HEADER MEMBRANE PROTEIN 17-APR-22 7ZLY TITLE CRYSTAL STRUCTURE OF HUMAN GPCR NIACIN RECEPTOR (HCA2) EXPRESSED FROM TITLE 2 SPODOPTERA FRUGIPERDA COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYDROXYCARBOXYLIC ACID RECEPTOR 2,SOLUBLE CYTOCHROME B562; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: G-PROTEIN COUPLED RECEPTOR 109A,G-PROTEIN COUPLED RECEPTOR COMPND 5 HM74A,NIACIN RECEPTOR 1,NICOTINIC ACID RECEPTOR,CYTOCHROME B-562; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 562; SOURCE 5 GENE: HCAR2, GPR109A, HCA2, HM74A, NIACR1, CYBC; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS NIACIN RECEPTOR, HYDROXYCARBOXYLIC ACID RECEPTOR 2, HCA2, GPCR, KEYWDS 2 MEMBRANE PROTEIN STRUCTURE, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR Y.YANG,H.J.KANG,R.G.GAO,J.J.WANG,J.F.FIBERTO,L.J.WU,J.H.TONG,G.W.HAN, AUTHOR 2 L.QU,Y.R.WU,R.PILESKI,X.M.LI,X.C.ZHANG,S.W.ZHAO,T.KENAKIN,Q.WANG, AUTHOR 3 R.C.STEVENS,W.PENG,B.L.ROTH,Z.H.RAO,Z.J.LIU REVDAT 1 12-APR-23 7ZLY 0 JRNL AUTH Y.YANG,H.J.KANG,R.GAO,J.WANG,G.W.HAN,J.F.DIBERTO,L.WU, JRNL AUTH 2 J.TONG,L.QU,Y.WU,R.PILESKI,X.LI,X.C.ZHANG,S.ZHAO,T.KENAKIN, JRNL AUTH 3 Q.WANG,R.C.STEVENS,W.PENG,B.L.ROTH,Z.RAO,Z.J.LIU JRNL TITL STRUCTURAL INSIGHTS INTO THE HUMAN NIACIN RECEPTOR HCA2-G I JRNL TITL 2 SIGNALLING COMPLEX. JRNL REF NAT COMMUN V. 14 1692 2023 JRNL REFN ESSN 2041-1723 JRNL PMID 36973264 JRNL DOI 10.1038/S41467-023-37177-6 REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.97 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8 REMARK 3 NUMBER OF REFLECTIONS : 25559 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.250 REMARK 3 FREE R VALUE : 0.280 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3088 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 94 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : NULL ; NULL ; NULL REMARK 3 BOND ANGLES : NULL ; NULL ; NULL REMARK 3 TORSION ANGLES : NULL ; NULL ; NULL REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL REMARK 3 GENERAL PLANES : NULL ; NULL ; NULL REMARK 3 ISOTROPIC THERMAL FACTORS : NULL ; NULL ; NULL REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : NULL ; NULL ; NULL REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : NULL ; NULL ; NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : NULL REMARK 3 BOND ANGLES (DEGREES) : NULL REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL REMARK 3 OTHER TORSION ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 7ZLY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JUN-22. REMARK 100 THE DEPOSITION ID IS D_1292122447. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 27-NOV-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SPRING-8 REMARK 200 BEAMLINE : BL41XU REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25559 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700 REMARK 200 RESOLUTION RANGE LOW (A) : 47.972 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8 REMARK 200 DATA REDUNDANCY : 5.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.1800 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.75 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 4PXZ REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.37 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM PH5.4 SODIUM CITRATE, 60MM REMARK 280 AMMONIUM CITRATE, 36% PEG400, AND 3% ADDITIVE 80 (40% PPG), REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,-Y,-Z+1/2 REMARK 290 4555 -X+1/2,-Y,Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 40.54000 REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.15500 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 40.54000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 43.15500 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2450 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19870 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 15.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 ASN A 2 REMARK 465 ARG A 3 REMARK 465 HIS A 4 REMARK 465 HIS A 5 REMARK 465 LEU A 6 REMARK 465 GLN A 7 REMARK 465 ASP A 8 REMARK 465 HIS A 9 REMARK 465 PHE A 10 REMARK 465 GLY A 172 REMARK 465 GLY A 173 REMARK 465 PRO A 265 REMARK 465 LYS A 266 REMARK 465 LEU A 267 REMARK 465 GLU A 268 REMARK 465 ASP A 269 REMARK 465 LYS A 270 REMARK 465 SER A 271 REMARK 465 PRO A 272 REMARK 465 ASP A 273 REMARK 465 SER A 274 REMARK 465 PRO A 275 REMARK 465 GLU A 276 REMARK 465 LEU A 419 REMARK 465 GLN A 420 REMARK 465 ARG A 421 REMARK 465 LYS A 422 REMARK 465 MET A 423 REMARK 465 THR A 424 REMARK 465 GLY A 425 REMARK 465 GLU A 426 REMARK 465 PRO A 427 REMARK 465 ASP A 428 REMARK 465 ASN A 429 REMARK 465 ASN A 430 REMARK 465 ARG A 431 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ILE A 13 CG1 CG2 CD1 REMARK 470 ASP A 14 CG OD1 OD2 REMARK 470 LYS A 15 CG CD CE NZ REMARK 470 LYS A 16 CG CD CE NZ REMARK 470 ASN A 17 CG OD1 ND2 REMARK 470 LYS A 28 CG CD CE NZ REMARK 470 LYS A 57 CG CD CE NZ REMARK 470 LYS A 60 CG CD CE NZ REMARK 470 LYS A 94 CG CD CE NZ REMARK 470 LYS A 164 CG CD CE NZ REMARK 470 LYS A 165 CG CD CE NZ REMARK 470 LYS A 166 CG CD CE NZ REMARK 470 GLN A 170 CG CD OE1 NE2 REMARK 470 ASN A 171 CG OD1 ND2 REMARK 470 LYS A 234 CG CD CE NZ REMARK 470 LYS A 238 CG CD CE NZ REMARK 470 LYS A 251 CG CD CE NZ REMARK 470 LYS A 261 CG CD CE NZ REMARK 470 MET A 277 CG SD CE REMARK 470 LYS A 278 CG CD CE NZ REMARK 470 ASP A 279 CG OD1 OD2 REMARK 470 PHE A 280 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG A 281 CG CD NE CZ NH1 NH2 REMARK 470 HIS A 282 CG ND1 CD2 CE1 NE2 REMARK 470 LEU A 297 CG CD1 CD2 REMARK 470 LYS A 302 CG CD CE NZ REMARK 470 LYS A 304 CG CD CE NZ REMARK 470 GLU A 305 CG CD OE1 OE2 REMARK 470 GLN A 312 CG CD OE1 NE2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN A 17 70.23 56.94 REMARK 500 PHE A 180 82.66 -66.03 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLA A 501 REMARK 610 OLA A 503 REMARK 610 OLA A 504 REMARK 610 OLA A 505 REMARK 610 OLA A 506 DBREF 7ZLY A 1 219 UNP Q8TDS4 HCAR2_HUMAN 1 219 DBREF 7ZLY A 220 324 UNP P0ABE7 C562_ECOLX 23 127 DBREF 7ZLY A 326 431 UNP Q8TDS4 HCAR2_HUMAN 220 325 SEQADV 7ZLY VAL A 70 UNP Q8TDS4 ALA 70 CONFLICT SEQADV 7ZLY TRP A 226 UNP P0ABE7 MET 29 CONFLICT SEQADV 7ZLY ILE A 321 UNP P0ABE7 HIS 124 CONFLICT SEQADV 7ZLY LEU A 325 UNP P0ABE7 LINKER SEQADV 7ZLY VAL A 393 UNP Q8TDS4 SER 287 CONFLICT SEQRES 1 A 431 MET ASN ARG HIS HIS LEU GLN ASP HIS PHE LEU GLU ILE SEQRES 2 A 431 ASP LYS LYS ASN CYS CYS VAL PHE ARG ASP ASP PHE ILE SEQRES 3 A 431 VAL LYS VAL LEU PRO PRO VAL LEU GLY LEU GLU PHE ILE SEQRES 4 A 431 PHE GLY LEU LEU GLY ASN GLY LEU ALA LEU TRP ILE PHE SEQRES 5 A 431 CYS PHE HIS LEU LYS SER TRP LYS SER SER ARG ILE PHE SEQRES 6 A 431 LEU PHE ASN LEU VAL VAL ALA ASP PHE LEU LEU ILE ILE SEQRES 7 A 431 CYS LEU PRO PHE LEU MET ASP ASN TYR VAL ARG ARG TRP SEQRES 8 A 431 ASP TRP LYS PHE GLY ASP ILE PRO CYS ARG LEU MET LEU SEQRES 9 A 431 PHE MET LEU ALA MET ASN ARG GLN GLY SER ILE ILE PHE SEQRES 10 A 431 LEU THR VAL VAL ALA VAL ASP ARG TYR PHE ARG VAL VAL SEQRES 11 A 431 HIS PRO HIS HIS ALA LEU ASN LYS ILE SER ASN ARG THR SEQRES 12 A 431 ALA ALA ILE ILE SER CYS LEU LEU TRP GLY ILE THR ILE SEQRES 13 A 431 GLY LEU THR VAL HIS LEU LEU LYS LYS LYS MET PRO ILE SEQRES 14 A 431 GLN ASN GLY GLY ALA ASN LEU CYS SER SER PHE SER ILE SEQRES 15 A 431 CYS HIS THR PHE GLN TRP HIS GLU ALA MET PHE LEU LEU SEQRES 16 A 431 GLU PHE PHE LEU PRO LEU GLY ILE ILE LEU PHE CYS SER SEQRES 17 A 431 ALA ARG ILE ILE TRP SER LEU ARG GLN ARG GLN ALA ASP SEQRES 18 A 431 LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS SEQRES 19 A 431 VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP SEQRES 20 A 431 ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN SEQRES 21 A 431 LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SEQRES 22 A 431 SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE SEQRES 23 A 431 LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN SEQRES 24 A 431 GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN SEQRES 25 A 431 LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU SEQRES 26 A 431 MET ASP ARG HIS ALA LYS ILE LYS ARG ALA ILE THR PHE SEQRES 27 A 431 ILE MET VAL VAL ALA ILE VAL PHE VAL ILE CYS PHE LEU SEQRES 28 A 431 PRO SER VAL VAL VAL ARG ILE ARG ILE PHE TRP LEU LEU SEQRES 29 A 431 HIS THR SER GLY THR GLN ASN CYS GLU VAL TYR ARG SER SEQRES 30 A 431 VAL ASP LEU ALA PHE PHE ILE THR LEU SER PHE THR TYR SEQRES 31 A 431 MET ASN VAL MET LEU ASP PRO VAL VAL TYR TYR PHE SER SEQRES 32 A 431 SER PRO SER PHE PRO ASN PHE PHE SER THR LEU ILE ASN SEQRES 33 A 431 ARG CYS LEU GLN ARG LYS MET THR GLY GLU PRO ASP ASN SEQRES 34 A 431 ASN ARG HET OLA A 501 11 HET OLA A 502 20 HET OLA A 503 7 HET OLA A 504 7 HET OLA A 505 8 HET OLA A 506 16 HET OLC A 507 25 HETNAM OLA OLEIC ACID HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 OLA 6(C18 H34 O2) FORMUL 8 OLC C21 H40 O4 HELIX 1 AA1 ASP A 23 PHE A 54 1 32 HELIX 2 AA2 LYS A 60 ARG A 89 1 30 HELIX 3 AA3 GLY A 96 VAL A 130 1 35 HELIX 4 AA4 HIS A 134 ILE A 139 5 6 HELIX 5 AA5 SER A 140 VAL A 160 1 21 HELIX 6 AA6 HIS A 161 LYS A 164 5 4 HELIX 7 AA7 GLN A 187 LYS A 238 1 52 HELIX 8 AA8 ALA A 243 THR A 263 1 21 HELIX 9 AA9 LYS A 278 GLU A 300 1 23 HELIX 10 AB1 LYS A 302 ALA A 310 1 9 HELIX 11 AB2 GLU A 311 ILE A 321 1 11 HELIX 12 AB3 ILE A 321 SER A 367 1 47 HELIX 13 AB4 ASN A 371 VAL A 374 5 4 HELIX 14 AB5 TYR A 375 TYR A 390 1 16 HELIX 15 AB6 MET A 391 PHE A 402 1 12 HELIX 16 AB7 PRO A 405 ARG A 417 1 13 SHEET 1 AA1 2 ILE A 13 ASP A 14 0 SHEET 2 AA1 2 CYS A 18 CYS A 19 -1 O CYS A 18 N ASP A 14 SSBOND 1 CYS A 18 CYS A 183 1555 1555 2.03 SSBOND 2 CYS A 19 CYS A 372 1555 1555 2.03 SSBOND 3 CYS A 100 CYS A 177 1555 1555 2.03 CISPEP 1 MET A 167 PRO A 168 0 -4.61 CRYST1 81.080 82.150 86.310 90.00 90.00 90.00 P 21 2 21 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.012333 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012173 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011586 0.00000 ATOM 1 N LEU A 11 24.127 53.853 98.100 1.00119.22 N ANISOU 1 N LEU A 11 14484 10522 20292 530 -1501 -1490 N ATOM 2 CA LEU A 11 23.398 53.014 97.156 1.00128.74 C ANISOU 2 CA LEU A 11 15865 11423 21625 534 -1668 -1787 C ATOM 3 C LEU A 11 22.532 52.000 97.901 1.00136.86 C ANISOU 3 C LEU A 11 16770 12182 23049 356 -1916 -1578 C ATOM 4 O LEU A 11 21.329 51.900 97.656 1.00134.70 O ANISOU 4 O LEU A 11 16547 11839 22792 204 -2104 -1627 O ATOM 5 CB LEU A 11 24.371 52.299 96.210 1.00128.60 C ANISOU 5 CB LEU A 11 15991 11151 21719 786 -1566 -2104 C ATOM 6 CG LEU A 11 23.830 51.510 95.009 1.00125.39 C ANISOU 6 CG LEU A 11 15850 10429 21365 846 -1714 -2507 C ATOM 7 CD1 LEU A 11 23.456 50.077 95.378 1.00128.63 C ANISOU 7 CD1 LEU A 11 16191 10452 22230 774 -1939 -2436 C ATOM 8 CD2 LEU A 11 22.645 52.224 94.381 1.00121.42 C ANISOU 8 CD2 LEU A 11 15507 10089 20537 706 -1847 -2650 C ATOM 9 N GLU A 12 23.156 51.254 98.807 1.00149.30 N ANISOU 9 N GLU A 12 18168 13598 24961 375 -1919 -1324 N ATOM 10 CA GLU A 12 22.453 50.208 99.527 1.00153.76 C ANISOU 10 CA GLU A 12 18604 13881 25938 221 -2136 -1096 C ATOM 11 C GLU A 12 21.442 50.805 100.505 1.00158.03 C ANISOU 11 C GLU A 12 19008 14662 26376 -13 -2188 -750 C ATOM 12 O GLU A 12 21.568 51.941 100.966 1.00151.64 O ANISOU 12 O GLU A 12 18162 14229 25226 -42 -2041 -609 O ATOM 13 CB GLU A 12 23.442 49.312 100.274 1.00151.29 C ANISOU 13 CB GLU A 12 18134 13351 25997 310 -2119 -883 C ATOM 14 CG GLU A 12 24.440 48.609 99.365 1.00149.73 C ANISOU 14 CG GLU A 12 18046 12907 25938 556 -2040 -1201 C ATOM 15 CD GLU A 12 23.772 47.659 98.387 1.00147.70 C ANISOU 15 CD GLU A 12 17959 12439 25722 553 -2181 -1500 C ATOM 16 OE1 GLU A 12 22.741 47.055 98.752 1.00148.21 O ANISOU 16 OE1 GLU A 12 17953 12402 25956 365 -2391 -1352 O ATOM 17 OE2 GLU A 12 24.274 47.517 97.253 1.00147.24 O ANISOU 17 OE2 GLU A 12 18108 12320 25518 742 -2078 -1872 O ATOM 18 N ILE A 13 20.419 50.011 100.813 1.00163.22 N ANISOU 18 N ILE A 13 19587 15079 27351 -179 -2394 -612 N ATOM 19 CA ILE A 13 19.382 50.416 101.757 1.00163.30 C ANISOU 19 CA ILE A 13 19449 15268 27328 -395 -2426 -259 C ATOM 20 C ILE A 13 19.999 50.545 103.144 1.00167.69 C ANISOU 20 C ILE A 13 19843 15990 27881 -412 -2308 157 C ATOM 21 O ILE A 13 20.529 49.575 103.699 1.00171.38 O ANISOU 21 O ILE A 13 20212 16216 28688 -384 -2367 337 O ATOM 22 CB ILE A 13 18.217 49.415 101.759 1.00161.01 C ANISOU 22 CB ILE A 13 19083 14663 27429 -557 -2664 -179 C ATOM 23 N ASP A 14 19.928 51.746 103.713 1.00167.95 N ANISOU 23 N ASP A 14 19859 16425 27529 -457 -2156 312 N ATOM 24 CA ASP A 14 20.500 51.995 105.027 1.00166.09 C ANISOU 24 CA ASP A 14 19514 16376 27216 -476 -2061 687 C ATOM 25 C ASP A 14 19.569 51.469 106.119 1.00167.49 C ANISOU 25 C ASP A 14 19548 16487 27604 -658 -2131 1096 C ATOM 26 O ASP A 14 18.500 50.914 105.854 1.00172.58 O ANISOU 26 O ASP A 14 20147 16931 28493 -773 -2251 1099 O ATOM 27 CB ASP A 14 20.781 53.485 105.215 1.00163.07 C ANISOU 27 CB ASP A 14 19193 16428 26339 -452 -1884 677 C ATOM 28 N LYS A 15 19.983 51.645 107.369 1.00166.98 N ANISOU 28 N LYS A 15 19412 16588 27444 -686 -2060 1459 N ATOM 29 CA LYS A 15 19.209 51.157 108.499 1.00165.10 C ANISOU 29 CA LYS A 15 19052 16310 27369 -840 -2088 1889 C ATOM 30 C LYS A 15 18.094 52.131 108.859 1.00161.12 C ANISOU 30 C LYS A 15 18552 16103 26565 -961 -1963 2004 C ATOM 31 O LYS A 15 18.165 53.328 108.563 1.00160.71 O ANISOU 31 O LYS A 15 18600 16349 26114 -918 -1843 1823 O ATOM 32 CB LYS A 15 20.114 50.933 109.711 1.00162.09 C ANISOU 32 CB LYS A 15 18624 15987 26976 -814 -2073 2241 C ATOM 33 N LYS A 16 17.054 51.594 109.505 1.00159.03 N ANISOU 33 N LYS A 16 18164 15739 26523 -1108 -1983 2322 N ATOM 34 CA LYS A 16 15.915 52.370 110.008 1.00151.98 C ANISOU 34 CA LYS A 16 17235 15093 25418 -1222 -1837 2508 C ATOM 35 C LYS A 16 15.108 52.994 108.870 1.00146.62 C ANISOU 35 C LYS A 16 16586 14453 24669 -1242 -1850 2174 C ATOM 36 O LYS A 16 14.703 54.155 108.944 1.00144.75 O ANISOU 36 O LYS A 16 16398 14525 24075 -1249 -1697 2143 O ATOM 37 CB LYS A 16 16.361 53.441 111.009 1.00150.20 C ANISOU 37 CB LYS A 16 17104 15262 24705 -1186 -1644 2684 C ATOM 38 N ASN A 17 14.873 52.213 107.814 1.00144.72 N ANISOU 38 N ASN A 17 16327 13886 24772 -1250 -2048 1923 N ATOM 39 CA ASN A 17 14.010 52.599 106.697 1.00138.13 C ANISOU 39 CA ASN A 17 15520 13026 23938 -1289 -2127 1628 C ATOM 40 C ASN A 17 14.491 53.908 106.061 1.00135.89 C ANISOU 40 C ASN A 17 15405 13059 23169 -1176 -2010 1313 C ATOM 41 O ASN A 17 13.861 54.966 106.161 1.00138.46 O ANISOU 41 O ASN A 17 15731 13658 23221 -1215 -1883 1341 O ATOM 42 CB ASN A 17 12.550 52.700 107.155 1.00132.17 C ANISOU 42 CB ASN A 17 14593 12297 23329 -1459 -2093 1911 C ATOM 43 N CYS A 18 15.638 53.790 105.388 1.00129.80 N ANISOU 43 N CYS A 18 14769 12226 22324 -1027 -2048 1020 N ATOM 44 CA CYS A 18 16.348 54.930 104.814 1.00117.56 C ANISOU 44 CA CYS A 18 13373 10952 20343 -900 -1926 746 C ATOM 45 C CYS A 18 17.022 54.489 103.522 1.00106.67 C ANISOU 45 C CYS A 18 12129 9364 19036 -767 -2033 339 C ATOM 46 O CYS A 18 18.028 53.771 103.554 1.00111.12 O ANISOU 46 O CYS A 18 12707 9757 19759 -662 -2053 307 O ATOM 47 CB CYS A 18 17.380 55.480 105.798 1.00126.86 C ANISOU 47 CB CYS A 18 14562 12375 21263 -829 -1763 935 C ATOM 48 SG CYS A 18 18.287 56.930 105.234 1.00136.85 S ANISOU 48 SG CYS A 18 15981 13977 22041 -690 -1611 660 S ATOM 49 N CYS A 19 16.487 54.937 102.390 1.00 93.11 N ANISOU 49 N CYS A 19 10522 7666 17190 -762 -2092 32 N ATOM 50 CA CYS A 19 17.040 54.623 101.077 1.00 93.12 C ANISOU 50 CA CYS A 19 10700 7497 17183 -626 -2172 -381 C ATOM 51 C CYS A 19 17.869 55.812 100.603 1.00 93.16 C ANISOU 51 C CYS A 19 10838 7815 16744 -487 -1982 -572 C ATOM 52 O CYS A 19 17.319 56.881 100.320 1.00100.74 O ANISOU 52 O CYS A 19 11839 9024 17414 -527 -1927 -625 O ATOM 53 CB CYS A 19 15.929 54.315 100.078 1.00 99.01 C ANISOU 53 CB CYS A 19 11513 8046 18058 -711 -2392 -600 C ATOM 54 SG CYS A 19 14.842 52.925 100.466 1.00108.17 S ANISOU 54 SG CYS A 19 12502 8796 19801 -896 -2657 -394 S ATOM 55 N VAL A 20 19.185 55.621 100.500 1.00 91.49 N ANISOU 55 N VAL A 20 10675 7575 16510 -321 -1882 -664 N ATOM 56 CA VAL A 20 20.111 56.656 100.056 1.00 87.11 C ANISOU 56 CA VAL A 20 10219 7284 15593 -180 -1693 -822 C ATOM 57 C VAL A 20 20.878 56.146 98.841 1.00 85.96 C ANISOU 57 C VAL A 20 10237 6945 15480 6 -1683 -1182 C ATOM 58 O VAL A 