           N  
ANISOU  516  N   SER A  73     9630  11447  12959   -225    598   1272       N  
ATOM    517  CA  SER A  73     -13.118  26.072   8.573  1.00 93.85           C  
ANISOU  517  CA  SER A  73     9703  11785  14170   -121    764   1454       C  
ATOM    518  C   SER A  73     -13.824  25.554   7.319  1.00 95.37           C  
ANISOU  518  C   SER A  73     9507  11843  14886   -171    190   1516       C  
ATOM    519  O   SER A  73     -14.913  24.946   7.413  1.00 98.94           O  
ANISOU  519  O   SER A  73     9476  12112  16003   -191    212   1715       O  
ATOM    520  CB  SER A  73     -13.421  27.577   8.845  1.00 95.16           C  
ANISOU  520  CB  SER A  73     9952  11894  14312     66   1088   1429       C  
ATOM    521  OG  SER A  73     -12.708  28.503   8.006  1.00 92.32           O  
ANISOU  521  OG  SER A  73     9880  11617  13581     95    760   1251       O  
ATOM    522  N   LEU A  74     -13.183  25.756   6.162  1.00 93.06           N  
ANISOU  522  N   LEU A  74     9455  11611  14293   -202   -325   1354       N  
ATOM    523  CA  LEU A  74     -13.822  25.498   4.870  1.00 94.70           C  
ANISOU  523  CA  LEU A  74     9447  11645  14889   -229   -940   1386       C  
ATOM    524  C   LEU A  74     -13.238  24.354   4.047  1.00 93.41           C  
ANISOU  524  C   LEU A  74     9475  11499  14518   -377  -1430   1291       C  
ATOM    525  O   LEU A  74     -13.904  23.865   3.115  1.00 95.51           O  
ANISOU  525  O   LEU A  74     9570  11563  15157   -427  -1963   1342       O  
ATOM    526  CB  LEU A  74     -13.806  26.771   4.046  1.00 94.59           C  
ANISOU  526  CB  LEU A  74     9605  11590  14745   -112  -1159   1302       C  
ATOM    527  CG  LEU A  74     -15.051  27.618   4.235  1.00 98.68           C  
ANISOU  527  CG  LEU A  74     9698  11908  15890     39  -1019   1467       C  
ATOM    528  CD1 LEU A  74     -15.229  27.960   5.686  1.00 99.82           C  
ANISOU  528  CD1 LEU A  74     9739  12103  16087    128   -257   1543       C  
ATOM    529  CD2 LEU A  74     -14.923  28.867   3.402  1.00 99.24           C  
ANISOU  529  CD2 LEU A  74    10007  11934  15767    150  -1271   1377       C  
ATOM    530  N   GLY A  75     -12.011  23.933   4.376  1.00 90.24           N  
ANISOU  530  N   GLY A  75     9439  11299  13551   -441  -1278   1155       N  
ATOM    531  CA  GLY A  75     -11.333  22.818   3.678  1.00 88.88           C  
ANISOU  531  CA  GLY A  75     9482  11135  13153   -556  -1648   1051       C  
ATOM    532  C   GLY A  75     -12.212  21.594   3.536  1.00 91.47           C  
ANISOU  532  C   GLY A  75     9475  11270  14008   -660  -1933   1185       C  
ATOM    533  O   GLY A  75     -12.271  20.992   2.473  1.00 92.62           O  
ANISOU  533  O   GLY A  75     9734  11273  14185   -718  -2458   1126       O  
ATOM    534  N   ARG A  76     -12.913  21.245   4.613  1.00 93.00           N  
ANISOU  534  N   ARG A  76     9290  11428  14618   -684  -1573   1374       N  
ATOM    535  CA  ARG A  76     -13.887  20.172   4.579  1.00 95.91           C  
ANISOU  535  CA  ARG A  76     9247  11578  15617   -795  -1792   1550       C  
ATOM    536  C   ARG A  76     -14.956  20.397   3.526  1.00 99.39           C  
ANISOU  536  C   ARG A  76     9404  11749  16611   -789  -2346   1624       C  
ATOM    537  O   ARG A  76     -15.612  19.440   3.143  1.00102.39           O  
ANISOU  537  O   ARG A  76     9529  11905  17469   -910  -2749   1726       O  
ATOM    538  CB  ARG A  76     -14.592  20.041   5.931  1.00 97.77           C  
ANISOU  538  CB  ARG A  76     9101  11784  16264   -793  -1195   1778       C  
ATOM    539  CG  ARG A  76     -13.888  19.203   6.988  1.00 98.83           C  
ANISOU  539  CG  ARG A  76     9430  12051  16071   -871   -812   1794       C  
ATOM    540  CD  ARG A  76     -14.871  18.788   8.145  1.00105.40           C  
ANISOU  540  CD  ARG A  76     9855  12744  17447   -901   -287   2077       C  
ATOM    541  NE  ARG A  76     -15.345  19.929   8.945  1.00108.85           N  
ANISOU  541  NE  ARG A  76    10208  13187  17962   -745    314   2164       N  
ATOM    542  CZ  ARG A  76     -14.645  20.532   9.907  1.00107.74           C  
ANISOU  542  CZ  ARG A  76    10486  13211  17241   -661    816   2091       C  
ATOM    543  NH1 ARG A  76     -13.417  20.126  10.243  1.00104.30           N  
ANISOU  543  NH1 ARG A  76    10532  12955  16142   -726    777   1949       N  
ATOM    544  NH2 ARG A  76     -15.183  21.560  10.537  1.00110.92           N  
ANISOU  544  NH2 ARG A  76    10830  13563  17752   -507   1338   2164       N  
ATOM    545  N   ILE A  77     -15.160  21.634   3.068  1.00 99.86           N  
ANISOU  545  N   ILE A  77     9507  11794  16643   -658  -2414   1587       N  
ATOM    546  CA  ILE A  77     -16.248  21.901   2.125  1.00104.13           C  
ANISOU  546  CA  ILE A  77     9757  12036  17771   -645  -2988   1688       C  
ATOM    547  C   ILE A  77     -15.781  21.948   0.683  1.00103.56           C  
ANISOU  547  C   ILE A  77    10194  11879  17273   -662  -3675   1502       C  
ATOM    548  O   ILE A  77     -16.235  21.144  -0.125  1.00106.33           O  
ANISOU  548  O   ILE A  77    10531  11977  17893   -771  -4309   1525       O  
ATOM    549  CB  ILE A  77     -17.041  23.169   2.485  1.00106.39           C  
ANISOU  549  CB  ILE A  77     9693  12259  18472   -480  -2697   1819       C  
ATOM    550  CG1 ILE A  77     -17.888  22.901   3.737  1.00109.59           C  
ANISOU  550  CG1 ILE A  77     9506  12601  19532   -472  -2097   2065       C  
ATOM    551  CG2 ILE A  77     -17.968  23.583   1.329  1.00109.90           C  
ANISOU  551  CG2 ILE A  77     9942  12386  19427   -452  -3419   1894       C  
ATOM    552  CD1 ILE A  77     -18.157  24.136   4.569  1.00111.26           C  
ANISOU  552  CD1 ILE A  77     9588  12868  19816   -274  -1436   2126       C  
ATOM    553  N   SER A  78     -14.910  22.889   0.352  1.00100.72           N  
ANISOU  553  N   SER A  78    10313  11692  16264   -559  -3554   1328       N  
ATOM    554  CA  SER A  78     -14.496  23.072  -1.036  1.00100.97           C  
ANISOU  554  CA  SER A  78    10893  11613  15860   -554  -4122   1169       C  
ATOM    555  C   SER A  78     -13.192  22.406  -1.314  1.00 97.78           C  
ANISOU  555  C   SER A  78    11035  11365  14751   -607  -4046    961       C  
ATOM    556  O   SER A  78     -12.822  22.268  -2.484  1.00 98.48           O  
ANISOU  556  O   SER A  78    11638  11319  14459   -614  -4482    827       O  
ATOM    557  CB  SER A  78     -14.334  24.549  -1.377  1.00100.56           C  
ANISOU  557  CB  SER A  78    11063  11603  15541   -409  -4045   1121       C  
ATOM    558  OG  SER A  78     -13.239  25.116  -0.693  1.00 96.52           O  
ANISOU  558  OG  SER A  78    10786  11406  14483   -355  -3423   1005       O  
ATOM    559  N   GLY A  79     -12.486  22.030  -0.243  1.00 94.80           N  
ANISOU  559  N   GLY A  79    10580  11242  14199   -630  -3483    941       N  
ATOM    560  CA  GLY A  79     -11.070  21.660  -0.323  1.00 91.48           C  
ANISOU  560  CA  GLY A  79    10623  11009  13128   -643  -3276    752       C  
ATOM    561  C   GLY A  79     -10.178  22.797   0.107  1.00 88.67           C  
ANISOU  561  C   GLY A  79    10451  10894  12343   -553  -2802    674       C  
ATOM    562  O   GLY A  79      -9.009  22.591   0.335  1.00 86.35           O  
ANISOU  562  O   GLY A  79    10403  10770  11636   -564  -2537    560       O  
ATOM    563  N   ALA A  80     -10.746  24.000   0.192  1.00 89.62           N  
ANISOU  563  N   ALA A  80    10440  10998  12614   -464  -2730    742       N  
ATOM    564  CA  ALA A  80     -10.027  25.207   0.551  1.00 87.39           C  
ANISOU  564  CA  ALA A  80    10339  10893  11971   -383  -2338    676       C  
ATOM    565  C   ALA A  80      -8.810  25.451  -0.365  1.00 85.78           C  
ANISOU  565  C   ALA A  80    10680  10740  11174   -377  -2390    501       C  
ATOM    566  O   ALA A  80      -7.682  25.557   0.087  1.00 83.70           O  
ANISOU  566  O   ALA A  80    10569  10658  10573   -392  -2043    417       O  
ATOM    567  CB  ALA A  80      -9.635  25.156   2.035  1.00 85.36           C  
ANISOU  567  CB  ALA A  80     9901  10839  11694   -398  -1793    712       C  
ATOM    568  N   HIS A  81      -9.036  25.521  -1.664  1.00 87.70           N  
ANISOU  568  N   HIS A  81    11231  10785  11306   -358  -2827    458       N  
ATOM    569  CA  HIS A  81      -7.934  25.772  -2.599  1.00 86.99           C  
ANISOU  569  CA  HIS A  81    11705  10696  10649   -339  -2802    311       C  
ATOM    570  C   HIS A  81      -7.513  27.231  -2.519  1.00 85.80           C  
ANISOU  570  C   HIS A  81    11682  10637  10282   -271  -2524    302       C  
ATOM    571  O   HIS A  81      -6.328  27.562  -2.456  1.00 84.01           O  
ANISOU  571  O   HIS A  81    11678  10544   9698   -278  -2182    217       O  
ATOM    572  CB  HIS A  81      -8.347  25.424  -4.035  1.00 90.18           C  
ANISOU  572  CB  HIS A  81    12528  10810  10929   -333  -3360    271       C  
ATOM    573  CG  HIS A  81      -8.611  23.971  -4.253  1.00 91.30           C  
ANISOU  573  CG  HIS A  81    12659  10819  11212   -409  -3670    249       C  
ATOM    574  ND1 HIS A  81      -8.284  23.337  -5.428  1.00 93.36           N  
ANISOU  574  ND1 HIS A  81    13493  10867  11114   -411  -3976    130       N  
ATOM    575  CD2 HIS A  81      -9.186  23.036  -3.460  1.00 91.22           C  
ANISOU  575  CD2 HIS A  81    12176  10827  11656   -484  -3714    335       C  
ATOM    576  CE1 HIS A  81      -8.648  22.065  -5.348  1.00 95.18           C  
ANISOU  576  CE1 HIS A  81    13594  10988  11582   -488  -4236    131       C  
ATOM    577  NE2 HIS A  81      -9.200  21.859  -4.166  1.00 93.65           N  
ANISOU  577  NE2 HIS A  81    12746  10935  11900   -541  -4086    265       N  
ATOM    578  N   ILE A  82      -8.508  28.105  -2.535  1.00 87.43           N  
ANISOU  578  N   ILE A  82    11721  10738  10760   -206  -2689    402       N  
ATOM    579  CA  ILE A  82      -8.293  29.564  -2.513  1.00 86.95           C  
ANISOU  579  CA  ILE A  82    11787  10710  10539   -131  -2488    406       C  
ATOM    580  C   ILE A  82      -7.072  30.049  -3.333  1.00 85.92           C  
ANISOU  580  C   ILE A  82    12208  10594   9844   -139  -2351    295       C  
ATOM    581  O   ILE A  82      -6.484  31.078  -3.034  1.00 84.97           O  
ANISOU  581  O   ILE A  82    12163  10564   9557   -121  -2041    281       O  
ATOM    582  CB  ILE A  82      -8.253  30.122  -1.047  1.00 85.09           C  
ANISOU  582  CB  ILE A  82    11185  10664  10479   -112  -2014    448       C  
ATOM    583  CG1 ILE A  82      -7.100  29.486  -0.232  1.00 82.04           C  
ANISOU  583  CG1 ILE A  82    10803  10498   9872   -200  -1647    370       C  
ATOM    584  CG2 ILE A  82      -9.631  29.908  -0.381  1.00 86.50           C  
ANISOU  584  CG2 ILE A  82    10852  10758  11254    -66  -2085    592       C  
ATOM    585  CD1 ILE A  82      -6.839  30.189   1.163  1.00 80.11           C  
ANISOU  585  CD1 ILE A  82    10393  10402   9644   -189  -1211    387       C  
ATOM    586  N   ASN A  83      -6.757  29.333  -4.400  1.00 86.94           N  
ANISOU  586  N   ASN A  83    12742  10592   9702   -161  -2582    226       N  
ATOM    587  CA  ASN A  83      -5.604  29.610  -5.204  1.00 86.76           C  
ANISOU  587  CA  ASN A  83    13244  10547   9173   -161  -2372    135       C  
ATOM    588  C   ASN A  83      -5.704  28.805  -6.495  1.00 89.44           C  
ANISOU  588  C   ASN A  83    14100  10638   9246   -153  -2736     75       C  
ATOM    589  O   ASN A  83      -5.805  27.593  -6.451  1.00 90.20           O  
ANISOU  589  O   ASN A  83    14122  10711   9439   -190  -2876     33       O  
ATOM    590  CB  ASN A  83      -4.356  29.206  -4.433  1.00 84.19           C  
ANISOU  590  CB  ASN A  83    12767  10451   8770   -220  -1876     70       C  
ATOM    591  CG  ASN A  83      -3.086  29.383  -5.251  1.00 85.41           C  
ANISOU  591  CG  ASN A  83    13388  10561   8503   -218  -1577     -6       C  
ATOM    592  OD1 ASN A  83      -3.038  29.055  -6.428  1.00 89.14           O  
ANISOU  592  OD1 ASN A  83    14362  10828   8678   -182  -1727    -52       O  
ATOM    593  ND2 ASN A  83      -2.056  29.902  -4.630  1.00 84.27           N  
ANISOU  593  ND2 ASN A  83    13101  10574   8345   -259  -1148    -10       N  
ATOM    594  N   PRO A  84      -5.658  29.450  -7.651  1.00 91.54           N  
ANISOU  594  N   PRO A  84    14954  10687   9140   -104  -2894     67       N  
ATOM    595  CA  PRO A  84      -5.767  28.762  -8.926  1.00 94.94           C  
ANISOU  595  CA  PRO A  84    16026  10824   9225    -86  -3261      3       C  
ATOM    596  C   PRO A  84      -4.587  27.880  -9.265  1.00 94.80           C  
ANISOU  596  C   PRO A  84    16348  10820   8852    -90  -2871   -126       C  
ATOM    597  O   PRO A  84      -4.795  26.808  -9.853  1.00 97.28           O  
ANISOU  597  O   PRO A  84    16972  10943   9049    -90  -3169   -200       O  
ATOM    598  CB  PRO A  84      -5.851  29.895  -9.936  1.00 97.57           C  
ANISOU  598  CB  PRO A  84    16949  10935   9190    -27  -3405     45       C  
ATOM    599  CG  PRO A  84      -6.339  31.016  -9.172  1.00 96.48           C  
ANISOU  599  CG  PRO A  84    16327  10928   9403    -12  -3366    155       C  
ATOM    600  CD  PRO A  84      -5.694  30.892  -7.833  1.00 92.29           C  
ANISOU  600  CD  PRO A  84    15187  10748   9131    -59  -2822    135       C  
ATOM    601  N   ALA A  85      -3.367  28.297  -8.907  1.00 92.57           N  
ANISOU  601  N   ALA A  85    16002  10728   8442    -93  -2230   -149       N  
ATOM    602  CA  ALA A  85      -2.183  27.436  -9.125  1.00 92.52           C  
ANISOU  602  CA  ALA A  85    16198  10731   8223    -81  -1792   -254       C  
ATOM    603  C   ALA A  85      -2.345  26.058  -8.417  1.00 91.04           C  
ANISOU  603  C   ALA A  85    15594  10643   8356   -118  -1911   -302       C  
ATOM    604  O   ALA A  85      -1.953  25.021  -8.961  1.00 92.62           O  
ANISOU  604  O   ALA A  85    16122  10700   8369    -84  -1876   -402       O  
ATOM    605  CB  ALA A  85      -0.885  28.138  -8.699  1.00 90.48           C  
ANISOU  605  CB  ALA A  85    15773  10654   7952    -96  -1124   -235       C  
ATOM    606  N   VAL A  86      -2.947  26.036  -7.225  1.00 88.53           N  
ANISOU  606  N   VAL A  86    14602  10535   8501   -181  -2036   -227       N  
ATOM    607  CA  VAL A  86      -3.198  24.758  -6.531  1.00 87.55           C  
ANISOU  607  CA  VAL A  86    14098  10480   8688   -228  -2165   -244       C  
ATOM    608  C   VAL A  86      -4.153  23.928  -7.351  1.00 90.47           C  
ANISOU  608  C   VAL A  86    14775  10568   9030   -226  -2744   -275       C  
ATOM    609  O   VAL A  86      -3.837  22.801  -7.694  1.00 91.55           O  
ANISOU  609  O   VAL A  86    15134  10589   9062   -220  -2777   -369       O  
ATOM    610  CB  VAL A  86      -3.788  24.925  -5.108  1.00 84.95           C  
ANISOU  610  CB  VAL A  86    13060  10382   8834   -291  -2169   -135       C  
ATOM    611  CG1 VAL A  86      -4.074  23.566  -4.463  1.00 83.96           C  
ANISOU  611  CG1 VAL A  86    12607  10288   9005   -347  -2298   -131       C  
ATOM    612  CG2 VAL A  86      -2.838  25.705  -4.245  1.00 82.69           C  
ANISOU  612  CG2 VAL A  86    12531  10334   8555   -306  -1677   -115       C  
ATOM    613  N   THR A  87      -5.304  24.511  -7.680  1.00 92.09           N  
ANISOU  613  N   THR A  87    15004  10632   9355   -231  -3225   -193       N  
ATOM    614  CA  THR A  87      -6.317  23.836  -8.473  1.00 95.69           C  
ANISOU  614  CA  THR A  87    15735  10767   9854   -250  -3906   -198       C  
ATOM    615  C   THR A  87      -5.761  23.259  -9.755  1.00 98.83           C  
ANISOU  615  C   THR A  87    16990  10879   9683   -198  -3985   -346       C  
ATOM    616  O   THR A  87      -6.033  22.112 -10.072  1.00100.62           O  
ANISOU  616  O   THR A  87    17395  10911   9926   -227  -4318   -414       O  
ATOM    617  CB  THR A  87      -7.459  24.768  -8.838  1.00 97.93           C  
ANISOU  617  CB  THR A  87    16014  10886  10309   -240  -4410    -81       C  
ATOM    618  OG1 THR A  87      -8.082  25.204  -7.624  1.00 95.92           O  
ANISOU  618  OG1 THR A  87    14962  10854  10631   -268  -4307     57       O  
ATOM    619  CG2 THR A  87      -8.485  24.047  -9.768  1.00102.12           C  
ANISOU  619  CG2 THR A  87    16886  11012  10901   -276  -5237    -81       C  
ATOM    620  N   ILE A  88      -4.974  24.052 -10.473  1.00 99.81           N  
ANISOU  620  N   ILE A  88    17668  10953   9303   -120  -3645   -391       N  
ATOM    621  CA  ILE A  88      -4.329  23.593 -11.715  1.00103.55           C  
ANISOU  621  CA  ILE A  88    19057  11129   9158    -42  -3565   -530       C  
ATOM    622  C   ILE A  88      -3.281  22.490 -11.471  1.00102.85           C  
ANISOU  622  C   ILE A  88    18941  11118   9021    -10  -3066   -651       C  
ATOM    623  O   ILE A  88      -3.196  21.511 -12.235  1.00106.19           O  
ANISOU  623  O   ILE A  88    19942  11254   9150     33  -3222   -778       O  
ATOM    624  CB  ILE A  88      -3.658  24.754 -12.465  1.00104.89           C  
