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***    ***

elNémo ID: 20112314435989170

Job options:

ID        	=	 20112314435989170
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


data_3HAP
# 
_entry.id   3HAP 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.287 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3HAP         
RCSB  RCSB052903   
WWPDB D_1000052903 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 3HAN . unspecified 
PDB 3HAO . unspecified 
PDB 3HAQ . unspecified 
PDB 3HAR . unspecified 
PDB 3HAS . unspecified 
# 
_pdbx_database_status.entry_id                        3HAP 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2009-05-02 
_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                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Joh, N.H.'   1 
'Yang, D.'    2 
'Bowie, J.U.' 3 
# 
_citation.id                        primary 
_citation.title                     
'Similar energetic contributions of packing in the core of membrane and water-soluble proteins.' 
_citation.journal_abbrev            J.Am.Chem.Soc. 
_citation.journal_volume            131 
_citation.page_first                10846 
_citation.page_last                 10847 
_citation.year                      2009 
_citation.journal_id_ASTM           JACSAT 
_citation.country                   US 
_citation.journal_id_ISSN           0002-7863 
_citation.journal_id_CSD            0004 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   19603754 
_citation.pdbx_database_id_DOI      10.1021/ja904711k 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Joh, N.H.'        1 
primary 'Oberai, A.'       2 
primary 'Yang, D.'         3 
primary 'Whitelegge, J.P.' 4 
primary 'Bowie, J.U.'      5 
# 
_cell.entry_id           3HAP 
_cell.length_a           44.951 
_cell.length_b           102.135 
_cell.length_c           128.027 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_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                         3HAP 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_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 Bacteriorhodopsin                                           26887.420 1   ? L111A ? ? 
2 non-polymer syn RETINAL                                                     284.436   1   ? ?     ? ? 
3 non-polymer syn DODECANE                                                    170.335   8   ? ?     ? ? 
4 non-polymer syn DECANE                                                      142.282   4   ? ?     ? ? 
5 non-polymer syn HEXADECANE                                                  226.441   1   ? ?     ? ? 
6 non-polymer syn '3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE' 614.877   1   ? ?     ? ? 
7 non-polymer syn HEPTANE                                                     100.202   1   ? ?     ? ? 
8 non-polymer syn nonane                                                      128.255   1   ? ?     ? ? 
9 water       nat water                                                       18.015    154 ? ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        BR 
# 
_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       
;QAQITGRPEWIWLALGTALMGLGTLYFLVKGMGVSDPDAKKFYAITTLVPAIAFTMYLSMLLGYGLTMVPFGGEQNPIYW
ARYADWLFTTPLLLLDLALLVDADQGTILAAVGADGIMIGTGLVGALTKVYSYRFVWWAISTAAMLYILYVLFFGFTSKA
ESMRPEVASTFKVLRNVTVVLWSAYPVVWLIGSEGAGIVPLNIETLLFMVLDVSAKVGFGLILLRSRAIFGEAEAPEPSA
GDGAAATSD
;
_entity_poly.pdbx_seq_one_letter_code_can   
;QAQITGRPEWIWLALGTALMGLGTLYFLVKGMGVSDPDAKKFYAITTLVPAIAFTMYLSMLLGYGLTMVPFGGEQNPIYW
ARYADWLFTTPLLLLDLALLVDADQGTILAAVGADGIMIGTGLVGALTKVYSYRFVWWAISTAAMLYILYVLFFGFTSKA
ESMRPEVASTFKVLRNVTVVLWSAYPVVWLIGSEGAGIVPLNIETLLFMVLDVSAKVGFGLILLRSRAIFGEAEAPEPSA
GDGAAATSD
;
_entity_poly.pdbx_strand_id                 A 
_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   GLN n 
1 2   ALA n 
1 3   GLN n 
1 4   ILE n 
1 5   THR n 
1 6   GLY n 
1 7   ARG n 
1 8   PRO n 
1 9   GLU n 
1 10  TRP n 
1 11  ILE n 
1 12  TRP n 
1 13  LEU n 
1 14  ALA n 
1 15  LEU n 
1 16  GLY n 
1 17  THR n 
1 18  ALA n 
1 19  LEU n 
1 20  MET n 
1 21  GLY n 
1 22  LEU n 
1 23  GLY n 
1 24  THR n 
1 25  LEU n 
1 26  TYR n 
1 27  PHE n 
1 28  LEU n 
1 29  VAL n 
1 30  LYS n 
1 31  GLY n 
1 32  MET n 
1 33  GLY n 
1 34  VAL n 
1 35  SER n 
1 36  ASP n 
1 37  PRO n 
1 38  ASP n 
1 39  ALA n 
1 40  LYS n 
1 41  LYS n 
1 42  PHE n 
1 43  TYR n 
1 44  ALA n 
1 45  ILE n 
1 46  THR n 
1 47  THR n 
1 48  LEU n 
1 49  VAL n 
1 50  PRO n 
1 51  ALA n 
1 52  ILE n 
1 53  ALA n 
1 54  PHE n 
1 55  THR n 
1 56  MET n 
1 57  TYR n 
1 58  LEU n 
1 59  SER n 
1 60  MET n 
1 61  LEU n 
1 62  LEU n 
1 63  GLY n 
1 64  TYR n 
1 65  GLY n 
1 66  LEU n 
1 67  THR n 
1 68  MET n 
1 69  VAL n 
1 70  PRO n 
1 71  PHE n 
1 72  GLY n 
1 73  GLY n 
1 74  GLU n 
1 75  GLN n 
1 76  ASN n 
1 77  PRO n 
1 78  ILE n 
1 79  TYR n 
1 80  TRP n 
1 81  ALA n 
1 82  ARG n 
1 83  TYR n 
1 84  ALA n 
1 85  ASP n 
1 86  TRP n 
1 87  LEU n 
1 88  PHE n 
1 89  THR n 
1 90  THR n 
1 91  PRO n 
1 92  LEU n 
1 93  LEU n 
1 94  LEU n 
1 95  LEU n 
1 96  ASP n 
1 97  LEU n 
1 98  ALA n 
1 99  LEU n 
1 100 LEU n 
1 101 VAL n 
1 102 ASP n 
1 103 ALA n 
1 104 ASP n 
1 105 GLN n 
1 106 GLY n 
1 107 THR n 
1 108 ILE n 
1 109 LEU n 
1 110 ALA n 
1 111 ALA n 
1 112 VAL n 
1 113 GLY n 
1 114 ALA n 
1 115 ASP n 
1 116 GLY n 
1 117 ILE n 
1 118 MET n 
1 119 ILE n 
1 120 GLY n 
1 121 THR n 
1 122 GLY n 
1 123 LEU n 
1 124 VAL n 
1 125 GLY n 
1 126 ALA n 
1 127 LEU n 
1 128 THR n 
1 129 LYS n 
1 130 VAL n 
1 131 TYR n 
1 132 SER n 
1 133 TYR n 
1 134 ARG n 
1 135 PHE n 
1 136 VAL n 
1 137 TRP n 
1 138 TRP n 
1 139 ALA n 
1 140 ILE n 
1 141 SER n 
1 142 THR n 
1 143 ALA n 
1 144 ALA n 
1 145 MET n 
1 146 LEU n 
1 147 TYR n 
1 148 ILE n 
1 149 LEU n 
1 150 TYR n 
1 151 VAL n 
1 152 LEU n 
1 153 PHE n 
1 154 PHE n 
1 155 GLY n 
1 156 PHE n 
1 157 THR n 
1 158 SER n 
1 159 LYS n 
1 160 ALA n 
1 161 GLU n 
1 162 SER n 
1 163 MET n 
1 164 ARG n 
1 165 PRO n 
1 166 GLU n 
1 167 VAL n 
1 168 ALA n 
1 169 SER n 
1 170 THR n 
1 171 PHE n 
1 172 LYS n 
1 173 VAL n 
1 174 LEU n 
1 175 ARG n 
1 176 ASN n 
1 177 VAL n 
1 178 THR n 
1 179 VAL n 
1 180 VAL n 
1 181 LEU n 
1 182 TRP n 
1 183 SER n 
1 184 ALA n 
1 185 TYR n 
1 186 PRO n 
1 187 VAL n 
1 188 VAL n 
1 189 TRP n 
1 190 LEU n 
1 191 ILE n 
1 192 GLY n 
1 193 SER n 
1 194 GLU n 
1 195 GLY n 
1 196 ALA n 
1 197 GLY n 
1 198 ILE n 
1 199 VAL n 
1 200 PRO n 
1 201 LEU n 
1 202 ASN n 
1 203 ILE n 
1 204 GLU n 
1 205 THR n 
1 206 LEU n 
1 207 LEU n 
1 208 PHE n 
1 209 MET n 
1 210 VAL n 
1 211 LEU n 
1 212 ASP n 
1 213 VAL n 
1 214 SER n 
1 215 ALA n 
1 216 LYS n 
1 217 VAL n 
1 218 GLY n 
1 219 PHE n 
1 220 GLY n 
1 221 LEU n 
1 222 ILE n 
1 223 LEU n 
1 224 LEU n 
1 225 ARG n 
1 226 SER n 
1 227 ARG n 
1 228 ALA n 
1 229 ILE n 
1 230 PHE n 
1 231 GLY n 
1 232 GLU n 
1 233 ALA n 
1 234 GLU n 
1 235 ALA n 
1 236 PRO n 
1 237 GLU n 
1 238 PRO n 
1 239 SER n 
1 240 ALA n 
1 241 GLY n 
1 242 ASP n 
1 243 GLY n 
1 244 ALA n 
1 245 ALA n 
1 246 ALA n 
1 247 THR n 
1 248 SER n 
1 249 ASP 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               'Halobacterium halobium' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'bop, VNG_1467G' 
_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      'Halobacterium salinarum' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2242 
_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      'Halobacterium salinarum' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     2242 
_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               L33 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    BACR_HALSA 
_struct_ref.pdbx_db_accession          P02945 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;QAQITGRPEWIWLALGTALMGLGTLYFLVKGMGVSDPDAKKFYAITTLVPAIAFTMYLSMLLGYGLTMVPFGGEQNPIYW
ARYADWLFTTPLLLLDLALLVDADQGTILALVGADGIMIGTGLVGALTKVYSYRFVWWAISTAAMLYILYVLFFGFTSKA
ESMRPEVASTFKVLRNVTVVLWSAYPVVWLIGSEGAGIVPLNIETLLFMVLDVSAKVGFGLILLRSRAIFGEAEAPEPSA
GDGAAATSD
;
_struct_ref.pdbx_align_begin           14 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              3HAP 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 249 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P02945 
_struct_ref_seq.db_align_beg                  14 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  262 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       249 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             3HAP 
_struct_ref_seq_dif.mon_id                       ALA 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      111 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   P02945 
_struct_ref_seq_dif.db_mon_id                    LEU 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          124 
_struct_ref_seq_dif.details                      ENGINEERED 
_struct_ref_seq_dif.pdbx_auth_seq_num            111 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
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 
CPS non-polymer         . '3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE' CHAPS 'C32 H58 N2 O7 S' 614.877 
D10 non-polymer         . DECANE                                                      ?     'C10 H22'         142.282 
D12 non-polymer         . DODECANE                                                    ?     'C12 H26'         170.335 
DD9 non-polymer         . nonane                                                      ?     'C9 H20'          128.255 
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  
HOH non-polymer         . WATER                                                       ?     'H2 O'            18.015  
HP6 non-polymer         . HEPTANE                                                     ?     'C7 H16'          100.202 
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 
R16 non-polymer         . HEXADECANE                                                  ?     'C16 H34'         226.441 
RET non-polymer         . RETINAL                                                     ?     'C20 H28 O'       284.436 
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.crystals_number   1 
_exptl.entry_id          3HAP 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.73 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_percent_sol   54.99 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'hanging drop, bicelle method' 
_exptl_crystal_grow.pH              4.0 
_exptl_crystal_grow.temp            310 
_exptl_crystal_grow.pdbx_details    
;400ul 4M NaPi, 30ul 6M 1,6-hexanediol, 35ul 100% triethylene glycol, 535 ul H2O, pH 4.0, hanging drop, bicelle method, temperature 310K
;
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 315' 
_diffrn_detector.pdbx_collection_date   2009-01-17 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9998 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.2.2' 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.9998 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.2.2 
# 
_reflns.entry_id                     3HAP 
_reflns.d_resolution_high            1.600 
_reflns.d_resolution_low             50.000 
_reflns.number_obs                   36787 
_reflns.pdbx_Rmerge_I_obs            0.050 
_reflns.pdbx_netI_over_sigmaI        22.431 
_reflns.pdbx_chi_squared             1.031 
_reflns.pdbx_redundancy              6.300 
_reflns.percent_possible_obs         93.900 
_reflns.observed_criterion_sigma_F   ? 
_reflns.observed_criterion_sigma_I   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
_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_scaling_rejects         ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             1.60 
_reflns_shell.d_res_low              1.66 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.Rmerge_I_obs           0.382 
_reflns_shell.meanI_over_sigI_obs    ? 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.pdbx_chi_squared       1.026 
_reflns_shell.pdbx_redundancy        4.10 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      3007 
_reflns_shell.percent_possible_all   78.40 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 3HAP 
_refine.ls_d_res_high                            1.600 
_refine.ls_d_res_low                             21.740 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    93.790 
_refine.ls_number_reflns_obs                     36725 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.169 
_refine.ls_R_factor_R_work                       0.167 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.192 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 7.800 
_refine.ls_number_reflns_R_free                  2871 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               19.588 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.000 
_refine.aniso_B[2][2]                            0.000 
_refine.aniso_B[3][3]                            0.000 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.961 
_refine.correlation_coeff_Fo_to_Fc_free          0.948 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       0.085 
_refine.pdbx_overall_ESU_R_Free                  0.084 
_refine.overall_SU_ML                            0.046 
_refine.overall_SU_B                             2.843 
_refine.solvent_model_details                    MASK 
_refine.pdbx_solvent_vdw_probe_radii             1.200 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD WITH PHASES' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                71.40 
_refine.B_iso_min                                8.99 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.20 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.overall_FOM_free_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_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1914 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         215 
_refine_hist.number_atoms_solvent             154 
_refine_hist.number_atoms_total               2283 
_refine_hist.d_res_high                       1.600 
_refine_hist.d_res_low                        21.740 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d         2202 0.010  0.022  ? 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg      2994 2.007  2.056  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg   289  3.822  5.000  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg   66   29.753 21.818 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg   346  12.296 15.000 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg   11   12.682 15.000 ? 'X-RAY DIFFRACTION' ? 
r_chiral_restr           350  0.177  0.200  ? 'X-RAY DIFFRACTION' ? 
r_gen_planes_refined     1506 0.006  0.020  ? 'X-RAY DIFFRACTION' ? 
r_nbd_refined            1109 0.208  0.200  ? 'X-RAY DIFFRACTION' ? 
r_nbtor_refined          1496 0.320  0.200  ? 'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined    138  0.123  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined   71   0.185  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined 8    0.149  0.200  ? 'X-RAY DIFFRACTION' ? 
r_mcbond_it              1255 0.605  1.500  ? 'X-RAY DIFFRACTION' ? 
r_mcangle_it             2008 0.938  2.000  ? 'X-RAY DIFFRACTION' ? 
r_scbond_it              1087 1.553  3.000  ? 'X-RAY DIFFRACTION' ? 
r_scangle_it             951  2.157  4.500  ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.d_res_high                       1.60 
_refine_ls_shell.d_res_low                        1.644 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               78.220 
_refine_ls_shell.number_reflns_R_work             2041 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.233 
_refine_ls_shell.R_factor_R_free                  0.291 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             178 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                2219 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3HAP 
_struct.title                     'Crystal structure of bacteriorhodopsin mutant L111A crystallized from bicelles' 
_struct.pdbx_descriptor           Bacteriorhodopsin 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3HAP 
_struct_keywords.text            
;bacteriorhodopsin, packing force, van der Waals, evolutionary constraint, membrane protein, integral membrane protein, helical membrane protein, proton transport, Cell membrane, Chromophore, Hydrogen ion transport, Ion transport, Membrane, Photoreceptor protein, Pyrrolidone carboxylic acid, Receptor, Retinal protein, Sensory transduction, Transmembrane, Transport, TRANSPORT PROTEIN
;
_struct_keywords.pdbx_keywords   'TRANSPORT PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 4 ? 
H N N 5 ? 
I N N 6 ? 
J N N 4 ? 
K N N 3 ? 
L N N 7 ? 
M N N 3 ? 
N N N 8 ? 
O N N 3 ? 
P N N 3 ? 
Q N N 3 ? 
R N N 4 ? 
S N N 9 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 GLU A 9   ? VAL A 34  ? GLU A 9   VAL A 34  1 ? 26 
HELX_P HELX_P2 2 ASP A 36  ? LEU A 62  ? ASP A 36  LEU A 62  1 ? 27 
HELX_P HELX_P3 3 TRP A 80  ? ASP A 102 ? TRP A 80  ASP A 102 1 ? 23 
HELX_P HELX_P4 4 ASP A 104 ? THR A 128 ? ASP A 104 THR A 128 1 ? 25 
HELX_P HELX_P5 5 VAL A 130 ? PHE A 154 ? VAL A 130 PHE A 154 1 ? 25 
HELX_P HELX_P6 6 PHE A 154 ? GLU A 161 ? PHE A 154 GLU A 161 1 ? 8  
HELX_P HELX_P7 7 ARG A 164 ? GLY A 192 ? ARG A 164 GLY A 192 1 ? 29 
HELX_P HELX_P8 8 PRO A 200 ? ARG A 225 ? PRO A 200 ARG A 225 1 ? 26 
HELX_P HELX_P9 9 SER A 226 ? PHE A 230 ? SER A 226 PHE A 230 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           LYS 
_struct_conn.ptnr1_label_seq_id            216 
_struct_conn.ptnr1_label_atom_id           NZ 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           RET 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           C15 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            LYS 
_struct_conn.ptnr1_auth_seq_id             216 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            RET 
_struct_conn.ptnr2_auth_seq_id             301 
_struct_conn.ptnr2_symmetry                1_555 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               1.269 
_struct_conn.pdbx_value_order              ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_struct_sheet.id               A 
_struct_sheet.type             ? 
_struct_sheet.number_strands   2 
_struct_sheet.details          ? 
# 
_struct_sheet_order.sheet_id     A 
_struct_sheet_order.range_id_1   1 
_struct_sheet_order.range_id_2   2 
_struct_sheet_order.offset       ? 
_struct_sheet_order.sense        anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 LEU A 66 ? PHE A 71 ? LEU A 66 PHE A 71 
A 2 GLU A 74 ? TYR A 79 ? GLU A 74 TYR A 79 
# 
_pdbx_struct_sheet_hbond.sheet_id                A 
_pdbx_struct_sheet_hbond.range_id_1              1 
_pdbx_struct_sheet_hbond.range_id_2              2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id   N 
_pdbx_struct_sheet_hbond.range_1_label_comp_id   THR 
_pdbx_struct_sheet_hbond.range_1_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_1_label_seq_id    67 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id    N 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id    THR 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id     67 
_pdbx_struct_sheet_hbond.range_2_label_atom_id   O 
_pdbx_struct_sheet_hbond.range_2_label_comp_id   ILE 
_pdbx_struct_sheet_hbond.range_2_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_2_label_seq_id    78 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id    O 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id    ILE 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id     78 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 12 'BINDING SITE FOR RESIDUE RET A 301' 
AC2 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE D12 A 402' 
AC3 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE D12 A 403' 
AC4 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE D12 A 405' 
AC5 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE D10 A 406' 
AC6 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE R16 A 411' 
AC7 Software ? ? ? ? 9  'BINDING SITE FOR RESIDUE CPS A 501' 
AC8 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE D10 A 250' 
AC9 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE D12 A 251' 
BC1 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE D12 A 254' 
BC2 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE D12 A 255' 
BC3 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE D12 A 256' 
BC4 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE D10 A 257' 
# 
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 12 TRP A 86  ? TRP A 86  . ? 1_555 ? 
2  AC1 12 THR A 90  ? THR A 90  . ? 1_555 ? 
3  AC1 12 TRP A 138 ? TRP A 138 . ? 1_555 ? 
4  AC1 12 SER A 141 ? SER A 141 . ? 1_555 ? 
5  AC1 12 THR A 142 ? THR A 142 . ? 1_555 ? 
6  AC1 12 TRP A 182 ? TRP A 182 . ? 1_555 ? 
7  AC1 12 TYR A 185 ? TYR A 185 . ? 1_555 ? 
8  AC1 12 PRO A 186 ? PRO A 186 . ? 1_555 ? 
9  AC1 12 TRP A 189 ? TRP A 189 . ? 1_555 ? 
10 AC1 12 ASP A 212 ? ASP A 212 . ? 1_555 ? 
11 AC1 12 ALA A 215 ? ALA A 215 . ? 1_555 ? 
12 AC1 12 LYS A 216 ? LYS A 216 . ? 1_555 ? 
13 AC2 1  D12 D .   ? D12 A 403 . ? 4_555 ? 
14 AC3 1  D12 C .   ? D12 A 402 . ? 4_555 ? 
15 AC4 1  ASN A 176 ? ASN A 176 . ? 4_555 ? 
16 AC5 5  THR A 17  ? THR A 17  . ? 1_555 ? 
17 AC5 5  ALA A 44  ? ALA A 44  . ? 8_455 ? 
18 AC5 5  D12 K .   ? D12 A 251 . ? 1_555 ? 
19 AC5 5  D12 Q .   ? D12 A 256 . ? 8_455 ? 
20 AC5 5  CPS I .   ? CPS A 501 . ? 1_555 ? 
21 AC6 1  VAL A 136 ? VAL A 136 . ? 4_555 ? 
22 AC7 9  GLY A 6   ? GLY A 6   . ? 1_555 ? 
23 AC7 9  LYS A 41  ? LYS A 41  . ? 8_455 ? 
24 AC7 9  LEU A 61  ? LEU A 61  . ? 1_555 ? 
25 AC7 9  GLN A 105 ? GLN A 105 . ? 8_455 ? 
26 AC7 9  ILE A 108 ? ILE A 108 . ? 8_455 ? 
27 AC7 9  HOH S .   ? HOH A 298 . ? 8_455 ? 
28 AC7 9  HOH S .   ? HOH A 329 . ? 1_555 ? 
29 AC7 9  HOH S .   ? HOH A 351 . ? 1_555 ? 
30 AC7 9  D10 F .   ? D10 A 406 . ? 1_555 ? 
31 AC8 1  LEU A 25  ? LEU A 25  . ? 1_555 ? 
32 AC9 2  LEU A 15  ? LEU A 15  . ? 1_555 ? 
33 AC9 2  D10 F .   ? D10 A 406 . ? 1_555 ? 
34 BC1 1  HOH S .   ? HOH A 375 . ? 1_555 ? 
35 BC2 1  ALA A 110 ? ALA A 110 . ? 1_555 ? 
36 BC3 3  LEU A 28  ? LEU A 28  . ? 1_555 ? 
37 BC3 3  LEU A 48  ? LEU A 48  . ? 1_555 ? 
38 BC3 3  D10 F .   ? D10 A 406 . ? 8_555 ? 
39 BC4 1  ILE A 203 ? ILE A 203 . ? 1_555 ? 
# 
_atom_sites.entry_id                    3HAP 
_atom_sites.fract_transf_matrix[1][1]   0.022246 
_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]   0.009791 
_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]   0.007811 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLY A 1 6   ? 8.055  19.701 -18.547 1.00 29.81 ? 6   GLY A N   1 
ATOM   2    C CA  . GLY A 1 6   ? 7.290  18.523 -19.046 1.00 29.21 ? 6   GLY A CA  1 
ATOM   3    C C   . GLY A 1 6   ? 7.904  17.176 -18.698 1.00 28.38 ? 6   GLY A C   1 
ATOM   4    O O   . GLY A 1 6   ? 7.377  16.138 -19.105 1.00 29.49 ? 6   GLY A O   1 
ATOM   5    N N   . ARG A 1 7   ? 9.005  17.193 -17.942 1.00 27.33 ? 7   ARG A N   1 
ATOM   6    C CA  A ARG A 1 7   ? 9.706  15.965 -17.547 0.60 26.38 ? 7   ARG A CA  1 
ATOM   7    C CA  B ARG A 1 7   ? 9.713  15.972 -17.544 0.40 26.23 ? 7   ARG A CA  1 
ATOM   8    C C   . ARG A 1 7   ? 8.882  15.190 -16.519 1.00 25.47 ? 7   ARG A C   1 
ATOM   9    O O   . ARG A 1 7   ? 8.373  15.778 -15.576 1.00 25.28 ? 7   ARG A O   1 
ATOM   10   C CB  A ARG A 1 7   ? 11.088 16.299 -16.979 0.60 26.31 ? 7   ARG A CB  1 
ATOM   11   C CB  B ARG A 1 7   ? 11.087 16.336 -16.972 0.40 26.24 ? 7   ARG A CB  1 
ATOM   12   C CG  A ARG A 1 7   ? 12.023 17.009 -17.962 0.60 26.83 ? 7   ARG A CG  1 
ATOM   13   C CG  B ARG A 1 7   ? 11.956 17.158 -17.932 0.40 26.46 ? 7   ARG A CG  1 
ATOM   14   C CD  A ARG A 1 7   ? 13.468 17.004 -17.468 0.60 26.99 ? 7   ARG A CD  1 
ATOM   15   C CD  B ARG A 1 7   ? 12.918 18.090 -17.200 0.40 26.48 ? 7   ARG A CD  1 
ATOM   16   N NE  A ARG A 1 7   ? 14.049 15.659 -17.468 0.60 27.77 ? 7   ARG A NE  1 
ATOM   17   N NE  B ARG A 1 7   ? 13.428 19.129 -18.096 0.40 27.18 ? 7   ARG A NE  1 
ATOM   18   C CZ  A ARG A 1 7   ? 14.715 15.126 -18.488 0.60 29.35 ? 7   ARG A CZ  1 
ATOM   19   C CZ  B ARG A 1 7   ? 14.091 20.216 -17.708 0.40 26.67 ? 7   ARG A CZ  1 
ATOM   20   N NH1 A ARG A 1 7   ? 14.901 15.812 -19.612 0.60 28.94 ? 7   ARG A NH1 1 
ATOM   21   N NH1 B ARG A 1 7   ? 14.344 20.433 -16.423 0.40 26.52 ? 7   ARG A NH1 1 
ATOM   22   N NH2 A ARG A 1 7   ? 15.198 13.899 -18.386 0.60 30.34 ? 7   ARG A NH2 1 
ATOM   23   N NH2 B ARG A 1 7   ? 14.502 21.095 -18.612 0.40 27.16 ? 7   ARG A NH2 1 
ATOM   24   N N   . PRO A 1 8   ? 8.743  13.853 -16.703 1.00 24.28 ? 8   PRO A N   1 
ATOM   25   C CA  . PRO A 1 8   ? 7.810  13.114 -15.834 1.00 23.09 ? 8   PRO A CA  1 
ATOM   26   C C   . PRO A 1 8   ? 8.108  13.196 -14.336 1.00 22.22 ? 8   PRO A C   1 
ATOM   27   O O   . PRO A 1 8   ? 7.193  13.052 -13.520 1.00 22.59 ? 8   PRO A O   1 
ATOM   28   C CB  . PRO A 1 8   ? 7.931  11.660 -16.315 1.00 23.38 ? 8   PRO A CB  1 
ATOM   29   C CG  . PRO A 1 8   ? 9.176  11.596 -17.116 1.00 23.79 ? 8   PRO A CG  1 
ATOM   30   C CD  . PRO A 1 8   ? 9.392  12.965 -17.690 1.00 24.06 ? 8   PRO A CD  1 
ATOM   31   N N   . GLU A 1 9   ? 9.371  13.420 -13.988 1.00 20.27 ? 9   GLU A N   1 
ATOM   32   C CA  . GLU A 1 9   ? 9.765  13.539 -12.575 1.00 19.04 ? 9   GLU A CA  1 
ATOM   33   C C   . GLU A 1 9   ? 9.319  14.864 -11.930 1.00 18.62 ? 9   GLU A C   1 
ATOM   34   O O   . GLU A 1 9   ? 9.462  15.039 -10.717 1.00 18.50 ? 9   GLU A O   1 
ATOM   35   C CB  . GLU A 1 9   ? 11.282 13.368 -12.423 1.00 18.58 ? 9   GLU A CB  1 
ATOM   36   C CG  . GLU A 1 9   ? 12.130 14.493 -13.004 1.00 18.70 ? 9   GLU A CG  1 
ATOM   37   C CD  . GLU A 1 9   ? 12.482 14.299 -14.477 1.00 19.12 ? 9   GLU A CD  1 
ATOM   38   O OE1 . GLU A 1 9   ? 11.849 13.456 -15.153 1.00 19.77 ? 9   GLU A OE1 1 
ATOM   39   O OE2 . GLU A 1 9   ? 13.385 15.016 -14.962 1.00 20.63 ? 9   GLU A OE2 1 
ATOM   40   N N   . TRP A 1 10  ? 8.782  15.793 -12.726 1.00 18.04 ? 10  TRP A N   1 
ATOM   41   C CA  . TRP A 1 10  ? 8.399  17.114 -12.206 1.00 17.59 ? 10  TRP A CA  1 
ATOM   42   C C   . TRP A 1 10  ? 7.427  17.015 -11.026 1.00 16.90 ? 10  TRP A C   1 
ATOM   43   O O   . TRP A 1 10  ? 7.498  17.817 -10.098 1.00 16.58 ? 10  TRP A O   1 
ATOM   44   C CB  . TRP A 1 10  ? 7.838  18.041 -13.306 1.00 18.77 ? 10  TRP A CB  1 
ATOM   45   C CG  . TRP A 1 10  ? 6.387  17.818 -13.639 1.00 19.88 ? 10  TRP A CG  1 
ATOM   46   C CD1 . TRP A 1 10  ? 5.893  17.108 -14.695 1.00 21.52 ? 10  TRP A CD1 1 
ATOM   47   C CD2 . TRP A 1 10  ? 5.242  18.325 -12.927 1.00 20.20 ? 10  TRP A CD2 1 
ATOM   48   N NE1 . TRP A 1 10  ? 4.520  17.128 -14.680 1.00 22.64 ? 10  TRP A NE1 1 
ATOM   49   C CE2 . TRP A 1 10  ? 4.092  17.868 -13.609 1.00 22.08 ? 10  TRP A CE2 1 
ATOM   50   C CE3 . TRP A 1 10  ? 5.078  19.117 -11.780 1.00 19.79 ? 10  TRP A CE3 1 
ATOM   51   C CZ2 . TRP A 1 10  ? 2.787  18.173 -13.180 1.00 21.20 ? 10  TRP A CZ2 1 
ATOM   52   C CZ3 . TRP A 1 10  ? 3.783  19.411 -11.347 1.00 20.99 ? 10  TRP A CZ3 1 
ATOM   53   C CH2 . TRP A 1 10  ? 2.655  18.941 -12.051 1.00 21.18 ? 10  TRP A CH2 1 
ATOM   54   N N   . ILE A 1 11  ? 6.548  16.012 -11.039 1.00 16.31 ? 11  ILE A N   1 
ATOM   55   C CA  . ILE A 1 11  ? 5.559  15.875 -9.970  1.00 16.64 ? 11  ILE A CA  1 
ATOM   56   C C   . ILE A 1 11  ? 6.224  15.657 -8.601  1.00 16.06 ? 11  ILE A C   1 
ATOM   57   O O   . ILE A 1 11  ? 5.761  16.192 -7.588  1.00 15.55 ? 11  ILE A O   1 
ATOM   58   C CB  . ILE A 1 11  ? 4.490  14.793 -10.288 1.00 17.68 ? 11  ILE A CB  1 
ATOM   59   C CG1 . ILE A 1 11  ? 3.389  14.781 -9.222  1.00 19.70 ? 11  ILE A CG1 1 
ATOM   60   C CG2 . ILE A 1 11  ? 5.106  13.423 -10.438 1.00 18.72 ? 11  ILE A CG2 1 
ATOM   61   C CD1 . ILE A 1 11  ? 2.530  16.053 -9.205  1.00 21.38 ? 11  ILE A CD1 1 
ATOM   62   N N   . TRP A 1 12  ? 7.328  14.909 -8.590  1.00 15.50 ? 12  TRP A N   1 
ATOM   63   C CA  . TRP A 1 12  ? 8.033  14.644 -7.327  1.00 15.34 ? 12  TRP A CA  1 
ATOM   64   C C   . TRP A 1 12  ? 8.889  15.834 -6.893  1.00 14.98 ? 12  TRP A C   1 
ATOM   65   O O   . TRP A 1 12  ? 9.066  16.090 -5.688  1.00 14.73 ? 12  TRP A O   1 
ATOM   66   C CB  . TRP A 1 12  ? 8.848  13.350 -7.426  1.00 15.58 ? 12  TRP A CB  1 
ATOM   67   C CG  . TRP A 1 12  ? 8.004  12.188 -7.905  1.00 16.15 ? 12  TRP A CG  1 
ATOM   68   C CD1 . TRP A 1 12  ? 8.216  11.431 -9.026  1.00 16.65 ? 12  TRP A CD1 1 
ATOM   69   C CD2 . TRP A 1 12  ? 6.794  11.695 -7.312  1.00 16.70 ? 12  TRP A CD2 1 
ATOM   70   N NE1 . TRP A 1 12  ? 7.230  10.477 -9.150  1.00 17.71 ? 12  TRP A NE1 1 
ATOM   71   C CE2 . TRP A 1 12  ? 6.339  10.622 -8.122  1.00 17.66 ? 12  TRP A CE2 1 
ATOM   72   C CE3 . TRP A 1 12  ? 6.061  12.040 -6.170  1.00 17.69 ? 12  TRP A CE3 1 
ATOM   73   C CZ2 . TRP A 1 12  ? 5.177  9.894  -7.825  1.00 18.33 ? 12  TRP A CZ2 1 
ATOM   74   C CZ3 . TRP A 1 12  ? 4.894  11.316 -5.877  1.00 18.27 ? 12  TRP A CZ3 1 
ATOM   75   C CH2 . TRP A 1 12  ? 4.477  10.250 -6.699  1.00 18.10 ? 12  TRP A CH2 1 
ATOM   76   N N   . LEU A 1 13  ? 9.387  16.583 -7.873  1.00 14.85 ? 13  LEU A N   1 
ATOM   77   C CA  . LEU A 1 13  ? 10.066 17.850 -7.588  1.00 14.34 ? 13  LEU A CA  1 
ATOM   78   C C   . LEU A 1 13  ? 9.080  18.851 -6.984  1.00 14.71 ? 13  LEU A C   1 
ATOM   79   O O   . LEU A 1 13  ? 9.407  19.551 -6.023  1.00 14.67 ? 13  LEU A O   1 
ATOM   80   C CB  . LEU A 1 13  ? 10.703 18.419 -8.848  1.00 14.59 ? 13  LEU A CB  1 
ATOM   81   C CG  . LEU A 1 13  ? 11.820 17.571 -9.460  1.00 14.16 ? 13  LEU A CG  1 
ATOM   82   C CD1 . LEU A 1 13  ? 12.315 18.173 -10.773 1.00 15.45 ? 13  LEU A CD1 1 