20 21.221 54.961 98.762 1.00 83.54 O ANISOU 58 O VAL A 20 9924 6317 15500 66 -1768 -1232 O ATOM 59 CB VAL A 20 21.081 57.070 101.184 1.00 83.83 C ANISOU 59 CB VAL A 20 9685 7057 15109 -148 -1548 -547 C ATOM 60 CG1 VAL A 20 21.978 58.213 100.734 1.00 81.75 C ANISOU 60 CG1 VAL A 20 9497 7062 14502 -22 -1366 -688 C ATOM 61 CG2 VAL A 20 20.301 57.472 102.425 1.00 81.67 C ANISOU 61 CG2 VAL A 20 9290 6953 14788 -318 -1550 -197 C ATOM 62 N PHE A 21 21.147 57.045 97.895 1.00 89.30 N ANISOU 62 N PHE A 21 10812 7559 15560 106 -1567 -1428 N ATOM 63 CA PHE A 21 21.902 56.732 96.691 1.00 94.81 C ANISOU 63 CA PHE A 21 11694 8124 16203 306 -1499 -1775 C ATOM 64 C PHE A 21 23.048 57.721 96.548 1.00 96.87 C ANISOU 64 C PHE A 21 11960 8656 16191 452 -1238 -1790 C ATOM 65 O PHE A 21 22.890 58.912 96.832 1.00 94.95 O ANISOU 65 O PHE A 21 11676 8726 15673 385 -1156 -1674 O ATOM 66 CB PHE A 21 21.013 56.791 95.442 1.00100.20 C ANISOU 66 CB PHE A 21 12602 8745 16724 292 -1630 -2093 C ATOM 67 CG PHE A 21 20.044 55.646 95.323 1.00 99.95 C ANISOU 67 CG PHE A 21 12592 8366 17016 180 -1914 -2150 C ATOM 68 CD1 PHE A 21 18.950 55.551 96.166 1.00100.57 C ANISOU 68 CD1 PHE A 21 12496 8433 17283 -40 -2075 -1878 C ATOM 69 CD2 PHE A 21 20.217 54.678 94.348 1.00102.53 C ANISOU 69 CD2 PHE A 21 13120 8370 17468 297 -2017 -2477 C ATOM 70 CE1 PHE A 21 18.058 54.504 96.051 1.00102.48 C ANISOU 70 CE1 PHE A 21 12731 8341 17867 -155 -2345 -1907 C ATOM 71 CE2 PHE A 21 19.326 53.627 94.227 1.00104.01 C ANISOU 71 CE2 PHE A 21 13329 8211 17980 183 -2311 -2537 C ATOM 72 CZ PHE A 21 18.245 53.541 95.080 1.00106.62 C ANISOU 72 CZ PHE A 21 13453 8528 18530 -51 -2482 -2240 C ATOM 73 N ARG A 22 24.200 57.225 96.106 1.00 95.51 N ANISOU 73 N ARG A 22 11824 8348 16119 654 -1106 -1926 N ATOM 74 CA ARG A 22 25.370 58.057 95.836 1.00 87.94 C ANISOU 74 CA ARG A 22 10854 7602 14957 812 -847 -1949 C ATOM 75 C ARG A 22 25.750 57.868 94.371 1.00 90.12 C ANISOU 75 C ARG A 22 11370 7778 15093 1016 -724 -2326 C ATOM 76 O ARG A 22 26.553 56.994 94.034 1.00 96.91 O ANISOU 76 O ARG A 22 12255 8400 16167 1194 -639 -2449 O ATOM 77 CB ARG A 22 26.537 57.714 96.759 1.00 91.37 C ANISOU 77 CB ARG A 22 11071 7985 15662 881 -761 -1708 C ATOM 78 CG ARG A 22 27.667 58.735 96.691 1.00 96.32 C ANISOU 78 CG ARG A 22 11625 8861 16112 996 -524 -1653 C ATOM 79 CD ARG A 22 28.947 58.236 97.345 1.00100.68 C ANISOU 79 CD ARG A 22 11971 9299 16984 1104 -450 -1466 C ATOM 80 NE ARG A 22 29.613 57.207 96.549 1.00102.50 N ANISOU 80 NE ARG A 22 12260 9234 17450 1321 -349 -1683 N ATOM 81 CZ ARG A 22 29.682 55.925 96.891 1.00105.13 C ANISOU 81 CZ ARG A 22 12535 9242 18168 1347 -468 -1649 C ATOM 82 NH1 ARG A 22 29.131 55.510 98.023 1.00105.46 N ANISOU 82 NH1 ARG A 22 12452 9223 18394 1162 -689 -1383 N ATOM 83 NH2 ARG A 22 30.308 55.059 96.104 1.00109.22 N ANISOU 83 NH2 ARG A 22 13124 9488 18886 1565 -351 -1874 N ATOM 84 N ASP A 23 25.175 58.694 93.502 1.00 94.05 N ANISOU 84 N ASP A 23 12053 8458 15225 1001 -707 -2503 N ATOM 85 CA ASP A 23 25.507 58.644 92.089 1.00105.97 C ANISOU 85 CA ASP A 23 13830 9916 16517 1197 -577 -2853 C ATOM 86 C ASP A 23 26.945 59.105 91.863 1.00108.46 C ANISOU 86 C ASP A 23 14084 10357 16769 1409 -241 -2834 C ATOM 87 O ASP A 23 27.526 59.847 92.662 1.00107.37 O ANISOU 87 O ASP A 23 13720 10426 16650 1370 -134 -2564 O ATOM 88 CB ASP A 23 24.538 59.514 91.285 1.00113.53 C ANISOU 88 CB ASP A 23 14988 11065 17082 1114 -657 -2997 C ATOM 89 CG ASP A 23 24.686 59.333 89.784 1.00123.89 C ANISOU 89 CG ASP A 23 16638 12297 18136 1301 -577 -3377 C ATOM 90 OD1 ASP A 23 25.518 58.508 89.351 1.00130.35 O ANISOU 90 OD1 ASP A 23 17544 12901 19082 1505 -441 -3548 O ATOM 91 OD2 ASP A 23 23.962 60.019 89.034 1.00125.97 O ANISOU 91 OD2 ASP A 23 17090 12709 18062 1250 -651 -3502 O ATOM 92 N ASP A 24 27.525 58.640 90.755 1.00119.01 N ANISOU 92 N ASP A 24 15629 11552 18039 1640 -74 -3126 N ATOM 93 CA ASP A 24 28.858 59.083 90.365 1.00125.34 C ANISOU 93 CA ASP A 24 16381 12466 18776 1863 284 -3122 C ATOM 94 C ASP A 24 28.880 60.549 89.963 1.00121.74 C ANISOU 94 C ASP A 24 15958 12376 17920 1842 435 -3070 C ATOM 95 O ASP A 24 29.935 61.186 90.050 1.00123.35 O ANISOU 95 O ASP A 24 16006 12737 18126 1948 696 -2927 O ATOM 96 CB ASP A 24 29.383 58.222 89.219 1.00136.22 C ANISOU 96 CB ASP A 24 18008 13600 20149 2132 454 -3463 C ATOM 97 CG ASP A 24 29.592 56.776 89.628 1.00144.63 C ANISOU 97 CG ASP A 24 19010 14275 21667 2189 348 -3501 C ATOM 98 OD1 ASP A 24 30.226 56.540 90.680 1.00145.63 O ANISOU 98 OD1 ASP A 24 18823 14356 22152 2164 360 -3217 O ATOM 99 OD2 ASP A 24 29.124 55.873 88.898 1.00149.57 O ANISOU 99 OD2 ASP A 24 19906 14629 22296 2258 234 -3814 O ATOM 100 N PHE A 25 27.740 61.094 89.532 1.00118.11 N ANISOU 100 N PHE A 25 15683 12045 17151 1704 265 -3168 N ATOM 101 CA PHE A 25 27.671 62.512 89.200 1.00115.57 C ANISOU 101 CA PHE A 25 15381 12060 16468 1666 381 -3097 C ATOM 102 C PHE A 25 27.909 63.377 90.429 1.00115.33 C ANISOU 102 C PHE A 25 15033 12239 16548 1517 380 -2741 C ATOM 103 O PHE A 25 28.480 64.468 90.319 1.00118.04 O ANISOU 103 O PHE A 25 15303 12823 16725 1552 573 -2629 O ATOM 104 CB PHE A 25 26.313 62.834 88.573 1.00113.99 C ANISOU 104 CB PHE A 25 15421 11921 15968 1533 149 -3253 C ATOM 105 CG PHE A 25 26.249 64.181 87.905 1.00111.01 C ANISOU 105 CG PHE A 25 15139 11851 15187 1541 281 -3245 C ATOM 106 CD1 PHE A 25 25.930 65.320 88.629 1.00104.25 C ANISOU 106 CD1 PHE A 25 14090 11245 14275 1370 241 -2988 C ATOM 107 CD2 PHE A 25 26.485 64.304 86.546 1.00115.13 C ANISOU 107 CD2 PHE A 25 15963 12403 15377 1723 444 -3494 C ATOM 108 CE1 PHE A 25 25.862 66.558 88.010 1.00104.07 C ANISOU 108 CE1 PHE A 25 14148 11484 13909 1376 352 -2971 C ATOM 109 CE2 PHE A 25 26.417 65.539 85.922 1.00114.41 C ANISOU 109 CE2 PHE A 25 15960 12591 14919 1727 561 -3462 C ATOM 110 CZ PHE A 25 26.105 66.666 86.655 1.00108.00 C ANISOU 110 CZ PHE A 25 14930 12014 14092 1550 509 -3196 C ATOM 111 N ILE A 26 27.485 62.908 91.604 1.00113.11 N ANISOU 111 N ILE A 26 14572 11862 16542 1352 164 -2556 N ATOM 112 CA ILE A 26 27.691 63.664 92.834 1.00109.67 C ANISOU 112 CA ILE A 26 13874 11609 16189 1213 143 -2231 C ATOM 113 C ILE A 26 29.163 63.654 93.227 1.00104.02 C ANISOU 113 C ILE A 26 12951 10886 15686 1348 346 -2080 C ATOM 114 O ILE A 26 29.711 64.669 93.673 1.00101.66 O ANISOU 114 O ILE A 26 12498 10798 15330 1314 437 -1887 O ATOM 115 CB ILE A 26 26.799 63.096 93.953 1.00110.98 C ANISOU 115 CB ILE A 26 13935 11668 16563 1012 -129 -2073 C ATOM 116 CG1 ILE A 26 25.323 63.239 93.579 1.00113.00 C ANISOU 116 CG1 ILE A 26 14350 11947 16639 868 -326 -2186 C ATOM 117 CG2 ILE A 26 27.094 63.773 95.281 1.00107.69 C ANISOU 117 CG2 ILE A 26 13282 11420 16214 889 -147 -1747 C ATOM 118 CD1 ILE A 26 24.386 62.458 94.472 1.00113.52 C ANISOU 118 CD1 ILE A 26 14329 11852 16950 696 -574 -2059 C ATOM 119 N VAL A 27 29.829 62.509 93.058 1.00103.60 N ANISOU 119 N VAL A 27 12883 10572 15907 1503 410 -2163 N ATOM 120 CA VAL A 27 31.230 62.391 93.441 1.00 98.82 C ANISOU 120 CA VAL A 27 12050 9925 15572 1638 589 -2003 C ATOM 121 C VAL A 27 32.153 63.118 92.470 1.00 96.34 C ANISOU 121 C VAL A 27 11763 9749 15093 1830 918 -2079 C ATOM 122 O VAL A 27 33.276 63.477 92.840 1.00101.91 O ANISOU 122 O VAL A 27 12231 10508 15980 1899 1068 -1882 O ATOM 123 CB VAL A 27 31.614 60.902 93.552 1.00102.74 C ANISOU 123 CB VAL A 27 12513 10076 16447 1754 558 -2063 C ATOM 124 CG1 VAL A 27 32.947 60.733 94.272 1.00105.67 C ANISOU 124 CG1 VAL A 27 12585 10389 17177 1844 663 -1817 C ATOM 125 CG2 VAL A 27 30.517 60.122 94.261 1.00104.00 C ANISOU 125 CG2 VAL A 27 12700 10079 16737 1568 240 -2028 C ATOM 126 N LYS A 28 31.706 63.367 91.240 1.00 99.06 N ANISOU 126 N LYS A 28 12385 10153 15101 1913 1026 -2341 N ATOM 127 CA LYS A 28 32.574 63.915 90.204 1.00107.85 C ANISOU 127 CA LYS A 28 13558 11374 16048 2124 1375 -2424 C ATOM 128 C LYS A 28 32.332 65.390 89.912 1.00116.82 C ANISOU 128 C LYS A 28 14723 12830 16836 2037 1437 -2346 C ATOM 129 O LYS A 28 33.287 66.108 89.601 1.00118.98 O ANISOU 129 O LYS A 28 14881 13235 17092 2150 1707 -2239 O ATOM 130 CB LYS A 28 32.415 63.115 88.906 1.00106.21 C ANISOU 130 CB LYS A 28 13680 10995 15678 2327 1500 -2784 C ATOM 131 N VAL A 29 31.092 65.867 90.020 1.00121.22 N ANISOU 131 N VAL A 29 15407 13501 17149 1840 1198 -2376 N ATOM 132 CA VAL A 29 30.749 67.212 89.566 1.00123.33 C ANISOU 132 CA VAL A 29 15747 14045 17069 1774 1252 -2342 C ATOM 133 C VAL A 29 30.681 68.182 90.740 1.00115.12 C ANISOU 133 C VAL A 29 14460 13177 16104 1572 1124 -2052 C ATOM 134 O VAL A 29 31.024 69.361 90.604 1.00117.10 O ANISOU 134 O VAL A 29 14642 13635 16216 1558 1248 -1932 O ATOM 135 CB VAL A 29 29.422 67.203 88.784 1.00123.50 C ANISOU 135 CB VAL A 29 16083 14083 16760 1706 1081 -2572 C ATOM 136 CG1 VAL A 29 29.111 68.586 88.228 1.00124.14 C ANISOU 136 CG1 VAL A 29 16242 14438 16488 1658 1148 -2530 C ATOM 137 CG2 VAL A 29 29.478 66.175 87.664 1.00126.70 C ANISOU 137 CG2 VAL A 29 16772 14289 17078 1904 1168 -2886 C ATOM 138 N LEU A 30 30.241 67.700 91.899 1.00104.34 N ANISOU 138 N LEU A 30 12973 11720 14952 1417 878 -1935 N ATOM 139 CA LEU A 30 30.056 68.575 93.054 1.00 93.50 C ANISOU 139 CA LEU A 30 11420 10501 13605 1225 738 -1687 C ATOM 140 C LEU A 30 31.360 69.054 93.695 1.00 87.02 C ANISOU 140 C LEU A 30 10335 9732 12995 1260 852 -1453 C ATOM 141 O LEU A 30 31.430 70.222 94.097 1.00 89.22 O ANISOU 141 O LEU A 30 10525 10197 13178 1159 838 -1304 O ATOM 142 CB LEU A 30 29.184 67.885 94.108 1.00 94.85 C ANISOU 142 CB LEU A 30 11559 10561 13918 1060 463 -1619 C ATOM 143 CG LEU A 30 27.710 67.708 93.734 1.00 94.54 C ANISOU 143 CG LEU A 30 11719 10506 13696 956 291 -1774 C ATOM 144 CD1 LEU A 30 26.881 67.355 94.958 1.00 92.41 C ANISOU 144 CD1 LEU A 30 11360 10186 13567 769 56 -1621 C ATOM 145 CD2 LEU A 30 27.170 68.959 93.058 1.00 91.72 C ANISOU 145 CD2 LEU A 30 11475 10375 13000 917 338 -1825 C ATOM 146 N PRO A 31 32.394 68.219 93.841 1.00 87.73 N ANISOU 146 N PRO A 31 10285 9652 13394 1392 945 -1407 N ATOM 147 CA PRO A 31 33.637 68.691 94.486 1.00 86.15 C ANISOU 147 CA PRO A 31 9805 9491 13437 1410 1014 -1158 C ATOM 148 C PRO A 31 34.222 69.922 93.810 1.00 85.76 C ANISOU 148 C PRO A 31 9713 9632 13242 1468 1234 -1113 C ATOM 149 O PRO A 31 34.601 70.874 94.509 1.00 85.08 O ANISOU 149 O PRO A 31 9456 9666 13202 1357 1166 -905 O ATOM 150 CB PRO A 31 34.575 67.478 94.379 1.00 80.22 C ANISOU 150 CB PRO A 31 8945 8500 13035 1593 1126 -1170 C ATOM 151 CG PRO A 31 33.658 66.325 94.417 1.00 81.38 C ANISOU 151 CG PRO A 31 9262 8468 13193 1567 966 -1334 C ATOM 152 CD PRO A 31 32.421 66.752 93.665 1.00 86.63 C ANISOU 152 CD PRO A 31 10204 9249 13462 1501 929 -1542 C ATOM 153 N PRO A 32 34.326 69.971 92.471 1.00 86.62 N ANISOU 153 N PRO A 32 9978 9767 13168 1638 1495 -1292 N ATOM 154 CA PRO A 32 34.824 71.216 91.862 1.00 86.44 C ANISOU 154 CA PRO A 32 9908 9936 13000 1676 1705 -1210 C ATOM 155 C PRO A 32 33.857 72.378 92.003 1.00 86.42 C ANISOU 155 C PRO A 32 10006 10135 12695 1489 1552 -1189 C ATOM 156 O PRO A 32 34.297 73.535 92.010 1.00 92.25 O ANISOU 156 O PRO A 32 10624 11019 13406 1449 1627 -1036 O ATOM 157 CB PRO A 32 35.046 70.834 90.392 1.00 89.19 C ANISOU 157 CB PRO A 32 10453 10254 13182 1913 2019 -1422 C ATOM 158 CG PRO A 32 34.133 69.711 90.159 1.00 89.32 C ANISOU 158 CG PRO A 32 10717 10117 13102 1927 1880 -1674 C ATOM 159 CD PRO A 32 34.111 68.936 91.440 1.00 88.67 C ANISOU 159 CD PRO A 32 10463 9877 13348 1815 1627 -1562 C ATOM 160 N VAL A 33 32.554 72.111 92.116 1.00 81.86 N ANISOU 160 N VAL A 33 9627 9554 11920 1373 1340 -1329 N ATOM 161 CA VAL A 33 31.604 73.185 92.386 1.00 75.63 C ANISOU 161 CA VAL A 33 8902 8937 10895 1195 1185 -1289 C ATOM 162 C VAL A 33 31.799 73.721 93.798 1.00 77.44 C ANISOU 162 C VAL A 33 8924 9205 11295 1030 1003 -1062 C ATOM 163 O VAL A 33 31.770 74.937 94.026 1.00 82.20 O ANISOU 163 O VAL A 33 9475 9956 11803 936 982 -952 O ATOM 164 CB VAL A 33 30.162 72.697 92.156 1.00 72.04 C ANISOU 164 CB VAL A 33 8683 8449 10238 1119 1006 -1478 C ATOM 165 CG1 VAL A 33 29.163 73.747 92.621 1.00 69.86 C ANISOU 165 CG1 VAL A 33 8430 8328 9784 933 840 -1408 C ATOM 166 CG2 VAL A 33 29.943 72.371 90.688 1.00 69.82 C ANISOU 166 CG2 VAL A 33 8651 8152 9727 1271 1155 -1712 C ATOM 167 N LEU A 34 32.007 72.826 94.768 1.00 76.72 N ANISOU 167 N LEU A 34 8728 8971 11452 994 860 -989 N ATOM 168 CA LEU A 34 32.300 73.263 96.129 1.00 78.66 C ANISOU 168 CA LEU A 34 8803 9244 11842 852 679 -772 C ATOM 169 C LEU A 34 33.578 74.088 96.185 1.00 78.17 C ANISOU 169 C LEU A 34 8530 9235 11938 889 785 -599 C ATOM 170 O LEU A 34 33.687 75.009 97.002 1.00 83.01 O ANISOU 170 O LEU A 34 9057 9933 12550 756 649 -452 O ATOM 171 CB LEU A 34 32.418 72.055 97.058 1.00 81.13 C ANISOU 171 CB LEU A 34 9044 9382 12399 830 522 -707 C ATOM 172 CG LEU A 34 31.200 71.145 97.205 1.00 76.08 C ANISOU 172 CG LEU A 34 8568 8656 11684 772 386 -828 C ATOM 173 CD1 LEU A 34 31.563 69.929 98.036 1.00 78.50 C ANISOU 173 CD1 LEU A 34 8772 8770 12284 776 266 -730 C ATOM 174 CD2 LEU A 34 30.040 71.898 97.834 1.00 75.22 C ANISOU 174 CD2 LEU A 34 8548 8683 11347 592 231 -796 C ATOM 175 N GLY A 35 34.552 73.774 95.329 1.00 73.18 N ANISOU 175 N GLY A 35 7810 8542 11453 1070 1028 -612 N ATOM 176 CA GLY A 35 35.781 74.548 95.308 1.00 76.89 C ANISOU 176 CA GLY A 35 8046 9050 12119 1109 1148 -424 C ATOM 177 C GLY A 35 35.590 75.931 94.717 1.00 77.23 C ANISOU 177 C GLY A 35 8136 9274 11936 1069 1246 -410 C ATOM 178 O GLY A 35 36.131 76.914 95.232 1.00 84.08 O ANISOU 178 O GLY A 35 8837 10199 12910 977 1177 -230 O ATOM 179 N LEU A 36 34.825 76.028 93.627 1.00 71.24 N ANISOU 179 N LEU A 36 7606 8594 10868 1134 1389 -596 N ATOM 180 CA LEU A 36 34.551 77.334 93.036 1.00 75.75 C ANISOU 180 CA LEU A 36 8236 9335 11211 1093 1471 -574 C ATOM 181 C LEU A 36 33.762 78.215 93.995 1.00 85.12 C ANISOU 181 C LEU A 36 9445 10604 12292 880 1202 -517 C ATOM 182 O LEU A 36 34.044 79.412 94.127 1.00 92.68 O ANISOU 182 O LEU A 36 10309 11650 13256 807 1195 -388 O ATOM 183 CB LEU A 36 33.801 77.168 91.715 1.00 72.45 C ANISOU 183 CB LEU A 36 8088 8976 10462 1199 1633 -785 C ATOM 184 CG LEU A 36 34.599 76.556 90.564 1.00 74.43 C ANISOU 184 CG LEU A 36 8366 9177 10737 1437 1962 -854 C ATOM 185 CD1 LEU A 36 33.712 76.359 89.347 1.00 77.59 C ANISOU 185 CD1 LEU A 36 9096 9632 10754 1521 2054 -1089 C ATOM 186 CD2 LEU A 36 35.796 77.429 90.223 1.00 77.89 C ANISOU 186 CD2 LEU A 36 8583 9681 11332 1509 2207 -642 C ATOM 187 N GLU A 37 32.772 77.638 94.680 1.00 81.60 N ANISOU 187 N GLU A 37 9123 10120 11762 783 989 -608 N ATOM 188 CA GLU A 37 32.053 78.387 95.704 1.00 76.67 C ANISOU 188 CA GLU A 37 8521 9562 11050 600 759 -551 C ATOM 189 C GLU A 37 32.971 78.779 96.853 1.00 71.37 C ANISOU 189 C GLU A 37 7648 8854 10616 516 621 -353 C ATOM 190 O GLU A 37 32.729 79.789 97.523 1.00 67.34 O ANISOU 190 O GLU A 37 7137 8411 10038 388 483 -284 O ATOM 191 CB GLU A 37 30.877 77.564 96.225 1.00 74.35 C ANISOU 191 CB GLU A 37 8375 9220 10655 530 593 -659 C ATOM 192 CG GLU A 37 29.828 77.266 95.178 1.00 76.75 C ANISOU 192 CG GLU A 37 8883 9550 10727 577 658 -852 C ATOM 193 CD GLU A 37 28.810 76.256 95.656 1.00 77.14 C ANISOU 193 CD GLU A 37 9032 9510 10766 517 499 -937 C ATOM 194 OE1 GLU A 37 29.140 75.462 96.562 1.00 77.57 O ANISOU 194 OE1 GLU A 37 9001 9458 11016 494 401 -861 O ATOM 195 OE2 GLU A 37 27.679 76.257 95.130 1.00 74.96 O ANISOU 195 OE2 GLU A 37 8911 9266 10305 490 462 -1060 O ATOM 196 N PHE A 38 34.024 77.997 97.095 1.00 71.81 N ANISOU 196 N PHE A 38 7536 8789 10958 590 641 -262 N ATOM 197 CA PHE A 38 34.961 78.332 98.161 1.00 75.00 C ANISOU 197 CA PHE A 38 7740 9144 11612 508 472 -61 C ATOM 198 C PHE A 38 35.883 79.473 97.751 1.00 81.04 C ANISOU 198 C PHE A 38 8334 9958 12500 517 575 71 C ATOM 199 O PHE A 38 36.228 80.326 98.576 1.00 86.11 O ANISOU 199 O PHE A 38 8887 10607 13224 390 385 200 O ATOM 200 CB PHE A 38 35.771 77.093 98.549 1.00 73.10 C ANISOU 200 CB PHE A 38 7355 8745 11673 583 442 15 C ATOM 201 CG PHE A 38 36.920 77.381 99.474 1.00 70.48 C ANISOU 201 CG PHE A 38 6786 8346 11648 520 272 242 C ATOM 202 CD1 PHE A 38 36.714 77.526 100.836 1.00 73.69 C ANISOU 202 CD1 PHE A 38 7227 8742 12030 360 -43 329 C ATOM 203 CD2 PHE A 38 38.208 77.501 98.979 1.00 65.26 C ANISOU 203 CD2 PHE A 38 5869 7626 11302 622 423 379 C ATOM 204 CE1 PHE A 38 37.772 77.791 101.687 1.00 74.08 C ANISOU 204 CE1 PHE A 38 7077 