ANISOU  624  CB  ILE A  88    19797  11229   8827     34  -3185   -520       C  
ATOM    625  CG1 ILE A  88      -4.717  25.725 -13.011  1.00107.21           C  
ANISOU  625  CG1 ILE A  88    20345  11327   9063     27  -3786   -416       C  
ATOM    626  CG2 ILE A  88      -2.774  24.224 -13.585  1.00107.96           C  
ANISOU  626  CG2 ILE A  88    21098  11337   8586    134  -2859   -661       C  
ATOM    627  CD1 ILE A  88      -4.208  27.158 -13.154  1.00105.89           C  
ANISOU  627  CD1 ILE A  88    20319  11240   8675     64  -3374   -336       C  
ATOM    628  N   ALA A  89      -2.500  22.636 -10.402  1.00 98.98           N  
ANISOU  628  N   ALA A  89    17801  10978   8830    -28  -2508   -612       N  
ATOM    629  CA  ALA A  89      -1.530  21.612 -10.013  1.00 97.89           C  
ANISOU  629  CA  ALA A  89    17500  10923   8773      2  -2076   -696       C  
ATOM    630  C   ALA A  89      -2.216  20.289  -9.641  1.00 98.01           C  
ANISOU  630  C   ALA A  89    17282  10874   9083    -57  -2524   -727       C  
ATOM    631  O   ALA A  89      -1.769  19.225 -10.067  1.00 99.99           O  
ANISOU  631  O   ALA A  89    17872  10944   9175      1  -2449   -850       O  
ATOM    632  CB  ALA A  89      -0.671  22.111  -8.864  1.00 93.86           C  
ANISOU  632  CB  ALA A  89    16310  10771   8582    -29  -1535   -619       C  
ATOM    633  N   LEU A  90      -3.305  20.354  -8.871  1.00 96.38           N  
ANISOU  633  N   LEU A  90    16514  10784   9323   -165  -2960   -611       N  
ATOM    634  CA  LEU A  90      -4.033  19.138  -8.451  1.00 96.68           C  
ANISOU  634  CA  LEU A  90    16263  10750   9720   -247  -3380   -603       C  
ATOM    635  C   LEU A  90      -4.713  18.461  -9.619  1.00101.25           C  
ANISOU  635  C   LEU A  90    17501  10907  10063   -245  -3990   -694       C  
ATOM    636  O   LEU A  90      -4.797  17.236  -9.671  1.00102.55           O  
ANISOU  636  O   LEU A  90    17745  10912  10307   -271  -4194   -765       O  
ATOM    637  CB  LEU A  90      -5.076  19.440  -7.375  1.00 94.76           C  
ANISOU  637  CB  LEU A  90    15265  10694  10047   -358  -3629   -430       C  
ATOM    638  CG  LEU A  90      -4.535  19.696  -5.953  1.00 90.66           C  
ANISOU  638  CG  LEU A  90    14075  10554   9819   -386  -3118   -344       C  
ATOM    639  CD1 LEU A  90      -5.627  20.254  -5.042  1.00 88.89           C  
ANISOU  639  CD1 LEU A  90    13255  10460  10061   -460  -3289   -173       C  
ATOM    640  CD2 LEU A  90      -3.946  18.424  -5.347  1.00 89.16           C  
ANISOU  640  CD2 LEU A  90    13688  10420   9771   -409  -2939   -384       C  
ATOM    641  N   TRP A  91      -5.191  19.264 -10.562  1.00103.98           N  
ANISOU  641  N   TRP A  91    18364  11039  10105   -218  -4318   -689       N  
ATOM    642  CA  TRP A  91      -5.788  18.742 -11.783  1.00108.95           C  
ANISOU  642  CA  TRP A  91    19778  11205  10413   -214  -4962   -781       C  
ATOM    643  C   TRP A  91      -4.755  18.020 -12.607  1.00111.17           C  
ANISOU  643  C   TRP A  91    20856  11271  10113    -94  -4606   -979       C  
ATOM    644  O   TRP A  91      -5.051  16.957 -13.140  1.00114.27           O  
ANISOU  644  O   TRP A  91    21689  11337  10392   -106  -5023  -1088       O  
ATOM    645  CB  TRP A  91      -6.372  19.863 -12.618  1.00111.70           C  
ANISOU  645  CB  TRP A  91    20586  11359  10496   -194  -5347   -723       C  
ATOM    646  CG  TRP A  91      -6.739  19.441 -13.979  1.00117.95           C  
ANISOU  646  CG  TRP A  91    22390  11637  10789   -170  -5950   -835       C  
ATOM    647  CD1 TRP A  91      -7.878  18.823 -14.355  1.00121.82           C  
ANISOU  647  CD1 TRP A  91    23005  11780  11503   -271  -6868   -817       C  
ATOM    648  CD2 TRP A  91      -5.956  19.616 -15.170  1.00121.90           C  
ANISOU  648  CD2 TRP A  91    23990  11864  10462    -37  -5685   -978       C  
ATOM    649  NE1 TRP A  91      -7.869  18.609 -15.708  1.00127.74           N  
ANISOU  649  NE1 TRP A  91    24916  12045  11574   -214  -7267   -953       N  
ATOM    650  CE2 TRP A  91      -6.698  19.082 -16.233  1.00127.74           C  
ANISOU  650  CE2 TRP A  91    25566  12083  10888    -61  -6514  -1056       C  
ATOM    651  CE3 TRP A  91      -4.699  20.179 -15.437  1.00121.20           C  
ANISOU  651  CE3 TRP A  91    24266  11893   9890     96  -4813  -1034       C  
ATOM    652  CZ2 TRP A  91      -6.227  19.075 -17.545  1.00132.98           C  
ANISOU  652  CZ2 TRP A  91    27507  12334  10686     57  -6476  -1202       C  
ATOM    653  CZ3 TRP A  91      -4.234  20.182 -16.744  1.00126.14           C  
ANISOU  653  CZ3 TRP A  91    26090  12121   9716    215  -4709  -1161       C  
ATOM    654  CH2 TRP A  91      -4.995  19.627 -17.778  1.00132.09           C  
ANISOU  654  CH2 TRP A  91    27747  12355  10086    203  -5522  -1251       C  
ATOM    655  N   SER A  92      -3.550  18.588 -12.695  1.00109.86           N  
ANISOU  655  N   SER A  92    20859  11261   9622     23  -3824  -1019       N  
ATOM    656  CA  SER A  92      -2.448  17.980 -13.455  1.00112.70           C  
ANISOU  656  CA  SER A  92    21934  11411   9474    171  -3311  -1192       C  
ATOM    657  C   SER A  92      -1.954  16.632 -12.905  1.00111.99           C  
ANISOU  657  C   SER A  92    21544  11358   9648    190  -3105  -1278       C  
ATOM    658  O   SER A  92      -1.144  15.965 -13.553  1.00114.74           O  
ANISOU  658  O   SER A  92    22490  11474   9631    329  -2726  -1432       O  
ATOM    659  CB  SER A  92      -1.258  18.917 -13.510  1.00111.54           C  
ANISOU  659  CB  SER A  92    21834  11442   9105    275  -2461  -1168       C  
ATOM    660  OG  SER A  92      -0.455  18.775 -12.356  1.00107.32           O  
ANISOU  660  OG  SER A  92    20457  11280   9041    263  -1919  -1115       O  
ATOM    661  N   ILE A  93      -2.414  16.252 -11.712  1.00108.69           N  
ANISOU  661  N   ILE A  93    20229  11210   9857     62  -3305  -1172       N  
ATOM    662  CA  ILE A  93      -2.157  14.918 -11.155  1.00108.31           C  
ANISOU  662  CA  ILE A  93    19892  11161  10099     54  -3260  -1229       C  
ATOM    663  C   ILE A  93      -3.390  14.009 -11.224  1.00110.57           C  
ANISOU  663  C   ILE A  93    20195  11200  10616    -78  -4093  -1228       C  
ATOM    664  O   ILE A  93      -3.309  12.839 -10.859  1.00110.65           O  
ANISOU  664  O   ILE A  93    20046  11146  10852   -100  -4151  -1274       O  
ATOM    665  CB  ILE A  93      -1.710  15.024  -9.681  1.00103.25           C  
ANISOU  665  CB  ILE A  93    18262  10970   9999     -4  -2862  -1094       C  
ATOM    666  CG1 ILE A  93      -0.426  15.848  -9.571  1.00101.91           C  
ANISOU  666  CG1 ILE A  93    18020  11008   9693    105  -2089  -1087       C  
ATOM    667  CG2 ILE A  93      -1.470  13.661  -9.075  1.00102.61           C  
ANISOU  667  CG2 ILE A  93    17892  10872  10222    -17  -2852  -1129       C  
ATOM    668  CD1 ILE A  93       0.071  15.947  -8.125  1.00 97.75           C  
ANISOU  668  CD1 ILE A  93    16603  10872   9667     42  -1774   -960       C  
ATOM    669  N   GLY A  94      -4.524  14.537 -11.685  1.00112.84           N  
ANISOU  669  N   GLY A  94    20651  11323  10900   -171  -4757  -1162       N  
ATOM    670  CA  GLY A  94      -5.785  13.779 -11.709  1.00115.42           C  
ANISOU  670  CA  GLY A  94    20875  11393  11584   -326  -5613  -1118       C  
ATOM    671  C   GLY A  94      -6.425  13.642 -10.331  1.00111.86           C  
ANISOU  671  C   GLY A  94    19336  11253  11911   -479  -5686   -916       C  
ATOM    672  O   GLY A  94      -7.171  12.697 -10.051  1.00113.42           O  
ANISOU  672  O   GLY A  94    19274  11294  12528   -609  -6166   -869       O  
ATOM    673  N   ARG A  95      -6.113  14.587  -9.464  1.00107.57           N  
ANISOU  673  N   ARG A  95    18198  11125  11550   -465  -5184   -793       N  
ATOM    674  CA  ARG A  95      -6.713  14.644  -8.157  1.00104.70           C  
ANISOU  674  CA  ARG A  95    16900  11044  11839   -587  -5168   -595       C  
ATOM    675  C   ARG A  95      -7.892  15.644  -8.158  1.00105.63           C  
ANISOU  675  C   ARG A  95    16728  11146  12260   -657  -5589   -433       C  
ATOM    676  O   ARG A  95      -8.638  15.758  -7.172  1.00104.61           O  
ANISOU  676  O   ARG A  95    15850  11176  12720   -755  -5626   -248       O  
ATOM    677  CB  ARG A  95      -5.638  15.041  -7.130  1.00100.23           C  
ANISOU  677  CB  ARG A  95    15897  10900  11284   -525  -4383   -564       C  
ATOM    678  CG  ARG A  95      -4.575  13.979  -6.938  1.00 99.74           C  
ANISOU  678  CG  ARG A  95    15937  10845  11112   -464  -4016   -678       C  
ATOM    679  CD  ARG A  95      -5.180  12.700  -6.313  1.00100.75           C  
ANISOU  679  CD  ARG A  95    15706  10882  11692   -588  -4337   -613       C  
ATOM    680  NE  ARG A  95      -4.246  12.121  -5.335  1.00 99.32           N  
ANISOU  680  NE  ARG A  95    15171  10920  11644   -561  -3849   -598       N  
ATOM    681  CZ  ARG A  95      -4.582  11.642  -4.132  1.00 98.62           C  
ANISOU  681  CZ  ARG A  95    14476  10985  12008   -674  -3833   -441       C  
ATOM    682  NH1 ARG A  95      -5.862  11.642  -3.733  1.00 99.63           N  
ANISOU  682  NH1 ARG A  95    14224  11075  12556   -822  -4213   -278       N  
ATOM    683  NH2 ARG A  95      -3.628  11.162  -3.317  1.00 96.96           N  
ANISOU  683  NH2 ARG A  95    14043  10941  11857   -636  -3427   -432       N  
ATOM    684  N   PHE A  96      -8.058  16.386  -9.249  1.00108.05           N  
ANISOU  684  N   PHE A  96    17639  11239  12176   -596  -5873   -489       N  
ATOM    685  CA  PHE A  96      -9.164  17.321  -9.347  1.00109.17           C  
ANISOU  685  CA  PHE A  96    17541  11313  12626   -644  -6329   -335       C  
ATOM    686  C   PHE A  96      -9.786  17.277 -10.730  1.00114.57           C  
ANISOU  686  C   PHE A  96    18991  11512  13030   -651  -7117   -400       C  
ATOM    687  O   PHE A  96      -9.062  17.307 -11.740  1.00116.16           O  
ANISOU  687  O   PHE A  96    20091  11530  12516   -548  -7036   -573       O  
ATOM    688  CB  PHE A  96      -8.716  18.736  -9.036  1.00106.14           C  
ANISOU  688  CB  PHE A  96    17011  11233  12084   -552  -5811   -282       C  
ATOM    689  CG  PHE A  96      -9.859  19.672  -8.738  1.00107.30           C  
ANISOU  689  CG  PHE A  96    16661  11383  12723   -589  -6138    -90       C  
ATOM    690  CD1 PHE A  96     -10.653  19.483  -7.618  1.00106.57           C  
ANISOU  690  CD1 PHE A  96    15703  11428  13360   -677  -6135     87       C  
ATOM    691  CD2 PHE A  96     -10.148  20.755  -9.574  1.00110.05           C  
ANISOU  691  CD2 PHE A  96    17419  11571  12823   -525  -6417    -72       C  
ATOM    692  CE1 PHE A  96     -11.724  20.361  -7.339  1.00107.76           C  
ANISOU  692  CE1 PHE A  96    15362  11550  14031   -683  -6371    274       C  
ATOM    693  CE2 PHE A  96     -11.203  21.634  -9.292  1.00110.78           C  
ANISOU  693  CE2 PHE A  96    17017  11643  13431   -536  -6713    114       C  
ATOM    694  CZ  PHE A  96     -11.987  21.433  -8.177  1.00109.61           C  
ANISOU  694  CZ  PHE A  96    15969  11627  14051   -607  -6671    283       C  
ATOM    695  N   PRO A  97     -11.138  17.200 -10.776  1.00117.76           N  
ANISOU  695  N   PRO A  97    19055  11669  14017   -773  -7888   -248       N  
ATOM    696  CA  PRO A  97     -11.862  17.106 -12.041  1.00123.53           C  
ANISOU  696  CA  PRO A  97    20484  11877  14573   -810  -8811   -285       C  
ATOM    697  C   PRO A  97     -11.656  18.323 -12.929  1.00124.75           C  
ANISOU  697  C   PRO A  97    21304  11940  14154   -689  -8854   -318       C  
ATOM    698  O   PRO A  97     -11.805  19.463 -12.485  1.00122.48           O  
ANISOU  698  O   PRO A  97    20571  11897  14068   -643  -8594   -186       O  
ATOM    699  CB  PRO A  97     -13.332  17.002 -11.604  1.00125.99           C  
ANISOU  699  CB  PRO A  97    19994  12031  15848   -966  -9499    -48       C  
ATOM    700  CG  PRO A  97     -13.371  17.494 -10.208  1.00121.36           C  
ANISOU  700  CG  PRO A  97    18385  11915  15812   -959  -8813    120       C  
ATOM    701  CD  PRO A  97     -12.063  17.099  -9.626  1.00116.65           C  
ANISOU  701  CD  PRO A  97    17860  11683  14780   -890  -7941    -22       C  
ATOM    702  N   GLY A  98     -11.319  18.070 -14.182  1.00128.62           N  
ANISOU  702  N   GLY A  98    22909  12049  13910   -635  -9170   -492       N  
ATOM    703  CA  GLY A  98     -11.091  19.136 -15.141  1.00130.61           C  
ANISOU  703  CA  GLY A  98    23960  12146  13522   -524  -9223   -524       C  
ATOM    704  C   GLY A  98     -12.298  20.038 -15.280  1.00132.96           C  
ANISOU  704  C   GLY A  98    23952  12273  14292   -577  -9961   -318       C  
ATOM    705  O   GLY A  98     -12.152  21.261 -15.470  1.00132.33           O  
ANISOU  705  O   GLY A  98    24010  12289  13982   -485  -9757   -255       O  
ATOM    706  N   ARG A  99     -13.491  19.428 -15.185  1.00135.70           N  
ANISOU  706  N   ARG A  99    23858  12343  15357   -726 -10824   -200       N  
ATOM    707  CA  ARG A  99     -14.768  20.150 -15.330  1.00138.97           C  
ANISOU  707  CA  ARG A  99    23886  12516  16400   -782 -11644     22       C  
ATOM    708  C   ARG A  99     -14.893  21.307 -14.320  1.00134.79           C  
ANISOU  708  C   ARG A  99    22404  12432  16378   -713 -11043    204       C  
ATOM    709  O   ARG A  99     -15.625  22.285 -14.555  1.00137.17           O  
ANISOU  709  O   ARG A  99    22565  12585  16969   -681 -11480    362       O  
ATOM    710  CB  ARG A  99     -15.955  19.178 -15.206  1.00141.53           C  
ANISOU  710  CB  ARG A  99    23693  12497  17583   -972 -12549    142       C  
ATOM    711  N   GLU A 100     -14.144  21.191 -13.220  1.00129.33           N  
ANISOU  711  N   GLU A 100    21128  12253  15757   -682 -10060    175       N  
ATOM    712  CA  GLU A 100     -14.264  22.092 -12.081  1.00125.46           C  
ANISOU  712  CA  GLU A 100    19711  12179  15780   -632  -9454    332       C  
ATOM    713  C   GLU A 100     -13.106  23.067 -11.918  1.00121.13           C  
ANISOU  713  C   GLU A 100    19431  11994  14599   -494  -8581    243       C  
ATOM    714  O   GLU A 100     -13.166  23.938 -11.039  1.00118.29           O  
ANISOU  714  O   GLU A 100    18426  11941  14576   -442  -8105    356       O  
ATOM    715  CB  GLU A 100     -14.423  21.272 -10.794  1.00122.54           C  
ANISOU  715  CB  GLU A 100    18404  12083  16071   -721  -9052    407       C  
ATOM    716  CG  GLU A 100     -15.802  20.648 -10.652  1.00127.54           C  
ANISOU  716  CG  GLU A 100    18416  12401  17642   -862  -9813    596       C  
ATOM    717  CD  GLU A 100     -15.928  19.707  -9.464  1.00125.99           C  
ANISOU  717  CD  GLU A 100    17415  12423  18035   -965  -9406    675       C  
ATOM    718  OE1 GLU A 100     -15.038  19.713  -8.571  1.00120.51           O  
ANISOU  718  OE1 GLU A 100    16528  12164  17097   -911  -8514    613       O  
ATOM    719  OE2 GLU A 100     -16.928  18.943  -9.443  1.00130.52           O  
ANISOU  719  OE2 GLU A 100    17569  12693  19331  -1110 -10022    812       O  
ATOM    720  N   VAL A 101     -12.066  22.960 -12.747  1.00121.15           N  
ANISOU  720  N   VAL A 101    20377  11935  13718   -432  -8348     50       N  
ATOM    721  CA  VAL A 101     -10.897  23.862 -12.610  1.00117.15           C  
ANISOU  721  CA  VAL A 101    20094  11748  12671   -319  -7491    -17       C  
ATOM    722  C   VAL A 101     -11.259  25.323 -12.952  1.00118.25           C  
ANISOU  722  C   VAL A 101    20348  11821  12761   -244  -7639    100       C  
ATOM    723  O   VAL A 101     -10.947  26.243 -12.203  1.00114.37           O  
ANISOU  723  O   VAL A 101    19396  11655  12403   -193  -7065    164       O  
ATOM    724  CB  VAL A 101      -9.710  23.398 -13.472  1.00117.85           C  
ANISOU  724  CB  VAL A 101    21157  11734  11886   -259  -7148   -227       C  
ATOM    725  CG1 VAL A 101      -8.454  24.164 -13.092  1.00113.38           C  
ANISOU  725  CG1 VAL A 101    20578  11531  10969   -172  -6179   -268       C  
ATOM    726  CG2 VAL A 101      -9.493  21.889 -13.322  1.00117.59           C  
ANISOU  726  CG2 VAL A 101    21119  11653  11905   -319  -7164   -348       C  
ATOM    727  N   VAL A 102     -11.942  25.521 -14.079  1.00123.75           N  
ANISOU  727  N   VAL A 102    21687  12059  13271   -241  -8463    131       N  
ATOM    728  CA  VAL A 102     -12.382  26.863 -14.499  1.00125.61           C  
ANISOU  728  CA  VAL A 102    22087  12159  13481   -168  -8732    259       C  
ATOM    729  C   VAL A 102     -13.417  27.460 -13.535  1.00124.71           C  
ANISOU  729  C   VAL A 102    20884  12175  14325   -170  -8872    468       C  
ATOM    730  O   VAL A 102     -13.318  28.625 -13.208  1.00122.88           O  
ANISOU  730  O   VAL A 102    20441  12112  14137    -85  -8520    545       O  
ATOM    731  CB  VAL A 102     -12.908  26.891 -15.980  1.00132.56           C  
ANISOU  731  CB  VAL A 102    24002  12449  13914   -167  -9693    255       C  
ATOM    732  CG1 VAL A 102     -14.039  27.889 -16.154  1.00135.55           C  
ANISOU  732  CG1 VAL A 102    24117  12591  14795   -140 -10399    466       C  