ATOM   83   C CD2 . LEU A 1 13  ? 12.961 17.403 -8.458  1.00 15.24 ? 13  LEU A CD2 1 
ATOM   84   N N   . ALA A 1 14  ? 7.863  18.890 -7.527  1.00 14.82 ? 14  ALA A N   1 
ATOM   85   C CA  . ALA A 1 14  ? 6.803  19.753 -6.991  1.00 14.85 ? 14  ALA A CA  1 
ATOM   86   C C   . ALA A 1 14  ? 6.409  19.361 -5.571  1.00 14.67 ? 14  ALA A C   1 
ATOM   87   O O   . ALA A 1 14  ? 6.311  20.220 -4.695  1.00 14.83 ? 14  ALA A O   1 
ATOM   88   C CB  . ALA A 1 14  ? 5.574  19.731 -7.910  1.00 15.01 ? 14  ALA A CB  1 
ATOM   89   N N   . LEU A 1 15  ? 6.188  18.069 -5.325  1.00 14.58 ? 15  LEU A N   1 
ATOM   90   C CA  A LEU A 1 15  ? 5.828  17.612 -3.987  0.70 14.41 ? 15  LEU A CA  1 
ATOM   91   C CA  B LEU A 1 15  ? 5.828  17.628 -3.982  0.30 14.43 ? 15  LEU A CA  1 
ATOM   92   C C   . LEU A 1 15  ? 6.973  17.861 -2.997  1.00 14.29 ? 15  LEU A C   1 
ATOM   93   O O   . LEU A 1 15  ? 6.745  18.262 -1.854  1.00 14.68 ? 15  LEU A O   1 
ATOM   94   C CB  A LEU A 1 15  ? 5.435  16.134 -4.014  0.70 14.80 ? 15  LEU A CB  1 
ATOM   95   C CB  B LEU A 1 15  ? 5.370  16.167 -3.981  0.30 14.67 ? 15  LEU A CB  1 
ATOM   96   C CG  A LEU A 1 15  ? 4.905  15.502 -2.726  0.70 14.42 ? 15  LEU A CG  1 
ATOM   97   C CG  B LEU A 1 15  ? 4.010  15.908 -4.642  0.30 14.73 ? 15  LEU A CG  1 
ATOM   98   C CD1 A LEU A 1 15  ? 3.834  16.363 -2.052  0.70 16.14 ? 15  LEU A CD1 1 
ATOM   99   C CD1 B LEU A 1 15  ? 3.715  14.423 -4.673  0.30 15.39 ? 15  LEU A CD1 1 
ATOM   100  C CD2 A LEU A 1 15  ? 4.392  14.097 -3.000  0.70 14.67 ? 15  LEU A CD2 1 
ATOM   101  C CD2 B LEU A 1 15  ? 2.892  16.648 -3.917  0.30 15.33 ? 15  LEU A CD2 1 
ATOM   102  N N   . GLY A 1 16  ? 8.206  17.633 -3.447  1.00 13.65 ? 16  GLY A N   1 
ATOM   103  C CA  . GLY A 1 16  ? 9.387  17.914 -2.612  1.00 13.16 ? 16  GLY A CA  1 
ATOM   104  C C   . GLY A 1 16  ? 9.445  19.387 -2.228  1.00 13.12 ? 16  GLY A C   1 
ATOM   105  O O   . GLY A 1 16  ? 9.689  19.722 -1.063  1.00 13.14 ? 16  GLY A O   1 
ATOM   106  N N   . THR A 1 17  ? 9.214  20.259 -3.212  1.00 12.97 ? 17  THR A N   1 
ATOM   107  C CA  A THR A 1 17  ? 9.208  21.700 -2.973  0.80 12.59 ? 17  THR A CA  1 
ATOM   108  C CA  B THR A 1 17  ? 9.198  21.709 -2.967  0.20 13.09 ? 17  THR A CA  1 
ATOM   109  C C   . THR A 1 17  ? 8.173  22.058 -1.899  1.00 12.96 ? 17  THR A C   1 
ATOM   110  O O   . THR A 1 17  ? 8.458  22.824 -0.966  1.00 13.21 ? 17  THR A O   1 
ATOM   111  C CB  A THR A 1 17  ? 8.908  22.468 -4.296  0.80 12.21 ? 17  THR A CB  1 
ATOM   112  C CB  B THR A 1 17  ? 8.843  22.533 -4.233  0.20 12.99 ? 17  THR A CB  1 
ATOM   113  O OG1 A THR A 1 17  ? 9.943  22.182 -5.245  0.80 11.69 ? 17  THR A OG1 1 
ATOM   114  O OG1 B THR A 1 17  ? 7.610  22.065 -4.780  0.20 13.97 ? 17  THR A OG1 1 
ATOM   115  C CG2 A THR A 1 17  ? 8.911  23.967 -4.042  0.80 12.61 ? 17  THR A CG2 1 
ATOM   116  C CG2 B THR A 1 17  ? 9.922  22.434 -5.279  0.20 12.96 ? 17  THR A CG2 1 
ATOM   117  N N   . ALA A 1 18  ? 6.968  21.498 -2.036  1.00 13.20 ? 18  ALA A N   1 
ATOM   118  C CA  . ALA A 1 18  ? 5.889  21.739 -1.079  1.00 13.07 ? 18  ALA A CA  1 
ATOM   119  C C   . ALA A 1 18  ? 6.255  21.284 0.330   1.00 12.81 ? 18  ALA A C   1 
ATOM   120  O O   . ALA A 1 18  ? 6.067  22.025 1.289   1.00 13.53 ? 18  ALA A O   1 
ATOM   121  C CB  . ALA A 1 18  ? 4.624  21.048 -1.528  1.00 13.39 ? 18  ALA A CB  1 
ATOM   122  N N   . LEU A 1 19  ? 6.767  20.059 0.455   1.00 12.57 ? 19  LEU A N   1 
ATOM   123  C CA  . LEU A 1 19  ? 7.063  19.494 1.769   1.00 12.07 ? 19  LEU A CA  1 
ATOM   124  C C   . LEU A 1 19  ? 8.241  20.198 2.449   1.00 11.91 ? 19  LEU A C   1 
ATOM   125  O O   . LEU A 1 19  ? 8.204  20.453 3.657   1.00 12.62 ? 19  LEU A O   1 
ATOM   126  C CB  . LEU A 1 19  ? 7.295  17.980 1.649   1.00 12.48 ? 19  LEU A CB  1 
ATOM   127  C CG  . LEU A 1 19  ? 6.055  17.202 1.194   1.00 13.27 ? 19  LEU A CG  1 
ATOM   128  C CD1 . LEU A 1 19  ? 6.404  15.754 0.855   1.00 13.48 ? 19  LEU A CD1 1 
ATOM   129  C CD2 . LEU A 1 19  ? 4.954  17.271 2.256   1.00 16.42 ? 19  LEU A CD2 1 
ATOM   130  N N   . MET A 1 20  ? 9.276  20.537 1.678   1.00 11.88 ? 20  MET A N   1 
ATOM   131  C CA  . MET A 1 20  ? 10.400 21.307 2.250   1.00 11.69 ? 20  MET A CA  1 
ATOM   132  C C   . MET A 1 20  ? 9.954  22.718 2.644   1.00 11.76 ? 20  MET A C   1 
ATOM   133  O O   . MET A 1 20  ? 10.363 23.238 3.685   1.00 12.05 ? 20  MET A O   1 
ATOM   134  C CB  . MET A 1 20  ? 11.572 21.386 1.270   1.00 12.08 ? 20  MET A CB  1 
ATOM   135  C CG  . MET A 1 20  ? 12.177 20.043 0.919   1.00 12.16 ? 20  MET A CG  1 
ATOM   136  S SD  . MET A 1 20  ? 12.826 19.206 2.376   1.00 12.65 ? 20  MET A SD  1 
ATOM   137  C CE  . MET A 1 20  ? 13.599 17.826 1.545   1.00 13.95 ? 20  MET A CE  1 
ATOM   138  N N   . GLY A 1 21  ? 9.129  23.338 1.799   1.00 12.28 ? 21  GLY A N   1 
ATOM   139  C CA  . GLY A 1 21  ? 8.625  24.686 2.108   1.00 12.03 ? 21  GLY A CA  1 
ATOM   140  C C   . GLY A 1 21  ? 7.773  24.729 3.366   1.00 12.34 ? 21  GLY A C   1 
ATOM   141  O O   . GLY A 1 21  ? 7.994  25.561 4.259   1.00 12.63 ? 21  GLY A O   1 
ATOM   142  N N   . LEU A 1 22  ? 6.819  23.810 3.459   1.00 12.74 ? 22  LEU A N   1 
ATOM   143  C CA  . LEU A 1 22  ? 5.946  23.736 4.636   1.00 12.76 ? 22  LEU A CA  1 
ATOM   144  C C   . LEU A 1 22  ? 6.746  23.399 5.904   1.00 12.75 ? 22  LEU A C   1 
ATOM   145  O O   . LEU A 1 22  ? 6.514  23.988 6.956   1.00 13.42 ? 22  LEU A O   1 
ATOM   146  C CB  . LEU A 1 22  ? 4.821  22.712 4.427   1.00 13.49 ? 22  LEU A CB  1 
ATOM   147  C CG  . LEU A 1 22  ? 3.797  23.091 3.360   1.00 14.36 ? 22  LEU A CG  1 
ATOM   148  C CD1 . LEU A 1 22  ? 3.010  21.856 2.901   1.00 17.11 ? 22  LEU A CD1 1 
ATOM   149  C CD2 . LEU A 1 22  ? 2.886  24.232 3.874   1.00 15.71 ? 22  LEU A CD2 1 
ATOM   150  N N   . GLY A 1 23  ? 7.688  22.463 5.790   1.00 12.88 ? 23  GLY A N   1 
ATOM   151  C CA  . GLY A 1 23  ? 8.573  22.115 6.909   1.00 12.67 ? 23  GLY A CA  1 
ATOM   152  C C   . GLY A 1 23  ? 9.354  23.321 7.394   1.00 12.38 ? 23  GLY A C   1 
ATOM   153  O O   . GLY A 1 23  ? 9.381  23.606 8.599   1.00 13.33 ? 23  GLY A O   1 
ATOM   154  N N   . THR A 1 24  ? 9.938  24.063 6.455   1.00 12.49 ? 24  THR A N   1 
ATOM   155  C CA  . THR A 1 24  ? 10.708 25.268 6.787   1.00 12.29 ? 24  THR A CA  1 
ATOM   156  C C   . THR A 1 24  ? 9.853  26.286 7.547   1.00 12.77 ? 24  THR A C   1 
ATOM   157  O O   . THR A 1 24  ? 10.283 26.836 8.580   1.00 13.16 ? 24  THR A O   1 
ATOM   158  C CB  . THR A 1 24  ? 11.293 25.949 5.513   1.00 12.44 ? 24  THR A CB  1 
ATOM   159  O OG1 . THR A 1 24  ? 12.103 25.013 4.784   1.00 12.79 ? 24  THR A OG1 1 
ATOM   160  C CG2 . THR A 1 24  ? 12.152 27.158 5.903   1.00 11.80 ? 24  THR A CG2 1 
ATOM   161  N N   . LEU A 1 25  ? 8.660  26.553 7.006   1.00 12.72 ? 25  LEU A N   1 
ATOM   162  C CA  A LEU A 1 25  ? 7.756  27.545 7.593   0.60 13.77 ? 25  LEU A CA  1 
ATOM   163  C CA  B LEU A 1 25  ? 7.752  27.534 7.571   0.40 13.41 ? 25  LEU A CA  1 
ATOM   164  C C   . LEU A 1 25  ? 7.369  27.159 9.011   1.00 13.52 ? 25  LEU A C   1 
ATOM   165  O O   . LEU A 1 25  ? 7.393  27.991 9.913   1.00 13.62 ? 25  LEU A O   1 
ATOM   166  C CB  A LEU A 1 25  ? 6.501  27.739 6.739   0.60 14.60 ? 25  LEU A CB  1 
ATOM   167  C CB  B LEU A 1 25  ? 6.530  27.638 6.662   0.40 13.77 ? 25  LEU A CB  1 
ATOM   168  C CG  A LEU A 1 25  ? 6.669  28.435 5.391   0.60 14.61 ? 25  LEU A CG  1 
ATOM   169  C CG  B LEU A 1 25  ? 5.491  28.705 6.944   0.40 13.22 ? 25  LEU A CG  1 
ATOM   170  C CD1 A LEU A 1 25  ? 5.320  28.952 4.937   0.60 16.39 ? 25  LEU A CD1 1 
ATOM   171  C CD1 B LEU A 1 25  ? 5.124  29.375 5.640   0.40 13.78 ? 25  LEU A CD1 1 
ATOM   172  C CD2 A LEU A 1 25  ? 7.680  29.584 5.426   0.60 17.11 ? 25  LEU A CD2 1 
ATOM   173  C CD2 B LEU A 1 25  ? 4.302  28.033 7.569   0.40 13.03 ? 25  LEU A CD2 1 
ATOM   174  N N   . TYR A 1 26  ? 7.034  25.886 9.216   1.00 13.53 ? 26  TYR A N   1 
ATOM   175  C CA  . TYR A 1 26  ? 6.630  25.411 10.532  1.00 13.84 ? 26  TYR A CA  1 
ATOM   176  C C   . TYR A 1 26  ? 7.782  25.523 11.541  1.00 12.79 ? 26  TYR A C   1 
ATOM   177  O O   . TYR A 1 26  ? 7.591  25.974 12.683  1.00 12.61 ? 26  TYR A O   1 
ATOM   178  C CB  . TYR A 1 26  ? 6.122  23.972 10.431  1.00 14.44 ? 26  TYR A CB  1 
ATOM   179  C CG  . TYR A 1 26  ? 5.694  23.395 11.752  1.00 16.78 ? 26  TYR A CG  1 
ATOM   180  C CD1 . TYR A 1 26  ? 4.571  23.892 12.421  1.00 18.55 ? 26  TYR A CD1 1 
ATOM   181  C CD2 . TYR A 1 26  ? 6.427  22.368 12.349  1.00 17.48 ? 26  TYR A CD2 1 
ATOM   182  C CE1 . TYR A 1 26  ? 4.174  23.360 13.639  1.00 20.17 ? 26  TYR A CE1 1 
ATOM   183  C CE2 . TYR A 1 26  ? 6.045  21.837 13.581  1.00 18.50 ? 26  TYR A CE2 1 
ATOM   184  C CZ  . TYR A 1 26  ? 4.929  22.334 14.213  1.00 19.82 ? 26  TYR A CZ  1 
ATOM   185  O OH  . TYR A 1 26  ? 4.568  21.801 15.426  1.00 21.62 ? 26  TYR A OH  1 
ATOM   186  N N   . PHE A 1 27  ? 8.987  25.125 11.116  1.00 12.25 ? 27  PHE A N   1 
ATOM   187  C CA  . PHE A 1 27  ? 10.157 25.194 12.005  1.00 12.01 ? 27  PHE A CA  1 
ATOM   188  C C   . PHE A 1 27  ? 10.495 26.639 12.362  1.00 12.30 ? 27  PHE A C   1 
ATOM   189  O O   . PHE A 1 27  ? 10.876 26.927 13.492  1.00 12.72 ? 27  PHE A O   1 
ATOM   190  C CB  . PHE A 1 27  ? 11.400 24.513 11.409  1.00 11.77 ? 27  PHE A CB  1 
ATOM   191  C CG  . PHE A 1 27  ? 11.272 23.017 11.177  1.00 11.26 ? 27  PHE A CG  1 
ATOM   192  C CD1 . PHE A 1 27  ? 10.249 22.256 11.750  1.00 12.60 ? 27  PHE A CD1 1 
ATOM   193  C CD2 . PHE A 1 27  ? 12.226 22.368 10.397  1.00 11.60 ? 27  PHE A CD2 1 
ATOM   194  C CE1 . PHE A 1 27  ? 10.170 20.863 11.526  1.00 11.00 ? 27  PHE A CE1 1 
ATOM   195  C CE2 . PHE A 1 27  ? 12.160 20.990 10.162  1.00 12.81 ? 27  PHE A CE2 1 
ATOM   196  C CZ  . PHE A 1 27  ? 11.125 20.232 10.717  1.00 11.50 ? 27  PHE A CZ  1 
ATOM   197  N N   . LEU A 1 28  ? 10.354 27.530 11.382  1.00 12.55 ? 28  LEU A N   1 
ATOM   198  C CA  A LEU A 1 28  ? 10.587 28.952 11.610  0.70 12.83 ? 28  LEU A CA  1 
ATOM   199  C CA  B LEU A 1 28  ? 10.567 28.963 11.581  0.30 12.96 ? 28  LEU A CA  1 
ATOM   200  C C   . LEU A 1 28  ? 9.586  29.530 12.618  1.00 13.17 ? 28  LEU A C   1 
ATOM   201  O O   . LEU A 1 28  ? 9.969  30.256 13.528  1.00 13.06 ? 28  LEU A O   1 
ATOM   202  C CB  A LEU A 1 28  ? 10.528 29.719 10.294  0.70 13.20 ? 28  LEU A CB  1 
ATOM   203  C CB  B LEU A 1 28  ? 10.409 29.689 10.241  0.30 13.22 ? 28  LEU A CB  1 
ATOM   204  C CG  A LEU A 1 28  ? 10.728 31.228 10.433  0.70 12.77 ? 28  LEU A CG  1 
ATOM   205  C CG  B LEU A 1 28  ? 11.114 31.025 9.993   0.30 13.61 ? 28  LEU A CG  1 
ATOM   206  C CD1 A LEU A 1 28  ? 12.187 31.553 10.775  0.70 13.34 ? 28  LEU A CD1 1 
ATOM   207  C CD1 B LEU A 1 28  ? 11.125 31.323 8.509   0.30 13.77 ? 28  LEU A CD1 1 
ATOM   208  C CD2 A LEU A 1 28  ? 10.298 31.933 9.154   0.70 13.33 ? 28  LEU A CD2 1 
ATOM   209  C CD2 B LEU A 1 28  ? 10.459 32.165 10.752  0.30 14.87 ? 28  LEU A CD2 1 
ATOM   210  N N   . VAL A 1 29  ? 8.309  29.207 12.468  1.00 13.02 ? 29  VAL A N   1 
ATOM   211  C CA  . VAL A 1 29  ? 7.295  29.710 13.394  1.00 13.55 ? 29  VAL A CA  1 
ATOM   212  C C   . VAL A 1 29  ? 7.580  29.235 14.810  1.00 14.36 ? 29  VAL A C   1 
ATOM   213  O O   . VAL A 1 29  ? 7.609  30.031 15.752  1.00 15.05 ? 29  VAL A O   1 
ATOM   214  C CB  . VAL A 1 29  ? 5.885  29.317 12.940  1.00 13.60 ? 29  VAL A CB  1 
ATOM   215  C CG1 . VAL A 1 29  ? 4.852  29.643 14.032  1.00 14.12 ? 29  VAL A CG1 1 
ATOM   216  C CG2 . VAL A 1 29  ? 5.567  30.032 11.625  1.00 13.10 ? 29  VAL A CG2 1 
ATOM   217  N N   . LYS A 1 30  ? 7.831  27.933 14.954  1.00 14.07 ? 30  LYS A N   1 
ATOM   218  C CA  . LYS A 1 30  ? 8.150  27.384 16.276  1.00 15.46 ? 30  LYS A CA  1 
ATOM   219  C C   . LYS A 1 30  ? 9.434  27.972 16.846  1.00 15.37 ? 30  LYS A C   1 
ATOM   220  O O   . LYS A 1 30  ? 9.476  28.333 18.027  1.00 16.09 ? 30  LYS A O   1 
ATOM   221  C CB  . LYS A 1 30  ? 8.230  25.860 16.218  1.00 15.96 ? 30  LYS A CB  1 
ATOM   222  C CG  . LYS A 1 30  ? 6.912  25.213 15.848  1.00 19.63 ? 30  LYS A CG  1 
ATOM   223  C CD  . LYS A 1 30  ? 5.816  25.601 16.848  1.00 26.19 ? 30  LYS A CD  1 
ATOM   224  C CE  . LYS A 1 30  ? 4.430  25.333 16.303  1.00 29.19 ? 30  LYS A CE  1 
ATOM   225  N NZ  . LYS A 1 30  ? 3.409  25.395 17.394  1.00 32.53 ? 30  LYS A NZ  1 
ATOM   226  N N   . GLY A 1 31  ? 10.458 28.104 16.002  1.00 15.15 ? 31  GLY A N   1 
ATOM   227  C CA  . GLY A 1 31  ? 11.776 28.591 16.430  1.00 15.77 ? 31  GLY A CA  1 
ATOM   228  C C   . GLY A 1 31  ? 11.790 30.041 16.862  1.00 16.56 ? 31  GLY A C   1 
ATOM   229  O O   . GLY A 1 31  ? 12.453 30.407 17.839  1.00 16.79 ? 31  GLY A O   1 
ATOM   230  N N   . MET A 1 32  ? 11.049 30.867 16.137  1.00 16.40 ? 32  MET A N   1 
ATOM   231  C CA  A MET A 1 32  ? 10.952 32.301 16.440  0.50 17.27 ? 32  MET A CA  1 
ATOM   232  C CA  B MET A 1 32  ? 11.003 32.281 16.478  0.50 17.47 ? 32  MET A CA  1 
ATOM   233  C C   . MET A 1 32  ? 10.242 32.523 17.773  1.00 17.94 ? 32  MET A C   1 
ATOM   234  O O   . MET A 1 32  ? 10.426 33.560 18.418  1.00 18.74 ? 32  MET A O   1 
ATOM   235  C CB  A MET A 1 32  ? 10.221 33.056 15.321  0.50 17.04 ? 32  MET A CB  1 
ATOM   236  C CB  B MET A 1 32  ? 10.447 33.094 15.321  0.50 17.09 ? 32  MET A CB  1 
ATOM   237  C CG  A MET A 1 32  ? 11.009 33.218 14.014  0.50 17.60 ? 32  MET A CG  1 
ATOM   238  C CG  B MET A 1 32  ? 11.422 33.124 14.166  0.50 17.59 ? 32  MET A CG  1 
ATOM   239  S SD  A MET A 1 32  ? 12.465 34.284 14.117  0.50 20.12 ? 32  MET A SD  1 
ATOM   240  S SD  B MET A 1 32  ? 11.065 34.389 12.968  0.50 18.44 ? 32  MET A SD  1 
ATOM   241  C CE  A MET A 1 32  ? 11.701 35.904 14.201  0.50 19.32 ? 32  MET A CE  1 
ATOM   242  C CE  B MET A 1 32  ? 11.380 35.883 13.911  0.50 18.12 ? 32  MET A CE  1 
ATOM   243  N N   . GLY A 1 33  ? 9.419  31.554 18.168  1.00 18.51 ? 33  GLY A N   1 
ATOM   244  C CA  . GLY A 1 33  ? 8.688  31.623 19.430  1.00 20.11 ? 33  GLY A CA  1 
ATOM   245  C C   . GLY A 1 33  ? 9.515  31.324 20.675  1.00 21.55 ? 33  GLY A C   1 
ATOM   246  O O   . GLY A 1 33  ? 9.256  31.886 21.740  1.00 22.05 ? 33  GLY A O   1 
ATOM   247  N N   . VAL A 1 34  ? 10.521 30.462 20.544  1.00 21.78 ? 34  VAL A N   1 
ATOM   248  C CA  A VAL A 1 34  ? 11.294 30.028 21.718  0.60 22.28 ? 34  VAL A CA  1 
ATOM   249  C CA  B VAL A 1 34  ? 11.335 29.992 21.674  0.40 22.21 ? 34  VAL A CA  1 
ATOM   250  C C   . VAL A 1 34  ? 12.312 31.068 22.172  1.00 22.71 ? 34  VAL A C   1 
ATOM   251  O O   . VAL A 1 34  ? 12.844 31.840 21.369  1.00 23.26 ? 34  VAL A O   1 
ATOM   252  C CB  A VAL A 1 34  ? 11.983 28.638 21.525  0.60 22.32 ? 34  VAL A CB  1 
ATOM   253  C CB  B VAL A 1 34  ? 12.094 28.689 21.275  0.40 22.07 ? 34  VAL A CB  1 
ATOM   254  C CG1 A VAL A 1 34  ? 10.961 27.579 21.127  0.60 21.73 ? 34  VAL A CG1 1 
ATOM   255  C CG1 B VAL A 1 34  ? 13.129 28.288 22.316  0.40 22.01 ? 34  VAL A CG1 1 
ATOM   256  C CG2 A VAL A 1 34  ? 13.124 28.713 20.525  0.60 22.89 ? 34  VAL A CG2 1 
ATOM   257  C CG2 B VAL A 1 34  ? 11.105 27.556 21.048  0.40 21.80 ? 34  VAL A CG2 1 
ATOM   258  N N   . SER A 1 35  ? 12.558 31.102 23.485  1.00 23.29 ? 35  SER A N   1 
ATOM   259  C CA  A SER A 1 35  ? 13.491 32.066 24.065  0.50 23.63 ? 35  SER A CA  1 
ATOM   260  C CA  B SER A 1 35  ? 13.486 32.066 24.077  0.50 23.77 ? 35  SER A CA  1 
ATOM   261  C C   . SER A 1 35  ? 14.806 31.439 24.531  1.00 23.83 ? 35  SER A C   1 
ATOM   262  O O   . SER A 1 35  ? 15.835 32.116 24.588  1.00 24.19 ? 35  SER A O   1 
ATOM   263  C CB  A SER A 1 35  ? 12.825 32.831 25.214  0.50 23.75 ? 35  SER A CB  1 
ATOM   264  C CB  B SER A 1 35  ? 12.821 32.790 25.250  0.50 23.91 ? 35  SER A CB  1 
ATOM   265  O OG  A SER A 1 35  ? 12.155 31.951 26.099  0.50 23.56 ? 35  SER A OG  1 
ATOM   266  O OG  B SER A 1 35  ? 11.768 33.621 24.798  0.50 24.61 ? 35  SER A OG  1 
ATOM   267  N N   . ASP A 1 36  ? 14.780 30.146 24.852  1.00 23.82 ? 36  ASP A N   1 
ATOM   268  C CA  . ASP A 1 36  ? 15.981 29.448 25.334  1.00 23.93 ? 36  ASP A CA  1 
ATOM   269  C C   . ASP A 1 36  ? 17.124 29.517 24.317  1.00 24.11 ? 36  ASP A C   1 
ATOM   270  O O   . ASP A 1 36  ? 16.951 29.094 23.178  1.00 23.30 ? 36  ASP A O   1 
ATOM   271  C CB  . ASP A 1 36  ? 15.661 27.989 25.661  1.00 24.13 ? 36  ASP A CB  1 
ATOM   272  C CG  . ASP A 1 36  ? 16.858 27.245 26.234  1.00 25.06 ? 36  ASP A CG  1 
ATOM   273  O OD1 . ASP A 1 36  ? 17.171 27.464 27.419  1.00 27.73 ? 36  ASP A OD1 1 
ATOM   274  O OD2 . ASP A 1 36  ? 17.486 26.442 25.511  1.00 24.32 ? 36  ASP A OD2 1 
ATOM   275  N N   . PRO A 1 37  ? 18.290 30.061 24.719  1.00 24.23 ? 37  PRO A N   1 
ATOM   276  C CA  . PRO A 1 37  ? 19.431 30.181 23.796  1.00 24.37 ? 37  PRO A CA  1 
ATOM   277  C C   . PRO A 1 37  ? 19.881 28.857 23.158  1.00 23.97 ? 37  PRO A C   1 
ATOM   278  O O   . PRO A 1 37  ? 20.120 28.817 21.945  1.00 24.14 ? 37  PRO A O   1 
ATOM   279  C CB  . PRO A 1 37  ? 20.536 30.785 24.676  1.00 24.90 ? 37  PRO A CB  1 
ATOM   280  C CG  . PRO A 1 37  ? 19.790 31.502 25.759  1.00 25.03 ? 37  PRO A CG  1 
ATOM   281  C CD  . PRO A 1 37  ? 18.597 30.639 26.044  1.00 24.58 ? 37  PRO A CD  1 
ATOM   282  N N   . ASP A 1 38  ? 19.980 27.786 23.947  1.00 23.62 ? 38  ASP A N   1 
ATOM   283  C CA  . ASP A 1 38  ? 20.357 26.483 23.384  1.00 23.18 ? 38  ASP A CA  1 
ATOM   284  C C   . ASP A 1 38  ? 19.337 26.008 22.357  1.00 22.07 ? 38  ASP A C   1 
ATOM   285  O O   . ASP A 1 38  ? 19.705 25.581 21.253  1.00 21.89 ? 38  ASP A O   1 
ATOM   286  C CB  . ASP A 1 38  ? 20.535 25.424 24.473  1.00 23.78 ? 38  ASP A CB  1 
ATOM   287  C CG  . ASP A 1 38  ? 21.911 25.481 25.122  1.00 26.96 ? 38  ASP A CG  1 
ATOM   288  O OD1 . ASP A 1 38  ? 22.687 26.412 24.813  1.00 29.66 ? 38  ASP A OD1 1 
ATOM   289  O OD2 . ASP A 1 38  ? 22.216 24.578 25.931  1.00 30.95 ? 38  ASP A OD2 1 
ATOM   290  N N   . ALA A 1 39  ? 18.055 26.083 22.702  1.00 20.24 ? 39  ALA A N   1 
ATOM   291  C CA  . ALA A 1 39  ? 17.024 25.615 21.770  1.00 19.40 ? 39  ALA A CA  1 
ATOM   292  C C   . ALA A 1 39  ? 17.039 26.427 20.481  1.00 19.06 ? 39  ALA A C   1 
ATOM   293  O O   . ALA A 1 39  ? 16.804 25.887 19.394  1.00 18.77 ? 39  ALA A O   1 
ATOM   294  C CB  . ALA A 1 39  ? 15.651 25.637 22.414  1.00 19.37 ? 39  ALA A CB  1 
ATOM   295  N N   . LYS A 1 40  ? 17.330 27.721 20.598  1.00 18.65 ? 40  LYS A N   1 
ATOM   296  C CA  . LYS A 1 40  ? 17.362 28.610 19.429  1.00 19.62 ? 40  LYS A CA  1 
ATOM   297  C C   . LYS A 1 40  ? 18.423 28.170 18.416  1.00 18.48 ? 40  LYS A C   1 
ATOM   298  O O   . LYS A 1 40  ? 18.188 28.254 17.205  1.00 18.67 ? 40  LYS A O   1 
ATOM   299  C CB  . LYS A 1 40  ? 17.596 30.065 19.851  1.00 19.33 ? 40  LYS A CB  1 
ATOM   300  C CG  . LYS A 1 40  ? 16.347 30.725 20.433  1.00 21.96 ? 40  LYS A CG  1 
ATOM   301  C CD  . LYS A 1 40  ? 16.519 32.229 20.675  1.00 22.87 ? 40  LYS A CD  1 
ATOM   302  C CE  . LYS A 1 40  ? 17.531 32.542 21.762  1.00 29.16 ? 40  LYS A CE  1 
ATOM   303  N NZ  . LYS A 1 40  ? 17.439 33.965 22.230  1.00 31.89 ? 40  LYS A NZ  1 
ATOM   304  N N   . LYS A 1 41  ? 19.573 27.703 18.915  1.00 17.94 ? 41  LYS A N   1 
ATOM   305  C CA  A LYS A 1 41  ? 20.648 27.213 18.063  0.50 17.34 ? 41  LYS A CA  1 
ATOM   306  C CA  B LYS A 1 41  ? 20.658 27.202 18.067  0.50 17.60 ? 41  LYS A CA  1 
ATOM   307  C C   . LYS A 1 41  ? 20.175 26.015 17.235  1.00 16.50 ? 41  LYS A C   1 
ATOM   308  O O   . LYS A 1 41  ? 20.375 25.971 16.020  1.00 16.77 ? 41  LYS A O   1 
ATOM   309  C CB  A LYS A 1 41  ? 21.852 26.828 18.916  0.50 17.76 ? 41  LYS A CB  1 
ATOM   310  C CB  B LYS A 1 41  ? 21.869 26.781 18.910  0.50 17.80 ? 41  LYS A CB  1 
ATOM   311  C CG  A LYS A 1 41  ? 23.149 26.737 18.157  0.50 18.37 ? 41  LYS A CG  1 
ATOM   312  C CG  B LYS A 1 41  ? 22.619 27.922 19.579  0.50 18.43 ? 41  LYS A CG  1 
ATOM   313  C CD  A LYS A 1 41  ? 24.273 26.378 19.115  0.50 20.40 ? 41  LYS A CD  1 
ATOM   314  C CD  B LYS A 1 41  ? 23.796 27.395 20.400  0.50 18.95 ? 41  LYS A CD  1 
ATOM   315  C CE  A LYS A 1 41  ? 25.622 26.475 18.435  0.50 22.20 ? 41  LYS A CE  1 
ATOM   316  C CE  B LYS A 1 41  ? 24.609 28.524 21.018  0.50 20.73 ? 41  LYS A CE  1 
ATOM   317  N NZ  A LYS A 1 41  ? 26.736 26.589 19.413  0.50 22.07 ? 41  LYS A NZ  1 
ATOM   318  N NZ  B LYS A 1 41  ? 25.322 29.331 19.986  0.50 21.64 ? 41  LYS A NZ  1 
ATOM   319  N N   . PHE A 1 42  ? 19.516 25.056 17.886  1.00 15.14 ? 42  PHE A N   1 
ATOM   320  C CA  . PHE A 1 42  ? 18.995 23.886 17.171  1.00 13.39 ? 42  PHE A CA  1 
ATOM   321  C C   . PHE A 1 42  ? 17.941 24.309 16.155  1.00 13.20 ? 42  PHE A C   1 
ATOM   322  O O   . PHE A 1 42  ? 17.889 23.776 15.047  1.00 12.45 ? 42  PHE A O   1 
ATOM   323  C CB  . PHE A 1 42  ? 18.400 22.865 18.147  1.00 13.40 ? 42  PHE A CB  1 
ATOM   324  C CG  . PHE A 1 42  ? 19.440 22.102 18.917  1.00 12.83 ? 42  PHE A CG  1 
ATOM   325  C CD1 . PHE A 1 42  ? 20.151 21.080 18.303  1.00 12.52 ? 42  PHE A CD1 1 
ATOM   326  C CD2 . PHE A 1 42  ? 19.710 22.408 20.256  1.00 14.18 ? 42  PHE A CD2 1 
ATOM   327  C CE1 . PHE A 1 42  ? 21.124 20.375 19.003  1.00 12.97 ? 42  PHE A CE1 1 
ATOM   328  C CE2 . PHE A 1 42  ? 20.675 21.700 20.977  1.00 13.60 ? 42  PHE A CE2 1 
ATOM   329  C CZ  . PHE A 1 42  ? 21.379 20.676 20.354  1.00 13.93 ? 42  PHE A CZ  1 
ATOM   330  N N   . TYR A 1 43  ? 17.100 25.265 16.539  1.00 13.19 ? 43  TYR A N   1 
ATOM   331  C CA  . TYR A 1 43  ? 16.082 25.760 15.597  1.00 13.45 ? 43  TYR A CA  1 
ATOM   332  C C   . TYR A 1 43  ? 16.706 26.440 14.387  1.00 13.76 ? 43  TYR A C   1 
ATOM   333  O O   . TYR A 1 43  ? 16.263 26.231 13.257  1.00 14.09 ? 43  TYR A O   1 
ATOM   334  C CB  . TYR A 1 43  ? 15.073 26.692 16.280  1.00 13.49 ? 43  TYR A CB  1 
ATOM   335  C CG  . TYR A 1 43  ? 13.882 25.963 16.871  1.00 13.62 ? 43  TYR A CG  1 
ATOM   336  C CD1 . TYR A 1 43  ? 12.837 25.514 16.061  1.00 13.65 ? 43  TYR A CD1 1 
ATOM   337  C CD2 . TYR A 1 43  ? 13.794 25.732 18.245  1.00 15.62 ? 43  TYR A CD2 1 
ATOM   338  C CE1 . TYR A 1 43  ? 11.730 24.860 16.605  1.00 14.18 ? 43  TYR A CE1 1 
ATOM   339  C CE2 . TYR A 1 43  ? 12.694 25.069 18.785  1.00 14.61 ? 43  TYR A CE2 1 
ATOM   340  C CZ  . TYR A 1 43  ? 11.678 24.643 17.962  1.00 14.73 ? 43  TYR A CZ  1 
ATOM   341  O OH  . TYR A 1 43  ? 10.595 23.990 18.516  1.00 17.26 ? 43  TYR A OH  1 
ATOM   342  N N   . ALA A 1 44  ? 17.740 27.244 14.615  1.00 14.05 ? 44  ALA A N   1 
ATOM   343  C CA  . ALA A 1 44  ? 18.394 27.939 13.501  1.00 13.99 ? 44  ALA A CA  1 
ATOM   344  C C   . ALA A 1 44  ? 18.994 26.943 12.502  1.00 14.49 ? 44  ALA A C   1 
ATOM   345  O O   . ALA A 1 44  ? 18.727 27.006 11.297  1.00 14.58 ? 44  ALA A O   1 
ATOM   346  C CB  . ALA A 1 44  ? 19.462 28.900 14.018  1.00 14.89 ? 44  ALA A CB  1 
ATOM   347  N N   . ILE A 1 45  ? 19.760 25.985 13.020  1.00 13.91 ? 45  ILE A N   1 
ATOM   348  C CA  . ILE A 1 45  ? 20.406 24.985 12.150  1.00 13.71 ? 45  ILE A CA  1 
ATOM   349  C C   . ILE A 1 45  ? 19.356 24.179 11.401  1.00 13.33 ? 45  ILE A C   1 
ATOM   350  O O   . ILE A 1 45  ? 19.447 23.957 10.183  1.00 13.99 ? 45  ILE A O   1 
ATOM   351  C CB  . ILE A 1 45  ? 21.269 24.034 12.989  1.00 13.91 ? 45  ILE A CB  1 
ATOM   352  C CG1 . ILE A 1 45  ? 22.447 24.811 13.591  1.00 14.78 ? 45  ILE A CG1 1 
ATOM   353  C CG2 . ILE A 1 45  ? 21.706 22.819 12.163  1.00 13.80 ? 45  ILE A CG2 1 
ATOM   354  C CD1 . ILE A 1 45  ? 23.171 24.081 14.724  1.00 17.57 ? 45  ILE A CD1 1 
ATOM   355  N N   . THR A 1 46  ? 18.343 23.744 12.145  1.00 13.37 ? 46  THR A N   1 
ATOM   356  C CA  . THR A 1 46  ? 17.343 22.801 11.645  1.00 13.22 ? 46  THR A CA  1 
ATOM   357  C C   . THR A 1 46  ? 16.325 23.447 10.693  1.00 13.55 ? 46  THR A C   1 
ATOM   358  O O   . THR A 1 46  ? 15.713 22.763 9.858   1.00 15.09 ? 46  THR A O   1 
ATOM   359  C CB  . THR A 1 46  ? 16.642 22.080 12.816  1.00 13.41 ? 46  THR A CB  1 
ATOM   360  O OG1 . THR A 1 46  ? 17.645 21.498 13.660  1.00 12.83 ? 46  THR A OG1 1 
ATOM   361  C CG2 . THR A 1 46  ? 15.736 20.932 12.308  1.00 13.71 ? 46  THR A CG2 1 
ATOM   362  N N   . THR A 1 47  ? 16.142 24.759 10.817  1.00 13.25 ? 47  THR A N   1 
ATOM   363  C CA  . THR A 1 47  ? 15.255 25.476 9.899   1.00 12.78 ? 47  THR A CA  1 
ATOM   364  C C   . THR A 1 47  ? 15.985 25.736 8.574   1.00 12.49 ? 47  THR A C   1 
ATOM   365  O O   . THR A 1 47  ? 15.377 25.700 7.496   1.00 12.91 ? 47  THR A O   1 
ATOM   366  C CB  . THR A 1 47  ? 14.745 26.780 10.544  1.00 11.91 ? 47  THR A CB  1 
ATOM   367  O OG1 . THR A 1 47  ? 14.092 26.467 11.788  1.00 13.66 ? 47  THR A OG1 1 
ATOM   368  C CG2 . THR A 1 47  ? 13.768 27.529 9.618   1.00 12.09 ? 47  THR A CG2 1 
ATOM   369  N N   . LEU A 1 48  ? 17.290 26.001 8.672   1.00 12.00 ? 48  LEU A N   1 
ATOM   370  C CA  A LEU A 1 48  ? 18.093 26.254 7.486   0.80 12.28 ? 48  LEU A CA  1 
ATOM   371  C CA  B LEU A 1 48  ? 18.145 26.233 7.495   0.20 12.24 ? 48  LEU A CA  1 
ATOM   372  C C   . LEU A 1 48  ? 18.141 25.041 6.543   1.00 12.32 ? 48  LEU A C   1 
ATOM   373  O O   . LEU A 1 48  ? 18.187 25.197 5.312   1.00 12.37 ? 48  LEU A O   1 
ATOM   374  C CB  A LEU A 1 48  ? 19.497 26.686 7.909   0.80 12.91 ? 48  LEU A CB  1 
ATOM   375  C CB  B LEU A 1 48  ? 19.598 26.512 7.913   0.20 12.45 ? 48  LEU A CB  1 
ATOM   376  C CG  A LEU A 1 48  ? 20.440 27.096 6.783   0.80 13.08 ? 48  LEU A CG  1 
ATOM   377  C CG  B LEU A 1 48  ? 20.291 27.886 7.827   0.20 12.65 ? 48  LEU A CG  1 
ATOM   378  C CD1 A LEU A 1 48  ? 19.840 28.215 5.926   0.80 13.60 ? 48  LEU A CD1 1 
ATOM   379  C CD1 B LEU A 1 48  ? 19.619 28.873 6.868   0.20 12.15 ? 48  LEU A CD1 1 
ATOM   380  C CD2 A LEU A 1 48  ? 21.782 27.530 7.372   0.80 13.44 ? 48  LEU A CD2 1 
ATOM   381  C CD2 B LEU A 1 48  ? 20.511 28.509 9.197   0.20 13.49 ? 48  LEU A CD2 1 
ATOM   382  N N   . VAL A 1 49  ? 18.110 23.843 7.117   1.00 11.66 ? 49  VAL A N   1 
ATOM   383  C CA  . VAL A 1 49  ? 18.210 22.612 6.341   1.00 11.74 ? 49  VAL A CA  1 
ATOM   384  C C   . VAL A 1 49  ? 17.106 22.480 5.269   1.00 11.89 ? 49  VAL A C   1 
ATOM   385  O O   . VAL A 1 49  ? 17.426 22.441 4.081   1.00 12.13 ? 49  VAL A O   1 
ATOM   386  C CB  . VAL A 1 49  ? 18.321 21.384 7.269   1.00 11.68 ? 49  VAL A CB  1 
ATOM   387  C CG1 . VAL A 1 49  ? 18.096 20.109 6.493   1.00 12.12 ? 49  VAL A CG1 1 
ATOM   388  C CG2 . VAL A 1 49  ? 19.708 21.383 7.958   1.00 11.77 ? 49  VAL A CG2 1 
ATOM   389  N N   . PRO A 1 50  ? 15.815 22.430 5.668   1.00 11.73 ? 50  PRO A N   1 
ATOM   390  C CA  . PRO A 1 50  ? 14.766 22.370 4.644   1.00 11.45 ? 50  PRO A CA  1 
ATOM   391  C C   . PRO A 1 50  ? 14.641 23.669 3.837   1.00 11.14 ? 50  PRO A C   1 
ATOM   392  O O   . PRO A 1 50  ? 14.154 23.649 2.709   1.00 11.59 ? 50  PRO A O   1 
ATOM   393  C CB  . PRO A 1 50  ? 13.496 22.063 5.453   1.00 11.53 ? 50  PRO A CB  1 
ATOM   394  C CG  . PRO A 1 50  ? 13.765 22.607 6.796   1.00 11.62 ? 50  PRO A CG  1 
ATOM   395  C CD  . PRO A 1 50  ? 15.246 22.359 7.028   1.00 11.93 ? 50  PRO A CD  1 
ATOM   396  N N   . ALA A 1 51  ? 15.107 24.789 4.391   1.00 11.43 ? 51  ALA A N   1 
ATOM   397  C CA  . ALA A 1 51  ? 15.115 26.036 3.599   1.00 12.27 ? 51  ALA A CA  1 
ATOM   398  C C   . ALA A 1 51  ? 16.012 25.923 2.356   1.00 12.01 ? 51  ALA A C   1 
ATOM   399  O O   . ALA A 1 51  ? 15.627 26.317 1.244   1.00 12.52 ? 51  ALA A O   1 
ATOM   400  C CB  . ALA A 1 51  ? 15.513 27.223 4.461   1.00 12.05 ? 51  ALA A CB  1 
ATOM   401  N N   . ILE A 1 52  ? 17.205 25.361 2.539   1.00 12.06 ? 52  ILE A N   1 
ATOM   402  C CA  . ILE A 1 52  ? 18.140 25.150 1.430   1.00 11.87 ? 52  ILE A CA  1 
ATOM   403  C C   . ILE A 1 52  ? 17.562 24.116 0.465   1.00 11.71 ? 52  ILE A C   1 
ATOM   404  O O   . ILE A 1 52  ? 17.582 24.315 -0.742  1.00 12.24 ? 52  ILE A O   1 
ATOM   405  C CB  . ILE A 1 52  ? 19.531 24.709 1.957   1.00 12.25 ? 52  ILE A CB  1 
ATOM   406  C CG1 . ILE A 1 52  ? 20.184 25.849 2.771   1.00 12.39 ? 52  ILE A CG1 1 
ATOM   407  C CG2 . ILE A 1 52  ? 20.428 24.230 0.806   1.00 12.66 ? 52  ILE A CG2 1 
ATOM   408  C CD1 . ILE A 1 52  ? 21.395 25.391 3.630   1.00 13.19 ? 52  ILE A CD1 1 
ATOM   409  N N   . ALA A 1 53  ? 17.021 23.023 1.006   1.00 11.45 ? 53  ALA A N   1 
ATOM   410  C CA  . ALA A 1 53  ? 16.408 22.001 0.148   1.00 11.69 ? 53  ALA A CA  1 
ATOM   411  C C   . ALA A 1 53  ? 15.239 22.561 -0.662  1.00 12.03 ? 53  ALA A C   1 
ATOM   412  O O   . ALA A 1 53  ? 15.087 22.236 -1.848  1.00 12.49 ? 53  ALA A O   1 
ATOM   413  C CB  . ALA A 1 53  ? 15.958 20.792 0.974   1.00 12.79 ? 53  ALA A CB  1 
ATOM   414  N N   . PHE A 1 54  ? 14.423 23.410 -0.039  1.00 12.85 ? 54  PHE A N   1 
ATOM   415  C CA  . PHE A 1 54  ? 13.331 24.073 -0.760  1.00 13.18 ? 54  PHE A CA  1 
ATOM   416  C C   . PHE A 1 54  ? 13.869 24.851 -1.966  1.00 13.32 ? 54  PHE A C   1 
ATOM   417  O O   . PHE A 1 54  ? 13.345 24.740 -3.080  1.00 12.69 ? 54  PHE A O   1 
ATOM   418  C CB  . PHE A 1 54  ? 12.565 24.995 0.187   1.00 13.78 ? 54  PHE A CB  1 
ATOM   419  C CG  . PHE A 1 54  ? 11.615 25.982 -0.525  1.00 14.37 ? 54  PHE A CG  1 
ATOM   420  C CD1 . PHE A 1 54  ? 10.329 25.575 -0.893  1.00 13.34 ? 54  PHE A CD1 1 
ATOM   421  C CD2 . PHE A 1 54  ? 12.005 27.294 -0.774  1.00 16.44 ? 54  PHE A CD2 1 
ATOM   422  C CE1 . PHE A 1 54  ? 9.428  26.460 -1.485  1.00 14.26 ? 54  PHE A CE1 1 
ATOM   423  C CE2 . PHE A 1 54  ? 11.113 28.192 -1.399  1.00 15.11 ? 54  PHE A CE2 1 
ATOM   424  C CZ  . PHE A 1 54  ? 9.831  27.763 -1.757  1.00 14.49 ? 54  PHE A CZ  1 
ATOM   425  N N   . THR A 1 55  ? 14.926 25.622 -1.750  1.00 12.93 ? 55  THR A N   1 
ATOM   426  C CA  A THR A 1 55  ? 15.460 26.445 -2.840  0.60 13.29 ? 55  THR A CA  1 
ATOM   427  C CA  B THR A 1 55  ? 15.503 26.446 -2.811  0.40 12.93 ? 55  THR A CA  1 
ATOM   428  C C   . THR A 1 55  ? 15.970 25.584 -3.988  1.00 13.11 ? 55  THR A C   1 