8719 12350 293 -246 535 C ATOM 205 CE2 PHE A 38 39.268 77.766 99.823 1.00 63.49 C ANISOU 205 CE2 PHE A 38 5404 7322 11397 553 230 602 C ATOM 206 CZ PHE A 38 39.051 77.910 101.178 1.00 68.52 C ANISOU 206 CZ PHE A 38 6096 7946 11995 383 -126 675 C ATOM 207 N ILE A 39 36.292 79.507 96.483 1.00 81.00 N ANISOU 207 N ILE A 39 8290 9978 12509 666 871 44 N ATOM 208 CA ILE A 39 37.233 80.527 96.029 1.00 83.16 C ANISOU 208 CA ILE A 39 8370 10286 12941 687 1005 204 C ATOM 209 C ILE A 39 36.548 81.887 95.945 1.00 82.58 C ANISOU 209 C ILE A 39 8405 10339 12633 569 947 191 C ATOM 210 O ILE A 39 36.984 82.861 96.569 1.00 84.73 O ANISOU 210 O ILE A 39 8550 10605 13038 450 794 333 O ATOM 211 CB ILE A 39 37.855 80.123 94.681 1.00 85.36 C ANISOU 211 CB ILE A 39 8593 10561 13279 901 1382 191 C ATOM 212 CG1 ILE A 39 38.713 78.866 94.849 1.00 90.65 C ANISOU 212 CG1 ILE A 39 9105 11075 14261 1026 1443 233 C ATOM 213 CG2 ILE A 39 38.681 81.262 94.111 1.00 87.19 C ANISOU 213 CG2 ILE A 39 8637 10848 13642 919 1556 373 C ATOM 214 CD1 ILE A 39 39.382 78.408 93.575 1.00 94.42 C ANISOU 214 CD1 ILE A 39 9533 11533 14809 1263 1844 213 C ATOM 215 N PHE A 40 35.467 81.974 95.165 1.00 77.03 N ANISOU 215 N PHE A 40 7938 9735 11595 600 1051 21 N ATOM 216 CA PHE A 40 34.770 83.248 95.019 1.00 72.30 C ANISOU 216 CA PHE A 40 7437 9246 10788 502 1006 13 C ATOM 217 C PHE A 40 34.103 83.677 96.319 1.00 67.80 C ANISOU 217 C PHE A 40 6934 8668 10157 326 698 0 C ATOM 218 O PHE A 40 34.013 84.878 96.599 1.00 74.72 O ANISOU 218 O PHE A 40 7796 9581 11012 225 607 61 O ATOM 219 CB PHE A 40 33.736 83.161 93.898 1.00 74.68 C ANISOU 219 CB PHE A 40 7974 9644 10755 576 1158 -158 C ATOM 220 CG PHE A 40 34.311 82.745 92.577 1.00 85.30 C ANISOU 220 CG PHE A 40 9318 11007 12085 764 1475 -171 C ATOM 221 CD1 PHE A 40 35.281 83.513 91.956 1.00 87.94 C ANISOU 221 CD1 PHE A 40 9486 11375 12553 825 1683 1 C ATOM 222 CD2 PHE A 40 33.875 81.590 91.949 1.00 92.93 C ANISOU 222 CD2 PHE A 40 10459 11948 12903 884 1570 -354 C ATOM 223 CE1 PHE A 40 35.813 83.133 90.739 1.00 93.58 C ANISOU 223 CE1 PHE A 40 10217 12114 13227 1016 2014 -5 C ATOM 224 CE2 PHE A 40 34.401 81.204 90.731 1.00 96.55 C ANISOU 224 CE2 PHE A 40 10956 12419 13310 1074 1875 -388 C ATOM 225 CZ PHE A 40 35.371 81.977 90.125 1.00 97.27 C ANISOU 225 CZ PHE A 40 10891 12560 13508 1147 2114 -211 C ATOM 226 N GLY A 41 33.632 82.720 97.119 1.00 60.52 N ANISOU 226 N GLY A 41 6096 7693 9206 294 547 -76 N ATOM 227 CA GLY A 41 33.033 83.069 98.396 1.00 60.41 C ANISOU 227 CA GLY A 41 6163 7676 9114 144 285 -78 C ATOM 228 C GLY A 41 34.032 83.675 99.362 1.00 62.60 C ANISOU 228 C GLY A 41 6281 7889 9617 51 98 86 C ATOM 229 O GLY A 41 33.725 84.647 100.057 1.00 66.18 O ANISOU 229 O GLY A 41 6796 8361 9988 -66 -66 96 O ATOM 230 N LEU A 42 35.240 83.112 99.420 1.00 63.33 N ANISOU 230 N LEU A 42 6165 7888 10009 104 107 214 N ATOM 231 CA LEU A 42 36.275 83.678 100.279 1.00 67.03 C ANISOU 231 CA LEU A 42 6457 8277 10736 10 -103 388 C ATOM 232 C LEU A 42 36.749 85.026 99.752 1.00 65.45 C ANISOU 232 C LEU A 42 6141 8100 10626 -21 -40 477 C ATOM 233 O LEU A 42 37.010 85.948 100.533 1.00 58.68 O ANISOU 233 O LEU A 42 5256 7203 9838 -151 -271 549 O ATOM 234 CB LEU A 42 37.448 82.707 100.400 1.00 48.35 C ANISOU 234 CB LEU A 42 3864 5794 8714 84 -103 524 C ATOM 235 CG LEU A 42 38.665 83.196 101.187 1.00 55.29 C ANISOU 235 CG LEU A 42 4510 6567 9932 -7 -336 735 C ATOM 236 CD1 LEU A 42 38.284 83.539 102.619 1.00 58.69 C ANISOU 236 CD1 LEU A 42 5095 6978 10226 -175 -706 726 C ATOM 237 CD2 LEU A 42 39.766 82.151 101.157 1.00 52.45 C ANISOU 237 CD2 LEU A 42 3902 6087 9940 91 -297 876 C ATOM 238 N LEU A 43 36.862 85.160 98.431 1.00 66.47 N ANISOU 238 N LEU A 43 6217 8289 10752 98 264 477 N ATOM 239 CA LEU A 43 37.301 86.424 97.852 1.00 73.64 C ANISOU 239 CA LEU A 43 7005 9219 11755 74 351 590 C ATOM 240 C LEU A 43 36.245 87.506 98.040 1.00 72.92 C ANISOU 240 C LEU A 43 7113 9197 11394 -32 246 489 C ATOM 241 O LEU A 43 36.562 88.635 98.433 1.00 71.77 O ANISOU 241 O LEU A 43 6898 9009 11363 -141 99 579 O ATOM 242 CB LEU A 43 37.631 86.229 96.371 1.00 81.09 C ANISOU 242 CB LEU A 43 7876 10222 12715 243 731 621 C ATOM 243 CG LEU A 43 38.237 87.411 95.613 1.00 87.95 C ANISOU 243 CG LEU A 43 8582 11113 13721 245 886 788 C ATOM 244 CD1 LEU A 43 39.264 86.918 94.609 1.00 92.71 C ANISOU 244 CD1 LEU A 43 8981 11705 14541 418 1223 921 C ATOM 245 CD2 LEU A 43 37.155 88.213 94.908 1.00 87.63 C ANISOU 245 CD2 LEU A 43 8757 11195 13341 235 977 683 C ATOM 246 N GLY A 44 34.981 87.178 97.769 1.00 72.92 N ANISOU 246 N GLY A 44 7356 9289 11063 -2 310 306 N ATOM 247 CA GLY A 44 33.927 88.170 97.907 1.00 68.75 C ANISOU 247 CA GLY A 44 7001 8819 10301 -85 233 217 C ATOM 248 C GLY A 44 33.703 88.586 99.349 1.00 67.79 C ANISOU 248 C GLY A 44 6957 8636 10164 -224 -69 193 C ATOM 249 O GLY A 44 33.700 89.778 99.671 1.00 76.64 O ANISOU 249 O GLY A 44 8084 9729 11308 -314 -185 222 O ATOM 250 N ASN A 45 33.512 87.609 100.238 1.00 65.04 N ANISOU 250 N ASN A 45 6685 8259 9768 -240 -200 141 N ATOM 251 CA ASN A 45 33.291 87.935 101.643 1.00 63.64 C ANISOU 251 CA ASN A 45 6621 8032 9525 -360 -477 118 C ATOM 252 C ASN A 45 34.538 88.525 102.285 1.00 62.97 C ANISOU 252 C ASN A 45 6375 7834 9715 -447 -693 265 C ATOM 253 O ASN A 45 34.430 89.359 103.191 1.00 61.93 O ANISOU 253 O ASN A 45 6346 7655 9528 -555 -916 242 O ATOM 254 CB ASN A 45 32.829 86.696 102.404 1.00 55.34 C ANISOU 254 CB ASN A 45 5686 6981 8360 -352 -551 62 C ATOM 255 CG ASN A 45 31.430 86.274 102.019 1.00 57.50 C ANISOU 255 CG ASN A 45 6135 7345 8367 -305 -406 -84 C ATOM 256 OD1 ASN A 45 30.451 86.704 102.628 1.00 60.17 O ANISOU 256 OD1 ASN A 45 6646 7717 8498 -359 -468 -166 O ATOM 257 ND2 ASN A 45 31.325 85.441 100.991 1.00 60.55 N ANISOU 257 ND2 ASN A 45 6480 7761 8767 -200 -211 -117 N ATOM 258 N GLY A 46 35.722 88.110 101.833 1.00 61.74 N ANISOU 258 N GLY A 46 5970 7623 9867 -398 -634 415 N ATOM 259 CA GLY A 46 36.941 88.735 102.317 1.00 60.04 C ANISOU 259 CA GLY A 46 5555 7286 9973 -485 -844 582 C ATOM 260 C GLY A 46 37.035 90.193 101.917 1.00 58.04 C ANISOU 260 C GLY A 46 5253 7013 9784 -546 -840 620 C ATOM 261 O GLY A 46 37.436 91.043 102.717 1.00 59.07 O ANISOU 261 O GLY A 46 5376 7041 10026 -672 -1117 663 O ATOM 262 N LEU A 47 36.666 90.505 100.673 1.00 54.12 N ANISOU 262 N LEU A 47 4737 6608 9220 -459 -540 607 N ATOM 263 CA LEU A 47 36.598 91.899 100.249 1.00 62.04 C ANISOU 263 CA LEU A 47 5715 7597 10261 -513 -522 646 C ATOM 264 C LEU A 47 35.558 92.660 101.059 1.00 70.47 C ANISOU 264 C LEU A 47 7047 8661 11068 -605 -710 481 C ATOM 265 O LEU A 47 35.815 93.772 101.533 1.00 84.52 O ANISOU 265 O LEU A 47 8816 10337 12959 -712 -906 511 O ATOM 266 CB LEU A 47 36.281 91.983 98.757 1.00 60.65 C ANISOU 266 CB LEU A 47 5509 7535 10000 -391 -162 663 C ATOM 267 CG LEU A 47 37.457 91.807 97.799 1.00 65.37 C ANISOU 267 CG LEU A 47 5820 8120 10899 -303 66 870 C ATOM 268 CD1 LEU A 47 36.965 91.828 96.363 1.00 69.20 C ANISOU 268 CD1 LEU A 47 6361 8739 11193 -172 420 854 C ATOM 269 CD2 LEU A 47 38.492 92.894 98.031 1.00 62.49 C ANISOU 269 CD2 LEU A 47 5214 7623 10909 -411 -79 1076 C ATOM 270 N ALA A 48 34.373 92.069 101.227 1.00 59.56 N ANISOU 270 N ALA A 48 5899 7376 9356 -560 -647 308 N ATOM 271 CA ALA A 48 33.333 92.701 102.031 1.00 62.06 C ANISOU 271 CA ALA A 48 6465 7692 9424 -625 -784 154 C ATOM 272 C ALA A 48 33.810 92.928 103.459 1.00 63.26 C ANISOU 272 C ALA A 48 6686 7724 9625 -739 -1121 148 C ATOM 273 O ALA A 48 33.640 94.018 104.019 1.00 64.09 O ANISOU 273 O ALA A 48 6899 7751 9700 -820 -1285 92 O ATOM 274 CB ALA A 48 32.067 91.845 102.012 1.00 64.72 C ANISOU 274 CB ALA A 48 6995 8143 9451 -554 -653 6 C ATOM 275 N LEU A 49 34.425 91.907 104.062 1.00 65.12 N ANISOU 275 N LEU A 49 6873 7934 9936 -744 -1240 205 N ATOM 276 CA LEU A 49 34.949 92.047 105.416 1.00 67.74 C ANISOU 276 CA LEU A 49 7284 8154 10301 -854 -1592 216 C ATOM 277 C LEU A 49 35.956 93.187 105.505 1.00 70.82 C ANISOU 277 C LEU A 49 7522 8396 10991 -957 -1802 323 C ATOM 278 O LEU A 49 36.025 93.888 106.521 1.00 66.08 O ANISOU 278 O LEU A 49 7075 7691 10340 -1062 -2100 263 O ATOM 279 CB LEU A 49 35.584 90.732 105.864 1.00 67.93 C ANISOU 279 CB LEU A 49 7223 8166 10421 -836 -1678 309 C ATOM 280 CG LEU A 49 36.199 90.700 107.262 1.00 68.46 C ANISOU 280 CG LEU A 49 7372 8123 10517 -948 -2071 349 C ATOM 281 CD1 LEU A 49 35.135 90.930 108.320 1.00 61.97 C ANISOU 281 CD1 LEU A 49 6920 7337 9289 -983 -2180 173 C ATOM 282 CD2 LEU A 49 36.912 89.379 107.490 1.00 73.09 C ANISOU 282 CD2 LEU A 49 7815 8691 11266 -917 -2129 482 C ATOM 283 N TRP A 50 36.741 93.394 104.447 1.00 71.65 N ANISOU 283 N TRP A 50 7331 8481 11411 -927 -1650 485 N ATOM 284 CA TRP A 50 37.699 94.493 104.445 1.00 73.91 C ANISOU 284 CA TRP A 50 7432 8615 12036 -1031 -1834 618 C ATOM 285 C TRP A 50 36.998 95.836 104.281 1.00 75.85 C ANISOU 285 C TRP A 50 7817 8832 12169 -1072 -1826 515 C ATOM 286 O TRP A 50 37.312 96.801 104.987 1.00 78.93 O ANISOU 286 O TRP A 50 8258 9068 12662 -1192 -2121 498 O ATOM 287 CB TRP A 50 38.731 94.290 103.336 1.00 71.58 C ANISOU 287 CB TRP A 50 6763 8311 12122 -972 -1626 850 C ATOM 288 CG TRP A 50 39.718 95.413 103.238 1.00 73.71 C ANISOU 288 CG TRP A 50 6797 8418 12792 -1080 -1786 1027 C ATOM 289 CD1 TRP A 50 39.639 96.507 102.425 1.00 74.22 C ANISOU 289 CD1 TRP A 50 6779 8464 12959 -1090 -1646 1087 C ATOM 290 CD2 TRP A 50 40.927 95.559 103.990 1.00 73.88 C ANISOU 290 CD2 TRP A 50 6623 8256 13190 -1203 -2141 1183 C ATOM 291 NE1 TRP A 50 40.728 97.322 102.621 1.00 72.94 N ANISOU 291 NE1 TRP A 50 6373 8113 13230 -1213 -1879 1274 N ATOM 292 CE2 TRP A 50 41.534 96.762 103.577 1.00 73.22 C ANISOU 292 CE2 TRP A 50 6332 8042 13447 -1287 -2195 1333 C ATOM 293 CE3 TRP A 50 41.558 94.787 104.970 1.00 74.40 C ANISOU 293 CE3 TRP A 50 6664 8248 13356 -1254 -2435 1228 C ATOM 294 CZ2 TRP A 50 42.740 97.210 104.110 1.00 72.06 C ANISOU 294 CZ2 TRP A 50 5943 7683 13751 -1427 -2542 1518 C ATOM 295 CZ3 TRP A 50 42.754 95.235 105.498 1.00 73.71 C ANISOU 295 CZ3 TRP A 50 6347 7960 13698 -1390 -2790 1410 C ATOM 296 CH2 TRP A 50 43.333 96.434 105.067 1.00 70.65 C ANISOU 296 CH2 TRP A 50 5746 7437 13662 -1477 -2845 1550 C ATOM 297 N ILE A 51 36.047 95.916 103.349 1.00 69.71 N ANISOU 297 N ILE A 51 7106 8188 11192 -973 -1506 443 N ATOM 298 CA ILE A 51 35.362 97.179 103.089 1.00 64.38 C ANISOU 298 CA ILE A 51 6537 7483 10440 -998 -1476 367 C ATOM 299 C ILE A 51 34.512 97.579 104.286 1.00 67.08 C ANISOU 299 C ILE A 51 7208 7779 10501 -1049 -1685 149 C ATOM 300 O ILE A 51 34.534 98.735 104.724 1.00 72.33 O ANISOU 300 O ILE A 51 7951 8302 11228 -1132 -1875 99 O ATOM 301 CB ILE A 51 34.514 97.076 101.809 1.00 58.54 C ANISOU 301 CB ILE A 51 5798 6903 9543 -876 -1105 355 C ATOM 302 CG1 ILE A 51 35.396 96.727 100.609 1.00 58.13 C ANISOU 302 CG1 ILE A 51 5452 6897 9737 -810 -874 567 C ATOM 303 CG2 ILE A 51 33.771 98.379 101.558 1.00 56.86 C ANISOU 303 CG2 ILE A 51 5686 6649 9267 -899 -1085 291 C ATOM 304 CD1 ILE A 51 34.615 96.446 99.350 1.00 60.94 C ANISOU 304 CD1 ILE A 51 5845 7419 9892 -682 -529 548 C ATOM 305 N PHE A 52 33.748 96.630 104.831 1.00 66.57 N ANISOU 305 N PHE A 52 7345 7823 10126 -993 -1640 19 N ATOM 306 CA PHE A 52 32.910 96.924 105.989 1.00 73.97 C ANISOU 306 CA PHE A 52 8607 8732 10766 -1020 -1788 -178 C ATOM 307 C PHE A 52 33.745 97.380 107.182 1.00 76.14 C ANISOU 307 C PHE A 52 8963 8834 11134 -1144 -2185 -187 C ATOM 308 O PHE A 52 33.455 98.410 107.800 1.00 80.31 O ANISOU 308 O PHE A 52 9685 9246 11582 -1196 -2347 -315 O ATOM 309 CB PHE A 52 32.076 95.697 106.363 1.00 79.72 C ANISOU 309 CB PHE A 52 9495 9604 11190 -942 -1663 -263 C ATOM 310 CG PHE A 52 30.850 95.501 105.510 1.00 78.64 C ANISOU 310 CG PHE A 52 9396 9608 10876 -837 -1341 -330 C ATOM 311 CD1 PHE A 52 29.781 96.379 105.587 1.00 80.68 C ANISOU 311 CD1 PHE A 52 9824 9862 10968 -815 -1268 -462 C ATOM 312 CD2 PHE A 52 30.755 94.416 104.655 1.00 76.56 C ANISOU 312 CD2 PHE A 52 9002 9466 10619 -757 -1126 -265 C ATOM 313 CE1 PHE A 52 28.650 96.188 104.809 1.00 82.42 C ANISOU 313 CE1 PHE A 52 10059 10202 11055 -726 -1004 -504 C ATOM 314 CE2 PHE A 52 29.630 94.220 103.876 1.00 77.37 C ANISOU 314 CE2 PHE A 52 9147 9684 10565 -672 -877 -327 C ATOM 315 CZ PHE A 52 28.575 95.105 103.955 1.00 81.46 C ANISOU 315 CZ PHE A 52 9813 10202 10938 -661 -825 -436 C ATOM 316 N CYS A 53 34.796 96.628 107.517 1.00 79.19 N ANISOU 316 N CYS A 53 9206 9184 11698 -1190 -2361 -54 N ATOM 317 CA CYS A 53 35.496 96.829 108.781 1.00 86.25 C ANISOU 317 CA CYS A 53 10220 9930 12621 -1308 -2779 -69 C ATOM 318 C CYS A 53 36.648 97.822 108.704 1.00 83.31 C ANISOU 318 C CYS A 53 9643 9353 12656 -1431 -3048 53 C ATOM 319 O CYS A 53 37.016 98.393 109.739 1.00 85.57 O ANISOU 319 O CYS A 53 10097 9481 12936 -1542 -3428 -16 O ATOM 320 CB CYS A 53 36.030 95.493 109.308 1.00 97.91 C ANISOU 320 CB CYS A 53 11654 11454 14093 -1304 -2884 28 C ATOM 321 SG CYS A 53 34.759 94.337 109.884 1.00104.22 S ANISOU 321 SG CYS A 53 12755 12438 14407 -1201 -2700 -112 S ATOM 322 N PHE A 54 37.217 98.054 107.528 1.00 81.20 N ANISOU 322 N PHE A 54 9033 9079 12740 -1417 -2869 235 N ATOM 323 CA PHE A 54 38.416 98.887 107.495 1.00 84.40 C ANISOU 323 CA PHE A 54 9195 9278 13594 -1545 -3136 398 C ATOM 324 C PHE A 54 38.326 100.062 106.534 1.00 83.06 C ANISOU 324 C PHE A 54 8885 9049 13626 -1551 -2977 452 C ATOM 325 O PHE A 54 38.794 101.150 106.874 1.00 88.92 O ANISOU 325 O PHE A 54 9609 9583 14594 -1674 -3260 464 O ATOM 326 CB PHE A 54 39.651 98.029 107.155 1.00 82.00 C ANISOU 326 CB PHE A 54 8523 8966 13669 -1550 -3151 660 C ATOM 327 CG PHE A 54 39.967 96.990 108.195 1.00 82.59 C ANISOU 327 CG PHE A 54 8697 9044 13637 -1573 -3399 651 C ATOM 328 CD1 PHE A 54 40.224 97.368 109.502 1.00 79.23 C ANISOU 328 CD1 PHE A 54 8494 8470 13142 -1703 -3865 564 C ATOM 329 CD2 PHE A 54 40.002 95.641 107.875 1.00 82.87 C ANISOU 329 CD2 PHE A 54 8626 9224 13636 -1464 -3178 728 C ATOM 330 CE1 PHE A 54 40.509 96.426 110.473 1.00 84.74 C ANISOU 330 CE1 PHE A 54 9301 9175 13721 -1726 -4108 575 C ATOM 331 CE2 PHE A 54 40.290 94.689 108.842 1.00 81.18 C ANISOU 331 CE2 PHE A 54 8500 9005 13341 -1487 -3414 741 C ATOM 332 CZ PHE A 54 40.544 95.083 110.144 1.00 86.31 C ANISOU 332 CZ PHE A 54 9368 9519 13909 -1620 -3880 676 C ATOM 333 N HIS A 55 37.758 99.873 105.341 1.00 77.39 N ANISOU 333 N HIS A 55 8069 8495 12840 -1428 -2554 494 N ATOM 334 CA HIS A 55 37.702 100.969 104.376 1.00 82.96 C ANISOU 334 CA HIS A 55 8632 9150 13739 -1432 -2398 582 C ATOM 335 C HIS A 55 36.811 102.102 104.879 1.00 89.79 C ANISOU 335 C HIS A 55 9786 9915 14413 -1470 -2521 369 C ATOM 336 O HIS A 55 37.276 103.232 105.075 1.00 97.69 O ANISOU 336 O HIS A 55 10737 10704 15677 -1582 -2755 404 O ATOM 337 CB HIS A 55 37.220 100.460 103.015 1.00 87.24 C ANISOU 337 CB HIS A 55 9058 9902 14185 -1283 -1935 661 C ATOM 338 CG HIS A 55 37.123 101.532 101.973 1.00 89.15 C ANISOU 338 CG HIS A 55 9167 10114 14591 -1278 -1757 776 C ATOM 339 ND1 HIS A 55 38.231 102.135 101.415 1.00 92.75 N ANISOU 339 ND1 HIS A 55 9295 10448 15499 -1344 -1776 1039 N ATOM 340 CD2 HIS A 55 36.046 102.113 101.394 1.00 87.73 C ANISOU 340 CD2 HIS A 55 9129 10005 14200 -1216 -1561 685 C ATOM 341 CE1 HIS A 55 37.840 103.038 100.533 1.00 93.50 C ANISOU 341 CE1 HIS A 55 9349 10544 15633 -1322 -1593 1108 C ATOM 342 NE2 HIS A 55 36.519 103.044 100.502 1.00 88.99 N ANISOU 342 NE2 HIS A 55 9062 10088 14663 -1245 -1470 893 N ATOM 343 N LEU A 56 35.525 101.824 105.092 1.00 88.81 N ANISOU 343 N LEU A 56 9957 9927 13861 -1375 -2363 152 N ATOM 344 CA LEU A 56 34.612 102.824 105.627 1.00 89.26 C ANISOU 344 CA LEU A 56 10300 9889 13724 -1385 -2446 -63 C ATOM 345 C LEU A 56 34.521 102.690 107.140 1.00 97.64 C ANISOU 345 C LEU A 56 11679 10867 14552 -1437 -2760 -266 C ATOM 346 O LEU A 56 34.491 101.579 107.677 1.00 97.67 O ANISOU 346 O LEU A 56 11772 10988 14349 -1406 -2771 -296 O ATOM 347 CB LEU A 56 33.228 102.694 104.990 1.00 84.14 C ANISOU 347 CB LEU A 56 9776 9420 12775 -1248 -2088 -166 C ATOM 348 CG LEU A 56 32.577 101.308 104.976 1.00 84.88 C ANISOU 348 CG LEU A 56 9953 9741 12557 -1141 -1876 -220 C ATOM 349 CD1 LEU A 56 31.674 101.114 106.184 1.00 93.25 C ANISOU 349 CD1 LEU A 56 11367 10812 13252 -1116 -1959 -458 C ATOM 350 CD2 LEU A 56 31.807 101.091 103.680 1.00 78.19 C ANISOU 350 CD2 LEU A 56 9009 9063 11635 -1028 -1509 -164 C ATOM 351 N LYS A 57 34.493 