ATOM    733  CG2 VAL A 102     -11.775  27.226 -16.942  1.00132.96           C  
ANISOU  733  CG2 VAL A 102    25227  12407  12886    -83  -9267    111       C  
ATOM    734  N   PRO A 103     -14.410  26.669 -13.084  1.00126.50           N  
ANISOU  734  N   PRO A 103    20427  12297  15339   -262  -9355    566       N  
ATOM    735  CA  PRO A 103     -15.352  27.153 -12.074  1.00125.91           C  
ANISOU  735  CA  PRO A 103    19266  12346  16226   -247  -9326    772       C  
ATOM    736  C   PRO A 103     -14.702  27.508 -10.753  1.00119.84           C  
ANISOU  736  C   PRO A 103    17867  12104  15561   -200  -8281    760       C  
ATOM    737  O   PRO A 103     -15.122  28.463 -10.089  1.00118.88           O  
ANISOU  737  O   PRO A 103    17180  12105  15884   -117  -8036    890       O  
ATOM    738  CB  PRO A 103     -16.272  25.956 -11.851  1.00128.74           C  
ANISOU  738  CB  PRO A 103    19099  12503  17314   -382  -9886    853       C  
ATOM    739  CG  PRO A 103     -16.258  25.236 -13.120  1.00133.41           C  
ANISOU  739  CG  PRO A 103    20618  12667  17402   -454 -10663    740       C  
ATOM    740  CD  PRO A 103     -14.872  25.398 -13.674  1.00130.72           C  
ANISOU  740  CD  PRO A 103    21250  12474  15944   -380 -10094    517       C  
ATOM    741  N   TYR A 104     -13.699  26.733 -10.359  1.00116.06           N  
ANISOU  741  N   TYR A 104    17503  11902  14694   -246  -7696    605       N  
ATOM    742  CA  TYR A 104     -12.957  27.041  -9.129  1.00110.63           C  
ANISOU  742  CA  TYR A 104    16329  11683  14021   -213  -6758    582       C  
ATOM    743  C   TYR A 104     -12.190  28.350  -9.254  1.00108.27           C  
ANISOU  743  C   TYR A 104    16377  11536  13226   -110  -6297    543       C  
ATOM    744  O   TYR A 104     -12.290  29.195  -8.374  1.00105.99           O  
ANISOU  744  O   TYR A 104    15586  11456  13230    -51  -5884    622       O  
ATOM    745  CB  TYR A 104     -12.011  25.884  -8.732  1.00107.63           C  
ANISOU  745  CB  TYR A 104    16016  11521  13356   -286  -6310    436       C  
ATOM    746  CG  TYR A 104     -12.527  25.015  -7.585  1.00106.74           C  
ANISOU  746  CG  TYR A 104    15096  11548  13914   -367  -6175    526       C  
ATOM    747  CD1 TYR A 104     -11.676  24.591  -6.558  1.00102.50           C  
ANISOU  747  CD1 TYR A 104    14296  11364  13283   -389  -5471    465       C  
ATOM    748  CD2 TYR A 104     -13.869  24.618  -7.524  1.00110.80           C  
ANISOU  748  CD2 TYR A 104    15108  11807  15185   -428  -6763    692       C  
ATOM    749  CE1 TYR A 104     -12.139  23.782  -5.506  1.00101.59           C  
ANISOU  749  CE1 TYR A 104    13520  11350  13728   -466  -5328    562       C  
ATOM    750  CE2 TYR A 104     -14.346  23.809  -6.467  1.00110.15           C  
ANISOU  750  CE2 TYR A 104    14294  11827  15731   -510  -6573    799       C  
ATOM    751  CZ  TYR A 104     -13.465  23.400  -5.461  1.00105.26           C  
ANISOU  751  CZ  TYR A 104    13510  11569  14917   -526  -5836    730       C  
ATOM    752  OH  TYR A 104     -13.903  22.611  -4.427  1.00104.58           O  
ANISOU  752  OH  TYR A 104    12792  11563  15380   -606  -5625    846       O  
ATOM    753  N   ILE A 105     -11.444  28.502 -10.350  1.00109.23           N  
ANISOU  753  N   ILE A 105    17386  11516  12601    -89  -6358    427       N  
ATOM    754  CA  ILE A 105     -10.581  29.668 -10.565  1.00107.55           C  
ANISOU  754  CA  ILE A 105    17573  11418  11873    -13  -5881    393       C  
ATOM    755  C   ILE A 105     -11.401  30.953 -10.638  1.00109.33           C  
ANISOU  755  C   ILE A 105    17640  11508  12391     69  -6169    544       C  
ATOM    756  O   ILE A 105     -11.008  31.974 -10.092  1.00106.70           O  
ANISOU  756  O   ILE A 105    17124  11380  12036    124  -5669    570       O  
ATOM    757  CB  ILE A 105      -9.714  29.503 -11.823  1.00109.50           C  
ANISOU  757  CB  ILE A 105    18854  11467  11284     -3  -5884    263       C  
ATOM    758  CG1 ILE A 105      -8.697  28.382 -11.608  1.00107.01           C  
ANISOU  758  CG1 ILE A 105    18628  11327  10703    -48  -5398    109       C  
ATOM    759  CG2 ILE A 105      -8.986  30.781 -12.149  1.00108.78           C  
ANISOU  759  CG2 ILE A 105    19175  11420  10738     64  -5465    274       C  
ATOM    760  CD1 ILE A 105      -7.736  28.172 -12.740  1.00108.98           C  
ANISOU  760  CD1 ILE A 105    19859  11390  10160    -13  -5212    -23       C  
ATOM    761  N   VAL A 106     -12.562  30.885 -11.274  1.00113.91           N  
ANISOU  761  N   VAL A 106    18260  11719  13302     75  -7009    652       N  
ATOM    762  CA  VAL A 106     -13.507  32.006 -11.279  1.00116.30           C  
ANISOU  762  CA  VAL A 106    18279  11852  14058    167  -7361    823       C  
ATOM    763  C   VAL A 106     -13.982  32.391  -9.864  1.00113.64           C  
ANISOU  763  C   VAL A 106    16927  11782  14469    216  -6907    926       C  
ATOM    764  O   VAL A 106     -14.030  33.562  -9.518  1.00112.63           O  
ANISOU  764  O   VAL A 106    16637  11717  14439    318  -6638    989       O  
ATOM    765  CB  VAL A 106     -14.727  31.689 -12.185  1.00122.51           C  
ANISOU  765  CB  VAL A 106    19208  12144  15196    149  -8451    939       C  
ATOM    766  CG1 VAL A 106     -15.888  32.621 -11.908  1.00125.00           C  
ANISOU  766  CG1 VAL A 106    18910  12291  16293    248  -8812   1151       C  
ATOM    767  CG2 VAL A 106     -14.318  31.778 -13.636  1.00125.55           C  
ANISOU  767  CG2 VAL A 106    20765  12196  14743    146  -8903    862       C  
ATOM    768  N   ALA A 107     -14.329  31.385  -9.063  1.00112.94           N  
ANISOU  768  N   ALA A 107    16215  11819  14880    146  -6808    942       N  
ATOM    769  CA  ALA A 107     -14.730  31.564  -7.654  1.00110.76           C  
ANISOU  769  CA  ALA A 107    15050  11784  15251    188  -6283   1032       C  
ATOM    770  C   ALA A 107     -13.627  32.251  -6.839  1.00105.79           C  
ANISOU  770  C   ALA A 107    14468  11533  14193    226  -5407    929       C  
ATOM    771  O   ALA A 107     -13.891  33.114  -5.992  1.00104.75           O  
ANISOU  771  O   ALA A 107    13915  11505  14378    323  -5022    998       O  
ATOM    772  CB  ALA A 107     -15.088  30.209  -7.033  1.00110.42           C  
ANISOU  772  CB  ALA A 107    14497  11800  15658     78  -6282   1055       C  
ATOM    773  N   GLN A 108     -12.392  31.848  -7.115  1.00103.06           N  
ANISOU  773  N   GLN A 108    14650  11356  13154    152  -5112    765       N  
ATOM    774  CA  GLN A 108     -11.206  32.446  -6.513  1.00 99.10           C  
ANISOU  774  CA  GLN A 108    14268  11161  12224    158  -4383    666       C  
ATOM    775  C   GLN A 108     -11.004  33.923  -6.912  1.00 99.83           C  
ANISOU  775  C   GLN A 108    14692  11178  12062    248  -4313    691       C  
ATOM    776  O   GLN A 108     -10.810  34.806  -6.061  1.00 98.03           O  
ANISOU  776  O   GLN A 108    14207  11111  11929    301  -3857    705       O  
ATOM    777  CB  GLN A 108      -9.976  31.604  -6.887  1.00 97.17           C  
ANISOU  777  CB  GLN A 108    14490  11037  11391     64  -4154    510       C  
ATOM    778  CG  GLN A 108      -9.890  30.278  -6.090  1.00 95.52           C  
ANISOU  778  CG  GLN A 108    13875  10999  11419    -21  -3990    474       C  
ATOM    779  CD  GLN A 108      -9.296  29.132  -6.865  1.00 95.57           C  
ANISOU  779  CD  GLN A 108    14342  10928  11042    -91  -4142    356       C  
ATOM    780  OE1 GLN A 108      -8.577  29.310  -7.841  1.00 96.56           O  
ANISOU  780  OE1 GLN A 108    15129  10948  10610    -76  -4137    270       O  
ATOM    781  NE2 GLN A 108      -9.603  27.942  -6.425  1.00 94.80           N  
ANISOU  781  NE2 GLN A 108    13918  10856  11246   -160  -4242    358       N  
ATOM    782  N   PHE A 109     -11.062  34.193  -8.210  1.00102.96           N  
ANISOU  782  N   PHE A 109    15713  11296  12112    264  -4783    700       N  
ATOM    783  CA  PHE A 109     -10.914  35.542  -8.709  1.00103.88           C  
ANISOU  783  CA  PHE A 109    16209  11290  11971    342  -4779    743       C  
ATOM    784  C   PHE A 109     -12.019  36.447  -8.165  1.00105.52           C  
ANISOU  784  C   PHE A 109    15877  11398  12817    466  -4933    887       C  
ATOM    785  O   PHE A 109     -11.715  37.527  -7.666  1.00104.17           O  
ANISOU  785  O   PHE A 109    15644  11325  12610    529  -4527    894       O  
ATOM    786  CB  PHE A 109     -10.927  35.536 -10.219  1.00107.92           C  
ANISOU  786  CB  PHE A 109    17540  11462  12003    339  -5330    747       C  
ATOM    787  CG  PHE A 109      -9.579  35.322 -10.833  1.00107.03           C  
ANISOU  787  CG  PHE A 109    18130  11415  11120    273  -4928    619       C  
ATOM    788  CD1 PHE A 109      -9.058  36.246 -11.731  1.00109.78           C  
ANISOU  788  CD1 PHE A 109    19198  11591  10921    302  -4873    639       C  
ATOM    789  CD2 PHE A 109      -8.841  34.206 -10.549  1.00104.59           C  
ANISOU  789  CD2 PHE A 109    17774  11305  10661    192  -4588    496       C  
ATOM    790  CE1 PHE A 109      -7.810  36.038 -12.327  1.00109.49           C  
ANISOU  790  CE1 PHE A 109    19799  11579  10222    251  -4421    542       C  
ATOM    791  CE2 PHE A 109      -7.598  33.999 -11.137  1.00104.28           C  
ANISOU  791  CE2 PHE A 109    18342  11290   9987    153  -4170    391       C  
ATOM    792  CZ  PHE A 109      -7.082  34.907 -12.021  1.00106.28           C  
ANISOU  792  CZ  PHE A 109    19285  11370   9726    183  -4056    417       C  
ATOM    793  N   ILE A 110     -13.282  36.011  -8.231  1.00108.67           N  
ANISOU  793  N   ILE A 110    15865  11580  13844    503  -5495   1006       N  
ATOM    794  CA  ILE A 110     -14.401  36.794  -7.675  1.00110.87           C  
ANISOU  794  CA  ILE A 110    15532  11731  14862    645  -5594   1163       C  
ATOM    795  C   ILE A 110     -14.211  37.097  -6.188  1.00107.41           C  
ANISOU  795  C   ILE A 110    14529  11602  14682    693  -4807   1138       C  
ATOM    796  O   ILE A 110     -14.443  38.218  -5.738  1.00107.55           O  
ANISOU  796  O   ILE A 110    14384  11591  14891    824  -4563   1188       O  
ATOM    797  CB  ILE A 110     -15.758  36.078  -7.860  1.00115.27           C  
ANISOU  797  CB  ILE A 110    15595  12007  16194    655  -6271   1313       C  
ATOM    798  CG1 ILE A 110     -16.186  36.122  -9.330  1.00120.21           C  
ANISOU  798  CG1 ILE A 110    16805  12214  16655    645  -7200   1375       C  
ATOM    799  CG2 ILE A 110     -16.842  36.725  -6.998  1.00117.20           C  
ANISOU  799  CG2 ILE A 110    15031  12169  17330    812  -6142   1479       C  
ATOM    800  CD1 ILE A 110     -17.506  35.401  -9.603  1.00125.19           C  
ANISOU  800  CD1 ILE A 110    16968  12505  18092    626  -8002   1534       C  
ATOM    801  N   GLY A 111     -13.796  36.082  -5.434  1.00104.50           N  
ANISOU  801  N   GLY A 111    13917  11494  14294    590  -4432   1060       N  
ATOM    802  CA  GLY A 111     -13.516  36.237  -4.008  1.00101.47           C  
ANISOU  802  CA  GLY A 111    13128  11386  14041    615  -3702   1024       C  
ATOM    803  C   GLY A 111     -12.361  37.178  -3.719  1.00 98.26           C  
ANISOU  803  C   GLY A 111    13110  11163  13061    612  -3201    907       C  
ATOM    804  O   GLY A 111     -12.394  37.946  -2.762  1.00 97.13           O  
ANISOU  804  O   GLY A 111    12753  11096  13058    697  -2756    908       O  
ATOM    805  N   ALA A 112     -11.336  37.112  -4.557  1.00 97.03           N  
ANISOU  805  N   ALA A 112    13546  11046  12273    511  -3265    809       N  
ATOM    806  CA  ALA A 112     -10.175  37.976  -4.422  1.00 94.94           C  
ANISOU  806  CA  ALA A 112    13647  10915  11509    478  -2835    719       C  
ATOM    807  C   ALA A 112     -10.518  39.471  -4.661  1.00 97.22           C  
ANISOU  807  C   ALA A 112    14083  11013  11844    604  -2896    788       C  
ATOM    808  O   ALA A 112     -10.089  40.367  -3.912  1.00 95.82           O  
ANISOU  808  O   ALA A 112    13881  10925  11602    631  -2471    751       O  
ATOM    809  CB  ALA A 112      -9.078  37.504  -5.384  1.00 93.89           C  
ANISOU  809  CB  ALA A 112    14090  10811  10773    354  -2868    630       C  
ATOM    810  N   ALA A 113     -11.291  39.732  -5.717  1.00101.12           N  
ANISOU  810  N   ALA A 113    14765  11210  12445    677  -3472    890       N  
ATOM    811  CA  ALA A 113     -11.713  41.095  -6.058  1.00103.41           C  
ANISOU  811  CA  ALA A 113    15208  11267  12815    809  -3625    977       C  
ATOM    812  C   ALA A 113     -12.564  41.667  -4.929  1.00104.08           C  
ANISOU  812  C   ALA A 113    14682  11339  13523    967  -3380   1037       C  
ATOM    813  O   ALA A 113     -12.396  42.829  -4.563  1.00103.95           O  
ANISOU  813  O   ALA A 113    14746  11287  13464   1051  -3105   1031       O  
ATOM    814  CB  ALA A 113     -12.483  41.106  -7.389  1.00107.82           C  
ANISOU  814  CB  ALA A 113    16076  11468  13423    858  -4397   1093       C  
ATOM    815  N   LEU A 114     -13.467  40.843  -4.382  1.00105.15           N  
ANISOU  815  N   LEU A 114    14232  11479  14241   1009  -3448   1099       N  
ATOM    816  CA  LEU A 114     -14.330  41.236  -3.255  1.00106.54           C  
ANISOU  816  CA  LEU A 114    13804  11623  15055   1174  -3111   1168       C  
ATOM    817  C   LEU A 114     -13.543  41.591  -1.985  1.00103.18           C  
ANISOU  817  C   LEU A 114    13387  11454  14365   1160  -2358   1041       C  
ATOM    818  O   LEU A 114     -13.863  42.559  -1.300  1.00103.86           O  
ANISOU  818  O   LEU A 114    13349  11455  14660   1316  -2033   1054       O  
ATOM    819  CB  LEU A 114     -15.341  40.127  -2.935  1.00108.57           C  
ANISOU  819  CB  LEU A 114    13440  11834  15977   1185  -3269   1274       C  
ATOM    820  CG  LEU A 114     -16.797  40.313  -3.359  1.00114.16           C  
ANISOU  820  CG  LEU A 114    13685  12176  17515   1342  -3787   1479       C  
ATOM    821  CD1 LEU A 114     -16.963  40.626  -4.836  1.00116.66           C  
ANISOU  821  CD1 LEU A 114    14440  12209  17676   1331  -4599   1542       C  
ATOM    822  CD2 LEU A 114     -17.536  39.033  -2.973  1.00115.50           C  
ANISOU  822  CD2 LEU A 114    13257  12345  18281   1285  -3862   1572       C  
ATOM    823  N   GLY A 115     -12.536  40.775  -1.663  1.00 99.81           N  
ANISOU  823  N   GLY A 115    13118  11306  13498    979  -2111    919       N  
ATOM    824  CA  GLY A 115     -11.684  41.000  -0.480  1.00 96.93           C  
ANISOU  824  CA  GLY A 115    12823  11164  12844    930  -1502    798       C  
ATOM    825  C   GLY A 115     -10.855  42.267  -0.625  1.00 96.39           C  
ANISOU  825  C   GLY A 115    13209  11062  12354    922  -1364    726       C  
ATOM    826  O   GLY A 115     -10.706  43.042   0.334  1.00 96.21           O  
ANISOU  826  O   GLY A 115    13202  11042  12313    987   -964    672       O  
ATOM    827  N   SER A 116     -10.333  42.490  -1.842  1.00 96.39           N  
ANISOU  827  N   SER A 116    13623  10994  12007    841  -1693    730       N  
ATOM    828  CA  SER A 116      -9.518  43.680  -2.155  1.00 95.75           C  
ANISOU  828  CA  SER A 116    13995  10847  11540    808  -1589    691       C  
ATOM    829  C   SER A 116     -10.372  44.970  -2.082  1.00 98.60           C  
ANISOU  829  C   SER A 116    14313  10944  12207   1014  -1640    767       C  
ATOM    830  O   SER A 116     -10.046  45.928  -1.350  1.00 98.04           O  
ANISOU  830  O   SER A 116    14338  10849  12061   1052  -1300    708       O  
ATOM    831  CB  SER A 116      -8.857  43.495  -3.525  1.00 95.60           C  
ANISOU  831  CB  SER A 116    14447  10781  11096    686  -1882    706       C  
ATOM    832  OG  SER A 116      -7.686  44.255  -3.596  1.00 94.12           O  
ANISOU  832  OG  SER A 116    14638  10625  10499    573  -1613    653       O  
ATOM    833  N   LEU A 117     -11.494  44.942  -2.807  1.00101.68           N  
ANISOU  833  N   LEU A 117    14543  11109  12983   1151  -2094    899       N  
ATOM    834  CA  LEU A 117     -12.485  46.022  -2.780  1.00105.03           C  
ANISOU  834  CA  LEU A 117    14820  11243  13844   1381  -2203    999       C  
ATOM    835  C   LEU A 117     -13.007  46.363  -1.379  1.00105.54           C  
ANISOU  835  C   LEU A 117    14477  11315  14309   1543  -1692    970       C  
ATOM    836  O   LEU A 117     -13.099  47.525  -1.032  1.00106.57           O  
ANISOU  836  O   LEU A 117    14717  11287  14486   1678  -1493    958       O  
ATOM    837  CB  LEU A 117     -13.694  45.681  -3.673  1.00108.80           C  
ANISOU  837  CB  LEU A 117    15061  11464  14812   1493  -2837   1166       C  
ATOM    838  CG  LEU A 117     -13.784  46.449  -4.998  1.00111.74           C  
ANISOU  838  CG  LEU A 117    15909  11546  15000   1524  -3391   1263       C  
ATOM    839  CD1 LEU A 117     -12.766  45.908  -6.026  1.00110.04           C  
ANISOU  839  CD1 LEU A 117    16311  11425  14074   1302  -3593   1210       C  
ATOM    840  CD2 LEU A 117     -15.216  46.404  -5.559  1.00116.65           C  
ANISOU  840  CD2 LEU A 117    16177  11828  16315   1698  -4023   1450       C  