ATOM   429  O O   . THR A 1 55  ? 15.792 25.941 -5.159  1.00 12.75 ? 55  THR A O   1 
ATOM   430  C CB  A THR A 1 55  ? 16.562 27.428 -2.388  0.60 13.33 ? 55  THR A CB  1 
ATOM   431  C CB  B THR A 1 55  ? 16.665 27.298 -2.261  0.40 12.87 ? 55  THR A CB  1 
ATOM   432  O OG1 A THR A 1 55  ? 17.736 26.707 -1.994  0.60 14.54 ? 55  THR A OG1 1 
ATOM   433  O OG1 B THR A 1 55  ? 16.181 28.136 -1.202  0.40 13.09 ? 55  THR A OG1 1 
ATOM   434  C CG2 A THR A 1 55  ? 16.077 28.317 -1.244  0.60 13.60 ? 55  THR A CG2 1 
ATOM   435  C CG2 B THR A 1 55  ? 17.267 28.170 -3.351  0.40 12.24 ? 55  THR A CG2 1 
ATOM   436  N N   . MET A 1 56  ? 16.565 24.436 -3.675  1.00 12.75 ? 56  MET A N   1 
ATOM   437  C CA  A MET A 1 56  ? 17.098 23.582 -4.731  0.60 13.18 ? 56  MET A CA  1 
ATOM   438  C CA  B MET A 1 56  ? 17.102 23.571 -4.726  0.40 12.99 ? 56  MET A CA  1 
ATOM   439  C C   . MET A 1 56  ? 16.010 22.762 -5.423  1.00 12.99 ? 56  MET A C   1 
ATOM   440  O O   . MET A 1 56  ? 16.050 22.580 -6.654  1.00 13.04 ? 56  MET A O   1 
ATOM   441  C CB  A MET A 1 56  ? 18.239 22.712 -4.205  0.60 13.37 ? 56  MET A CB  1 
ATOM   442  C CB  B MET A 1 56  ? 18.215 22.675 -4.183  0.40 13.10 ? 56  MET A CB  1 
ATOM   443  C CG  A MET A 1 56  ? 19.439 23.528 -3.679  0.60 14.50 ? 56  MET A CG  1 
ATOM   444  C CG  B MET A 1 56  ? 19.436 23.458 -3.701  0.40 13.19 ? 56  MET A CG  1 
ATOM   445  S SD  A MET A 1 56  ? 20.033 24.875 -4.748  0.60 19.20 ? 56  MET A SD  1 
ATOM   446  S SD  B MET A 1 56  ? 20.326 24.341 -5.007  0.40 14.04 ? 56  MET A SD  1 
ATOM   447  C CE  A MET A 1 56  ? 20.340 24.032 -6.289  0.60 17.69 ? 56  MET A CE  1 
ATOM   448  C CE  B MET A 1 56  ? 21.315 25.450 -4.002  0.40 14.71 ? 56  MET A CE  1 
ATOM   449  N N   . TYR A 1 57  ? 15.034 22.272 -4.648  1.00 12.97 ? 57  TYR A N   1 
ATOM   450  C CA  . TYR A 1 57  ? 13.881 21.589 -5.242  1.00 13.14 ? 57  TYR A CA  1 
ATOM   451  C C   . TYR A 1 57  ? 13.148 22.551 -6.185  1.00 13.23 ? 57  TYR A C   1 
ATOM   452  O O   . TYR A 1 57  ? 12.751 22.182 -7.293  1.00 13.82 ? 57  TYR A O   1 
ATOM   453  C CB  . TYR A 1 57  ? 12.937 21.029 -4.163  1.00 13.13 ? 57  TYR A CB  1 
ATOM   454  C CG  . TYR A 1 57  ? 13.268 19.595 -3.847  1.00 12.74 ? 57  TYR A CG  1 
ATOM   455  C CD1 . TYR A 1 57  ? 12.670 18.558 -4.567  1.00 11.40 ? 57  TYR A CD1 1 
ATOM   456  C CD2 . TYR A 1 57  ? 14.190 19.269 -2.849  1.00 12.91 ? 57  TYR A CD2 1 
ATOM   457  C CE1 . TYR A 1 57  ? 12.981 17.210 -4.292  1.00 12.29 ? 57  TYR A CE1 1 
ATOM   458  C CE2 . TYR A 1 57  ? 14.514 17.931 -2.572  1.00 12.19 ? 57  TYR A CE2 1 
ATOM   459  C CZ  . TYR A 1 57  ? 13.905 16.914 -3.301  1.00 13.79 ? 57  TYR A CZ  1 
ATOM   460  O OH  . TYR A 1 57  ? 14.216 15.594 -3.064  1.00 12.86 ? 57  TYR A OH  1 
ATOM   461  N N   . LEU A 1 58  ? 12.986 23.788 -5.728  1.00 13.20 ? 58  LEU A N   1 
ATOM   462  C CA  . LEU A 1 58  ? 12.300 24.787 -6.529  1.00 13.91 ? 58  LEU A CA  1 
ATOM   463  C C   . LEU A 1 58  ? 13.071 25.069 -7.813  1.00 13.69 ? 58  LEU A C   1 
ATOM   464  O O   . LEU A 1 58  ? 12.481 25.127 -8.892  1.00 13.61 ? 58  LEU A O   1 
ATOM   465  C CB  . LEU A 1 58  ? 12.071 26.058 -5.706  1.00 13.37 ? 58  LEU A CB  1 
ATOM   466  C CG  . LEU A 1 58  ? 11.338 27.201 -6.407  1.00 15.68 ? 58  LEU A CG  1 
ATOM   467  C CD1 . LEU A 1 58  ? 10.011 26.738 -6.993  1.00 16.41 ? 58  LEU A CD1 1 
ATOM   468  C CD2 . LEU A 1 58  ? 11.153 28.345 -5.393  1.00 15.71 ? 58  LEU A CD2 1 
ATOM   469  N N   . SER A 1 59  ? 14.388 25.219 -7.691  1.00 13.56 ? 59  SER A N   1 
ATOM   470  C CA  A SER A 1 59  ? 15.260 25.448 -8.849  0.70 13.60 ? 59  SER A CA  1 
ATOM   471  C CA  B SER A 1 59  ? 15.240 25.456 -8.859  0.30 13.80 ? 59  SER A CA  1 
ATOM   472  C C   . SER A 1 59  ? 15.103 24.314 -9.866  1.00 13.45 ? 59  SER A C   1 
ATOM   473  O O   . SER A 1 59  ? 14.920 24.553 -11.067 1.00 13.88 ? 59  SER A O   1 
ATOM   474  C CB  A SER A 1 59  ? 16.720 25.572 -8.400  0.70 13.76 ? 59  SER A CB  1 
ATOM   475  C CB  B SER A 1 59  ? 16.702 25.638 -8.449  0.30 13.90 ? 59  SER A CB  1 
ATOM   476  O OG  A SER A 1 59  ? 16.930 26.787 -7.691  0.70 13.82 ? 59  SER A OG  1 
ATOM   477  O OG  B SER A 1 59  ? 17.249 24.428 -7.970  0.30 14.92 ? 59  SER A OG  1 
ATOM   478  N N   . MET A 1 60  ? 15.157 23.069 -9.380  1.00 14.04 ? 60  MET A N   1 
ATOM   479  C CA  . MET A 1 60  ? 14.997 21.905 -10.267 1.00 14.22 ? 60  MET A CA  1 
ATOM   480  C C   . MET A 1 60  ? 13.606 21.847 -10.905 1.00 14.32 ? 60  MET A C   1 
ATOM   481  O O   . MET A 1 60  ? 13.465 21.524 -12.090 1.00 15.18 ? 60  MET A O   1 
ATOM   482  C CB  . MET A 1 60  ? 15.309 20.600 -9.533  1.00 14.64 ? 60  MET A CB  1 
ATOM   483  C CG  . MET A 1 60  ? 16.779 20.497 -9.154  1.00 13.25 ? 60  MET A CG  1 
ATOM   484  S SD  . MET A 1 60  ? 17.227 18.865 -8.512  1.00 15.74 ? 60  MET A SD  1 
ATOM   485  C CE  . MET A 1 60  ? 16.606 18.976 -6.827  1.00 16.49 ? 60  MET A CE  1 
ATOM   486  N N   . LEU A 1 61  ? 12.581 22.167 -10.119 1.00 14.64 ? 61  LEU A N   1 
ATOM   487  C CA  . LEU A 1 61  ? 11.214 22.204 -10.621 1.00 15.17 ? 61  LEU A CA  1 
ATOM   488  C C   . LEU A 1 61  ? 11.123 23.154 -11.820 1.00 15.49 ? 61  LEU A C   1 
ATOM   489  O O   . LEU A 1 61  ? 10.465 22.835 -12.815 1.00 16.61 ? 61  LEU A O   1 
ATOM   490  C CB  . LEU A 1 61  ? 10.238 22.629 -9.501  1.00 14.90 ? 61  LEU A CB  1 
ATOM   491  C CG  . LEU A 1 61  ? 8.752  22.778 -9.857  1.00 14.87 ? 61  LEU A CG  1 
ATOM   492  C CD1 . LEU A 1 61  ? 8.156  21.486 -10.422 1.00 15.43 ? 61  LEU A CD1 1 
ATOM   493  C CD2 . LEU A 1 61  ? 7.953  23.259 -8.640  1.00 15.14 ? 61  LEU A CD2 1 
ATOM   494  N N   . LEU A 1 62  ? 11.802 24.297 -11.717 1.00 15.48 ? 62  LEU A N   1 
ATOM   495  C CA  . LEU A 1 62  ? 11.770 25.340 -12.753 1.00 16.37 ? 62  LEU A CA  1 
ATOM   496  C C   . LEU A 1 62  ? 12.805 25.125 -13.858 1.00 16.93 ? 62  LEU A C   1 
ATOM   497  O O   . LEU A 1 62  ? 13.017 26.016 -14.691 1.00 17.26 ? 62  LEU A O   1 
ATOM   498  C CB  . LEU A 1 62  ? 11.928 26.721 -12.122 1.00 16.35 ? 62  LEU A CB  1 
ATOM   499  C CG  . LEU A 1 62  ? 10.771 27.173 -11.229 1.00 17.50 ? 62  LEU A CG  1 
ATOM   500  C CD1 . LEU A 1 62  ? 11.133 28.479 -10.540 1.00 18.23 ? 62  LEU A CD1 1 
ATOM   501  C CD2 . LEU A 1 62  ? 9.460  27.318 -12.008 1.00 20.12 ? 62  LEU A CD2 1 
ATOM   502  N N   . GLY A 1 63  ? 13.449 23.960 -13.854 1.00 16.82 ? 63  GLY A N   1 
ATOM   503  C CA  . GLY A 1 63  ? 14.282 23.539 -14.993 1.00 17.15 ? 63  GLY A CA  1 
ATOM   504  C C   . GLY A 1 63  ? 15.770 23.833 -14.881 1.00 17.47 ? 63  GLY A C   1 
ATOM   505  O O   . GLY A 1 63  ? 16.515 23.688 -15.866 1.00 18.38 ? 63  GLY A O   1 
ATOM   506  N N   . TYR A 1 64  ? 16.216 24.241 -13.695 1.00 17.41 ? 64  TYR A N   1 
ATOM   507  C CA  . TYR A 1 64  ? 17.632 24.493 -13.453 1.00 18.00 ? 64  TYR A CA  1 
ATOM   508  C C   . TYR A 1 64  ? 18.279 23.304 -12.755 1.00 18.09 ? 64  TYR A C   1 
ATOM   509  O O   . TYR A 1 64  ? 17.579 22.410 -12.283 1.00 17.63 ? 64  TYR A O   1 
ATOM   510  C CB  . TYR A 1 64  ? 17.831 25.762 -12.621 1.00 18.31 ? 64  TYR A CB  1 
ATOM   511  C CG  . TYR A 1 64  ? 17.504 26.995 -13.399 1.00 19.09 ? 64  TYR A CG  1 
ATOM   512  C CD1 . TYR A 1 64  ? 16.195 27.448 -13.486 1.00 19.03 ? 64  TYR A CD1 1 
ATOM   513  C CD2 . TYR A 1 64  ? 18.498 27.687 -14.084 1.00 19.76 ? 64  TYR A CD2 1 
ATOM   514  C CE1 . TYR A 1 64  ? 15.875 28.573 -14.221 1.00 20.01 ? 64  TYR A CE1 1 
ATOM   515  C CE2 . TYR A 1 64  ? 18.196 28.821 -14.829 1.00 21.11 ? 64  TYR A CE2 1 
ATOM   516  C CZ  . TYR A 1 64  ? 16.878 29.258 -14.888 1.00 21.79 ? 64  TYR A CZ  1 
ATOM   517  O OH  . TYR A 1 64  ? 16.554 30.373 -15.619 1.00 21.26 ? 64  TYR A OH  1 
ATOM   518  N N   . GLY A 1 65  ? 19.611 23.305 -12.703 1.00 18.49 ? 65  GLY A N   1 
ATOM   519  C CA  . GLY A 1 65  ? 20.374 22.258 -12.016 1.00 18.88 ? 65  GLY A CA  1 
ATOM   520  C C   . GLY A 1 65  ? 20.334 20.894 -12.686 1.00 19.21 ? 65  GLY A C   1 
ATOM   521  O O   . GLY A 1 65  ? 20.523 19.873 -12.027 1.00 18.40 ? 65  GLY A O   1 
ATOM   522  N N   . LEU A 1 66  ? 20.087 20.880 -13.994 1.00 19.48 ? 66  LEU A N   1 
ATOM   523  C CA  . LEU A 1 66  ? 20.055 19.656 -14.786 1.00 20.81 ? 66  LEU A CA  1 
ATOM   524  C C   . LEU A 1 66  ? 21.007 19.812 -15.954 1.00 21.02 ? 66  LEU A C   1 
ATOM   525  O O   . LEU A 1 66  ? 20.969 20.809 -16.670 1.00 21.11 ? 66  LEU A O   1 
ATOM   526  C CB  . LEU A 1 66  ? 18.641 19.396 -15.309 1.00 20.73 ? 66  LEU A CB  1 
ATOM   527  C CG  . LEU A 1 66  ? 18.389 18.208 -16.245 1.00 21.99 ? 66  LEU A CG  1 
ATOM   528  C CD1 . LEU A 1 66  ? 18.690 16.870 -15.585 1.00 22.95 ? 66  LEU A CD1 1 
ATOM   529  C CD2 . LEU A 1 66  ? 16.949 18.234 -16.748 1.00 22.44 ? 66  LEU A CD2 1 
ATOM   530  N N   . THR A 1 67  ? 21.871 18.826 -16.139 1.00 21.47 ? 67  THR A N   1 
ATOM   531  C CA  . THR A 1 67  ? 22.772 18.833 -17.284 1.00 21.58 ? 67  THR A CA  1 
ATOM   532  C C   . THR A 1 67  ? 22.795 17.457 -17.929 1.00 21.98 ? 67  THR A C   1 
ATOM   533  O O   . THR A 1 67  ? 22.443 16.468 -17.292 1.00 22.06 ? 67  THR A O   1 
ATOM   534  C CB  . THR A 1 67  ? 24.184 19.300 -16.882 1.00 22.07 ? 67  THR A CB  1 
ATOM   535  O OG1 . THR A 1 67  ? 24.946 19.582 -18.066 1.00 22.34 ? 67  THR A OG1 1 
ATOM   536  C CG2 . THR A 1 67  ? 24.915 18.247 -16.020 1.00 22.27 ? 67  THR A CG2 1 
ATOM   537  N N   . MET A 1 68  ? 23.197 17.400 -19.197 1.00 21.39 ? 68  MET A N   1 
ATOM   538  C CA  . MET A 1 68  ? 23.331 16.134 -19.911 1.00 21.69 ? 68  MET A CA  1 
ATOM   539  C C   . MET A 1 68  ? 24.788 15.699 -19.832 1.00 20.91 ? 68  MET A C   1 
ATOM   540  O O   . MET A 1 68  ? 25.702 16.506 -20.039 1.00 21.45 ? 68  MET A O   1 
ATOM   541  C CB  . MET A 1 68  ? 22.880 16.268 -21.377 1.00 22.58 ? 68  MET A CB  1 
ATOM   542  C CG  . MET A 1 68  ? 21.408 16.693 -21.566 1.00 25.57 ? 68  MET A CG  1 
ATOM   543  S SD  . MET A 1 68  ? 20.143 15.644 -20.783 1.00 32.16 ? 68  MET A SD  1 
ATOM   544  C CE  . MET A 1 68  ? 20.256 14.148 -21.746 1.00 30.65 ? 68  MET A CE  1 
ATOM   545  N N   . VAL A 1 69  ? 25.007 14.434 -19.487 1.00 19.48 ? 69  VAL A N   1 
ATOM   546  C CA  . VAL A 1 69  ? 26.353 13.890 -19.429 1.00 18.02 ? 69  VAL A CA  1 
ATOM   547  C C   . VAL A 1 69  ? 26.441 12.666 -20.339 1.00 17.85 ? 69  VAL A C   1 
ATOM   548  O O   . VAL A 1 69  ? 25.647 11.738 -20.202 1.00 17.73 ? 69  VAL A O   1 
ATOM   549  C CB  . VAL A 1 69  ? 26.730 13.481 -17.992 1.00 17.56 ? 69  VAL A CB  1 
ATOM   550  C CG1 . VAL A 1 69  ? 28.144 12.936 -17.956 1.00 18.27 ? 69  VAL A CG1 1 
ATOM   551  C CG2 . VAL A 1 69  ? 26.569 14.659 -17.021 1.00 17.00 ? 69  VAL A CG2 1 
ATOM   552  N N   . PRO A 1 70  ? 27.406 12.659 -21.277 1.00 17.65 ? 70  PRO A N   1 
ATOM   553  C CA  . PRO A 1 70  ? 27.544 11.478 -22.123 1.00 17.66 ? 70  PRO A CA  1 
ATOM   554  C C   . PRO A 1 70  ? 28.281 10.345 -21.415 1.00 17.75 ? 70  PRO A C   1 
ATOM   555  O O   . PRO A 1 70  ? 29.390 10.541 -20.924 1.00 18.00 ? 70  PRO A O   1 
ATOM   556  C CB  . PRO A 1 70  ? 28.373 12.001 -23.300 1.00 17.57 ? 70  PRO A CB  1 
ATOM   557  C CG  . PRO A 1 70  ? 29.233 13.055 -22.692 1.00 17.81 ? 70  PRO A CG  1 
ATOM   558  C CD  . PRO A 1 70  ? 28.386 13.711 -21.622 1.00 17.35 ? 70  PRO A CD  1 
ATOM   559  N N   . PHE A 1 71  ? 27.657 9.170  -21.353 1.00 17.96 ? 71  PHE A N   1 
ATOM   560  C CA  . PHE A 1 71  ? 28.349 7.951  -20.922 1.00 18.07 ? 71  PHE A CA  1 
ATOM   561  C C   . PHE A 1 71  ? 27.557 6.723  -21.349 1.00 18.91 ? 71  PHE A C   1 
ATOM   562  O O   . PHE A 1 71  ? 26.340 6.797  -21.535 1.00 18.96 ? 71  PHE A O   1 
ATOM   563  C CB  . PHE A 1 71  ? 28.645 7.944  -19.410 1.00 17.18 ? 71  PHE A CB  1 
ATOM   564  C CG  . PHE A 1 71  ? 27.424 8.000  -18.519 1.00 16.75 ? 71  PHE A CG  1 
ATOM   565  C CD1 . PHE A 1 71  ? 26.792 6.827  -18.112 1.00 15.55 ? 71  PHE A CD1 1 
ATOM   566  C CD2 . PHE A 1 71  ? 26.952 9.217  -18.029 1.00 16.34 ? 71  PHE A CD2 1 
ATOM   567  C CE1 . PHE A 1 71  ? 25.686 6.867  -17.258 1.00 16.26 ? 71  PHE A CE1 1 
ATOM   568  C CE2 . PHE A 1 71  ? 25.859 9.262  -17.171 1.00 14.73 ? 71  PHE A CE2 1 
ATOM   569  C CZ  . PHE A 1 71  ? 25.220 8.079  -16.790 1.00 15.31 ? 71  PHE A CZ  1 
ATOM   570  N N   . GLY A 1 72  ? 28.260 5.611  -21.531 1.00 20.36 ? 72  GLY A N   1 
ATOM   571  C CA  . GLY A 1 72  ? 27.633 4.383  -21.996 1.00 21.99 ? 72  GLY A CA  1 
ATOM   572  C C   . GLY A 1 72  ? 26.996 4.551  -23.364 1.00 23.46 ? 72  GLY A C   1 
ATOM   573  O O   . GLY A 1 72  ? 26.025 3.868  -23.685 1.00 24.03 ? 72  GLY A O   1 
ATOM   574  N N   . GLY A 1 73  ? 27.540 5.470  -24.162 1.00 24.14 ? 73  GLY A N   1 
ATOM   575  C CA  . GLY A 1 73  ? 27.082 5.675  -25.537 1.00 25.61 ? 73  GLY A CA  1 
ATOM   576  C C   . GLY A 1 73  ? 25.827 6.513  -25.704 1.00 26.68 ? 73  GLY A C   1 
ATOM   577  O O   . GLY A 1 73  ? 25.283 6.607  -26.809 1.00 26.94 ? 73  GLY A O   1 
ATOM   578  N N   . GLU A 1 74  ? 25.359 7.127  -24.616 1.00 26.95 ? 74  GLU A N   1 
ATOM   579  C CA  . GLU A 1 74  ? 24.155 7.950  -24.675 1.00 27.78 ? 74  GLU A CA  1 
ATOM   580  C C   . GLU A 1 74  ? 24.267 9.210  -23.827 1.00 26.80 ? 74  GLU A C   1 
ATOM   581  O O   . GLU A 1 74  ? 25.184 9.339  -23.018 1.00 26.37 ? 74  GLU A O   1 
ATOM   582  C CB  . GLU A 1 74  ? 22.908 7.143  -24.298 1.00 27.83 ? 74  GLU A CB  1 
ATOM   583  C CG  . GLU A 1 74  ? 22.837 6.663  -22.856 1.00 29.95 ? 74  GLU A CG  1 
ATOM   584  C CD  . GLU A 1 74  ? 21.523 5.944  -22.525 1.00 30.87 ? 74  GLU A CD  1 
ATOM   585  O OE1 . GLU A 1 74  ? 20.710 5.712  -23.448 1.00 35.16 ? 74  GLU A OE1 1 
ATOM   586  O OE2 . GLU A 1 74  ? 21.310 5.614  -21.333 1.00 34.72 ? 74  GLU A OE2 1 
ATOM   587  N N   . GLN A 1 75  ? 23.349 10.146 -24.063 1.00 26.58 ? 75  GLN A N   1 
ATOM   588  C CA  . GLN A 1 75  ? 23.271 11.397 -23.309 1.00 26.19 ? 75  GLN A CA  1 
ATOM   589  C C   . GLN A 1 75  ? 22.335 11.194 -22.138 1.00 25.32 ? 75  GLN A C   1 
ATOM   590  O O   . GLN A 1 75  ? 21.158 10.868 -22.321 1.00 25.76 ? 75  GLN A O   1 
ATOM   591  C CB  . GLN A 1 75  ? 22.758 12.535 -24.193 1.00 26.82 ? 75  GLN A CB  1 
ATOM   592  C CG  . GLN A 1 75  ? 23.705 12.936 -25.327 1.00 29.13 ? 75  GLN A CG  1 
ATOM   593  C CD  . GLN A 1 75  ? 24.966 13.627 -24.839 1.00 32.35 ? 75  GLN A CD  1 
ATOM   594  O OE1 . GLN A 1 75  ? 25.041 14.092 -23.699 1.00 35.70 ? 75  GLN A OE1 1 
ATOM   595  N NE2 . GLN A 1 75  ? 25.966 13.706 -25.711 1.00 34.72 ? 75  GLN A NE2 1 
ATOM   596  N N   . ASN A 1 76  ? 22.860 11.403 -20.935 1.00 23.59 ? 76  ASN A N   1 
ATOM   597  C CA  . ASN A 1 76  ? 22.142 11.070 -19.712 1.00 22.88 ? 76  ASN A CA  1 
ATOM   598  C C   . ASN A 1 76  ? 21.807 12.322 -18.907 1.00 22.18 ? 76  ASN A C   1 
ATOM   599  O O   . ASN A 1 76  ? 22.693 13.128 -18.644 1.00 21.08 ? 76  ASN A O   1 
ATOM   600  C CB  . ASN A 1 76  ? 22.998 10.135 -18.873 1.00 22.79 ? 76  ASN A CB  1 
ATOM   601  C CG  . ASN A 1 76  ? 23.422 8.886  -19.636 1.00 24.20 ? 76  ASN A CG  1 
ATOM   602  O OD1 . ASN A 1 76  ? 24.539 8.796  -20.161 1.00 24.50 ? 76  ASN A OD1 1 
ATOM   603  N ND2 . ASN A 1 76  ? 22.531 7.911  -19.689 1.00 25.05 ? 76  ASN A ND2 1 
ATOM   604  N N   . PRO A 1 77  ? 20.529 12.484 -18.513 1.00 21.90 ? 77  PRO A N   1 
ATOM   605  C CA  . PRO A 1 77  ? 20.122 13.646 -17.715 1.00 21.35 ? 77  PRO A CA  1 
ATOM   606  C C   . PRO A 1 77  ? 20.544 13.517 -16.248 1.00 20.30 ? 77  PRO A C   1 
ATOM   607  O O   . PRO A 1 77  ? 20.131 12.582 -15.563 1.00 21.44 ? 77  PRO A O   1 
ATOM   608  C CB  . PRO A 1 77  ? 18.591 13.642 -17.843 1.00 21.44 ? 77  PRO A CB  1 
ATOM   609  C CG  . PRO A 1 77  ? 18.231 12.217 -18.070 1.00 22.12 ? 77  PRO A CG  1 
ATOM   610  C CD  . PRO A 1 77  ? 19.393 11.591 -18.818 1.00 22.33 ? 77  PRO A CD  1 
ATOM   611  N N   . ILE A 1 78  ? 21.360 14.457 -15.777 1.00 18.56 ? 78  ILE A N   1 
ATOM   612  C CA  . ILE A 1 78  ? 21.900 14.400 -14.419 1.00 16.98 ? 78  ILE A CA  1 
ATOM   613  C C   . ILE A 1 78  ? 21.531 15.676 -13.675 1.00 16.74 ? 78  ILE A C   1 
ATOM   614  O O   . ILE A 1 78  ? 21.905 16.778 -14.085 1.00 15.81 ? 78  ILE A O   1 
ATOM   615  C CB  . ILE A 1 78  ? 23.444 14.251 -14.433 1.00 16.95 ? 78  ILE A CB  1 
ATOM   616  C CG1 . ILE A 1 78  ? 23.855 12.967 -15.179 1.00 16.66 ? 78  ILE A CG1 1 
ATOM   617  C CG2 . ILE A 1 78  ? 24.029 14.323 -12.993 1.00 17.26 ? 78  ILE A CG2 1 
ATOM   618  C CD1 . ILE A 1 78  ? 23.484 11.666 -14.462 1.00 15.15 ? 78  ILE A CD1 1 
ATOM   619  N N   . TYR A 1 79  ? 20.790 15.514 -12.580 1.00 16.43 ? 79  TYR A N   1 
ATOM   620  C CA  . TYR A 1 79  ? 20.457 16.631 -11.690 1.00 16.64 ? 79  TYR A CA  1 
ATOM   621  C C   . TYR A 1 79  ? 21.628 16.945 -10.769 1.00 16.71 ? 79  TYR A C   1 
ATOM   622  O O   . TYR A 1 79  ? 21.853 16.246 -9.775  1.00 17.72 ? 79  TYR A O   1 
ATOM   623  C CB  . TYR A 1 79  ? 19.207 16.317 -10.861 1.00 16.88 ? 79  TYR A CB  1 
ATOM   624  C CG  . TYR A 1 79  ? 17.910 16.508 -11.627 1.00 16.17 ? 79  TYR A CG  1 
ATOM   625  C CD1 . TYR A 1 79  ? 17.440 17.789 -11.921 1.00 16.20 ? 79  TYR A CD1 1 
ATOM   626  C CD2 . TYR A 1 79  ? 17.150 15.411 -12.052 1.00 17.59 ? 79  TYR A CD2 1 
ATOM   627  C CE1 . TYR A 1 79  ? 16.247 17.986 -12.621 1.00 16.35 ? 79  TYR A CE1 1 
ATOM   628  C CE2 . TYR A 1 79  ? 15.948 15.596 -12.748 1.00 19.24 ? 79  TYR A CE2 1 
ATOM   629  C CZ  . TYR A 1 79  ? 15.509 16.883 -13.034 1.00 17.54 ? 79  TYR A CZ  1 
ATOM   630  O OH  . TYR A 1 79  ? 14.335 17.089 -13.739 1.00 17.79 ? 79  TYR A OH  1 
ATOM   631  N N   . TRP A 1 80  ? 22.380 17.984 -11.109 1.00 16.01 ? 80  TRP A N   1 
ATOM   632  C CA  . TRP A 1 80  ? 23.509 18.383 -10.269 1.00 15.88 ? 80  TRP A CA  1 
ATOM   633  C C   . TRP A 1 80  ? 23.092 19.268 -9.090  1.00 15.44 ? 80  TRP A C   1 
ATOM   634  O O   . TRP A 1 80  ? 23.835 19.390 -8.117  1.00 14.57 ? 80  TRP A O   1 
ATOM   635  C CB  . TRP A 1 80  ? 24.643 19.015 -11.097 1.00 17.11 ? 80  TRP A CB  1 
ATOM   636  C CG  . TRP A 1 80  ? 24.264 20.273 -11.820 1.00 17.37 ? 80  TRP A CG  1 
ATOM   637  C CD1 . TRP A 1 80  ? 23.765 20.373 -13.092 1.00 19.18 ? 80  TRP A CD1 1 
ATOM   638  C CD2 . TRP A 1 80  ? 24.368 21.615 -11.322 1.00 18.76 ? 80  TRP A CD2 1 
ATOM   639  N NE1 . TRP A 1 80  ? 23.558 21.691 -13.412 1.00 20.05 ? 80  TRP A NE1 1 
ATOM   640  C CE2 . TRP A 1 80  ? 23.908 22.475 -12.345 1.00 19.69 ? 80  TRP A CE2 1 
ATOM   641  C CE3 . TRP A 1 80  ? 24.796 22.170 -10.112 1.00 19.97 ? 80  TRP A CE3 1 
ATOM   642  C CZ2 . TRP A 1 80  ? 23.876 23.866 -12.198 1.00 20.04 ? 80  TRP A CZ2 1 
ATOM   643  C CZ3 . TRP A 1 80  ? 24.757 23.564 -9.966  1.00 20.85 ? 80  TRP A CZ3 1 
ATOM   644  C CH2 . TRP A 1 80  ? 24.301 24.386 -11.009 1.00 20.17 ? 80  TRP A CH2 1 
ATOM   645  N N   . ALA A 1 81  ? 21.904 19.869 -9.153  1.00 15.34 ? 81  ALA A N   1 
ATOM   646  C CA  . ALA A 1 81  ? 21.445 20.756 -8.073  1.00 15.24 ? 81  ALA A CA  1 
ATOM   647  C C   . ALA A 1 81  ? 21.337 20.036 -6.724  1.00 14.84 ? 81  ALA A C   1 
ATOM   648  O O   . ALA A 1 81  ? 21.448 20.661 -5.653  1.00 14.87 ? 81  ALA A O   1 
ATOM   649  C CB  . ALA A 1 81  ? 20.107 21.384 -8.427  1.00 16.42 ? 81  ALA A CB  1 
ATOM   650  N N   . ARG A 1 82  ? 21.108 18.729 -6.774  1.00 14.23 ? 82  ARG A N   1 
ATOM   651  C CA  . ARG A 1 82  ? 21.003 17.906 -5.564  1.00 13.33 ? 82  ARG A CA  1 
ATOM   652  C C   . ARG A 1 82  ? 22.266 18.083 -4.715  1.00 13.23 ? 82  ARG A C   1 
ATOM   653  O O   . ARG A 1 82  ? 22.202 18.136 -3.490  1.00 12.88 ? 82  ARG A O   1 
ATOM   654  C CB  . ARG A 1 82  ? 20.872 16.419 -5.916  1.00 13.81 ? 82  ARG A CB  1 
ATOM   655  C CG  . ARG A 1 82  ? 19.665 16.055 -6.745  1.00 14.31 ? 82  ARG A CG  1 
ATOM   656  C CD  . ARG A 1 82  ? 19.395 14.561 -6.591  1.00 14.34 ? 82  ARG A CD  1 
ATOM   657  N NE  . ARG A 1 82  ? 18.410 14.102 -7.575  1.00 15.48 ? 82  ARG A NE  1 
ATOM   658  C CZ  . ARG A 1 82  ? 17.095 14.162 -7.388  1.00 17.84 ? 82  ARG A CZ  1 
ATOM   659  N NH1 . ARG A 1 82  ? 16.601 14.673 -6.274  1.00 20.05 ? 82  ARG A NH1 1 
ATOM   660  N NH2 . ARG A 1 82  ? 16.277 13.700 -8.329  1.00 19.85 ? 82  ARG A NH2 1 
ATOM   661  N N   . TYR A 1 83  ? 23.418 18.153 -5.386  1.00 12.93 ? 83  TYR A N   1 
ATOM   662  C CA  . TYR A 1 83  ? 24.715 18.248 -4.693  1.00 13.28 ? 83  TYR A CA  1 
ATOM   663  C C   . TYR A 1 83  ? 24.930 19.610 -4.068  1.00 13.00 ? 83  TYR A C   1 
ATOM   664  O O   . TYR A 1 83  ? 25.612 19.725 -3.046  1.00 13.49 ? 83  TYR A O   1 
ATOM   665  C CB  . TYR A 1 83  ? 25.881 17.851 -5.623  1.00 12.87 ? 83  TYR A CB  1 
ATOM   666  C CG  . TYR A 1 83  ? 25.659 16.467 -6.197  1.00 12.64 ? 83  TYR A CG  1 
ATOM   667  C CD1 . TYR A 1 83  ? 26.148 15.335 -5.558  1.00 13.72 ? 83  TYR A CD1 1 
ATOM   668  C CD2 . TYR A 1 83  ? 24.887 16.296 -7.345  1.00 13.10 ? 83  TYR A CD2 1 
ATOM   669  C CE1 . TYR A 1 83  ? 25.904 14.060 -6.092  1.00 12.84 ? 83  TYR A CE1 1 
ATOM   670  C CE2 . TYR A 1 83  ? 24.631 15.044 -7.871  1.00 13.23 ? 83  TYR A CE2 1 
ATOM   671  C CZ  . TYR A 1 83  ? 25.140 13.933 -7.241  1.00 13.20 ? 83  TYR A CZ  1 
ATOM   672  O OH  . TYR A 1 83  ? 24.879 12.684 -7.768  1.00 15.38 ? 83  TYR A OH  1 
ATOM   673  N N   . ALA A 1 84  ? 24.331 20.642 -4.659  1.00 12.93 ? 84  ALA A N   1 
ATOM   674  C CA  . ALA A 1 84  ? 24.416 21.976 -4.092  1.00 13.02 ? 84  ALA A CA  1 
ATOM   675  C C   . ALA A 1 84  ? 23.622 22.048 -2.788  1.00 13.52 ? 84  ALA A C   1 
ATOM   676  O O   . ALA A 1 84  ? 24.050 22.701 -1.833  1.00 14.85 ? 84  ALA A O   1 
ATOM   677  C CB  . ALA A 1 84  ? 23.942 23.024 -5.101  1.00 13.52 ? 84  ALA A CB  1 
ATOM   678  N N   . ASP A 1 85  ? 22.496 21.339 -2.752  1.00 12.55 ? 85  ASP A N   1 
ATOM   679  C CA  . ASP A 1 85  ? 21.679 21.172 -1.541  1.00 12.38 ? 85  ASP A CA  1 
ATOM   680  C C   . ASP A 1 85  ? 22.497 20.387 -0.522  1.00 11.39 ? 85  ASP A C   1 
ATOM   681  O O   . ASP A 1 85  ? 22.852 20.900 0.554   1.00 11.72 ? 85  ASP A O   1 
ATOM   682  C CB  . ASP A 1 85  ? 20.399 20.423 -1.961  1.00 12.89 ? 85  ASP A CB  1 
ATOM   683  C CG  . ASP A 1 85  ? 19.532 19.946 -0.807  1.00 14.12 ? 85  ASP A CG  1 
ATOM   684  O OD1 . ASP A 1 85  ? 19.996 19.835 0.350   1.00 14.92 ? 85  ASP A OD1 1 
ATOM   685  O OD2 . ASP A 1 85  ? 18.350 19.641 -1.104  1.00 13.69 ? 85  ASP A OD2 1 
ATOM   686  N N   . TRP A 1 86  ? 22.888 19.178 -0.895  1.00 11.32 ? 86  TRP A N   1 
ATOM   687  C CA  . TRP A 1 86  ? 23.523 18.270 0.060   1.00 11.20 ? 86  TRP A CA  1 
ATOM   688  C C   . TRP A 1 86  ? 24.872 18.762 0.613   1.00 10.98 ? 86  TRP A C   1 
ATOM   689  O O   . TRP A 1 86  ? 25.231 18.453 1.765   1.00 11.39 ? 86  TRP A O   1 
ATOM   690  C CB  . TRP A 1 86  ? 23.699 16.902 -0.585  1.00 11.79 ? 86  TRP A CB  1 
ATOM   691  C CG  . TRP A 1 86  ? 22.439 16.224 -1.005  1.00 12.18 ? 86  TRP A CG  1 
ATOM   692  C CD1 . TRP A 1 86  ? 21.169 16.431 -0.528  1.00 11.99 ? 86  TRP A CD1 1 
ATOM   693  C CD2 . TRP A 1 86  ? 22.351 15.152 -1.943  1.00 12.70 ? 86  TRP A CD2 1 
ATOM   694  N NE1 . TRP A 1 86  ? 20.281 15.574 -1.165  1.00 12.69 ? 86  TRP A NE1 1 
ATOM   695  C CE2 . TRP A 1 86  ? 20.987 14.774 -2.029  1.00 12.40 ? 86  TRP A CE2 1 
ATOM   696  C CE3 . TRP A 1 86  ? 23.290 14.496 -2.753  1.00 12.12 ? 86  TRP A CE3 1 
ATOM   697  C CZ2 . TRP A 1 86  ? 20.540 13.751 -2.889  1.00 13.12 ? 86  TRP A CZ2 1 
ATOM   698  C CZ3 . TRP A 1 86  ? 22.842 13.493 -3.612  1.00 13.75 ? 86  TRP A CZ3 1 
ATOM   699  C CH2 . TRP A 1 86  ? 21.480 13.125 -3.660  1.00 12.49 ? 86  TRP A CH2 1 
ATOM   700  N N   . LEU A 1 87  ? 25.621 19.512 -0.193  1.00 10.96 ? 87  LEU A N   1 
ATOM   701  C CA  A LEU A 1 87  ? 26.890 20.056 0.280   0.80 10.56 ? 87  LEU A CA  1 
ATOM   702  C CA  B LEU A 1 87  ? 26.887 20.104 0.254   0.20 11.07 ? 87  LEU A CA  1 
ATOM   703  C C   . LEU A 1 87  ? 26.716 20.837 1.579   1.00 10.54 ? 87  LEU A C   1 
ATOM   704  O O   . LEU A 1 87  ? 27.594 20.775 2.455   1.00 11.68 ? 87  LEU A O   1 
ATOM   705  C CB  A LEU A 1 87  ? 27.535 20.960 -0.776  0.80 10.32 ? 87  LEU A CB  1 
ATOM   706  C CB  B LEU A 1 87  ? 27.450 21.077 -0.794  0.20 11.14 ? 87  LEU A CB  1 
ATOM   707  C CG  A LEU A 1 87  ? 28.891 21.583 -0.415  0.80 8.99  ? 87  LEU A CG  1 
ATOM   708  C CG  B LEU A 1 87  ? 28.542 20.614 -1.768  0.20 12.30 ? 87  LEU A CG  1 
ATOM   709  C CD1 A LEU A 1 87  ? 29.993 20.545 -0.265  0.80 11.82 ? 87  LEU A CD1 1 
ATOM   710  C CD1 B LEU A 1 87  ? 28.727 21.628 -2.884  0.20 13.39 ? 87  LEU A CD1 1 
ATOM   711  C CD2 A LEU A 1 87  ? 29.272 22.626 -1.480  0.80 10.92 ? 87  LEU A CD2 1 
ATOM   712  C CD2 B LEU A 1 87  ? 29.872 20.352 -1.054  0.20 12.67 ? 87  LEU A CD2 1 
ATOM   713  N N   . PHE A 1 88  ? 25.587 21.538 1.719   1.00 10.43 ? 88  PHE A N   1 
ATOM   714  C CA  . PHE A 1 88  ? 25.347 22.327 2.934   1.00 11.14 ? 88  PHE A CA  1 
ATOM   715  C C   . PHE A 1 88  ? 24.432 21.633 3.954   1.00 11.73 ? 88  PHE A C   1 
ATOM   716  O O   . PHE A 1 88  ? 24.647 21.747 5.175   1.00 12.82 ? 88  PHE A O   1 
ATOM   717  C CB  . PHE A 1 88  ? 24.808 23.702 2.557   1.00 12.14 ? 88  PHE A CB  1 
ATOM   718  C CG  . PHE A 1 88  ? 25.723 24.464 1.638   1.00 12.50 ? 88  PHE A CG  1 
ATOM   719  C CD1 . PHE A 1 88  ? 26.870 25.079 2.128   1.00 15.07 ? 88  PHE A CD1 1 
ATOM   720  C CD2 . PHE A 1 88  ? 25.446 24.541 0.275   1.00 14.74 ? 88  PHE A CD2 1 
ATOM   721  C CE1 . PHE A 1 88  ? 27.725 25.768 1.262   1.00 14.66 ? 88  PHE A CE1 1 
ATOM   722  C CE2 . PHE A 1 88  ? 26.304 25.242 -0.623  1.00 18.00 ? 88  PHE A CE2 1 
ATOM   723  C CZ  . PHE A 1 88  ? 27.438 25.882 -0.108  1.00 19.55 ? 88  PHE A CZ  1 
ATOM   724  N N   . THR A 1 89  ? 23.416 20.923 3.475   1.00 11.00 ? 89  THR A N   1 
ATOM   725  C CA  . THR A 1 89  ? 22.433 20.342 4.400   1.00 11.09 ? 89  THR A CA  1 
ATOM   726  C C   . THR A 1 89  ? 22.962 19.136 5.168   1.00 11.30 ? 89  THR A C   1 
ATOM   727  O O   . THR A 1 89  ? 22.642 18.955 6.338   1.00 11.73 ? 89  THR A O   1 
ATOM   728  C CB  . THR A 1 89  ? 21.121 19.976 3.694   1.00 10.72 ? 89  THR A CB  1 
ATOM   729  O OG1 . THR A 1 89  ? 21.390 19.094 2.605   1.00 11.47 ? 89  THR A OG1 1 
ATOM   730  C CG2 . THR A 1 89  ? 20.432 21.247 3.144   1.00 12.06 ? 89  THR A CG2 1 
ATOM   731  N N   . THR A 1 90  ? 23.777 18.309 4.520   1.00 11.64 ? 90  THR A N   1 
ATOM   732  C CA  . THR A 1 90  ? 24.290 17.145 5.235   1.00 11.88 ? 90  THR A CA  1 
ATOM   733  C C   . THR A 1 90  ? 25.219 17.501 6.416   1.00 12.01 ? 90  THR A C   1 
ATOM   734  O O   . THR A 1 90  ? 25.049 16.941 7.507   1.00 12.21 ? 90  THR A O   1 
ATOM   735  C CB  . THR A 1 90  ? 24.858 16.040 4.291   1.00 11.92 ? 90  THR A CB  1 
ATOM   736  O OG1 . THR A 1 90  ? 25.887 16.558 3.422   1.00 11.30 ? 90  THR A OG1 1 
ATOM   737  C CG2 . THR A 1 90  ? 23.731 15.471 3.455   1.00 11.56 ? 90  THR A CG2 1 
ATOM   738  N N   . PRO A 1 91  ? 26.184 18.433 6.230   1.00 11.73 ? 91  PRO A N   1 
ATOM   739  C CA  . PRO A 1 91  ? 26.954 18.823 7.435   1.00 11.88 ? 91  PRO A CA  1 
ATOM   740  C C   . PRO A 1 91  ? 26.117 19.548 8.503   1.00 11.18 ? 91  PRO A C   1 
ATOM   741  O O   . PRO A 1 91  ? 26.447 19.445 9.689   1.00 10.93 ? 91  PRO A O   1 
ATOM   742  C CB  . PRO A 1 91  ? 28.060 19.747 6.913   1.00 13.12 ? 91  PRO A CB  1 
ATOM   743  C CG  . PRO A 1 91  ? 27.814 19.954 5.493   1.00 13.22 ? 91  PRO A CG  1 
ATOM   744  C CD  . PRO A 1 91  ? 26.676 19.100 5.006   1.00 12.35 ? 91  PRO A CD  1 
ATOM   745  N N   . LEU A 1 92  ? 25.087 20.300 8.099   1.00 10.88 ? 92  LEU A N   1 
ATOM   746  C CA  . LEU A 1 92  ? 24.194 20.926 9.079   1.00 11.66 ? 92  LEU A CA  1 
ATOM   747  C C   . LEU A 1 92  ? 23.494 19.869 9.938   1.00 11.74 ? 92  LEU A C   1 
ATOM   748  O O   . LEU A 1 92  ? 23.397 20.011 11.160  1.00 11.51 ? 92  LEU A O   1 
ATOM   749  C CB  . LEU A 1 92  ? 23.184 21.862 8.405   1.00 12.02 ? 92  LEU A CB  1 
ATOM   750  C CG  . LEU A 1 92  ? 23.784 23.182 7.906   1.00 13.29 ? 92  LEU A CG  1 
ATOM   751  C CD1 . LEU A 1 92  ? 22.780 23.866 6.989   1.00 13.41 ? 92  LEU A CD1 1 
ATOM   752  C CD2 . LEU A 1 92  ? 24.153 24.120 9.072   1.00 14.56 ? 92  LEU A CD2 1 
ATOM   753  N N   . LEU A 1 93  ? 23.046 18.783 9.300   1.00 11.06 ? 93  LEU A N   1 
ATOM   754  C CA  . LEU A 1 93  ? 22.439 17.674 10.045  1.00 11.11 ? 93  LEU A CA  1 
ATOM   755  C C   . LEU A 1 93  ? 23.446 17.063 11.023  1.00 11.22 ? 93  LEU A C   1 
ATOM   756  O O   . LEU A 1 93  ? 23.116 16.775 12.172  1.00 11.19 ? 93  LEU A O   1 
ATOM   757  C CB  . LEU A 1 93  ? 21.906 16.613 9.089   1.00 10.76 ? 93  LEU A CB  1 
ATOM   758  C CG  . LEU A 1 93  ? 20.638 17.082 8.358   1.00 10.54 ? 93  LEU A CG  1 
ATOM   759  C CD1 . LEU A 1 93  ? 20.255 16.154 7.203   1.00 12.98 ? 93  LEU A CD1 1 
ATOM   760  C CD2 . LEU A 1 93  ? 19.449 17.256 9.322   1.00 12.82 ? 93  LEU A CD2 1 
ATOM   761  N N   . LEU A 1 94  ? 24.678 16.871 10.556  1.00 11.92 ? 94  LEU A N   1 
ATOM   762  C CA  . LEU A 1 94  ? 25.746 16.352 11.431  1.00 12.25 ? 94  LEU A CA  1 
ATOM   763  C C   . LEU A 1 94  ? 26.021 17.274 12.609  1.00 12.60 ? 94  LEU A C   1 
ATOM   764  O O   . LEU A 1 94  ? 26.223 16.807 13.727  1.00 12.84 ? 94  LEU A O   1 
ATOM   765  C CB  . LEU A 1 94  ? 27.036 16.103 10.647  1.00 12.79 ? 94  LEU A CB  1 
ATOM   766  C CG  . LEU A 1 94  ? 26.942 15.033 9.556   1.00 13.09 ? 94  LEU A CG  1 
ATOM   767  C CD1 . LEU A 1 94  ? 28.281 14.918 8.847   1.00 14.29 ? 94  LEU A CD1 1 
ATOM   768  C CD2 . LEU A 1 94  ? 26.518 13.660 10.117  1.00 14.77 ? 94  LEU A CD2 1 
ATOM   769  N N   . LEU A 1 95  ? 26.019 18.578 12.349  1.00 12.29 ? 95  LEU A N   1 
ATOM   770  C CA  A LEU A 1 95  ? 26.209 19.570 13.405  0.60 12.55 ? 95  LEU A CA  1 
ATOM   771  C CA  B LEU A 1 95  ? 26.210 19.571 13.402  0.40 12.93 ? 95  LEU A CA  1 
ATOM   772  C C   . LEU A 1 95  ? 25.108 19.465 14.462  1.00 12.89 ? 95  LEU A C   1 
ATOM   773  O O   . LEU A 1 95  ? 25.385 19.552 15.665  1.00 12.97 ? 95  LEU A O   1 