103.831 107.825 1.00106.89 N ANISOU 351 N LYS A 57 13033 11828 15753 -1515 -3021 -402 N ATOM 352 CA LYS A 57 34.470 103.869 109.281 1.00109.38 C ANISOU 352 CA LYS A 57 13692 12037 15831 -1567 -3349 -606 C ATOM 353 C LYS A 57 33.085 104.149 109.846 1.00106.49 C ANISOU 353 C LYS A 57 13712 11716 15035 -1463 -3207 -880 C ATOM 354 O LYS A 57 32.917 104.134 111.069 1.00109.90 O ANISOU 354 O LYS A 57 14483 12086 15188 -1477 -3421 -1068 O ATOM 355 CB LYS A 57 35.459 104.922 109.795 1.00115.13 C ANISOU 355 CB LYS A 57 14402 12466 16877 -1729 -3790 -597 C ATOM 356 N SER A 58 32.095 104.398 108.995 1.00103.36 N ANISOU 356 N SER A 58 13274 11421 14576 -1354 -2851 -897 N ATOM 357 CA SER A 58 30.737 104.694 109.432 1.00104.44 C ANISOU 357 CA SER A 58 13724 11594 14364 -1241 -2676 -1128 C ATOM 358 C SER A 58 29.885 103.434 109.326 1.00 98.48 C ANISOU 358 C SER A 58 13009 11104 13305 -1123 -2372 -1128 C ATOM 359 O SER A 58 29.756 102.857 108.241 1.00 92.27 O ANISOU 359 O SER A 58 11971 10474 12613 -1076 -2123 -973 O ATOM 360 CB SER A 58 30.133 105.824 108.598 1.00107.56 C ANISOU 360 CB SER A 58 14040 11908 14920 -1199 -2506 -1135 C ATOM 361 OG SER A 58 30.100 105.482 107.223 1.00108.38 O ANISOU 361 OG SER A 58 13823 12163 15195 -1161 -2236 -921 O ATOM 362 N TRP A 59 29.305 103.016 110.450 1.00 98.84 N ANISOU 362 N TRP A 59 13378 11191 12984 -1076 -2395 -1299 N ATOM 363 CA TRP A 59 28.433 101.847 110.513 1.00 95.26 C ANISOU 363 CA TRP A 59 12985 10963 12245 -971 -2125 -1302 C ATOM 364 C TRP A 59 26.990 102.315 110.654 1.00 96.64 C ANISOU 364 C TRP A 59 13360 11165 12192 -846 -1864 -1466 C ATOM 365 O TRP A 59 26.593 102.807 111.716 1.00 93.97 O ANISOU 365 O TRP A 59 13349 10735 11622 -815 -1938 -1658 O ATOM 366 CB TRP A 59 28.822 100.935 111.675 1.00 95.26 C ANISOU 366 CB TRP A 59 13182 11004 12008 -1003 -2313 -1327 C ATOM 367 CG TRP A 59 29.999 100.058 111.396 1.00 94.24 C ANISOU 367 CG TRP A 59 12801 10912 12094 -1087 -2469 -1125 C ATOM 368 CD1 TRP A 59 31.298 100.296 111.735 1.00 99.68 C ANISOU 368 CD1 TRP A 59 13416 11451 13007 -1216 -2835 -1051 C ATOM 369 CD2 TRP A 59 29.985 98.792 110.725 1.00 90.69 C ANISOU 369 CD2 TRP A 59 12132 10645 11681 -1043 -2265 -970 C ATOM 370 NE1 TRP A 59 32.095 99.259 111.314 1.00101.10 N ANISOU 370 NE1 TRP A 59 13327 11714 13373 -1245 -2849 -847 N ATOM 371 CE2 TRP A 59 31.312 98.323 110.690 1.00 95.36 C ANISOU 371 CE2 TRP A 59 12520 11188 12523 -1136 -2498 -807 C ATOM 372 CE3 TRP A 59 28.978 98.012 110.148 1.00 87.09 C ANISOU 372 CE3 TRP A 59 11629 10371 11090 -934 -1922 -956 C ATOM 373 CZ2 TRP A 59 31.659 97.108 110.102 1.00 92.55 C ANISOU 373 CZ2 TRP A 59 11931 10960 12275 -1108 -2373 -643 C ATOM 374 CZ3 TRP A 59 29.325 96.807 109.564 1.00 85.66 C ANISOU 374 CZ3 TRP A 59 11232 10309 11005 -920 -1826 -804 C ATOM 375 CH2 TRP A 59 30.654 96.367 109.546 1.00 87.03 C ANISOU 375 CH2 TRP A 59 11220 10431 11416 -998 -2038 -656 C ATOM 376 N LYS A 60 26.211 102.161 109.590 1.00106.72 N ANISOU 376 N LYS A 60 14448 12562 13537 -768 -1562 -1390 N ATOM 377 CA LYS A 60 24.789 102.459 109.629 1.00111.30 C ANISOU 377 CA LYS A 60 15158 13183 13948 -643 -1293 -1505 C ATOM 378 C LYS A 60 24.005 101.217 110.046 1.00112.34 C ANISOU 378 C LYS A 60 15377 13503 13806 -566 -1097 -1504 C ATOM 379 O LYS A 60 24.535 100.107 110.111 1.00109.68 O ANISOU 379 O LYS A 60 14969 13272 13434 -607 -1153 -1402 O ATOM 380 CB LYS A 60 24.311 102.971 108.269 1.00108.50 C ANISOU 380 CB LYS A 60 14555 12849 13823 -605 -1102 -1407 C ATOM 381 N SER A 61 22.716 101.418 110.334 1.00105.70 N ANISOU 381 N SER A 61 14675 12689 12795 -450 -860 -1607 N ATOM 382 CA SER A 61 21.884 100.309 110.792 1.00 98.34 C ANISOU 382 CA SER A 61 13822 11918 11626 -377 -659 -1592 C ATOM 383 C SER A 61 21.693 99.259 109.706 1.00 93.53 C ANISOU 383 C SER A 61 12926 11471 11141 -379 -520 -1420 C ATOM 384 O SER A 61 21.461 98.085 110.016 1.00 91.30 O ANISOU 384 O SER A 61 12655 11310 10723 -366 -446 -1362 O ATOM 385 CB SER A 61 20.527 100.828 111.267 1.00100.10 C ANISOU 385 CB SER A 61 14216 12121 11695 -244 -407 -1717 C ATOM 386 OG SER A 61 19.772 101.344 110.185 1.00103.23 O ANISOU 386 OG SER A 61 14401 12515 12306 -191 -230 -1670 O ATOM 387 N SER A 62 21.786 99.656 108.435 1.00 89.80 N ANISOU 387 N SER A 62 12210 10994 10917 -394 -487 -1336 N ATOM 388 CA SER A 62 21.607 98.707 107.343 1.00 81.68 C ANISOU 388 CA SER A 62 10944 10108 9983 -389 -367 -1194 C ATOM 389 C SER A 62 22.838 97.828 107.153 1.00 84.78 C ANISOU 389 C SER A 62 11225 10543 10444 -470 -520 -1090 C ATOM 390 O SER A 62 22.710 96.641 106.833 1.00 94.25 O ANISOU 390 O SER A 62 12335 11861 11616 -458 -441 -1014 O ATOM 391 CB SER A 62 21.277 99.452 106.050 1.00 79.29 C ANISOU 391 CB SER A 62 10454 9790 9884 -369 -280 -1135 C ATOM 392 OG SER A 62 20.068 100.181 106.177 1.00 85.08 O ANISOU 392 OG SER A 62 11258 10480 10588 -285 -128 -1212 O ATOM 393 N ARG A 63 24.035 98.387 107.341 1.00 82.97 N ANISOU 393 N ARG A 63 10987 10204 10333 -551 -744 -1080 N ATOM 394 CA ARG A 63 25.248 97.590 107.187 1.00 83.53 C ANISOU 394 CA ARG A 63 10924 10299 10513 -620 -887 -964 C ATOM 395 C ARG A 63 25.424 96.608 108.338 1.00 81.88 C ANISOU 395 C ARG A 63 10873 10127 10112 -635 -983 -983 C ATOM 396 O ARG A 63 26.062 95.563 108.165 1.00 82.28 O ANISOU 396 O ARG A 63 10802 10237 10224 -660 -1024 -876 O ATOM 397 CB ARG A 63 26.468 98.502 107.071 1.00 87.30 C ANISOU 397 CB ARG A 63 11315 10632 11222 -710 -1109 -920 C ATOM 398 CG ARG A 63 26.518 99.295 105.777 1.00 86.39 C ANISOU 398 CG ARG A 63 10995 10496 11335 -704 -1011 -836 C ATOM 399 CD ARG A 63 27.492 100.457 105.870 1.00 88.80 C ANISOU 399 CD ARG A 63 11252 10618 11870 -793 -1229 -811 C ATOM 400 NE ARG A 63 27.433 101.299 104.680 1.00 95.14 N ANISOU 400 NE ARG A 63 11876 11394 12878 -783 -1118 -716 N ATOM 401 CZ ARG A 63 27.938 102.526 104.605 1.00106.33 C ANISOU 401 CZ ARG A 63 13248 12639 14513 -846 -1256 -693 C ATOM 402 NH1 ARG A 63 28.540 103.063 105.657 1.00113.07 N ANISOU 402 NH1 ARG A 63 14233 13320 15408 -928 -1531 -779 N ATOM 403 NH2 ARG A 63 27.835 103.218 103.478 1.00112.72 N ANISOU 403 NH2 ARG A 63 13892 13439 15499 -831 -1133 -578 N ATOM 404 N ILE A 64 24.869 96.920 109.510 1.00 76.56 N ANISOU 404 N ILE A 64 10475 9415 9201 -613 -1009 -1111 N ATOM 405 CA ILE A 64 24.948 95.999 110.639 1.00 76.10 C ANISOU 405 CA ILE A 64 10595 9402 8919 -620 -1086 -1113 C ATOM 406 C ILE A 64 24.131 94.744 110.354 1.00 77.17 C ANISOU 406 C ILE A 64 10653 9687 8980 -559 -857 -1038 C ATOM 407 O ILE A 64 24.600 93.618 110.560 1.00 78.75 O ANISOU 407 O ILE A 64 10808 9941 9173 -586 -921 -941 O ATOM 408 CB ILE A 64 24.489 96.697 111.931 1.00 71.87 C ANISOU 408 CB ILE A 64 10406 8793 8107 -593 -1135 -1274 C ATOM 409 CG1 ILE A 64 25.409 97.876 112.249 1.00 73.13 C ANISOU 409 CG1 ILE A 64 10653 8773 8361 -671 -1423 -1356 C ATOM 410 CG2 ILE A 64 24.465 95.718 113.093 1.00 70.47 C ANISOU 410 CG2 ILE A 64 10438 8682 7654 -590 -1185 -1255 C ATOM 411 CD1 ILE A 64 24.928 98.733 113.393 1.00 74.27 C ANISOU 411 CD1 ILE A 64 11165 8817 8236 -630 -1466 -1554 C ATOM 412 N PHE A 65 22.897 94.919 109.874 1.00 73.84 N ANISOU 412 N PHE A 65 10206 9320 8531 -479 -604 -1073 N ATOM 413 CA PHE A 65 22.100 93.772 109.451 1.00 66.50 C ANISOU 413 CA PHE A 65 9168 8510 7589 -433 -409 -994 C ATOM 414 C PHE A 65 22.762 93.049 108.286 1.00 69.66 C ANISOU 414 C PHE A 65 9312 8951 8205 -465 -437 -885 C ATOM 415 O PHE A 65 22.696 91.817 108.188 1.00 77.10 O ANISOU 415 O PHE A 65 10187 9959 9148 -460 -396 -810 O ATOM 416 CB PHE A 65 20.690 94.222 109.062 1.00 55.13 C ANISOU 416 CB PHE A 65 7713 7097 6137 -351 -166 -1038 C ATOM 417 CG PHE A 65 19.901 94.813 110.195 1.00 52.22 C ANISOU 417 CG PHE A 65 7591 6694 5555 -288 -69 -1141 C ATOM 418 CD1 PHE A 65 19.970 94.268 111.467 1.00 58.03 C ANISOU 418 CD1 PHE A 65 8547 7451 6051 -286 -99 -1148 C ATOM 419 CD2 PHE A 65 19.089 95.916 109.987 1.00 54.10 C ANISOU 419 CD2 PHE A 65 7851 6877 5828 -222 64 -1225 C ATOM 420 CE1 PHE A 65 19.241 94.813 112.511 1.00 66.03 C ANISOU 420 CE1 PHE A 65 9817 8438 6833 -209 23 -1247 C ATOM 421 CE2 PHE A 65 18.359 96.466 111.026 1.00 58.74 C ANISOU 421 CE2 PHE A 65 8674 7423 6221 -142 187 -1330 C ATOM 422 CZ PHE A 65 18.435 95.914 112.289 1.00 62.37 C ANISOU 422 CZ PHE A 65 9372 7913 6413 -131 178 -1346 C ATOM 423 N LEU A 66 23.414 93.799 107.397 1.00 60.27 N ANISOU 423 N LEU A 66 7984 7713 7201 -490 -496 -873 N ATOM 424 CA LEU A 66 24.010 93.207 106.206 1.00 59.26 C ANISOU 424 CA LEU A 66 7630 7627 7259 -497 -476 -775 C ATOM 425 C LEU A 66 25.321 92.494 106.509 1.00 62.46 C ANISOU 425 C LEU A 66 7973 8006 7753 -550 -646 -694 C ATOM 426 O LEU A 66 25.664 91.520 105.829 1.00 50.42 O ANISOU 426 O LEU A 66 6302 6528 6327 -533 -597 -618 O ATOM 427 CB LEU A 66 24.231 94.288 105.150 1.00 46.78 C ANISOU 427 CB LEU A 66 5926 6010 5839 -498 -452 -762 C ATOM 428 CG LEU A 66 24.631 93.810 103.758 1.00 51.55 C ANISOU 428 CG LEU A 66 6324 6674 6589 -477 -368 -669 C ATOM 429 CD1 LEU A 66 23.514 92.989 103.136 1.00 57.71 C ANISOU 429 CD1 LEU A 66 7089 7551 7287 -416 -202 -682 C ATOM 430 CD2 LEU A 66 24.970 95.004 102.895 1.00 52.91 C ANISOU 430 CD2 LEU A 66 6397 6800 6904 -486 -359 -630 C ATOM 431 N PHE A 67 26.063 92.956 107.517 1.00 70.05 N ANISOU 431 N PHE A 67 9045 8882 8690 -611 -857 -709 N ATOM 432 CA PHE A 67 27.319 92.305 107.867 1.00 66.76 C ANISOU 432 CA PHE A 67 8553 8425 8387 -667 -1050 -612 C ATOM 433 C PHE A 67 27.103 90.922 108.471 1.00 65.72 C ANISOU 433 C PHE A 67 8480 8355 8136 -650 -1039 -568 C ATOM 434 O PHE A 67 28.034 90.110 108.474 1.00 60.13 O ANISOU 434 O PHE A 67 7653 7628 7566 -673 -1146 -464 O ATOM 435 CB PHE A 67 28.115 93.190 108.827 1.00 61.22 C ANISOU 435 CB PHE A 67 7971 7600 7689 -749 -1326 -641 C ATOM 436 CG PHE A 67 29.481 92.660 109.151 1.00 57.63 C ANISOU 436 CG PHE A 67 7406 7084 7408 -818 -1565 -519 C ATOM 437 CD1 PHE A 67 30.509 92.748 108.228 1.00 56.02 C ANISOU 437 CD1 PHE A 67 6922 6836 7526 -839 -1588 -400 C ATOM 438 CD2 PHE A 67 29.737 92.075 110.380 1.00 61.30 C ANISOU 438 CD2 PHE A 67 8039 7531 7722 -856 -1761 -506 C ATOM 439 CE1 PHE A 67 31.767 92.259 108.523 1.00 61.66 C ANISOU 439 CE1 PHE A 67 7500 7482 8447 -896 -1802 -269 C ATOM 440 CE2 PHE A 67 30.993 91.585 110.682 1.00 64.61 C ANISOU 440 CE2 PHE A 67 8337 7882 8329 -921 -2006 -376 C ATOM 441 CZ PHE A 67 32.008 91.677 109.753 1.00 65.67 C ANISOU 441 CZ PHE A 67 8165 7963 8823 -940 -2026 -257 C ATOM 442 N ASN A 68 25.899 90.634 108.975 1.00 64.65 N ANISOU 442 N ASN A 68 8506 8282 7775 -606 -904 -628 N ATOM 443 CA ASN A 68 25.624 89.300 109.500 1.00 63.41 C ANISOU 443 CA ASN A 68 8388 8177 7526 -592 -875 -561 C ATOM 444 C ASN A 68 25.710 88.243 108.407 1.00 59.34 C ANISOU 444 C ASN A 68 7652 7699 7194 -559 -765 -490 C ATOM 445 O ASN A 68 26.069 87.093 108.684 1.00 61.39 O ANISOU 445 O ASN A 68 7873 7957 7495 -563 -816 -404 O ATOM 446 CB ASN A 68 24.249 89.260 110.165 1.00 64.26 C ANISOU 446 CB ASN A 68 8684 8342 7390 -547 -712 -617 C ATOM 447 CG ASN A 68 24.177 90.119 111.411 1.00 70.22 C ANISOU 447 CG ASN A 68 9712 9058 7910 -561 -809 -696 C ATOM 448 OD1 ASN A 68 24.682 89.743 112.469 1.00 71.66 O ANISOU 448 OD1 ASN A 68 10048 9224 7956 -597 -975 -656 O ATOM 449 ND2 ASN A 68 23.535 91.275 111.295 1.00 80.32 N ANISOU 449 ND2 ASN A 68 11069 10316 9134 -526 -710 -813 N ATOM 450 N LEU A 69 25.379 88.610 107.167 1.00 54.43 N ANISOU 450 N LEU A 69 6901 7103 6677 -520 -619 -527 N ATOM 451 CA LEU A 69 25.537 87.678 106.056 1.00 56.74 C ANISOU 451 CA LEU A 69 7017 7420 7120 -480 -524 -484 C ATOM 452 C LEU A 69 26.999 87.300 105.863 1.00 60.35 C ANISOU 452 C LEU A 69 7330 7823 7778 -495 -644 -396 C ATOM 453 O LEU A 69 27.311 86.147 105.545 1.00 69.37 O ANISOU 453 O LEU A 69 8377 8958 9021 -463 -617 -344 O ATOM 454 CB LEU A 69 24.966 88.284 104.775 1.00 57.36 C ANISOU 454 CB LEU A 69 7019 7538 7237 -437 -370 -537 C ATOM 455 CG LEU A 69 23.445 88.387 104.688 1.00 61.15 C ANISOU 455 CG LEU A 69 7577 8068 7588 -408 -234 -600 C ATOM 456 CD1 LEU A 69 23.037 89.200 103.471 1.00 58.65 C ANISOU 456 CD1 LEU A 69 7190 7778 7316 -376 -136 -635 C ATOM 457 CD2 LEU A 69 22.828 86.999 104.642 1.00 62.87 C ANISOU 457 CD2 LEU A 69 7778 8309 7800 -387 -174 -577 C ATOM 458 N VAL A 70 27.908 88.259 106.051 1.00 61.77 N ANISOU 458 N VAL A 70 7478 7945 8046 -542 -778 -372 N ATOM 459 CA VAL A 70 29.335 87.953 105.981 1.00 64.50 C ANISOU 459 CA VAL A 70 7659 8223 8625 -563 -907 -260 C ATOM 460 C VAL A 70 29.711 86.957 107.070 1.00 59.46 C ANISOU 460 C VAL A 70 7074 7550 7967 -593 -1070 -190 C ATOM 461 O VAL A 70 30.426 85.979 106.823 1.00 65.49 O ANISOU 461 O VAL A 70 7690 8282 8910 -566 -1082 -98 O ATOM 462 CB VAL A 70 30.169 89.242 106.087 1.00 72.65 C ANISOU 462 CB VAL A 70 8643 9180 9779 -627 -1054 -234 C ATOM 463 CG1 VAL A 70 31.654 88.922 105.983 1.00 76.62 C ANISOU 463 CG1 VAL A 70 8931 9604 10578 -650 -1182 -90 C ATOM 464 CG2 VAL A 70 29.753 90.235 105.017 1.00 73.42 C ANISOU 464 CG2 VAL A 70 8691 9309 9898 -598 -889 -281 C ATOM 465 N VAL A 71 29.232 87.194 108.292 1.00 55.39 N ANISOU 465 N VAL A 71 6780 7036 7229 -641 -1190 -226 N ATOM 466 CA VAL A 71 29.483 86.259 109.384 1.00 59.39 C ANISOU 466 CA VAL A 71 7374 7521 7670 -670 -1346 -144 C ATOM 467 C VAL A 71 28.844 84.909 109.083 1.00 69.75 C ANISOU 467 C VAL A 71 8646 8878 8978 -610 -1183 -114 C ATOM 468 O VAL A 71 29.455 83.854 109.297 1.00 74.92 O ANISOU 468 O VAL A 71 9215 9489 9762 -607 -1266 -4 O ATOM 469 CB VAL A 71 28.978 86.847 110.715 1.00 61.33 C ANISOU 469 CB VAL A 71 7910 7774 7617 -717 -1469 -200 C ATOM 470 CG1 VAL A 71 29.084 85.820 111.831 1.00 62.63 C ANISOU 470 CG1 VAL A 71 8195 7937 7665 -740 -1603 -98 C ATOM 471 CG2 VAL A 71 29.763 88.102 111.068 1.00 65.50 C ANISOU 471 CG2 VAL A 71 8485 8219 8183 -787 -1692 -235 C ATOM 472 N ALA A 72 27.614 84.919 108.561 1.00 63.73 N ANISOU 472 N ALA A 72 7930 8185 8098 -564 -963 -203 N ATOM 473 CA ALA A 72 26.937 83.666 108.245 1.00 60.05 C ANISOU 473 CA ALA A 72 7425 7740 7651 -518 -830 -180 C ATOM 474 C ALA A 72 27.607 82.932 107.089 1.00 59.91 C ANISOU 474 C ALA A 72 7196 7683 7886 -465 -770 -158 C ATOM 475 O ALA A 72 27.505 81.703 106.996 1.00 62.99 O ANISOU 475 O ALA A 72 7538 8041 8357 -435 -740 -114 O ATOM 476 CB ALA A 72 25.466 83.929 107.924 1.00 56.01 C ANISOU 476 CB ALA A 72 6992 7298 6991 -490 -636 -271 C ATOM 477 N ASP A 73 28.296 83.657 106.203 1.00 50.19 N ANISOU 477 N ASP A 73 5842 6444 6785 -445 -741 -183 N ATOM 478 CA ASP A 73 28.931 83.013 105.058 1.00 53.82 C ANISOU 478 CA ASP A 73 6120 6871 7456 -372 -640 -169 C ATOM 479 C ASP A 73 30.242 82.337 105.441 1.00 65.74 C ANISOU 479 C ASP A 73 7496 8291 9193 -371 -776 -41 C ATOM 480 O ASP A 73 30.560 81.262 104.921 1.00 77.19 O ANISOU 480 O ASP A 73 8839 9691 10798 -301 -705 -17 O ATOM 481 CB ASP A 73 29.169 84.028 103.941 1.00 50.65 C ANISOU 481 CB ASP A 73 5637 6504 7104 -340 -526 -215 C ATOM 482 CG ASP A 73 27.895 84.403 103.213 1.00 63.06 C ANISOU 482 CG ASP A 73 7299 8154 8507 -314 -370 -331 C ATOM 483 OD1 ASP A 73 26.814 83.909 103.600 1.00 68.97 O ANISOU 483 OD1 ASP A 73 8157 8925 9123 -324 -351 -374 O ATOM 484 OD2 ASP A 73 27.975 85.196 102.252 1.00 68.78 O ANISOU 484 OD2 ASP A 73 7973 8912 9247 -286 -272 -359 O ATOM 485 N PHE A 74 31.016 82.948 106.341 1.00 59.97 N ANISOU 485 N PHE A 74 6766 7521 8497 -445 -985 42 N ATOM 486 CA PHE A 74 32.279 82.344 106.748 1.00 66.88 C ANISOU 486 CA PHE A 74 7493 8300 9620 -453 -1148 188 C ATOM 487 C PHE A 74 32.081 81.037 107.505 1.00 69.58 C ANISOU 487 C PHE A 74 7888 8603 9945 -451 -1226 257 C ATOM 488 O PHE A 74 32.999 80.211 107.532 1.00 69.49 O ANISOU 488 O PHE A 74 7718 8501 10183 -421 -1297 373 O ATOM 489 CB PHE A 74 33.091 83.325 107.593 1.00 68.33 C ANISOU 489 CB PHE A 74 7683 8439 9842 -551 -1407 261 C ATOM 490 CG PHE A 74 33.964 84.240 106.781 1.00 77.13 C ANISOU 490 CG PHE A 74 8603 9521 11183 -547 -1374 291 C ATOM 491 CD1 PHE A 74 35.220 83.829 106.365 1.00 79.47 C ANISOU 491 CD1 PHE A 74 8631 9730 11833 -509 -1391 431 C ATOM 492 CD2 PHE A 74 33.528 85.507 106.429 1.00 82.98 C ANISOU 492 CD2 PHE A 74 9414 10309 11808 -574 -1313 199 C ATOM 493 CE1 PHE A 74 36.027 84.666 105.615 1.00 83.85 C ANISOU 493 CE1 PHE A 74 8986 10255 12617 -502 -1334 490 C ATOM 494 CE2 PHE A 74 34.330 86.349 105.679 1.00 81.90 C ANISOU 494 CE2 PHE A 74 9087 10135 11895 -575 -1276 255 C ATOM 495 CZ PHE A 74 35.581 85.928 105.272 1.00 83.99 C