ATOM    841  N   LEU A 118     -13.389  45.345  -0.609  1.00105.23           N  
ANISOU  841  N   LEU A 118    14006  11423  14555   1541  -1476    966       N  
ATOM    842  CA  LEU A 118     -13.915  45.545   0.743  1.00106.51           C  
ANISOU  842  CA  LEU A 118    13837  11569  15063   1701   -921    948       C  
ATOM    843  C   LEU A 118     -12.873  46.167   1.681  1.00104.22           C  
ANISOU  843  C   LEU A 118    13945  11405  14249   1634   -420    778       C  
ATOM    844  O   LEU A 118     -13.196  47.080   2.460  1.00106.24           O  
ANISOU  844  O   LEU A 118    14226  11502  14639   1812    -53    748       O  
ATOM    845  CB  LEU A 118     -14.446  44.224   1.356  1.00106.61           C  
ANISOU  845  CB  LEU A 118    13363  11713  15432   1678   -765    995       C  
ATOM    846  CG  LEU A 118     -15.975  44.084   1.433  1.00111.26           C  
ANISOU  846  CG  LEU A 118    13312  12051  16911   1899   -827   1182       C  
ATOM    847  CD1 LEU A 118     -16.625  45.274   2.175  1.00114.12           C  
ANISOU  847  CD1 LEU A 118    13555  12170  17637   2183   -379   1207       C  
ATOM    848  CD2 LEU A 118     -16.578  43.958   0.053  1.00113.86           C  
ANISOU  848  CD2 LEU A 118    13524  12180  17559   1900  -1604   1324       C  
ATOM    849  N   PHE A 119     -11.639  45.667   1.629  1.00100.36           N  
ANISOU  849  N   PHE A 119    13766  11166  13201   1383   -415    669       N  
ATOM    850  CA  PHE A 119     -10.580  46.266   2.429  1.00 98.43           C  
ANISOU  850  CA  PHE A 119    13903  11000  12497   1284    -65    523       C  
ATOM    851  C   PHE A 119     -10.451  47.717   2.067  1.00 99.91           C  
ANISOU  851  C   PHE A 119    14415  10959  12585   1361   -122    515       C  
ATOM    852  O   PHE A 119     -10.403  48.568   2.954  1.00100.95           O  
ANISOU  852  O   PHE A 119    14713  10974  12670   1453    209    436       O  
ATOM    853  CB  PHE A 119      -9.242  45.600   2.199  1.00 95.01           C  
ANISOU  853  CB  PHE A 119    13707  10814  11577   1002   -138    442       C  
ATOM    854  CG  PHE A 119      -8.207  45.986   3.212  1.00 93.77           C  
ANISOU  854  CG  PHE A 119    13840  10730  11059    881    176    307       C  
ATOM    855  CD1 PHE A 119      -8.065  45.237   4.387  1.00 93.84           C  
ANISOU  855  CD1 PHE A 119    13758  10878  11019    841    458    242       C  
ATOM    856  CD2 PHE A 119      -7.373  47.078   3.001  1.00 93.52           C  
ANISOU  856  CD2 PHE A 119    14193  10595  10746    795    155    256       C  
ATOM    857  CE1 PHE A 119      -7.110  45.582   5.345  1.00 92.91           C  
ANISOU  857  CE1 PHE A 119    13961  10782  10560    720    656    121       C  
ATOM    858  CE2 PHE A 119      -6.412  47.435   3.935  1.00 93.18           C  
ANISOU  858  CE2 PHE A 119    14414  10573  10416    661    357    138       C  
ATOM    859  CZ  PHE A 119      -6.278  46.694   5.114  1.00 93.30           C  
ANISOU  859  CZ  PHE A 119    14369  10714  10368    625    579     66       C  
ATOM    860  N   LEU A 120     -10.403  47.998   0.760  1.00100.41           N  
ANISOU  860  N   LEU A 120    14628  10928  12593   1326   -548    600       N  
ATOM    861  CA  LEU A 120     -10.324  49.396   0.255  1.00102.24           C  
ANISOU  861  CA  LEU A 120    15196  10907  12742   1397   -657    625       C  
ATOM    862  C   LEU A 120     -11.399  50.273   0.907  1.00105.50           C  
ANISOU  862  C   LEU A 120    15424  11057  13606   1695   -463    651       C  
ATOM    863  O   LEU A 120     -11.063  51.309   1.478  1.00106.10           O  
ANISOU  863  O   LEU A 120    15781  11003  13529   1738   -209    567       O  
ATOM    864  CB  LEU A 120     -10.412  49.442  -1.292  1.00103.20           C  
ANISOU  864  CB  LEU A 120    15501  10914  12798   1361  -1178    752       C  
ATOM    865  CG  LEU A 120     -10.476  50.800  -2.029  1.00105.47           C  
ANISOU  865  CG  LEU A 120    16149  10898  13026   1443  -1385    826       C  
ATOM    866  CD1 LEU A 120      -9.376  51.779  -1.608  1.00104.03           C  
ANISOU  866  CD1 LEU A 120    16369  10701  12458   1316  -1079    726       C  
ATOM    867  CD2 LEU A 120     -10.420  50.579  -3.528  1.00105.99           C  
ANISOU  867  CD2 LEU A 120    16499  10875  12896   1365  -1885    946       C  
ATOM    868  N   ALA A 121     -12.662  49.826   0.843  1.00107.88           N  
ANISOU  868  N   ALA A 121    15243  11258  14488   1895   -569    770       N  
ATOM    869  CA  ALA A 121     -13.810  50.528   1.451  1.00111.94           C  
ANISOU  869  CA  ALA A 121    15466  11495  15571   2215   -329    824       C  
ATOM    870  C   ALA A 121     -13.641  50.720   2.957  1.00111.97           C  
ANISOU  870  C   ALA A 121    15540  11534  15471   2285    339    680       C  
ATOM    871  O   ALA A 121     -13.923  51.784   3.506  1.00114.62           O  
ANISOU  871  O   ALA A 121    16022  11624  15904   2485    632    636       O  
ATOM    872  CB  ALA A 121     -15.100  49.780   1.181  1.00114.56           C  
ANISOU  872  CB  ALA A 121    15174  11734  16618   2372   -537    994       C  
ATOM    873  N   CYS A 122     -13.175  49.675   3.622  1.00109.43           N  
ANISOU  873  N   CYS A 122    15167  11490  14923   2122    565    606       N  
ATOM    874  CA  CYS A 122     -12.931  49.735   5.053  1.00109.57           C  
ANISOU  874  CA  CYS A 122    15361  11534  14738   2157   1149    470       C  
ATOM    875  C   CYS A 122     -11.964  50.856   5.456  1.00108.98           C  
ANISOU  875  C   CYS A 122    15897  11367  14144   2083   1268    310       C  
ATOM    876  O   CYS A 122     -12.217  51.555   6.415  1.00111.64           O  
ANISOU  876  O   CYS A 122    16438  11502  14477   2259   1690    224       O  
ATOM    877  CB  CYS A 122     -12.401  48.379   5.563  1.00106.56           C  
ANISOU  877  CB  CYS A 122    14903  11471  14115   1944   1253    427       C  
ATOM    878  SG  CYS A 122     -13.666  47.127   5.863  1.00108.18           S  
ANISOU  878  SG  CYS A 122    14429  11710  14964   2080   1432    582       S  
ATOM    879  N   VAL A 123     -10.874  51.033   4.721  1.00106.09           N  
ANISOU  879  N   VAL A 123    15834  11112  13364   1827    914    276       N  
ATOM    880  CA  VAL A 123      -9.801  51.919   5.159  1.00105.50           C  
ANISOU  880  CA  VAL A 123    16299  10969  12819   1685    993    134       C  
ATOM    881  C   VAL A 123      -9.903  53.318   4.564  1.00108.08           C  
ANISOU  881  C   VAL A 123    16875  10997  13194   1789    843    159       C  
ATOM    882  O   VAL A 123      -9.777  54.320   5.282  1.00110.28           O  
ANISOU  882  O   VAL A 123    17506  11046  13349   1872   1073     51       O  
ATOM    883  CB  VAL A 123      -8.439  51.327   4.827  1.00101.62           C  
ANISOU  883  CB  VAL A 123    15969  10740  11902   1329    769     93       C  
ATOM    884  CG1 VAL A 123      -7.296  52.289   5.189  1.00100.98           C  
ANISOU  884  CG1 VAL A 123    16389  10545  11434   1152    777    -24       C  
ATOM    885  CG2 VAL A 123      -8.292  50.035   5.567  1.00 99.88           C  
ANISOU  885  CG2 VAL A 123    15560  10774  11616   1239    929     55       C  
ATOM    886  N   GLY A 124     -10.148  53.391   3.257  1.00108.28           N  
ANISOU  886  N   GLY A 124    16771  10991  13379   1788    442    304       N  
ATOM    887  CA  GLY A 124     -10.148  54.658   2.517  1.00110.16           C  
ANISOU  887  CA  GLY A 124    17286  10947  13621   1850    227    359       C  
ATOM    888  C   GLY A 124      -9.201  54.539   1.343  1.00107.91           C  
ANISOU  888  C   GLY A 124    17220  10778  13004   1572   -137    427       C  
ATOM    889  O   GLY A 124      -8.528  53.525   1.195  1.00104.99           O  
ANISOU  889  O   GLY A 124    16782  10693  12418   1352   -179    412       O  
ATOM    890  N   PRO A 125      -9.137  55.568   0.495  1.00109.74           N  
ANISOU  890  N   PRO A 125    17738  10764  13194   1590   -369    512       N  
ATOM    891  CA  PRO A 125      -8.264  55.576  -0.689  1.00108.51           C  
ANISOU  891  CA  PRO A 125    17870  10652  12705   1346   -646    601       C  
ATOM    892  C   PRO A 125      -6.780  55.389  -0.349  1.00105.69           C  
ANISOU  892  C   PRO A 125    17729  10484  11943   1015   -459    503       C  
ATOM    893  O   PRO A 125      -6.010  54.844  -1.162  1.00103.83           O  
ANISOU  893  O   PRO A 125    17584  10395  11471    799   -565    565       O  
ATOM    894  CB  PRO A 125      -8.469  56.980  -1.271  1.00111.73           C  
ANISOU  894  CB  PRO A 125    18613  10691  13148   1451   -808    688       C  
ATOM    895  CG  PRO A 125      -9.732  57.463  -0.694  1.00115.03           C  
ANISOU  895  CG  PRO A 125    18791  10885  14032   1802   -738    683       C  
ATOM    896  CD  PRO A 125      -9.846  56.844   0.661  1.00113.51           C  
ANISOU  896  CD  PRO A 125    18333  10872  13924   1850   -331    528       C  
ATOM    897  N   ALA A 126      -6.389  55.877   0.836  1.00105.62           N  
ANISOU  897  N   ALA A 126    17827  10427  11877    987   -191    357       N  
ATOM    898  CA  ALA A 126      -5.033  55.701   1.359  1.00103.40           C  
ANISOU  898  CA  ALA A 126    17694  10282  11311    679    -68    262       C  
ATOM    899  C   ALA A 126      -4.568  54.265   1.139  1.00100.45           C  
ANISOU  899  C   ALA A 126    17056  10256  10853    516    -86    277       C  
ATOM    900  O   ALA A 126      -3.420  54.019   0.765  1.00 98.99           O  
ANISOU  900  O   ALA A 126    16954  10174  10484    248    -97    301       O  
ATOM    901  CB  ALA A 126      -4.998  56.071   2.844  1.00104.01           C  
ANISOU  901  CB  ALA A 126    17884  10270  11364    727    167     87       C  
ATOM    902  N   ALA A 127      -5.497  53.329   1.354  1.00100.00           N  
ANISOU  902  N   ALA A 127    16660  10351  10984    689    -72    275       N  
ATOM    903  CA  ALA A 127      -5.273  51.892   1.191  1.00 97.48           C  
ANISOU  903  CA  ALA A 127    16069  10339  10628    581   -101    286       C  
ATOM    904  C   ALA A 127      -4.647  51.535  -0.141  1.00 96.85           C  
ANISOU  904  C   ALA A 127    16092  10328  10379    416   -285    394       C  
ATOM    905  O   ALA A 127      -3.889  50.575  -0.219  1.00 95.13           O  
ANISOU  905  O   ALA A 127    15778  10331  10037    239   -242    376       O  
ATOM    906  CB  ALA A 127      -6.598  51.129   1.375  1.00 97.67           C  
ANISOU  906  CB  ALA A 127    15717  10426  10968    821   -115    315       C  
ATOM    907  N   ALA A 128      -4.972  52.301  -1.181  1.00 99.19           N  
ANISOU  907  N   ALA A 128    16618  10406  10662    489   -474    509       N  
ATOM    908  CA  ALA A 128      -4.439  52.088  -2.539  1.00 99.49           C  
ANISOU  908  CA  ALA A 128    16894  10436  10470    358   -617    626       C  
ATOM    909  C   ALA A 128      -3.302  53.073  -2.839  1.00100.40           C  
ANISOU  909  C   ALA A 128    17369  10399  10378    156   -481    665       C  
ATOM    910  O   ALA A 128      -2.185  52.682  -3.216  1.00 99.49           O  
ANISOU  910  O   ALA A 128    17333  10382  10087    -70   -335    690       O  
ATOM    911  CB  ALA A 128      -5.551  52.269  -3.568  1.00101.97           C  
ANISOU  911  CB  ALA A 128    17309  10560  10876    560   -966    754       C  
ATOM    912  N   THR A 129      -3.586  54.353  -2.665  1.00102.33           N  
ANISOU  912  N   THR A 129    17811  10378  10690    241   -509    680       N  
ATOM    913  CA  THR A 129      -2.587  55.361  -2.963  1.00103.86           C  
ANISOU  913  CA  THR A 129    18345  10381  10736     45   -403    737       C  
ATOM    914  C   THR A 129      -1.345  55.299  -2.061  1.00102.52           C  
ANISOU  914  C   THR A 129    18078  10313  10560   -215   -175    640       C  
ATOM    915  O   THR A 129      -0.245  55.665  -2.495  1.00103.52           O  
ANISOU  915  O   THR A 129    18370  10355  10605   -454    -57    720       O  
ATOM    916  CB  THR A 129      -3.176  56.733  -2.848  1.00106.54           C  
ANISOU  916  CB  THR A 129    18911  10395  11176    196   -495    758       C  
ATOM    917  OG1 THR A 129      -3.920  56.799  -1.621  1.00106.25           O  
ANISOU  917  OG1 THR A 129    18643  10370  11358    387   -445    612       O  
ATOM    918  CG2 THR A 129      -4.076  57.007  -4.077  1.00108.86           C  
ANISOU  918  CG2 THR A 129    19416  10497  11449    382   -785    920       C  
ATOM    919  N   VAL A 130      -1.506  54.861  -0.819  1.00100.85           N  
ANISOU  919  N   VAL A 130    17617  10246  10458   -175   -122    487       N  
ATOM    920  CA  VAL A 130      -0.355  54.680   0.056  1.00 99.75           C  
ANISOU  920  CA  VAL A 130    17395  10185  10319   -424     -8    400       C  
ATOM    921  C   VAL A 130      -0.013  53.220   0.267  1.00 97.24           C  
ANISOU  921  C   VAL A 130    16753  10191  10003   -500     44    362       C  
ATOM    922  O   VAL A 130       1.166  52.914   0.420  1.00 97.16           O  
ANISOU  922  O   VAL A 130    16657  10244  10014   -747    113    369       O  
ATOM    923  CB  VAL A 130      -0.569  55.288   1.407  1.00100.42           C  
ANISOU  923  CB  VAL A 130    17561  10143  10452   -365     -3    247       C  
ATOM    924  CG1 VAL A 130       0.750  55.309   2.157  1.00100.31           C  
ANISOU  924  CG1 VAL A 130    17558  10116  10440   -667     -1    188       C  
ATOM    925  CG2 VAL A 130      -1.121  56.660   1.241  1.00102.73           C  
ANISOU  925  CG2 VAL A 130    18160  10105  10766   -225    -49    268       C  
ATOM    926  N   GLY A 131      -1.014  52.333   0.282  1.00 95.72           N  
ANISOU  926  N   GLY A 131    16357  10173   9840   -295      0    336       N  
ATOM    927  CA  GLY A 131      -0.789  50.903   0.523  1.00 93.21           C  
ANISOU  927  CA  GLY A 131    15738  10147   9530   -350     36    297       C  
ATOM    928  C   GLY A 131      -0.647  50.014  -0.705  1.00 92.46           C  
ANISOU  928  C   GLY A 131    15592  10180   9359   -379     15    397       C  
ATOM    929  O   GLY A 131      -0.185  48.872  -0.585  1.00 90.78           O  
ANISOU  929  O   GLY A 131    15161  10180   9150   -466     69    370       O  
ATOM    930  N   GLY A 132      -1.070  50.516  -1.873  1.00 94.06           N  
ANISOU  930  N   GLY A 132    16043  10225   9471   -296    -78    508       N  
ATOM    931  CA  GLY A 132      -1.046  49.758  -3.144  1.00 94.05           C  
ANISOU  931  CA  GLY A 132    16149  10274   9314   -297   -126    600       C  
ATOM    932  C   GLY A 132      -1.978  48.578  -3.184  1.00 92.75           C  
ANISOU  932  C   GLY A 132    15754  10275   9213   -147   -300    567       C  
ATOM    933  O   GLY A 132      -1.845  47.713  -4.018  1.00 92.30           O  
ANISOU  933  O   GLY A 132    15767  10284   9019   -170   -339    603       O  
ATOM    934  N   LEU A 133      -2.921  48.560  -2.252  1.00 92.65           N  
ANISOU  934  N   LEU A 133    15482  10299   9421      8   -379    499       N  
ATOM    935  CA  LEU A 133      -3.777  47.400  -1.991  1.00 91.66           C  
ANISOU  935  CA  LEU A 133    15034  10337   9457    126   -495    469       C  
ATOM    936  C   LEU A 133      -2.967  46.095  -1.829  1.00 89.55           C  
ANISOU  936  C   LEU A 133    14597  10317   9110    -28   -377    416       C  
ATOM    937  O   LEU A 133      -3.495  44.967  -2.047  1.00 88.78           O  
ANISOU  937  O   LEU A 133    14321  10335   9078     28   -509    417       O  
ATOM    938  CB  LEU A 133      -4.864  47.283  -3.085  1.00 93.54           C  
ANISOU  938  CB  LEU A 133    15358  10435   9749    290   -840    571       C  
ATOM    939  CG  LEU A 133      -5.912  48.408  -3.077  1.00 95.78           C  
ANISOU  939  CG  LEU A 133    15676  10466  10250    495  -1004    630       C  
ATOM    940  CD1 LEU A 133      -6.807  48.327  -4.272  1.00 96.82           C  
ANISOU  940  CD1 LEU A 133    15944  10413  10428    620  -1434    753       C  
ATOM    941  CD2 LEU A 133      -6.725  48.363  -1.764  1.00 95.42           C  
ANISOU  941  CD2 LEU A 133    15224  10468  10563    647   -863    563       C  
ATOM    942  N   GLY A 134      -1.704  46.255  -1.395  1.00 88.66           N  
ANISOU  942  N   GLY A 134    14516  10259   8912   -222   -156    377       N  
ATOM    943  CA  GLY A 134      -0.779  45.124  -1.184  1.00 86.66           C  
ANISOU  943  CA  GLY A 134    14083  10205   8640   -371    -33    338       C  
ATOM    944  C   GLY A 134      -0.512  44.303  -2.410  1.00 86.65           C  
ANISOU  944  C   GLY A 134    14199  10231   8493   -394    -43    391       C  
ATOM    945  O   GLY A 134      -0.248  43.131  -2.280  1.00 84.94           O  
ANISOU  945  O   GLY A 134    13792  10176   8304   -430    -11    352       O  
ATOM    946  N   ALA A 135      -0.579  44.936  -3.590  1.00 88.60           N  
ANISOU  946  N   ALA A 135    14816  10289   8557   -366    -82    480       N  
ATOM    947  CA  ALA A 135      -0.400  44.236  -4.876  1.00 89.67           C  
ANISOU  947  CA  ALA A 135    15226  10383   8461   -364    -87    530       C  
ATOM    948  C   ALA A 135       1.034  43.820  -5.018  1.00 89.49           C  
ANISOU  948  C   ALA A 135    15188  10417   8397   -535    275    535       C  
ATOM    949  O   ALA A 135       1.923  44.456  -4.445  1.00 89.41           O  