ATOM   774  C CB  A LEU A 1 95  ? 26.253 20.983 12.820  0.60 12.32 ? 95  LEU A CB  1 
ATOM   775  C CB  B LEU A 1 95  ? 26.281 20.980 12.799  0.40 13.08 ? 95  LEU A CB  1 
ATOM   776  C CG  A LEU A 1 95  ? 26.551 22.085 13.846  0.60 11.85 ? 95  LEU A CG  1 
ATOM   777  C CG  B LEU A 1 95  ? 27.648 21.403 12.238  0.40 14.71 ? 95  LEU A CG  1 
ATOM   778  C CD1 A LEU A 1 95  ? 27.867 21.820 14.605  0.60 12.38 ? 95  LEU A CD1 1 
ATOM   779  C CD1 B LEU A 1 95  ? 27.493 22.472 11.168  0.40 15.91 ? 95  LEU A CD1 1 
ATOM   780  C CD2 A LEU A 1 95  ? 26.574 23.447 13.171  0.60 13.04 ? 95  LEU A CD2 1 
ATOM   781  C CD2 B LEU A 1 95  ? 28.583 21.881 13.349  0.40 16.07 ? 95  LEU A CD2 1 
ATOM   782  N N   . ASP A 1 96  ? 23.855 19.274 14.023  1.00 12.64 ? 96  ASP A N   1 
ATOM   783  C CA  . ASP A 1 96  ? 22.730 19.047 14.973  1.00 12.63 ? 96  ASP A CA  1 
ATOM   784  C C   . ASP A 1 96  ? 23.070 17.869 15.890  1.00 12.80 ? 96  ASP A C   1 
ATOM   785  O O   . ASP A 1 96  ? 22.928 17.951 17.117  1.00 12.94 ? 96  ASP A O   1 
ATOM   786  C CB  . ASP A 1 96  ? 21.425 18.722 14.225  1.00 13.03 ? 96  ASP A CB  1 
ATOM   787  C CG  . ASP A 1 96  ? 20.477 19.927 14.077  1.00 13.42 ? 96  ASP A CG  1 
ATOM   788  O OD1 . ASP A 1 96  ? 20.643 20.964 14.770  1.00 12.79 ? 96  ASP A OD1 1 
ATOM   789  O OD2 . ASP A 1 96  ? 19.525 19.800 13.265  1.00 12.38 ? 96  ASP A OD2 1 
ATOM   790  N N   . LEU A 1 97  ? 23.526 16.769 15.292  1.00 12.31 ? 97  LEU A N   1 
ATOM   791  C CA  . LEU A 1 97  ? 23.866 15.586 16.084  1.00 12.37 ? 97  LEU A CA  1 
ATOM   792  C C   . LEU A 1 97  ? 25.036 15.864 17.014  1.00 12.86 ? 97  LEU A C   1 
ATOM   793  O O   . LEU A 1 97  ? 25.031 15.452 18.181  1.00 13.31 ? 97  LEU A O   1 
ATOM   794  C CB  . LEU A 1 97  ? 24.186 14.401 15.159  1.00 11.94 ? 97  LEU A CB  1 
ATOM   795  C CG  . LEU A 1 97  ? 22.998 13.881 14.337  1.00 13.10 ? 97  LEU A CG  1 
ATOM   796  C CD1 . LEU A 1 97  ? 23.452 12.810 13.350  1.00 14.33 ? 97  LEU A CD1 1 
ATOM   797  C CD2 . LEU A 1 97  ? 21.884 13.348 15.240  1.00 14.47 ? 97  LEU A CD2 1 
ATOM   798  N N   . ALA A 1 98  ? 26.028 16.592 16.501  1.00 12.81 ? 98  ALA A N   1 
ATOM   799  C CA  . ALA A 1 98  ? 27.242 16.887 17.264  1.00 13.32 ? 98  ALA A CA  1 
ATOM   800  C C   . ALA A 1 98  ? 26.923 17.744 18.478  1.00 13.79 ? 98  ALA A C   1 
ATOM   801  O O   . ALA A 1 98  ? 27.476 17.538 19.572  1.00 14.35 ? 98  ALA A O   1 
ATOM   802  C CB  . ALA A 1 98  ? 28.251 17.592 16.375  1.00 13.41 ? 98  ALA A CB  1 
ATOM   803  N N   . LEU A 1 99  ? 26.027 18.702 18.298  1.00 13.65 ? 99  LEU A N   1 
ATOM   804  C CA  . LEU A 1 99  ? 25.682 19.592 19.402  1.00 14.96 ? 99  LEU A CA  1 
ATOM   805  C C   . LEU A 1 99  ? 24.899 18.855 20.469  1.00 15.18 ? 99  LEU A C   1 
ATOM   806  O O   . LEU A 1 99  ? 25.038 19.149 21.658  1.00 15.37 ? 99  LEU A O   1 
ATOM   807  C CB  . LEU A 1 99  ? 24.870 20.781 18.894  1.00 15.51 ? 99  LEU A CB  1 
ATOM   808  C CG  . LEU A 1 99  ? 25.676 21.775 18.069  1.00 16.82 ? 99  LEU A CG  1 
ATOM   809  C CD1 . LEU A 1 99  ? 24.741 22.835 17.521  1.00 19.34 ? 99  LEU A CD1 1 
ATOM   810  C CD2 . LEU A 1 99  ? 26.812 22.418 18.888  1.00 19.83 ? 99  LEU A CD2 1 
ATOM   811  N N   . LEU A 1 100 ? 24.080 17.898 20.048  1.00 15.13 ? 100 LEU A N   1 
ATOM   812  C CA  A LEU A 1 100 ? 23.272 17.137 20.983  0.60 15.99 ? 100 LEU A CA  1 
ATOM   813  C CA  B LEU A 1 100 ? 23.281 17.114 20.991  0.40 15.50 ? 100 LEU A CA  1 
ATOM   814  C C   . LEU A 1 100 ? 24.159 16.364 21.963  1.00 16.00 ? 100 LEU A C   1 
ATOM   815  O O   . LEU A 1 100 ? 23.837 16.272 23.145  1.00 17.16 ? 100 LEU A O   1 
ATOM   816  C CB  A LEU A 1 100 ? 22.355 16.187 20.207  0.60 16.73 ? 100 LEU A CB  1 
ATOM   817  C CB  B LEU A 1 100 ? 22.405 16.091 20.273  0.40 15.75 ? 100 LEU A CB  1 
ATOM   818  C CG  A LEU A 1 100 ? 21.002 15.787 20.787  0.60 16.69 ? 100 LEU A CG  1 
ATOM   819  C CG  B LEU A 1 100 ? 21.019 16.518 19.816  0.40 13.66 ? 100 LEU A CG  1 
ATOM   820  C CD1 A LEU A 1 100 ? 20.182 16.974 21.308  0.60 15.71 ? 100 LEU A CD1 1 
ATOM   821  C CD1 B LEU A 1 100 ? 20.439 15.376 19.009  0.40 12.38 ? 100 LEU A CD1 1 
ATOM   822  C CD2 A LEU A 1 100 ? 20.232 15.044 19.723  0.60 14.87 ? 100 LEU A CD2 1 
ATOM   823  C CD2 B LEU A 1 100 ? 20.092 16.891 20.975  0.40 13.60 ? 100 LEU A CD2 1 
ATOM   824  N N   . VAL A 1 101 ? 25.274 15.826 21.463  1.00 15.76 ? 101 VAL A N   1 
ATOM   825  C CA  . VAL A 1 101 ? 26.139 14.944 22.264  1.00 16.03 ? 101 VAL A CA  1 
ATOM   826  C C   . VAL A 1 101 ? 27.403 15.614 22.797  1.00 16.41 ? 101 VAL A C   1 
ATOM   827  O O   . VAL A 1 101 ? 28.251 14.959 23.400  1.00 17.01 ? 101 VAL A O   1 
ATOM   828  C CB  . VAL A 1 101 ? 26.522 13.656 21.481  1.00 16.15 ? 101 VAL A CB  1 
ATOM   829  C CG1 . VAL A 1 101 ? 25.267 12.953 21.019  1.00 16.74 ? 101 VAL A CG1 1 
ATOM   830  C CG2 . VAL A 1 101 ? 27.453 13.965 20.295  1.00 15.41 ? 101 VAL A CG2 1 
ATOM   831  N N   . ASP A 1 102 ? 27.514 16.921 22.558  1.00 17.03 ? 102 ASP A N   1 
ATOM   832  C CA  A ASP A 1 102 ? 28.720 17.666 22.949  0.60 17.64 ? 102 ASP A CA  1 
ATOM   833  C CA  B ASP A 1 102 ? 28.709 17.702 22.886  0.40 17.32 ? 102 ASP A CA  1 
ATOM   834  C C   . ASP A 1 102 ? 29.973 17.043 22.328  1.00 17.65 ? 102 ASP A C   1 
ATOM   835  O O   . ASP A 1 102 ? 30.969 16.833 23.024  1.00 17.98 ? 102 ASP A O   1 
ATOM   836  C CB  A ASP A 1 102 ? 28.879 17.690 24.482  0.60 18.18 ? 102 ASP A CB  1 
ATOM   837  C CB  B ASP A 1 102 ? 28.816 17.957 24.393  0.40 17.57 ? 102 ASP A CB  1 
ATOM   838  C CG  A ASP A 1 102 ? 27.952 18.682 25.166  0.60 20.31 ? 102 ASP A CG  1 
ATOM   839  C CG  B ASP A 1 102 ? 29.942 18.908 24.739  0.40 17.98 ? 102 ASP A CG  1 
ATOM   840  O OD1 A ASP A 1 102 ? 27.219 19.419 24.478  0.60 22.04 ? 102 ASP A OD1 1 
ATOM   841  O OD1 B ASP A 1 102 ? 30.258 19.790 23.914  0.40 18.17 ? 102 ASP A OD1 1 
ATOM   842  O OD2 A ASP A 1 102 ? 27.962 18.729 26.417  0.60 23.27 ? 102 ASP A OD2 1 
ATOM   843  O OD2 B ASP A 1 102 ? 30.517 18.756 25.833  0.40 19.08 ? 102 ASP A OD2 1 
ATOM   844  N N   . ALA A 1 103 ? 29.922 16.723 21.035  1.00 17.26 ? 103 ALA A N   1 
ATOM   845  C CA  . ALA A 1 103 ? 31.061 16.116 20.344  1.00 17.78 ? 103 ALA A CA  1 
ATOM   846  C C   . ALA A 1 103 ? 32.257 17.063 20.333  1.00 18.26 ? 103 ALA A C   1 
ATOM   847  O O   . ALA A 1 103 ? 32.082 18.287 20.359  1.00 18.32 ? 103 ALA A O   1 
ATOM   848  C CB  . ALA A 1 103 ? 30.674 15.722 18.923  1.00 17.56 ? 103 ALA A CB  1 
ATOM   849  N N   . ASP A 1 104 ? 33.461 16.487 20.297  1.00 18.81 ? 104 ASP A N   1 
ATOM   850  C CA  . ASP A 1 104 ? 34.700 17.268 20.266  1.00 19.54 ? 104 ASP A CA  1 
ATOM   851  C C   . ASP A 1 104 ? 34.804 18.075 18.977  1.00 18.92 ? 104 ASP A C   1 
ATOM   852  O O   . ASP A 1 104 ? 34.364 17.622 17.916  1.00 18.48 ? 104 ASP A O   1 
ATOM   853  C CB  . ASP A 1 104 ? 35.931 16.356 20.373  1.00 20.01 ? 104 ASP A CB  1 
ATOM   854  C CG  . ASP A 1 104 ? 36.025 15.634 21.715  1.00 23.26 ? 104 ASP A CG  1 
ATOM   855  O OD1 . ASP A 1 104 ? 35.325 16.004 22.683  1.00 24.41 ? 104 ASP A OD1 1 
ATOM   856  O OD2 . ASP A 1 104 ? 36.823 14.677 21.793  1.00 25.83 ? 104 ASP A OD2 1 
ATOM   857  N N   . GLN A 1 105 ? 35.406 19.256 19.079  1.00 18.72 ? 105 GLN A N   1 
ATOM   858  C CA  . GLN A 1 105 ? 35.642 20.100 17.907  1.00 18.49 ? 105 GLN A CA  1 
ATOM   859  C C   . GLN A 1 105 ? 36.331 19.342 16.759  1.00 17.16 ? 105 GLN A C   1 
ATOM   860  O O   . GLN A 1 105 ? 35.916 19.440 15.601  1.00 16.14 ? 105 GLN A O   1 
ATOM   861  C CB  . GLN A 1 105 ? 36.463 21.329 18.310  1.00 18.91 ? 105 GLN A CB  1 
ATOM   862  C CG  . GLN A 1 105 ? 36.477 22.427 17.248  1.00 20.57 ? 105 GLN A CG  1 
ATOM   863  C CD  . GLN A 1 105 ? 37.329 23.630 17.648  1.00 21.75 ? 105 GLN A CD  1 
ATOM   864  O OE1 . GLN A 1 105 ? 37.260 24.693 17.017  1.00 25.67 ? 105 GLN A OE1 1 
ATOM   865  N NE2 . GLN A 1 105 ? 38.146 23.463 18.690  1.00 24.14 ? 105 GLN A NE2 1 
ATOM   866  N N   . GLY A 1 106 ? 37.380 18.588 17.078  1.00 16.10 ? 106 GLY A N   1 
ATOM   867  C CA  . GLY A 1 106 ? 38.106 17.807 16.074  1.00 16.01 ? 106 GLY A CA  1 
ATOM   868  C C   . GLY A 1 106 ? 37.258 16.740 15.398  1.00 15.93 ? 106 GLY A C   1 
ATOM   869  O O   . GLY A 1 106 ? 37.386 16.492 14.194  1.00 15.46 ? 106 GLY A O   1 
ATOM   870  N N   . THR A 1 107 ? 36.372 16.114 16.173  1.00 15.81 ? 107 THR A N   1 
ATOM   871  C CA  A THR A 1 107 ? 35.462 15.100 15.641  0.80 16.22 ? 107 THR A CA  1 
ATOM   872  C CA  B THR A 1 107 ? 35.489 15.096 15.609  0.20 15.89 ? 107 THR A CA  1 
ATOM   873  C C   . THR A 1 107 ? 34.508 15.736 14.633  1.00 15.77 ? 107 THR A C   1 
ATOM   874  O O   . THR A 1 107 ? 34.202 15.155 13.582  1.00 16.53 ? 107 THR A O   1 
ATOM   875  C CB  A THR A 1 107 ? 34.635 14.451 16.765  0.80 16.29 ? 107 THR A CB  1 
ATOM   876  C CB  B THR A 1 107 ? 34.732 14.291 16.686  0.20 15.87 ? 107 THR A CB  1 
ATOM   877  O OG1 A THR A 1 107 ? 35.508 13.940 17.783  0.80 16.14 ? 107 THR A OG1 1 
ATOM   878  O OG1 B THR A 1 107 ? 33.992 15.180 17.531  0.20 15.72 ? 107 THR A OG1 1 
ATOM   879  C CG2 A THR A 1 107 ? 33.782 13.321 16.214  0.80 16.57 ? 107 THR A CG2 1 
ATOM   880  C CG2 B THR A 1 107 ? 35.708 13.467 17.523  0.20 15.78 ? 107 THR A CG2 1 
ATOM   881  N N   . ILE A 1 108 ? 34.030 16.932 14.970  1.00 15.46 ? 108 ILE A N   1 
ATOM   882  C CA  . ILE A 1 108 ? 33.146 17.684 14.078  1.00 15.72 ? 108 ILE A CA  1 
ATOM   883  C C   . ILE A 1 108 ? 33.887 18.051 12.796  1.00 15.43 ? 108 ILE A C   1 
ATOM   884  O O   . ILE A 1 108 ? 33.361 17.860 11.704  1.00 15.20 ? 108 ILE A O   1 
ATOM   885  C CB  . ILE A 1 108 ? 32.585 18.961 14.744  1.00 15.66 ? 108 ILE A CB  1 
ATOM   886  C CG1 . ILE A 1 108 ? 31.737 18.584 15.966  1.00 16.78 ? 108 ILE A CG1 1 
ATOM   887  C CG2 . ILE A 1 108 ? 31.768 19.803 13.724  1.00 16.91 ? 108 ILE A CG2 1 
ATOM   888  C CD1 . ILE A 1 108 ? 31.304 19.765 16.813  1.00 15.93 ? 108 ILE A CD1 1 
ATOM   889  N N   . LEU A 1 109 ? 35.098 18.596 12.923  1.00 14.88 ? 109 LEU A N   1 
ATOM   890  C CA  . LEU A 1 109 ? 35.877 18.957 11.726  1.00 15.60 ? 109 LEU A CA  1 
ATOM   891  C C   . LEU A 1 109 ? 36.082 17.747 10.801  1.00 15.41 ? 109 LEU A C   1 
ATOM   892  O O   . LEU A 1 109 ? 35.940 17.849 9.572   1.00 15.67 ? 109 LEU A O   1 
ATOM   893  C CB  . LEU A 1 109 ? 37.235 19.557 12.118  1.00 15.65 ? 109 LEU A CB  1 
ATOM   894  C CG  . LEU A 1 109 ? 38.078 20.042 10.931  1.00 17.36 ? 109 LEU A CG  1 
ATOM   895  C CD1 . LEU A 1 109 ? 37.405 21.210 10.226  1.00 19.40 ? 109 LEU A CD1 1 
ATOM   896  C CD2 . LEU A 1 109 ? 39.482 20.441 11.392  1.00 17.60 ? 109 LEU A CD2 1 
ATOM   897  N N   . ALA A 1 110 ? 36.415 16.605 11.394  1.00 14.45 ? 110 ALA A N   1 
ATOM   898  C CA  . ALA A 1 110 ? 36.673 15.388 10.621  1.00 15.11 ? 110 ALA A CA  1 
ATOM   899  C C   . ALA A 1 110 ? 35.412 14.874 9.916   1.00 14.43 ? 110 ALA A C   1 
ATOM   900  O O   . ALA A 1 110 ? 35.463 14.500 8.740   1.00 14.76 ? 110 ALA A O   1 
ATOM   901  C CB  . ALA A 1 110 ? 37.245 14.292 11.525  1.00 15.34 ? 110 ALA A CB  1 
ATOM   902  N N   . ALA A 1 111 ? 34.289 14.859 10.633  1.00 14.02 ? 111 ALA A N   1 
ATOM   903  C CA  . ALA A 1 111 ? 33.011 14.431 10.057  1.00 14.15 ? 111 ALA A CA  1 
ATOM   904  C C   . ALA A 1 111 ? 32.548 15.358 8.931   1.00 13.94 ? 111 ALA A C   1 
ATOM   905  O O   . ALA A 1 111 ? 32.136 14.887 7.878   1.00 14.23 ? 111 ALA A O   1 
ATOM   906  C CB  . ALA A 1 111 ? 31.931 14.343 11.126  1.00 13.92 ? 111 ALA A CB  1 
ATOM   907  N N   . VAL A 1 112 ? 32.602 16.663 9.174   1.00 14.10 ? 112 VAL A N   1 
ATOM   908  C CA  . VAL A 1 112 ? 32.222 17.655 8.160   1.00 14.05 ? 112 VAL A CA  1 
ATOM   909  C C   . VAL A 1 112 ? 33.181 17.587 6.950   1.00 14.45 ? 112 VAL A C   1 
ATOM   910  O O   . VAL A 1 112 ? 32.743 17.689 5.799   1.00 14.42 ? 112 VAL A O   1 
ATOM   911  C CB  . VAL A 1 112 ? 32.112 19.076 8.785   1.00 14.38 ? 112 VAL A CB  1 
ATOM   912  C CG1 . VAL A 1 112 ? 31.953 20.151 7.711   1.00 14.91 ? 112 VAL A CG1 1 
ATOM   913  C CG2 . VAL A 1 112 ? 30.945 19.108 9.797   1.00 13.95 ? 112 VAL A CG2 1 
ATOM   914  N N   . GLY A 1 113 ? 34.478 17.389 7.207   1.00 14.16 ? 113 GLY A N   1 
ATOM   915  C CA  . GLY A 1 113 ? 35.458 17.176 6.130   1.00 14.01 ? 113 GLY A CA  1 
ATOM   916  C C   . GLY A 1 113 ? 35.116 15.953 5.283   1.00 14.23 ? 113 GLY A C   1 
ATOM   917  O O   . GLY A 1 113 ? 35.113 16.016 4.044   1.00 15.06 ? 113 GLY A O   1 
ATOM   918  N N   . ALA A 1 114 ? 34.827 14.834 5.950   1.00 13.76 ? 114 ALA A N   1 
ATOM   919  C CA  . ALA A 1 114 ? 34.414 13.611 5.250   1.00 12.82 ? 114 ALA A CA  1 
ATOM   920  C C   . ALA A 1 114 ? 33.139 13.843 4.431   1.00 13.23 ? 114 ALA A C   1 
ATOM   921  O O   . ALA A 1 114 ? 32.990 13.305 3.332   1.00 12.72 ? 114 ALA A O   1 
ATOM   922  C CB  . ALA A 1 114 ? 34.186 12.464 6.249   1.00 14.03 ? 114 ALA A CB  1 
ATOM   923  N N   . ASP A 1 115 ? 32.224 14.627 4.991   1.00 12.75 ? 115 ASP A N   1 
ATOM   924  C CA  . ASP A 1 115 ? 30.956 14.949 4.326   1.00 12.67 ? 115 ASP A CA  1 
ATOM   925  C C   . ASP A 1 115 ? 31.218 15.726 3.017   1.00 12.34 ? 115 ASP A C   1 
ATOM   926  O O   . ASP A 1 115 ? 30.612 15.435 1.976   1.00 12.04 ? 115 ASP A O   1 
ATOM   927  C CB  . ASP A 1 115 ? 30.058 15.724 5.293   1.00 13.27 ? 115 ASP A CB  1 
ATOM   928  C CG  . ASP A 1 115 ? 28.610 15.737 4.857   1.00 15.45 ? 115 ASP A CG  1 
ATOM   929  O OD1 . ASP A 1 115 ? 28.346 16.089 3.697   1.00 16.62 ? 115 ASP A OD1 1 
ATOM   930  O OD2 . ASP A 1 115 ? 27.734 15.423 5.672   1.00 19.50 ? 115 ASP A OD2 1 
ATOM   931  N N   . GLY A 1 116 ? 32.111 16.719 3.075   1.00 12.37 ? 116 GLY A N   1 
ATOM   932  C CA  . GLY A 1 116 ? 32.509 17.464 1.863   1.00 12.79 ? 116 GLY A CA  1 
ATOM   933  C C   . GLY A 1 116 ? 33.117 16.550 0.809   1.00 12.85 ? 116 GLY A C   1 
ATOM   934  O O   . GLY A 1 116 ? 32.801 16.660 -0.382  1.00 13.89 ? 116 GLY A O   1 
ATOM   935  N N   . ILE A 1 117 ? 33.983 15.636 1.240   1.00 12.90 ? 117 ILE A N   1 
ATOM   936  C CA  . ILE A 1 117 ? 34.545 14.644 0.329   1.00 13.70 ? 117 ILE A CA  1 
ATOM   937  C C   . ILE A 1 117 ? 33.432 13.793 -0.288  1.00 12.94 ? 117 ILE A C   1 
ATOM   938  O O   . ILE A 1 117 ? 33.450 13.538 -1.493  1.00 13.54 ? 117 ILE A O   1 
ATOM   939  C CB  . ILE A 1 117 ? 35.591 13.731 1.035   1.00 14.30 ? 117 ILE A CB  1 
ATOM   940  C CG1 . ILE A 1 117 ? 36.849 14.544 1.381   1.00 14.59 ? 117 ILE A CG1 1 
ATOM   941  C CG2 . ILE A 1 117 ? 35.948 12.541 0.152   1.00 14.46 ? 117 ILE A CG2 1 
ATOM   942  C CD1 . ILE A 1 117 ? 37.767 13.853 2.396   1.00 16.58 ? 117 ILE A CD1 1 
ATOM   943  N N   . MET A 1 118 ? 32.486 13.347 0.545   1.00 12.18 ? 118 MET A N   1 
ATOM   944  C CA  . MET A 1 118 ? 31.369 12.507 0.099   1.00 11.63 ? 118 MET A CA  1 
ATOM   945  C C   . MET A 1 118 ? 30.578 13.209 -0.985  1.00 11.48 ? 118 MET A C   1 
ATOM   946  O O   . MET A 1 118 ? 30.321 12.647 -2.051  1.00 11.78 ? 118 MET A O   1 
ATOM   947  C CB  . MET A 1 118 ? 30.472 12.149 1.297   1.00 11.19 ? 118 MET A CB  1 
ATOM   948  C CG  . MET A 1 118 ? 29.237 11.335 0.930   1.00 11.82 ? 118 MET A CG  1 
ATOM   949  S SD  . MET A 1 118 ? 28.196 11.073 2.391   1.00 11.99 ? 118 MET A SD  1 
ATOM   950  C CE  . MET A 1 118 ? 27.375 12.674 2.474   1.00 13.60 ? 118 MET A CE  1 
ATOM   951  N N   . ILE A 1 119 ? 30.211 14.459 -0.732  1.00 10.95 ? 119 ILE A N   1 
ATOM   952  C CA  . ILE A 1 119 ? 29.405 15.180 -1.701  1.00 12.31 ? 119 ILE A CA  1 
ATOM   953  C C   . ILE A 1 119 ? 30.215 15.556 -2.950  1.00 12.34 ? 119 ILE A C   1 
ATOM   954  O O   . ILE A 1 119 ? 29.734 15.395 -4.070  1.00 13.25 ? 119 ILE A O   1 
ATOM   955  C CB  . ILE A 1 119 ? 28.716 16.420 -1.056  1.00 12.34 ? 119 ILE A CB  1 
ATOM   956  C CG1 . ILE A 1 119 ? 27.757 15.985 0.068   1.00 13.49 ? 119 ILE A CG1 1 
ATOM   957  C CG2 . ILE A 1 119 ? 27.972 17.184 -2.097  1.00 13.11 ? 119 ILE A CG2 1 
ATOM   958  C CD1 . ILE A 1 119 ? 26.744 14.859 -0.321  1.00 11.99 ? 119 ILE A CD1 1 
ATOM   959  N N   . GLY A 1 120 ? 31.439 16.056 -2.760  1.00 12.07 ? 120 GLY A N   1 
ATOM   960  C CA  . GLY A 1 120 ? 32.288 16.465 -3.891  1.00 12.52 ? 120 GLY A CA  1 
ATOM   961  C C   . GLY A 1 120 ? 32.590 15.309 -4.827  1.00 12.17 ? 120 GLY A C   1 
ATOM   962  O O   . GLY A 1 120 ? 32.425 15.424 -6.053  1.00 12.16 ? 120 GLY A O   1 
ATOM   963  N N   . THR A 1 121 ? 33.011 14.175 -4.266  1.00 12.66 ? 121 THR A N   1 
ATOM   964  C CA  . THR A 1 121 ? 33.308 12.999 -5.107  1.00 12.08 ? 121 THR A CA  1 
ATOM   965  C C   . THR A 1 121 ? 32.041 12.412 -5.750  1.00 12.16 ? 121 THR A C   1 
ATOM   966  O O   . THR A 1 121 ? 32.092 11.930 -6.885  1.00 12.37 ? 121 THR A O   1 
ATOM   967  C CB  . THR A 1 121 ? 34.109 11.894 -4.357  1.00 12.76 ? 121 THR A CB  1 
ATOM   968  O OG1 . THR A 1 121 ? 33.399 11.487 -3.170  1.00 12.62 ? 121 THR A OG1 1 
ATOM   969  C CG2 . THR A 1 121 ? 35.503 12.412 -3.961  1.00 12.96 ? 121 THR A CG2 1 
ATOM   970  N N   . GLY A 1 122 ? 30.911 12.450 -5.036  1.00 11.63 ? 122 GLY A N   1 
ATOM   971  C CA  . GLY A 1 122 ? 29.619 12.038 -5.617  1.00 11.78 ? 122 GLY A CA  1 
ATOM   972  C C   . GLY A 1 122 ? 29.306 12.884 -6.850  1.00 11.54 ? 122 GLY A C   1 
ATOM   973  O O   . GLY A 1 122 ? 28.897 12.350 -7.888  1.00 12.55 ? 122 GLY A O   1 
ATOM   974  N N   . LEU A 1 123 ? 29.544 14.194 -6.757  1.00 11.56 ? 123 LEU A N   1 
ATOM   975  C CA  . LEU A 1 123 ? 29.276 15.093 -7.888  1.00 11.19 ? 123 LEU A CA  1 
ATOM   976  C C   . LEU A 1 123 ? 30.240 14.816 -9.049  1.00 11.74 ? 123 LEU A C   1 
ATOM   977  O O   . LEU A 1 123 ? 29.830 14.740 -10.223 1.00 12.69 ? 123 LEU A O   1 
ATOM   978  C CB  . LEU A 1 123 ? 29.363 16.566 -7.453  1.00 10.81 ? 123 LEU A CB  1 
ATOM   979  C CG  . LEU A 1 123 ? 29.128 17.571 -8.590  1.00 11.00 ? 123 LEU A CG  1 
ATOM   980  C CD1 . LEU A 1 123 ? 27.771 17.340 -9.289  1.00 13.04 ? 123 LEU A CD1 1 
ATOM   981  C CD2 . LEU A 1 123 ? 29.202 18.978 -8.017  1.00 12.13 ? 123 LEU A CD2 1 
ATOM   982  N N   . VAL A 1 124 ? 31.524 14.658 -8.726  1.00 12.25 ? 124 VAL A N   1 
ATOM   983  C CA  . VAL A 1 124 ? 32.507 14.308 -9.759  1.00 11.96 ? 124 VAL A CA  1 
ATOM   984  C C   . VAL A 1 124 ? 32.079 13.016 -10.469 1.00 12.11 ? 124 VAL A C   1 
ATOM   985  O O   . VAL A 1 124 ? 32.048 12.966 -11.709 1.00 12.68 ? 124 VAL A O   1 
ATOM   986  C CB  . VAL A 1 124 ? 33.935 14.195 -9.194  1.00 12.44 ? 124 VAL A CB  1 
ATOM   987  C CG1 . VAL A 1 124 ? 34.902 13.671 -10.273 1.00 12.79 ? 124 VAL A CG1 1 
ATOM   988  C CG2 . VAL A 1 124 ? 34.405 15.556 -8.698  1.00 12.86 ? 124 VAL A CG2 1 
ATOM   989  N N   . GLY A 1 125 ? 31.730 11.990 -9.695  1.00 12.63 ? 125 GLY A N   1 
ATOM   990  C CA  . GLY A 1 125 ? 31.208 10.740 -10.283 1.00 13.14 ? 125 GLY A CA  1 
ATOM   991  C C   . GLY A 1 125 ? 30.003 10.983 -11.187 1.00 13.01 ? 125 GLY A C   1 
ATOM   992  O O   . GLY A 1 125 ? 29.921 10.431 -12.294 1.00 13.92 ? 125 GLY A O   1 
ATOM   993  N N   . ALA A 1 126 ? 29.076 11.826 -10.732 1.00 12.87 ? 126 ALA A N   1 
ATOM   994  C CA  . ALA A 1 126 ? 27.837 12.091 -11.468 1.00 13.22 ? 126 ALA A CA  1 
ATOM   995  C C   . ALA A 1 126 ? 28.098 12.747 -12.826 1.00 13.36 ? 126 ALA A C   1 
ATOM   996  O O   . ALA A 1 126 ? 27.269 12.657 -13.734 1.00 12.99 ? 126 ALA A O   1 
ATOM   997  C CB  . ALA A 1 126 ? 26.886 12.961 -10.628 1.00 12.63 ? 126 ALA A CB  1 
ATOM   998  N N   . LEU A 1 127 ? 29.252 13.407 -12.941 1.00 13.65 ? 127 LEU A N   1 
ATOM   999  C CA  . LEU A 1 127 ? 29.606 14.190 -14.138 1.00 13.87 ? 127 LEU A CA  1 
ATOM   1000 C C   . LEU A 1 127 ? 30.639 13.520 -15.026 1.00 13.72 ? 127 LEU A C   1 
ATOM   1001 O O   . LEU A 1 127 ? 31.021 14.077 -16.064 1.00 13.41 ? 127 LEU A O   1 
ATOM   1002 C CB  . LEU A 1 127 ? 30.147 15.555 -13.725 1.00 14.57 ? 127 LEU A CB  1 
ATOM   1003 C CG  . LEU A 1 127 ? 29.242 16.439 -12.871 1.00 14.74 ? 127 LEU A CG  1 
ATOM   1004 C CD1 . LEU A 1 127 ? 29.997 17.690 -12.425 1.00 15.75 ? 127 LEU A CD1 1 
ATOM   1005 C CD2 . LEU A 1 127 ? 27.963 16.792 -13.617 1.00 16.10 ? 127 LEU A CD2 1 
ATOM   1006 N N   . THR A 1 128 ? 31.086 12.335 -14.624 1.00 13.07 ? 128 THR A N   1 
ATOM   1007 C CA  . THR A 1 128 ? 32.205 11.677 -15.278 1.00 13.43 ? 128 THR A CA  1 
ATOM   1008 C C   . THR A 1 128 ? 31.760 10.975 -16.555 1.00 13.83 ? 128 THR A C   1 
ATOM   1009 O O   . THR A 1 128 ? 30.740 10.293 -16.572 1.00 13.41 ? 128 THR A O   1 
ATOM   1010 C CB  . THR A 1 128 ? 32.918 10.722 -14.280 1.00 13.36 ? 128 THR A CB  1 
ATOM   1011 O OG1 . THR A 1 128 ? 33.675 11.510 -13.355 1.00 13.46 ? 128 THR A OG1 1 
ATOM   1012 C CG2 . THR A 1 128 ? 33.878 9.787  -14.994 1.00 14.23 ? 128 THR A CG2 1 
ATOM   1013 N N   . LYS A 1 129 ? 32.537 11.161 -17.627 1.00 13.95 ? 129 LYS A N   1 
ATOM   1014 C CA  . LYS A 1 129 ? 32.144 10.660 -18.949 1.00 15.35 ? 129 LYS A CA  1 
ATOM   1015 C C   . LYS A 1 129 ? 32.546 9.210  -19.245 1.00 15.78 ? 129 LYS A C   1 
ATOM   1016 O O   . LYS A 1 129 ? 31.943 8.573  -20.116 1.00 17.42 ? 129 LYS A O   1 
ATOM   1017 C CB  . LYS A 1 129 ? 32.615 11.604 -20.069 1.00 15.01 ? 129 LYS A CB  1 
ATOM   1018 C CG  . LYS A 1 129 ? 32.046 13.003 -19.961 1.00 16.07 ? 129 LYS A CG  1 
ATOM   1019 C CD  . LYS A 1 129 ? 32.722 13.976 -20.940 1.00 17.74 ? 129 LYS A CD  1 
ATOM   1020 C CE  . LYS A 1 129 ? 32.122 15.356 -20.813 1.00 21.15 ? 129 LYS A CE  1 
ATOM   1021 N NZ  . LYS A 1 129 ? 32.793 16.344 -21.728 1.00 25.01 ? 129 LYS A NZ  1 
ATOM   1022 N N   . VAL A 1 130 ? 33.556 8.703  -18.543 1.00 15.54 ? 130 VAL A N   1 
ATOM   1023 C CA  . VAL A 1 130 ? 33.991 7.310  -18.696 1.00 15.96 ? 130 VAL A CA  1 
ATOM   1024 C C   . VAL A 1 130 ? 33.191 6.464  -17.716 1.00 15.81 ? 130 VAL A C   1 
ATOM   1025 O O   . VAL A 1 130 ? 33.314 6.654  -16.512 1.00 15.23 ? 130 VAL A O   1 
ATOM   1026 C CB  . VAL A 1 130 ? 35.504 7.142  -18.399 1.00 16.28 ? 130 VAL A CB  1 
ATOM   1027 C CG1 . VAL A 1 130 ? 35.899 5.673  -18.476 1.00 17.42 ? 130 VAL A CG1 1 
ATOM   1028 C CG2 . VAL A 1 130 ? 36.353 7.988  -19.360 1.00 18.04 ? 130 VAL A CG2 1 
ATOM   1029 N N   . TYR A 1 131 ? 32.381 5.537  -18.229 1.00 15.95 ? 131 TYR A N   1 
ATOM   1030 C CA  . TYR A 1 131 ? 31.391 4.828  -17.392 1.00 15.77 ? 131 TYR A CA  1 
ATOM   1031 C C   . TYR A 1 131 ? 32.014 4.161  -16.177 1.00 16.15 ? 131 TYR A C   1 
ATOM   1032 O O   . TYR A 1 131 ? 31.515 4.319  -15.053 1.00 16.41 ? 131 TYR A O   1 
ATOM   1033 C CB  . TYR A 1 131 ? 30.634 3.774  -18.215 1.00 15.86 ? 131 TYR A CB  1 
ATOM   1034 C CG  . TYR A 1 131 ? 29.184 3.538  -17.825 1.00 14.38 ? 131 TYR A CG  1 
ATOM   1035 C CD1 . TYR A 1 131 ? 28.706 3.820  -16.530 1.00 13.37 ? 131 TYR A CD1 1 
ATOM   1036 C CD2 . TYR A 1 131 ? 28.284 3.037  -18.762 1.00 15.43 ? 131 TYR A CD2 1 
ATOM   1037 C CE1 . TYR A 1 131 ? 27.360 3.592  -16.197 1.00 13.61 ? 131 TYR A CE1 1 
ATOM   1038 C CE2 . TYR A 1 131 ? 26.957 2.821  -18.455 1.00 15.77 ? 131 TYR A CE2 1 
ATOM   1039 C CZ  . TYR A 1 131 ? 26.489 3.104  -17.173 1.00 15.70 ? 131 TYR A CZ  1 
ATOM   1040 O OH  . TYR A 1 131 ? 25.156 2.882  -16.894 1.00 15.41 ? 131 TYR A OH  1 
ATOM   1041 N N   . SER A 1 132 ? 33.094 3.410  -16.393 1.00 16.22 ? 132 SER A N   1 
ATOM   1042 C CA  A SER A 1 132 ? 33.740 2.671  -15.310 0.50 16.45 ? 132 SER A CA  1 
ATOM   1043 C CA  B SER A 1 132 ? 33.738 2.667  -15.309 0.50 16.40 ? 132 SER A CA  1 
ATOM   1044 C C   . SER A 1 132 ? 34.219 3.600  -14.205 1.00 16.45 ? 132 SER A C   1 
ATOM   1045 O O   . SER A 1 132 ? 34.119 3.264  -13.034 1.00 16.67 ? 132 SER A O   1 
ATOM   1046 C CB  A SER A 1 132 ? 34.900 1.831  -15.839 0.50 16.68 ? 132 SER A CB  1 
ATOM   1047 C CB  B SER A 1 132 ? 34.901 1.820  -15.830 0.50 16.62 ? 132 SER A CB  1 
ATOM   1048 O OG  A SER A 1 132 ? 34.413 0.828  -16.709 0.50 17.53 ? 132 SER A OG  1 
ATOM   1049 O OG  B SER A 1 132 ? 35.816 2.613  -16.558 0.50 17.19 ? 132 SER A OG  1 
ATOM   1050 N N   . TYR A 1 133 ? 34.718 4.781  -14.590 1.00 16.18 ? 133 TYR A N   1 
ATOM   1051 C CA  . TYR A 1 133 ? 35.239 5.753  -13.625 1.00 16.80 ? 133 TYR A CA  1 
ATOM   1052 C C   . TYR A 1 133 ? 34.137 6.404  -12.788 1.00 15.48 ? 133 TYR A C   1 
ATOM   1053 O O   . TYR A 1 133 ? 34.395 6.826  -11.664 1.00 15.38 ? 133 TYR A O   1 
ATOM   1054 C CB  . TYR A 1 133 ? 36.077 6.848  -14.304 1.00 18.59 ? 133 TYR A CB  1 
ATOM   1055 C CG  . TYR A 1 133 ? 37.315 6.367  -15.028 1.00 22.16 ? 133 TYR A CG  1 
ATOM   1056 C CD1 . TYR A 1 133 ? 37.820 5.084  -14.830 1.00 24.37 ? 133 TYR A CD1 1 
ATOM   1057 C CD2 . TYR A 1 133 ? 37.996 7.219  -15.903 1.00 24.15 ? 133 TYR A CD2 1 
ATOM   1058 C CE1 . TYR A 1 133 ? 38.962 4.649  -15.505 1.00 26.27 ? 133 TYR A CE1 1 
ATOM   1059 C CE2 . TYR A 1 133 ? 39.135 6.799  -16.572 1.00 26.39 ? 133 TYR A CE2 1 
ATOM   1060 C CZ  . TYR A 1 133 ? 39.608 5.513  -16.367 1.00 25.12 ? 133 TYR A CZ  1 
ATOM   1061 O OH  . TYR A 1 133 ? 40.740 5.103  -17.040 1.00 27.27 ? 133 TYR A OH  1 
ATOM   1062 N N   . ARG A 1 134 ? 32.917 6.501  -13.322 1.00 13.71 ? 134 ARG A N   1 
ATOM   1063 C CA  . ARG A 1 134 ? 31.797 7.006  -12.504 1.00 13.11 ? 134 ARG A CA  1 
ATOM   1064 C C   . ARG A 1 134 ? 31.722 6.205  -11.211 1.00 12.82 ? 134 ARG A C   1 
ATOM   1065 O O   . ARG A 1 134 ? 31.485 6.763  -10.137 1.00 13.35 ? 134 ARG A O   1 
ATOM   1066 C CB  . ARG A 1 134 ? 30.464 6.907  -13.244 1.00 12.93 ? 134 ARG A CB  1 
ATOM   1067 C CG  . ARG A 1 134 ? 30.435 7.742  -14.525 1.00 13.76 ? 134 ARG A CG  1 
ATOM   1068 C CD  . ARG A 1 134 ? 29.109 7.594  -15.286 1.00 12.75 ? 134 ARG A CD  1 
ATOM   1069 N NE  . ARG A 1 134 ? 27.971 8.122  -14.532 1.00 13.09 ? 134 ARG A NE  1 
ATOM   1070 C CZ  . ARG A 1 134 ? 27.639 9.416  -14.484 1.00 12.84 ? 134 ARG A CZ  1 
ATOM   1071 N NH1 . ARG A 1 134 ? 28.354 10.328 -15.163 1.00 12.96 ? 134 ARG A NH1 1 
ATOM   1072 N NH2 . ARG A 1 134 ? 26.585 9.809  -13.776 1.00 13.02 ? 134 ARG A NH2 1 
ATOM   1073 N N   . PHE A 1 135 ? 31.958 4.902  -11.317 1.00 12.33 ? 135 PHE A N   1 
ATOM   1074 C CA  . PHE A 1 135 ? 31.840 4.021  -10.138 1.00 12.90 ? 135 PHE A CA  1 
ATOM   1075 C C   . PHE A 1 135 ? 33.039 4.087  -9.187  1.00 13.38 ? 135 PHE A C   1 
ATOM   1076 O O   . PHE A 1 135 ? 32.909 3.793  -7.991  1.00 13.59 ? 135 PHE A O   1 
ATOM   1077 C CB  . PHE A 1 135 ? 31.509 2.582  -10.554 1.00 12.68 ? 135 PHE A CB  1 
ATOM   1078 C CG  . PHE A 1 135 ? 30.182 2.459  -11.275 1.00 12.80 ? 135 PHE A CG  1 
ATOM   1079 C CD1 . PHE A 1 135 ? 28.981 2.627  -10.575 1.00 13.15 ? 135 PHE A CD1 1 
ATOM   1080 C CD2 . PHE A 1 135 ? 30.129 2.168  -12.633 1.00 14.22 ? 135 PHE A CD2 1 
ATOM   1081 C CE1 . PHE A 1 135 ? 27.753 2.518  -11.228 1.00 13.26 ? 135 PHE A CE1 1 
ATOM   1082 C CE2 . PHE A 1 135 ? 28.896 2.063  -13.309 1.00 16.01 ? 135 PHE A CE2 1 
ATOM   1083 C CZ  . PHE A 1 135 ? 27.709 2.238  -12.599 1.00 14.33 ? 135 PHE A CZ  1 
ATOM   1084 N N   . VAL A 1 136 ? 34.201 4.490  -9.704  1.00 13.94 ? 136 VAL A N   1 
ATOM   1085 C CA  . VAL A 1 136 ? 35.358 4.741  -8.836  1.00 14.03 ? 136 VAL A CA  1 
ATOM   1086 C C   . VAL A 1 136 ? 35.014 5.898  -7.895  1.00 13.54 ? 136 VAL A C   1 
ATOM   1087 O O   . VAL A 1 136 ? 35.185 5.781  -6.685  1.00 13.63 ? 136 VAL A O   1 
ATOM   1088 C CB  . VAL A 1 136 ? 36.648 5.104  -9.636  1.00 14.61 ? 136 VAL A CB  1 
ATOM   1089 C CG1 . VAL A 1 136 ? 37.767 5.508  -8.689  1.00 15.21 ? 136 VAL A CG1 1 
ATOM   1090 C CG2 . VAL A 1 136 ? 37.091 3.929  -10.476 1.00 14.99 ? 136 VAL A CG2 1 
ATOM   1091 N N   . TRP A 1 137 ? 34.500 6.998  -8.452  1.00 13.21 ? 137 TRP A N   1 
ATOM   1092 C CA  . TRP A 1 137 ? 34.099 8.150  -7.634  1.00 12.47 ? 137 TRP A CA  1 
ATOM   1093 C C   . TRP A 1 137 ? 32.968 7.796  -6.666  1.00 12.34 ? 137 TRP A C   1 
ATOM   1094 O O   . TRP A 1 137 ? 33.007 8.175  -5.490  1.00 12.49 ? 137 TRP A O   1 
ATOM   1095 C CB  . TRP A 1 137 ? 33.721 9.337  -8.517  1.00 13.97 ? 137 TRP A CB  1 
ATOM   1096 C CG  . TRP A 1 137 ? 34.903 9.858  -9.276  1.00 14.11 ? 137 TRP A CG  1 
ATOM   1097 C CD1 . TRP A 1 137 ? 35.164 9.696  -10.612 1.00 15.25 ? 137 TRP A CD1 1 
ATOM   1098 C CD2 . TRP A 1 137 ? 35.989 10.633 -8.744  1.00 14.99 ? 137 TRP A CD2 1 
ATOM   1099 N NE1 . TRP A 1 137 ? 36.350 10.335 -10.940 1.00 14.56 ? 137 TRP A NE1 1 
ATOM   1100 C CE2 . TRP A 1 137 ? 36.879 10.899 -9.812  1.00 14.83 ? 137 TRP A CE2 1 
ATOM   1101 C CE3 . TRP A 1 137 ? 36.310 11.109 -7.460  1.00 16.60 ? 137 TRP A CE3 1 
ATOM   1102 C CZ2 . TRP A 1 137 ? 38.055 11.646 -9.643  1.00 15.14 ? 137 TRP A CZ2 1 
ATOM   1103 C CZ3 . TRP A 1 137 ? 37.483 11.852 -7.294  1.00 16.63 ? 137 TRP A CZ3 1 
ATOM   1104 C CH2 . TRP A 1 137 ? 38.342 12.105 -8.382  1.00 15.78 ? 137 TRP A CH2 1 
ATOM   1105 N N   . TRP A 1 138 ? 31.985 7.041  -7.154  1.00 11.32 ? 138 TRP A N   1 
ATOM   1106 C CA  . TRP A 1 138 ? 30.911 6.522  -6.289  1.00 11.75 ? 138 TRP A CA  1 
ATOM   1107 C C   . TRP A 1 138 ? 31.471 5.723  -5.092  1.00 11.86 ? 138 TRP A C   1 
ATOM   1108 O O   . TRP A 1 138 ? 31.006 5.870  -3.948  1.00 11.64 ? 138 TRP A O   1 
ATOM   1109 C CB  . TRP A 1 138 ? 29.940 5.669  -7.123  1.00 11.92 ? 138 TRP A CB  1 
ATOM   1110 C CG  . TRP A 1 138 ? 28.917 4.935  -6.287  1.00 11.81 ? 138 TRP A CG  1 
ATOM   1111 C CD1 . TRP A 1 138 ? 27.673 5.381  -5.929  1.00 11.51 ? 138 TRP A CD1 1 
ATOM   1112 C CD2 . TRP A 1 138 ? 29.054 3.635  -5.701  1.00 12.83 ? 138 TRP A CD2 1 
ATOM   1113 N NE1 . TRP A 1 138 ? 27.030 4.443  -5.153  1.00 11.65 ? 138 TRP A NE1 1 
ATOM   1114 C CE2 . TRP A 1 138 ? 27.859 3.362  -5.000  1.00 12.11 ? 138 TRP A CE2 1 
ATOM   1115 C CE3 . TRP A 1 138 ? 30.077 2.673  -5.701  1.00 12.80 ? 138 TRP A CE3 1 
ATOM   1116 C CZ2 . TRP A 1 138 ? 27.667 2.173  -4.290  1.00 11.75 ? 138 TRP A CZ2 1 
ATOM   1117 C CZ3 . TRP A 1 138 ? 29.886 1.500  -5.007  1.00 12.81 ? 138 TRP A CZ3 1 
ATOM   1118 C CH2 . TRP A 1 138 ? 28.683 1.250  -4.321  1.00 12.93 ? 138 TRP A CH2 1 
ATOM   1119 N N   . ALA A 1 139 ? 32.470 4.878  -5.348  1.00 11.85 ? 139 ALA A N   1 