ANISOU 495 CZ PHE A 74 9081 10322 12508 -540 -1280 407 C ATOM 496 N LEU A 75 30.914 80.828 108.118 1.00 68.67 N ANISOU 496 N LEU A 75 7978 8547 9566 -478 -1204 206 N ATOM 497 CA LEU A 75 30.634 79.533 108.729 1.00 66.01 C ANISOU 497 CA LEU A 75 7681 8172 9229 -473 -1245 290 C ATOM 498 C LEU A 75 30.611 78.431 107.678 1.00 65.02 C ANISOU 498 C LEU A 75 7408 7990 9307 -378 -1077 264 C ATOM 499 O LEU A 75 31.049 77.304 107.936 1.00 69.60 O ANISOU 499 O LEU A 75 7909 8476 10058 -354 -1143 367 O ATOM 500 CB LEU A 75 29.309 79.578 109.489 1.00 62.95 C ANISOU 500 CB LEU A 75 7524 7862 8532 -512 -1204 254 C ATOM 501 CG LEU A 75 29.229 80.539 110.677 1.00 57.47 C ANISOU 501 CG LEU A 75 7037 7216 7584 -590 -1358 265 C ATOM 502 CD1 LEU A 75 27.876 80.431 111.365 1.00 46.20 C ANISOU 502 CD1 LEU A 75 5821 5865 5869 -599 -1250 245 C ATOM 503 CD2 LEU A 75 30.357 80.276 111.661 1.00 59.44 C ANISOU 503 CD2 LEU A 75 7287 7393 7903 -645 -1647 417 C ATOM 504 N LEU A 76 30.109 78.740 106.482 1.00 63.12 N ANISOU 504 N LEU A 76 7141 7794 9047 -319 -870 124 N ATOM 505 CA LEU A 76 30.117 77.770 105.395 1.00 65.11 C ANISOU 505 CA LEU A 76 7290 7986 9464 -220 -716 66 C ATOM 506 C LEU A 76 31.464 77.721 104.686 1.00 72.77 C ANISOU 506 C LEU A 76 8059 8888 10702 -142 -679 107 C ATOM 507 O LEU A 76 31.861 76.659 104.193 1.00 77.54 O ANISOU 507 O LEU A 76 8563 9394 11504 -53 -611 113 O ATOM 508 CB LEU A 76 29.005 78.096 104.397 1.00 59.94 C ANISOU 508 CB LEU A 76 6715 7406 8654 -189 -533 -97 C ATOM 509 CG LEU A 76 28.861 77.179 103.183 1.00 59.59 C ANISOU 509 CG LEU A 76 6622 7302 8718 -86 -384 -198 C ATOM 510 CD1 LEU A 76 28.701 75.734 103.619 1.00 64.90 C ANISOU 510 CD1 LEU A 76 7289 7856 9515 -76 -444 -149 C ATOM 511 CD2 LEU A 76 27.682 77.617 102.331 1.00 56.35 C ANISOU 511 CD2 LEU A 76 6315 6971 8124 -80 -264 -345 C ATOM 512 N ILE A 77 32.177 78.849 104.631 1.00 71.25 N ANISOU 512 N ILE A 77 7797 8731 10543 -168 -715 143 N ATOM 513 CA ILE A 77 33.476 78.881 103.964 1.00 73.61 C ANISOU 513 CA ILE A 77 7874 8966 11129 -94 -656 213 C ATOM 514 C ILE A 77 34.470 77.979 104.685 1.00 73.38 C ANISOU 514 C ILE A 77 7703 8810 11370 -88 -818 377 C ATOM 515 O ILE A 77 35.272 77.282 104.051 1.00 73.32 O ANISOU 515 O ILE A 77 7515 8710 11634 22 -710 419 O ATOM 516 CB ILE A 77 33.988 80.331 103.868 1.00 79.03 C ANISOU 516 CB ILE A 77 8503 9704 11821 -147 -689 247 C ATOM 517 CG1 ILE A 77 33.080 81.159 102.957 1.00 79.42 C ANISOU 517 CG1 ILE A 77 8663 9865 11648 -129 -502 100 C ATOM 518 CG2 ILE A 77 35.424 80.366 103.364 1.00 78.68 C ANISOU 518 CG2 ILE A 77 8190 9579 12124 -84 -647 375 C ATOM 519 CD1 ILE A 77 33.459 82.621 102.883 1.00 79.03 C ANISOU 519 CD1 ILE A 77 8572 9854 11603 -189 -538 134 C ATOM 520 N ILE A 78 34.428 77.971 106.020 1.00 73.94 N ANISOU 520 N ILE A 78 7859 8868 11366 -198 -1076 477 N ATOM 521 CA ILE A 78 35.341 77.134 106.793 1.00 74.57 C ANISOU 521 CA ILE A 78 7815 8825 11693 -205 -1274 657 C ATOM 522 C ILE A 78 35.104 75.660 106.492 1.00 78.89 C ANISOU 522 C ILE A 78 8332 9283 12361 -111 -1167 648 C ATOM 523 O ILE A 78 36.052 74.873 106.375 1.00 82.51 O ANISOU 523 O ILE A 78 8594 9611 13146 -37 -1185 757 O ATOM 524 CB ILE A 78 35.193 77.436 108.297 1.00 68.51 C ANISOU 524 CB ILE A 78 7211 8079 10742 -343 -1578 755 C ATOM 525 CG1 ILE A 78 35.649 78.862 108.605 1.00 62.10 C ANISOU 525 CG1 ILE A 78 6411 7307 9875 -433 -1726 765 C ATOM 526 CG2 ILE A 78 35.975 76.428 109.130 1.00 71.04 C ANISOU 526 CG2 ILE A 78 7433 8275 11285 -354 -1801 954 C ATOM 527 CD1 ILE A 78 35.380 79.292 110.030 1.00 60.02 C ANISOU 527 CD1 ILE A 78 6378 7074 9351 -560 -2010 810 C ATOM 528 N CYS A 79 33.839 75.263 106.349 1.00 75.14 N ANISOU 528 N CYS A 79 8037 8858 11655 -110 -1060 522 N ATOM 529 CA CYS A 79 33.503 73.857 106.160 1.00 69.53 C ANISOU 529 CA CYS A 79 7319 8041 11059 -41 -996 510 C ATOM 530 C CYS A 79 33.684 73.385 104.724 1.00 69.02 C ANISOU 530 C CYS A 79 7159 7915 11151 108 -744 371 C ATOM 531 O CYS A 79 33.727 72.173 104.489 1.00 68.52 O ANISOU 531 O CYS A 79 7051 7717 11267 188 -702 364 O ATOM 532 CB CYS A 79 32.059 73.599 106.593 1.00 67.44 C ANISOU 532 CB CYS A 79 7268 7836 10521 -109 -993 450 C ATOM 533 SG CYS A 79 31.673 74.062 108.299 1.00 73.67 S ANISOU 533 SG CYS A 79 8230 8706 11054 -260 -1234 600 S ATOM 534 N LEU A 80 33.784 74.305 103.764 1.00 70.00 N ANISOU 534 N LEU A 80 7267 8128 11203 152 -577 262 N ATOM 535 CA LEU A 80 33.863 73.903 102.362 1.00 72.48 C ANISOU 535 CA LEU A 80 7545 8403 11591 302 -320 114 C ATOM 536 C LEU A 80 35.069 73.029 102.034 1.00 78.50 C ANISOU 536 C LEU A 80 8100 9005 12720 438 -249 190 C ATOM 537 O LEU A 80 34.900 72.068 101.263 1.00 77.97 O ANISOU 537 O LEU A 80 8061 8840 12724 561 -99 67 O ATOM 538 CB LEU A 80 33.829 75.148 101.466 1.00 70.61 C ANISOU 538 CB LEU A 80 7328 8301 11199 320 -161 25 C ATOM 539 CG LEU A 80 32.419 75.641 101.136 1.00 69.04 C ANISOU 539 CG LEU A 80 7346 8223 10662 263 -118 -133 C ATOM 540 CD1 LEU A 80 32.461 76.974 100.413 1.00 67.91 C ANISOU 540 CD1 LEU A 80 7210 8209 10383 263 0 -176 C ATOM 541 CD2 LEU A 80 31.680 74.601 100.305 1.00 64.24 C ANISOU 541 CD2 LEU A 80 6844 7551 10013 349 -2 -298 C ATOM 542 N PRO A 81 36.282 73.285 102.542 1.00 85.99 N ANISOU 542 N PRO A 81 8839 9907 13928 431 -350 382 N ATOM 543 CA PRO A 81 37.371 72.327 102.283 1.00 91.21 C ANISOU 543 CA PRO A 81 9282 10393 14982 572 -277 470 C ATOM 544 C PRO A 81 37.106 70.950 102.868 1.00 89.96 C ANISOU 544 C PRO A 81 9153 10082 14945 582 -398 502 C ATOM 545 O PRO A 81 37.417 69.940 102.224 1.00 97.74 O ANISOU 545 O PRO A 81 10070 10918 16147 735 -245 442 O ATOM 546 CB PRO A 81 38.595 72.999 102.924 1.00 93.81 C ANISOU 546 CB PRO A 81 9374 10706 15562 517 -436 704 C ATOM 547 CG PRO A 81 38.037 73.998 103.878 1.00 92.20 C ANISOU 547 CG PRO A 81 9318 10635 15080 324 -679 741 C ATOM 548 CD PRO A 81 36.778 74.484 103.241 1.00 85.97 C ANISOU 548 CD PRO A 81 8769 9987 13908 309 -521 521 C ATOM 549 N PHE A 82 36.532 70.879 104.072 1.00 80.46 N ANISOU 549 N PHE A 82 8059 8907 13607 429 -660 599 N ATOM 550 CA PHE A 82 36.190 69.582 104.647 1.00 82.29 C ANISOU 550 CA PHE A 82 8326 8996 13945 427 -773 654 C ATOM 551 C PHE A 82 35.072 68.909 103.862 1.00 78.41 C ANISOU 551 C PHE A 82 8006 8475 13312 481 -610 431 C ATOM 552 O PHE A 82 35.069 67.683 103.702 1.00 80.26 O ANISOU 552 O PHE A 82 8213 8529 13753 563 -588 412 O ATOM 553 CB PHE A 82 35.786 69.741 106.112 1.00 78.21 C ANISOU 553 CB PHE A 82 7912 8538 13268 251 -1065 823 C ATOM 554 CG PHE A 82 36.878 70.281 106.986 1.00 77.19 C ANISOU 554 CG PHE A 82 7640 8409 13281 184 -1296 1045 C ATOM 555 CD1 PHE A 82 37.809 69.430 107.558 1.00 76.83 C ANISOU 555 CD1 PHE A 82 7412 8195 13585 214 -1461 1255 C ATOM 556 CD2 PHE A 82 36.972 71.638 107.240 1.00 72.29 C ANISOU 556 CD2 PHE A 82 7066 7938 12465 88 -1372 1048 C ATOM 557 CE1 PHE A 82 38.815 69.924 108.363 1.00 82.92 C ANISOU 557 CE1 PHE A 82 8047 8955 14504 142 -1716 1470 C ATOM 558 CE2 PHE A 82 37.975 72.139 108.044 1.00 71.41 C ANISOU 558 CE2 PHE A 82 6830 7805 12496 14 -1625 1246 C ATOM 559 CZ PHE A 82 38.898 71.281 108.607 1.00 80.46 C ANISOU 559 CZ PHE A 82 7794 8790 13988 37 -1808 1460 C ATOM 560 N LEU A 83 34.112 69.695 103.370 1.00 76.69 N ANISOU 560 N LEU A 83 7962 8415 12763 434 -514 265 N ATOM 561 CA LEU A 83 33.028 69.126 102.577 1.00 71.65 C ANISOU 561 CA LEU A 83 7484 7745 11995 473 -394 54 C ATOM 562 C LEU A 83 33.555 68.547 101.271 1.00 69.70 C ANISOU 562 C LEU A 83 7190 7378 11914 666 -168 -109 C ATOM 563 O LEU A 83 33.108 67.482 100.832 1.00 72.71 O ANISOU 563 O LEU A 83 7645 7609 12372 733 -132 -234 O ATOM 564 CB LEU A 83 31.963 70.189 102.311 1.00 69.95 C ANISOU 564 CB LEU A 83 7438 7724 11414 384 -353 -67 C ATOM 565 CG LEU A 83 30.559 69.680 101.979 1.00 66.01 C ANISOU 565 CG LEU A 83 7111 7207 10761 349 -342 -215 C ATOM 566 CD1 LEU A 83 30.022 68.822 103.115 1.00 68.39 C ANISOU 566 CD1 LEU A 83 7429 7420 11136 251 -519 -69 C ATOM 567 CD2 LEU A 83 29.627 70.845 101.700 1.00 61.06 C ANISOU 567 CD2 LEU A 83 6615 6773 9813 272 -300 -309 C ATOM 568 N MET A 84 34.509 69.233 100.637 1.00 75.74 N ANISOU 568 N MET A 84 7840 8199 12741 761 -8 -109 N ATOM 569 CA MET A 84 35.155 68.670 99.457 1.00 87.64 C ANISOU 569 CA MET A 84 9298 9588 14412 970 242 -240 C ATOM 570 C MET A 84 35.841 67.351 99.785 1.00 99.00 C ANISOU 570 C MET A 84 10597 10785 16235 1067 203 -156 C ATOM 571 O MET A 84 35.755 66.389 99.014 1.00101.46 O ANISOU 571 O MET A 84 10974 10937 16638 1211 338 -326 O ATOM 572 CB MET A 84 36.160 69.664 98.878 1.00 94.83 C ANISOU 572 CB MET A 84 10065 10600 15365 1050 429 -186 C ATOM 573 CG MET A 84 35.619 70.513 97.748 1.00104.36 C ANISOU 573 CG MET A 84 11439 11968 16246 1085 628 -371 C ATOM 574 SD MET A 84 36.868 71.653 97.136 1.00116.27 S ANISOU 574 SD MET A 84 12744 13579 17853 1174 856 -252 S ATOM 575 CE MET A 84 37.083 72.700 98.572 1.00113.56 C ANISOU 575 CE MET A 84 12264 13333 17550 947 547 0 C ATOM 576 N ASP A 85 36.516 67.285 100.937 1.00 98.69 N ANISOU 576 N ASP A 85 10373 10701 16423 991 1 102 N ATOM 577 CA ASP A 85 37.202 66.059 101.330 1.00 96.95 C ANISOU 577 CA ASP A 85 9996 10243 16599 1076 -62 220 C ATOM 578 C ASP A 85 36.225 64.910 101.548 1.00 92.78 C ANISOU 578 C ASP A 85 9621 9572 16059 1044 -167 137 C ATOM 579 O ASP A 85 36.601 63.741 101.405 1.00 90.71 O ANISOU 579 O ASP A 85 9285 9073 16106 1166 -139 129 O ATOM 580 CB ASP A 85 38.025 66.304 102.596 1.00 96.68 C ANISOU 580 CB ASP A 85 9756 10206 16772 972 -314 534 C ATOM 581 CG ASP A 85 38.796 65.074 103.039 1.00100.47 C ANISOU 581 CG ASP A 85 10046 10433 17693 1059 -401 693 C ATOM 582 OD1 ASP A 85 39.847 64.779 102.432 1.00102.66 O ANISOU 582 OD1 ASP A 85 10118 10584 18302 1238 -221 711 O ATOM 583 OD2 ASP A 85 38.348 64.401 103.991 1.00101.15 O ANISOU 583 OD2 ASP A 85 10183 10444 17804 954 -637 814 O ATOM 584 N ASN A 86 34.974 65.217 101.893 1.00 84.74 N ANISOU 584 N ASN A 86 8803 8677 14719 885 -284 83 N ATOM 585 CA ASN A 86 33.989 64.162 102.102 1.00 85.31 C ANISOU 585 CA ASN A 86 9001 8610 14804 839 -386 28 C ATOM 586 C ASN A 86 33.413 63.667 100.780 1.00 83.73 C ANISOU 586 C ASN A 86 8958 8317 14538 959 -207 -283 C ATOM 587 O ASN A 86 33.240 62.457 100.591 1.00 85.06 O ANISOU 587 O ASN A 86 9151 8250 14917 1026 -228 -356 O ATOM 588 CB ASN A 86 32.870 64.659 103.018 1.00 84.24 C ANISOU 588 CB ASN A 86 8994 8634 14381 629 -564 118 C ATOM 589 CG ASN A 86 32.072 63.525 103.633 1.00 84.88 C ANISOU 589 CG ASN A 86 9127 8555 14567 555 -713 190 C ATOM 590 OD1 ASN A 86 32.635 62.520 104.068 1.00 88.22 O ANISOU 590 OD1 ASN A 86 9433 8776 15310 601 -799 325 O ATOM 591 ND2 ASN A 86 30.753 63.679 103.669 1.00 83.03 N ANISOU 591 ND2 ASN A 86 9052 8402 14093 441 -744 117 N ATOM 592 N TYR A 87 33.119 64.582 99.853 1.00 81.26 N ANISOU 592 N TYR A 87 8765 8175 13936 986 -47 -467 N ATOM 593 CA TYR A 87 32.528 64.178 98.581 1.00 85.77 C ANISOU 593 CA TYR A 87 9527 8672 14390 1092 93 -769 C ATOM 594 C TYR A 87 33.529 63.445 97.696 1.00 93.27 C ANISOU 594 C TYR A 87 10426 9432 15581 1333 304 -893 C ATOM 595 O TYR A 87 33.132 62.587 96.899 1.00 97.94 O ANISOU 595 O TYR A 87 11173 9849 16190 1433 358 -1127 O ATOM 596 CB TYR A 87 31.957 65.396 97.852 1.00 88.10 C ANISOU 596 CB TYR A 87 9969 9209 14297 1055 193 -905 C ATOM 597 CG TYR A 87 30.613 65.859 98.383 1.00 91.83 C ANISOU 597 CG TYR A 87 10556 9812 14523 852 17 -882 C ATOM 598 CD1 TYR A 87 30.497 66.398 99.658 1.00 89.36 C ANISOU 598 CD1 TYR A 87 10154 9616 14183 692 -137 -644 C ATOM 599 CD2 TYR A 87 29.464 65.764 97.608 1.00 95.78 C ANISOU 599 CD2 TYR A 87 11259 10312 14822 827 4 -1095 C ATOM 600 CE1 TYR A 87 29.277 66.824 100.149 1.00 87.78 C ANISOU 600 CE1 TYR A 87 10054 9531 13766 528 -256 -617 C ATOM 601 CE2 TYR A 87 28.235 66.189 98.092 1.00 94.46 C ANISOU 601 CE2 TYR A 87 11161 10253 14474 650 -141 -1053 C ATOM 602 CZ TYR A 87 28.150 66.719 99.364 1.00 89.83 C ANISOU 602 CZ TYR A 87 10475 9785 13871 509 -249 -812 C ATOM 603 OH TYR A 87 26.938 67.147 99.859 1.00 88.93 O ANISOU 603 OH TYR A 87 10427 9777 13586 354 -352 -764 O ATOM 604 N VAL A 88 34.821 63.757 97.815 1.00 96.30 N ANISOU 604 N VAL A 88 10595 9831 16165 1432 425 -743 N ATOM 605 CA VAL A 88 35.812 63.024 97.034 1.00 99.74 C ANISOU 605 CA VAL A 88 10954 10071 16870 1680 659 -837 C ATOM 606 C VAL A 88 36.027 61.633 97.615 1.00104.92 C ANISOU 606 C VAL A 88 11515 10433 17919 1720 528 -764 C ATOM 607 O VAL A 88 36.381 60.696 96.888 1.00107.17 O ANISOU 607 O VAL A 88 11835 10489 18398 1920 684 -933 O ATOM 608 CB VAL A 88 37.134 63.811 96.948 1.00101.67 C ANISOU 608 CB VAL A 88 10959 10415 17256 1777 845 -671 C ATOM 609 CG1 VAL A 88 36.904 65.160 96.284 1.00105.51 C ANISOU 609 CG1 VAL A 88 11547 11173 17368 1744 987 -744 C ATOM 610 CG2 VAL A 88 37.753 63.982 98.327 1.00100.94 C ANISOU 610 CG2 VAL A 88 10603 10329 17422 1645 611 -329 C ATOM 611 N ARG A 89 35.813 61.468 98.920 1.00104.26 N ANISOU 611 N ARG A 89 11325 10339 17948 1540 246 -515 N ATOM 612 CA ARG A 89 35.944 60.177 99.578 1.00 98.97 C ANISOU 612 CA ARG A 89 10562 9395 17648 1553 89 -402 C ATOM 613 C ARG A 89 34.627 59.414 99.636 1.00 92.33 C ANISOU 613 C ARG A 89 9925 8439 16715 1448 -71 -528 C ATOM 614 O ARG A 89 34.517 58.448 100.400 1.00 96.07 O ANISOU 614 O ARG A 89 10329 8715 17460 1397 -255 -381 O ATOM 615 CB ARG A 89 36.510 60.356 100.988 1.00 99.88 C ANISOU 615 CB ARG A 89 10451 9550 17947 1422 -139 -29 C ATOM 616 CG ARG A 89 37.934 60.882 101.014 1.00105.69 C ANISOU 616 CG ARG A 89 10928 10323 18906 1528 -31 135 C ATOM 617 CD ARG A 89 38.511 60.860 102.418 1.00111.10 C ANISOU 617 CD ARG A 89 11403 10995 19816 1402 -313 501 C ATOM 618 NE ARG A 89 39.861 61.416 102.458 1.00114.89 N ANISOU 618 NE ARG A 89 11612 11503 20539 1484 -248 674 N ATOM 619 CZ ARG A 89 40.959 60.738 102.140 1.00118.56 C ANISOU 619 CZ ARG A 89 11843 11750 21456 1682 -117 736 C ATOM 620 NH1 ARG A 89 40.870 59.472 101.753 1.00122.50 N ANISOU 620 NH1 ARG A 89 12370 11980 22193 1827 -36 616 N ATOM 621 NH2 ARG A 89 42.146 61.325 102.206 1.00118.21 N ANISOU 621 NH2 ARG A 89 11526 11740 21650 1738 -68 922 N ATOM 622 N ARG A 90 33.632 59.828 98.850 1.00 88.70 N ANISOU 622 N ARG A 90 9705 8093 15906 1409 -18 -776 N ATOM 623 CA ARG A 90 32.340 59.149 98.783 1.00 94.70 C ANISOU 623 CA ARG A 90 10648 8735 16599 1306 -174 -906 C ATOM 624 C ARG A 90 31.685 59.087 100.162 1.00 98.29 C ANISOU 624 C ARG A 90 11031 9236 17080 1078 -434 -621 C ATOM 625 O ARG A 90 31.219 58.038 100.612 1.00107.18 O ANISOU 625 O ARG A 90 12151 10143 18431 1024 -591 -556 O ATOM 626 CB ARG A 90 32.491 57.754 98.175 1.00101.89 C ANISOU 626 CB ARG A 90 11611 9288 17815 1468 -143 -1092 C ATOM 627 CG ARG A 90 33.151 57.767 96.809 1.00111.95 C ANISOU 627 CG ARG A 90 12989 10510 19037 1719 147 -1384 C ATOM 628 CD ARG A 90 33.946 56.499 96.563 1.00124.22 C ANISOU 628 CD ARG A 90 14474 11712 21012 1929 229 -1452 C ATOM 629 NE ARG A 90 34.589 56.512 95.253 1.00132.42 N ANISOU 629 NE ARG A 90 15632 12705 21979 2193 548 -1735 N ATOM 630 CZ ARG A 90 34.028 56.043 94.144 1.00140.81 C ANISOU 630 CZ ARG A 90 16991 13633 22880 2297 611 -2100 C ATOM 631 NH1 ARG A 90 32.809 55.523 94.186 1.00140.85 N ANISOU 631 NH1 ARG A 90 17173 13522 22820 2146 353 -2217 N ATOM 632 NH2 ARG A 90 34.684 56.095 92.993 1.00147.27 N ANISOU 632 NH2 ARG A 90 17931 14425 23599 2552 931 -2341 N ATOM 633 N TRP A 91 31.673 60.238 100.839 1.00 91.71 N ANISOU 633 N TRP A 91 10149 8683 16012 951 -470 -444 N ATOM 634 CA TRP A 91 31.053 60.406 102.152 1.00 88.40 C ANISOU 634 CA TRP A 91 9700 8364 15525 743 -677 -178 C ATOM 635 C TRP A 91 31.755 59.589 103.232 1.00 89.16 C ANISOU 635 C TRP A 91 9619 8296 15960 734 -825 111 C ATOM 636 O TRP A 91 31.139 59.208 104.229 1.00 95.62 O ANISOU 636 O TRP A 91 10439 9092 16800 590 -1000 317 O ATOM 637 CB TRP A 91 29.559 60.070 102.112 1.00 88.45 C ANISOU 637 CB TRP A 91 9858 8338 15412 614 -775 -259 C ATOM 638 CG TRP A 91 28.811 60.844 101.071 1.00 94.72 C ANISOU 638 CG TRP A 91 10823 9282 15886 613 -670 -525 C ATOM 639 CD1 TRP A 91 29.166 62.044 100.527 1.00 96.93 C ANISOU 639 CD1 TRP A 91 11136 9792 15901 658 -523 -618 C ATOM 640 CD2 TRP A 91 27.586 60.462 100.436 1.00 98.41 C ANISOU 640 CD2 TRP A 91 11442 9664 16285 560 -725 -715 C ATOM 641 NE1 TRP A 91 28.234 62.437 99.598 1.00 97.45 N ANISOU 641 NE1 TRP A 91 11376 9931 15720 641 -480 -850 N ATOM 642 CE2 TRP A 91 27.254 61.483 99.523 1.00 97.79 C ANISOU 642 CE2 