ANISOU  949  O   ALA A 135    15056  10393   8523   -675    484    547       O  
ATOM    950  CB  ALA A 135      -0.797  45.091  -6.043  1.00 92.52           C  
ANISOU  950  CB  ALA A 135    16078  10485   8590   -294   -218    636       C  
ATOM    951  N   THR A 136       1.254  42.723  -5.733  1.00 89.64           N  
ANISOU  951  N   THR A 136    15307  10477   8276   -522    337    526       N  
ATOM    952  CA  THR A 136       2.603  42.185  -5.884  1.00 90.00           C  
ANISOU  952  CA  THR A 136    15282  10560   8352   -653    729    535       C  
ATOM    953  C   THR A 136       3.233  42.757  -7.136  1.00 93.15           C  
ANISOU  953  C   THR A 136    16175  10725   8494   -689   1027    648       C  
ATOM    954  O   THR A 136       2.552  43.000  -8.126  1.00 95.10           O  
ANISOU  954  O   THR A 136    16913  10804   8418   -586    869    694       O  
ATOM    955  CB  THR A 136       2.652  40.586  -5.903  1.00 88.88           C  
ANISOU  955  CB  THR A 136    14974  10572   8226   -613    723    455       C  
ATOM    956  OG1 THR A 136       1.684  40.052  -6.810  1.00 89.81           O  
ANISOU  956  OG1 THR A 136    15439  10609   8075   -473    453    441       O  
ATOM    957  CG2 THR A 136       2.443  39.961  -4.468  1.00 85.22           C  
ANISOU  957  CG2 THR A 136    13966  10342   8070   -632    563    366       C  
ATOM    958  N   ALA A 137       4.532  42.996  -7.080  1.00 94.21           N  
ANISOU  958  N   ALA A 137    16186  10815   8793   -841   1450    710       N  
ATOM    959  CA  ALA A 137       5.269  43.397  -8.269  1.00 98.02           C  
ANISOU  959  CA  ALA A 137    17117  11062   9065   -882   1870    838       C  
ATOM    960  C   ALA A 137       6.730  43.355  -7.901  1.00 98.98           C  
ANISOU  960  C   ALA A 137    16852  11180   9575  -1056   2329    899       C  
ATOM    961  O   ALA A 137       7.047  43.434  -6.715  1.00 97.15           O  
ANISOU  961  O   ALA A 137    16099  11082   9732  -1162   2195    856       O  
ATOM    962  CB  ALA A 137       4.880  44.744  -8.695  1.00 99.76           C  
ANISOU  962  CB  ALA A 137    17721  11076   9109   -885   1784    937       C  
ATOM    963  N   PRO A 138       7.622  43.223  -8.895  1.00102.21           N  
ANISOU  963  N   PRO A 138    17524  11407   9903  -1083   2867   1008       N  
ATOM    964  CA  PRO A 138       9.055  43.006  -8.649  1.00103.92           C  
ANISOU  964  CA  PRO A 138    17302  11589  10594  -1230   3354   1088       C  
ATOM    965  C   PRO A 138       9.642  44.096  -7.802  1.00104.19           C  
ANISOU  965  C   PRO A 138    16943  11573  11071  -1437   3309   1169       C  
ATOM    966  O   PRO A 138       9.091  45.170  -7.782  1.00104.47           O  
ANISOU  966  O   PRO A 138    17223  11525  10947  -1458   3089   1198       O  
ATOM    967  CB  PRO A 138       9.667  43.077 -10.042  1.00108.70           C  
ANISOU  967  CB  PRO A 138    18433  11921  10949  -1201   3984   1228       C  
ATOM    968  CG  PRO A 138       8.578  42.722 -10.946  1.00108.99           C  
ANISOU  968  CG  PRO A 138    19165  11914  10332  -1006   3761   1156       C  
ATOM    969  CD  PRO A 138       7.307  43.234 -10.324  1.00105.28           C  
ANISOU  969  CD  PRO A 138    18672  11578   9752   -965   3052   1069       C  
ATOM    970  N   PHE A 139      10.752  43.849  -7.122  1.00104.90           N  
ANISOU  970  N   PHE A 139    16447  11677  11732  -1589   3481   1212       N  
ATOM    971  CA  PHE A 139      11.367  44.897  -6.296  1.00105.87           C  
ANISOU  971  CA  PHE A 139    16215  11702  12311  -1814   3366   1292       C  
ATOM    972  C   PHE A 139      12.562  45.522  -6.979  1.00110.76           C  
ANISOU  972  C   PHE A 139    16791  12027  13264  -1975   3954   1516       C  
ATOM    973  O   PHE A 139      13.068  44.975  -7.943  1.00113.63           O  
ANISOU  973  O   PHE A 139    17302  12287  13586  -1906   4517   1603       O  
ATOM    974  CB  PHE A 139      11.724  44.360  -4.903  1.00103.70           C  
ANISOU  974  CB  PHE A 139    15318  11592  12491  -1908   2998   1200       C  
ATOM    975  CG  PHE A 139      10.562  44.373  -3.948  1.00 99.79           C  
ANISOU  975  CG  PHE A 139    14882  11301  11732  -1823   2400   1021       C  
ATOM    976  CD1 PHE A 139       9.446  43.576  -4.182  1.00 97.13           C  
ANISOU  976  CD1 PHE A 139    14787  11155  10965  -1604   2235    893       C  
ATOM    977  CD2 PHE A 139      10.562  45.196  -2.843  1.00 99.43           C  
ANISOU  977  CD2 PHE A 139    14684  11220  11876  -1958   2023    987       C  
ATOM    978  CE1 PHE A 139       8.360  43.596  -3.324  1.00 94.08           C  
ANISOU  978  CE1 PHE A 139    14419  10927  10401  -1518   1767    756       C  
ATOM    979  CE2 PHE A 139       9.467  45.218  -1.977  1.00 96.41           C  
ANISOU  979  CE2 PHE A 139    14403  10992  11235  -1852   1573    829       C  
ATOM    980  CZ  PHE A 139       8.368  44.418  -2.219  1.00 93.69           C  
ANISOU  980  CZ  PHE A 139    14233  10843  10520  -1630   1477    724       C  
ATOM    981  N   PRO A 140      12.990  46.697  -6.503  1.00112.36           N  
ANISOU  981  N   PRO A 140    16832  12065  13797  -2185   3849   1615       N  
ATOM    982  CA  PRO A 140      14.147  47.414  -7.073  1.00117.69           C  
ANISOU  982  CA  PRO A 140    17400  12421  14896  -2379   4398   1861       C  
ATOM    983  C   PRO A 140      15.382  46.545  -7.345  1.00120.99           C  
ANISOU  983  C   PRO A 140    17342  12758  15869  -2424   4957   1983       C  
ATOM    984  O   PRO A 140      15.976  45.976  -6.420  1.00120.31           O  
ANISOU  984  O   PRO A 140    16617  12754  16342  -2513   4730   1949       O  
ATOM    985  CB  PRO A 140      14.469  48.464  -6.019  1.00118.02           C  
ANISOU  985  CB  PRO A 140    17110  12353  15378  -2624   3974   1889       C  
ATOM    986  CG  PRO A 140      13.152  48.672  -5.262  1.00113.59           C  
ANISOU  986  CG  PRO A 140    16814  12004  14341  -2499   3301   1664       C  
ATOM    987  CD  PRO A 140      12.209  47.547  -5.586  1.00109.77           C  
ANISOU  987  CD  PRO A 140    16569  11791  13347  -2223   3242   1506       C  
ATOM    988  N   GLY A 141      15.744  46.459  -8.625  1.00124.97           N  
ANISOU  988  N   GLY A 141    18204  13070  16207  -2349   5693   2132       N  
ATOM    989  CA  GLY A 141      16.855  45.622  -9.098  1.00128.85           C  
ANISOU  989  CA  GLY A 141    18345  13439  17175  -2333   6387   2259       C  
ATOM    990  C   GLY A 141      16.473  44.169  -9.389  1.00126.94           C  
ANISOU  990  C   GLY A 141    18249  13399  16581  -2070   6464   2089       C  
ATOM    991  O   GLY A 141      17.342  43.284  -9.437  1.00129.38           O  
ANISOU  991  O   GLY A 141    18122  13661  17375  -2036   6879   2139       O  
ATOM    992  N   ILE A 142      15.180  43.917  -9.600  1.00123.01           N  
ANISOU  992  N   ILE A 142    18352  13097  15291  -1880   6061   1897       N  
ATOM    993  CA  ILE A 142      14.688  42.572  -9.893  1.00121.04           C  
ANISOU  993  CA  ILE A 142    18311  13018  14662  -1641   6046   1725       C  
ATOM    994  C   ILE A 142      13.959  42.513 -11.242  1.00122.77           C  
ANISOU  994  C   ILE A 142    19495  13116  14036  -1443   6312   1706       C  
ATOM    995  O   ILE A 142      12.844  43.045 -11.372  1.00120.64           O  
ANISOU  995  O   ILE A 142    19724  12904  13212  -1392   5834   1632       O  
ATOM    996  CB  ILE A 142      13.732  42.079  -8.796  1.00115.00           C  
ANISOU  996  CB  ILE A 142    17326  12592  13775  -1593   5209   1498       C  
ATOM    997  CG1 ILE A 142      14.488  41.912  -7.476  1.00113.98           C  
ANISOU  997  CG1 ILE A 142    16342  12556  14411  -1765   4929   1504       C  
ATOM    998  CG2 ILE A 142      13.095  40.766  -9.209  1.00113.24           C  
ANISOU  998  CG2 ILE A 142    17404  12511  13111  -1356   5163   1333       C  
ATOM    999  CD1 ILE A 142      15.449  40.714  -7.453  1.00115.76           C  
ANISOU  999  CD1 ILE A 142    16082  12763  15138  -1718   5296   1530       C  
ATOM   1000  N   GLY A 143      14.575  41.840 -12.222  1.00127.01           N  
ANISOU 1000  N   GLY A 143    20312  13459  14486  -1322   7050   1772       N  
ATOM   1001  CA  GLY A 143      13.994  41.680 -13.565  1.00129.60           C  
ANISOU 1001  CA  GLY A 143    21669  13608  13966  -1128   7335   1754       C  
ATOM   1002  C   GLY A 143      12.850  40.673 -13.621  1.00126.04           C  
ANISOU 1002  C   GLY A 143    21593  13356  12943   -926   6766   1508       C  
ATOM   1003  O   GLY A 143      12.586  39.979 -12.646  1.00121.76           O  
ANISOU 1003  O   GLY A 143    20481  13096  12686   -923   6268   1359       O  
ATOM   1004  N   TYR A 144      12.157  40.612 -14.759  1.00128.34           N  
ANISOU 1004  N   TYR A 144    22869  13468  12428   -769   6805   1477       N  
ATOM   1005  CA  TYR A 144      11.038  39.673 -14.943  1.00125.85           C  
ANISOU 1005  CA  TYR A 144    22976  13271  11571   -590   6229   1261       C  
ATOM   1006  C   TYR A 144      11.546  38.231 -14.904  1.00126.32           C  
ANISOU 1006  C   TYR A 144    22802  13378  11814   -468   6526   1145       C  
ATOM   1007  O   TYR A 144      10.869  37.324 -14.376  1.00122.42           O  
ANISOU 1007  O   TYR A 144    22102  13112  11301   -396   5958    961       O  
ATOM   1008  CB  TYR A 144      10.271  39.946 -16.254  1.00129.22           C  
ANISOU 1008  CB  TYR A 144    24585  13414  11098   -461   6176   1273       C  
ATOM   1009  CG  TYR A 144      11.081  39.721 -17.542  1.00137.03           C  
ANISOU 1009  CG  TYR A 144    26345  14013  11706   -358   7110   1378       C  
ATOM   1010  CD1 TYR A 144      11.031  38.491 -18.245  1.00139.43           C  
ANISOU 1010  CD1 TYR A 144    27213  14185  11579   -157   7312   1240       C  
ATOM   1011  CD2 TYR A 144      11.886  40.745 -18.075  1.00142.47           C  
ANISOU 1011  CD2 TYR A 144    27256  14429  12448   -455   7824   1621       C  
ATOM   1012  CE1 TYR A 144      11.761  38.297 -19.424  1.00146.43           C  
ANISOU 1012  CE1 TYR A 144    28893  14675  12067    -38   8233   1329       C  
ATOM   1013  CE2 TYR A 144      12.614  40.566 -19.268  1.00149.13           C  
ANISOU 1013  CE2 TYR A 144    28864  14880  12920   -349   8773   1735       C  
ATOM   1014  CZ  TYR A 144      12.553  39.349 -19.926  1.00151.63           C  
ANISOU 1014  CZ  TYR A 144    29758  15069  12785   -132   8992   1584       C  
ATOM   1015  OH  TYR A 144      13.295  39.210 -21.082  1.00159.08           O  
ANISOU 1015  OH  TYR A 144    31509  15591  13344    -11  10006   1698       O  
ATOM   1016  N   GLY A 145      12.736  38.016 -15.474  1.00131.43           N  
ANISOU 1016  N   GLY A 145    23481  13786  12671   -437   7449   1265       N  
ATOM   1017  CA  GLY A 145      13.348  36.693 -15.478  1.00132.57           C  
ANISOU 1017  CA  GLY A 145    23388  13922  13059   -303   7839   1175       C  
ATOM   1018  C   GLY A 145      13.386  36.157 -14.047  1.00127.08           C  
ANISOU 1018  C   GLY A 145    21644  13588  13054   -390   7296   1080       C  
ATOM   1019  O   GLY A 145      12.831  35.090 -13.727  1.00124.20           O  
ANISOU 1019  O   GLY A 145    21220  13391  12580   -285   6860    894       O  
ATOM   1020  N   GLN A 146      14.008  36.925 -13.165  1.00125.70           N  
ANISOU 1020  N   GLN A 146    20683  13508  13570   -596   7274   1214       N  
ATOM   1021  CA  GLN A 146      14.226  36.474 -11.802  1.00121.42           C  
ANISOU 1021  CA  GLN A 146    19191  13242  13700   -693   6820   1155       C  
ATOM   1022  C   GLN A 146      12.913  36.451 -11.038  1.00115.36           C  
ANISOU 1022  C   GLN A 146    18428  12779  12626   -708   5867    986       C  
ATOM   1023  O   GLN A 146      12.729  35.633 -10.142  1.00112.06           O  
ANISOU 1023  O   GLN A 146    17532  12585  12461   -699   5446    870       O  
ATOM   1024  CB  GLN A 146      15.222  37.380 -11.086  1.00122.50           C  
ANISOU 1024  CB  GLN A 146    18576  13340  14630   -926   6975   1348       C  
ATOM   1025  CG  GLN A 146      16.499  37.702 -11.857  1.00129.27           C  
ANISOU 1025  CG  GLN A 146    19379  13850  15887   -951   7958   1576       C  
ATOM   1026  CD  GLN A 146      17.219  38.896 -11.281  1.00130.91           C  
ANISOU 1026  CD  GLN A 146    19003  13976  16759  -1221   7979   1782       C  
ATOM   1027  OE1 GLN A 146      17.064  40.027 -11.753  1.00132.89           O  
ANISOU 1027  OE1 GLN A 146    19657  14085  16751  -1316   8108   1900       O  
ATOM   1028  NE2 GLN A 146      17.997  38.658 -10.236  1.00130.48           N  
ANISOU 1028  NE2 GLN A 146    18016  13988  17573  -1354   7789   1831       N  
ATOM   1029  N   ALA A 147      12.002  37.351 -11.394  1.00114.46           N  
ANISOU 1029  N   ALA A 147    18852  12647  11992   -726   5552    988       N  
ATOM   1030  CA  ALA A 147      10.718  37.488 -10.693  1.00109.44           C  
ANISOU 1030  CA  ALA A 147    18194  12257  11130   -734   4706    858       C  
ATOM   1031  C   ALA A 147       9.820  36.276 -10.856  1.00107.71           C  
ANISOU 1031  C   ALA A 147    18241  12142  10543   -565   4334    677       C  
ATOM   1032  O   ALA A 147       9.124  35.908  -9.904  1.00103.73           O  
ANISOU 1032  O   ALA A 147    17358  11885  10169   -581   3749    572       O  
ATOM   1033  CB  ALA A 147       9.980  38.716 -11.149  1.00109.78           C  
ANISOU 1033  CB  ALA A 147    18758  12200  10752   -764   4495    920       C  
ATOM   1034  N   ILE A 148       9.810  35.667 -12.044  1.00111.14           N  
ANISOU 1034  N   ILE A 148    19360  12358  10509   -410   4666    643       N  
ATOM   1035  CA  ILE A 148       9.071  34.410 -12.222  1.00110.07           C  
ANISOU 1035  CA  ILE A 148    19474  12274  10075   -262   4318    468       C  
ATOM   1036  C   ILE A 148       9.786  33.205 -11.585  1.00109.05           C  
ANISOU 1036  C   ILE A 148    18743  12260  10431   -232   4496    401       C  
ATOM   1037  O   ILE A 148       9.128  32.276 -11.111  1.00106.21           O  
ANISOU 1037  O   ILE A 148    18229  12059  10065   -183   4019    267       O  
ATOM   1038  CB  ILE A 148       8.736  34.084 -13.706  1.00114.60           C  
ANISOU 1038  CB  ILE A 148    21101  12531   9912    -98   4511    427       C  
ATOM   1039  CG1 ILE A 148       9.989  34.013 -14.568  1.00120.24           C  
ANISOU 1039  CG1 ILE A 148    22124  12955  10608    -34   5478    522       C  
ATOM   1040  CG2 ILE A 148       7.789  35.126 -14.298  1.00114.95           C  
ANISOU 1040  CG2 ILE A 148    21783  12454   9440   -112   4123    479       C  
ATOM   1041  CD1 ILE A 148       9.967  32.829 -15.527  1.00124.18           C  
ANISOU 1041  CD1 ILE A 148    23336  13217  10629    171   5723    393       C  
ATOM   1042  N   LEU A 149      11.121  33.220 -11.574  1.00111.75           N  
ANISOU 1042  N   LEU A 149    18725  12497  11237   -263   5172    511       N  
ATOM   1043  CA  LEU A 149      11.894  32.125 -10.967  1.00111.33           C  
ANISOU 1043  CA  LEU A 149    18055  12515  11731   -228   5345    473       C  
ATOM   1044  C   LEU A 149      11.725  32.116  -9.435  1.00106.66           C  
ANISOU 1044  C   LEU A 149    16644  12237  11644   -375   4735    456       C  
ATOM   1045  O   LEU A 149      11.555  31.053  -8.819  1.00104.77           O  
ANISOU 1045  O   LEU A 149    16099  12139  11571   -328   4439    354       O  
ATOM   1046  CB  LEU A 149      13.388  32.215 -11.334  1.00115.98           C  
ANISOU 1046  CB  LEU A 149    18389  12871  12808   -223   6229    628       C  
ATOM   1047  CG  LEU A 149      14.249  31.098 -10.741  1.00115.39           C  
ANISOU 1047  CG  LEU A 149    17639  12822  13381   -169   6412    610       C  
ATOM   1048  CD1 LEU A 149      13.852  29.802 -11.366  1.00115.36           C  
ANISOU 1048  CD1 LEU A 149    18143  12737  12953     54   6464    437       C  
ATOM   1049  CD2 LEU A 149      15.724  31.365 -10.909  1.00119.56           C  
ANISOU 1049  CD2 LEU A 149    17712  13121  14595   -198   7215    805       C  
ATOM   1050  N   THR A 150      11.771  33.286  -8.809  1.00105.23           N  
ANISOU 1050  N   THR A 150    16162  12138  11682   -550   4546    556       N  
ATOM   1051  CA  THR A 150      11.596  33.323  -7.367  1.00101.43           C  
ANISOU 1051  CA  THR A 150    15041  11907  11591   -681   3982    533       C  
ATOM   1052  C   THR A 150      10.144  32.981  -7.002  1.00 97.61           C  
ANISOU 1052  C   THR A 150    14770  11626  10692   -627   3323    388       C  
ATOM   1053  O   THR A 150       9.894  32.424  -5.939  1.00 94.95           O  
ANISOU 1053  O   THR A 150    14017  11481  10580   -662   2919    330       O  
ATOM   1054  CB  THR A 150      11.939  34.675  -6.760  1.00101.12           C  
ANISOU 1054  CB  THR A 150    14707  11870  11844   -879   3897    655       C  
ATOM   1055  OG1 THR A 150      10.814  35.543  -6.901  1.00 99.68           O  
ANISOU 1055  OG1 THR A 150    14957  11742  11176   -885   3546    620       O  
ATOM   1056  CG2 THR A 150      13.171  35.285  -7.426  1.00105.72           C  
ANISOU 1056  CG2 THR A 150    15225  12189  12754   -943   4587    832       C  
ATOM   1057  N   GLU A 151       9.193  33.341  -7.865  1.00 97.97           N  