ATOM   1120 C CA  . ALA A 1 139 ? 33.075 4.065  -4.284  1.00 12.01 ? 139 ALA A CA  1 
ATOM   1121 C C   . ALA A 1 139 ? 33.822 4.920  -3.259  1.00 12.34 ? 139 ALA A C   1 
ATOM   1122 O O   . ALA A 1 139 ? 33.741 4.685  -2.055  1.00 12.93 ? 139 ALA A O   1 
ATOM   1123 C CB  . ALA A 1 139 ? 34.020 3.025  -4.890  1.00 12.66 ? 139 ALA A CB  1 
ATOM   1124 N N   . ILE A 1 140 ? 34.536 5.931  -3.731  1.00 12.58 ? 140 ILE A N   1 
ATOM   1125 C CA  . ILE A 1 140 ? 35.223 6.841  -2.821  1.00 12.56 ? 140 ILE A CA  1 
ATOM   1126 C C   . ILE A 1 140 ? 34.210 7.582  -1.937  1.00 12.63 ? 140 ILE A C   1 
ATOM   1127 O O   . ILE A 1 140 ? 34.373 7.705  -0.715  1.00 12.49 ? 140 ILE A O   1 
ATOM   1128 C CB  . ILE A 1 140 ? 36.093 7.829  -3.609  1.00 12.67 ? 140 ILE A CB  1 
ATOM   1129 C CG1 . ILE A 1 140 ? 37.209 7.060  -4.304  1.00 14.35 ? 140 ILE A CG1 1 
ATOM   1130 C CG2 . ILE A 1 140 ? 36.676 8.902  -2.680  1.00 13.09 ? 140 ILE A CG2 1 
ATOM   1131 C CD1 . ILE A 1 140 ? 37.946 7.891  -5.339  1.00 15.76 ? 140 ILE A CD1 1 
ATOM   1132 N N   . SER A 1 141 ? 33.157 8.064  -2.571  1.00 11.79 ? 141 SER A N   1 
ATOM   1133 C CA  . SER A 1 141 ? 32.102 8.800  -1.867  1.00 11.75 ? 141 SER A CA  1 
ATOM   1134 C C   . SER A 1 141 ? 31.417 7.907  -0.818  1.00 11.83 ? 141 SER A C   1 
ATOM   1135 O O   . SER A 1 141 ? 31.144 8.329  0.311   1.00 11.25 ? 141 SER A O   1 
ATOM   1136 C CB  . SER A 1 141 ? 31.094 9.288  -2.892  1.00 11.91 ? 141 SER A CB  1 
ATOM   1137 O OG  . SER A 1 141 ? 30.025 9.952  -2.257  1.00 12.30 ? 141 SER A OG  1 
ATOM   1138 N N   . THR A 1 142 ? 31.143 6.661  -1.210  1.00 11.85 ? 142 THR A N   1 
ATOM   1139 C CA  A THR A 1 142 ? 30.532 5.700  -0.305  0.80 11.58 ? 142 THR A CA  1 
ATOM   1140 C CA  B THR A 1 142 ? 30.515 5.720  -0.285  0.20 11.79 ? 142 THR A CA  1 
ATOM   1141 C C   . THR A 1 142 ? 31.443 5.414  0.897   1.00 11.72 ? 142 THR A C   1 
ATOM   1142 O O   . THR A 1 142 ? 30.983 5.342  2.037   1.00 11.30 ? 142 THR A O   1 
ATOM   1143 C CB  A THR A 1 142 ? 30.138 4.431  -1.093  0.80 11.55 ? 142 THR A CB  1 
ATOM   1144 C CB  B THR A 1 142 ? 29.966 4.432  -0.985  0.20 11.86 ? 142 THR A CB  1 
ATOM   1145 O OG1 A THR A 1 142 ? 29.133 4.802  -2.050  0.80 10.44 ? 142 THR A OG1 1 
ATOM   1146 O OG1 B THR A 1 142 ? 29.010 3.784  -0.133  0.20 11.78 ? 142 THR A OG1 1 
ATOM   1147 C CG2 A THR A 1 142 ? 29.586 3.317  -0.168  0.80 10.96 ? 142 THR A CG2 1 
ATOM   1148 C CG2 B THR A 1 142 ? 31.072 3.452  -1.331  0.20 11.85 ? 142 THR A CG2 1 
ATOM   1149 N N   . ALA A 1 143 ? 32.749 5.270  0.643   1.00 11.87 ? 143 ALA A N   1 
ATOM   1150 C CA  . ALA A 1 143 ? 33.704 5.086  1.746   1.00 12.01 ? 143 ALA A CA  1 
ATOM   1151 C C   . ALA A 1 143 ? 33.670 6.273  2.724   1.00 12.09 ? 143 ALA A C   1 
ATOM   1152 O O   . ALA A 1 143 ? 33.709 6.080  3.947   1.00 12.19 ? 143 ALA A O   1 
ATOM   1153 C CB  . ALA A 1 143 ? 35.118 4.886  1.221   1.00 12.79 ? 143 ALA A CB  1 
ATOM   1154 N N   . ALA A 1 144 ? 33.609 7.493  2.190   1.00 12.10 ? 144 ALA A N   1 
ATOM   1155 C CA  . ALA A 1 144 ? 33.509 8.682  3.041   1.00 12.23 ? 144 ALA A CA  1 
ATOM   1156 C C   . ALA A 1 144 ? 32.207 8.655  3.862   1.00 11.34 ? 144 ALA A C   1 
ATOM   1157 O O   . ALA A 1 144 ? 32.207 8.946  5.075   1.00 11.38 ? 144 ALA A O   1 
ATOM   1158 C CB  . ALA A 1 144 ? 33.595 9.942  2.207   1.00 11.40 ? 144 ALA A CB  1 
ATOM   1159 N N   . MET A 1 145 ? 31.098 8.260  3.230   1.00 11.21 ? 145 MET A N   1 
ATOM   1160 C CA  A MET A 1 145 ? 29.826 8.153  3.954   0.80 10.86 ? 145 MET A CA  1 
ATOM   1161 C CA  B MET A 1 145 ? 29.826 8.143  3.931   0.20 11.10 ? 145 MET A CA  1 
ATOM   1162 C C   . MET A 1 145 ? 29.948 7.137  5.078   1.00 10.74 ? 145 MET A C   1 
ATOM   1163 O O   . MET A 1 145 ? 29.484 7.372  6.192   1.00 10.36 ? 145 MET A O   1 
ATOM   1164 C CB  A MET A 1 145 ? 28.666 7.724  3.043   0.80 10.60 ? 145 MET A CB  1 
ATOM   1165 C CB  B MET A 1 145 ? 28.729 7.717  2.950   0.20 11.39 ? 145 MET A CB  1 
ATOM   1166 C CG  A MET A 1 145 ? 27.311 7.729  3.758   0.80 11.57 ? 145 MET A CG  1 
ATOM   1167 C CG  B MET A 1 145 ? 27.314 7.879  3.469   0.20 12.94 ? 145 MET A CG  1 
ATOM   1168 S SD  A MET A 1 145 ? 26.111 6.649  2.970   0.80 11.98 ? 145 MET A SD  1 
ATOM   1169 S SD  B MET A 1 145 ? 26.769 6.447  4.397   0.20 16.34 ? 145 MET A SD  1 
ATOM   1170 C CE  A MET A 1 145 ? 26.866 5.063  3.283   0.80 13.92 ? 145 MET A CE  1 
ATOM   1171 C CE  B MET A 1 145 ? 26.629 5.219  3.105   0.20 15.50 ? 145 MET A CE  1 
ATOM   1172 N N   . LEU A 1 146 ? 30.559 5.995  4.790   1.00 10.19 ? 146 LEU A N   1 
ATOM   1173 C CA  . LEU A 1 146 ? 30.664 4.960  5.818   1.00 11.00 ? 146 LEU A CA  1 
ATOM   1174 C C   . LEU A 1 146 ? 31.537 5.397  6.999   1.00 11.20 ? 146 LEU A C   1 
ATOM   1175 O O   . LEU A 1 146 ? 31.280 5.018  8.154   1.00 12.07 ? 146 LEU A O   1 
ATOM   1176 C CB  . LEU A 1 146 ? 31.150 3.639  5.212   1.00 11.45 ? 146 LEU A CB  1 
ATOM   1177 C CG  . LEU A 1 146 ? 30.099 3.047  4.272   1.00 11.70 ? 146 LEU A CG  1 
ATOM   1178 C CD1 . LEU A 1 146 ? 30.725 1.981  3.352   1.00 12.95 ? 146 LEU A CD1 1 
ATOM   1179 C CD2 . LEU A 1 146 ? 28.904 2.446  5.037   1.00 14.68 ? 146 LEU A CD2 1 
ATOM   1180 N N   . TYR A 1 147 ? 32.558 6.201  6.719   1.00 11.94 ? 147 TYR A N   1 
ATOM   1181 C CA  . TYR A 1 147 ? 33.340 6.819  7.784   1.00 12.43 ? 147 TYR A CA  1 
ATOM   1182 C C   . TYR A 1 147 ? 32.405 7.623  8.689   1.00 11.90 ? 147 TYR A C   1 
ATOM   1183 O O   . TYR A 1 147 ? 32.450 7.507  9.906   1.00 11.64 ? 147 TYR A O   1 
ATOM   1184 C CB  . TYR A 1 147 ? 34.439 7.733  7.205   1.00 13.67 ? 147 TYR A CB  1 
ATOM   1185 C CG  . TYR A 1 147 ? 35.109 8.560  8.277   1.00 15.05 ? 147 TYR A CG  1 
ATOM   1186 C CD1 . TYR A 1 147 ? 36.080 7.998  9.116   1.00 17.18 ? 147 TYR A CD1 1 
ATOM   1187 C CD2 . TYR A 1 147 ? 34.710 9.876  8.507   1.00 15.42 ? 147 TYR A CD2 1 
ATOM   1188 C CE1 . TYR A 1 147 ? 36.665 8.755  10.133  1.00 18.17 ? 147 TYR A CE1 1 
ATOM   1189 C CE2 . TYR A 1 147 ? 35.291 10.639 9.516   1.00 16.95 ? 147 TYR A CE2 1 
ATOM   1190 C CZ  . TYR A 1 147 ? 36.267 10.064 10.317  1.00 17.30 ? 147 TYR A CZ  1 
ATOM   1191 O OH  . TYR A 1 147 ? 36.835 10.813 11.326  1.00 19.09 ? 147 TYR A OH  1 
ATOM   1192 N N   . ILE A 1 148 ? 31.554 8.434  8.077   1.00 11.57 ? 148 ILE A N   1 
ATOM   1193 C CA  . ILE A 1 148 ? 30.640 9.271  8.847   1.00 11.17 ? 148 ILE A CA  1 
ATOM   1194 C C   . ILE A 1 148 ? 29.684 8.412  9.679   1.00 10.91 ? 148 ILE A C   1 
ATOM   1195 O O   . ILE A 1 148 ? 29.478 8.665  10.874  1.00 11.22 ? 148 ILE A O   1 
ATOM   1196 C CB  . ILE A 1 148 ? 29.849 10.204 7.917   1.00 10.96 ? 148 ILE A CB  1 
ATOM   1197 C CG1 . ILE A 1 148 ? 30.789 11.224 7.262   1.00 11.24 ? 148 ILE A CG1 1 
ATOM   1198 C CG2 . ILE A 1 148 ? 28.697 10.885 8.669   1.00 12.00 ? 148 ILE A CG2 1 
ATOM   1199 C CD1 . ILE A 1 148 ? 30.137 11.983 6.098   1.00 12.92 ? 148 ILE A CD1 1 
ATOM   1200 N N   . LEU A 1 149 ? 29.101 7.382  9.070   1.00 10.61 ? 149 LEU A N   1 
ATOM   1201 C CA  . LEU A 1 149 ? 28.152 6.543  9.813   1.00 11.03 ? 149 LEU A CA  1 
ATOM   1202 C C   . LEU A 1 149 ? 28.856 5.818  10.959  1.00 10.49 ? 149 LEU A C   1 
ATOM   1203 O O   . LEU A 1 149 ? 28.297 5.661  12.031  1.00 11.74 ? 149 LEU A O   1 
ATOM   1204 C CB  . LEU A 1 149 ? 27.414 5.563  8.890   1.00 11.06 ? 149 LEU A CB  1 
ATOM   1205 C CG  . LEU A 1 149 ? 26.586 6.252  7.797   1.00 12.17 ? 149 LEU A CG  1 
ATOM   1206 C CD1 . LEU A 1 149 ? 25.775 5.183  7.075   1.00 13.60 ? 149 LEU A CD1 1 
ATOM   1207 C CD2 . LEU A 1 149 ? 25.675 7.357  8.359   1.00 13.15 ? 149 LEU A CD2 1 
ATOM   1208 N N   . TYR A 1 150 ? 30.097 5.399  10.718  1.00 10.09 ? 150 TYR A N   1 
ATOM   1209 C CA  . TYR A 1 150 ? 30.885 4.744  11.769  1.00 11.31 ? 150 TYR A CA  1 
ATOM   1210 C C   . TYR A 1 150 ? 31.086 5.693  12.945  1.00 11.13 ? 150 TYR A C   1 
ATOM   1211 O O   . TYR A 1 150 ? 30.865 5.326  14.106  1.00 12.08 ? 150 TYR A O   1 
ATOM   1212 C CB  . TYR A 1 150 ? 32.238 4.262  11.232  1.00 11.78 ? 150 TYR A CB  1 
ATOM   1213 C CG  . TYR A 1 150 ? 33.013 3.490  12.280  1.00 12.14 ? 150 TYR A CG  1 
ATOM   1214 C CD1 . TYR A 1 150 ? 33.034 2.091  12.273  1.00 13.55 ? 150 TYR A CD1 1 
ATOM   1215 C CD2 . TYR A 1 150 ? 33.713 4.168  13.285  1.00 13.60 ? 150 TYR A CD2 1 
ATOM   1216 C CE1 . TYR A 1 150 ? 33.750 1.381  13.261  1.00 15.69 ? 150 TYR A CE1 1 
ATOM   1217 C CE2 . TYR A 1 150 ? 34.416 3.471  14.265  1.00 14.35 ? 150 TYR A CE2 1 
ATOM   1218 C CZ  . TYR A 1 150 ? 34.429 2.093  14.241  1.00 16.57 ? 150 TYR A CZ  1 
ATOM   1219 O OH  . TYR A 1 150 ? 35.134 1.437  15.227  1.00 17.59 ? 150 TYR A OH  1 
ATOM   1220 N N   . VAL A 1 151 ? 31.491 6.927  12.657  1.00 11.63 ? 151 VAL A N   1 
ATOM   1221 C CA  A VAL A 1 151 ? 31.738 7.934  13.694  0.60 12.30 ? 151 VAL A CA  1 
ATOM   1222 C CA  B VAL A 1 151 ? 31.746 7.845  13.755  0.40 12.12 ? 151 VAL A CA  1 
ATOM   1223 C C   . VAL A 1 151 ? 30.450 8.240  14.462  1.00 12.23 ? 151 VAL A C   1 
ATOM   1224 O O   . VAL A 1 151 ? 30.456 8.389  15.680  1.00 12.62 ? 151 VAL A O   1 
ATOM   1225 C CB  A VAL A 1 151 ? 32.298 9.231  13.069  0.60 12.28 ? 151 VAL A CB  1 
ATOM   1226 C CB  B VAL A 1 151 ? 32.608 9.058  13.354  0.40 12.25 ? 151 VAL A CB  1 
ATOM   1227 C CG1 A VAL A 1 151 ? 32.375 10.355 14.091  0.60 13.56 ? 151 VAL A CG1 1 
ATOM   1228 C CG1 B VAL A 1 151 ? 34.001 8.591  12.931  0.40 12.30 ? 151 VAL A CG1 1 
ATOM   1229 C CG2 A VAL A 1 151 ? 33.684 8.982  12.480  0.60 13.44 ? 151 VAL A CG2 1 
ATOM   1230 C CG2 B VAL A 1 151 ? 31.956 9.869  12.257  0.40 13.04 ? 151 VAL A CG2 1 
ATOM   1231 N N   . LEU A 1 152 ? 29.340 8.347  13.724  1.00 12.51 ? 152 LEU A N   1 
ATOM   1232 C CA  . LEU A 1 152 ? 28.045 8.612  14.371  1.00 12.75 ? 152 LEU A CA  1 
ATOM   1233 C C   . LEU A 1 152 ? 27.660 7.452  15.277  1.00 13.37 ? 152 LEU A C   1 
ATOM   1234 O O   . LEU A 1 152 ? 27.241 7.646  16.422  1.00 13.83 ? 152 LEU A O   1 
ATOM   1235 C CB  . LEU A 1 152 ? 26.936 8.814  13.343  1.00 13.51 ? 152 LEU A CB  1 
ATOM   1236 C CG  . LEU A 1 152 ? 26.956 10.091 12.518  1.00 15.51 ? 152 LEU A CG  1 
ATOM   1237 C CD1 . LEU A 1 152 ? 25.709 10.090 11.643  1.00 16.40 ? 152 LEU A CD1 1 
ATOM   1238 C CD2 . LEU A 1 152 ? 26.981 11.331 13.395  1.00 17.29 ? 152 LEU A CD2 1 
ATOM   1239 N N   . PHE A 1 153 ? 27.828 6.232  14.770  1.00 13.20 ? 153 PHE A N   1 
ATOM   1240 C CA  . PHE A 1 153 ? 27.359 5.065  15.497  1.00 13.64 ? 153 PHE A CA  1 
ATOM   1241 C C   . PHE A 1 153 ? 28.210 4.758  16.716  1.00 14.20 ? 153 PHE A C   1 
ATOM   1242 O O   . PHE A 1 153 ? 27.678 4.405  17.766  1.00 15.37 ? 153 PHE A O   1 
ATOM   1243 C CB  . PHE A 1 153 ? 27.278 3.830  14.587  1.00 13.67 ? 153 PHE A CB  1 
ATOM   1244 C CG  . PHE A 1 153 ? 26.545 2.666  15.218  1.00 14.80 ? 153 PHE A CG  1 
ATOM   1245 C CD1 . PHE A 1 153 ? 27.238 1.529  15.627  1.00 15.06 ? 153 PHE A CD1 1 
ATOM   1246 C CD2 . PHE A 1 153 ? 25.171 2.717  15.395  1.00 16.07 ? 153 PHE A CD2 1 
ATOM   1247 C CE1 . PHE A 1 153 ? 26.560 0.446  16.228  1.00 18.29 ? 153 PHE A CE1 1 
ATOM   1248 C CE2 . PHE A 1 153 ? 24.489 1.645  15.993  1.00 16.88 ? 153 PHE A CE2 1 
ATOM   1249 C CZ  . PHE A 1 153 ? 25.190 0.510  16.391  1.00 16.48 ? 153 PHE A CZ  1 
ATOM   1250 N N   . PHE A 1 154 ? 29.528 4.864  16.575  1.00 13.89 ? 154 PHE A N   1 
ATOM   1251 C CA  . PHE A 1 154 ? 30.433 4.534  17.668  1.00 14.68 ? 154 PHE A CA  1 
ATOM   1252 C C   . PHE A 1 154 ? 30.813 5.773  18.460  1.00 15.11 ? 154 PHE A C   1 
ATOM   1253 O O   . PHE A 1 154 ? 30.482 5.874  19.646  1.00 15.99 ? 154 PHE A O   1 
ATOM   1254 C CB  . PHE A 1 154 ? 31.650 3.771  17.131  1.00 15.17 ? 154 PHE A CB  1 
ATOM   1255 C CG  . PHE A 1 154 ? 31.333 2.352  16.740  1.00 15.00 ? 154 PHE A CG  1 
ATOM   1256 C CD1 . PHE A 1 154 ? 31.230 1.364  17.715  1.00 17.60 ? 154 PHE A CD1 1 
ATOM   1257 C CD2 . PHE A 1 154 ? 31.136 2.006  15.408  1.00 16.39 ? 154 PHE A CD2 1 
ATOM   1258 C CE1 . PHE A 1 154 ? 30.912 0.048  17.365  1.00 17.52 ? 154 PHE A CE1 1 
ATOM   1259 C CE2 . PHE A 1 154 ? 30.831 0.696  15.043  1.00 15.94 ? 154 PHE A CE2 1 
ATOM   1260 C CZ  . PHE A 1 154 ? 30.720 -0.285 16.027  1.00 17.73 ? 154 PHE A CZ  1 
ATOM   1261 N N   . GLY A 1 155 ? 31.447 6.736  17.798  1.00 14.87 ? 155 GLY A N   1 
ATOM   1262 C CA  . GLY A 1 155 ? 31.962 7.940  18.480  1.00 14.40 ? 155 GLY A CA  1 
ATOM   1263 C C   . GLY A 1 155 ? 30.895 8.825  19.106  1.00 13.76 ? 155 GLY A C   1 
ATOM   1264 O O   . GLY A 1 155 ? 30.974 9.188  20.299  1.00 14.12 ? 155 GLY A O   1 
ATOM   1265 N N   . PHE A 1 156 ? 29.892 9.198  18.319  1.00 13.70 ? 156 PHE A N   1 
ATOM   1266 C CA  . PHE A 1 156 ? 28.861 10.097 18.842  1.00 13.26 ? 156 PHE A CA  1 
ATOM   1267 C C   . PHE A 1 156 ? 28.037 9.394  19.920  1.00 12.84 ? 156 PHE A C   1 
ATOM   1268 O O   . PHE A 1 156 ? 27.629 10.022 20.898  1.00 13.03 ? 156 PHE A O   1 
ATOM   1269 C CB  . PHE A 1 156 ? 27.940 10.634 17.734  1.00 13.24 ? 156 PHE A CB  1 
ATOM   1270 C CG  . PHE A 1 156 ? 28.532 11.765 16.906  1.00 14.42 ? 156 PHE A CG  1 
ATOM   1271 C CD1 . PHE A 1 156 ? 29.851 11.735 16.463  1.00 15.48 ? 156 PHE A CD1 1 
ATOM   1272 C CD2 . PHE A 1 156 ? 27.715 12.818 16.497  1.00 14.18 ? 156 PHE A CD2 1 
ATOM   1273 C CE1 . PHE A 1 156 ? 30.363 12.773 15.655  1.00 17.07 ? 156 PHE A CE1 1 
ATOM   1274 C CE2 . PHE A 1 156 ? 28.216 13.862 15.683  1.00 15.70 ? 156 PHE A CE2 1 
ATOM   1275 C CZ  . PHE A 1 156 ? 29.548 13.834 15.274  1.00 14.30 ? 156 PHE A CZ  1 
ATOM   1276 N N   . THR A 1 157 ? 27.801 8.093  19.756  1.00 12.41 ? 157 THR A N   1 
ATOM   1277 C CA  . THR A 1 157 ? 27.035 7.354  20.750  1.00 13.13 ? 157 THR A CA  1 
ATOM   1278 C C   . THR A 1 157 ? 27.793 7.305  22.064  1.00 13.38 ? 157 THR A C   1 
ATOM   1279 O O   . THR A 1 157 ? 27.194 7.517  23.119  1.00 14.45 ? 157 THR A O   1 
ATOM   1280 C CB  . THR A 1 157 ? 26.656 5.951  20.272  1.00 12.62 ? 157 THR A CB  1 
ATOM   1281 O OG1 . THR A 1 157 ? 25.897 6.077  19.062  1.00 12.80 ? 157 THR A OG1 1 
ATOM   1282 C CG2 . THR A 1 157 ? 25.807 5.239  21.323  1.00 14.46 ? 157 THR A CG2 1 
ATOM   1283 N N   . SER A 1 158 ? 29.108 7.102  21.996  1.00 13.95 ? 158 SER A N   1 
ATOM   1284 C CA  A SER A 1 158 ? 29.937 7.106  23.206  0.60 14.11 ? 158 SER A CA  1 
ATOM   1285 C CA  B SER A 1 158 ? 29.937 7.109  23.201  0.40 14.29 ? 158 SER A CA  1 
ATOM   1286 C C   . SER A 1 158 ? 29.807 8.439  23.942  1.00 14.46 ? 158 SER A C   1 
ATOM   1287 O O   . SER A 1 158 ? 29.654 8.466  25.171  1.00 14.33 ? 158 SER A O   1 
ATOM   1288 C CB  A SER A 1 158 ? 31.404 6.843  22.875  0.60 14.54 ? 158 SER A CB  1 
ATOM   1289 C CB  B SER A 1 158 ? 31.394 6.824  22.847  0.40 14.61 ? 158 SER A CB  1 
ATOM   1290 O OG  A SER A 1 158 ? 32.156 6.728  24.074  0.60 15.23 ? 158 SER A OG  1 
ATOM   1291 O OG  B SER A 1 158 ? 31.554 5.459  22.510  0.40 16.00 ? 158 SER A OG  1 
ATOM   1292 N N   . LYS A 1 159 ? 29.856 9.543  23.194  1.00 14.70 ? 159 LYS A N   1 
ATOM   1293 C CA  . LYS A 1 159 ? 29.645 10.889 23.765  1.00 14.98 ? 159 LYS A CA  1 
ATOM   1294 C C   . LYS A 1 159 ? 28.237 11.063 24.344  1.00 15.23 ? 159 LYS A C   1 
ATOM   1295 O O   . LYS A 1 159 ? 28.058 11.674 25.394  1.00 15.17 ? 159 LYS A O   1 
ATOM   1296 C CB  . LYS A 1 159 ? 29.904 11.969 22.705  1.00 15.55 ? 159 LYS A CB  1 
ATOM   1297 C CG  . LYS A 1 159 ? 31.372 12.168 22.388  1.00 17.70 ? 159 LYS A CG  1 
ATOM   1298 C CD  . LYS A 1 159 ? 32.032 12.911 23.549  1.00 20.83 ? 159 LYS A CD  1 
ATOM   1299 C CE  . LYS A 1 159 ? 33.499 13.171 23.291  1.00 24.77 ? 159 LYS A CE  1 
ATOM   1300 N NZ  . LYS A 1 159 ? 34.098 13.906 24.447  1.00 26.58 ? 159 LYS A NZ  1 
ATOM   1301 N N   . ALA A 1 160 ? 27.236 10.526 23.652  1.00 14.58 ? 160 ALA A N   1 
ATOM   1302 C CA  . ALA A 1 160 ? 25.851 10.614 24.102  1.00 15.52 ? 160 ALA A CA  1 
ATOM   1303 C C   . ALA A 1 160 ? 25.644 9.974  25.466  1.00 16.65 ? 160 ALA A C   1 
ATOM   1304 O O   . ALA A 1 160 ? 24.825 10.454 26.254  1.00 16.42 ? 160 ALA A O   1 
ATOM   1305 C CB  . ALA A 1 160 ? 24.918 9.990  23.068  1.00 15.49 ? 160 ALA A CB  1 
ATOM   1306 N N   . GLU A 1 161 ? 26.420 8.928  25.746  1.00 17.28 ? 161 GLU A N   1 
ATOM   1307 C CA  A GLU A 1 161 ? 26.245 8.189  26.993  0.35 17.59 ? 161 GLU A CA  1 
ATOM   1308 C CA  B GLU A 1 161 ? 26.294 8.175  26.995  0.35 17.68 ? 161 GLU A CA  1 
ATOM   1309 C CA  C GLU A 1 161 ? 26.313 8.163  26.994  0.30 17.63 ? 161 GLU A CA  1 
ATOM   1310 C C   . GLU A 1 161 ? 26.634 9.002  28.229  1.00 17.50 ? 161 GLU A C   1 
ATOM   1311 O O   . GLU A 1 161 ? 26.306 8.612  29.357  1.00 18.33 ? 161 GLU A O   1 
ATOM   1312 C CB  A GLU A 1 161 ? 26.971 6.837  26.955  0.35 18.14 ? 161 GLU A CB  1 
ATOM   1313 C CB  B GLU A 1 161 ? 27.155 6.913  26.950  0.35 18.30 ? 161 GLU A CB  1 
ATOM   1314 C CB  C GLU A 1 161 ? 27.229 6.929  26.968  0.30 18.19 ? 161 GLU A CB  1 
ATOM   1315 C CG  A GLU A 1 161 ? 26.545 5.916  25.804  0.35 19.04 ? 161 GLU A CG  1 
ATOM   1316 C CG  B GLU A 1 161 ? 26.459 5.745  26.279  0.35 19.65 ? 161 GLU A CG  1 
ATOM   1317 C CG  C GLU A 1 161 ? 26.934 5.907  25.863  0.30 19.37 ? 161 GLU A CG  1 
ATOM   1318 C CD  A GLU A 1 161 ? 25.058 5.990  25.484  0.35 19.58 ? 161 GLU A CD  1 
ATOM   1319 C CD  B GLU A 1 161 ? 27.417 4.687  25.772  0.35 20.91 ? 161 GLU A CD  1 
ATOM   1320 C CD  C GLU A 1 161 ? 25.587 5.205  26.006  0.30 20.95 ? 161 GLU A CD  1 
ATOM   1321 O OE1 A GLU A 1 161 ? 24.233 5.617  26.348  0.35 21.16 ? 161 GLU A OE1 1 
ATOM   1322 O OE1 B GLU A 1 161 ? 28.594 4.665  26.200  0.35 21.57 ? 161 GLU A OE1 1 
ATOM   1323 O OE1 C GLU A 1 161 ? 24.986 5.240  27.106  0.30 22.09 ? 161 GLU A OE1 1 
ATOM   1324 O OE2 A GLU A 1 161 ? 24.715 6.419  24.359  0.35 20.61 ? 161 GLU A OE2 1 
ATOM   1325 O OE2 B GLU A 1 161 ? 26.985 3.873  24.932  0.35 22.61 ? 161 GLU A OE2 1 
ATOM   1326 O OE2 C GLU A 1 161 ? 25.132 4.603  25.009  0.30 21.21 ? 161 GLU A OE2 1 
ATOM   1327 N N   . SER A 1 162 ? 27.300 10.141 28.021  1.00 16.49 ? 162 SER A N   1 
ATOM   1328 C CA  A SER A 1 162 ? 27.642 11.044 29.123  0.80 16.12 ? 162 SER A CA  1 
ATOM   1329 C CA  B SER A 1 162 ? 27.641 11.036 29.131  0.20 15.73 ? 162 SER A CA  1 
ATOM   1330 C C   . SER A 1 162 ? 26.573 12.106 29.366  1.00 15.36 ? 162 SER A C   1 
ATOM   1331 O O   . SER A 1 162 ? 26.638 12.851 30.345  1.00 15.04 ? 162 SER A O   1 
ATOM   1332 C CB  A SER A 1 162 ? 28.995 11.707 28.867  0.80 16.88 ? 162 SER A CB  1 
ATOM   1333 C CB  B SER A 1 162 ? 29.008 11.686 28.907  0.20 15.95 ? 162 SER A CB  1 
ATOM   1334 O OG  A SER A 1 162 ? 30.025 10.741 28.992  0.80 19.61 ? 162 SER A OG  1 
ATOM   1335 O OG  B SER A 1 162 ? 29.012 12.463 27.728  0.20 15.67 ? 162 SER A OG  1 
ATOM   1336 N N   . MET A 1 163 ? 25.595 12.172 28.468  1.00 14.32 ? 163 MET A N   1 
ATOM   1337 C CA  . MET A 1 163 ? 24.500 13.140 28.578  1.00 14.59 ? 163 MET A CA  1 
ATOM   1338 C C   . MET A 1 163 ? 23.353 12.572 29.412  1.00 14.45 ? 163 MET A C   1 
ATOM   1339 O O   . MET A 1 163 ? 23.342 11.369 29.707  1.00 14.19 ? 163 MET A O   1 
ATOM   1340 C CB  . MET A 1 163 ? 23.984 13.505 27.170  1.00 14.89 ? 163 MET A CB  1 
ATOM   1341 C CG  . MET A 1 163 ? 25.069 14.000 26.204  1.00 17.86 ? 163 MET A CG  1 
ATOM   1342 S SD  . MET A 1 163 ? 25.916 15.509 26.773  1.00 25.34 ? 163 MET A SD  1 
ATOM   1343 C CE  . MET A 1 163 ? 24.696 16.729 26.383  1.00 25.89 ? 163 MET A CE  1 
ATOM   1344 N N   . ARG A 1 164 ? 22.395 13.428 29.795  1.00 14.84 ? 164 ARG A N   1 
ATOM   1345 C CA  A ARG A 1 164 ? 21.162 12.970 30.443  0.60 15.75 ? 164 ARG A CA  1 
ATOM   1346 C CA  B ARG A 1 164 ? 21.188 12.944 30.459  0.40 15.49 ? 164 ARG A CA  1 
ATOM   1347 C C   . ARG A 1 164 ? 20.510 11.912 29.555  1.00 15.74 ? 164 ARG A C   1 
ATOM   1348 O O   . ARG A 1 164 ? 20.553 12.040 28.332  1.00 15.04 ? 164 ARG A O   1 
ATOM   1349 C CB  A ARG A 1 164 ? 20.161 14.117 30.609  0.60 15.89 ? 164 ARG A CB  1 
ATOM   1350 C CB  B ARG A 1 164 ? 20.222 14.089 30.777  0.40 15.56 ? 164 ARG A CB  1 
ATOM   1351 C CG  A ARG A 1 164 ? 20.615 15.267 31.476  0.60 17.48 ? 164 ARG A CG  1 
ATOM   1352 C CG  B ARG A 1 164 ? 20.593 14.898 32.006  0.40 16.44 ? 164 ARG A CG  1 
ATOM   1353 C CD  A ARG A 1 164 ? 19.482 16.274 31.669  0.60 18.09 ? 164 ARG A CD  1 
ATOM   1354 C CD  B ARG A 1 164 ? 19.516 15.912 32.367  0.40 17.06 ? 164 ARG A CD  1 
ATOM   1355 N NE  A ARG A 1 164 ? 19.186 17.079 30.481  0.60 23.72 ? 164 ARG A NE  1 
ATOM   1356 N NE  B ARG A 1 164 ? 19.953 16.828 33.422  0.40 20.11 ? 164 ARG A NE  1 
ATOM   1357 C CZ  A ARG A 1 164 ? 18.084 16.966 29.739  0.60 23.72 ? 164 ARG A CZ  1 
ATOM   1358 C CZ  B ARG A 1 164 ? 19.256 17.872 33.864  0.40 21.50 ? 164 ARG A CZ  1 
ATOM   1359 N NH1 A ARG A 1 164 ? 17.150 16.072 30.044  0.60 25.21 ? 164 ARG A NH1 1 
ATOM   1360 N NH1 B ARG A 1 164 ? 18.068 18.164 33.347  0.40 22.05 ? 164 ARG A NH1 1 
ATOM   1361 N NH2 A ARG A 1 164 ? 17.911 17.755 28.691  0.60 25.17 ? 164 ARG A NH2 1 
ATOM   1362 N NH2 B ARG A 1 164 ? 19.753 18.636 34.826  0.40 22.83 ? 164 ARG A NH2 1 
ATOM   1363 N N   . PRO A 1 165 ? 19.911 10.867 30.155  1.00 15.79 ? 165 PRO A N   1 
ATOM   1364 C CA  . PRO A 1 165 ? 19.244 9.859  29.328  1.00 15.92 ? 165 PRO A CA  1 
ATOM   1365 C C   . PRO A 1 165 ? 18.262 10.407 28.295  1.00 16.20 ? 165 PRO A C   1 
ATOM   1366 O O   . PRO A 1 165 ? 18.189 9.836  27.192  1.00 16.59 ? 165 PRO A O   1 
ATOM   1367 C CB  . PRO A 1 165 ? 18.542 8.969  30.356  1.00 16.54 ? 165 PRO A CB  1 
ATOM   1368 C CG  . PRO A 1 165 ? 19.434 9.045  31.527  1.00 17.02 ? 165 PRO A CG  1 
ATOM   1369 C CD  . PRO A 1 165 ? 19.872 10.486 31.584  1.00 15.98 ? 165 PRO A CD  1 
ATOM   1370 N N   . GLU A 1 166 ? 17.550 11.494 28.599  1.00 15.95 ? 166 GLU A N   1 
ATOM   1371 C CA  A GLU A 1 166 ? 16.599 12.027 27.623  0.60 16.12 ? 166 GLU A CA  1 
ATOM   1372 C CA  B GLU A 1 166 ? 16.602 12.107 27.652  0.40 16.50 ? 166 GLU A CA  1 
ATOM   1373 C C   . GLU A 1 166 ? 17.306 12.592 26.384  1.00 16.14 ? 166 GLU A C   1 
ATOM   1374 O O   . GLU A 1 166 ? 16.772 12.492 25.270  1.00 15.76 ? 166 GLU A O   1 
ATOM   1375 C CB  A GLU A 1 166 ? 15.629 13.030 28.259  0.60 16.45 ? 166 GLU A CB  1 
ATOM   1376 C CB  B GLU A 1 166 ? 15.836 13.270 28.308  0.40 16.61 ? 166 GLU A CB  1 
ATOM   1377 C CG  A GLU A 1 166 ? 14.533 13.529 27.311  0.60 17.99 ? 166 GLU A CG  1 
ATOM   1378 C CG  B GLU A 1 166 ? 16.715 14.439 28.772  0.40 17.80 ? 166 GLU A CG  1 
ATOM   1379 C CD  A GLU A 1 166 ? 15.037 14.616 26.383  0.60 18.24 ? 166 GLU A CD  1 
ATOM   1380 C CD  B GLU A 1 166 ? 15.930 15.668 29.202  0.40 18.44 ? 166 GLU A CD  1 
ATOM   1381 O OE1 A GLU A 1 166 ? 15.971 15.341 26.793  0.60 18.87 ? 166 GLU A OE1 1 
ATOM   1382 O OE1 B GLU A 1 166 ? 14.866 15.517 29.848  0.40 21.34 ? 166 GLU A OE1 1 
ATOM   1383 O OE2 A GLU A 1 166 ? 14.520 14.728 25.242  0.60 20.68 ? 166 GLU A OE2 1 
ATOM   1384 O OE2 B GLU A 1 166 ? 16.392 16.792 28.904  0.40 21.49 ? 166 GLU A OE2 1 
ATOM   1385 N N   . VAL A 1 167 ? 18.498 13.151 26.569  1.00 14.81 ? 167 VAL A N   1 
ATOM   1386 C CA  . VAL A 1 167 ? 19.308 13.669 25.467  1.00 14.16 ? 167 VAL A CA  1 
ATOM   1387 C C   . VAL A 1 167 ? 19.884 12.480 24.695  1.00 13.58 ? 167 VAL A C   1 
ATOM   1388 O O   . VAL A 1 167 ? 19.825 12.436 23.452  1.00 13.35 ? 167 VAL A O   1 
ATOM   1389 C CB  . VAL A 1 167 ? 20.446 14.603 25.977  1.00 14.44 ? 167 VAL A CB  1 
ATOM   1390 C CG1 . VAL A 1 167 ? 21.398 14.964 24.845  1.00 15.16 ? 167 VAL A CG1 1 
ATOM   1391 C CG2 . VAL A 1 167 ? 19.857 15.859 26.575  1.00 14.69 ? 167 VAL A CG2 1 
ATOM   1392 N N   . ALA A 1 168 ? 20.430 11.500 25.417  1.00 13.69 ? 168 ALA A N   1 
ATOM   1393 C CA  . ALA A 1 168 ? 20.969 10.303 24.756  1.00 13.69 ? 168 ALA A CA  1 
ATOM   1394 C C   . ALA A 1 168 ? 19.894 9.592  23.927  1.00 13.60 ? 168 ALA A C   1 
ATOM   1395 O O   . ALA A 1 168 ? 20.165 9.132  22.806  1.00 13.80 ? 168 ALA A O   1 
ATOM   1396 C CB  . ALA A 1 168 ? 21.549 9.340  25.785  1.00 13.99 ? 168 ALA A CB  1 
ATOM   1397 N N   . SER A 1 169 ? 18.678 9.525  24.466  1.00 13.65 ? 169 SER A N   1 
ATOM   1398 C CA  A SER A 1 169 ? 17.558 8.838  23.813  0.50 14.02 ? 169 SER A CA  1 
ATOM   1399 C CA  B SER A 1 169 ? 17.592 8.821  23.785  0.50 13.72 ? 169 SER A CA  1 
ATOM   1400 C C   . SER A 1 169 ? 17.163 9.517  22.505  1.00 13.34 ? 169 SER A C   1 
ATOM   1401 O O   . SER A 1 169 ? 16.946 8.856  21.487  1.00 13.96 ? 169 SER A O   1 
ATOM   1402 C CB  A SER A 1 169 ? 16.346 8.791  24.750  0.50 14.38 ? 169 SER A CB  1 
ATOM   1403 C CB  B SER A 1 169 ? 16.403 8.632  24.719  0.50 14.14 ? 169 SER A CB  1 
ATOM   1404 O OG  A SER A 1 169 ? 15.321 7.987  24.197  0.50 16.41 ? 169 SER A OG  1 
ATOM   1405 O OG  B SER A 1 169 ? 16.756 7.717  25.730  0.50 14.08 ? 169 SER A OG  1 
ATOM   1406 N N   . THR A 1 170 ? 17.045 10.841 22.552  1.00 13.03 ? 170 THR A N   1 
ATOM   1407 C CA  . THR A 1 170 ? 16.719 11.634 21.361  1.00 12.68 ? 170 THR A CA  1 
ATOM   1408 C C   . THR A 1 170 ? 17.842 11.481 20.337  1.00 12.10 ? 170 THR A C   1 
ATOM   1409 O O   . THR A 1 170 ? 17.572 11.244 19.134  1.00 12.01 ? 170 THR A O   1 
ATOM   1410 C CB  . THR A 1 170 ? 16.497 13.118 21.730  1.00 13.76 ? 170 THR A CB  1 
ATOM   1411 O OG1 . THR A 1 170 ? 15.381 13.207 22.627  1.00 14.43 ? 170 THR A OG1 1 
ATOM   1412 C CG2 . THR A 1 170 ? 16.201 13.967 20.488  1.00 13.31 ? 170 THR A CG2 1 
ATOM   1413 N N   . PHE A 1 171 ? 19.090 11.558 20.806  1.00 11.68 ? 171 PHE A N   1 
ATOM   1414 C CA  . PHE A 1 171 ? 20.216 11.331 19.894  1.00 11.28 ? 171 PHE A CA  1 
ATOM   1415 C C   . PHE A 1 171 ? 20.103 9.964  19.216  1.00 11.51 ? 171 PHE A C   1 
ATOM   1416 O O   . PHE A 1 171 ? 20.323 9.855  18.007  1.00 11.84 ? 171 PHE A O   1 
ATOM   1417 C CB  . PHE A 1 171 ? 21.591 11.429 20.574  1.00 11.51 ? 171 PHE A CB  1 
ATOM   1418 C CG  . PHE A 1 171 ? 22.692 10.852 19.712  1.00 10.63 ? 171 PHE A CG  1 
ATOM   1419 C CD1 . PHE A 1 171 ? 23.159 11.554 18.608  1.00 12.07 ? 171 PHE A CD1 1 
ATOM   1420 C CD2 . PHE A 1 171 ? 23.181 9.568  19.955  1.00 12.11 ? 171 PHE A CD2 1 
ATOM   1421 C CE1 . PHE A 1 171 ? 24.131 11.010 17.781  1.00 12.35 ? 171 PHE A CE1 1 
ATOM   1422 C CE2 . PHE A 1 171 ? 24.155 9.018  19.149  1.00 12.63 ? 171 PHE A CE2 1 
ATOM   1423 C CZ  . PHE A 1 171 ? 24.615 9.735  18.045  1.00 12.51 ? 171 PHE A CZ  1 
ATOM   1424 N N   . LYS A 1 172 ? 19.784 8.917  19.984  1.00 11.54 ? 172 LYS A N   1 
ATOM   1425 C CA  . LYS A 1 172 ? 19.757 7.568  19.389  1.00 11.93 ? 172 LYS A CA  1 
ATOM   1426 C C   . LYS A 1 172 ? 18.681 7.437  18.320  1.00 11.59 ? 172 LYS A C   1 
ATOM   1427 O O   . LYS A 1 172 ? 18.912 6.812  17.281  1.00 11.58 ? 172 LYS A O   1 
ATOM   1428 C CB  . LYS A 1 172 ? 19.622 6.482  20.459  1.00 12.35 ? 172 LYS A CB  1 
ATOM   1429 C CG  . LYS A 1 172 ? 20.868 6.340  21.299  1.00 15.34 ? 172 LYS A CG  1 
ATOM   1430 C CD  . LYS A 1 172 ? 20.627 5.328  22.406  1.00 19.53 ? 172 LYS A CD  1 
ATOM   1431 C CE  . LYS A 1 172 ? 21.815 5.269  23.346  1.00 24.57 ? 172 LYS A CE  1 
ATOM   1432 N NZ  . LYS A 1 172 ? 21.613 4.248  24.422  1.00 27.11 ? 172 LYS A NZ  1 
ATOM   1433 N N   . VAL A 1 173 ? 17.527 8.060  18.538  1.00 11.22 ? 173 VAL A N   1 
ATOM   1434 C CA  . VAL A 1 173 ? 16.468 8.033  17.517  1.00 11.21 ? 173 VAL A CA  1 
ATOM   1435 C C   . VAL A 1 173 ? 16.973 8.719  16.238  1.00 11.02 ? 173 VAL A C   1 
ATOM   1436 O O   . VAL A 1 173 ? 16.860 8.185  15.131  1.00 11.63 ? 173 VAL A O   1 
ATOM   1437 C CB  . VAL A 1 173 ? 15.173 8.703  18.004  1.00 11.13 ? 173 VAL A CB  1 
ATOM   1438 C CG1 . VAL A 1 173 ? 14.160 8.836  16.842  1.00 13.18 ? 173 VAL A CG1 1 
ATOM   1439 C CG2 . VAL A 1 173 ? 14.575 7.907  19.163  1.00 12.89 ? 173 VAL A CG2 1 
ATOM   1440 N N   . LEU A 1 174 ? 17.551 9.908  16.401  1.00 10.31 ? 174 LEU A N   1 
ATOM   1441 C CA  . LEU A 1 174 ? 17.996 10.690 15.241  1.00 10.62 ? 174 LEU A CA  1 
ATOM   1442 C C   . LEU A 1 174 ? 19.169 10.000 14.544  1.00 10.58 ? 174 LEU A C   1 
ATOM   1443 O O   . LEU A 1 174 ? 19.276 10.020 13.295  1.00 11.65 ? 174 LEU A O   1 
ATOM   1444 C CB  . LEU A 1 174 ? 18.392 12.091 15.683  1.00 10.88 ? 174 LEU A CB  1 
ATOM   1445 C CG  . LEU A 1 174 ? 17.208 12.915 16.187  1.00 10.27 ? 174 LEU A CG  1 
ATOM   1446 C CD1 . LEU A 1 174 ? 17.736 14.160 16.911  1.00 12.09 ? 174 LEU A CD1 1 
ATOM   1447 C CD2 . LEU A 1 174 ? 16.292 13.302 15.026  1.00 12.84 ? 174 LEU A CD2 1 
ATOM   1448 N N   . ARG A 1 175 ? 20.046 9.392  15.338  1.00 10.72 ? 175 ARG A N   1 
ATOM   1449 C CA  . ARG A 1 175 ? 21.176 8.629  14.799  1.00 10.39 ? 175 ARG A CA  1 
ATOM   1450 C C   . ARG A 1 175 ? 20.637 7.498  13.926  1.00 10.52 ? 175 ARG A C   1 
ATOM   1451 O O   . ARG A 1 175 ? 21.107 7.268  12.804  1.00 11.47 ? 175 ARG A O   1 
ATOM   1452 C CB  . ARG A 1 175 ? 21.977 8.019  15.949  1.00 10.91 ? 175 ARG A CB  1 
ATOM   1453 C CG  . ARG A 1 175 ? 23.138 7.103  15.514  1.00 11.26 ? 175 ARG A CG  1 
ATOM   1454 C CD  . ARG A 1 175 ? 23.552 6.209  16.713  1.00 13.33 ? 175 ARG A CD  1 
ATOM   1455 N NE  . ARG A 1 175 ? 22.516 5.206  16.962  1.00 13.43 ? 175 ARG A NE  1 
ATOM   1456 C CZ  . ARG A 1 175 ? 22.513 4.340  17.977  1.00 16.93 ? 175 ARG A CZ  1 
ATOM   1457 N NH1 . ARG A 1 175 ? 23.492 4.337  18.880  1.00 16.79 ? 175 ARG A NH1 1 
ATOM   1458 N NH2 . ARG A 1 175 ? 21.520 3.458  18.084  1.00 17.89 ? 175 ARG A NH2 1 
ATOM   1459 N N   . ASN A 1 176 ? 19.640 6.796  14.451  1.00 10.41 ? 176 ASN A N   1 
ATOM   1460 C CA  . ASN A 1 176 ? 19.060 5.651  13.749  1.00 10.50 ? 176 ASN A CA  1 
ATOM   1461 C C   . ASN A 1 176 ? 18.374 6.046  12.449  1.00 10.49 ? 176 ASN A C   1 
ATOM   1462 O O   . ASN A 1 176 ? 18.544 5.392  11.416  1.00 11.45 ? 176 ASN A O   1 
ATOM   1463 C CB  . ASN A 1 176 ? 18.069 4.923  14.654  1.00 10.93 ? 176 ASN A CB  1 
ATOM   1464 C CG  . ASN A 1 176 ? 18.755 4.156  15.762  1.00 12.05 ? 176 ASN A CG  1 