TRP A 91 11493 9782 15878 579 -613 -917 C ATOM 643 CE3 TRP A 91 26.735 59.359 100.553 1.00104.90 C ANISOU 643 CE3 TRP A 91 12293 10250 17313 491 -876 -720 C ATOM 644 CZ2 TRP A 91 26.108 61.432 98.732 1.00 99.35 C ANISOU 644 CZ2 TRP A 91 11855 9955 15940 533 -665 -1124 C ATOM 645 CZ3 TRP A 91 25.598 59.311 99.768 1.00104.72 C ANISOU 645 CZ3 TRP A 91 12421 10192 17175 439 -928 -930 C ATOM 646 CH2 TRP A 91 25.295 60.341 98.869 1.00102.69 C ANISOU 646 CH2 TRP A 91 12297 10140 16580 460 -831 -1131 C ATOM 647 N ASP A 92 33.043 59.310 103.047 1.00 89.24 N ANISOU 647 N ASP A 92 9471 8189 16247 891 -751 148 N ATOM 648 CA ASP A 92 33.860 58.684 104.081 1.00 94.07 C ANISOU 648 CA ASP A 92 9889 8664 17189 887 -907 452 C ATOM 649 C ASP A 92 34.449 59.793 104.944 1.00 93.81 C ANISOU 649 C ASP A 92 9766 8876 17002 791 -995 683 C ATOM 650 O ASP A 92 35.387 60.481 104.530 1.00 98.60 O ANISOU 650 O ASP A 92 10266 9565 17633 885 -877 656 O ATOM 651 CB ASP A 92 34.957 57.821 103.463 1.00 97.28 C ANISOU 651 CB ASP A 92 10145 8801 18015 1110 -789 390 C ATOM 652 CG ASP A 92 35.699 56.994 104.496 1.00 94.78 C ANISOU 652 CG ASP A 92 9623 8295 18095 1108 -977 711 C ATOM 653 OD1 ASP A 92 35.123 56.730 105.573 1.00 89.96 O ANISOU 653 OD1 ASP A 92 9039 7696 17447 938 -1202 941 O ATOM 654 OD2 ASP A 92 36.862 56.617 104.234 1.00 93.18 O ANISOU 654 OD2 ASP A 92 9229 7931 18245 1280 -893 748 O ATOM 655 N TRP A 93 33.894 59.975 106.139 1.00 88.51 N ANISOU 655 N TRP A 93 9145 8315 16171 607 -1199 912 N ATOM 656 CA TRP A 93 34.297 61.063 107.026 1.00 88.24 C ANISOU 656 CA TRP A 93 9085 8512 15929 498 -1317 1106 C ATOM 657 C TRP A 93 35.575 60.664 107.749 1.00 93.54 C ANISOU 657 C TRP A 93 9540 9058 16941 538 -1479 1379 C ATOM 658 O TRP A 93 35.537 59.987 108.779 1.00 88.65 O ANISOU 658 O TRP A 93 8899 8347 16435 460 -1689 1634 O ATOM 659 CB TRP A 93 33.177 61.390 108.005 1.00 83.81 C ANISOU 659 CB TRP A 93 8695 8111 15036 305 -1450 1230 C ATOM 660 CG TRP A 93 33.428 62.620 108.816 1.00 84.69 C ANISOU 660 CG TRP A 93 8849 8471 14860 196 -1555 1361 C ATOM 661 CD1 TRP A 93 33.688 62.679 110.152 1.00 90.11 C ANISOU 661 CD1 TRP A 93 9544 9206 15489 88 -1787 1651 C ATOM 662 CD2 TRP A 93 33.451 63.972 108.342 1.00 81.07 C ANISOU 662 CD2 TRP A 93 8447 8231 14127 187 -1446 1203 C ATOM 663 NE1 TRP A 93 33.869 63.984 110.542 1.00 89.99 N ANISOU 663 NE1 TRP A 93 9599 9416 15176 12 -1839 1661 N ATOM 664 CE2 TRP A 93 33.728 64.798 109.449 1.00 82.06 C ANISOU 664 CE2 TRP A 93 8612 8513 14052 69 -1630 1394 C ATOM 665 CE3 TRP A 93 33.260 64.564 107.090 1.00 79.91 C ANISOU 665 CE3 TRP A 93 8332 8154 13875 266 -1221 924 C ATOM 666 CZ2 TRP A 93 33.821 66.184 109.342 1.00 75.67 C ANISOU 666 CZ2 TRP A 93 7862 7910 12980 27 -1598 1307 C ATOM 667 CZ3 TRP A 93 33.354 65.939 106.985 1.00 73.78 C ANISOU 667 CZ3 TRP A 93 7600 7594 12837 223 -1180 863 C ATOM 668 CH2 TRP A 93 33.632 66.734 108.105 1.00 69.86 C ANISOU 668 CH2 TRP A 93 7130 7233 12180 104 -1368 1050 C ATOM 669 N LYS A 94 36.719 61.096 107.213 1.00 99.00 N ANISOU 669 N LYS A 94 10062 9745 17809 659 -1383 1348 N ATOM 670 CA LYS A 94 38.000 60.753 107.818 1.00102.34 C ANISOU 670 CA LYS A 94 10240 10036 18610 705 -1540 1614 C ATOM 671 C LYS A 94 38.245 61.501 109.122 1.00108.05 C ANISOU 671 C LYS A 94 10972 10924 19157 531 -1832 1888 C ATOM 672 O LYS A 94 39.143 61.119 109.878 1.00123.47 O ANISOU 672 O LYS A 94 12752 12764 21397 527 -2051 2160 O ATOM 673 CB LYS A 94 39.136 61.037 106.837 1.00102.96 C ANISOU 673 CB LYS A 94 10110 10060 18952 890 -1328 1516 C ATOM 674 N PHE A 95 37.471 62.548 109.404 1.00 98.92 N ANISOU 674 N PHE A 95 10022 10022 17540 392 -1850 1819 N ATOM 675 CA PHE A 95 37.667 63.349 110.602 1.00 93.35 C ANISOU 675 CA PHE A 95 9377 9478 16614 234 -2119 2034 C ATOM 676 C PHE A 95 36.886 62.747 111.771 1.00102.35 C ANISOU 676 C PHE A 95 10684 10616 17587 106 -2316 2231 C ATOM 677 O PHE A 95 36.195 61.737 111.636 1.00107.00 O ANISOU 677 O PHE A 95 11315 11076 18265 131 -2245 2212 O ATOM 678 CB PHE A 95 37.272 64.798 110.326 1.00 79.35 C ANISOU 678 CB PHE A 95 7745 7958 14445 166 -2027 1860 C ATOM 679 CG PHE A 95 37.795 65.319 109.019 1.00 74.92 C ANISOU 679 CG PHE A 95 7052 7405 14010 298 -1770 1650 C ATOM 680 CD1 PHE A 95 39.142 65.600 108.861 1.00 74.45 C ANISOU 680 CD1 PHE A 95 6737 7281 14271 368 -1806 1758 C ATOM 681 CD2 PHE A 95 36.946 65.507 107.941 1.00 69.75 C ANISOU 681 CD2 PHE A 95 6523 6817 13163 354 -1493 1362 C ATOM 682 CE1 PHE A 95 39.631 66.072 107.656 1.00 72.54 C ANISOU 682 CE1 PHE A 95 6369 7050 14143 499 -1535 1591 C ATOM 683 CE2 PHE A 95 37.429 65.980 106.733 1.00 67.14 C ANISOU 683 CE2 PHE A 95 6095 6502 12914 483 -1245 1184 C ATOM 684 CZ PHE A 95 38.774 66.262 106.591 1.00 69.78 C ANISOU 684 CZ PHE A 95 6176 6780 13556 560 -1248 1302 C ATOM 685 N GLY A 96 36.999 63.373 112.942 1.00105.34 N ANISOU 685 N GLY A 96 11170 11135 17720 -32 -2569 2427 N ATOM 686 CA GLY A 96 36.501 62.800 114.174 1.00112.38 C ANISOU 686 CA GLY A 96 12209 12024 18468 -142 -2776 2677 C ATOM 687 C GLY A 96 35.032 63.073 114.426 1.00114.08 C ANISOU 687 C GLY A 96 12699 12405 18240 -235 -2653 2585 C ATOM 688 O GLY A 96 34.289 63.538 113.560 1.00112.84 O ANISOU 688 O GLY A 96 12609 12335 17929 -210 -2407 2317 O ATOM 689 N ASP A 97 34.615 62.765 115.658 1.00115.06 N ANISOU 689 N ASP A 97 12983 12571 18165 -342 -2829 2835 N ATOM 690 CA ASP A 97 33.235 62.984 116.077 1.00109.64 C ANISOU 690 CA ASP A 97 12548 12040 17071 -429 -2709 2810 C ATOM 691 C ASP A 97 32.914 64.472 116.144 1.00107.30 C ANISOU 691 C ASP A 97 12435 11996 16339 -485 -2653 2640 C ATOM 692 O ASP A 97 31.965 64.946 115.508 1.00103.75 O ANISOU 692 O ASP A 97 12066 11647 15707 -481 -2414 2415 O ATOM 693 CB ASP A 97 33.000 62.314 117.436 1.00111.02 C ANISOU 693 CB ASP A 97 12850 12201 17132 -517 -2903 3155 C ATOM 694 CG ASP A 97 31.633 62.639 118.038 1.00111.67 C ANISOU 694 CG ASP A 97 13199 12465 16766 -605 -2768 3175 C ATOM 695 OD1 ASP A 97 30.701 63.011 117.294 1.00110.41 O ANISOU 695 OD1 ASP A 97 13075 12378 16497 -591 -2511 2936 O ATOM 696 OD2 ASP A 97 31.492 62.522 119.273 1.00115.13 O ANISOU 696 OD2 ASP A 97 13812 12973 16958 -683 -2917 3443 O ATOM 697 N ILE A 98 33.695 65.225 116.922 1.00108.20 N ANISOU 697 N ILE A 98 12617 12199 16295 -542 -2893 2748 N ATOM 698 CA ILE A 98 33.429 66.657 117.077 1.00106.46 C ANISOU 698 CA ILE A 98 12588 12194 15666 -598 -2869 2591 C ATOM 699 C ILE A 98 33.527 67.408 115.757 1.00106.01 C ANISOU 699 C ILE A 98 12404 12166 15707 -529 -2659 2289 C ATOM 700 O ILE A 98 32.671 68.267 115.496 1.00104.28 O ANISOU 700 O ILE A 98 12337 12102 15184 -550 -2483 2099 O ATOM 701 CB ILE A 98 34.322 67.245 118.177 1.00107.03 C ANISOU 701 CB ILE A 98 12764 12319 15583 -678 -3217 2766 C ATOM 702 CG1 ILE A 98 34.088 66.508 119.500 1.00109.67 C ANISOU 702 CG1 ILE A 98 13277 12649 15745 -745 -3407 3073 C ATOM 703 CG2 ILE A 98 34.062 68.734 118.343 1.00100.79 C ANISOU 703 CG2 ILE A 98 12184 11723 14387 -733 -3206 2586 C ATOM 704 CD1 ILE A 98 34.999 66.954 120.627 1.00114.37 C ANISOU 704 CD1 ILE A 98 13996 13275 16184 -826 -3804 3266 C ATOM 705 N PRO A 99 34.516 67.164 114.883 1.00108.97 N ANISOU 705 N PRO A 99 12510 12402 16490 -437 -2649 2238 N ATOM 706 CA PRO A 99 34.526 67.877 113.593 1.00109.72 C ANISOU 706 CA PRO A 99 12512 12541 16636 -364 -2413 1960 C ATOM 707 C PRO A 99 33.276 67.662 112.757 1.00108.17 C ANISOU 707 C PRO A 99 12390 12376 16332 -326 -2118 1750 C ATOM 708 O PRO A 99 32.926 68.535 111.952 1.00117.31 O ANISOU 708 O PRO A 99 13580 13641 17350 -305 -1941 1527 O ATOM 709 CB PRO A 99 35.771 67.315 112.895 1.00113.67 C ANISOU 709 CB PRO A 99 12706 12853 17628 -251 -2426 1997 C ATOM 710 CG PRO A 99 36.670 66.944 114.002 1.00117.00 C ANISOU 710 CG PRO A 99 13068 13192 18196 -304 -2761 2293 C ATOM 711 CD PRO A 99 35.771 66.412 115.083 1.00114.45 C ANISOU 711 CD PRO A 99 12976 12910 17599 -395 -2861 2446 C ATOM 712 N CYS A 100 32.588 66.531 112.916 1.00101.98 N ANISOU 712 N CYS A 100 11629 11492 15627 -323 -2076 1827 N ATOM 713 CA CYS A 100 31.377 66.309 112.134 1.00 93.45 C ANISOU 713 CA CYS A 100 10609 10422 14475 -301 -1836 1637 C ATOM 714 C CYS A 100 30.188 67.069 112.710 1.00 84.05 C ANISOU 714 C CYS A 100 9647 9428 12860 -399 -1773 1617 C ATOM 715 O CYS A 100 29.410 67.662 111.955 1.00 83.34 O ANISOU 715 O CYS A 100 9609 9428 12628 -389 -1587 1405 O ATOM 716 CB CYS A 100 31.062 64.816 112.049 1.00 95.67 C ANISOU 716 CB CYS A 100 10813 10495 15043 -267 -1825 1725 C ATOM 717 SG CYS A 100 29.487 64.464 111.239 1.00 89.99 S ANISOU 717 SG CYS A 100 10172 9762 14257 -272 -1597 1528 S ATOM 718 N ARG A 101 30.028 67.060 114.037 1.00 80.43 N ANISOU 718 N ARG A 101 9333 9035 12192 -486 -1920 1841 N ATOM 719 CA ARG A 101 28.925 67.796 114.648 1.00 81.45 C ANISOU 719 CA ARG A 101 9689 9349 11910 -559 -1829 1830 C ATOM 720 C ARG A 101 29.030 69.287 114.358 1.00 82.30 C ANISOU 720 C ARG A 101 9878 9618 11775 -564 -1785 1633 C ATOM 721 O ARG A 101 28.019 69.950 114.100 1.00 81.32 O ANISOU 721 O ARG A 101 9858 9612 11428 -576 -1605 1492 O ATOM 722 CB ARG A 101 28.894 67.561 116.158 1.00 85.22 C ANISOU 722 CB ARG A 101 10336 9873 12173 -635 -1995 2112 C ATOM 723 CG ARG A 101 28.766 66.113 116.595 1.00 89.82 C ANISOU 723 CG ARG A 101 10850 10297 12982 -643 -2052 2358 C ATOM 724 CD ARG A 101 28.383 66.052 118.066 1.00 95.25 C ANISOU 724 CD ARG A 101 11764 11083 13344 -720 -2141 2626 C ATOM 725 NE ARG A 101 28.714 64.773 118.687 1.00102.59 N ANISOU 725 NE ARG A 101 12627 11857 14495 -734 -2294 2925 N ATOM 726 CZ ARG A 101 28.407 64.455 119.941 1.00108.85 C ANISOU 726 CZ ARG A 101 13602 12707 15050 -794 -2371 3210 C ATOM 727 NH1 ARG A 101 27.755 65.323 120.704 1.00110.99 N ANISOU 727 NH1 ARG A 101 14145 13186 14839 -835 -2289 3215 N ATOM 728 NH2 ARG A 101 28.748 63.272 120.432 1.00110.67 N ANISOU 728 NH2 ARG A 101 13752 12780 15518 -806 -2519 3494 N ATOM 729 N LEU A 102 30.248 69.832 114.399 1.00 80.53 N ANISOU 729 N LEU A 102 9591 9387 11621 -557 -1956 1635 N ATOM 730 CA LEU A 102 30.426 71.260 114.165 1.00 73.91 C ANISOU 730 CA LEU A 102 8819 8678 10585 -571 -1941 1468 C ATOM 731 C LEU A 102 30.134 71.626 112.715 1.00 75.43 C ANISOU 731 C LEU A 102 8894 8877 10888 -501 -1708 1220 C ATOM 732 O LEU A 102 29.552 72.682 112.443 1.00 77.49 O ANISOU 732 O LEU A 102 9256 9265 10921 -515 -1592 1065 O ATOM 733 CB LEU A 102 31.842 71.683 114.553 1.00 71.59 C ANISOU 733 CB LEU A 102 8453 8346 10402 -591 -2208 1558 C ATOM 734 CG LEU A 102 32.177 71.606 116.043 1.00 74.15 C ANISOU 734 CG LEU A 102 8949 8687 10537 -675 -2493 1786 C ATOM 735 CD1 LEU A 102 33.647 71.909 116.275 1.00 74.06 C ANISOU 735 CD1 LEU A 102 8810 8600 10730 -697 -2791 1883 C ATOM 736 CD2 LEU A 102 31.299 72.562 116.836 1.00 78.55 C ANISOU 736 CD2 LEU A 102 9822 9416 10607 -737 -2462 1727 C ATOM 737 N MET A 103 30.527 70.767 111.771 1.00 73.29 N ANISOU 737 N MET A 103 8423 8466 10957 -417 -1637 1180 N ATOM 738 CA MET A 103 30.287 71.069 110.364 1.00 69.84 C ANISOU 738 CA MET A 103 7905 8037 10595 -342 -1422 947 C ATOM 739 C MET A 103 28.796 71.088 110.048 1.00 70.65 C ANISOU 739 C MET A 103 8128 8207 10509 -361 -1245 829 C ATOM 740 O MET A 103 28.324 71.960 109.311 1.00 75.67 O ANISOU 740 O MET A 103 8800 8940 11010 -348 -1109 651 O ATOM 741 CB MET A 103 31.005 70.060 109.471 1.00 60.35 C ANISOU 741 CB MET A 103 6501 6657 9773 -233 -1373 922 C ATOM 742 CG MET A 103 31.037 70.473 108.010 1.00 61.41 C ANISOU 742 CG MET A 103 6568 6806 9961 -139 -1166 689 C ATOM 743 SD MET A 103 31.324 69.112 106.867 1.00 75.72 S ANISOU 743 SD MET A 103 8239 8405 12124 5 -1037 592 S ATOM 744 CE MET A 103 29.808 68.181 107.072 1.00 71.39 C ANISOU 744 CE MET A 103 7823 7802 11499 -53 -1022 575 C ATOM 745 N LEU A 104 28.040 70.132 110.592 1.00 68.16 N ANISOU 745 N LEU A 104 7858 7832 10205 -395 -1251 946 N ATOM 746 CA LEU A 104 26.597 70.130 110.378 1.00 71.72 C ANISOU 746 CA LEU A 104 8395 8335 10519 -424 -1098 871 C ATOM 747 C LEU A 104 25.945 71.340 111.033 1.00 68.59 C ANISOU 747 C LEU A 104 8168 8127 9766 -484 -1053 862 C ATOM 748 O LEU A 104 25.018 71.935 110.471 1.00 71.20 O ANISOU 748 O LEU A 104 8536 8536 9980 -484 -905 721 O ATOM 749 CB LEU A 104 25.986 68.834 110.912 1.00 73.45 C ANISOU 749 CB LEU A 104 8604 8436 10868 -456 -1122 1040 C ATOM 750 CG LEU A 104 26.474 67.526 110.287 1.00 70.70 C ANISOU 750 CG LEU A 104 8102 7866 10896 -393 -1162 1042 C ATOM 751 CD1 LEU A 104 25.744 66.339 110.898 1.00 69.25 C ANISOU 751 CD1 LEU A 104 7914 7561 10836 -443 -1192 1229 C ATOM 752 CD2 LEU A 104 26.302 67.545 108.774 1.00 49.86 C ANISOU 752 CD2 LEU A 104 5399 5173 8373 -315 -1035 773 C ATOM 753 N PHE A 105 26.421 71.720 112.220 1.00 64.86 N ANISOU 753 N PHE A 105 7807 7718 9118 -532 -1191 1008 N ATOM 754 CA PHE A 105 25.891 72.900 112.893 1.00 69.47 C ANISOU 754 CA PHE A 105 8583 8465 9348 -574 -1152 979 C ATOM 755 C PHE A 105 26.155 74.158 112.075 1.00 75.87 C ANISOU 755 C PHE A 105 9375 9347 10103 -549 -1101 769 C ATOM 756 O PHE A 105 25.247 74.964 111.841 1.00 82.17 O ANISOU 756 O PHE A 105 10252 10242 10726 -550 -954 652 O ATOM 757 CB PHE A 105 26.505 73.013 114.289 1.00 70.30 C ANISOU 757 CB PHE A 105 8839 8603 9269 -624 -1350 1162 C ATOM 758 CG PHE A 105 26.137 74.271 115.018 1.00 69.96 C ANISOU 758 CG PHE A 105 9026 8707 8847 -655 -1333 1107 C ATOM 759 CD1 PHE A 105 24.882 74.419 115.584 1.00 72.69 C ANISOU 759 CD1 PHE A 105 9534 9146 8941 -664 -1155 1137 C ATOM 760 CD2 PHE A 105 27.053 75.300 115.154 1.00 73.67 C ANISOU 760 CD2 PHE A 105 9549 9208 9234 -671 -1494 1031 C ATOM 761 CE1 PHE A 105 24.542 75.574 116.260 1.00 74.24 C ANISOU 761 CE1 PHE A 105 9959 9463 8787 -672 -1119 1071 C ATOM 762 CE2 PHE A 105 26.721 76.457 115.829 1.00 77.14 C ANISOU 762 CE2 PHE A 105 10222 9758 9331 -695 -1493 959 C ATOM 763 CZ PHE A 105 25.464 76.594 116.384 1.00 77.96 C ANISOU 763 CZ PHE A 105 10506 9954 9162 -688 -1296 970 C ATOM 764 N MET A 106 27.396 74.330 111.611 1.00 76.72 N ANISOU 764 N MET A 106 9361 9400 10388 -521 -1215 736 N ATOM 765 CA MET A 106 27.748 75.523 110.847 1.00 74.93 C ANISOU 765 CA MET A 106 9100 9233 10135 -501 -1171 571 C ATOM 766 C MET A 106 27.058 75.542 109.489 1.00 70.16 C ANISOU 766 C MET A 106 8416 8636 9607 -444 -962 399 C ATOM 767 O MET A 106 26.700 76.614 108.986 1.00 67.11 O ANISOU 767 O MET A 106 8067 8335 9095 -440 -869 267 O ATOM 768 CB MET A 106 29.265 75.607 110.686 1.00 73.98 C ANISOU 768 CB MET A 106 8836 9040 10235 -484 -1331 619 C ATOM 769 CG MET A 106 30.003 75.767 112.005 1.00 74.97 C ANISOU 769 CG MET A 106 9050 9158 10277 -554 -1593 782 C ATOM 770 SD MET A 106 31.790 75.575 111.869 1.00 79.05 S ANISOU 770 SD MET A 106 9334 9548 11154 -539 -1810 897 S ATOM 771 CE MET A 106 32.225 77.055 110.962 1.00 81.86 C ANISOU 771 CE MET A 106 9613 9959 11530 -529 -1739 735 C ATOM 772 N LEU A 107 26.864 74.372 108.876 1.00 63.09 N ANISOU 772 N LEU A 107 7419 7637 8916 -400 -902 396 N ATOM 773 CA LEU A 107 26.142 74.321 107.608 1.00 58.06 C ANISOU 773 CA LEU A 107 6740 6995 8324 -351 -738 227 C ATOM 774 C LEU A 107 24.694 74.760 107.787 1.00 53.90 C ANISOU 774 C LEU A 107 6325 6559 7594 -397 -636 190 C ATOM 775 O LEU A 107 24.155 75.508 106.963 1.00 47.09 O ANISOU 775 O LEU A 107 5472 5762 6657 -379 -532 49 O ATOM 776 CB LEU A 107 26.210 72.912 107.016 1.00 62.29 C ANISOU 776 CB LEU A 107 7176 7375 9118 -298 -727 223 C ATOM 777 CG LEU A 107 27.168 72.715 105.840 1.00 66.98 C ANISOU 777 CG LEU A 107 7649 7892 9909 -195 -677 110 C ATOM 778 CD1 LEU A 107 28.574 73.132 106.224 1.00 73.93 C ANISOU 778 CD1 LEU A 107 8442 8771 10876 -179 -770 205 C ATOM 779 CD2 LEU A 107 27.151 71.270 105.366 1.00 70.84 C ANISOU 779 CD2 LEU A 107 8074 8202 10641 -136 -670 91 C ATOM 780 N ALA A 108 24.049 74.306 108.863 1.00 52.87 N ANISOU 780 N ALA A 108 6272 6433 7384 -451 -657 334 N ATOM 781 CA ALA A 108 22.689 74.743 109.154 1.00 53.61 C ANISOU 781 CA ALA A 108 6454 6611 7305 -485 -535 330 C ATOM 782 C ALA A 108 22.662 76.180 109.653 1.00 57.05 C ANISOU 782 C ALA A 108 7017 7181 7479 -499 -510 286 C ATOM 783 O ALA A 108 21.702 76.912 109.386 1.00 59.33 O ANISOU 783 O ALA A 108 7341 7540 7659 -497 -382 205 O ATOM 784 CB ALA A 108 22.045 73.812 110.176 1.00 51.92 C ANISOU 784 CB ALA A 108 6278 6359 7090 -530 -533 525 C ATOM 785 N MET A 109 23.702 76.600 110.376 1.00 56.60 N ANISOU 785 N MET A 109 7027 7143 7337 -513 -647 337 N ATOM 786 CA MET A 109 23.781 77.989 110.816 