ANISOU 1057  N   GLU A 151    15457  11601  10166   -547   3208    350       N  
ATOM   1058  CA  GLU A 151       7.791  32.965  -7.666  1.00 95.07           C  
ANISOU 1058  CA  GLU A 151    15274  11369   9480   -485   2606    236       C  
ATOM   1059  C   GLU A 151       7.536  31.489  -7.930  1.00 95.02           C  
ANISOU 1059  C   GLU A 151    15382  11360   9362   -358   2528    118       C  
ATOM   1060  O   GLU A 151       6.615  30.896  -7.372  1.00 92.73           O  
ANISOU 1060  O   GLU A 151    14962  11217   9054   -343   2036     39       O  
ATOM   1061  CB  GLU A 151       6.882  33.809  -8.545  1.00 96.20           C  
ANISOU 1061  CB  GLU A 151    16048  11385   9118   -440   2444    252       C  
ATOM   1062  CG  GLU A 151       6.575  35.200  -7.943  1.00 95.38           C  
ANISOU 1062  CG  GLU A 151    15775  11349   9116   -554   2236    329       C  
ATOM   1063  CD  GLU A 151       5.500  35.202  -6.842  1.00 92.08           C  
ANISOU 1063  CD  GLU A 151    15022  11149   8814   -570   1653    267       C  
ATOM   1064  OE1 GLU A 151       5.632  36.059  -5.930  1.00 91.73           O  
ANISOU 1064  OE1 GLU A 151    14645  11190   9016   -676   1575    309       O  
ATOM   1065  OE2 GLU A 151       4.528  34.390  -6.910  1.00 89.96           O  
ANISOU 1065  OE2 GLU A 151    14851  10931   8397   -478   1296    184       O  
ATOM   1066  N   ALA A 152       8.336  30.893  -8.788  1.00 98.22           N  
ANISOU 1066  N   ALA A 152    16046  11570   9703   -263   3038    112       N  
ATOM   1067  CA  ALA A 152       8.230  29.470  -9.016  1.00 98.65           C  
ANISOU 1067  CA  ALA A 152    16212  11586   9684   -139   3004     -6       C  
ATOM   1068  C   ALA A 152       8.835  28.734  -7.823  1.00 96.45           C  
ANISOU 1068  C   ALA A 152    15172  11484   9991   -192   2951     -6       C  
ATOM   1069  O   ALA A 152       8.197  27.850  -7.241  1.00 94.04           O  
ANISOU 1069  O   ALA A 152    14698  11311   9723   -177   2525    -89       O  
ATOM   1070  CB  ALA A 152       8.927  29.083 -10.334  1.00103.48           C  
ANISOU 1070  CB  ALA A 152    17417  11886  10015      7   3637    -20       C  
ATOM   1071  N   ILE A 153      10.055  29.112  -7.447  1.00 97.52           N  
ANISOU 1071  N   ILE A 153    14847  11596  10610   -264   3352    105       N  
ATOM   1072  CA  ILE A 153      10.741  28.464  -6.326  1.00 96.10           C  
ANISOU 1072  CA  ILE A 153    13959  11533  11022   -320   3262    128       C  
ATOM   1073  C   ILE A 153       9.924  28.601  -5.082  1.00 91.60           C  
ANISOU 1073  C   ILE A 153    13081  11218  10506   -435   2613    106       C  
ATOM   1074  O   ILE A 153       9.962  27.757  -4.238  1.00 89.82           O  
ANISOU 1074  O   ILE A 153    12497  11098  10534   -446   2363     79       O  
ATOM   1075  CB  ILE A 153      12.144  29.062  -6.078  1.00 98.62           C  
ANISOU 1075  CB  ILE A 153    13791  11751  11930   -415   3695    282       C  
ATOM   1076  CG1 ILE A 153      13.104  28.616  -7.187  1.00103.29           C  
ANISOU 1076  CG1 ILE A 153    14569  12062  12614   -268   4456    317       C  
ATOM   1077  CG2 ILE A 153      12.672  28.659  -4.683  1.00 96.60           C  
ANISOU 1077  CG2 ILE A 153    12801  11625  12279   -523   3359    324       C  
ATOM   1078  CD1 ILE A 153      14.445  29.282  -7.123  1.00106.46           C  
ANISOU 1078  CD1 ILE A 153    14496  12309  13646   -360   4957    500       C  
ATOM   1079  N   GLY A 154       9.184  29.690  -4.994  1.00 90.40           N  
ANISOU 1079  N   GLY A 154    13107  11137  10105   -511   2378    125       N  
ATOM   1080  CA  GLY A 154       8.303  29.974  -3.862  1.00 86.87           C  
ANISOU 1080  CA  GLY A 154    12448  10898   9662   -598   1839    106       C  
ATOM   1081  C   GLY A 154       7.137  29.033  -3.816  1.00 84.96           C  
ANISOU 1081  C   GLY A 154    12361  10742   9177   -513   1471      7       C  
ATOM   1082  O   GLY A 154       6.948  28.367  -2.805  1.00 83.15           O  
ANISOU 1082  O   GLY A 154    11800  10646   9147   -547   1200     -9       O  
ATOM   1083  N   THR A 155       6.386  28.960  -4.924  1.00 85.96           N  
ANISOU 1083  N   THR A 155    13014  10759   8888   -412   1449    -48       N  
ATOM   1084  CA  THR A 155       5.141  28.171  -4.999  1.00 84.55           C  
ANISOU 1084  CA  THR A 155    13004  10613   8506   -348   1028   -127       C  
ATOM   1085  C   THR A 155       5.424  26.660  -5.116  1.00 85.30           C  
ANISOU 1085  C   THR A 155    13069  10660   8682   -273   1065   -202       C  
ATOM   1086  O   THR A 155       4.535  25.793  -4.939  1.00 83.97           O  
ANISOU 1086  O   THR A 155    12909  10522   8473   -250    701   -256       O  
ATOM   1087  CB  THR A 155       4.252  28.656  -6.166  1.00 86.05           C  
ANISOU 1087  CB  THR A 155    13798  10647   8250   -278    889   -149       C  
ATOM   1088  OG1 THR A 155       4.417  30.070  -6.352  1.00 86.27           O  
ANISOU 1088  OG1 THR A 155    13940  10645   8195   -326   1034    -70       O  
ATOM   1089  CG2 THR A 155       2.785  28.369  -5.860  1.00 84.24           C  
ANISOU 1089  CG2 THR A 155    13543  10482   7984   -272    328   -174       C  
ATOM   1090  N   PHE A 156       6.680  26.352  -5.424  1.00 87.56           N  
ANISOU 1090  N   PHE A 156    13297  10840   9130   -234   1527   -192       N  
ATOM   1091  CA  PHE A 156       7.143  24.977  -5.457  1.00 88.46           C  
ANISOU 1091  CA  PHE A 156    13327  10886   9397   -149   1630   -254       C  
ATOM   1092  C   PHE A 156       7.170  24.393  -4.084  1.00 85.61           C  
ANISOU 1092  C   PHE A 156    12395  10710   9424   -229   1343   -225       C  
ATOM   1093  O   PHE A 156       6.718  23.276  -3.903  1.00 85.10           O  
ANISOU 1093  O   PHE A 156    12319  10649   9366   -188   1110   -285       O  
ATOM   1094  CB  PHE A 156       8.540  24.904  -6.069  1.00 92.16           C  
ANISOU 1094  CB  PHE A 156    13803  11171  10042    -73   2265   -226       C  
ATOM   1095  CG  PHE A 156       9.227  23.587  -5.845  1.00 93.40           C  
ANISOU 1095  CG  PHE A 156    13706  11261  10519     15   2406   -264       C  
ATOM   1096  CD1 PHE A 156       8.985  22.495  -6.703  1.00 95.09           C  
ANISOU 1096  CD1 PHE A 156    14383  11288  10458    172   2481   -389       C  
ATOM   1097  CD2 PHE A 156      10.123  23.443  -4.794  1.00 92.76           C  
ANISOU 1097  CD2 PHE A 156    12963  11267  11016    -56   2430   -174       C  
ATOM   1098  CE1 PHE A 156       9.623  21.284  -6.504  1.00 96.62           C  
ANISOU 1098  CE1 PHE A 156    14353  11396  10964    269   2624   -426       C  
ATOM   1099  CE2 PHE A 156      10.759  22.234  -4.582  1.00 94.46           C  
ANISOU 1099  CE2 PHE A 156    12928  11396  11566     36   2532   -196       C  
ATOM   1100  CZ  PHE A 156      10.511  21.145  -5.432  1.00 96.34           C  
ANISOU 1100  CZ  PHE A 156    13601  11460  11542    206   2653   -323       C  
ATOM   1101  N   LEU A 157       7.731  25.145  -3.133  1.00 84.30           N  
ANISOU 1101  N   LEU A 157    11802  10662   9566   -348   1348   -129       N  
ATOM   1102  CA  LEU A 157       7.772  24.726  -1.738  1.00 82.06           C  
ANISOU 1102  CA  LEU A 157    11058  10527   9594   -438   1041    -88       C  
ATOM   1103  C   LEU A 157       6.363  24.657  -1.160  1.00 79.38           C  
ANISOU 1103  C   LEU A 157    10784  10330   9046   -475    606   -110       C  
ATOM   1104  O   LEU A 157       6.050  23.721  -0.462  1.00 78.32           O  
ANISOU 1104  O   LEU A 157    10481  10254   9023   -485    376   -113       O  
ATOM   1105  CB  LEU A 157       8.642  25.648  -0.883  1.00 82.01           C  
ANISOU 1105  CB  LEU A 157    10685  10563   9912   -569   1075     15       C  
ATOM   1106  CG  LEU A 157       8.700  25.214   0.586  1.00 80.37           C  
ANISOU 1106  CG  LEU A 157    10115  10464   9956   -663    713     60       C  
ATOM   1107  CD1 LEU A 157       9.402  23.901   0.706  1.00 81.37           C  
ANISOU 1107  CD1 LEU A 157    10014  10512  10390   -598    748     62       C  
ATOM   1108  CD2 LEU A 157       9.387  26.207   1.421  1.00 80.76           C  
ANISOU 1108  CD2 LEU A 157     9920  10518  10246   -806    633    147       C  
ATOM   1109  N   LEU A 158       5.516  25.641  -1.439  1.00 78.62           N  
ANISOU 1109  N   LEU A 158    10915  10268   8691   -493    511   -109       N  
ATOM   1110  CA  LEU A 158       4.126  25.558  -1.012  1.00 76.98           C  
ANISOU 1110  CA  LEU A 158    10735  10150   8363   -504    152   -115       C  
ATOM   1111  C   LEU A 158       3.488  24.234  -1.456  1.00 77.47           C  
ANISOU 1111  C   LEU A 158    10922  10143   8368   -434    -26   -175       C  
ATOM   1112  O   LEU A 158       3.087  23.419  -0.630  1.00 76.34           O  
ANISOU 1112  O   LEU A 158    10554  10071   8382   -467   -228   -154       O  
ATOM   1113  CB  LEU A 158       3.312  26.749  -1.539  1.00 77.00           C  
ANISOU 1113  CB  LEU A 158    10996  10134   8128   -494     89   -106       C  
ATOM   1114  CG  LEU A 158       1.780  26.712  -1.314  1.00 76.06           C  
ANISOU 1114  CG  LEU A 158    10889  10052   7960   -479   -261    -95       C  
ATOM   1115  CD1 LEU A 158       1.381  26.204   0.104  1.00 73.92           C  
ANISOU 1115  CD1 LEU A 158    10254   9918   7915   -538   -402    -48       C  
ATOM   1116  CD2 LEU A 158       1.149  28.122  -1.634  1.00 75.55           C  
ANISOU 1116  CD2 LEU A 158    10996   9959   7750   -467   -306    -63       C  
ATOM   1117  N   MET A 159       3.403  24.015  -2.766  1.00 79.73           N  
ANISOU 1117  N   MET A 159    11619  10262   8414   -344     42   -246       N  
ATOM   1118  CA  MET A 159       2.684  22.839  -3.290  1.00 80.78           C  
ANISOU 1118  CA  MET A 159    11959  10276   8457   -287   -206   -315       C  
ATOM   1119  C   MET A 159       3.231  21.521  -2.719  1.00 80.59           C  
ANISOU 1119  C   MET A 159    11683  10259   8678   -280   -181   -332       C  
ATOM   1120  O   MET A 159       2.481  20.581  -2.423  1.00 79.81           O  
ANISOU 1120  O   MET A 159    11516  10148   8659   -298   -479   -338       O  
ATOM   1121  CB  MET A 159       2.708  22.803  -4.823  1.00 83.44           C  
ANISOU 1121  CB  MET A 159    12899  10372   8430   -184   -117   -403       C  
ATOM   1122  CG  MET A 159       1.701  21.835  -5.404  1.00 84.40           C  
ANISOU 1122  CG  MET A 159    13318  10332   8419   -151   -523   -472       C  
ATOM   1123  SD  MET A 159       0.038  22.302  -4.989  1.00 83.09           S  
ANISOU 1123  SD  MET A 159    12981  10234   8358   -235  -1075   -391       S  
ATOM   1124  CE  MET A 159      -0.836  20.741  -5.247  1.00 83.83           C  
ANISOU 1124  CE  MET A 159    13171  10145   8536   -242  -1537   -445       C  
ATOM   1125  N   LEU A 160       4.549  21.487  -2.565  1.00 81.38           N  
ANISOU 1125  N   LEU A 160    11622  10354   8946   -258    169   -322       N  
ATOM   1126  CA  LEU A 160       5.247  20.341  -1.997  1.00 81.65           C  
ANISOU 1126  CA  LEU A 160    11382  10370   9269   -239    210   -320       C  
ATOM   1127  C   LEU A 160       4.735  19.994  -0.616  1.00 79.15           C  
ANISOU 1127  C   LEU A 160    10701  10216   9158   -346   -110   -240       C  
ATOM   1128  O   LEU A 160       4.605  18.843  -0.299  1.00 79.36           O  
ANISOU 1128  O   LEU A 160    10644  10203   9308   -335   -259   -246       O  
ATOM   1129  CB  LEU A 160       6.767  20.609  -1.948  1.00 83.09           C  
ANISOU 1129  CB  LEU A 160    11346  10510   9715   -211    617   -283       C  
ATOM   1130  CG  LEU A 160       7.627  19.373  -1.754  1.00 84.04           C  
ANISOU 1130  CG  LEU A 160    11258  10522  10150   -134    727   -294       C  
ATOM   1131  CD1 LEU A 160       7.391  18.466  -2.966  1.00 85.88           C  
ANISOU 1131  CD1 LEU A 160    11958  10539  10133     18    848   -426       C  
ATOM   1132  CD2 LEU A 160       9.089  19.745  -1.588  1.00 84.96           C  
ANISOU 1132  CD2 LEU A 160    11040  10582  10661   -122   1085   -218       C  
ATOM   1133  N   VAL A 161       4.440  21.004   0.181  1.00 77.64           N  
ANISOU 1133  N   VAL A 161    10347  10178   8974   -443   -191   -163       N  
ATOM   1134  CA  VAL A 161       3.849  20.798   1.488  1.00 76.37           C  
ANISOU 1134  CA  VAL A 161     9947  10143   8929   -536   -436    -80       C  
ATOM   1135  C   VAL A 161       2.415  20.328   1.330  1.00 76.31           C  
ANISOU 1135  C   VAL A 161    10040  10121   8832   -537   -684    -83       C  
ATOM   1136  O   VAL A 161       1.999  19.342   1.996  1.00 76.42           O  
ANISOU 1136  O   VAL A 161     9915  10136   8983   -573   -850    -37       O  
ATOM   1137  CB  VAL A 161       3.890  22.069   2.359  1.00 75.34           C  
ANISOU 1137  CB  VAL A 161     9704  10135   8787   -623   -423    -11       C  
ATOM   1138  CG1 VAL A 161       2.861  22.017   3.490  1.00 74.53           C  
ANISOU 1138  CG1 VAL A 161     9513  10125   8678   -688   -618     63       C  
ATOM   1139  CG2 VAL A 161       5.301  22.226   2.938  1.00 76.60           C  
ANISOU 1139  CG2 VAL A 161     9655  10283   9168   -668   -323     30       C  
ATOM   1140  N   ILE A 162       1.678  20.990   0.425  1.00 76.63           N  
ANISOU 1140  N   ILE A 162    10319  10116   8681   -503   -728   -122       N  
ATOM   1141  CA  ILE A 162       0.278  20.626   0.130  1.00 76.76           C  
ANISOU 1141  CA  ILE A 162    10404  10068   8692   -508  -1025   -111       C  
ATOM   1142  C   ILE A 162       0.149  19.135  -0.269  1.00 78.21           C  
ANISOU 1142  C   ILE A 162    10667  10105   8943   -487  -1194   -160       C  
ATOM   1143  O   ILE A 162      -0.871  18.473   0.039  1.00 78.77           O  
ANISOU 1143  O   ILE A 162    10618  10137   9174   -540  -1459   -104       O  
ATOM   1144  CB  ILE A 162      -0.332  21.542  -0.968  1.00 77.46           C  
ANISOU 1144  CB  ILE A 162    10795  10068   8568   -462  -1108   -149       C  
ATOM   1145  CG1 ILE A 162      -0.389  22.980  -0.446  1.00 75.71           C  
ANISOU 1145  CG1 ILE A 162    10467   9977   8323   -486   -978    -88       C  
ATOM   1146  CG2 ILE A 162      -1.704  21.037  -1.367  1.00 78.19           C  
ANISOU 1146  CG2 ILE A 162    10936  10033   8740   -472  -1499   -129       C  
ATOM   1147  CD1 ILE A 162      -0.733  23.951  -1.425  1.00 75.79           C  
ANISOU 1147  CD1 ILE A 162    10767   9899   8130   -438  -1018   -111       C  
ATOM   1148  N   MET A 163       1.166  18.600  -0.948  1.00 79.30           N  
ANISOU 1148  N   MET A 163    11002  10134   8995   -408  -1021   -257       N  
ATOM   1149  CA  MET A 163       1.187  17.168  -1.282  1.00 80.78           C  
ANISOU 1149  CA  MET A 163    11297  10155   9241   -372  -1147   -319       C  
ATOM   1150  C   MET A 163       1.422  16.350  -0.039  1.00 79.47           C  
ANISOU 1150  C   MET A 163    10760  10076   9360   -434  -1179   -231       C  
ATOM   1151  O   MET A 163       0.740  15.355   0.204  1.00 79.65           O  
ANISOU 1151  O   MET A 163    10726  10023   9516   -478  -1425   -202       O  
ATOM   1152  CB  MET A 163       2.304  16.873  -2.297  1.00 82.98           C  
ANISOU 1152  CB  MET A 163    11899  10268   9363   -238   -852   -444       C  
ATOM   1153  CG  MET A 163       2.122  17.537  -3.679  1.00 84.83           C  
ANISOU 1153  CG  MET A 163    12661  10346   9223   -162   -797   -537       C  
ATOM   1154  SD  MET A 163       0.624  17.002  -4.523  1.00 86.06           S  
ANISOU 1154  SD  MET A 163    13217  10280   9203   -185  -1352   -594       S  
ATOM   1155  CE  MET A 163       0.911  15.201  -4.433  1.00 88.51           C  
ANISOU 1155  CE  MET A 163    13542  10416   9671   -148  -1433   -668       C  
ATOM   1156  N   GLY A 164       2.403  16.814   0.731  1.00 78.40           N  
ANISOU 1156  N   GLY A 164    10396  10071   9323   -445   -954   -179       N  
ATOM   1157  CA  GLY A 164       2.964  16.078   1.838  1.00 78.16           C  
ANISOU 1157  CA  GLY A 164    10087  10079   9530   -485   -976    -99       C  
ATOM   1158  C   GLY A 164       2.135  16.052   3.091  1.00 77.00           C  
ANISOU 1158  C   GLY A 164     9743  10048   9467   -604  -1152     36       C  
ATOM   1159  O   GLY A 164       2.227  15.088   3.860  1.00 77.64           O  
ANISOU 1159  O   GLY A 164     9697  10097   9705   -641  -1257    107       O  
ATOM   1160  N   VAL A 165       1.325  17.069   3.317  1.00 75.87           N  
ANISOU 1160  N   VAL A 165     9592  10010   9223   -653  -1158     81       N  
ATOM   1161  CA  VAL A 165       0.566  17.092   4.551  1.00 75.56           C  
ANISOU 1161  CA  VAL A 165     9398  10054   9258   -745  -1220    217       C  
ATOM   1162  C   VAL A 165      -0.934  17.137   4.342  1.00 76.06           C  
ANISOU 1162  C   VAL A 165     9437  10086   9378   -773  -1337    266       C  
ATOM   1163  O   VAL A 165      -1.677  17.163   5.315  1.00 76.21           O  
ANISOU 1163  O   VAL A 165     9321  10144   9491   -836  -1309    394       O  
ATOM   1164  CB  VAL A 165       1.016  18.267   5.429  1.00 74.92           C  
ANISOU 1164  CB  VAL A 165     9284  10101   9081   -780  -1082    264       C  
ATOM   1165  CG1 VAL A 165       0.216  19.571   5.094  1.00 74.63           C  
ANISOU 1165  CG1 VAL A 165     9311  10124   8920   -766  -1007    251       C  