ATOM   1465 O OD1 . ASN A 1 176 ? 19.992 4.125  15.836  1.00 12.76 ? 176 ASN A OD1 1 
ATOM   1466 N ND2 . ASN A 1 176 ? 17.960 3.535  16.637  1.00 14.83 ? 176 ASN A ND2 1 
ATOM   1467 N N   . VAL A 1 177 ? 17.632 7.147  12.491  1.00 10.35 ? 177 VAL A N   1 
ATOM   1468 C CA  . VAL A 1 177 ? 16.996 7.696  11.292  1.00 11.10 ? 177 VAL A CA  1 
ATOM   1469 C C   . VAL A 1 177 ? 18.067 8.056  10.265  1.00 11.31 ? 177 VAL A C   1 
ATOM   1470 O O   . VAL A 1 177 ? 17.940 7.748  9.079   1.00 12.01 ? 177 VAL A O   1 
ATOM   1471 C CB  . VAL A 1 177 ? 16.170 8.951  11.676  1.00 11.24 ? 177 VAL A CB  1 
ATOM   1472 C CG1 . VAL A 1 177 ? 15.800 9.806  10.452  1.00 13.04 ? 177 VAL A CG1 1 
ATOM   1473 C CG2 . VAL A 1 177 ? 14.922 8.527  12.470  1.00 11.80 ? 177 VAL A CG2 1 
ATOM   1474 N N   . THR A 1 178 ? 19.135 8.704  10.728  1.00 11.59 ? 178 THR A N   1 
ATOM   1475 C CA  . THR A 1 178 ? 20.248 9.092  9.857   1.00 11.95 ? 178 THR A CA  1 
ATOM   1476 C C   . THR A 1 178 ? 20.939 7.879  9.210   1.00 11.76 ? 178 THR A C   1 
ATOM   1477 O O   . THR A 1 178 ? 21.121 7.839  7.992   1.00 12.04 ? 178 THR A O   1 
ATOM   1478 C CB  . THR A 1 178 ? 21.248 9.966  10.649  1.00 12.42 ? 178 THR A CB  1 
ATOM   1479 O OG1 . THR A 1 178 ? 20.573 11.161 11.060  1.00 11.93 ? 178 THR A OG1 1 
ATOM   1480 C CG2 . THR A 1 178 ? 22.490 10.340 9.812   1.00 12.24 ? 178 THR A CG2 1 
ATOM   1481 N N   . VAL A 1 179 ? 21.258 6.858  10.000  1.00 11.38 ? 179 VAL A N   1 
ATOM   1482 C CA  . VAL A 1 179 ? 21.929 5.678  9.429   1.00 10.69 ? 179 VAL A CA  1 
ATOM   1483 C C   . VAL A 1 179 ? 21.047 4.990  8.388   1.00 10.76 ? 179 VAL A C   1 
ATOM   1484 O O   . VAL A 1 179 ? 21.513 4.659  7.291   1.00 11.01 ? 179 VAL A O   1 
ATOM   1485 C CB  . VAL A 1 179 ? 22.316 4.674  10.535  1.00 10.71 ? 179 VAL A CB  1 
ATOM   1486 C CG1 . VAL A 1 179 ? 22.726 3.327  9.924   1.00 11.52 ? 179 VAL A CG1 1 
ATOM   1487 C CG2 . VAL A 1 179 ? 23.447 5.277  11.372  1.00 10.83 ? 179 VAL A CG2 1 
ATOM   1488 N N   . VAL A 1 180 ? 19.763 4.831  8.706   1.00 11.08 ? 180 VAL A N   1 
ATOM   1489 C CA  . VAL A 1 180 ? 18.870 4.119  7.775   1.00 10.98 ? 180 VAL A CA  1 
ATOM   1490 C C   . VAL A 1 180 ? 18.689 4.927  6.480   1.00 10.76 ? 180 VAL A C   1 
ATOM   1491 O O   . VAL A 1 180 ? 18.792 4.380  5.374   1.00 12.02 ? 180 VAL A O   1 
ATOM   1492 C CB  . VAL A 1 180 ? 17.510 3.805  8.399   1.00 11.41 ? 180 VAL A CB  1 
ATOM   1493 C CG1 . VAL A 1 180 ? 16.531 3.290  7.320   1.00 13.07 ? 180 VAL A CG1 1 
ATOM   1494 C CG2 . VAL A 1 180 ? 17.648 2.788  9.536   1.00 11.14 ? 180 VAL A CG2 1 
ATOM   1495 N N   . LEU A 1 181 ? 18.436 6.227  6.601   1.00 9.89  ? 181 LEU A N   1 
ATOM   1496 C CA  . LEU A 1 181 ? 18.153 7.012  5.397   1.00 9.80  ? 181 LEU A CA  1 
ATOM   1497 C C   . LEU A 1 181 ? 19.404 7.256  4.559   1.00 10.36 ? 181 LEU A C   1 
ATOM   1498 O O   . LEU A 1 181 ? 19.385 7.077  3.328   1.00 10.35 ? 181 LEU A O   1 
ATOM   1499 C CB  . LEU A 1 181 ? 17.494 8.343  5.785   1.00 10.33 ? 181 LEU A CB  1 
ATOM   1500 C CG  . LEU A 1 181 ? 16.120 8.194  6.443   1.00 10.66 ? 181 LEU A CG  1 
ATOM   1501 C CD1 . LEU A 1 181 ? 15.646 9.548  6.943   1.00 13.27 ? 181 LEU A CD1 1 
ATOM   1502 C CD2 . LEU A 1 181 ? 15.111 7.624  5.448   1.00 12.80 ? 181 LEU A CD2 1 
ATOM   1503 N N   . TRP A 1 182 ? 20.497 7.647  5.215   1.00 10.69 ? 182 TRP A N   1 
ATOM   1504 C CA  . TRP A 1 182 ? 21.727 7.982  4.472   1.00 10.59 ? 182 TRP A CA  1 
ATOM   1505 C C   . TRP A 1 182 ? 22.256 6.748  3.733   1.00 10.79 ? 182 TRP A C   1 
ATOM   1506 O O   . TRP A 1 182 ? 22.699 6.863  2.577   1.00 11.62 ? 182 TRP A O   1 
ATOM   1507 C CB  . TRP A 1 182 ? 22.811 8.544  5.396   1.00 11.44 ? 182 TRP A CB  1 
ATOM   1508 C CG  . TRP A 1 182 ? 22.568 9.946  5.898   1.00 10.49 ? 182 TRP A CG  1 
ATOM   1509 C CD1 . TRP A 1 182 ? 21.382 10.494 6.311   1.00 11.58 ? 182 TRP A CD1 1 
ATOM   1510 C CD2 . TRP A 1 182 ? 23.575 10.950 6.115   1.00 10.12 ? 182 TRP A CD2 1 
ATOM   1511 N NE1 . TRP A 1 182 ? 21.584 11.799 6.740   1.00 10.91 ? 182 TRP A NE1 1 
ATOM   1512 C CE2 . TRP A 1 182 ? 22.921 12.098 6.637   1.00 11.81 ? 182 TRP A CE2 1 
ATOM   1513 C CE3 . TRP A 1 182 ? 24.963 10.997 5.899   1.00 12.60 ? 182 TRP A CE3 1 
ATOM   1514 C CZ2 . TRP A 1 182 ? 23.619 13.276 6.961   1.00 11.94 ? 182 TRP A CZ2 1 
ATOM   1515 C CZ3 . TRP A 1 182 ? 25.661 12.189 6.219   1.00 12.30 ? 182 TRP A CZ3 1 
ATOM   1516 C CH2 . TRP A 1 182 ? 24.972 13.305 6.736   1.00 11.81 ? 182 TRP A CH2 1 
ATOM   1517 N N   . SER A 1 183 ? 22.159 5.573  4.364   1.00 10.67 ? 183 SER A N   1 
ATOM   1518 C CA  . SER A 1 183 ? 22.755 4.361  3.764   1.00 11.64 ? 183 SER A CA  1 
ATOM   1519 C C   . SER A 1 183 ? 22.051 3.988  2.446   1.00 11.61 ? 183 SER A C   1 
ATOM   1520 O O   . SER A 1 183 ? 22.604 3.222  1.643   1.00 11.95 ? 183 SER A O   1 
ATOM   1521 C CB  . SER A 1 183 ? 22.719 3.185  4.748   1.00 12.52 ? 183 SER A CB  1 
ATOM   1522 O OG  . SER A 1 183 ? 21.399 2.732  4.939   1.00 14.91 ? 183 SER A OG  1 
ATOM   1523 N N   . ALA A 1 184 ? 20.843 4.517  2.238   1.00 10.52 ? 184 ALA A N   1 
ATOM   1524 C CA  . ALA A 1 184 ? 20.077 4.208  1.007   1.00 11.20 ? 184 ALA A CA  1 
ATOM   1525 C C   . ALA A 1 184 ? 20.539 5.021  -0.194  1.00 11.18 ? 184 ALA A C   1 
ATOM   1526 O O   . ALA A 1 184 ? 20.388 4.581  -1.344  1.00 10.86 ? 184 ALA A O   1 
ATOM   1527 C CB  . ALA A 1 184 ? 18.589 4.406  1.234   1.00 11.22 ? 184 ALA A CB  1 
ATOM   1528 N N   . TYR A 1 185 ? 21.077 6.214  0.063   1.00 10.48 ? 185 TYR A N   1 
ATOM   1529 C CA  . TYR A 1 185 ? 21.451 7.112  -1.041  1.00 10.36 ? 185 TYR A CA  1 
ATOM   1530 C C   . TYR A 1 185 ? 22.452 6.485  -2.019  1.00 10.80 ? 185 TYR A C   1 
ATOM   1531 O O   . TYR A 1 185 ? 22.247 6.560  -3.228  1.00 10.62 ? 185 TYR A O   1 
ATOM   1532 C CB  . TYR A 1 185 ? 21.989 8.453  -0.524  1.00 11.10 ? 185 TYR A CB  1 
ATOM   1533 C CG  . TYR A 1 185 ? 20.926 9.393  -0.013  1.00 10.22 ? 185 TYR A CG  1 
ATOM   1534 C CD1 . TYR A 1 185 ? 20.383 9.230  1.262   1.00 11.46 ? 185 TYR A CD1 1 
ATOM   1535 C CD2 . TYR A 1 185 ? 20.486 10.466 -0.789  1.00 11.43 ? 185 TYR A CD2 1 
ATOM   1536 C CE1 . TYR A 1 185 ? 19.424 10.104 1.749   1.00 11.16 ? 185 TYR A CE1 1 
ATOM   1537 C CE2 . TYR A 1 185 ? 19.521 11.354 -0.308  1.00 12.00 ? 185 TYR A CE2 1 
ATOM   1538 C CZ  . TYR A 1 185 ? 18.993 11.162 0.962   1.00 10.89 ? 185 TYR A CZ  1 
ATOM   1539 O OH  . TYR A 1 185 ? 18.025 12.029 1.460   1.00 12.21 ? 185 TYR A OH  1 
ATOM   1540 N N   . PRO A 1 186 ? 23.545 5.881  -1.525  1.00 10.41 ? 186 PRO A N   1 
ATOM   1541 C CA  . PRO A 1 186 ? 24.476 5.285  -2.504  1.00 10.81 ? 186 PRO A CA  1 
ATOM   1542 C C   . PRO A 1 186 ? 23.840 4.193  -3.355  1.00 10.98 ? 186 PRO A C   1 
ATOM   1543 O O   . PRO A 1 186 ? 24.234 4.024  -4.516  1.00 11.36 ? 186 PRO A O   1 
ATOM   1544 C CB  . PRO A 1 186 ? 25.613 4.690  -1.642  1.00 10.70 ? 186 PRO A CB  1 
ATOM   1545 C CG  . PRO A 1 186 ? 25.137 4.768  -0.215  1.00 10.59 ? 186 PRO A CG  1 
ATOM   1546 C CD  . PRO A 1 186 ? 24.056 5.826  -0.144  1.00 11.23 ? 186 PRO A CD  1 
ATOM   1547 N N   . VAL A 1 187 ? 22.871 3.465  -2.796  1.00 10.74 ? 187 VAL A N   1 
ATOM   1548 C CA  . VAL A 1 187 ? 22.173 2.399  -3.553  1.00 11.13 ? 187 VAL A CA  1 
ATOM   1549 C C   . VAL A 1 187 ? 21.269 3.019  -4.625  1.00 11.23 ? 187 VAL A C   1 
ATOM   1550 O O   . VAL A 1 187 ? 21.276 2.583  -5.788  1.00 11.77 ? 187 VAL A O   1 
ATOM   1551 C CB  . VAL A 1 187 ? 21.383 1.467  -2.613  1.00 11.83 ? 187 VAL A CB  1 
ATOM   1552 C CG1 . VAL A 1 187 ? 20.601 0.412  -3.422  1.00 13.14 ? 187 VAL A CG1 1 
ATOM   1553 C CG2 . VAL A 1 187 ? 22.354 0.790  -1.673  1.00 12.61 ? 187 VAL A CG2 1 
ATOM   1554 N N   . VAL A 1 188 ? 20.543 4.079  -4.287  1.00 11.18 ? 188 VAL A N   1 
ATOM   1555 C CA  . VAL A 1 188 ? 19.701 4.747  -5.296  1.00 10.84 ? 188 VAL A CA  1 
ATOM   1556 C C   . VAL A 1 188 ? 20.585 5.261  -6.449  1.00 11.24 ? 188 VAL A C   1 
ATOM   1557 O O   . VAL A 1 188 ? 20.265 5.073  -7.618  1.00 11.99 ? 188 VAL A O   1 
ATOM   1558 C CB  . VAL A 1 188 ? 18.859 5.877  -4.652  1.00 11.80 ? 188 VAL A CB  1 
ATOM   1559 C CG1 . VAL A 1 188 ? 18.048 6.624  -5.697  1.00 12.04 ? 188 VAL A CG1 1 
ATOM   1560 C CG2 . VAL A 1 188 ? 17.945 5.270  -3.582  1.00 11.80 ? 188 VAL A CG2 1 
ATOM   1561 N N   . TRP A 1 189 ? 21.720 5.862  -6.112  1.00 11.42 ? 189 TRP A N   1 
ATOM   1562 C CA  . TRP A 1 189 ? 22.635 6.395  -7.135  1.00 11.69 ? 189 TRP A CA  1 
ATOM   1563 C C   . TRP A 1 189 ? 23.165 5.253  -8.010  1.00 11.65 ? 189 TRP A C   1 
ATOM   1564 O O   . TRP A 1 189 ? 23.159 5.342  -9.245  1.00 11.69 ? 189 TRP A O   1 
ATOM   1565 C CB  . TRP A 1 189 ? 23.777 7.083  -6.419  1.00 12.32 ? 189 TRP A CB  1 
ATOM   1566 C CG  . TRP A 1 189 ? 24.659 8.016  -7.205  1.00 12.92 ? 189 TRP A CG  1 
ATOM   1567 C CD1 . TRP A 1 189 ? 24.663 9.380  -7.131  1.00 14.22 ? 189 TRP A CD1 1 
ATOM   1568 C CD2 . TRP A 1 189 ? 25.719 7.658  -8.114  1.00 12.23 ? 189 TRP A CD2 1 
ATOM   1569 N NE1 . TRP A 1 189 ? 25.645 9.898  -7.945  1.00 14.10 ? 189 TRP A NE1 1 
ATOM   1570 C CE2 . TRP A 1 189 ? 26.312 8.864  -8.555  1.00 13.83 ? 189 TRP A CE2 1 
ATOM   1571 C CE3 . TRP A 1 189 ? 26.217 6.442  -8.603  1.00 14.05 ? 189 TRP A CE3 1 
ATOM   1572 C CZ2 . TRP A 1 189 ? 27.395 8.886  -9.443  1.00 13.34 ? 189 TRP A CZ2 1 
ATOM   1573 C CZ3 . TRP A 1 189 ? 27.291 6.466  -9.497  1.00 13.37 ? 189 TRP A CZ3 1 
ATOM   1574 C CH2 . TRP A 1 189 ? 27.855 7.680  -9.918  1.00 13.61 ? 189 TRP A CH2 1 
ATOM   1575 N N   . LEU A 1 190 ? 23.581 4.158  -7.364  1.00 10.86 ? 190 LEU A N   1 
ATOM   1576 C CA  . LEU A 1 190 ? 24.156 3.010  -8.070  1.00 11.78 ? 190 LEU A CA  1 
ATOM   1577 C C   . LEU A 1 190 ? 23.194 2.426  -9.097  1.00 11.41 ? 190 LEU A C   1 
ATOM   1578 O O   . LEU A 1 190 ? 23.611 2.062  -10.204 1.00 11.71 ? 190 LEU A O   1 
ATOM   1579 C CB  . LEU A 1 190 ? 24.540 1.923  -7.056  1.00 11.96 ? 190 LEU A CB  1 
ATOM   1580 C CG  . LEU A 1 190 ? 25.257 0.672  -7.572  1.00 13.39 ? 190 LEU A CG  1 
ATOM   1581 C CD1 . LEU A 1 190 ? 26.662 1.050  -8.032  1.00 16.09 ? 190 LEU A CD1 1 
ATOM   1582 C CD2 . LEU A 1 190 ? 25.336 -0.402 -6.480  1.00 13.87 ? 190 LEU A CD2 1 
ATOM   1583 N N   . ILE A 1 191 ? 21.918 2.319  -8.733  1.00 10.98 ? 191 ILE A N   1 
ATOM   1584 C CA  . ILE A 1 191 ? 20.937 1.630  -9.598  1.00 11.74 ? 191 ILE A CA  1 
ATOM   1585 C C   . ILE A 1 191 ? 20.167 2.583  -10.511 1.00 12.22 ? 191 ILE A C   1 
ATOM   1586 O O   . ILE A 1 191 ? 19.458 2.136  -11.413 1.00 12.03 ? 191 ILE A O   1 
ATOM   1587 C CB  . ILE A 1 191 ? 19.921 0.774  -8.779  1.00 12.00 ? 191 ILE A CB  1 
ATOM   1588 C CG1 . ILE A 1 191 ? 19.008 1.671  -7.923  1.00 12.03 ? 191 ILE A CG1 1 
ATOM   1589 C CG2 . ILE A 1 191 ? 20.660 -0.238 -7.927  1.00 12.67 ? 191 ILE A CG2 1 
ATOM   1590 C CD1 . ILE A 1 191 ? 17.980 0.892  -7.049  1.00 11.90 ? 191 ILE A CD1 1 
ATOM   1591 N N   . GLY A 1 192 ? 20.297 3.883  -10.251 1.00 12.31 ? 192 GLY A N   1 
ATOM   1592 C CA  . GLY A 1 192 ? 19.473 4.891  -10.926 1.00 12.50 ? 192 GLY A CA  1 
ATOM   1593 C C   . GLY A 1 192 ? 20.165 5.583  -12.083 1.00 13.54 ? 192 GLY A C   1 
ATOM   1594 O O   . GLY A 1 192 ? 21.101 5.046  -12.666 1.00 12.82 ? 192 GLY A O   1 
ATOM   1595 N N   . SER A 1 193 ? 19.711 6.808  -12.367 1.00 13.52 ? 193 SER A N   1 
ATOM   1596 C CA  A SER A 1 193 ? 20.142 7.580  -13.543 0.60 14.29 ? 193 SER A CA  1 
ATOM   1597 C CA  B SER A 1 193 ? 20.147 7.568  -13.547 0.40 14.43 ? 193 SER A CA  1 
ATOM   1598 C C   . SER A 1 193 ? 21.648 7.840  -13.620 1.00 14.21 ? 193 SER A C   1 
ATOM   1599 O O   . SER A 1 193 ? 22.218 7.986  -14.731 1.00 15.07 ? 193 SER A O   1 
ATOM   1600 C CB  A SER A 1 193 ? 19.405 8.926  -13.564 0.60 14.35 ? 193 SER A CB  1 
ATOM   1601 C CB  B SER A 1 193 ? 19.398 8.899  -13.598 0.40 14.53 ? 193 SER A CB  1 
ATOM   1602 O OG  A SER A 1 193 ? 19.828 9.758  -12.499 0.60 15.16 ? 193 SER A OG  1 
ATOM   1603 O OG  B SER A 1 193 ? 18.005 8.671  -13.568 0.40 16.38 ? 193 SER A OG  1 
ATOM   1604 N N   . GLU A 1 194 ? 22.276 7.947  -12.453 1.00 14.00 ? 194 GLU A N   1 
ATOM   1605 C CA  . GLU A 1 194 ? 23.680 8.303  -12.353 1.00 14.42 ? 194 GLU A CA  1 
ATOM   1606 C C   . GLU A 1 194 ? 24.589 7.102  -12.508 1.00 13.94 ? 194 GLU A C   1 
ATOM   1607 O O   . GLU A 1 194 ? 25.764 7.251  -12.826 1.00 14.11 ? 194 GLU A O   1 
ATOM   1608 C CB  . GLU A 1 194 ? 23.964 8.979  -11.006 1.00 14.59 ? 194 GLU A CB  1 
ATOM   1609 C CG  . GLU A 1 194 ? 23.145 10.244 -10.730 1.00 17.43 ? 194 GLU A CG  1 
ATOM   1610 C CD  . GLU A 1 194 ? 21.812 9.960  -10.017 1.00 19.42 ? 194 GLU A CD  1 
ATOM   1611 O OE1 . GLU A 1 194 ? 21.370 8.787  -9.972  1.00 20.75 ? 194 GLU A OE1 1 
ATOM   1612 O OE2 . GLU A 1 194 ? 21.196 10.916 -9.499  1.00 22.14 ? 194 GLU A OE2 1 
ATOM   1613 N N   . GLY A 1 195 ? 24.044 5.913  -12.241 1.00 13.49 ? 195 GLY A N   1 
ATOM   1614 C CA  . GLY A 1 195 ? 24.836 4.694  -12.227 1.00 13.46 ? 195 GLY A CA  1 
ATOM   1615 C C   . GLY A 1 195 ? 24.416 3.739  -13.316 1.00 12.75 ? 195 GLY A C   1 
ATOM   1616 O O   . GLY A 1 195 ? 24.643 4.005  -14.502 1.00 13.51 ? 195 GLY A O   1 
ATOM   1617 N N   . ALA A 1 196 ? 23.800 2.628  -12.912 1.00 12.39 ? 196 ALA A N   1 
ATOM   1618 C CA  . ALA A 1 196 ? 23.472 1.535  -13.833 1.00 12.25 ? 196 ALA A CA  1 
ATOM   1619 C C   . ALA A 1 196 ? 22.291 1.825  -14.774 1.00 12.47 ? 196 ALA A C   1 
ATOM   1620 O O   . ALA A 1 196 ? 22.112 1.114  -15.786 1.00 13.07 ? 196 ALA A O   1 
ATOM   1621 C CB  . ALA A 1 196 ? 23.214 0.248  -13.045 1.00 12.31 ? 196 ALA A CB  1 
ATOM   1622 N N   . GLY A 1 197 ? 21.490 2.840  -14.439 1.00 12.27 ? 197 GLY A N   1 
ATOM   1623 C CA  . GLY A 1 197 ? 20.369 3.277  -15.290 1.00 13.15 ? 197 GLY A CA  1 
ATOM   1624 C C   . GLY A 1 197 ? 19.218 2.294  -15.342 1.00 12.85 ? 197 GLY A C   1 
ATOM   1625 O O   . GLY A 1 197 ? 18.474 2.237  -16.333 1.00 14.40 ? 197 GLY A O   1 
ATOM   1626 N N   . ILE A 1 198 ? 19.080 1.513  -14.274 1.00 12.86 ? 198 ILE A N   1 
ATOM   1627 C CA  . ILE A 1 198 ? 18.028 0.520  -14.174 1.00 12.95 ? 198 ILE A CA  1 
ATOM   1628 C C   . ILE A 1 198 ? 16.739 1.176  -13.714 1.00 13.59 ? 198 ILE A C   1 
ATOM   1629 O O   . ILE A 1 198 ? 15.695 0.976  -14.314 1.00 14.43 ? 198 ILE A O   1 
ATOM   1630 C CB  . ILE A 1 198 ? 18.410 -0.583 -13.178 1.00 12.88 ? 198 ILE A CB  1 
ATOM   1631 C CG1 . ILE A 1 198 ? 19.689 -1.293 -13.646 1.00 12.52 ? 198 ILE A CG1 1 
ATOM   1632 C CG2 . ILE A 1 198 ? 17.259 -1.570 -12.992 1.00 12.13 ? 198 ILE A CG2 1 
ATOM   1633 C CD1 . ILE A 1 198 ? 20.314 -2.235 -12.599 1.00 13.29 ? 198 ILE A CD1 1 
ATOM   1634 N N   . VAL A 1 199 ? 16.816 1.959  -12.639 1.00 13.76 ? 199 VAL A N   1 
ATOM   1635 C CA  . VAL A 1 199 ? 15.646 2.677  -12.137 1.00 13.93 ? 199 VAL A CA  1 
ATOM   1636 C C   . VAL A 1 199 ? 15.540 3.987  -12.906 1.00 14.43 ? 199 VAL A C   1 
ATOM   1637 O O   . VAL A 1 199 ? 16.508 4.748  -12.964 1.00 13.67 ? 199 VAL A O   1 
ATOM   1638 C CB  . VAL A 1 199 ? 15.762 2.931  -10.617 1.00 14.31 ? 199 VAL A CB  1 
ATOM   1639 C CG1 . VAL A 1 199 ? 14.567 3.755  -10.100 1.00 14.82 ? 199 VAL A CG1 1 
ATOM   1640 C CG2 . VAL A 1 199 ? 15.855 1.594  -9.877  1.00 14.11 ? 199 VAL A CG2 1 
ATOM   1641 N N   . PRO A 1 200 ? 14.379 4.227  -13.543 1.00 15.11 ? 200 PRO A N   1 
ATOM   1642 C CA  . PRO A 1 200 ? 14.201 5.448  -14.334 1.00 15.37 ? 200 PRO A CA  1 
ATOM   1643 C C   . PRO A 1 200 ? 14.197 6.702  -13.478 1.00 15.91 ? 200 PRO A C   1 
ATOM   1644 O O   . PRO A 1 200 ? 13.913 6.644  -12.272 1.00 16.13 ? 200 PRO A O   1 
ATOM   1645 C CB  . PRO A 1 200 ? 12.836 5.251  -15.013 1.00 16.26 ? 200 PRO A CB  1 
ATOM   1646 C CG  . PRO A 1 200 ? 12.157 4.224  -14.225 1.00 16.56 ? 200 PRO A CG  1 
ATOM   1647 C CD  . PRO A 1 200 ? 13.185 3.359  -13.581 1.00 15.09 ? 200 PRO A CD  1 
ATOM   1648 N N   . LEU A 1 201 ? 14.512 7.815  -14.125 1.00 15.92 ? 201 LEU A N   1 
ATOM   1649 C CA  . LEU A 1 201 ? 14.683 9.091  -13.431 1.00 16.14 ? 201 LEU A CA  1 
ATOM   1650 C C   . LEU A 1 201 ? 13.433 9.521  -12.657 1.00 16.39 ? 201 LEU A C   1 
ATOM   1651 O O   . LEU A 1 201 ? 13.550 10.103 -11.573 1.00 15.20 ? 201 LEU A O   1 
ATOM   1652 C CB  . LEU A 1 201 ? 15.134 10.165 -14.425 1.00 16.68 ? 201 LEU A CB  1 
ATOM   1653 C CG  . LEU A 1 201 ? 15.468 11.556 -13.888 1.00 16.42 ? 201 LEU A CG  1 
ATOM   1654 C CD1 . LEU A 1 201 ? 16.525 11.498 -12.784 1.00 16.67 ? 201 LEU A CD1 1 
ATOM   1655 C CD2 . LEU A 1 201 ? 15.903 12.458 -15.051 1.00 16.79 ? 201 LEU A CD2 1 
ATOM   1656 N N   . ASN A 1 202 ? 12.239 9.226  -13.173 1.00 16.46 ? 202 ASN A N   1 
ATOM   1657 C CA  . ASN A 1 202 ? 11.031 9.617  -12.448 1.00 16.68 ? 202 ASN A CA  1 
ATOM   1658 C C   . ASN A 1 202 ? 10.914 8.906  -11.103 1.00 16.12 ? 202 ASN A C   1 
ATOM   1659 O O   . ASN A 1 202 ? 10.623 9.544  -10.086 1.00 16.31 ? 202 ASN A O   1 
ATOM   1660 C CB  . ASN A 1 202 ? 9.754  9.506  -13.301 1.00 17.77 ? 202 ASN A CB  1 
ATOM   1661 C CG  . ASN A 1 202 ? 9.397  8.072  -13.673 1.00 20.32 ? 202 ASN A CG  1 
ATOM   1662 O OD1 . ASN A 1 202 ? 10.263 7.222  -13.862 1.00 22.68 ? 202 ASN A OD1 1 
ATOM   1663 N ND2 . ASN A 1 202 ? 8.094  7.808  -13.800 1.00 25.20 ? 202 ASN A ND2 1 
ATOM   1664 N N   . ILE A 1 203 ? 11.196 7.598  -11.087 1.00 15.39 ? 203 ILE A N   1 
ATOM   1665 C CA  A ILE A 1 203 ? 11.138 6.819  -9.853  0.60 15.17 ? 203 ILE A CA  1 
ATOM   1666 C CA  B ILE A 1 203 ? 11.134 6.820  -9.851  0.40 15.14 ? 203 ILE A CA  1 
ATOM   1667 C C   . ILE A 1 203 ? 12.300 7.193  -8.927  1.00 14.93 ? 203 ILE A C   1 
ATOM   1668 O O   . ILE A 1 203 ? 12.134 7.307  -7.708  1.00 14.71 ? 203 ILE A O   1 
ATOM   1669 C CB  A ILE A 1 203 ? 11.122 5.288  -10.136 0.60 15.30 ? 203 ILE A CB  1 
ATOM   1670 C CB  B ILE A 1 203 ? 11.117 5.291  -10.120 0.40 15.24 ? 203 ILE A CB  1 
ATOM   1671 C CG1 A ILE A 1 203 ? 9.867  4.904  -10.940 0.60 15.67 ? 203 ILE A CG1 1 
ATOM   1672 C CG1 B ILE A 1 203 ? 10.004 4.929  -11.116 0.40 15.31 ? 203 ILE A CG1 1 
ATOM   1673 C CG2 A ILE A 1 203 ? 11.242 4.490  -8.830  0.60 15.77 ? 203 ILE A CG2 1 
ATOM   1674 C CG2 B ILE A 1 203 ? 10.976 4.516  -8.803  0.40 15.66 ? 203 ILE A CG2 1 
ATOM   1675 C CD1 A ILE A 1 203 ? 8.561  5.354  -10.303 0.60 14.87 ? 203 ILE A CD1 1 
ATOM   1676 C CD1 B ILE A 1 203 ? 9.940  3.459  -11.460 0.40 15.10 ? 203 ILE A CD1 1 
ATOM   1677 N N   . GLU A 1 204 ? 13.482 7.393  -9.501  1.00 14.52 ? 204 GLU A N   1 
ATOM   1678 C CA  . GLU A 1 204 ? 14.620 7.837  -8.701  1.00 14.13 ? 204 GLU A CA  1 
ATOM   1679 C C   . GLU A 1 204 ? 14.316 9.147  -7.975  1.00 13.62 ? 204 GLU A C   1 
ATOM   1680 O O   . GLU A 1 204 ? 14.649 9.327  -6.801  1.00 13.23 ? 204 GLU A O   1 
ATOM   1681 C CB  . GLU A 1 204 ? 15.827 8.037  -9.582  1.00 14.66 ? 204 GLU A CB  1 
ATOM   1682 C CG  . GLU A 1 204 ? 17.003 8.563  -8.819  1.00 17.09 ? 204 GLU A CG  1 
ATOM   1683 C CD  . GLU A 1 204 ? 18.254 8.443  -9.597  1.00 18.60 ? 204 GLU A CD  1 
ATOM   1684 O OE1 . GLU A 1 204 ? 18.190 8.615  -10.831 1.00 21.67 ? 204 GLU A OE1 1 
ATOM   1685 O OE2 . GLU A 1 204 ? 19.286 8.150  -8.969  1.00 22.04 ? 204 GLU A OE2 1 
ATOM   1686 N N   . THR A 1 205 ? 13.687 10.071 -8.692  1.00 13.14 ? 205 THR A N   1 
ATOM   1687 C CA  . THR A 1 205 ? 13.342 11.372 -8.100  1.00 12.44 ? 205 THR A CA  1 
ATOM   1688 C C   . THR A 1 205 ? 12.332 11.194 -6.944  1.00 12.88 ? 205 THR A C   1 
ATOM   1689 O O   . THR A 1 205 ? 12.443 11.872 -5.917  1.00 12.23 ? 205 THR A O   1 
ATOM   1690 C CB  . THR A 1 205 ? 12.835 12.347 -9.183  1.00 12.93 ? 205 THR A CB  1 
ATOM   1691 O OG1 . THR A 1 205 ? 13.846 12.466 -10.200 1.00 12.83 ? 205 THR A OG1 1 
ATOM   1692 C CG2 . THR A 1 205 ? 12.558 13.723 -8.583  1.00 13.37 ? 205 THR A CG2 1 
ATOM   1693 N N   . LEU A 1 206 ? 11.362 10.293 -7.110  1.00 12.83 ? 206 LEU A N   1 
ATOM   1694 C CA  . LEU A 1 206 ? 10.454 9.915  -6.021  1.00 13.47 ? 206 LEU A CA  1 
ATOM   1695 C C   . LEU A 1 206 ? 11.240 9.387  -4.814  1.00 12.83 ? 206 LEU A C   1 
ATOM   1696 O O   . LEU A 1 206 ? 10.999 9.796  -3.670  1.00 12.86 ? 206 LEU A O   1 
ATOM   1697 C CB  . LEU A 1 206 ? 9.473  8.846  -6.504  1.00 13.63 ? 206 LEU A CB  1 
ATOM   1698 C CG  . LEU A 1 206 ? 8.620  8.113  -5.467  1.00 13.95 ? 206 LEU A CG  1 
ATOM   1699 C CD1 . LEU A 1 206 ? 7.753  9.078  -4.659  1.00 15.22 ? 206 LEU A CD1 1 
ATOM   1700 C CD2 . LEU A 1 206 ? 7.767  7.032  -6.147  1.00 15.18 ? 206 LEU A CD2 1 
ATOM   1701 N N   . LEU A 1 207 ? 12.171 8.471  -5.061  1.00 12.69 ? 207 LEU A N   1 
ATOM   1702 C CA  . LEU A 1 207 ? 12.952 7.893  -3.969  1.00 11.84 ? 207 LEU A CA  1 
ATOM   1703 C C   . LEU A 1 207 ? 13.779 8.945  -3.242  1.00 11.77 ? 207 LEU A C   1 
ATOM   1704 O O   . LEU A 1 207 ? 13.741 9.011  -1.997  1.00 12.07 ? 207 LEU A O   1 
ATOM   1705 C CB  . LEU A 1 207 ? 13.862 6.764  -4.461  1.00 12.13 ? 207 LEU A CB  1 
ATOM   1706 C CG  . LEU A 1 207 ? 13.135 5.553  -5.067  1.00 11.86 ? 207 LEU A CG  1 
ATOM   1707 C CD1 . LEU A 1 207 ? 14.139 4.573  -5.690  1.00 13.98 ? 207 LEU A CD1 1 
ATOM   1708 C CD2 . LEU A 1 207 ? 12.265 4.844  -4.025  1.00 15.60 ? 207 LEU A CD2 1 
ATOM   1709 N N   . PHE A 1 208 ? 14.511 9.781  -3.989  1.00 11.30 ? 208 PHE A N   1 
ATOM   1710 C CA  . PHE A 1 208 ? 15.276 10.850 -3.319  1.00 12.04 ? 208 PHE A CA  1 
ATOM   1711 C C   . PHE A 1 208 ? 14.361 11.831 -2.568  1.00 12.41 ? 208 PHE A C   1 
ATOM   1712 O O   . PHE A 1 208 ? 14.757 12.365 -1.538  1.00 12.40 ? 208 PHE A O   1 
ATOM   1713 C CB  . PHE A 1 208 ? 16.160 11.647 -4.285  1.00 12.18 ? 208 PHE A CB  1 
ATOM   1714 C CG  . PHE A 1 208 ? 17.450 10.961 -4.676  1.00 11.93 ? 208 PHE A CG  1 
ATOM   1715 C CD1 . PHE A 1 208 ? 18.248 10.331 -3.730  1.00 12.20 ? 208 PHE A CD1 1 
ATOM   1716 C CD2 . PHE A 1 208 ? 17.884 10.991 -6.002  1.00 12.19 ? 208 PHE A CD2 1 
ATOM   1717 C CE1 . PHE A 1 208 ? 19.452 9.720  -4.093  1.00 12.83 ? 208 PHE A CE1 1 
ATOM   1718 C CE2 . PHE A 1 208 ? 19.093 10.387 -6.371  1.00 13.98 ? 208 PHE A CE2 1 
ATOM   1719 C CZ  . PHE A 1 208 ? 19.878 9.758  -5.419  1.00 13.08 ? 208 PHE A CZ  1 
ATOM   1720 N N   . MET A 1 209 ? 13.163 12.098 -3.090  1.00 12.14 ? 209 MET A N   1 
ATOM   1721 C CA  A MET A 1 209 ? 12.240 13.006 -2.408  0.50 12.17 ? 209 MET A CA  1 
ATOM   1722 C CA  B MET A 1 209 ? 12.201 12.993 -2.410  0.50 12.57 ? 209 MET A CA  1 
ATOM   1723 C C   . MET A 1 209 ? 11.819 12.423 -1.054  1.00 12.31 ? 209 MET A C   1 
ATOM   1724 O O   . MET A 1 209 ? 11.847 13.124 -0.038  1.00 12.28 ? 209 MET A O   1 
ATOM   1725 C CB  A MET A 1 209 ? 11.040 13.334 -3.303  0.50 12.38 ? 209 MET A CB  1 
ATOM   1726 C CB  B MET A 1 209 ? 10.931 13.205 -3.246  0.50 12.42 ? 209 MET A CB  1 
ATOM   1727 C CG  A MET A 1 209 ? 10.114 14.405 -2.741  0.50 12.95 ? 209 MET A CG  1 
ATOM   1728 C CG  B MET A 1 209 ? 9.913  14.166 -2.596  0.50 12.79 ? 209 MET A CG  1 
ATOM   1729 S SD  A MET A 1 209 ? 8.860  13.669 -1.689  0.50 15.71 ? 209 MET A SD  1 
ATOM   1730 S SD  B MET A 1 209 ? 8.229  13.915 -3.192  0.50 14.73 ? 209 MET A SD  1 
ATOM   1731 C CE  A MET A 1 209 ? 7.833  12.829 -2.909  0.50 15.03 ? 209 MET A CE  1 
ATOM   1732 C CE  B MET A 1 209 ? 7.679  12.559 -2.154  0.50 15.65 ? 209 MET A CE  1 
ATOM   1733 N N   . VAL A 1 210 ? 11.463 11.139 -1.032  1.00 12.19 ? 210 VAL A N   1 
ATOM   1734 C CA  . VAL A 1 210 ? 11.079 10.496 0.224   1.00 12.62 ? 210 VAL A CA  1 
ATOM   1735 C C   . VAL A 1 210 ? 12.247 10.530 1.195   1.00 11.62 ? 210 VAL A C   1 
ATOM   1736 O O   . VAL A 1 210 ? 12.081 10.881 2.366   1.00 12.52 ? 210 VAL A O   1 
ATOM   1737 C CB  . VAL A 1 210 ? 10.608 9.039  -0.018  1.00 13.42 ? 210 VAL A CB  1 
ATOM   1738 C CG1 . VAL A 1 210 ? 10.403 8.296  1.294   1.00 15.38 ? 210 VAL A CG1 1 
ATOM   1739 C CG2 . VAL A 1 210 ? 9.304  9.049  -0.834  1.00 14.29 ? 210 VAL A CG2 1 
ATOM   1740 N N   . LEU A 1 211 ? 13.427 10.158 0.711   1.00 11.52 ? 211 LEU A N   1 
ATOM   1741 C CA  . LEU A 1 211 ? 14.623 10.133 1.577   1.00 10.99 ? 211 LEU A CA  1 
ATOM   1742 C C   . LEU A 1 211 ? 14.929 11.540 2.098   1.00 11.10 ? 211 LEU A C   1 
ATOM   1743 O O   . LEU A 1 211 ? 15.123 11.720 3.296   1.00 11.08 ? 211 LEU A O   1 
ATOM   1744 C CB  . LEU A 1 211 ? 15.834 9.580  0.820   1.00 11.12 ? 211 LEU A CB  1 
ATOM   1745 C CG  . LEU A 1 211 ? 15.756 8.090  0.492   1.00 10.84 ? 211 LEU A CG  1 
ATOM   1746 C CD1 . LEU A 1 211 ? 16.895 7.758  -0.475  1.00 12.83 ? 211 LEU A CD1 1 
ATOM   1747 C CD2 . LEU A 1 211 ? 15.871 7.234  1.757   1.00 12.73 ? 211 LEU A CD2 1 
ATOM   1748 N N   . ASP A 1 212 ? 14.947 12.520 1.196   1.00 10.92 ? 212 ASP A N   1 
ATOM   1749 C CA  . ASP A 1 212 ? 15.289 13.903 1.547   1.00 10.88 ? 212 ASP A CA  1 
ATOM   1750 C C   . ASP A 1 212 ? 14.309 14.468 2.578   1.00 10.58 ? 212 ASP A C   1 
ATOM   1751 O O   . ASP A 1 212 ? 14.718 15.065 3.573   1.00 11.80 ? 212 ASP A O   1 
ATOM   1752 C CB  . ASP A 1 212 ? 15.221 14.803 0.308   1.00 10.89 ? 212 ASP A CB  1 
ATOM   1753 C CG  . ASP A 1 212 ? 16.437 14.669 -0.628  1.00 13.28 ? 212 ASP A CG  1 
ATOM   1754 O OD1 . ASP A 1 212 ? 17.464 14.040 -0.288  1.00 13.36 ? 212 ASP A OD1 1 
ATOM   1755 O OD2 . ASP A 1 212 ? 16.365 15.263 -1.724  1.00 13.84 ? 212 ASP A OD2 1 
ATOM   1756 N N   . VAL A 1 213 ? 13.011 14.322 2.309   1.00 11.11 ? 213 VAL A N   1 
ATOM   1757 C CA  . VAL A 1 213 ? 11.986 14.869 3.219   1.00 11.26 ? 213 VAL A CA  1 
ATOM   1758 C C   . VAL A 1 213 ? 12.068 14.191 4.593   1.00 10.87 ? 213 VAL A C   1 
ATOM   1759 O O   . VAL A 1 213 ? 12.024 14.862 5.638   1.00 12.11 ? 213 VAL A O   1 
ATOM   1760 C CB  . VAL A 1 213 ? 10.572 14.773 2.600   1.00 11.23 ? 213 VAL A CB  1 
ATOM   1761 C CG1 . VAL A 1 213 ? 9.494  15.158 3.620   1.00 12.43 ? 213 VAL A CG1 1 
ATOM   1762 C CG2 . VAL A 1 213 ? 10.481 15.638 1.327   1.00 11.84 ? 213 VAL A CG2 1 
ATOM   1763 N N   . SER A 1 214 ? 12.223 12.872 4.599   1.00 10.68 ? 214 SER A N   1 
ATOM   1764 C CA  . SER A 1 214 ? 12.394 12.131 5.859   1.00 10.85 ? 214 SER A CA  1 
ATOM   1765 C C   . SER A 1 214 ? 13.644 12.582 6.638   1.00 11.01 ? 214 SER A C   1 
ATOM   1766 O O   . SER A 1 214 ? 13.589 12.756 7.857   1.00 11.25 ? 214 SER A O   1 
ATOM   1767 C CB  . SER A 1 214 ? 12.464 10.634 5.566   1.00 11.59 ? 214 SER A CB  1 
ATOM   1768 O OG  . SER A 1 214 ? 11.267 10.202 4.956   1.00 12.82 ? 214 SER A OG  1 
ATOM   1769 N N   . ALA A 1 215 ? 14.749 12.774 5.916   1.00 10.87 ? 215 ALA A N   1 
ATOM   1770 C CA  . ALA A 1 215 ? 16.048 13.090 6.513   1.00 11.54 ? 215 ALA A CA  1 
ATOM   1771 C C   . ALA A 1 215 ? 16.164 14.522 7.030   1.00 11.45 ? 215 ALA A C   1 
ATOM   1772 O O   . ALA A 1 215 ? 17.079 14.832 7.806   1.00 12.03 ? 215 ALA A O   1 
ATOM   1773 C CB  . ALA A 1 215 ? 17.178 12.794 5.501   1.00 11.86 ? 215 ALA A CB  1 
ATOM   1774 N N   . LYS A 1 216 ? 15.261 15.389 6.569   1.00 11.82 ? 216 LYS A N   1 
ATOM   1775 C CA  . LYS A 1 216 ? 15.287 16.826 6.914   1.00 11.76 ? 216 LYS A CA  1 
ATOM   1776 C C   . LYS A 1 216 ? 14.059 17.220 7.743   1.00 12.26 ? 216 LYS A C   1 
ATOM   1777 O O   . LYS A 1 216 ? 14.189 17.694 8.881   1.00 12.73 ? 216 LYS A O   1 
ATOM   1778 C CB  . LYS A 1 216 ? 15.373 17.685 5.635   1.00 12.14 ? 216 LYS A CB  1 
ATOM   1779 C CG  . LYS A 1 216 ? 16.611 17.396 4.836   1.00 12.61 ? 216 LYS A CG  1 
ATOM   1780 C CD  . LYS A 1 216 ? 16.763 18.336 3.644   1.00 14.51 ? 216 LYS A CD  1 
ATOM   1781 C CE  . LYS A 1 216 ? 18.143 18.178 3.024   1.00 15.75 ? 216 LYS A CE  1 
ATOM   1782 N NZ  . LYS A 1 216 ? 18.325 16.872 2.325   1.00 17.45 ? 216 LYS A NZ  1 
ATOM   1783 N N   . VAL A 1 217 ? 12.868 17.016 7.176   1.00 11.82 ? 217 VAL A N   1 
ATOM   1784 C CA  . VAL A 1 217 ? 11.631 17.392 7.872   1.00 11.95 ? 217 VAL A CA  1 
ATOM   1785 C C   . VAL A 1 217 ? 11.293 16.360 8.946   1.00 11.79 ? 217 VAL A C   1 
ATOM   1786 O O   . VAL A 1 217 ? 10.928 16.731 10.063  1.00 12.20 ? 217 VAL A O   1 
ATOM   1787 C CB  . VAL A 1 217 ? 10.459 17.647 6.899   1.00 12.00 ? 217 VAL A CB  1 
ATOM   1788 C CG1 . VAL A 1 217 ? 9.192  18.098 7.667   1.00 11.95 ? 217 VAL A CG1 1 
ATOM   1789 C CG2 . VAL A 1 217 ? 10.853 18.729 5.886   1.00 12.86 ? 217 VAL A CG2 1 
ATOM   1790 N N   . GLY A 1 218 ? 11.409 15.070 8.619   1.00 11.47 ? 218 GLY A N   1 
ATOM   1791 C CA  . GLY A 1 218 ? 11.188 14.014 9.624   1.00 11.43 ? 218 GLY A CA  1 
ATOM   1792 C C   . GLY A 1 218 ? 12.158 14.135 10.783  1.00 11.14 ? 218 GLY A C   1 
ATOM   1793 O O   . GLY A 1 218 ? 11.763 14.210 11.947  1.00 12.04 ? 218 GLY A O   1 
ATOM   1794 N N   . PHE A 1 219 ? 13.442 14.179 10.453  1.00 10.63 ? 219 PHE A N   1 
ATOM   1795 C CA  . PHE A 1 219 ? 14.509 14.411 11.436  1.00 10.39 ? 219 PHE A CA  1 
ATOM   1796 C C   . PHE A 1 219 ? 14.214 15.656 12.271  1.00 10.45 ? 219 PHE A C   1 
ATOM   1797 O O   . PHE A 1 219 ? 14.259 15.617 13.506  1.00 10.83 ? 219 PHE A O   1 
ATOM   1798 C CB  . PHE A 1 219 ? 15.809 14.587 10.645  1.00 10.51 ? 219 PHE A CB  1 
ATOM   1799 C CG  . PHE A 1 219 ? 17.050 14.828 11.464  1.00 10.75 ? 219 PHE A CG  1 
ATOM   1800 C CD1 . PHE A 1 219 ? 17.328 16.087 11.988  1.00 10.75 ? 219 PHE A CD1 1 
ATOM   1801 C CD2 . PHE A 1 219 ? 18.001 13.811 11.621  1.00 11.55 ? 219 PHE A CD2 1 
ATOM   1802 C CE1 . PHE A 1 219 ? 18.507 16.336 12.721  1.00 10.88 ? 219 PHE A CE1 1 
ATOM   1803 C CE2 . PHE A 1 219 ? 19.209 14.047 12.318  1.00 10.85 ? 219 PHE A CE2 1 
ATOM   1804 C CZ  . PHE A 1 219 ? 19.466 15.319 12.876  1.00 10.38 ? 219 PHE A CZ  1 
ATOM   1805 N N   . GLY A 1 220 ? 13.911 16.766 11.604  1.00 10.10 ? 220 GLY A N   1 
ATOM   1806 C CA  . GLY A 1 220 ? 13.662 18.031 12.302  1.00 11.63 ? 220 GLY A CA  1 
ATOM   1807 C C   . GLY A 1 220 ? 12.469 17.959 13.232  1.00 12.20 ? 220 GLY A C   1 
ATOM   1808 O O   . GLY A 1 220 ? 12.497 18.503 14.335  1.00 13.17 ? 220 GLY A O   1 
ATOM   1809 N N   . LEU A 1 221 ? 11.400 17.290 12.802  1.00 12.75 ? 221 LEU A N   1 
ATOM   1810 C CA  . LEU A 1 221 ? 10.225 17.135 13.680  1.00 13.54 ? 221 LEU A CA  1 