1.00 60.03 C ANISOU 786 CA MET A 109 7595 7675 7541 -527 -656 271 C ATOM 787 C MET A 109 23.925 78.936 109.632 1.00 63.26 C ANISOU 787 C MET A 109 7922 8108 8004 -495 -596 100 C ATOM 788 O MET A 109 23.366 80.039 109.640 1.00 64.51 O ANISOU 788 O MET A 109 8165 8340 8005 -496 -517 14 O ATOM 789 CB MET A 109 24.945 78.164 111.787 1.00 61.98 C ANISOU 789 CB MET A 109 7922 7908 7718 -561 -869 363 C ATOM 790 CG MET A 109 24.633 77.748 113.209 1.00 70.01 C ANISOU 790 CG MET A 109 9120 8950 8530 -597 -921 523 C ATOM 791 SD MET A 109 23.996 79.118 114.186 1.00 79.31 S ANISOU 791 SD MET A 109 10580 10245 9308 -607 -863 456 S ATOM 792 CE MET A 109 25.446 80.166 114.250 1.00 79.69 C ANISOU 792 CE MET A 109 10658 10266 9355 -639 -1125 376 C ATOM 793 N ASN A 110 24.672 78.522 108.606 1.00 63.27 N ANISOU 793 N ASN A 110 7766 8045 8227 -459 -618 56 N ATOM 794 CA ASN A 110 24.820 79.359 107.420 1.00 56.47 C ANISOU 794 CA ASN A 110 6833 7213 7409 -422 -543 -83 C ATOM 795 C ASN A 110 23.514 79.457 106.645 1.00 59.14 C ANISOU 795 C ASN A 110 7175 7589 7707 -403 -388 -178 C ATOM 796 O ASN A 110 23.140 80.541 106.184 1.00 62.71 O ANISOU 796 O ASN A 110 7651 8105 8071 -396 -319 -267 O ATOM 797 CB ASN A 110 25.928 78.813 106.520 1.00 61.45 C ANISOU 797 CB ASN A 110 7307 7767 8273 -369 -569 -94 C ATOM 798 CG ASN A 110 25.941 79.470 105.154 1.00 61.32 C ANISOU 798 CG ASN A 110 7227 7784 8287 -317 -451 -224 C ATOM 799 OD1 ASN A 110 25.322 78.980 104.209 1.00 58.74 O ANISOU 799 OD1 ASN A 110 6878 7444 7995 -274 -350 -307 O ATOM 800 ND2 ASN A 110 26.653 80.584 105.042 1.00 63.01 N ANISOU 800 ND2 ASN A 110 7419 8035 8488 -324 -477 -234 N ATOM 801 N ARG A 111 22.807 78.336 106.487 1.00 66.29 N ANISOU 801 N ARG A 111 8046 8440 8701 -400 -349 -150 N ATOM 802 CA ARG A 111 21.562 78.352 105.726 1.00 65.99 C ANISOU 802 CA ARG A 111 7992 8416 8664 -393 -242 -227 C ATOM 803 C ARG A 111 20.471 79.105 106.477 1.00 68.77 C ANISOU 803 C ARG A 111 8431 8847 8851 -425 -160 -194 C ATOM 804 O ARG A 111 19.866 80.039 105.941 1.00 70.04 O ANISOU 804 O ARG A 111 8597 9065 8951 -413 -85 -278 O ATOM 805 CB ARG A 111 21.116 76.923 105.415 1.00 59.19 C ANISOU 805 CB ARG A 111 7066 7447 7976 -393 -255 -199 C ATOM 806 CG ARG A 111 20.050 76.831 104.333 1.00 53.23 C ANISOU 806 CG ARG A 111 6276 6675 7275 -386 -202 -301 C ATOM 807 CD ARG A 111 19.293 75.519 104.422 1.00 51.40 C ANISOU 807 CD ARG A 111 5996 6328 7208 -418 -232 -238 C ATOM 808 NE ARG A 111 18.255 75.567 105.447 1.00 56.92 N ANISOU 808 NE ARG A 111 6706 7059 7862 -474 -172 -97 N ATOM 809 CZ ARG A 111 16.954 75.655 105.187 1.00 60.89 C ANISOU 809 CZ ARG A 111 7165 7561 8410 -504 -117 -91 C ATOM 810 NH1 ARG A 111 16.529 75.691 103.930 1.00 50.86 N ANISOU 810 NH1 ARG A 111 5852 6256 7216 -492 -154 -225 N ATOM 811 NH2 ARG A 111 16.079 75.698 106.182 1.00 68.88 N ANISOU 811 NH2 ARG A 111 8174 8603 9393 -540 -25 60 N ATOM 812 N GLN A 112 20.209 78.715 107.727 1.00 69.70 N ANISOU 812 N GLN A 112 8622 8968 8895 -458 -161 -62 N ATOM 813 CA GLN A 112 19.169 79.383 108.501 1.00 72.03 C ANISOU 813 CA GLN A 112 9009 9334 9024 -467 -41 -24 C ATOM 814 C GLN A 112 19.524 80.837 108.770 1.00 73.09 C ANISOU 814 C GLN A 112 9254 9542 8976 -453 -38 -108 C ATOM 815 O GLN A 112 18.635 81.696 108.803 1.00 72.30 O ANISOU 815 O GLN A 112 9193 9492 8787 -434 85 -152 O ATOM 816 CB GLN A 112 18.928 78.640 109.815 1.00 78.71 C ANISOU 816 CB GLN A 112 9935 10173 9798 -494 -28 151 C ATOM 817 CG GLN A 112 17.543 78.847 110.396 1.00 86.07 C ANISOU 817 CG GLN A 112 10906 11152 10644 -490 158 224 C ATOM 818 CD GLN A 112 16.456 78.235 109.534 1.00 94.39 C ANISOU 818 CD GLN A 112 11789 12149 11926 -500 231 235 C ATOM 819 OE1 GLN A 112 16.410 77.019 109.344 1.00 98.74 O ANISOU 819 OE1 GLN A 112 12244 12607 12665 -530 172 315 O ATOM 820 NE2 GLN A 112 15.577 79.077 109.000 1.00 96.71 N ANISOU 820 NE2 GLN A 112 12041 12481 12224 -479 338 157 N ATOM 821 N GLY A 113 20.813 81.133 108.947 1.00 71.42 N ANISOU 821 N GLY A 113 9078 9321 8738 -460 -178 -127 N ATOM 822 CA GLY A 113 21.220 82.511 109.165 1.00 61.97 C ANISOU 822 CA GLY A 113 7977 8165 7403 -458 -209 -210 C ATOM 823 C GLY A 113 21.074 83.369 107.922 1.00 59.70 C ANISOU 823 C GLY A 113 7597 7891 7194 -432 -151 -331 C ATOM 824 O GLY A 113 20.613 84.513 107.998 1.00 64.33 O ANISOU 824 O GLY A 113 8252 8511 7678 -419 -88 -399 O ATOM 825 N SER A 114 21.460 82.832 106.762 1.00 50.43 N ANISOU 825 N SER A 114 6280 6686 6194 -415 -167 -358 N ATOM 826 CA SER A 114 21.305 83.583 105.521 1.00 51.65 C ANISOU 826 CA SER A 114 6363 6863 6399 -386 -109 -455 C ATOM 827 C SER A 114 19.834 83.815 105.201 1.00 58.95 C ANISOU 827 C SER A 114 7285 7817 7296 -375 13 -484 C ATOM 828 O SER A 114 19.466 84.872 104.678 1.00 71.97 O ANISOU 828 O SER A 114 8931 9498 8917 -358 63 -545 O ATOM 829 CB SER A 114 21.999 82.858 104.367 1.00 57.61 C ANISOU 829 CB SER A 114 6998 7580 7309 -356 -132 -479 C ATOM 830 OG SER A 114 23.410 82.970 104.462 1.00 65.66 O ANISOU 830 OG SER A 114 7980 8573 8395 -355 -221 -450 O ATOM 831 N ILE A 115 18.978 82.843 105.518 1.00 54.79 N ANISOU 831 N ILE A 115 6742 7270 6806 -386 55 -422 N ATOM 832 CA ILE A 115 17.549 82.997 105.262 1.00 51.61 C ANISOU 832 CA ILE A 115 6302 6880 6427 -380 162 -421 C ATOM 833 C ILE A 115 16.975 84.130 106.106 1.00 54.32 C ANISOU 833 C ILE A 115 6738 7270 6632 -365 264 -417 C ATOM 834 O ILE A 115 16.230 84.982 105.607 1.00 55.07 O ANISOU 834 O ILE A 115 6799 7383 6742 -341 336 -462 O ATOM 835 CB ILE A 115 16.812 81.668 105.517 1.00 46.43 C ANISOU 835 CB ILE A 115 5589 6173 5881 -406 178 -327 C ATOM 836 CG1 ILE A 115 17.124 80.661 104.408 1.00 55.62 C ANISOU 836 CG1 ILE A 115 6664 7266 7201 -408 83 -373 C ATOM 837 CG2 ILE A 115 15.312 81.893 105.620 1.00 37.94 C ANISOU 837 CG2 ILE A 115 4463 5106 4847 -406 300 -278 C ATOM 838 CD1 ILE A 115 16.469 79.306 104.603 1.00 50.54 C ANISOU 838 CD1 ILE A 115 5957 6537 6707 -442 65 -286 C ATOM 839 N ILE A 116 17.326 84.167 107.393 1.00 49.84 N ANISOU 839 N ILE A 116 6301 6715 5922 -371 267 -367 N ATOM 840 CA ILE A 116 16.753 85.166 108.291 1.00 51.28 C ANISOU 840 CA ILE A 116 6612 6930 5943 -340 382 -380 C ATOM 841 C ILE A 116 17.251 86.561 107.932 1.00 62.89 C ANISOU 841 C ILE A 116 8128 8402 7366 -323 340 -498 C ATOM 842 O ILE A 116 16.460 87.499 107.780 1.00 65.26 O ANISOU 842 O ILE A 116 8430 8708 7659 -284 450 -545 O ATOM 843 CB ILE A 116 17.066 84.814 109.756 1.00 49.98 C ANISOU 843 CB ILE A 116 6619 6778 5593 -348 377 -303 C ATOM 844 CG1 ILE A 116 16.346 83.525 110.157 1.00 55.88 C ANISOU 844 CG1 ILE A 116 7311 7519 6402 -361 459 -153 C ATOM 845 CG2 ILE A 116 16.674 85.962 110.677 1.00 54.17 C ANISOU 845 CG2 ILE A 116 7337 7335 5912 -301 486 -355 C ATOM 846 CD1 ILE A 116 16.637 83.070 111.572 1.00 55.33 C ANISOU 846 CD1 ILE A 116 7418 7469 6138 -368 457 -44 C ATOM 847 N PHE A 117 18.568 86.720 107.783 1.00 62.26 N ANISOU 847 N PHE A 117 8066 8305 7286 -352 181 -533 N ATOM 848 CA PHE A 117 19.126 88.050 107.570 1.00 51.66 C ANISOU 848 CA PHE A 117 6765 6946 5918 -349 125 -623 C ATOM 849 C PHE A 117 18.877 88.579 106.164 1.00 54.21 C ANISOU 849 C PHE A 117 6945 7273 6381 -331 160 -665 C ATOM 850 O PHE A 117 18.936 89.795 105.960 1.00 65.13 O ANISOU 850 O PHE A 117 8352 8637 7759 -319 161 -725 O ATOM 851 CB PHE A 117 20.623 88.051 107.880 1.00 45.00 C ANISOU 851 CB PHE A 117 5957 6069 5071 -393 -66 -618 C ATOM 852 CG PHE A 117 20.930 88.021 109.348 1.00 49.69 C ANISOU 852 CG PHE A 117 6750 6652 5480 -413 -145 -598 C ATOM 853 CD1 PHE A 117 20.667 89.124 110.143 1.00 54.50 C ANISOU 853 CD1 PHE A 117 7545 7243 5919 -395 -130 -679 C ATOM 854 CD2 PHE A 117 21.475 86.892 109.936 1.00 54.17 C ANISOU 854 CD2 PHE A 117 7333 7217 6033 -443 -241 -501 C ATOM 855 CE1 PHE A 117 20.942 89.103 111.496 1.00 60.14 C ANISOU 855 CE1 PHE A 117 8486 7948 6415 -407 -213 -673 C ATOM 856 CE2 PHE A 117 21.755 86.865 111.290 1.00 55.97 C ANISOU 856 CE2 PHE A 117 7767 7440 6058 -463 -333 -470 C ATOM 857 CZ PHE A 117 21.488 87.973 112.071 1.00 60.32 C ANISOU 857 CZ PHE A 117 8531 7984 6404 -444 -321 -561 C ATOM 858 N LEU A 118 18.602 87.707 105.190 1.00 48.98 N ANISOU 858 N LEU A 118 6150 6624 5836 -329 176 -637 N ATOM 859 CA LEU A 118 18.157 88.199 103.890 1.00 51.63 C ANISOU 859 CA LEU A 118 6385 6972 6261 -308 211 -670 C ATOM 860 C LEU A 118 16.750 88.773 103.972 1.00 58.44 C ANISOU 860 C LEU A 118 7240 7839 7126 -279 329 -670 C ATOM 861 O LEU A 118 16.391 89.652 103.181 1.00 60.95 O ANISOU 861 O LEU A 118 7507 8157 7492 -258 348 -696 O ATOM 862 CB LEU A 118 18.220 87.088 102.842 1.00 47.37 C ANISOU 862 CB LEU A 118 5745 6436 5818 -309 178 -658 C ATOM 863 CG LEU A 118 19.584 86.844 102.196 1.00 50.48 C ANISOU 863 CG LEU A 118 6104 6824 6253 -307 103 -670 C ATOM 864 CD1 LEU A 118 19.533 85.641 101.269 1.00 51.51 C ANISOU 864 CD1 LEU A 118 6173 6942 6455 -290 90 -681 C ATOM 865 CD2 LEU A 118 20.048 88.082 101.445 1.00 44.42 C ANISOU 865 CD2 LEU A 118 5314 6073 5490 -293 107 -693 C ATOM 866 N THR A 119 15.943 88.289 104.919 1.00 57.65 N ANISOU 866 N THR A 119 7178 7739 6988 -272 418 -624 N ATOM 867 CA THR A 119 14.631 88.883 105.146 1.00 61.26 C ANISOU 867 CA THR A 119 7615 8191 7469 -230 562 -608 C ATOM 868 C THR A 119 14.755 90.213 105.876 1.00 57.30 C ANISOU 868 C THR A 119 7246 7670 6856 -190 618 -674 C ATOM 869 O THR A 119 14.096 91.193 105.508 1.00 60.30 O ANISOU 869 O THR A 119 7586 8027 7297 -148 688 -701 O ATOM 870 CB THR A 119 13.746 87.917 105.933 1.00 64.30 C ANISOU 870 CB THR A 119 7986 8579 7867 -228 671 -512 C ATOM 871 OG1 THR A 119 13.524 86.731 105.160 1.00 54.42 O ANISOU 871 OG1 THR A 119 6603 7315 6760 -269 599 -460 O ATOM 872 CG2 THR A 119 12.409 88.559 106.264 1.00 73.70 C ANISOU 872 CG2 THR A 119 9139 9758 9105 -170 856 -477 C ATOM 873 N VAL A 120 15.603 90.267 106.908 1.00 53.32 N ANISOU 873 N VAL A 120 6905 7160 6193 -202 569 -704 N ATOM 874 CA VAL A 120 15.811 91.510 107.648 1.00 54.94 C ANISOU 874 CA VAL A 120 7273 7324 6277 -169 586 -793 C ATOM 875 C VAL A 120 16.332 92.602 106.723 1.00 54.82 C ANISOU 875 C VAL A 120 7199 7268 6362 -178 494 -855 C ATOM 876 O VAL A 120 15.944 93.772 106.835 1.00 51.05 O ANISOU 876 O VAL A 120 6772 6737 5888 -133 553 -919 O ATOM 877 CB VAL A 120 16.761 91.267 108.835 1.00 50.69 C ANISOU 877 CB VAL A 120 6931 6780 5548 -198 483 -811 C ATOM 878 CG1 VAL A 120 17.085 92.574 109.540 1.00 50.81 C ANISOU 878 CG1 VAL A 120 7141 6730 5435 -173 449 -930 C ATOM 879 CG2 VAL A 120 16.142 90.275 109.798 1.00 54.46 C ANISOU 879 CG2 VAL A 120 7483 7302 5909 -179 601 -726 C ATOM 880 N VAL A 121 17.214 92.235 105.791 1.00 54.92 N ANISOU 880 N VAL A 121 7103 7297 6467 -229 363 -829 N ATOM 881 CA VAL A 121 17.677 93.188 104.788 1.00 54.15 C ANISOU 881 CA VAL A 121 6927 7171 6477 -238 300 -850 C ATOM 882 C VAL A 121 16.508 93.690 103.950 1.00 55.51 C ANISOU 882 C VAL A 121 6996 7347 6750 -192 405 -833 C ATOM 883 O VAL A 121 16.390 94.891 103.676 1.00 64.22 O ANISOU 883 O VAL A 121 8096 8397 7907 -170 413 -862 O ATOM 884 CB VAL A 121 18.771 92.545 103.916 1.00 53.65 C ANISOU 884 CB VAL A 121 6762 7137 6486 -282 189 -804 C ATOM 885 CG1 VAL A 121 18.931 93.307 102.617 1.00 51.50 C ANISOU 885 CG1 VAL A 121 6381 6864 6324 -276 181 -786 C ATOM 886 CG2 VAL A 121 20.091 92.499 104.672 1.00 53.14 C ANISOU 886 CG2 VAL A 121 6772 7037 6384 -329 52 -810 C ATOM 887 N ALA A 122 15.616 92.784 103.545 1.00 54.40 N ANISOU 887 N ALA A 122 6760 7252 6656 -183 467 -778 N ATOM 888 CA ALA A 122 14.471 93.184 102.732 1.00 58.68 C ANISOU 888 CA ALA A 122 7187 7791 7317 -148 531 -744 C ATOM 889 C ALA A 122 13.474 94.006 103.541 1.00 58.58 C ANISOU 889 C ALA A 122 7214 7727 7316 -84 676 -761 C ATOM 890 O ALA A 122 12.898 94.971 103.027 1.00 59.91 O ANISOU 890 O ALA A 122 7319 7854 7589 -46 709 -756 O ATOM 891 CB ALA A 122 13.793 91.951 102.136 1.00 61.89 C ANISOU 891 CB ALA A 122 7484 8238 7793 -167 522 -682 C ATOM 892 N VAL A 123 13.255 93.638 104.806 1.00 57.62 N ANISOU 892 N VAL A 123 7203 7604 7087 -61 777 -775 N ATOM 893 CA VAL A 123 12.331 94.391 105.650 1.00 59.72 C ANISOU 893 CA VAL A 123 7531 7821 7340 23 958 -800 C ATOM 894 C VAL A 123 12.882 95.782 105.937 1.00 69.67 C ANISOU 894 C VAL A 123 8921 9000 8549 53 928 -910 C ATOM 895 O VAL A 123 12.136 96.770 105.947 1.00 63.25 O ANISOU 895 O VAL A 123 8094 8118 7821 127 1038 -936 O ATOM 896 CB VAL A 123 12.043 93.613 106.947 1.00 49.04 C ANISOU 896 CB VAL A 123 6295 6497 5842 47 1088 -777 C ATOM 897 CG1 VAL A 123 11.220 94.454 107.908 1.00 48.55 C ANISOU 897 CG1 VAL A 123 6342 6383 5722 156 1308 -819 C ATOM 898 CG2 VAL A 123 11.321 92.315 106.632 1.00 52.11 C ANISOU 898 CG2 VAL A 123 6521 6935 6343 18 1126 -648 C ATOM 899 N ASP A 124 14.193 95.884 106.173 1.00 72.18 N ANISOU 899 N ASP A 124 9358 9308 8759 -5 769 -972 N ATOM 900 CA ASP A 124 14.810 97.188 106.395 1.00 66.59 C ANISOU 900 CA ASP A 124 8764 8499 8037 2 696 -1073 C ATOM 901 C ASP A 124 14.610 98.095 105.188 1.00 58.18 C ANISOU 901 C ASP A 124 7544 7389 7173 8 667 -1040 C ATOM 902 O ASP A 124 14.089 99.208 105.313 1.00 57.76 O ANISOU 902 O ASP A 124 7519 7239 7188 72 739 -1091 O ATOM 903 CB ASP A 124 16.297 97.017 106.712 1.00 68.53 C ANISOU 903 CB ASP A 124 9110 8738 8191 -82 492 -1107 C ATOM 904 CG ASP A 124 17.024 98.341 106.860 1.00 70.05 C ANISOU 904 CG ASP A 124 9397 8805 8416 -97 371 -1199 C ATOM 905 OD1 ASP A 124 17.268 99.014 105.836 1.00 70.92 O ANISOU 905 OD1 ASP A 124 9370 8878 8700 -118 314 -1159 O ATOM 906 OD2 ASP A 124 17.351 98.713 108.007 1.00 76.61 O ANISOU 906 OD2 ASP A 124 10449 9565 9094 -88 324 -1306 O ATOM 907 N ARG A 125 15.010 97.626 104.003 1.00 54.73 N ANISOU 907 N ARG A 125 6953 7018 6825 -50 569 -953 N ATOM 908 CA ARG A 125 14.818 98.410 102.790 1.00 59.78 C ANISOU 908 CA ARG A 125 7456 7631 7626 -46 539 -895 C ATOM 909 C ARG A 125 13.343 98.647 102.491 1.00 63.97 C ANISOU 909 C ARG A 125 7884 8149 8274 25 668 -848 C ATOM 910 O ARG A 125 13.009 99.618 101.803 1.00 63.61 O ANISOU 910 O ARG A 125 7759 8043 8366 51 659 -812 O ATOM 911 CB ARG A 125 15.493 97.717 101.604 1.00 61.53 C ANISOU 911 CB ARG A 125 7566 7941 7870 -108 434 -811 C ATOM 912 CG ARG A 125 15.713 98.614 100.395 1.00 69.85 C ANISOU 912 CG ARG A 125 8524 8973 9042 -115 377 -741 C ATOM 913 CD ARG A 125 16.646 99.770 100.727 1.00 76.70 C ANISOU 913 CD ARG A 125 9452 9733 9957 -137 309 -776 C ATOM 914 NE ARG A 125 17.992 99.313 101.061 1.00 74.15 N ANISOU 914 NE ARG A 125 9174 9425 9575 -201 212 -790 N ATOM 915 CZ ARG A 125 18.999 99.256 100.195 1.00 64.66 C ANISOU 915 CZ ARG A 125 7886 8255 8427 -246 145 -705 C ATOM 916 NH1 ARG A 125 18.814 99.630 98.936 1.00 65.91 N ANISOU 916 NH1 ARG A 125 7939 8446 8658 -233 167 -603 N ATOM 917 NH2 ARG A 125 20.192 98.826 100.586 1.00 53.02 N ANISOU 917 NH2 ARG A 125 6429 6780 6936 -298 61 -707 N ATOM 918 N TYR A 126 12.456 97.785 102.998 1.00 63.33 N ANISOU 918 N TYR A 126 7784 8114 8166 56 784 -828 N ATOM 919 CA TYR A 126 11.024 97.997 102.811 1.00 59.21 C ANISOU 919 CA TYR A 126 7135 7564 7799 125 912 -764 C ATOM 920 C TYR A 126 10.547 99.230 103.564 1.00 63.05 C ANISOU 920 C TYR A 126 7697 7931 8328 222 1050 -835 C ATOM 921 O TYR A 126 9.673 99.960 103.083 1.00 62.91 O ANISOU 921 O TYR A 126 7555 7848 8499 280 1107 -783 O ATOM 922 CB TYR A 126 10.246 96.762 103.261 1.00 54.33 C ANISOU 922 CB TYR A 126 6465 7008 7170 129 1012 -706 C ATOM 923 CG TYR A 126 8.742 96.930 103.226 1.00 54.41 C ANISOU 923 CG TYR A 126 6318 6978 7377 202 1162 -620 C ATOM 924 CD1 TYR A 126 8.040 96.812 102.035 1.00 47.46 C ANISOU 924 CD1 TYR A 126 5236 6104 6693 179 1068 -510 C ATOM 925 CD2 TYR A 126 8.023 97.196 104.387 1.00 41.96 C ANISOU 925 CD2 TYR A 126 4798 5353 5793 299 1396 -640 C ATOM 926 CE1 TYR A 126 6.666 96.961 101.995 1.00 45.18 C ANISOU 926 CE1 TYR A 126 4772 5765 6630 239 1182 -409 C ATOM 927 CE2 TYR A 126 6.647 97.347 104.357 1.00 48.42 C ANISOU 927 CE2 TYR A 126 5439 6126 6834 375 1556 -539 C ATOM 928 CZ TYR A 126 5.974 97.228 103.157 1.00 54.78 C ANISOU 928 CZ TYR A 126 6010 6928 7875 339 1437 -417 C ATOM 929 OH TYR A 126 4.605 97.376 103.116 1.00 73.21 O ANISOU 929 OH TYR A 126 8137 9204 10476 409 1572 -295 O ATOM 930 N PHE A 127 11.104 99.477 104.749 1.00 62.71 N ANISOU 930 N PHE A 127 7868 7847 8114 244 1097 -958 N ATOM 931 CA PHE A 127 10.714 100.656 105.509 1.00 66.12 C ANISOU 931 CA PHE A 127 8417 8147 8559 347 1227 -1060 C ATOM 932 C PHE A 127 11.442 101.910 105.038 