ATOM   1166  CG2 VAL A 165       0.915  17.906   6.905  1.00 74.57           C  
ANISOU 1166  CG2 VAL A 165     9174  10083   9075   -860  -1111    396       C  
ATOM   1167  N   ALA A 166      -1.376  17.129   3.085  1.00 77.00           N  
ANISOU 1167  N   ALA A 166     9701  10099   9457   -725  -1469    176       N  
ATOM   1168  CA  ALA A 166      -2.802  17.307   2.748  1.00 78.03           C  
ANISOU 1168  CA  ALA A 166     9778  10159   9712   -752  -1658    230       C  
ATOM   1169  C   ALA A 166      -3.269  16.294   1.726  1.00 80.05           C  
ANISOU 1169  C   ALA A 166    10173  10200  10042   -750  -1970    168       C  
ATOM   1170  O   ALA A 166      -4.274  15.634   1.975  1.00 82.00           O  
ANISOU 1170  O   ALA A 166    10241  10349  10566   -826  -2171    269       O  
ATOM   1171  CB  ALA A 166      -3.081  18.683   2.243  1.00 77.49           C  
ANISOU 1171  CB  ALA A 166     9799  10134   9508   -704  -1611    201       C  
ATOM   1172  N   VAL A 167      -2.564  16.141   0.604  1.00 80.54           N  
ANISOU 1172  N   VAL A 167    10573  10157   9874   -669  -1999     13       N  
ATOM   1173  CA  VAL A 167      -2.996  15.152  -0.418  1.00 82.92           C  
ANISOU 1173  CA  VAL A 167    11128  10199  10178   -662  -2331    -70       C  
ATOM   1174  C   VAL A 167      -2.661  13.665  -0.064  1.00 83.68           C  
ANISOU 1174  C   VAL A 167    11172  10194  10427   -688  -2388    -73       C  
ATOM   1175  O   VAL A 167      -3.508  12.756  -0.267  1.00 85.32           O  
ANISOU 1175  O   VAL A 167    11376  10211  10832   -758  -2728    -45       O  
ATOM   1176  CB  VAL A 167      -2.431  15.470  -1.838  1.00 84.23           C  
ANISOU 1176  CB  VAL A 167    11810  10220   9972   -547  -2319   -245       C  
ATOM   1177  CG1 VAL A 167      -3.159  14.591  -2.898  1.00 86.85           C  
ANISOU 1177  CG1 VAL A 167    12498  10231  10268   -554  -2769   -327       C  
ATOM   1178  CG2 VAL A 167      -2.549  16.933  -2.170  1.00 82.68           C  
ANISOU 1178  CG2 VAL A 167    11701  10116   9596   -515  -2222   -237       C  
ATOM   1179  N   ASP A 168      -1.438  13.451   0.468  1.00 82.43           N  
ANISOU 1179  N   ASP A 168    10959  10139  10223   -636  -2088    -95       N  
ATOM   1180  CA  ASP A 168      -0.923  12.112   0.810  1.00 82.83           C  
ANISOU 1180  CA  ASP A 168    10971  10086  10414   -632  -2111    -99       C  
ATOM   1181  C   ASP A 168      -1.699  11.410   1.955  1.00 82.30           C  
ANISOU 1181  C   ASP A 168    10584  10037  10649   -769  -2256     81       C  
ATOM   1182  O   ASP A 168      -1.736  11.850   3.115  1.00 80.61           O  
ANISOU 1182  O   ASP A 168    10115  10002  10511   -830  -2103    222       O  
ATOM   1183  CB  ASP A 168       0.552  12.193   1.177  1.00 81.99           C  
ANISOU 1183  CB  ASP A 168    10811  10071  10270   -544  -1786   -130       C  
ATOM   1184  CG  ASP A 168       1.247  10.845   1.139  1.00 83.96           C  
ANISOU 1184  CG  ASP A 168    11109  10146  10645   -481  -1799   -179       C  
ATOM   1185  OD1 ASP A 168       2.374  10.796   0.621  1.00 85.91           O  
ANISOU 1185  OD1 ASP A 168    11478  10326  10838   -345  -1555   -284       O  
ATOM   1186  OD2 ASP A 168       0.711   9.837   1.633  1.00 84.76           O  
ANISOU 1186  OD2 ASP A 168    11113  10158  10932   -558  -2019   -103       O  
ATOM   1187  N   GLU A 169      -2.268  10.275   1.595  1.00 83.46           N  
ANISOU 1187  N   GLU A 169    10803   9960  10947   -813  -2541     72       N  
ATOM   1188  CA  GLU A 169      -3.001   9.397   2.508  1.00 83.83           C  
ANISOU 1188  CA  GLU A 169    10587   9952  11313   -949  -2679    246       C  
ATOM   1189  C   GLU A 169      -2.352   9.150   3.855  1.00 82.85           C  
ANISOU 1189  C   GLU A 169    10264   9967  11250   -974  -2451    377       C  
ATOM   1190  O   GLU A 169      -3.054   8.896   4.840  1.00 83.91           O  
ANISOU 1190  O   GLU A 169    10178  10120  11583  -1093  -2441    568       O  
ATOM   1191  CB  GLU A 169      -3.171   8.054   1.817  1.00 84.06           C  
ANISOU 1191  CB  GLU A 169    10812   9678  11446   -960  -2989    167       C  
ATOM   1192  CG  GLU A 169      -3.463   8.187   0.287  1.00 91.13           C  
ANISOU 1192  CG  GLU A 169    12110  10364  12150   -898  -3253    -22       C  
ATOM   1193  CD  GLU A 169      -4.531   9.297  -0.054  1.00 95.07           C  
ANISOU 1193  CD  GLU A 169    12531  10913  12679   -957  -3412     33       C  
ATOM   1194  OE1 GLU A 169      -4.135  10.519  -0.104  1.00 94.24           O  
ANISOU 1194  OE1 GLU A 169    12447  11015  12346   -879  -3152      2       O  
ATOM   1195  OE2 GLU A 169      -5.742   8.919  -0.259  1.00 97.55           O  
ANISOU 1195  OE2 GLU A 169    12739  11031  13294  -1084  -3814    118       O  
ATOM   1196  N   ARG A 170      -1.008   9.210   3.878  1.00 82.42           N  
ANISOU 1196  N   ARG A 170    10303   9973  11041   -860  -2271    285       N  
ATOM   1197  CA  ARG A 170      -0.207   8.961   5.089  1.00 81.39           C  
ANISOU 1197  CA  ARG A 170    10033   9927  10963   -873  -2146    399       C  
ATOM   1198  C   ARG A 170       0.037  10.216   5.916  1.00 80.26           C  
ANISOU 1198  C   ARG A 170     9793  10016  10687   -894  -1943    474       C  
ATOM   1199  O   ARG A 170       0.742  10.148   6.909  1.00 80.64           O  
ANISOU 1199  O   ARG A 170     9789  10113  10738   -909  -1894    564       O  
ATOM   1200  CB  ARG A 170       1.123   8.244   4.764  1.00 80.20           C  
ANISOU 1200  CB  ARG A 170     9969   9660  10842   -743  -2114    291       C  
ATOM   1201  CG  ARG A 170       0.984   6.689   4.651  1.00 83.27           C  
ANISOU 1201  CG  ARG A 170    10423   9798  11420   -748  -2321    295       C  
ATOM   1202  CD  ARG A 170       1.959   5.828   5.502  1.00 84.39           C  
ANISOU 1202  CD  ARG A 170    10471   9865  11728   -713  -2334    380       C  
ATOM   1203  NE  ARG A 170       3.211   5.565   4.781  1.00 88.60           N  
ANISOU 1203  NE  ARG A 170    11075  10281  12307   -522  -2212    223       N  
ATOM   1204  CZ  ARG A 170       4.463   5.758   5.250  1.00 91.16           C  
ANISOU 1204  CZ  ARG A 170    11244  10641  12752   -435  -2095    252       C  
ATOM   1205  NH1 ARG A 170       4.694   6.173   6.506  1.00 90.79           N  
ANISOU 1205  NH1 ARG A 170    11028  10732  12736   -531  -2157    426       N  
ATOM   1206  NH2 ARG A 170       5.517   5.492   4.460  1.00 93.14           N  
ANISOU 1206  NH2 ARG A 170    11525  10745  13121   -244  -1919    114       N  
ATOM   1207  N   ALA A 171      -0.589  11.335   5.555  1.00 80.28           N  
ANISOU 1207  N   ALA A 171     9799  10126  10577   -901  -1867    448       N  
ATOM   1208  CA  ALA A 171      -0.377  12.595   6.292  1.00 79.47           C  
ANISOU 1208  CA  ALA A 171     9652  10216  10329   -914  -1675    500       C  
ATOM   1209  C   ALA A 171      -1.123  12.651   7.642  1.00 79.93           C  
ANISOU 1209  C   ALA A 171     9623  10322  10423  -1020  -1599    697       C  
ATOM   1210  O   ALA A 171      -2.310  12.325   7.722  1.00 81.04           O  
ANISOU 1210  O   ALA A 171     9667  10398  10726  -1086  -1621    796       O  
ATOM   1211  CB  ALA A 171      -0.756  13.822   5.428  1.00 78.85           C  
ANISOU 1211  CB  ALA A 171     9632  10213  10115   -869  -1605    405       C  
ATOM   1212  N   PRO A 172      -0.424  13.102   8.700  1.00 79.75           N  
ANISOU 1212  N   PRO A 172     9659  10382  10260  -1036  -1501    760       N  
ATOM   1213  CA  PRO A 172      -0.986  13.147  10.041  1.00 80.46           C  
ANISOU 1213  CA  PRO A 172     9799  10480  10293  -1119  -1383    941       C  
ATOM   1214  C   PRO A 172      -2.154  14.114  10.084  1.00 80.48           C  
ANISOU 1214  C   PRO A 172     9752  10547  10279  -1127  -1174    984       C  
ATOM   1215  O   PRO A 172      -1.988  15.293   9.785  1.00 79.21           O  
ANISOU 1215  O   PRO A 172     9629  10489   9979  -1075  -1090    892       O  
ATOM   1216  CB  PRO A 172       0.166  13.669  10.889  1.00 80.34           C  
ANISOU 1216  CB  PRO A 172     9942  10511  10072  -1117  -1399    946       C  
ATOM   1217  CG  PRO A 172       0.989  14.475   9.966  1.00 79.03           C  
ANISOU 1217  CG  PRO A 172     9727  10421   9878  -1041  -1417    777       C  
ATOM   1218  CD  PRO A 172       0.862  13.829   8.617  1.00 79.00           C  
ANISOU 1218  CD  PRO A 172     9617  10359  10041   -978  -1481    663       C  
ATOM   1219  N   PRO A 173      -3.337  13.621  10.458  1.00 82.11           N  
ANISOU 1219  N   PRO A 173     9850  10670  10678  -1188  -1074   1136       N  
ATOM   1220  CA  PRO A 173      -4.560  14.381  10.282  1.00 82.90           C  
ANISOU 1220  CA  PRO A 173     9798  10781  10919  -1177   -894   1186       C  
ATOM   1221  C   PRO A 173      -4.648  15.552  11.249  1.00 83.14           C  
ANISOU 1221  C   PRO A 173     9986  10892  10711  -1146   -574   1236       C  
ATOM   1222  O   PRO A 173      -4.273  15.403  12.431  1.00 84.36           O  
ANISOU 1222  O   PRO A 173    10379  11025  10650  -1181   -441   1331       O  
ATOM   1223  CB  PRO A 173      -5.682  13.357  10.569  1.00 85.16           C  
ANISOU 1223  CB  PRO A 173     9884  10908  11564  -1267   -854   1376       C  
ATOM   1224  CG  PRO A 173      -5.015  12.126  10.987  1.00 85.79           C  
ANISOU 1224  CG  PRO A 173    10077  10908  11610  -1326   -995   1422       C  
ATOM   1225  CD  PRO A 173      -3.585  12.464  11.307  1.00 84.05           C  
ANISOU 1225  CD  PRO A 173    10117  10790  11029  -1274  -1061   1310       C  
ATOM   1226  N   GLY A 174      -5.158  16.688  10.734  1.00 82.37           N  
ANISOU 1226  N   GLY A 174     9804  10853  10640  -1077   -476   1173       N  
ATOM   1227  CA  GLY A 174      -5.395  17.892  11.522  1.00 82.32           C  
ANISOU 1227  CA  GLY A 174     9948  10890  10439  -1026   -154   1203       C  
ATOM   1228  C   GLY A 174      -4.298  18.891  11.437  1.00 79.86           C  
ANISOU 1228  C   GLY A 174     9869  10687   9787   -984   -227   1046       C  
ATOM   1229  O   GLY A 174      -4.543  20.012  11.760  1.00 79.93           O  
ANISOU 1229  O   GLY A 174     9988  10719   9663   -929    -20   1030       O  
ATOM   1230  N   PHE A 175      -3.099  18.481  11.022  1.00 78.18           N  
ANISOU 1230  N   PHE A 175     9716  10513   9477  -1008   -501    940       N  
ATOM   1231  CA  PHE A 175      -1.943  19.392  10.951  1.00 76.99           C  
ANISOU 1231  CA  PHE A 175     9733  10435   9085   -989   -580    814       C  
ATOM   1232  C   PHE A 175      -1.979  20.245   9.701  1.00 76.10           C  
ANISOU 1232  C   PHE A 175     9517  10381   9015   -923   -614    684       C  
ATOM   1233  O   PHE A 175      -1.400  21.346   9.678  1.00 75.35           O  
ANISOU 1233  O   PHE A 175     9545  10333   8749   -904   -580    606       O  
ATOM   1234  CB  PHE A 175      -0.606  18.648  11.033  1.00 76.39           C  
ANISOU 1234  CB  PHE A 175     9704  10340   8981  -1031   -824    780       C  
ATOM   1235  CG  PHE A 175      -0.249  18.232  12.422  1.00 77.45           C  
ANISOU 1235  CG  PHE A 175    10071  10399   8957  -1097   -853    896       C  
ATOM   1236  CD1 PHE A 175       0.436  19.085  13.245  1.00 77.58           C  
ANISOU 1236  CD1 PHE A 175    10360  10399   8718  -1124   -889    885       C  
ATOM   1237  CD2 PHE A 175      -0.635  17.002  12.931  1.00 78.84           C  
ANISOU 1237  CD2 PHE A 175    10245  10488   9222  -1141   -869   1027       C  
ATOM   1238  CE1 PHE A 175       0.744  18.719  14.550  1.00 79.05           C  
ANISOU 1238  CE1 PHE A 175    10865  10471   8698  -1187   -971    996       C  
ATOM   1239  CE2 PHE A 175      -0.309  16.632  14.229  1.00 79.71           C  
ANISOU 1239  CE2 PHE A 175    10654  10498   9132  -1202   -908   1149       C  
ATOM   1240  CZ  PHE A 175       0.376  17.492  15.033  1.00 79.70           C  
ANISOU 1240  CZ  PHE A 175    10974  10472   8838  -1222   -972   1131       C  
ATOM   1241  N   ALA A 176      -2.674  19.735   8.677  1.00 76.64           N  
ANISOU 1241  N   ALA A 176     9398  10416   9304   -898   -708    669       N  
ATOM   1242  CA  ALA A 176      -2.870  20.440   7.364  1.00 76.34           C  
ANISOU 1242  CA  ALA A 176     9328  10388   9289   -833   -787    560       C  
ATOM   1243  C   ALA A 176      -2.934  21.996   7.365  1.00 76.06           C  
ANISOU 1243  C   ALA A 176     9389  10407   9105   -781   -641    519       C  
ATOM   1244  O   ALA A 176      -2.092  22.702   6.733  1.00 74.95           O  
ANISOU 1244  O   ALA A 176     9363  10302   8813   -760   -671    412       O  
ATOM   1245  CB  ALA A 176      -4.162  19.907   6.682  1.00 77.50           C  
ANISOU 1245  CB  ALA A 176     9288  10434   9724   -825   -912    614       C  
ATOM   1246  N   GLY A 177      -3.995  22.508   8.010  1.00 77.10           N  
ANISOU 1246  N   GLY A 177     9461  10514   9319   -753   -455    614       N  
ATOM   1247  CA  GLY A 177      -4.292  23.945   7.978  1.00 76.84           C  
ANISOU 1247  CA  GLY A 177     9504  10493   9198   -682   -312    584       C  
ATOM   1248  C   GLY A 177      -3.138  24.729   8.518  1.00 75.69           C  
ANISOU 1248  C   GLY A 177     9610  10402   8747   -708   -253    509       C  
ATOM   1249  O   GLY A 177      -2.594  25.574   7.822  1.00 74.59           O  
ANISOU 1249  O   GLY A 177     9550  10285   8504   -690   -308    416       O  
ATOM   1250  N   LEU A 178      -2.744  24.367   9.738  1.00 76.19           N  
ANISOU 1250  N   LEU A 178     9813  10457   8678   -765   -176    562       N  
ATOM   1251  CA  LEU A 178      -1.662  25.012  10.463  1.00 76.05           C  
ANISOU 1251  CA  LEU A 178    10061  10439   8395   -815   -200    512       C  
ATOM   1252  C   LEU A 178      -0.353  24.928   9.686  1.00 74.57           C  
ANISOU 1252  C   LEU A 178     9820  10289   8223   -865   -426    422       C  
ATOM   1253  O   LEU A 178       0.273  25.949   9.433  1.00 74.62           O  
ANISOU 1253  O   LEU A 178     9915  10296   8143   -874   -441    353       O  
ATOM   1254  CB  LEU A 178      -1.471  24.368  11.843  1.00 77.60           C  
ANISOU 1254  CB  LEU A 178    10463  10576   8445   -877   -173    602       C  
ATOM   1255  CG  LEU A 178      -0.540  25.113  12.803  1.00 78.68           C  
ANISOU 1255  CG  LEU A 178    10962  10648   8284   -935   -253    567       C  
ATOM   1256  CD1 LEU A 178      -1.172  26.470  13.163  1.00 79.76           C  
ANISOU 1256  CD1 LEU A 178    11327  10733   8246   -862     -2    533       C  
ATOM   1257  CD2 LEU A 178      -0.250  24.243  14.061  1.00 80.17           C  
ANISOU 1257  CD2 LEU A 178    11408  10742   8309  -1007   -328    666       C  
ATOM   1258  N   VAL A 179       0.058  23.738   9.287  1.00 73.85           N  
ANISOU 1258  N   VAL A 179     9581  10205   8274   -891   -567    430       N  
ATOM   1259  CA  VAL A 179       1.317  23.620   8.562  1.00 73.51           C  
ANISOU 1259  CA  VAL A 179     9469  10164   8299   -913   -696    357       C  
ATOM   1260  C   VAL A 179       1.345  24.389   7.245  1.00 73.19           C  
ANISOU 1260  C   VAL A 179     9406  10140   8263   -857   -630    270       C  
ATOM   1261  O   VAL A 179       2.297  25.117   7.004  1.00 73.49           O  
ANISOU 1261  O   VAL A 179     9475  10164   8282   -884   -616    227       O  
ATOM   1262  CB  VAL A 179       1.671  22.170   8.184  1.00 73.76           C  
ANISOU 1262  CB  VAL A 179     9354  10169   8504   -912   -813    366       C  
ATOM   1263  CG1 VAL A 179       2.961  22.185   7.293  1.00 73.26           C  
ANISOU 1263  CG1 VAL A 179     9207  10077   8551   -899   -836    288       C  
ATOM   1264  CG2 VAL A 179       1.815  21.253   9.431  1.00 74.67           C  
ANISOU 1264  CG2 VAL A 179     9507  10240   8625   -975   -919    468       C  
ATOM   1265  N   ILE A 180       0.331  24.201   6.395  1.00 73.22           N  
ANISOU 1265  N   ILE A 180     9369  10140   8310   -789   -615    258       N  
ATOM   1266  CA  ILE A 180       0.268  24.864   5.080  1.00 73.29           C  
ANISOU 1266  CA  ILE A 180     9447  10127   8273   -730   -594    186       C  
ATOM   1267  C   ILE A 180       0.330  26.402   5.195  1.00 73.39           C  
ANISOU 1267  C   ILE A 180     9576  10149   8159   -727   -489    171       C  
ATOM   1268  O   ILE A 180       0.965  27.104   4.389  1.00 73.64           O  
ANISOU 1268  O   ILE A 180     9701  10154   8124   -721   -435    121       O  
ATOM   1269  CB  ILE A 180      -1.041  24.480   4.284  1.00 74.00           C  
ANISOU 1269  CB  ILE A 180     9510  10164   8441   -667   -701    197       C  
ATOM   1270  CG1 ILE A 180      -0.941  23.050   3.726  1.00 75.20           C  
ANISOU 1270  CG1 ILE A 180     9629  10256   8687   -667   -841    174       C  
ATOM   1271  CG2 ILE A 180      -1.271  25.436   3.121  1.00 73.39           C  
ANISOU 1271  CG2 ILE A 180     9592  10034   8258   -606   -718    145       C  
ATOM   1272  CD1 ILE A 180      -2.143  22.589   2.922  1.00 76.08           C  
ANISOU 1272  CD1 ILE A 180     9737  10265   8905   -633  -1046    184       C  
ATOM   1273  N   GLY A 181      -0.360  26.934   6.192  1.00 73.63           N  
ANISOU 1273  N   GLY A 181     9631  10192   8155   -724   -426    220       N  
ATOM   1274  CA  GLY A 181      -0.403  28.372   6.381  1.00 73.69           C  