ATOM   1811 C C   . LEU A 1 221 ? 10.578 16.382 14.955  1.00 13.61 ? 221 LEU A C   1 
ATOM   1812 O O   . LEU A 1 221 ? 10.157 16.767 16.043  1.00 14.66 ? 221 LEU A O   1 
ATOM   1813 C CB  . LEU A 1 221 ? 9.077  16.430 12.954  1.00 13.68 ? 221 LEU A CB  1 
ATOM   1814 C CG  . LEU A 1 221 ? 8.332  17.346 11.972  1.00 14.49 ? 221 LEU A CG  1 
ATOM   1815 C CD1 . LEU A 1 221 ? 7.535  16.476 11.006  1.00 14.14 ? 221 LEU A CD1 1 
ATOM   1816 C CD2 . LEU A 1 221 ? 7.441  18.411 12.663  1.00 15.16 ? 221 LEU A CD2 1 
ATOM   1817 N N   . ILE A 1 222 ? 11.353 15.312 14.815  1.00 13.09 ? 222 ILE A N   1 
ATOM   1818 C CA  . ILE A 1 222 ? 11.779 14.541 15.987  1.00 13.39 ? 222 ILE A CA  1 
ATOM   1819 C C   . ILE A 1 222 ? 12.638 15.399 16.925  1.00 13.63 ? 222 ILE A C   1 
ATOM   1820 O O   . ILE A 1 222 ? 12.401 15.456 18.129  1.00 14.11 ? 222 ILE A O   1 
ATOM   1821 C CB  . ILE A 1 222 ? 12.565 13.271 15.579  1.00 13.41 ? 222 ILE A CB  1 
ATOM   1822 C CG1 . ILE A 1 222 ? 11.676 12.331 14.760  1.00 13.50 ? 222 ILE A CG1 1 
ATOM   1823 C CG2 . ILE A 1 222 ? 13.101 12.559 16.833  1.00 14.02 ? 222 ILE A CG2 1 
ATOM   1824 C CD1 . ILE A 1 222 ? 12.452 11.256 13.957  1.00 13.96 ? 222 ILE A CD1 1 
ATOM   1825 N N   . LEU A 1 223 ? 13.631 16.071 16.358  1.00 12.95 ? 223 LEU A N   1 
ATOM   1826 C CA  . LEU A 1 223 ? 14.530 16.905 17.143  1.00 12.31 ? 223 LEU A CA  1 
ATOM   1827 C C   . LEU A 1 223 ? 13.800 18.050 17.837  1.00 12.53 ? 223 LEU A C   1 
ATOM   1828 O O   . LEU A 1 223 ? 13.954 18.258 19.046  1.00 13.35 ? 223 LEU A O   1 
ATOM   1829 C CB  . LEU A 1 223 ? 15.647 17.469 16.245  1.00 12.24 ? 223 LEU A CB  1 
ATOM   1830 C CG  . LEU A 1 223 ? 16.665 18.370 16.962  1.00 11.91 ? 223 LEU A CG  1 
ATOM   1831 C CD1 . LEU A 1 223 ? 17.432 17.660 18.101  1.00 13.44 ? 223 LEU A CD1 1 
ATOM   1832 C CD2 . LEU A 1 223 ? 17.633 18.945 15.933  1.00 12.79 ? 223 LEU A CD2 1 
ATOM   1833 N N   . LEU A 1 224 ? 13.005 18.785 17.070  1.00 12.75 ? 224 LEU A N   1 
ATOM   1834 C CA  . LEU A 1 224 ? 12.478 20.059 17.567  1.00 13.83 ? 224 LEU A CA  1 
ATOM   1835 C C   . LEU A 1 224 ? 11.300 19.899 18.535  1.00 15.92 ? 224 LEU A C   1 
ATOM   1836 O O   . LEU A 1 224 ? 10.956 20.852 19.249  1.00 16.90 ? 224 LEU A O   1 
ATOM   1837 C CB  . LEU A 1 224 ? 12.161 21.010 16.406  1.00 12.93 ? 224 LEU A CB  1 
ATOM   1838 C CG  . LEU A 1 224 ? 13.379 21.403 15.550  1.00 11.72 ? 224 LEU A CG  1 
ATOM   1839 C CD1 . LEU A 1 224 ? 12.961 22.269 14.369  1.00 13.06 ? 224 LEU A CD1 1 
ATOM   1840 C CD2 . LEU A 1 224 ? 14.425 22.124 16.387  1.00 11.01 ? 224 LEU A CD2 1 
ATOM   1841 N N   . ARG A 1 225 ? 10.712 18.700 18.585  1.00 16.61 ? 225 ARG A N   1 
ATOM   1842 C CA  A ARG A 1 225 ? 9.645  18.404 19.548  0.50 17.80 ? 225 ARG A CA  1 
ATOM   1843 C CA  B ARG A 1 225 ? 9.647  18.412 19.555  0.50 17.96 ? 225 ARG A CA  1 
ATOM   1844 C C   . ARG A 1 225 ? 10.194 17.843 20.868  1.00 17.92 ? 225 ARG A C   1 
ATOM   1845 O O   . ARG A 1 225 ? 9.439  17.629 21.831  1.00 18.37 ? 225 ARG A O   1 
ATOM   1846 C CB  A ARG A 1 225 ? 8.608  17.460 18.922  0.50 17.80 ? 225 ARG A CB  1 
ATOM   1847 C CB  B ARG A 1 225 ? 8.583  17.485 18.951  0.50 17.98 ? 225 ARG A CB  1 
ATOM   1848 C CG  A ARG A 1 225 ? 7.828  18.098 17.768  0.50 18.63 ? 225 ARG A CG  1 
ATOM   1849 C CG  B ARG A 1 225 ? 8.993  16.033 18.773  0.50 19.26 ? 225 ARG A CG  1 
ATOM   1850 C CD  A ARG A 1 225 ? 6.732  17.195 17.198  0.50 19.63 ? 225 ARG A CD  1 
ATOM   1851 C CD  B ARG A 1 225 ? 7.790  15.191 18.334  0.50 20.11 ? 225 ARG A CD  1 
ATOM   1852 N NE  A ARG A 1 225 ? 5.420  17.513 17.767  0.50 24.34 ? 225 ARG A NE  1 
ATOM   1853 N NE  B ARG A 1 225 ? 8.168  14.004 17.565  0.50 25.25 ? 225 ARG A NE  1 
ATOM   1854 C CZ  A ARG A 1 225 ? 4.901  16.947 18.854  0.50 25.75 ? 225 ARG A CZ  1 
ATOM   1855 C CZ  B ARG A 1 225 ? 7.777  13.750 16.317  0.50 25.94 ? 225 ARG A CZ  1 
ATOM   1856 N NH1 A ARG A 1 225 ? 5.569  16.010 19.518  0.50 27.35 ? 225 ARG A NH1 1 
ATOM   1857 N NH1 B ARG A 1 225 ? 8.176  12.638 15.714  0.50 27.40 ? 225 ARG A NH1 1 
ATOM   1858 N NH2 A ARG A 1 225 ? 3.703  17.320 19.281  0.50 27.11 ? 225 ARG A NH2 1 
ATOM   1859 N NH2 B ARG A 1 225 ? 6.981  14.595 15.668  0.50 27.41 ? 225 ARG A NH2 1 
ATOM   1860 N N   . SER A 1 226 ? 11.507 17.612 20.916  1.00 17.36 ? 226 SER A N   1 
ATOM   1861 C CA  A SER A 1 226 ? 12.154 17.015 22.089  0.70 17.16 ? 226 SER A CA  1 
ATOM   1862 C CA  B SER A 1 226 ? 12.131 17.015 22.097  0.30 17.48 ? 226 SER A CA  1 
ATOM   1863 C C   . SER A 1 226 ? 12.561 18.041 23.143  1.00 17.49 ? 226 SER A C   1 
ATOM   1864 O O   . SER A 1 226 ? 12.842 19.197 22.823  1.00 17.79 ? 226 SER A O   1 
ATOM   1865 C CB  A SER A 1 226 ? 13.386 16.205 21.663  0.70 17.09 ? 226 SER A CB  1 
ATOM   1866 C CB  B SER A 1 226 ? 13.327 16.150 21.693  0.30 17.42 ? 226 SER A CB  1 
ATOM   1867 O OG  A SER A 1 226 ? 14.508 17.043 21.417  0.70 14.87 ? 226 SER A OG  1 
ATOM   1868 O OG  B SER A 1 226 ? 13.966 15.605 22.835  0.30 16.98 ? 226 SER A OG  1 
ATOM   1869 N N   . ARG A 1 227 ? 12.611 17.601 24.401  1.00 17.80 ? 227 ARG A N   1 
ATOM   1870 C CA  A ARG A 1 227 ? 13.117 18.442 25.480  0.70 18.74 ? 227 ARG A CA  1 
ATOM   1871 C CA  B ARG A 1 227 ? 13.119 18.427 25.494  0.30 18.06 ? 227 ARG A CA  1 
ATOM   1872 C C   . ARG A 1 227 ? 14.641 18.514 25.432  1.00 18.28 ? 227 ARG A C   1 
ATOM   1873 O O   . ARG A 1 227 ? 15.246 19.381 26.057  1.00 18.55 ? 227 ARG A O   1 
ATOM   1874 C CB  A ARG A 1 227 ? 12.625 17.935 26.846  0.70 19.47 ? 227 ARG A CB  1 
ATOM   1875 C CB  B ARG A 1 227 ? 12.696 17.855 26.850  0.30 18.26 ? 227 ARG A CB  1 
ATOM   1876 C CG  A ARG A 1 227 ? 12.163 16.470 26.862  0.70 22.50 ? 227 ARG A CG  1 
ATOM   1877 C CG  B ARG A 1 227 ? 11.196 17.870 27.116  0.30 18.01 ? 227 ARG A CG  1 
ATOM   1878 C CD  A ARG A 1 227 ? 10.955 16.243 25.928  0.70 26.98 ? 227 ARG A CD  1 
ATOM   1879 C CD  B ARG A 1 227 ? 10.854 17.022 28.338  0.30 20.02 ? 227 ARG A CD  1 
ATOM   1880 N NE  A ARG A 1 227 ? 10.602 14.835 25.739  0.70 30.04 ? 227 ARG A NE  1 
ATOM   1881 N NE  B ARG A 1 227 ? 11.065 15.599 28.078  0.30 20.94 ? 227 ARG A NE  1 
ATOM   1882 C CZ  A ARG A 1 227 ? 11.217 13.990 24.915  0.70 30.62 ? 227 ARG A CZ  1 
ATOM   1883 C CZ  B ARG A 1 227 ? 11.015 14.638 28.997  0.30 21.31 ? 227 ARG A CZ  1 
ATOM   1884 N NH1 A ARG A 1 227 ? 12.254 14.377 24.192  0.70 32.83 ? 227 ARG A NH1 1 
ATOM   1885 N NH1 B ARG A 1 227 ? 10.755 14.924 30.267  0.30 22.45 ? 227 ARG A NH1 1 
ATOM   1886 N NH2 A ARG A 1 227 ? 10.797 12.739 24.824  0.70 32.76 ? 227 ARG A NH2 1 
ATOM   1887 N NH2 B ARG A 1 227 ? 11.227 13.380 28.640  0.30 21.81 ? 227 ARG A NH2 1 
ATOM   1888 N N   . ALA A 1 228 ? 15.248 17.610 24.662  1.00 18.16 ? 228 ALA A N   1 
ATOM   1889 C CA  . ALA A 1 228 ? 16.713 17.507 24.570  1.00 18.32 ? 228 ALA A CA  1 
ATOM   1890 C C   . ALA A 1 228 ? 17.409 18.775 24.086  1.00 18.48 ? 228 ALA A C   1 
ATOM   1891 O O   . ALA A 1 228 ? 18.593 18.982 24.379  1.00 19.33 ? 228 ALA A O   1 
ATOM   1892 C CB  . ALA A 1 228 ? 17.106 16.333 23.679  1.00 18.12 ? 228 ALA A CB  1 
ATOM   1893 N N   . ILE A 1 229 ? 16.691 19.611 23.334  1.00 18.61 ? 229 ILE A N   1 
ATOM   1894 C CA  . ILE A 1 229 ? 17.294 20.809 22.754  1.00 18.43 ? 229 ILE A CA  1 
ATOM   1895 C C   . ILE A 1 229 ? 17.395 21.988 23.737  1.00 19.18 ? 229 ILE A C   1 
ATOM   1896 O O   . ILE A 1 229 ? 18.069 22.982 23.448  1.00 18.28 ? 229 ILE A O   1 
ATOM   1897 C CB  . ILE A 1 229 ? 16.559 21.255 21.460  1.00 18.01 ? 229 ILE A CB  1 
ATOM   1898 C CG1 . ILE A 1 229 ? 15.109 21.639 21.761  1.00 18.27 ? 229 ILE A CG1 1 
ATOM   1899 C CG2 . ILE A 1 229 ? 16.644 20.168 20.385  1.00 18.35 ? 229 ILE A CG2 1 
ATOM   1900 C CD1 . ILE A 1 229 ? 14.426 22.379 20.616  1.00 18.03 ? 229 ILE A CD1 1 
ATOM   1901 N N   . PHE A 1 230 ? 16.747 21.856 24.897  1.00 20.58 ? 230 PHE A N   1 
ATOM   1902 C CA  . PHE A 1 230 ? 16.714 22.933 25.892  1.00 22.47 ? 230 PHE A CA  1 
ATOM   1903 C C   . PHE A 1 230 ? 17.877 22.934 26.881  1.00 23.98 ? 230 PHE A C   1 
ATOM   1904 O O   . PHE A 1 230 ? 18.269 21.882 27.377  1.00 25.12 ? 230 PHE A O   1 
ATOM   1905 C CB  . PHE A 1 230 ? 15.372 22.938 26.621  1.00 22.48 ? 230 PHE A CB  1 
ATOM   1906 C CG  . PHE A 1 230 ? 14.258 23.481 25.782  1.00 22.21 ? 230 PHE A CG  1 
ATOM   1907 C CD1 . PHE A 1 230 ? 13.543 22.646 24.930  1.00 22.72 ? 230 PHE A CD1 1 
ATOM   1908 C CD2 . PHE A 1 230 ? 13.971 24.837 25.789  1.00 23.68 ? 230 PHE A CD2 1 
ATOM   1909 C CE1 . PHE A 1 230 ? 12.532 23.151 24.130  1.00 24.45 ? 230 PHE A CE1 1 
ATOM   1910 C CE2 . PHE A 1 230 ? 12.964 25.353 24.990  1.00 24.87 ? 230 PHE A CE2 1 
ATOM   1911 C CZ  . PHE A 1 230 ? 12.241 24.512 24.160  1.00 23.97 ? 230 PHE A CZ  1 
ATOM   1912 N N   . GLY A 1 231 ? 18.417 24.127 27.140  1.00 25.16 ? 231 GLY A N   1 
ATOM   1913 C CA  . GLY A 1 231 ? 19.501 24.306 28.109  1.00 26.52 ? 231 GLY A CA  1 
ATOM   1914 C C   . GLY A 1 231 ? 18.971 24.364 29.528  1.00 27.34 ? 231 GLY A C   1 
HETATM 1915 C C1  . RET B 2 .   ? 26.245 10.459 -3.065  1.00 15.09 ? 301 RET A C1  1 
HETATM 1916 C C2  . RET B 2 .   ? 26.589 9.853  -4.410  1.00 16.79 ? 301 RET A C2  1 
HETATM 1917 C C3  . RET B 2 .   ? 26.977 8.394  -4.328  1.00 15.38 ? 301 RET A C3  1 
HETATM 1918 C C4  . RET B 2 .   ? 27.740 8.012  -3.047  1.00 13.94 ? 301 RET A C4  1 
HETATM 1919 C C5  . RET B 2 .   ? 27.016 8.505  -1.812  1.00 13.07 ? 301 RET A C5  1 
HETATM 1920 C C6  . RET B 2 .   ? 26.255 9.613  -1.798  1.00 13.29 ? 301 RET A C6  1 
HETATM 1921 C C7  . RET B 2 .   ? 25.606 9.973  -0.491  1.00 13.22 ? 301 RET A C7  1 
HETATM 1922 C C8  . RET B 2 .   ? 24.590 10.820 -0.340  1.00 13.25 ? 301 RET A C8  1 
HETATM 1923 C C9  . RET B 2 .   ? 23.932 11.134 0.940   1.00 12.72 ? 301 RET A C9  1 
HETATM 1924 C C10 . RET B 2 .   ? 23.027 12.129 0.941   1.00 12.83 ? 301 RET A C10 1 
HETATM 1925 C C11 . RET B 2 .   ? 22.248 12.602 2.082   1.00 13.11 ? 301 RET A C11 1 
HETATM 1926 C C12 . RET B 2 .   ? 21.297 13.485 1.804   1.00 14.80 ? 301 RET A C12 1 
HETATM 1927 C C13 . RET B 2 .   ? 20.428 14.121 2.785   1.00 15.77 ? 301 RET A C13 1 
HETATM 1928 C C14 . RET B 2 .   ? 19.720 15.183 2.313   1.00 20.39 ? 301 RET A C14 1 
HETATM 1929 C C15 . RET B 2 .   ? 18.827 16.002 3.100   1.00 20.88 ? 301 RET A C15 1 
HETATM 1930 C C16 . RET B 2 .   ? 26.039 11.991 -2.959  1.00 14.76 ? 301 RET A C16 1 
HETATM 1931 C C17 . RET B 2 .   ? 24.749 10.253 -3.381  1.00 13.98 ? 301 RET A C17 1 
HETATM 1932 C C18 . RET B 2 .   ? 27.182 7.652  -0.584  1.00 16.37 ? 301 RET A C18 1 
HETATM 1933 C C19 . RET B 2 .   ? 24.230 10.318 2.171   1.00 12.70 ? 301 RET A C19 1 
HETATM 1934 C C20 . RET B 2 .   ? 20.386 13.630 4.203   1.00 17.18 ? 301 RET A C20 1 
HETATM 1935 C C1  . D12 C 3 .   ? 41.570 3.068  12.804  1.00 52.90 ? 402 D12 A C1  1 
HETATM 1936 C C2  . D12 C 3 .   ? 40.792 3.063  11.505  1.00 53.22 ? 402 D12 A C2  1 
HETATM 1937 C C3  . D12 C 3 .   ? 41.262 1.949  10.574  1.00 53.34 ? 402 D12 A C3  1 
HETATM 1938 C C4  . D12 C 3 .   ? 40.809 2.208  9.139   1.00 53.51 ? 402 D12 A C4  1 
HETATM 1939 C C5  . D12 C 3 .   ? 40.907 0.948  8.281   1.00 53.47 ? 402 D12 A C5  1 
HETATM 1940 C C6  . D12 C 3 .   ? 39.544 0.298  8.167   1.00 53.31 ? 402 D12 A C6  1 
HETATM 1941 C C7  . D12 C 3 .   ? 39.174 -0.236 7.083   1.00 53.15 ? 402 D12 A C7  1 
HETATM 1942 C C8  . D12 C 3 .   ? 38.831 -0.902 6.132   1.00 52.89 ? 402 D12 A C8  1 
HETATM 1943 C C9  . D12 C 3 .   ? 38.468 -1.742 5.356   1.00 53.24 ? 402 D12 A C9  1 
HETATM 1944 C C10 . D12 C 3 .   ? 38.161 -2.766 4.663   1.00 53.15 ? 402 D12 A C10 1 
HETATM 1945 C C11 . D12 C 3 .   ? 38.074 -2.651 3.382   1.00 53.30 ? 402 D12 A C11 1 
HETATM 1946 C C12 . D12 C 3 .   ? 37.877 -2.834 2.119   1.00 53.40 ? 402 D12 A C12 1 
HETATM 1947 C C1  . D12 D 3 .   ? 34.251 -0.194 -2.536  1.00 37.03 ? 403 D12 A C1  1 
HETATM 1948 C C2  . D12 D 3 .   ? 35.292 -0.873 -3.403  1.00 36.63 ? 403 D12 A C2  1 
HETATM 1949 C C3  . D12 D 3 .   ? 34.649 -1.696 -4.513  1.00 36.60 ? 403 D12 A C3  1 
HETATM 1950 C C4  . D12 D 3 .   ? 35.605 -2.744 -5.066  1.00 37.14 ? 403 D12 A C4  1 
HETATM 1951 C C5  . D12 D 3 .   ? 35.177 -3.227 -6.449  1.00 37.09 ? 403 D12 A C5  1 
HETATM 1952 C C6  . D12 D 3 .   ? 36.416 -3.481 -7.277  1.00 36.90 ? 403 D12 A C6  1 
HETATM 1953 C C7  . D12 D 3 .   ? 36.335 -3.892 -8.485  1.00 36.64 ? 403 D12 A C7  1 
HETATM 1954 C C8  . D12 D 3 .   ? 36.525 -4.204 -9.627  1.00 37.58 ? 403 D12 A C8  1 
HETATM 1955 C C9  . D12 D 3 .   ? 36.899 -4.385 -10.749 1.00 38.56 ? 403 D12 A C9  1 
HETATM 1956 C C10 . D12 D 3 .   ? 37.353 -4.351 -11.937 1.00 39.55 ? 403 D12 A C10 1 
HETATM 1957 C C11 . D12 D 3 .   ? 37.452 -5.413 -12.621 1.00 40.12 ? 403 D12 A C11 1 
HETATM 1958 C C12 . D12 D 3 .   ? 37.576 -6.370 -13.444 1.00 40.88 ? 403 D12 A C12 1 
HETATM 1959 C C1  . D12 E 3 .   ? 11.439 -4.640 -3.682  1.00 43.15 ? 405 D12 A C1  1 
HETATM 1960 C C2  . D12 E 3 .   ? 12.541 -4.711 -4.718  1.00 42.97 ? 405 D12 A C2  1 
HETATM 1961 C C3  . D12 E 3 .   ? 12.005 -5.012 -6.116  1.00 42.60 ? 405 D12 A C3  1 
HETATM 1962 C C4  . D12 E 3 .   ? 12.915 -4.405 -7.187  1.00 42.49 ? 405 D12 A C4  1 
HETATM 1963 C C5  . D12 E 3 .   ? 12.744 -5.050 -8.564  1.00 41.27 ? 405 D12 A C5  1 
HETATM 1964 C C6  . D12 E 3 .   ? 13.780 -4.466 -9.505  1.00 40.71 ? 405 D12 A C6  1 
HETATM 1965 C C7  . D12 E 3 .   ? 13.737 -4.639 -10.770 1.00 41.02 ? 405 D12 A C7  1 
HETATM 1966 C C8  . D12 E 3 .   ? 13.926 -4.577 -11.965 1.00 40.88 ? 405 D12 A C8  1 
HETATM 1967 C C9  . D12 E 3 .   ? 13.982 -4.772 -13.150 1.00 40.93 ? 405 D12 A C9  1 
HETATM 1968 C C10 . D12 E 3 .   ? 13.915 -5.206 -14.353 1.00 41.05 ? 405 D12 A C10 1 
HETATM 1969 C C11 . D12 E 3 .   ? 14.249 -4.456 -15.348 1.00 40.93 ? 405 D12 A C11 1 
HETATM 1970 C C12 . D12 E 3 .   ? 14.571 -3.876 -16.449 1.00 38.93 ? 405 D12 A C12 1 
HETATM 1971 C C1  . D10 F 4 .   ? 3.041  23.442 -5.054  1.00 38.67 ? 406 D10 A C1  1 
HETATM 1972 C C2  . D10 F 4 .   ? 4.347  23.472 -5.809  1.00 38.24 ? 406 D10 A C2  1 
HETATM 1973 C C3  . D10 F 4 .   ? 4.115  24.174 -7.140  1.00 38.34 ? 406 D10 A C3  1 
HETATM 1974 C C4  . D10 F 4 .   ? 4.072  23.187 -8.300  1.00 37.46 ? 406 D10 A C4  1 
HETATM 1975 C C5  . D10 F 4 .   ? 2.690  23.135 -8.938  1.00 35.88 ? 406 D10 A C5  1 
HETATM 1976 C C6  . D10 F 4 .   ? 2.769  23.172 -10.458 1.00 34.17 ? 406 D10 A C6  1 
HETATM 1977 C C7  . D10 F 4 .   ? 1.425  22.798 -11.075 1.00 33.90 ? 406 D10 A C7  1 
HETATM 1978 C C8  . D10 F 4 .   ? 1.503  22.830 -12.595 1.00 34.09 ? 406 D10 A C8  1 
HETATM 1979 C C9  . D10 F 4 .   ? 0.532  21.826 -13.202 1.00 34.22 ? 406 D10 A C9  1 
HETATM 1980 C C10 . D10 F 4 .   ? 0.705  21.778 -14.703 1.00 33.89 ? 406 D10 A C10 1 
HETATM 1981 C C1  . D10 G 4 .   ? 41.202 6.796  -2.991  1.00 43.21 ? 409 D10 A C1  1 
HETATM 1982 C C2  . D10 G 4 .   ? 41.388 5.535  -3.801  1.00 43.21 ? 409 D10 A C2  1 
HETATM 1983 C C3  . D10 G 4 .   ? 41.186 5.838  -5.281  1.00 43.49 ? 409 D10 A C3  1 
HETATM 1984 C C4  . D10 G 4 .   ? 41.951 4.851  -6.157  1.00 43.37 ? 409 D10 A C4  1 
HETATM 1985 C C5  . D10 G 4 .   ? 41.044 4.221  -7.207  1.00 43.81 ? 409 D10 A C5  1 
HETATM 1986 C C6  . D10 G 4 .   ? 41.806 3.918  -8.492  1.00 43.69 ? 409 D10 A C6  1 
HETATM 1987 C C7  . D10 G 4 .   ? 40.960 3.101  -9.465  1.00 43.57 ? 409 D10 A C7  1 
HETATM 1988 C C8  . D10 G 4 .   ? 41.767 2.721  -10.700 1.00 43.69 ? 409 D10 A C8  1 
HETATM 1989 C C9  . D10 G 4 .   ? 40.862 2.332  -11.863 1.00 43.78 ? 409 D10 A C9  1 
HETATM 1990 C C10 . D10 G 4 .   ? 41.663 2.279  -13.143 1.00 43.77 ? 409 D10 A C10 1 
HETATM 1991 C C27 . R16 H 5 .   ? 38.883 -0.272 15.553  1.00 41.74 ? 411 R16 A C27 1 
HETATM 1992 C C28 . R16 H 5 .   ? 38.443 -0.240 14.366  1.00 41.70 ? 411 R16 A C28 1 
HETATM 1993 C C29 . R16 H 5 .   ? 37.913 -0.176 13.303  1.00 41.18 ? 411 R16 A C29 1 
HETATM 1994 C C30 . R16 H 5 .   ? 37.269 -0.122 12.297  1.00 40.78 ? 411 R16 A C30 1 
HETATM 1995 C C31 . R16 H 5 .   ? 36.655 -0.205 11.277  1.00 38.83 ? 411 R16 A C31 1 
HETATM 1996 C C32 . R16 H 5 .   ? 36.031 -0.390 10.279  1.00 37.15 ? 411 R16 A C32 1 
HETATM 1997 C C33 . R16 H 5 .   ? 35.362 -0.398 9.271   1.00 35.71 ? 411 R16 A C33 1 
HETATM 1998 C C34 . R16 H 5 .   ? 34.436 -0.284 8.468   1.00 33.04 ? 411 R16 A C34 1 
HETATM 1999 C C35 . R16 H 5 .   ? 33.345 0.045  8.031   1.00 31.51 ? 411 R16 A C35 1 
HETATM 2000 C C36 . R16 H 5 .   ? 32.218 0.452  7.938   1.00 29.12 ? 411 R16 A C36 1 
HETATM 2001 C C37 . R16 H 5 .   ? 31.112 0.862  8.199   1.00 28.13 ? 411 R16 A C37 1 
HETATM 2002 C C38 . R16 H 5 .   ? 29.312 1.465  9.624   1.00 26.21 ? 411 R16 A C38 1 
HETATM 2003 C C39 . R16 H 5 .   ? 30.162 1.242  8.827   1.00 27.52 ? 411 R16 A C39 1 
HETATM 2004 C C40 . R16 H 5 .   ? 28.418 1.592  10.390  1.00 25.90 ? 411 R16 A C40 1 
HETATM 2005 C C41 . R16 H 5 .   ? 27.431 1.699  11.038  1.00 26.47 ? 411 R16 A C41 1 
HETATM 2006 C C42 . R16 H 5 .   ? 26.307 1.748  11.603  1.00 27.13 ? 411 R16 A C42 1 
HETATM 2007 C C1  . CPS I 6 .   ? 4.398  23.223 -15.080 1.00 45.53 ? 501 CPS A C1  1 
HETATM 2008 C C2  . CPS I 6 .   ? 5.907  23.190 -14.800 1.00 45.09 ? 501 CPS A C2  1 
HETATM 2009 C C3  . CPS I 6 .   ? 6.158  25.339 -16.241 1.00 43.69 ? 501 CPS A C3  1 
HETATM 2010 C C4  . CPS I 6 .   ? 6.966  26.098 -17.306 1.00 43.44 ? 501 CPS A C4  1 
HETATM 2011 C C5  . CPS I 6 .   ? 8.476  26.076 -17.027 1.00 43.75 ? 501 CPS A C5  1 
HETATM 2012 C C6  . CPS I 6 .   ? 8.914  24.620 -16.879 1.00 43.78 ? 501 CPS A C6  1 
HETATM 2013 C C7  . CPS I 6 .   ? 10.442 24.615 -16.968 1.00 43.66 ? 501 CPS A C7  1 
HETATM 2014 C C8  . CPS I 6 .   ? 10.746 25.784 -17.906 1.00 44.02 ? 501 CPS A C8  1 
HETATM 2015 C C9  . CPS I 6 .   ? 9.411  26.508 -18.172 1.00 44.20 ? 501 CPS A C9  1 
HETATM 2016 C C10 . CPS I 6 .   ? 8.762  26.905 -15.760 1.00 43.17 ? 501 CPS A C10 1 
HETATM 2017 C C11 . CPS I 6 .   ? 6.124  23.906 -13.463 1.00 44.47 ? 501 CPS A C11 1 
HETATM 2018 C C12 . CPS I 6 .   ? 3.901  22.261 -16.164 1.00 45.94 ? 501 CPS A C12 1 
HETATM 2019 C C13 . CPS I 6 .   ? 4.387  20.825 -15.988 1.00 45.96 ? 501 CPS A C13 1 
HETATM 2020 C C14 . CPS I 6 .   ? 5.902  20.801 -15.813 1.00 45.42 ? 501 CPS A C14 1 
HETATM 2021 C C15 . CPS I 6 .   ? 6.399  21.730 -14.691 1.00 45.06 ? 501 CPS A C15 1 
HETATM 2022 C C16 . CPS I 6 .   ? 7.928  21.599 -14.585 1.00 44.73 ? 501 CPS A C16 1 
HETATM 2023 C C17 . CPS I 6 .   ? 8.724  22.416 -15.611 1.00 44.50 ? 501 CPS A C17 1 
HETATM 2024 C C18 . CPS I 6 .   ? 8.219  23.860 -15.736 1.00 44.28 ? 501 CPS A C18 1 
HETATM 2025 C C19 . CPS I 6 .   ? 6.683  23.919 -15.931 1.00 44.29 ? 501 CPS A C19 1 
HETATM 2026 C C20 . CPS I 6 .   ? 9.554  28.015 -18.463 1.00 44.92 ? 501 CPS A C20 1 
HETATM 2027 C C21 . CPS I 6 .   ? 8.272  28.595 -19.058 1.00 44.64 ? 501 CPS A C21 1 
HETATM 2028 C C22 . CPS I 6 .   ? 10.766 28.371 -19.338 1.00 45.74 ? 501 CPS A C22 1 
HETATM 2029 C C23 . CPS I 6 .   ? 10.546 28.189 -20.843 1.00 46.64 ? 501 CPS A C23 1 
HETATM 2030 C C24 . CPS I 6 .   ? 11.875 28.102 -21.559 1.00 46.74 ? 501 CPS A C24 1 
HETATM 2031 O O2  . CPS I 6 .   ? 4.043  20.078 -17.163 1.00 46.75 ? 501 CPS A O2  1 
HETATM 2032 O O3  . CPS I 6 .   ? 8.703  21.765 -16.893 1.00 44.39 ? 501 CPS A O3  1 
HETATM 2033 O O4  . CPS I 6 .   ? 6.679  25.538 -18.595 1.00 42.37 ? 501 CPS A O4  1 
HETATM 2034 C C1  . D10 J 4 .   ? 10.571 30.598 3.395   1.00 54.51 ? 250 D10 A C1  1 
HETATM 2035 C C2  . D10 J 4 .   ? 11.643 30.157 2.425   1.00 54.81 ? 250 D10 A C2  1 
HETATM 2036 C C3  . D10 J 4 .   ? 12.099 31.353 1.594   1.00 54.46 ? 250 D10 A C3  1 
HETATM 2037 C C4  . D10 J 4 .   ? 13.397 31.065 0.843   1.00 54.40 ? 250 D10 A C4  1 
HETATM 2038 C C5  . D10 J 4 .   ? 13.765 32.228 -0.074  1.00 53.96 ? 250 D10 A C5  1 
HETATM 2039 C C6  . D10 J 4 .   ? 14.676 31.794 -1.221  1.00 53.77 ? 250 D10 A C6  1 
HETATM 2040 C C7  . D10 J 4 .   ? 13.910 31.675 -2.536  1.00 53.38 ? 250 D10 A C7  1 
HETATM 2041 C C8  . D10 J 4 .   ? 14.850 31.430 -3.712  1.00 53.07 ? 250 D10 A C8  1 
HETATM 2042 C C9  . D10 J 4 .   ? 14.346 30.289 -4.592  1.00 52.86 ? 250 D10 A C9  1 
HETATM 2043 C C10 . D10 J 4 .   ? 15.010 30.352 -5.947  1.00 52.55 ? 250 D10 A C10 1 
HETATM 2044 C C1  . D12 K 3 .   ? -1.525 21.822 3.503   1.00 51.02 ? 251 D12 A C1  1 
HETATM 2045 C C2  . D12 K 3 .   ? -1.707 22.166 2.039   1.00 51.12 ? 251 D12 A C2  1 
HETATM 2046 C C3  . D12 K 3 .   ? -0.468 22.841 1.458   1.00 51.02 ? 251 D12 A C3  1 
HETATM 2047 C C4  . D12 K 3 .   ? -0.445 22.717 -0.061  1.00 50.83 ? 251 D12 A C4  1 
HETATM 2048 C C5  . D12 K 3 .   ? 0.977  22.795 -0.614  1.00 51.00 ? 251 D12 A C5  1 
HETATM 2049 C C6  . D12 K 3 .   ? 0.932  22.938 -2.121  1.00 50.92 ? 251 D12 A C6  1 
HETATM 2050 C C7  . D12 K 3 .   ? 1.021  21.925 -2.871  1.00 51.37 ? 251 D12 A C7  1 
HETATM 2051 C C8  . D12 K 3 .   ? 1.215  21.076 -3.702  1.00 51.73 ? 251 D12 A C8  1 
HETATM 2052 C C9  . D12 K 3 .   ? 1.552  20.392 -4.629  1.00 51.88 ? 251 D12 A C9  1 
HETATM 2053 C C10 . D12 K 3 .   ? 2.115  19.695 -5.523  1.00 51.99 ? 251 D12 A C10 1 
HETATM 2054 C C11 . D12 K 3 .   ? 1.489  19.347 -6.560  1.00 52.11 ? 251 D12 A C11 1 
HETATM 2055 C C12 . D12 K 3 .   ? 0.952  19.027 -7.660  1.00 51.76 ? 251 D12 A C12 1 
HETATM 2056 C C20 . HP6 L 7 .   ? 7.909  -1.872 -4.163  1.00 42.90 ? 401 HP6 A C20 1 
HETATM 2057 C C21 . HP6 L 7 .   ? 8.582  -1.943 -5.519  1.00 43.62 ? 401 HP6 A C21 1 
HETATM 2058 C C22 . HP6 L 7 .   ? 7.793  -2.831 -6.476  1.00 43.42 ? 401 HP6 A C22 1 
HETATM 2059 C C23 . HP6 L 7 .   ? 8.451  -2.890 -7.801  1.00 43.67 ? 401 HP6 A C23 1 
HETATM 2060 C C24 . HP6 L 7 .   ? 8.845  -3.089 -8.918  1.00 43.63 ? 401 HP6 A C24 1 
HETATM 2061 C C25 . HP6 L 7 .   ? 9.038  -3.288 -10.080 1.00 42.94 ? 401 HP6 A C25 1 
HETATM 2062 C C26 . HP6 L 7 .   ? 9.089  -3.535 -11.320 1.00 42.54 ? 401 HP6 A C26 1 
HETATM 2063 C C1  . D12 M 3 .   ? 38.901 -1.831 -2.492  1.00 54.39 ? 252 D12 A C1  1 
HETATM 2064 C C2  . D12 M 3 .   ? 38.960 -3.261 -2.987  1.00 54.23 ? 252 D12 A C2  1 
HETATM 2065 C C3  . D12 M 3 .   ? 39.489 -3.339 -4.417  1.00 53.97 ? 252 D12 A C3  1 
HETATM 2066 C C4  . D12 M 3 .   ? 39.447 -4.775 -4.928  1.00 54.18 ? 252 D12 A C4  1 
HETATM 2067 C C5  . D12 M 3 .   ? 39.775 -4.856 -6.416  1.00 54.12 ? 252 D12 A C5  1 
HETATM 2068 C C6  . D12 M 3 .   ? 39.581 -6.277 -6.896  1.00 54.09 ? 252 D12 A C6  1 
HETATM 2069 C C7  . D12 M 3 .   ? 40.007 -6.616 -8.031  1.00 54.36 ? 252 D12 A C7  1 
HETATM 2070 C C8  . D12 M 3 .   ? 40.483 -6.924 -9.076  1.00 54.76 ? 252 D12 A C8  1 
HETATM 2071 C C9  . D12 M 3 .   ? 40.945 -7.002 -10.203 1.00 55.27 ? 252 D12 A C9  1 
HETATM 2072 C C10 . D12 M 3 .   ? 41.360 -6.718 -11.384 1.00 55.68 ? 252 D12 A C10 1 
HETATM 2073 C C11 . D12 M 3 .   ? 41.509 -7.652 -12.237 1.00 56.00 ? 252 D12 A C11 1 
HETATM 2074 C C12 . D12 M 3 .   ? 41.697 -8.408 -13.254 1.00 55.73 ? 252 D12 A C12 1 
HETATM 2075 C C1  . DD9 N 8 .   ? 39.750 13.286 -2.526  1.00 41.22 ? 253 DD9 A C1  1 
HETATM 2076 C C2  . DD9 N 8 .   ? 40.038 11.901 -3.059  1.00 40.71 ? 253 DD9 A C2  1 
HETATM 2077 C C3  . DD9 N 8 .   ? 40.915 12.007 -4.304  1.00 40.00 ? 253 DD9 A C3  1 
HETATM 2078 C C4  . DD9 N 8 .   ? 41.135 10.640 -4.941  1.00 39.85 ? 253 DD9 A C4  1 
HETATM 2079 C C5  . DD9 N 8 .   ? 41.321 10.753 -6.451  1.00 39.24 ? 253 DD9 A C5  1 
HETATM 2080 C C6  . DD9 N 8 .   ? 41.266 9.383  -7.121  1.00 38.41 ? 253 DD9 A C6  1 
HETATM 2081 C C7  . DD9 N 8 .   ? 41.043 9.507  -8.622  1.00 38.23 ? 253 DD9 A C7  1 
HETATM 2082 C C8  . DD9 N 8 .   ? 40.404 8.247  -9.190  1.00 37.86 ? 253 DD9 A C8  1 
HETATM 2083 C C9  . DD9 N 8 .   ? 40.461 8.245  -10.701 1.00 37.96 ? 253 DD9 A C9  1 
HETATM 2084 C C1  . D12 O 3 .   ? 12.841 0.109  -6.094  1.00 47.75 ? 254 D12 A C1  1 
HETATM 2085 C C2  . D12 O 3 .   ? 12.242 0.480  -7.433  1.00 48.10 ? 254 D12 A C2  1 
HETATM 2086 C C3  . D12 O 3 .   ? 12.853 -0.347 -8.558  1.00 48.33 ? 254 D12 A C3  1 
HETATM 2087 C C4  . D12 O 3 .   ? 11.906 -0.449 -9.747  1.00 48.80 ? 254 D12 A C4  1 
HETATM 2088 C C5  . D12 O 3 .   ? 12.489 0.228  -10.982 1.00 49.72 ? 254 D12 A C5  1 
HETATM 2089 C C6  . D12 O 3 .   ? 12.596 -0.786 -12.096 1.00 50.48 ? 254 D12 A C6  1 
HETATM 2090 C C7  . D12 O 3 .   ? 12.220 -0.477 -13.256 1.00 51.45 ? 254 D12 A C7  1 
HETATM 2091 C C8  . D12 O 3 .   ? 11.851 -0.058 -14.303 1.00 52.31 ? 254 D12 A C8  1 
HETATM 2092 C C9  . D12 O 3 .   ? 11.446 0.459  -15.295 1.00 52.83 ? 254 D12 A C9  1 
HETATM 2093 C C10 . D12 O 3 .   ? 10.903 1.002  -16.298 1.00 53.04 ? 254 D12 A C10 1 
HETATM 2094 C C11 . D12 O 3 .   ? 11.612 1.564  -17.171 1.00 53.20 ? 254 D12 A C11 1 
HETATM 2095 C C12 . D12 O 3 .   ? 12.301 2.093  -18.077 1.00 53.05 ? 254 D12 A C12 1 
HETATM 2096 C C1  . D12 P 3 .   ? 40.031 16.624 8.304   1.00 54.59 ? 255 D12 A C1  1 
HETATM 2097 C C2  . D12 P 3 .   ? 39.692 16.065 6.938   1.00 54.94 ? 255 D12 A C2  1 
HETATM 2098 C C3  . D12 P 3 .   ? 38.558 15.048 7.017   1.00 55.22 ? 255 D12 A C3  1 
HETATM 2099 C C4  . D12 P 3 .   ? 39.042 13.642 6.672   1.00 55.55 ? 255 D12 A C4  1 
HETATM 2100 C C5  . D12 P 3 .   ? 38.530 12.620 7.689   1.00 55.87 ? 255 D12 A C5  1 
HETATM 2101 C C6  . D12 P 3 .   ? 39.147 11.261 7.430   1.00 55.96 ? 255 D12 A C6  1 
HETATM 2102 C C7  . D12 P 3 .   ? 38.686 10.522 6.508   1.00 56.07 ? 255 D12 A C7  1 
HETATM 2103 C C8  . D12 P 3 .   ? 38.181 10.003 5.547   1.00 56.17 ? 255 D12 A C8  1 
HETATM 2104 C C9  . D12 P 3 .   ? 37.811 9.727  4.425   1.00 56.13 ? 255 D12 A C9  1 
HETATM 2105 C C10 . D12 P 3 .   ? 37.138 9.543  3.360   1.00 55.77 ? 255 D12 A C10 1 
HETATM 2106 C C11 . D12 P 3 .   ? 37.493 8.667  2.525   1.00 55.60 ? 255 D12 A C11 1 
HETATM 2107 C C12 . D12 P 3 .   ? 37.774 7.856  1.594   1.00 55.28 ? 255 D12 A C12 1 
HETATM 2108 C C1  . D12 Q 3 .   ? 21.717 32.652 14.561  1.00 53.71 ? 256 D12 A C1  1 
HETATM 2109 C C2  . D12 Q 3 .   ? 20.459 32.935 13.763  1.00 53.32 ? 256 D12 A C2  1 
HETATM 2110 C C3  . D12 Q 3 .   ? 20.754 33.112 12.277  1.00 53.35 ? 256 D12 A C3  1 
HETATM 2111 C C4  . D12 Q 3 .   ? 20.441 31.841 11.490  1.00 53.35 ? 256 D12 A C4  1 
HETATM 2112 C C5  . D12 Q 3 .   ? 19.208 32.013 10.608  1.00 53.49 ? 256 D12 A C5  1 
HETATM 2113 C C6  . D12 Q 3 .   ? 18.346 30.766 10.650  1.00 53.36 ? 256 D12 A C6  1 
HETATM 2114 C C7  . D12 Q 3 .   ? 17.510 30.555 9.717   1.00 52.99 ? 256 D12 A C7  1 
HETATM 2115 C C8  . D12 Q 3 .   ? 16.645 30.532 8.886   1.00 52.34 ? 256 D12 A C8  1 
HETATM 2116 C C9  . D12 Q 3 .   ? 15.932 30.433 7.922   1.00 52.13 ? 256 D12 A C9  1 
HETATM 2117 C C10 . D12 Q 3 .   ? 15.161 30.051 6.972   1.00 51.93 ? 256 D12 A C10 1 
HETATM 2118 C C11 . D12 Q 3 .   ? 14.266 30.856 6.495   1.00 51.79 ? 256 D12 A C11 1 
HETATM 2119 C C12 . D12 Q 3 .   ? 13.347 31.399 5.738   1.00 51.95 ? 256 D12 A C12 1 
HETATM 2120 C C1  . D10 R 4 .   ? 9.319  4.695  -0.813  1.00 47.88 ? 257 D10 A C1  1 
HETATM 2121 C C2  . D10 R 4 .   ? 8.175  4.381  -1.750  1.00 48.16 ? 257 D10 A C2  1 
HETATM 2122 C C3  . D10 R 4 .   ? 8.685  4.373  -3.185  1.00 47.92 ? 257 D10 A C3  1 
HETATM 2123 C C4  . D10 R 4 .   ? 8.113  3.202  -3.974  1.00 47.85 ? 257 D10 A C4  1 
HETATM 2124 C C5  . D10 R 4 .   ? 8.496  3.307  -5.445  1.00 47.83 ? 257 D10 A C5  1 
HETATM 2125 C C6  . D10 R 4 .   ? 8.397  1.957  -6.145  1.00 47.95 ? 257 D10 A C6  1 
HETATM 2126 C C7  . D10 R 4 .   ? 7.746  2.100  -7.515  1.00 47.96 ? 257 D10 A C7  1 
HETATM 2127 C C8  . D10 R 4 .   ? 8.567  1.395  -8.588  1.00 48.48 ? 257 D10 A C8  1 
HETATM 2128 C C9  . D10 R 4 .   ? 7.702  0.447  -9.409  1.00 48.72 ? 257 D10 A C9  1 
HETATM 2129 C C10 . D10 R 4 .   ? 7.615  0.946  -10.833 1.00 48.90 ? 257 D10 A C10 1 
HETATM 2130 O O   . HOH S 9 .   ? 13.941 14.186 -5.655  1.00 14.79 ? 258 HOH A O   1 
HETATM 2131 O O   . HOH S 9 .   ? 19.287 12.804 8.421   1.00 14.79 ? 259 HOH A O   1 
HETATM 2132 O O   . HOH S 9 .   ? 17.811 15.956 -3.931  1.00 16.86 ? 260 HOH A O   1 
HETATM 2133 O O   . HOH S 9 .   ? 11.955 8.880  -16.119 1.00 21.30 ? 261 HOH A O   1 
HETATM 2134 O O   . HOH S 9 .   ? 28.017 12.561 32.659  1.00 18.44 ? 262 HOH A O   1 
HETATM 2135 O O   . HOH S 9 .   ? 17.747 5.663  -15.256 1.00 23.88 ? 263 HOH A O   1 
HETATM 2136 O O   . HOH S 9 .   ? 17.737 18.814 -3.635  1.00 16.59 ? 264 HOH A O   1 
HETATM 2137 O O   . HOH S 9 .   ? 17.244 17.474 -0.159  1.00 19.95 ? 265 HOH A O   1 
HETATM 2138 O O   . HOH S 9 .   ? 23.007 8.727  29.495  1.00 25.79 ? 266 HOH A O   1 
HETATM 2139 O O   . HOH S 9 .   ? 22.235 16.251 34.663  1.00 20.22 ? 267 HOH A O   1 
HETATM 2140 O O   . HOH S 9 .   ? 16.205 6.104  21.846  1.00 22.20 ? 268 HOH A O   1 
HETATM 2141 O O   . HOH S 9 .   ? 31.216 6.100  -21.072 1.00 22.50 ? 269 HOH A O   1 
HETATM 2142 O O   . HOH S 9 .   ? 30.264 16.287 -17.477 1.00 19.61 ? 270 HOH A O   1 
HETATM 2143 O O   . HOH S 9 .   ? 34.887 12.833 -17.395 1.00 24.87 ? 271 HOH A O   1 
HETATM 2144 O O   . HOH S 9 .   ? 29.553 18.798 2.559   1.00 20.73 ? 272 HOH A O   1 
HETATM 2145 O O   . HOH S 9 .   ? 31.242 9.562  -22.905 1.00 23.18 ? 273 HOH A O   1 
HETATM 2146 O O   . HOH S 9 .   ? 19.894 12.675 -12.258 1.00 24.89 ? 274 HOH A O   1 
HETATM 2147 O O   . HOH S 9 .   ? 33.844 13.554 19.993  1.00 23.22 ? 275 HOH A O   1 
HETATM 2148 O O   . HOH S 9 .   ? 14.784 7.647  -16.956 1.00 24.07 ? 276 HOH A O   1 
HETATM 2149 O O   . HOH S 9 .   ? 11.164 13.604 19.758  1.00 24.95 ? 277 HOH A O   1 
HETATM 2150 O O   . HOH S 9 .   ? 29.351 14.120 25.808  1.00 22.52 ? 278 HOH A O   1 
HETATM 2151 O O   . HOH S 9 .   ? 28.651 16.668 -19.778 1.00 24.29 ? 279 HOH A O   1 
HETATM 2152 O O   . HOH S 9 .   ? 11.075 21.083 21.845  1.00 23.21 ? 280 HOH A O   1 
HETATM 2153 O O   . HOH S 9 .   ? 35.000 12.415 13.177  1.00 25.88 ? 281 HOH A O   1 
HETATM 2154 O O   . HOH S 9 .   ? 10.637 23.872 21.207  1.00 27.16 ? 282 HOH A O   1 
HETATM 2155 O O   . HOH S 9 .   ? 18.494 12.414 -9.911  1.00 23.32 ? 283 HOH A O   1 
HETATM 2156 O O   . HOH S 9 .   ? 29.547 7.689  -24.294 1.00 28.60 ? 284 HOH A O   1 