ANISOU 1274  CA  GLY A 181     9779  10178   8043   -709   -329    200       C  
ATOM   1275  C   GLY A 181       0.953  28.857   6.816  1.00 73.78           C  
ANISOU 1275  C   GLY A 181     9879  10175   7977   -805   -348    169       C  
ATOM   1276  O   GLY A 181       1.528  29.731   6.161  1.00 73.61           O  
ANISOU 1276  O   GLY A 181     9919  10122   7927   -820   -318    131       O  
ATOM   1277  N   LEU A 182       1.470  28.265   7.911  1.00 74.03           N  
ANISOU 1277  N   LEU A 182     9921  10203   8004   -879   -426    203       N  
ATOM   1278  CA  LEU A 182       2.772  28.653   8.480  1.00 74.46           C  
ANISOU 1278  CA  LEU A 182    10039  10199   8054   -991   -546    194       C  
ATOM   1279  C   LEU A 182       3.876  28.583   7.417  1.00 74.66           C  
ANISOU 1279  C   LEU A 182     9891  10210   8267  -1022   -555    170       C  
ATOM   1280  O   LEU A 182       4.814  29.413   7.415  1.00 75.65           O  
ANISOU 1280  O   LEU A 182    10024  10262   8457  -1103   -587    164       O  
ATOM   1281  CB  LEU A 182       3.130  27.782   9.683  1.00 75.01           C  
ANISOU 1281  CB  LEU A 182    10154  10234   8111  -1059   -706    250       C  
ATOM   1282  CG  LEU A 182       2.402  28.065  10.991  1.00 75.51           C  
ANISOU 1282  CG  LEU A 182    10517  10245   7926  -1054   -662    283       C  
ATOM   1283  CD1 LEU A 182       2.754  26.983  12.068  1.00 75.90           C  
ANISOU 1283  CD1 LEU A 182    10662  10240   7935  -1120   -837    359       C  
ATOM   1284  CD2 LEU A 182       2.725  29.478  11.454  1.00 75.78           C  
ANISOU 1284  CD2 LEU A 182    10823  10180   7791  -1096   -687    233       C  
ATOM   1285  N   THR A 183       3.758  27.602   6.517  1.00 74.01           N  
ANISOU 1285  N   THR A 183     9669  10165   8285   -958   -507    161       N  
ATOM   1286  CA  THR A 183       4.717  27.445   5.443  1.00 74.57           C  
ANISOU 1286  CA  THR A 183     9630  10193   8510   -952   -414    137       C  
ATOM   1287  C   THR A 183       4.706  28.657   4.562  1.00 74.85           C  
ANISOU 1287  C   THR A 183     9792  10196   8454   -935   -258    109       C  
ATOM   1288  O   THR A 183       5.776  29.180   4.248  1.00 76.30           O  
ANISOU 1288  O   THR A 183     9913  10304   8773   -994   -166    123       O  
ATOM   1289  CB  THR A 183       4.405  26.235   4.572  1.00 74.62           C  
ANISOU 1289  CB  THR A 183     9589  10208   8555   -862   -373    111       C  
ATOM   1290  OG1 THR A 183       4.431  25.032   5.357  1.00 75.15           O  
ANISOU 1290  OG1 THR A 183     9537  10288   8728   -879   -518    147       O  
ATOM   1291  CG2 THR A 183       5.412  26.151   3.362  1.00 76.00           C  
ANISOU 1291  CG2 THR A 183     9737  10296   8842   -825   -170     79       C  
ATOM   1292  N   VAL A 184       3.512  29.087   4.146  1.00 74.03           N  
ANISOU 1292  N   VAL A 184     9842  10120   8164   -856   -233     88       N  
ATOM   1293  CA  VAL A 184       3.359  30.326   3.347  1.00 74.51           C  
ANISOU 1293  CA  VAL A 184    10075  10128   8106   -832   -122     73       C  
ATOM   1294  C   VAL A 184       4.026  31.498   4.066  1.00 74.99           C  
ANISOU 1294  C   VAL A 184    10164  10141   8189   -934   -119     90       C  
ATOM   1295  O   VAL A 184       4.843  32.222   3.504  1.00 75.30           O  
ANISOU 1295  O   VAL A 184    10227  10100   8285   -986     -3    102       O  
ATOM   1296  CB  VAL A 184       1.838  30.673   3.089  1.00 74.30           C  
ANISOU 1296  CB  VAL A 184    10173  10114   7944   -729   -181     69       C  
ATOM   1297  CG1 VAL A 184       1.666  32.109   2.627  1.00 73.44           C  
ANISOU 1297  CG1 VAL A 184    10249   9934   7722   -710   -116     69       C  
ATOM   1298  CG2 VAL A 184       1.188  29.666   2.089  1.00 74.00           C  
ANISOU 1298  CG2 VAL A 184    10161  10060   7895   -645   -258     53       C  
ATOM   1299  N   GLY A 185       3.655  31.635   5.338  1.00 75.20           N  
ANISOU 1299  N   GLY A 185    10217  10189   8167   -964   -241     95       N  
ATOM   1300  CA  GLY A 185       4.179  32.674   6.225  1.00 76.31           C  
ANISOU 1300  CA  GLY A 185    10466  10245   8282  -1065   -314     96       C  
ATOM   1301  C   GLY A 185       5.681  32.758   6.116  1.00 77.53           C  
ANISOU 1301  C   GLY A 185    10469  10314   8676  -1198   -362    127       C  
ATOM   1302  O   GLY A 185       6.266  33.865   5.957  1.00 78.60           O  
ANISOU 1302  O   GLY A 185    10657  10340   8867  -1282   -341    138       O  
ATOM   1303  N   GLY A 186       6.303  31.586   6.178  1.00 77.63           N  
ANISOU 1303  N   GLY A 186    10264  10348   8882  -1218   -421    155       N  
ATOM   1304  CA  GLY A 186       7.762  31.479   6.021  1.00 79.58           C  
ANISOU 1304  CA  GLY A 186    10263  10490   9486  -1325   -445    209       C  
ATOM   1305  C   GLY A 186       8.292  31.979   4.671  1.00 80.25           C  
ANISOU 1305  C   GLY A 186    10281  10513   9697  -1311   -137    227       C  
ATOM   1306  O   GLY A 186       9.280  32.712   4.616  1.00 81.88           O  
ANISOU 1306  O   GLY A 186    10367  10585  10159  -1428   -110    284       O  
ATOM   1307  N   ILE A 187       7.629  31.561   3.590  1.00 79.17           N  
ANISOU 1307  N   ILE A 187    10254  10444   9384  -1173     85    190       N  
ATOM   1308  CA  ILE A 187       8.043  31.925   2.234  1.00 80.28           C  
ANISOU 1308  CA  ILE A 187    10456  10500   9546  -1135    418    208       C  
ATOM   1309  C   ILE A 187       8.002  33.466   2.082  1.00 80.92           C  
ANISOU 1309  C   ILE A 187    10712  10502   9532  -1204    470    232       C  
ATOM   1310  O   ILE A 187       8.972  34.097   1.626  1.00 83.02           O  
ANISOU 1310  O   ILE A 187    10896  10632  10017  -1289    671    301       O  
ATOM   1311  CB  ILE A 187       7.141  31.206   1.158  1.00 79.33           C  
ANISOU 1311  CB  ILE A 187    10563  10430   9148   -972    543    148       C  
ATOM   1312  CG1 ILE A 187       7.261  29.695   1.288  1.00 79.40           C  
ANISOU 1312  CG1 ILE A 187    10411  10481   9276   -913    494    123       C  
ATOM   1313  CG2 ILE A 187       7.515  31.604  -0.250  1.00 80.65           C  
ANISOU 1313  CG2 ILE A 187    10940  10472   9231   -922    895    165       C  
ATOM   1314  CD1 ILE A 187       6.067  28.948   0.758  1.00 78.69           C  
ANISOU 1314  CD1 ILE A 187    10534  10447   8916   -790    411     58       C  
ATOM   1315  N   ILE A 188       6.882  34.067   2.495  1.00 79.29           N  
ANISOU 1315  N   ILE A 188    10726  10357   9042  -1165    308    186       N  
ATOM   1316  CA  ILE A 188       6.720  35.503   2.381  1.00 79.54           C  
ANISOU 1316  CA  ILE A 188    10954  10300   8967  -1208    336    199       C  
ATOM   1317  C   ILE A 188       7.874  36.189   3.087  1.00 81.34           C  
ANISOU 1317  C   ILE A 188    11026  10399   9481  -1392    252    251       C  
ATOM   1318  O   ILE A 188       8.472  37.060   2.527  1.00 82.89           O  
ANISOU 1318  O   ILE A 188    11244  10463   9788  -1469    411    310       O  
ATOM   1319  CB  ILE A 188       5.365  35.989   2.939  1.00 78.16           C  
ANISOU 1319  CB  ILE A 188    10989  10185   8525  -1121    174    144       C  
ATOM   1320  CG1 ILE A 188       4.217  35.461   2.063  1.00 76.69           C  
ANISOU 1320  CG1 ILE A 188    10925  10069   8146   -955    211    120       C  
ATOM   1321  CG2 ILE A 188       5.338  37.518   3.004  1.00 77.99           C  
ANISOU 1321  CG2 ILE A 188    11163  10036   8435  -1171    180    154       C  
ATOM   1322  CD1 ILE A 188       2.838  36.003   2.405  1.00 75.68           C  
ANISOU 1322  CD1 ILE A 188    10935   9956   7863   -848     99     96       C  
ATOM   1323  N   THR A 189       8.215  35.757   4.295  1.00 81.64           N  
ANISOU 1323  N   THR A 189    10919  10446   9656  -1473    -22    244       N  
ATOM   1324  CA  THR A 189       9.346  36.333   5.021  1.00 84.09           C  
ANISOU 1324  CA  THR A 189    11083  10588  10280  -1668   -219    299       C  
ATOM   1325  C   THR A 189      10.648  36.445   4.158  1.00 86.67           C  
ANISOU 1325  C   THR A 189    11101  10772  11057  -1766     21    411       C  
ATOM   1326  O   THR A 189      11.312  37.490   4.120  1.00 89.14           O  
ANISOU 1326  O   THR A 189    11377  10907  11583  -1912     21    477       O  
ATOM   1327  CB  THR A 189       9.583  35.572   6.351  1.00 84.25           C  
ANISOU 1327  CB  THR A 189    11020  10612  10378  -1729   -592    288       C  
ATOM   1328  OG1 THR A 189       8.445  35.787   7.195  1.00 82.94           O  
ANISOU 1328  OG1 THR A 189    11203  10512   9799  -1658   -729    204       O  
ATOM   1329  CG2 THR A 189      10.896  36.042   7.049  1.00 87.07           C  
ANISOU 1329  CG2 THR A 189    11193  10742  11148  -1952   -900    364       C  
ATOM   1330  N   THR A 190      11.002  35.394   3.443  1.00 86.77           N  
ANISOU 1330  N   THR A 190    10902  10833  11233  -1681    266    440       N  
ATOM   1331  CA  THR A 190      12.198  35.449   2.605  1.00 89.77           C  
ANISOU 1331  CA  THR A 190    10994  11055  12061  -1740    604    556       C  
ATOM   1332  C   THR A 190      11.933  36.139   1.247  1.00 90.52           C  
ANISOU 1332  C   THR A 190    11360  11105  11927  -1669   1060    578       C  
ATOM   1333  O   THR A 190      12.667  37.059   0.848  1.00 92.91           O  
ANISOU 1333  O   THR A 190    11593  11227  12483  -1788   1265    683       O  
ATOM   1334  CB  THR A 190      12.739  34.063   2.303  1.00 90.39           C  
ANISOU 1334  CB  THR A 190    10778  11154  12412  -1649    767    578       C  
ATOM   1335  OG1 THR A 190      12.887  33.318   3.510  1.00 90.71           O  
ANISOU 1335  OG1 THR A 190    10623  11232  12612  -1695    325    564       O  
ATOM   1336  CG2 THR A 190      14.074  34.182   1.620  1.00 94.30           C  
ANISOU 1336  CG2 THR A 190    10913  11437  13480  -1715   1147    719       C  
ATOM   1337  N   ILE A 191      10.886  35.685   0.544  1.00 88.52           N  
ANISOU 1337  N   ILE A 191    11435  10987  11210  -1485   1188    492       N  
ATOM   1338  CA  ILE A 191      10.615  36.091  -0.842  1.00 89.40           C  
ANISOU 1338  CA  ILE A 191    11889  11032  11047  -1391   1585    512       C  
ATOM   1339  C   ILE A 191       9.911  37.448  -0.973  1.00 89.17           C  
ANISOU 1339  C   ILE A 191    12202  10963  10715  -1419   1502    511       C  
ATOM   1340  O   ILE A 191       9.905  38.058  -2.057  1.00 90.60           O  
ANISOU 1340  O   ILE A 191    12675  11024  10724  -1388   1812    567       O  
ATOM   1341  CB  ILE A 191       9.778  35.015  -1.528  1.00 87.92           C  
ANISOU 1341  CB  ILE A 191    11949  10955  10502  -1195   1646    420       C  
ATOM   1342  CG1 ILE A 191      10.627  33.773  -1.731  1.00 90.14           C  
ANISOU 1342  CG1 ILE A 191    11959  11204  11085  -1147   1869    434       C  
ATOM   1343  CG2 ILE A 191       9.297  35.465  -2.873  1.00 89.39           C  
ANISOU 1343  CG2 ILE A 191    12621  11048  10295  -1094   1921    428       C  
ATOM   1344  CD1 ILE A 191      11.826  33.994  -2.671  1.00 94.81           C  
ANISOU 1344  CD1 ILE A 191    12477  11577  11968  -1166   2434    552       C  
ATOM   1345  N   GLY A 192       9.345  37.922   0.140  1.00 87.66           N  
ANISOU 1345  N   GLY A 192    12010  10842  10454  -1468   1104    453       N  
ATOM   1346  CA  GLY A 192       8.530  39.142   0.189  1.00 87.00           C  
ANISOU 1346  CA  GLY A 192    12243  10720  10092  -1461    983    431       C  
ATOM   1347  C   GLY A 192       9.169  40.338  -0.460  1.00 89.58           C  
ANISOU 1347  C   GLY A 192    12679  10840  10519  -1570   1218    538       C  
ATOM   1348  O   GLY A 192       8.566  40.981  -1.309  1.00 90.31           O  
ANISOU 1348  O   GLY A 192    13128  10873  10314  -1491   1344    555       O  
ATOM   1349  N   ASN A 193      10.395  40.652  -0.077  1.00 91.65           N  
ANISOU 1349  N   ASN A 193    12632  10959  11231  -1762   1256    628       N  
ATOM   1350  CA  ASN A 193      11.031  41.833  -0.624  1.00 94.32           C  
ANISOU 1350  CA  ASN A 193    13039  11070  11729  -1895   1482    752       C  
ATOM   1351  C   ASN A 193      11.688  41.582  -1.973  1.00 96.76           C  
ANISOU 1351  C   ASN A 193    13369  11268  12129  -1865   2048    875       C  
ATOM   1352  O   ASN A 193      12.481  42.408  -2.427  1.00100.14           O  
ANISOU 1352  O   ASN A 193    13756  11474  12816  -2002   2330   1019       O  
ATOM   1353  CB  ASN A 193      12.051  42.388   0.359  1.00 96.40           C  
ANISOU 1353  CB  ASN A 193    12961  11170  12497  -2139   1243    816       C  
ATOM   1354  CG  ASN A 193      12.213  43.874   0.231  1.00 98.50           C  
ANISOU 1354  CG  ASN A 193    13410  11214  12803  -2280   1252    890       C  
ATOM   1355  OD1 ASN A 193      11.588  44.624   0.972  1.00 98.86           O  
ANISOU 1355  OD1 ASN A 193    13688  11241  12632  -2295    905    801       O  
ATOM   1356  ND2 ASN A 193      13.039  44.320  -0.730  1.00101.67           N  
ANISOU 1356  ND2 ASN A 193    13736  11418  13476  -2375   1691   1060       N  
ATOM   1357  N   ILE A 194      11.374  40.466  -2.616  1.00 95.57           N  
ANISOU 1357  N   ILE A 194    13314  11235  11765  -1688   2238    824       N  
ATOM   1358  CA  ILE A 194      11.889  40.204  -3.953  1.00 98.57           C  
ANISOU 1358  CA  ILE A 194    13862  11479  12112  -1621   2821    920       C  
ATOM   1359  C   ILE A 194      10.779  40.320  -4.992  1.00 97.86           C  
ANISOU 1359  C   ILE A 194    14415  11399  11367  -1442   2884    868       C  
ATOM   1360  O   ILE A 194      10.999  40.876  -6.069  1.00100.93           O  
ANISOU 1360  O   ILE A 194    15171  11596  11583  -1432   3286    973       O  
ATOM   1361  CB  ILE A 194      12.581  38.822  -4.060  1.00 99.46           C  
ANISOU 1361  CB  ILE A 194    13653  11625  12511  -1551   3061    915       C  
ATOM   1362  CG1 ILE A 194      13.714  38.712  -3.029  1.00100.85           C  
ANISOU 1362  CG1 ILE A 194    13163  11748  13408  -1732   2924    991       C  
ATOM   1363  CG2 ILE A 194      13.148  38.615  -5.475  1.00103.11           C  
ANISOU 1363  CG2 ILE A 194    14372  11894  12912  -1462   3764   1014       C  
ATOM   1364  CD1 ILE A 194      14.166  37.269  -2.757  1.00100.54           C  
ANISOU 1364  CD1 ILE A 194    12756  11785  13660  -1648   2945    954       C  
ATOM   1365  N   THR A 195       9.604  39.770  -4.699  1.00 94.42           N  
ANISOU 1365  N   THR A 195    14128  11157  10590  -1305   2485    724       N  
ATOM   1366  CA  THR A 195       8.480  39.873  -5.631  1.00 94.06           C  
ANISOU 1366  CA  THR A 195    14659  11090   9988  -1144   2416    682       C  
ATOM   1367  C   THR A 195       7.153  40.135  -4.988  1.00 91.12           C  
ANISOU 1367  C   THR A 195    14351  10857   9414  -1074   1890    584       C  
ATOM   1368  O   THR A 195       6.138  40.165  -5.662  1.00 91.04           O  
ANISOU 1368  O   THR A 195    14742  10820   9029   -941   1730    556       O  
ATOM   1369  CB  THR A 195       8.304  38.591  -6.448  1.00 94.62           C  
ANISOU 1369  CB  THR A 195    14956  11177   9818   -986   2565    621       C  
ATOM   1370  OG1 THR A 195       7.719  37.564  -5.620  1.00 90.62           O  
ANISOU 1370  OG1 THR A 195    14164  10891   9376   -928   2186    495       O  
ATOM   1371  CG2 THR A 195       9.654  38.172  -7.059  1.00 97.61           C  
ANISOU 1371  CG2 THR A 195    15244  11400  10441  -1016   3182    713       C  
ATOM   1372  N   GLY A 196       7.149  40.320  -3.691  1.00 89.43           N  
ANISOU 1372  N   GLY A 196    13763  10758   9460  -1159   1620    540       N  
ATOM   1373  CA  GLY A 196       5.895  40.442  -2.962  1.00 87.33           C  
ANISOU 1373  CA  GLY A 196    13516  10616   9051  -1071   1205    447       C  
ATOM   1374  C   GLY A 196       5.292  39.096  -2.616  1.00 85.47           C  
ANISOU 1374  C   GLY A 196    13122  10565   8788   -966   1020    354       C  
ATOM   1375  O   GLY A 196       4.170  39.039  -2.104  1.00 84.08           O  
ANISOU 1375  O   GLY A 196    12944  10479   8525   -875    732    294       O  
ATOM   1376  N   SER A 197       6.035  38.022  -2.901  1.00 86.10           N  
ANISOU 1376  N   SER A 197    13060  10675   8980   -975   1214    353       N  
ATOM   1377  CA  SER A 197       5.644  36.640  -2.557  1.00 84.27           C  
ANISOU 1377  CA  SER A 197    12655  10595   8767   -897   1058    272       C  
ATOM   1378  C   SER A 197       4.140  36.351  -2.746  1.00 82.97           C  
ANISOU 1378  C   SER A 197    12686  10489   8350   -754    752    214       C  
ATOM   1379  O   SER A 197       3.402  36.173  -1.797  1.00 81.50           O  
ANISOU 1379  O   SER A 197    12308  10421   8239   -733    503    175       O  
ATOM   1380  CB  SER A 197       6.107  36.337  -1.134  1.00 82.82           C  
ANISOU 1380  CB  SER A 197    12048  10526   8896  -1000    909    253       C  
ATOM   1381  OG  SER A 197       6.225  34.951  -0.939  1.00 81.76           O  
ANISOU 1381  OG  SER A 197    11719  10489   8858   -958    876    211       O  
ATOM   1382  N   SER A 198       3.688  36.341  -3.987  1.00 84.35           N  
ANISOU 1