HETATM 2157 O O   . HOH S 9 .   ? 23.186 18.500 24.709  1.00 26.89 ? 285 HOH A O   1 
HETATM 2158 O O   . HOH S 9 .   ? 19.133 22.911 -16.147 1.00 30.45 ? 286 HOH A O   1 
HETATM 2159 O O   . HOH S 9 .   ? 6.489  32.420 16.577  1.00 22.09 ? 287 HOH A O   1 
HETATM 2160 O O   . HOH S 9 .   ? 38.985 18.311 19.496  1.00 28.06 ? 288 HOH A O   1 
HETATM 2161 O O   . HOH S 9 .   ? 12.604 11.426 -16.877 1.00 28.51 ? 289 HOH A O   1 
HETATM 2162 O O   . HOH S 9 .   ? 36.147 12.267 -14.052 1.00 31.33 ? 290 HOH A O   1 
HETATM 2163 O O   . HOH S 9 .   ? 33.853 2.540  -19.163 1.00 24.40 ? 291 HOH A O   1 
HETATM 2164 O O   . HOH S 9 .   ? 7.584  27.801 19.813  1.00 29.98 ? 292 HOH A O   1 
HETATM 2165 O O   . HOH S 9 .   ? 13.184 19.560 -14.088 1.00 24.69 ? 293 HOH A O   1 
HETATM 2166 O O   . HOH S 9 .   ? 29.655 3.414  21.080  1.00 37.26 ? 294 HOH A O   1 
HETATM 2167 O O   . HOH S 9 .   ? 21.047 13.782 -9.307  0.60 19.71 ? 295 HOH A O   1 
HETATM 2168 O O   . HOH S 9 .   ? 11.949 28.996 25.434  1.00 38.15 ? 296 HOH A O   1 
HETATM 2169 O O   . HOH S 9 .   ? 35.531 2.669  17.559  1.00 37.31 ? 297 HOH A O   1 
HETATM 2170 O O   . HOH S 9 .   ? 29.695 19.778 20.143  1.00 37.03 ? 298 HOH A O   1 
HETATM 2171 O O   . HOH S 9 .   ? 22.664 5.589  -16.014 1.00 28.54 ? 299 HOH A O   1 
HETATM 2172 O O   . HOH S 9 .   ? 33.390 9.390  24.453  1.00 39.27 ? 300 HOH A O   1 
HETATM 2173 O O   . HOH S 9 .   ? 16.191 19.692 9.314   1.00 27.43 ? 302 HOH A O   1 
HETATM 2174 O O   . HOH S 9 .   ? 21.304 31.065 20.635  1.00 34.97 ? 303 HOH A O   1 
HETATM 2175 O O   . HOH S 9 .   ? 6.528  8.826  -11.378 1.00 30.07 ? 304 HOH A O   1 
HETATM 2176 O O   . HOH S 9 .   ? 18.867 2.681  -18.977 1.00 48.64 ? 305 HOH A O   1 
HETATM 2177 O O   . HOH S 9 .   ? 31.678 19.886 3.986   1.00 27.88 ? 306 HOH A O   1 
HETATM 2178 O O   . HOH S 9 .   ? 23.007 22.890 -15.883 1.00 33.61 ? 307 HOH A O   1 
HETATM 2179 O O   . HOH S 9 .   ? 18.892 6.891  27.227  1.00 29.70 ? 308 HOH A O   1 
HETATM 2180 O O   . HOH S 9 .   ? 13.755 32.619 18.970  1.00 29.61 ? 309 HOH A O   1 
HETATM 2181 O O   . HOH S 9 .   ? 31.294 10.133 26.924  1.00 37.69 ? 310 HOH A O   1 
HETATM 2182 O O   . HOH S 9 .   ? 32.921 11.179 19.017  1.00 41.90 ? 311 HOH A O   1 
HETATM 2183 O O   . HOH S 9 .   ? 20.663 9.461  -16.630 1.00 36.31 ? 312 HOH A O   1 
HETATM 2184 O O   . HOH S 9 .   ? 19.024 1.275  18.298  1.00 31.96 ? 313 HOH A O   1 
HETATM 2185 O O   . HOH S 9 .   ? 37.788 10.234 -13.452 1.00 37.22 ? 314 HOH A O   1 
HETATM 2186 O O   . HOH S 9 .   ? 19.319 19.386 26.965  1.00 44.82 ? 315 HOH A O   1 
HETATM 2187 O O   . HOH S 9 .   ? 18.762 1.900  4.435   1.00 31.57 ? 316 HOH A O   1 
HETATM 2188 O O   . HOH S 9 .   ? 5.378  15.094 -17.698 1.00 41.69 ? 317 HOH A O   1 
HETATM 2189 O O   . HOH S 9 .   ? 19.933 27.668 27.112  1.00 45.03 ? 318 HOH A O   1 
HETATM 2190 O O   . HOH S 9 .   ? 33.697 9.176  21.639  1.00 35.19 ? 319 HOH A O   1 
HETATM 2191 O O   . HOH S 9 .   ? 13.108 9.614  22.563  1.00 40.51 ? 320 HOH A O   1 
HETATM 2192 O O   . HOH S 9 .   ? 21.266 0.241  -18.224 1.00 41.96 ? 321 HOH A O   1 
HETATM 2193 O O   . HOH S 9 .   ? 27.488 1.987  19.777  1.00 42.55 ? 322 HOH A O   1 
HETATM 2194 O O   . HOH S 9 .   ? 37.909 9.502  13.425  1.00 39.87 ? 323 HOH A O   1 
HETATM 2195 O O   . HOH S 9 .   ? 35.996 20.224 21.639  1.00 33.10 ? 324 HOH A O   1 
HETATM 2196 O O   . HOH S 9 .   ? 32.050 15.196 -24.393 1.00 40.91 ? 325 HOH A O   1 
HETATM 2197 O O   . HOH S 9 .   ? 12.349 35.540 18.120  1.00 39.16 ? 326 HOH A O   1 
HETATM 2198 O O   . HOH S 9 .   ? 23.415 2.390  21.028  1.00 40.53 ? 327 HOH A O   1 
HETATM 2199 O O   . HOH S 9 .   ? 25.415 6.107  30.316  1.00 42.32 ? 328 HOH A O   1 
HETATM 2200 O O   . HOH S 9 .   ? 10.032 19.470 -16.412 1.00 42.14 ? 329 HOH A O   1 
HETATM 2201 O O   . HOH S 9 .   ? 13.981 11.251 24.840  1.00 42.15 ? 330 HOH A O   1 
HETATM 2202 O O   . HOH S 9 .   ? 22.169 5.185  -18.474 1.00 33.03 ? 331 HOH A O   1 
HETATM 2203 O O   . HOH S 9 .   ? 34.314 6.866  16.268  1.00 28.50 ? 332 HOH A O   1 
HETATM 2204 O O   . HOH S 9 .   ? 37.025 13.330 24.297  1.00 51.60 ? 333 HOH A O   1 
HETATM 2205 O O   . HOH S 9 .   ? 37.625 1.625  -19.057 1.00 49.92 ? 334 HOH A O   1 
HETATM 2206 O O   . HOH S 9 .   ? 34.800 9.575  17.170  1.00 36.17 ? 335 HOH A O   1 
HETATM 2207 O O   . HOH S 9 .   ? 34.846 5.175  18.238  1.00 36.13 ? 336 HOH A O   1 
HETATM 2208 O O   . HOH S 9 .   ? 8.025  22.346 17.829  1.00 50.95 ? 337 HOH A O   1 
HETATM 2209 O O   . HOH S 9 .   ? 10.707 20.008 -13.913 1.00 30.29 ? 338 HOH A O   1 
HETATM 2210 O O   . HOH S 9 .   ? 27.519 19.147 -18.502 1.00 35.70 ? 339 HOH A O   1 
HETATM 2211 O O   . HOH S 9 .   ? 22.374 18.355 27.593  1.00 34.46 ? 340 HOH A O   1 
HETATM 2212 O O   . HOH S 9 .   ? 17.762 8.318  -16.497 1.00 36.39 ? 341 HOH A O   1 
HETATM 2213 O O   . HOH S 9 .   ? 36.249 10.965 15.031  1.00 34.00 ? 342 HOH A O   1 
HETATM 2214 O O   . HOH S 9 .   ? 8.657  19.618 15.635  1.00 34.33 ? 343 HOH A O   1 
HETATM 2215 O O   . HOH S 9 .   ? 25.522 2.058  23.164  1.00 45.82 ? 344 HOH A O   1 
HETATM 2216 O O   . HOH S 9 .   ? 26.455 25.627 21.809  1.00 54.17 ? 345 HOH A O   1 
HETATM 2217 O O   . HOH S 9 .   ? 16.744 4.832  24.078  1.00 40.11 ? 346 HOH A O   1 
HETATM 2218 O O   . HOH S 9 .   ? 6.003  10.505 -13.358 1.00 44.56 ? 347 HOH A O   1 
HETATM 2219 O O   . HOH S 9 .   ? 28.926 21.610 21.793  1.00 32.63 ? 348 HOH A O   1 
HETATM 2220 O O   . HOH S 9 .   ? 16.750 0.221  -18.140 1.00 43.98 ? 349 HOH A O   1 
HETATM 2221 O O   . HOH S 9 .   ? 10.149 7.408  -17.326 1.00 39.88 ? 350 HOH A O   1 
HETATM 2222 O O   . HOH S 9 .   ? 6.614  26.484 -21.192 1.00 38.19 ? 351 HOH A O   1 
HETATM 2223 O O   . HOH S 9 .   ? 21.253 19.889 24.161  1.00 46.59 ? 352 HOH A O   1 
HETATM 2224 O O   . HOH S 9 .   ? 16.258 9.454  -18.229 1.00 39.98 ? 353 HOH A O   1 
HETATM 2225 O O   . HOH S 9 .   ? 22.744 22.105 24.135  1.00 43.82 ? 354 HOH A O   1 
HETATM 2226 O O   . HOH S 9 .   ? 34.006 8.396  -22.599 1.00 41.76 ? 355 HOH A O   1 
HETATM 2227 O O   . HOH S 9 .   ? 21.327 20.647 28.308  1.00 53.86 ? 356 HOH A O   1 
HETATM 2228 O O   . HOH S 9 .   ? 20.828 2.004  22.946  1.00 59.36 ? 357 HOH A O   1 
HETATM 2229 O O   . HOH S 9 .   ? 13.328 11.624 20.669  1.00 49.86 ? 358 HOH A O   1 
HETATM 2230 O O   . HOH S 9 .   ? 26.481 21.128 22.669  1.00 42.86 ? 359 HOH A O   1 
HETATM 2231 O O   . HOH S 9 .   ? 35.740 16.062 -20.776 1.00 37.32 ? 360 HOH A O   1 
HETATM 2232 O O   . HOH S 9 .   ? 9.435  32.050 24.509  1.00 48.88 ? 361 HOH A O   1 
HETATM 2233 O O   . HOH S 9 .   ? 9.556  11.852 18.124  1.00 49.37 ? 362 HOH A O   1 
HETATM 2234 O O   . HOH S 9 .   ? 13.474 6.361  22.244  1.00 44.19 ? 363 HOH A O   1 
HETATM 2235 O O   . HOH S 9 .   ? 16.484 15.703 33.597  1.00 51.40 ? 364 HOH A O   1 
HETATM 2236 O O   . HOH S 9 .   ? 33.015 16.442 24.633  1.00 52.36 ? 365 HOH A O   1 
HETATM 2237 O O   . HOH S 9 .   ? 14.553 5.447  -18.371 1.00 35.65 ? 366 HOH A O   1 
HETATM 2238 O O   . HOH S 9 .   ? 11.512 5.353  19.801  1.00 57.19 ? 367 HOH A O   1 
HETATM 2239 O O   . HOH S 9 .   ? 10.630 9.443  18.719  1.00 58.02 ? 368 HOH A O   1 
HETATM 2240 O O   . HOH S 9 .   ? 16.296 4.471  19.661  1.00 32.97 ? 369 HOH A O   1 
HETATM 2241 O O   . HOH S 9 .   ? 8.235  12.308 12.959  1.00 45.78 ? 370 HOH A O   1 
HETATM 2242 O O   . HOH S 9 .   ? 15.483 20.940 -13.797 1.00 37.57 ? 371 HOH A O   1 
HETATM 2243 O O   . HOH S 9 .   ? 24.125 4.643  -20.508 1.00 58.44 ? 372 HOH A O   1 
HETATM 2244 O O   . HOH S 9 .   ? 9.236  5.201  -16.011 1.00 51.94 ? 373 HOH A O   1 
HETATM 2245 O O   . HOH S 9 .   ? 14.949 -0.633 -16.287 1.00 50.24 ? 374 HOH A O   1 
HETATM 2246 O O   . HOH S 9 .   ? 11.090 4.907  -18.052 1.00 46.84 ? 375 HOH A O   1 
HETATM 2247 O O   . HOH S 9 .   ? 14.533 11.423 -18.771 1.00 45.39 ? 376 HOH A O   1 
HETATM 2248 O O   . HOH S 9 .   ? 23.126 19.754 -21.098 1.00 45.32 ? 377 HOH A O   1 
HETATM 2249 O O   . HOH S 9 .   ? 19.332 7.786  -20.650 1.00 53.15 ? 378 HOH A O   1 
HETATM 2250 O O   . HOH S 9 .   ? 16.136 13.148 -21.204 1.00 53.07 ? 379 HOH A O   1 
HETATM 2251 O O   . HOH S 9 .   ? 21.270 25.125 -14.718 1.00 36.90 ? 380 HOH A O   1 
HETATM 2252 O O   . HOH S 9 .   ? 18.861 31.529 -16.925 1.00 35.28 ? 381 HOH A O   1 
HETATM 2253 O O   . HOH S 9 .   ? 22.477 7.594  32.008  0.50 36.54 ? 382 HOH A O   1 
HETATM 2254 O O   . HOH S 9 .   ? 33.149 4.595  -21.335 1.00 41.53 ? 383 HOH A O   1 
HETATM 2255 O O   . HOH S 9 .   ? 31.872 11.672 -24.707 1.00 40.59 ? 384 HOH A O   1 
HETATM 2256 O O   . HOH S 9 .   ? 25.225 0.973  19.945  1.00 51.53 ? 385 HOH A O   1 
HETATM 2257 O O   . HOH S 9 .   ? 21.545 6.788  28.427  1.00 42.61 ? 386 HOH A O   1 
HETATM 2258 O O   . HOH S 9 .   ? 0.742  22.931 14.948  1.00 59.63 ? 387 HOH A O   1 
HETATM 2259 O O   . HOH S 9 .   ? 37.799 14.417 -12.723 1.00 46.35 ? 388 HOH A O   1 
HETATM 2260 O O   . HOH S 9 .   ? 30.961 4.024  -22.812 1.00 68.55 ? 389 HOH A O   1 
HETATM 2261 O O   . HOH S 9 .   ? 30.250 10.540 32.425  1.00 48.05 ? 390 HOH A O   1 
HETATM 2262 O O   . HOH S 9 .   ? 8.817  24.931 22.837  1.00 46.01 ? 391 HOH A O   1 
HETATM 2263 O O   . HOH S 9 .   ? 36.168 10.839 -17.669 1.00 48.70 ? 392 HOH A O   1 
HETATM 2264 O O   . HOH S 9 .   ? 24.446 23.804 22.404  1.00 53.83 ? 393 HOH A O   1 
HETATM 2265 O O   . HOH S 9 .   ? 30.834 1.721  -21.383 1.00 52.50 ? 394 HOH A O   1 
HETATM 2266 O O   . HOH S 9 .   ? 5.183  28.589 18.648  1.00 47.47 ? 395 HOH A O   1 
HETATM 2267 O O   . HOH S 9 .   ? 9.603  14.095 21.984  1.00 45.04 ? 396 HOH A O   1 
HETATM 2268 O O   . HOH S 9 .   ? 28.899 3.080  23.460  1.00 52.73 ? 397 HOH A O   1 
HETATM 2269 O O   . HOH S 9 .   ? 35.750 10.329 -22.286 1.00 48.86 ? 398 HOH A O   1 
HETATM 2270 O O   . HOH S 9 .   ? 38.189 16.456 -11.046 1.00 47.76 ? 399 HOH A O   1 
HETATM 2271 O O   . HOH S 9 .   ? 21.418 27.147 -16.545 1.00 54.02 ? 400 HOH A O   1 
HETATM 2272 O O   . HOH S 9 .   ? 19.564 32.398 -14.516 1.00 57.73 ? 404 HOH A O   1 
HETATM 2273 O O   . HOH S 9 .   ? 7.378  25.183 20.389  1.00 48.22 ? 407 HOH A O   1 
HETATM 2274 O O   . HOH S 9 .   ? 14.580 8.999  28.149  1.00 55.79 ? 408 HOH A O   1 
HETATM 2275 O O   . HOH S 9 .   ? -0.605 22.817 12.640  1.00 71.40 ? 410 HOH A O   1 
HETATM 2276 O O   . HOH S 9 .   ? 1.093  25.382 15.439  1.00 48.02 ? 412 HOH A O   1 
HETATM 2277 O O   . HOH S 9 .   ? 27.435 9.955  -26.701 1.00 57.65 ? 413 HOH A O   1 
HETATM 2278 O O   . HOH S 9 .   ? 22.662 13.238 -9.534  0.40 13.91 ? 414 HOH A O   1 
HETATM 2279 O O   . HOH S 9 .   ? 1.854  17.092 -17.317 1.00 38.95 ? 415 HOH A O   1 
HETATM 2280 O O   . HOH S 9 .   ? 39.443 13.337 14.747  1.00 55.77 ? 416 HOH A O   1 
HETATM 2281 O O   . HOH S 9 .   ? 3.031  28.146 17.397  1.00 49.42 ? 417 HOH A O   1 
HETATM 2282 O O   . HOH S 9 .   ? 15.165 2.537  -16.654 1.00 44.71 ? 418 HOH A O   1 
HETATM 2283 O O   . HOH S 9 .   ? 16.911 4.089  -17.449 1.00 41.50 ? 419 HOH A 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   GLN 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   GLN 3   3   ?   ?   ?   A . n 
A 1 4   ILE 4   4   ?   ?   ?   A . n 
A 1 5   THR 5   5   ?   ?   ?   A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   ARG 7   7   7   ARG ARG A . n 
A 1 8   PRO 8   8   8   PRO PRO A . n 
A 1 9   GLU 9   9   9   GLU GLU A . n 
A 1 10  TRP 10  10  10  TRP TRP A . n 
A 1 11  ILE 11  11  11  ILE ILE A . n 
A 1 12  TRP 12  12  12  TRP TRP A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  ALA 14  14  14  ALA ALA A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  THR 17  17  17  THR THR A . n 
A 1 18  ALA 18  18  18  ALA ALA A . n 
A 1 19  LEU 19  19  19  LEU LEU A . n 
A 1 20  MET 20  20  20  MET MET A . n 
A 1 21  GLY 21  21  21  GLY GLY A . n 
A 1 22  LEU 22  22  22  LEU LEU A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  TYR 26  26  26  TYR TYR A . n 
A 1 27  PHE 27  27  27  PHE PHE A . n 
A 1 28  LEU 28  28  28  LEU LEU A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  GLY 31  31  31  GLY GLY A . n 
A 1 32  MET 32  32  32  MET MET A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  SER 35  35  35  SER SER A . n 
A 1 36  ASP 36  36  36  ASP ASP A . n 
A 1 37  PRO 37  37  37  PRO PRO A . n 
A 1 38  ASP 38  38  38  ASP ASP A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  LYS 40  40  40  LYS LYS A . n 
A 1 41  LYS 41  41  41  LYS LYS A . n 
A 1 42  PHE 42  42  42  PHE PHE A . n 
A 1 43  TYR 43  43  43  TYR TYR A . n 
A 1 44  ALA 44  44  44  ALA ALA A . n 
A 1 45  ILE 45  45  45  ILE ILE A . n 
A 1 46  THR 46  46  46  THR THR A . n 
A 1 47  THR 47  47  47  THR THR A . n 
A 1 48  LEU 48  48  48  LEU LEU A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  PRO 50  50  50  PRO PRO A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  ILE 52  52  52  ILE ILE A . n 
A 1 53  ALA 53  53  53  ALA ALA A . n 
A 1 54  PHE 54  54  54  PHE PHE A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  MET 56  56  56  MET MET A . n 
A 1 57  TYR 57  57  57  TYR TYR A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  MET 60  60  60  MET MET A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  LEU 62  62  62  LEU LEU A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  TYR 64  64  64  TYR TYR A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  THR 67  67  67  THR THR A . n 
A 1 68  MET 68  68  68  MET MET A . n 
A 1 69  VAL 69  69  69  VAL VAL A . n 
A 1 70  PRO 70  70  70  PRO PRO A . n 
A 1 71  PHE 71  71  71  PHE PHE A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  GLU 74  74  74  GLU GLU A . n 
A 1 75  GLN 75  75  75  GLN GLN A . n 
A 1 76  ASN 76  76  76  ASN ASN A . n 
A 1 77  PRO 77  77  77  PRO PRO A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  TYR 79  79  79  TYR TYR A . n 
A 1 80  TRP 80  80  80  TRP TRP A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  ARG 82  82  82  ARG ARG A . n 
A 1 83  TYR 83  83  83  TYR TYR A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  TRP 86  86  86  TRP TRP A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  PHE 88  88  88  PHE PHE A . n 
A 1 89  THR 89  89  89  THR THR A . n 
A 1 90  THR 90  90  90  THR THR A . n 
A 1 91  PRO 91  91  91  PRO PRO A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  LEU 94  94  94  LEU LEU A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  ALA 98  98  98  ALA ALA A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 VAL 101 101 101 VAL VAL A . n 
A 1 102 ASP 102 102 102 ASP ASP A . n 
A 1 103 ALA 103 103 103 ALA ALA A . n 
A 1 104 ASP 104 104 104 ASP ASP A . n 
A 1 105 GLN 105 105 105 GLN GLN A . n 
A 1 106 GLY 106 106 106 GLY GLY A . n 
A 1 107 THR 107 107 107 THR THR A . n 
A 1 108 ILE 108 108 108 ILE ILE A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 ALA 111 111 111 ALA ALA A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 GLY 113 113 113 GLY GLY A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 ASP 115 115 115 ASP ASP A . n 
A 1 116 GLY 116 116 116 GLY GLY A . n 
A 1 117 ILE 117 117 117 ILE ILE A . n 
A 1 118 MET 118 118 118 MET MET A . n 
A 1 119 ILE 119 119 119 ILE ILE A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 THR 121 121 121 THR THR A . n 
A 1 122 GLY 122 122 122 GLY GLY A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 VAL 124 124 124 VAL VAL A . n 
A 1 125 GLY 125 125 125 GLY GLY A . n 
A 1 126 ALA 126 126 126 ALA ALA A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 THR 128 128 128 THR THR A . n 
A 1 129 LYS 129 129 129 LYS LYS A . n 
A 1 130 VAL 130 130 130 VAL VAL A . n 
A 1 131 TYR 131 131 131 TYR TYR A . n 
A 1 132 SER 132 132 132 SER SER A . n 
A 1 133 TYR 133 133 133 TYR TYR A . n 
A 1 134 ARG 134 134 134 ARG ARG A . n 
A 1 135 PHE 135 135 135 PHE PHE A . n 
A 1 136 VAL 136 136 136 VAL VAL A . n 
A 1 137 TRP 137 137 137 TRP TRP A . n 
A 1 138 TRP 138 138 138 TRP TRP A . n 
A 1 139 ALA 139 139 139 ALA ALA A . n 
A 1 140 ILE 140 140 140 ILE ILE A . n 
A 1 141 SER 141 141 141 SER SER A . n 
A 1 142 THR 142 142 142 THR THR A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 MET 145 145 145 MET MET A . n 
A 1 146 LEU 146 146 146 LEU LEU A . n 
A 1 147 TYR 147 147 147 TYR TYR A . n 
A 1 148 ILE 148 148 148 ILE ILE A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 TYR 150 150 150 TYR TYR A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 PHE 153 153 153 PHE PHE A . n 
A 1 154 PHE 154 154 154 PHE PHE A . n 
A 1 155 GLY 155 155 155 GLY GLY A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 THR 157 157 157 THR THR A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 LYS 159 159 159 LYS LYS A . n 
A 1 160 ALA 160 160 160 ALA ALA A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 SER 162 162 162 SER SER A . n 
A 1 163 MET 163 163 163 MET MET A . n 
A 1 164 ARG 164 164 164 ARG ARG A . n 
A 1 165 PRO 165 165 165 PRO PRO A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 VAL 167 167 167 VAL VAL A . n 
A 1 168 ALA 168 168 168 ALA ALA A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 THR 170 170 170 THR THR A . n 
A 1 171 PHE 171 171 171 PHE PHE A . n 
A 1 172 LYS 172 172 172 LYS LYS A . n 
A 1 173 VAL 173 173 173 VAL VAL A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 ARG 175 175 175 ARG ARG A . n 
A 1 176 ASN 176 176 176 ASN ASN A . n 
A 1 177 VAL 177 177 177 VAL VAL A . n 
A 1 178 THR 178 178 178 THR THR A . n 
A 1 179 VAL 179 179 179 VAL VAL A . n 
A 1 180 VAL 180 180 180 VAL VAL A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 TRP 182 182 182 TRP TRP A . n 
A 1 183 SER 183 183 183 SER SER A . n 
A 1 184 ALA 184 184 184 ALA ALA A . n 
A 1 185 TYR 185 185 185 TYR TYR A . n 
A 1 186 PRO 186 186 186 PRO PRO A . n 
A 1 187 VAL 187 187 187 VAL VAL A . n 
A 1 188 VAL 188 188 188 VAL VAL A . n 
A 1 189 TRP 189 189 189 TRP TRP A . n 
A 1 190 LEU 190 190 190 LEU LEU A . n 
A 1 191 ILE 191 191 191 ILE ILE A . n 
A 1 192 GLY 192 192 192 GLY GLY A . n 
A 1 193 SER 193 193 193 SER SER A . n 
A 1 194 GLU 194 194 194 GLU GLU A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 ALA 196 196 196 ALA ALA A . n 
A 1 197 GLY 197 197 197 GLY GLY A . n 
A 1 198 ILE 198 198 198 ILE ILE A . n 
A 1 199 VAL 199 199 199 VAL VAL A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 LEU 201 201 201 LEU LEU A . n 
A 1 202 ASN 202 202 202 ASN ASN A . n 
A 1 203 ILE 203 203 203 ILE ILE A . n 
A 1 204 GLU 204 204 204 GLU GLU A . n 
A 1 205 THR 205 205 205 THR THR A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 PHE 208 208 208 PHE PHE A . n 
A 1 209 MET 209 209 209 MET MET A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 ASP 212 212 212 ASP ASP A . n 
A 1 213 VAL 213 213 213 VAL VAL A . n 
A 1 214 SER 214 214 214 SER SER A . n 
A 1 215 ALA 215 215 215 ALA ALA A . n 
A 1 216 LYS 216 216 216 LYS LYS A . n 
A 1 217 VAL 217 217 217 VAL VAL A . n 
A 1 218 GLY 218 218 218 GLY GLY A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 GLY 220 220 220 GLY GLY A . n 
A 1 221 LEU 221 221 221 LEU LEU A . n 
A 1 222 ILE 222 222 222 ILE ILE A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 LEU 224 224 224 LEU LEU A . n 
A 1 225 ARG 225 225 225 ARG ARG A . n 
A 1 226 SER 226 226 226 SER SER A . n 
A 1 227 ARG 227 227 227 ARG ARG A . n 
A 1 228 ALA 228 228 228 ALA ALA A . n 
A 1 229 ILE 229 229 229 ILE ILE A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 GLY 231 231 231 GLY GLY A . n 
A 1 232 GLU 232 232 ?   ?   ?   A . n 
A 1 233 ALA 233 233 ?   ?   ?   A . n 
A 1 234 GLU 234 234 ?   ?   ?   A . n 
A 1 235 ALA 235 235 ?   ?   ?   A . n 
A 1 236 PRO 236 236 ?   ?   ?   A . n 
A 1 237 GLU 237 237 ?   ?   ?   A . n 
A 1 238 PRO 238 238 ?   ?   ?   A . n 
A 1 239 SER 239 239 ?   ?   ?   A . n 
A 1 240 ALA 240 240 ?   ?   ?   A . n 
A 1 241 GLY 241 241 ?   ?   ?   A . n 
A 1 242 ASP 242 242 ?   ?   ?   A . n 
A 1 243 GLY 243 243 ?   ?   ?   A . n 
A 1 244 ALA 244 244 ?   ?   ?   A . n 
A 1 245 ALA 245 245 ?   ?   ?   A . n 
A 1 246 ALA 246 246 ?   ?   ?   A . n 
A 1 247 THR 247 247 ?   ?   ?   A . n 
A 1 248 SER 248 248 ?   ?   ?   A . n 
A 1 249 ASP 249 249 ?   ?   ?   A . 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 
B 2 RET 1   301 301 RET RET A . 
C 3 D12 1   402 402 D12 D12 A . 
D 3 D12 1   403 403 D12 D12 A . 
E 3 D12 1   405 405 D12 D12 A . 
F 4 D10 1   406 406 D10 D10 A . 
G 4 D10 1   409 409 D10 D10 A . 
H 5 R16 1   411 411 R16 R16 A . 
I 6 CPS 1   501 501 CPS CPS A . 
J 4 D10 1   250 250 D10 D10 A . 
K 3 D12 1   251 251 D12 D12 A . 
L 7 HP6 1   401 401 HP6 HP6 A . 
M 3 D12 1   252 252 D12 D12 A . 
N 8 DD9 1   253 253 DD9 DD9 A . 
O 3 D12 1   254 254 D12 D12 A . 
P 3 D12 1   255 255 D12 D12 A . 
Q 3 D12 1   256 256 D12 D12 A . 
R 4 D10 1   257 257 D10 D10 A . 
S 9 HOH 1   258 258 HOH HOH A . 
S 9 HOH 2   259 259 HOH HOH A . 
S 9 HOH 3   260 260 HOH HOH A . 
S 9 HOH 4   261 261 HOH HOH A . 
S 9 HOH 5   262 262 HOH HOH A . 
S 9 HOH 6   263 263 HOH HOH A . 
S 9 HOH 7   264 264 HOH HOH A . 
S 9 HOH 8   265 265 HOH HOH A . 
S 9 HOH 9   266 266 HOH HOH A . 
S 9 HOH 10  267 267 HOH HOH A . 
S 9 HOH 11  268 268 HOH HOH A . 
S 9 HOH 12  269 269 HOH HOH A . 
S 9 HOH 13  270 270 HOH HOH A . 
S 9 HOH 14  271 271 HOH HOH A . 
S 9 HOH 15  272 272 HOH HOH A . 
S 9 HOH 16  273 273 HOH HOH A . 
S 9 HOH 17  274 274 HOH HOH A . 
S 9 HOH 18  275 275 HOH HOH A . 
S 9 HOH 19  276 276 HOH HOH A . 
S 9 HOH 20  277 277 HOH HOH A . 
S 9 HOH 21  278 278 HOH HOH A . 
S 9 HOH 22  279 279 HOH HOH A . 
S 9 HOH 23  280 280 HOH HOH A . 
S 9 HOH 24  281 281 HOH HOH A . 
S 9 HOH 25  282 282 HOH HOH A . 
S 9 HOH 26  283 283 HOH HOH A . 
S 9 HOH 27  284 284 HOH HOH A . 
S 9 HOH 28  285 285 HOH HOH A . 
S 9 HOH 29  286 286 HOH HOH A . 
S 9 HOH 30  287 287 HOH HOH A . 
S 9 HOH 31  288 288 HOH HOH A . 
S 9 HOH 32  289 289 HOH HOH A . 
S 9 HOH 33  290 290 HOH HOH A . 
S 9 HOH 34  291 291 HOH HOH A . 
S 9 HOH 35  292 292 HOH HOH A . 
S 9 HOH 36  293 293 HOH HOH A . 
S 9 HOH 37  294 294 HOH HOH A . 
S 9 HOH 38  295 295 HOH HOH A . 
S 9 HOH 39  296 296 HOH HOH A . 
S 9 HOH 40  297 297 HOH HOH A . 
S 9 HOH 41  298 298 HOH HOH A . 
S 9 HOH 42  299 299 HOH HOH A . 
S 9 HOH 43  300 300 HOH HOH A . 
S 9 HOH 44  302 302 HOH HOH A . 
S 9 HOH 45  303 303 HOH HOH A . 
S 9 HOH 46  304 304 HOH HOH A . 
S 9 HOH 47  305 305 HOH HOH A . 
S 9 HOH 48  306 306 HOH HOH A . 
S 9 HOH 49  307 307 HOH HOH A . 
S 9 HOH 50  308 308 HOH HOH A . 
S 9 HOH 51  309 309 HOH HOH A . 
S 9 HOH 52  310 310 HOH HOH A . 
S 9 HOH 53  311 311 HOH HOH A . 
S 9 HOH 54  312 312 HOH HOH A . 
S 9 HOH 55  313 313 HOH HOH A . 
S 9 HOH 56  314 314 HOH HOH A . 
S 9 HOH 57  315 315 HOH HOH A . 
S 9 HOH 58  316 316 HOH HOH A . 
S 9 HOH 59  317 317 HOH HOH A . 
S 9 HOH 60  318 318 HOH HOH A . 
S 9 HOH 61  319 319 HOH HOH A . 
S 9 HOH 62  320 320 HOH HOH A . 
S 9 HOH 63  321 321 HOH HOH A . 
S 9 HOH 64  322 322 HOH HOH A . 
S 9 HOH 65  323 323 HOH HOH A . 
S 9 HOH 66  324 324 HOH HOH A . 
S 9 HOH 67  325 325 HOH HOH A . 
S 9 HOH 68  326 326 HOH HOH A . 
S 9 HOH 69  327 327 HOH HOH A . 
S 9 HOH 70  328 328 HOH HOH A . 
S 9 HOH 71  329 329 HOH HOH A . 
S 9 HOH 72  330 330 HOH HOH A . 
S 9 HOH 73  331 331 HOH HOH A . 
S 9 HOH 74  332 332 HOH HOH A . 
S 9 HOH 75  333 333 HOH HOH A . 
S 9 HOH 76  334 334 HOH HOH A . 
S 9 HOH 77  335 335 HOH HOH A . 
S 9 HOH 78  336 336 HOH HOH A . 
S 9 HOH 79  337 337 HOH HOH A . 
S 9 HOH 80  338 338 HOH HOH A . 
S 9 HOH 81  339 339 HOH HOH A . 
S 9 HOH 82  340 340 HOH HOH A . 
S 9 HOH 83  341 341 HOH HOH A . 
S 9 HOH 84  342 342 HOH HOH A . 
S 9 HOH 85  343 343 HOH HOH A . 
S 9 HOH 86  344 344 HOH HOH A . 
S 9 HOH 87  345 345 HOH HOH A . 
S 9 HOH 88  346 346 HOH HOH A . 
S 9 HOH 89  347 347 HOH HOH A . 
S 9 HOH 90  348 348 HOH HOH A . 
S 9 HOH 91  349 349 HOH HOH A . 
S 9 HOH 92  350 350 HOH HOH A . 
S 9 HOH 93  351 351 HOH HOH A . 
S 9 HOH 94  352 352 HOH HOH A . 
S 9 HOH 95  353 353 HOH HOH A . 
S 9 HOH 96  354 354 HOH HOH A . 
S 9 HOH 97  355 355 HOH HOH A . 
S 9 HOH 98  356 356 HOH HOH A . 
S 9 HOH 99  357 357 HOH HOH A . 
S 9 HOH 100 358 358 HOH HOH A . 
S 9 HOH 101 359 359 HOH HOH A . 
S 9 HOH 102 360 360 HOH HOH A . 
S 9 HOH 103 361 361 HOH HOH A . 
S 9 HOH 104 362 362 HOH HOH A . 
S 9 HOH 105 363 363 HOH HOH A . 
S 9 HOH 106 364 364 HOH HOH A . 
S 9 HOH 107 365 365 HOH HOH A . 
S 9 HOH 108 366 366 HOH HOH A . 
S 9 HOH 109 367 367 HOH HOH A . 
S 9 HOH 110 368 368 HOH HOH A . 
S 9 HOH 111 369 369 HOH HOH A . 
S 9 HOH 112 370 370 HOH HOH A . 
S 9 HOH 113 371 371 HOH HOH A . 
S 9 HOH 114 372 372 HOH HOH A . 
S 9 HOH 115 373 373 HOH HOH A . 
S 9 HOH 116 374 374 HOH HOH A . 
S 9 HOH 117 375 375 HOH HOH A . 
S 9 HOH 118 376 376 HOH HOH A . 
S 9 HOH 119 377 377 HOH HOH A . 
S 9 HOH 120 378 378 HOH HOH A . 
S 9 HOH 121 379 379 HOH HOH A . 
S 9 HOH 122 380 380 HOH HOH A . 
S 9 HOH 123 381 381 HOH HOH A . 
S 9 HOH 124 382 382 HOH HOH A . 
S 9 HOH 125 383 383 HOH HOH A . 
S 9 HOH 126 384 384 HOH HOH A . 
S 9 HOH 127 385 385 HOH HOH A . 
S 9 HOH 128 386 386 HOH HOH A . 
S 9 HOH 129 387 387 HOH HOH A . 
S 9 HOH 130 388 388 HOH HOH A . 
S 9 HOH 131 389 389 HOH HOH A . 
S 9 HOH 132 390 390 HOH HOH A . 
S 9 HOH 133 391 391 HOH HOH A . 
S 9 HOH 134 392 392 HOH HOH A . 
S 9 HOH 135 393 393 HOH HOH A . 
S 9 HOH 136 394 394 HOH HOH A . 
S 9 HOH 137 395 395 HOH HOH A . 
S 9 HOH 138 396 396 HOH HOH A . 
S 9 HOH 139 397 397 HOH HOH A . 
S 9 HOH 140 398 398 HOH HOH A . 
S 9 HOH 141 399 399 HOH HOH A . 
S 9 HOH 142 400 400 HOH HOH A . 
S 9 HOH 143 404 404 HOH HOH A . 
S 9 HOH 144 407 407 HOH HOH A . 
S 9 HOH 145 408 408 HOH HOH A . 
S 9 HOH 146 410 410 HOH HOH A . 
S 9 HOH 147 412 412 HOH HOH A . 
S 9 HOH 148 413 413 HOH HOH A . 
S 9 HOH 149 414 414 HOH HOH A . 
S 9 HOH 150 415 415 HOH HOH A . 
S 9 HOH 151 416 416 HOH HOH A . 
S 9 HOH 152 417 417 HOH HOH A . 
S 9 HOH 153 418 418 HOH HOH A . 
S 9 HOH 154 419 419 HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_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,J,K,L,M,N,O,P,Q,R,S 
# 
_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 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     382 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   S 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 2009-09-22 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2017-11-01 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Refinement description'    
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    3 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            software 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 DENZO       .        ?               package 'Zbyszek Otwinowski' hkl@hkl-xray.com      'data reduction'  
http://www.hkl-xray.com/                     ?          ? 
2 SCALEPACK   .        ?               package 'Zbyszek Otwinowski' hkl@hkl-xray.com      'data scaling'    
http://www.hkl-xray.com/                     ?          ? 
3 REFMAC      5.2.0019 ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 
4 PDB_EXTRACT 3.005    'June 11, 2008' package PDB                  help@deposit.rcsb.org 'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   NZ 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   LYS 
_pdbx_validate_close_contact.auth_seq_id_1    216 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   C14 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   RET 
_pdbx_validate_close_contact.auth_seq_id_2    301 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.19 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    PHE 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     154 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -95.05 
_pdbx_validate_torsion.psi             -60.93 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLY 231 ? O   ? A GLY 231 O   
2  1 N 1 A CPS 501 ? C25 ? I CPS 1   C25 
3  1 N 1 A CPS 501 ? C26 ? I CPS 1   C26 
4  1 N 1 A CPS 501 ? C27 ? I CPS 1   C27 
5  1 N 1 A CPS 501 ? C28 ? I CPS 1   C28 
6  1 N 1 A CPS 501 ? C29 ? I CPS 1   C29 
7  1 N 1 A CPS 501 ? C30 ? I CPS 1   C30 
8  1 N 1 A CPS 501 ? C31 ? I CPS 1   C31 
9  1 N 1 A CPS 501 ? C32 ? I CPS 1   C32 
10 1 N 1 A CPS 501 ? N1  ? I CPS 1   N1  
11 1 N 1 A CPS 501 ? N2  ? I CPS 1   N2  
12 1 N 1 A CPS 501 ? O1  ? I CPS 1   O1  
13 1 N 1 A CPS 501 ? O2S ? I CPS 1   O2S 
14 1 N 1 A CPS 501 ? O3S ? I CPS 1   O3S 
15 1 N 1 A CPS 501 ? O1S ? I CPS 1   O1S 
16 1 N 1 A CPS 501 ? S   ? I CPS 1   S   
# 
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 GLN 1   ? A GLN 1   
2  1 Y 1 A ALA 2   ? A ALA 2   
3  1 Y 1 A GLN 3   ? A GLN 3   
4  1 Y 1 A ILE 4   ? A ILE 4   
5  1 Y 1 A THR 5   ? A THR 5   
6  1 Y 1 A GLU 232 ? A GLU 232 
7  1 Y 1 A ALA 233 ? A ALA 233 
8  1 Y 1 A GLU 234 ? A GLU 234 
9  1 Y 1 A ALA 235 ? A ALA 235 
10 1 Y 1 A PRO 236 ? A PRO 236 
11 1 Y 1 A GLU 237 ? A GLU 237 
12 1 Y 1 A PRO 238 ? A PRO 238 
13 1 Y 1 A SER 239 ? A SER 239 
14 1 Y 1 A ALA 240 ? A ALA 240 
15 1 Y 1 A GLY 241 ? A GLY 241 
16 1 Y 1 A ASP 242 ? A ASP 242 
17 1 Y 1 A GLY 243 ? A GLY 243 
18 1 Y 1 A ALA 244 ? A ALA 244 
19 1 Y 1 A ALA 245 ? A ALA 245 
20 1 Y 1 A ALA 246 ? A ALA 246 
21 1 Y 1 A THR 247 ? A THR 247 
22 1 Y 1 A SER 248 ? A SER 248 
23 1 Y 1 A ASP 249 ? A ASP 249 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 RETINAL                                                     RET 
3 DODECANE                                                    D12 
4 DECANE                                                      D10 
5 HEXADECANE                                                  R16 
6 '3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE' CPS 
7 HEPTANE                                                     HP6 
8 nonane                                                      DD9 
9 water                                                       HOH 
# 



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.