1.00 78.42 C ANISOU 932 C PHE A 127 10005 9589 10201 326 1083 -1117 C ATOM 933 O PHE A 127 10.883 103.007 105.126 1.00 85.72 O ANISOU 933 O PHE A 127 10932 10383 11253 413 1169 -1158 O ATOM 934 CB PHE A 127 10.955 100.423 107.001 1.00 62.67 C ANISOU 934 CB PHE A 127 8237 7705 7871 387 1327 -1179 C ATOM 935 CG PHE A 127 9.875 99.617 107.665 1.00 71.08 C ANISOU 935 CG PHE A 127 9278 8833 8897 461 1567 -1115 C ATOM 936 CD1 PHE A 127 9.938 98.232 107.692 1.00 70.75 C ANISOU 936 CD1 PHE A 127 9181 8917 8784 393 1546 -1017 C ATOM 937 CD2 PHE A 127 8.788 100.245 108.253 1.00 77.78 C ANISOU 937 CD2 PHE A 127 10146 9602 9806 605 1829 -1139 C ATOM 938 CE1 PHE A 127 8.940 97.490 108.300 1.00 70.14 C ANISOU 938 CE1 PHE A 127 9061 8887 8703 454 1770 -929 C ATOM 939 CE2 PHE A 127 7.788 99.508 108.862 1.00 79.34 C ANISOU 939 CE2 PHE A 127 10297 9856 9995 678 2079 -1050 C ATOM 940 CZ PHE A 127 7.864 98.129 108.884 1.00 77.24 C ANISOU 940 CZ PHE A 127 9967 9717 9664 595 2044 -936 C ATOM 941 N ARG A 128 12.673 101.781 104.535 1.00 79.81 N ANISOU 941 N ARG A 128 10189 9799 10335 216 874 -1107 N ATOM 942 CA ARG A 128 13.356 102.952 103.992 1.00 77.30 C ANISOU 942 CA ARG A 128 9862 9368 10140 186 740 -1120 C ATOM 943 C ARG A 128 12.616 103.511 102.783 1.00 77.58 C ANISOU 943 C ARG A 128 9689 9382 10404 213 755 -992 C ATOM 944 O ARG A 128 12.639 104.723 102.544 1.00 86.69 O ANISOU 944 O ARG A 128 10832 10398 11707 239 725 -1001 O ATOM 945 CB ARG A 128 14.796 102.604 103.604 1.00 80.21 C ANISOU 945 CB ARG A 128 10235 9787 10455 66 539 -1091 C ATOM 946 CG ARG A 128 15.622 101.915 104.685 1.00 90.96 C ANISOU 946 CG ARG A 128 11772 11178 11609 21 476 -1183 C ATOM 947 CD ARG A 128 16.088 102.871 105.770 1.00102.03 C ANISOU 947 CD ARG A 128 13396 12422 12948 35 413 -1340 C ATOM 948 NE ARG A 128 17.308 102.385 106.409 1.00110.47 N ANISOU 948 NE ARG A 128 14588 13504 13879 -53 238 -1383 N ATOM 949 CZ ARG A 128 17.822 102.883 107.529 1.00118.20 C ANISOU 949 CZ ARG A 128 15805 14368 14738 -59 136 -1528 C ATOM 950 NH1 ARG A 128 17.217 103.884 108.154 1.00123.80 N ANISOU 950 NH1 ARG A 128 16675 14935 15428 29 216 -1667 N ATOM 951 NH2 ARG A 128 18.939 102.373 108.029 1.00115.40 N ANISOU 951 NH2 ARG A 128 15534 14029 14284 -150 -56 -1537 N ATOM 952 N VAL A 129 11.939 102.651 102.031 1.00 70.18 N ANISOU 952 N VAL A 129 8594 8567 9504 205 782 -871 N ATOM 953 CA VAL A 129 11.296 103.028 100.778 1.00 64.74 C ANISOU 953 CA VAL A 129 7714 7879 9004 213 746 -729 C ATOM 954 C VAL A 129 9.806 103.279 100.965 1.00 68.32 C ANISOU 954 C VAL A 129 8064 8274 9619 317 902 -693 C ATOM 955 O VAL A 129 9.290 104.321 100.565 1.00 83.04 O ANISOU 955 O VAL A 129 9845 10027 11679 372 913 -644 O ATOM 956 CB VAL A 129 11.555 101.941 99.710 1.00 58.70 C ANISOU 956 CB VAL A 129 6854 7272 8179 133 634 -621 C ATOM 957 CG1 VAL A 129 10.726 102.196 98.466 1.00 59.46 C ANISOU 957 CG1 VAL A 129 6781 7380 8433 144 581 -475 C ATOM 958 CG2 VAL A 129 13.042 101.878 99.373 1.00 60.38 C ANISOU 958 CG2 VAL A 129 7132 7523 8286 49 506 -630 C ATOM 959 N VAL A 130 9.093 102.341 101.589 1.00 67.65 N ANISOU 959 N VAL A 130 7968 8254 9483 349 1030 -698 N ATOM 960 CA VAL A 130 7.636 102.428 101.635 1.00 70.00 C ANISOU 960 CA VAL A 130 8110 8507 9981 441 1181 -619 C ATOM 961 C VAL A 130 7.169 103.333 102.771 1.00 73.10 C ANISOU 961 C VAL A 130 8603 8758 10414 574 1399 -728 C ATOM 962 O VAL A 130 6.213 104.098 102.611 1.00 78.10 O ANISOU 962 O VAL A 130 9107 9283 11284 670 1501 -672 O ATOM 963 CB VAL A 130 7.031 101.014 101.734 1.00 70.44 C ANISOU 963 CB VAL A 130 8076 8679 10009 413 1227 -545 C ATOM 964 CG1 VAL A 130 5.582 101.066 102.201 1.00 73.09 C ANISOU 964 CG1 VAL A 130 8267 8954 10550 520 1442 -472 C ATOM 965 CG2 VAL A 130 7.128 100.317 100.383 1.00 67.68 C ANISOU 965 CG2 VAL A 130 7596 8425 9692 310 1010 -430 C ATOM 966 N HIS A 131 7.837 103.283 103.923 1.00 73.75 N ANISOU 966 N HIS A 131 8926 8828 10265 588 1468 -886 N ATOM 967 CA HIS A 131 7.451 104.058 105.104 1.00 81.72 C ANISOU 967 CA HIS A 131 10097 9707 11245 725 1685 -1023 C ATOM 968 C HIS A 131 8.650 104.858 105.601 1.00 82.76 C ANISOU 968 C HIS A 131 10482 9742 11222 697 1562 -1200 C ATOM 969 O HIS A 131 9.233 104.540 106.645 1.00 82.85 O ANISOU 969 O HIS A 131 10733 9772 10972 692 1582 -1332 O ATOM 970 CB HIS A 131 6.912 103.139 106.202 1.00 90.69 C ANISOU 970 CB HIS A 131 11316 10921 12223 785 1912 -1041 C ATOM 971 CG HIS A 131 5.722 102.333 105.779 1.00105.62 C ANISOU 971 CG HIS A 131 12938 12885 14309 803 2026 -853 C ATOM 972 ND1 HIS A 131 5.643 100.968 105.956 1.00109.90 N ANISOU 972 ND1 HIS A 131 13441 13565 14750 738 2038 -771 N ATOM 973 CD2 HIS A 131 4.568 102.701 105.174 1.00110.50 C ANISOU 973 CD2 HIS A 131 13298 13439 15247 871 2108 -719 C ATOM 974 CE1 HIS A 131 4.490 100.531 105.481 1.00110.27 C ANISOU 974 CE1 HIS A 131 13219 13626 15051 759 2117 -600 C ATOM 975 NE2 HIS A 131 3.818 101.562 105.003 1.00111.06 N ANISOU 975 NE2 HIS A 131 13179 13608 15410 839 2156 -562 N ATOM 976 N PRO A 132 9.041 105.914 104.878 1.00 83.07 N ANISOU 976 N PRO A 132 10472 9665 11427 673 1416 -1195 N ATOM 977 CA PRO A 132 10.272 106.636 105.248 1.00 80.15 C ANISOU 977 CA PRO A 132 10309 9188 10955 617 1251 -1339 C ATOM 978 C PRO A 132 10.236 107.258 106.634 1.00 78.76 C ANISOU 978 C PRO A 132 10419 8868 10639 725 1378 -1560 C ATOM 979 O PRO A 132 11.296 107.436 107.249 1.00 75.10 O ANISOU 979 O PRO A 132 10181 8354 10001 663 1227 -1699 O ATOM 980 CB PRO A 132 10.387 107.710 104.157 1.00 74.13 C ANISOU 980 CB PRO A 132 9392 8309 10464 594 1120 -1248 C ATOM 981 CG PRO A 132 9.603 107.178 103.009 1.00 71.83 C ANISOU 981 CG PRO A 132 8828 8139 10326 580 1130 -1035 C ATOM 982 CD PRO A 132 8.456 106.434 103.630 1.00 78.57 C ANISOU 982 CD PRO A 132 9646 9058 11149 675 1360 -1031 C ATOM 983 N HIS A 133 9.055 107.595 107.148 1.00 80.87 N ANISOU 983 N HIS A 133 10690 9058 10977 889 1648 -1597 N ATOM 984 CA HIS A 133 8.935 108.273 108.432 1.00 92.48 C ANISOU 984 CA HIS A 133 12459 10376 12303 1021 1803 -1824 C ATOM 985 C HIS A 133 8.593 107.326 109.576 1.00 92.18 C ANISOU 985 C HIS A 133 12602 10460 11962 1087 2017 -1881 C ATOM 986 O HIS A 133 8.373 107.788 110.701 1.00 92.88 O ANISOU 986 O HIS A 133 12968 10444 11879 1220 2192 -2067 O ATOM 987 CB HIS A 133 7.882 109.379 108.345 1.00103.40 C ANISOU 987 CB HIS A 133 13757 11567 13963 1190 2002 -1842 C ATOM 988 CG HIS A 133 8.102 110.335 107.214 1.00107.09 C ANISOU 988 CG HIS A 133 14035 11906 14748 1135 1808 -1754 C ATOM 989 ND1 HIS A 133 7.274 110.385 106.114 1.00107.49 N ANISOU 989 ND1 HIS A 133 13752 11982 15107 1148 1835 -1533 N ATOM 990 CD2 HIS A 133 9.055 111.275 107.010 1.00106.90 C ANISOU 990 CD2 HIS A 133 14106 11722 14790 1062 1572 -1837 C ATOM 991 CE1 HIS A 133 7.704 111.317 105.282 1.00105.36 C ANISOU 991 CE1 HIS A 133 13392 11585 15055 1092 1639 -1480 C ATOM 992 NE2 HIS A 133 8.784 111.872 105.802 1.00106.42 N ANISOU 992 NE2 HIS A 133 13771 11601 15061 1038 1486 -1657 N ATOM 993 N HIS A 134 8.544 106.021 109.321 1.00 90.83 N ANISOU 993 N HIS A 134 12294 10500 11715 1003 2011 -1726 N ATOM 994 CA HIS A 134 8.260 105.068 110.383 1.00 96.81 C ANISOU 994 CA HIS A 134 13210 11376 12196 1053 2206 -1745 C ATOM 995 C HIS A 134 9.413 105.021 111.381 1.00 99.49 C ANISOU 995 C HIS A 134 13919 11707 12177 999 2051 -1929 C ATOM 996 O HIS A 134 10.565 105.312 111.049 1.00104.73 O ANISOU 996 O HIS A 134 14634 12328 12831 869 1741 -1982 O ATOM 997 CB HIS A 134 8.007 103.677 109.803 1.00 99.94 C ANISOU 997 CB HIS A 134 13362 11976 12635 958 2192 -1529 C ATOM 998 CG HIS A 134 7.277 102.760 110.735 1.00105.64 C ANISOU 998 CG HIS A 134 14143 12800 13196 1039 2470 -1477 C ATOM 999 ND1 HIS A 134 7.919 102.007 111.695 1.00106.67 N ANISOU 999 ND1 HIS A 134 14529 13022 12979 1000 2449 -1535 N ATOM 1000 CD2 HIS A 134 5.958 102.482 110.858 1.00108.51 C ANISOU 1000 CD2 HIS A 134 14331 13181 13715 1157 2779 -1350 C ATOM 1001 CE1 HIS A 134 7.026 101.303 112.368 1.00109.25 C ANISOU 1001 CE1 HIS A 134 14847 13427 13237 1092 2746 -1442 C ATOM 1002 NE2 HIS A 134 5.829 101.573 111.880 1.00110.15 N ANISOU 1002 NE2 HIS A 134 14691 13495 13664 1187 2957 -1327 N ATOM 1003 N ALA A 135 9.088 104.645 112.621 1.00100.18 N ANISOU 1003 N ALA A 135 14261 11831 11972 1101 2269 -2010 N ATOM 1004 CA ALA A 135 10.082 104.645 113.690 1.00100.74 C ANISOU 1004 CA ALA A 135 14725 11882 11670 1067 2121 -2192 C ATOM 1005 C ALA A 135 11.199 103.635 113.458 1.00107.73 C ANISOU 1005 C ALA A 135 15578 12909 12445 872 1819 -2102 C ATOM 1006 O ALA A 135 12.301 103.819 113.987 1.00113.60 O ANISOU 1006 O ALA A 135 16572 13603 12989 792 1563 -2232 O ATOM 1007 CB ALA A 135 9.408 104.373 115.035 1.00 97.87 C ANISOU 1007 CB ALA A 135 14648 11552 10988 1229 2449 -2269 C ATOM 1008 N LEU A 136 10.946 102.580 112.679 1.00104.50 N ANISOU 1008 N LEU A 136 14866 12659 12179 796 1830 -1885 N ATOM 1009 CA LEU A 136 11.962 101.565 112.425 1.00100.94 C ANISOU 1009 CA LEU A 136 14369 12334 11649 630 1572 -1795 C ATOM 1010 C LEU A 136 13.097 102.067 111.542 1.00 97.13 C ANISOU 1010 C LEU A 136 13790 11786 11327 494 1238 -1811 C ATOM 1011 O LEU A 136 14.129 101.394 111.451 1.00 95.70 O ANISOU 1011 O LEU A 136 13609 11675 11076 365 1009 -1767 O ATOM 1012 CB LEU A 136 11.321 100.328 111.791 1.00 99.63 C ANISOU 1012 CB LEU A 136 13913 12330 11614 596 1680 -1575 C ATOM 1013 CG LEU A 136 10.411 99.501 112.703 1.00100.50 C ANISOU 1013 CG LEU A 136 14090 12531 11563 690 1976 -1502 C ATOM 1014 CD1 LEU A 136 9.703 98.405 111.921 1.00 99.85 C ANISOU 1014 CD1 LEU A 136 13676 12564 11697 647 2051 -1280 C ATOM 1015 CD2 LEU A 136 11.211 98.908 113.853 1.00 99.20 C ANISOU 1015 CD2 LEU A 136 14238 12424 11029 654 1891 -1559 C ATOM 1016 N ASN A 137 12.937 103.223 110.895 1.00 95.41 N ANISOU 1016 N ASN A 137 13480 11430 11341 523 1216 -1855 N ATOM 1017 CA ASN A 137 14.000 103.780 110.069 1.00 90.31 C ANISOU 1017 CA ASN A 137 12738 10711 10864 400 925 -1847 C ATOM 1018 C ASN A 137 15.054 104.516 110.882 1.00 96.95 C ANISOU 1018 C ASN A 137 13865 11403 11568 357 701 -2028 C ATOM 1019 O ASN A 137 16.167 104.724 110.387 1.00100.86 O ANISOU 1019 O ASN A 137 14291 11856 12174 227 429 -1999 O ATOM 1020 CB ASN A 137 13.410 104.726 109.023 1.00 81.02 C ANISOU 1020 CB ASN A 137 11341 9439 10005 442 976 -1791 C ATOM 1021 CG ASN A 137 12.658 103.991 107.937 1.00 72.55 C ANISOU 1021 CG ASN A 137 9954 8508 9103 434 1076 -1587 C ATOM 1022 OD1 ASN A 137 13.167 103.034 107.356 1.00 72.23 O ANISOU 1022 OD1 ASN A 137 9790 8606 9048 330 961 -1472 O ATOM 1023 ND2 ASN A 137 11.435 104.428 107.664 1.00 73.09 N ANISOU 1023 ND2 ASN A 137 9896 8530 9344 548 1281 -1545 N ATOM 1024 N LYS A 138 14.731 104.914 112.113 1.00 97.35 N ANISOU 1024 N LYS A 138 14237 11367 11383 463 808 -2211 N ATOM 1025 CA LYS A 138 15.639 105.674 112.962 1.00105.63 C ANISOU 1025 CA LYS A 138 15603 12248 12284 429 573 -2414 C ATOM 1026 C LYS A 138 16.291 104.807 114.034 1.00103.46 C ANISOU 1026 C LYS A 138 15592 12063 11653 377 452 -2457 C ATOM 1027 O LYS A 138 16.631 105.302 115.113 1.00108.35 O ANISOU 1027 O LYS A 138 16576 12563 12027 406 349 -2656 O ATOM 1028 CB LYS A 138 14.897 106.845 113.602 1.00120.26 C ANISOU 1028 CB LYS A 138 17688 13906 14099 592 745 -2622 C ATOM 1029 CG LYS A 138 14.058 107.649 112.620 1.00127.88 C ANISOU 1029 CG LYS A 138 18386 14781 15421 669 906 -2558 C ATOM 1030 CD LYS A 138 14.929 108.400 111.628 1.00131.91 C ANISOU 1030 CD LYS A 138 18709 15168 16241 536 615 -2504 C ATOM 1031 CE LYS A 138 14.288 108.431 110.250 1.00132.67 C ANISOU 1031 CE LYS A 138 18413 15327 16669 540 726 -2290 C ATOM 1032 NZ LYS A 138 12.861 108.848 110.310 1.00134.97 N ANISOU 1032 NZ LYS A 138 18663 15568 17052 725 1055 -2309 N ATOM 1033 N ILE A 139 16.486 103.520 113.752 1.00101.19 N ANISOU 1033 N ILE A 139 15138 11975 11333 301 444 -2276 N ATOM 1034 CA ILE A 139 17.015 102.600 114.752 1.00104.29 C ANISOU 1034 CA ILE A 139 15757 12464 11403 259 345 -2280 C ATOM 1035 C ILE A 139 18.503 102.858 114.954 1.00101.04 C ANISOU 1035 C ILE A 139 15449 11953 10989 108 -77 -2336 C ATOM 1036 O ILE A 139 19.263 103.011 113.988 1.00 99.26 O ANISOU 1036 O ILE A 139 14964 11696 11056 -8 -274 -2241 O ATOM 1037 CB ILE A 139 16.738 101.146 114.338 1.00105.08 C ANISOU 1037 CB ILE A 139 15624 12782 11521 226 464 -2059 C ATOM 1038 CG1 ILE A 139 15.288 100.773 114.655 1.00108.07 C ANISOU 1038 CG1 ILE A 139 16004 13248 11809 378 866 -2018 C ATOM 1039 CG2 ILE A 139 17.695 100.187 115.020 1.00106.54 C ANISOU 1039 CG2 ILE A 139 15944 13047 11489 126 244 -2012 C ATOM 1040 CD1 ILE A 139 14.951 99.323 114.375 1.00110.82 C ANISOU 1040 CD1 ILE A 139 16148 13785 12175 344 975 -1806 C ATOM 1041 N SER A 140 18.922 102.915 116.215 1.00102.46 N ANISOU 1041 N SER A 140 16012 12079 10840 111 -219 -2480 N ATOM 1042 CA SER A 140 20.318 103.150 116.544 1.00103.93 C ANISOU 1042 CA SER A 140 16315 12152 11021 -36 -656 -2533 C ATOM 1043 C SER A 140 21.166 101.921 116.232 1.00103.86 C ANISOU 1043 C SER A 140 16096 12292 11075 -169 -830 -2321 C ATOM 1044 O SER A 140 20.664 100.805 116.073 1.00105.22 O ANISOU 1044 O SER A 140 16138 12651 11191 -138 -623 -2171 O ATOM 1045 CB SER A 140 20.466 103.520 118.020 1.00108.95 C ANISOU 1045 CB SER A 140 17458 12688 11251 9 -778 -2753 C ATOM 1046 OG SER A 140 21.831 103.556 118.397 1.00111.87 O ANISOU 1046 OG SER A 140 17931 12962 11611 -150 -1242 -2773 O ATOM 1047 N ASN A 141 22.479 102.143 116.148 1.00107.22 N ANISOU 1047 N ASN A 141 16478 12611 11649 -318 -1220 -2305 N ATOM 1048 CA ASN A 141 23.401 101.045 115.878 1.00110.38 C ANISOU 1048 CA ASN A 141 16673 13122 12144 -439 -1403 -2107 C ATOM 1049 C ASN A 141 23.384 100.021 117.004 1.00110.24 C ANISOU 1049 C ASN A 141 16911 13220 11755 -424 -1424 -2085 C ATOM 1050 O ASN A 141 23.503 98.815 116.758 1.00110.12 O ANISOU 1050 O ASN A 141 16715 13358 11767 -453 -1375 -1902 O ATOM 1051 CB ASN A 141 24.814 101.585 115.668 1.00117.84 C ANISOU 1051 CB ASN A 141 17523 13906 13347 -595 -1819 -2088 C ATOM 1052 CG ASN A 141 24.910 102.513 114.476 1.00120.34 C ANISOU 1052 CG ASN A 141 17552 14118 14055 -620 -1792 -2057 C ATOM 1053 OD1 ASN A 141 23.903 103.036 113.999 1.00123.99 O ANISOU 1053 OD1 ASN A 141 17972 14582 14556 -516 -1512 -2109 O ATOM 1054 ND2 ASN A 141 26.126 102.723 113.988 1.00117.98 N ANISOU 1054 ND2 ASN A 141 17040 13724 14064 -758 -2081 -1951 N ATOM 1055 N ARG A 142 23.244 100.482 118.248 1.00114.84 N ANISOU 1055 N ARG A 142 17930 13724 11979 -374 -1499 -2271 N ATOM 1056 CA ARG A 142 23.153 99.553 119.370 1.00119.04 C ANISOU 1056 CA ARG A 142 18745 14374 12112 -347 -1497 -2239 C ATOM 1057 C ARG A 142 21.860 98.750 119.310 1.00122.85 C ANISOU 1057 C ARG A 142 19167 15046 12466 -213 -1034 -2143 C ATOM 1058 O ARG A 142 21.848 97.557 119.634 1.00136.92 O ANISOU 1058 O ARG A 142 20935 16974 14114 -225 -989 -1983 O ATOM 1059 CB ARG A 142 23.254 100.314 120.692 1.00125.84 C ANISOU 1059 CB ARG A 142 20129 15102 12580 -310 -1670 -2477 C ATOM 1060 CG ARG A 142 23.229 99.428 121.927 1.00130.79 C ANISOU 1060 CG ARG A 142 21103 15847 12744 -283 -1696 -2441 C ATOM 1061 CD ARG A 142 23.063 100.255 123.191 1.00136.75 C ANISOU 1061 CD ARG A 142 22271 16519 13170 -199 -1721 -2638 C ATOM 1062 NE ARG A 142 21.808 101.003 123.191 1.00139.75 N ANISOU 1062 NE ARG A 142 22742 16880 13475 -18 -1298 -2790 N ATOM 1063 CZ ARG A 142 20.658 100.534 123.664 1.00140.79 C ANISOU 1063 CZ ARG A 142 22990 17162 13342 143 -864 -2754 C ATOM 1064 NH1 ARG A 142 20.598 99.314 124.179 1.00141.18 N ANISOU 1064 NH1 ARG A 142 23096 17390 13156 139 -799 -2572 N ATOM 1065 NH2 ARG A 142 19.566 101.284 123.622 1.00141.93 N ANISOU 1065 NH2 ARG A 142 23172 17269 13487 307 -491 -2881 N ATOM 1066 N THR A 143 20.764 99.386 118.890 1.00107.16 N ANISOU 1066 N THR A 143 17124 13042 10550 -88 -695 -2223 N ATOM 1067 CA THR A 143 19.498 98.672 118.767 1.00 97.04 C ANISOU 1067 CA THR A 143 15738 11921 9214 33 -262 -2113 C ATOM 1068 C THR A 143 19.552 97.647 117.639 1.00 89.84 C ANISOU 1068 C THR A 143 14383 11135 8619 -40 -217 -1880 C ATOM 1069 O THR A 143 19.040 96.531 117.783 1.00 91.44 O ANISOU 1069 O THR A 143 14520 11482 8740 -13 -33 -1727 O ATOM 1070 CB THR A 143 18.356 99.664 118.544 1.00 95.43 C ANISOU 1070 CB THR A 143 15547 11644 9066 182 61 -2243 C ATOM 1071 OG1 THR A 143 18.415 100.691 119.541 1.00105.91 O ANISOU 1071 OG1 THR A 143 17302 12822 10115 253 -6 -2492 O ATOM 1072 CG2 THR A 143 17.011 98.961 118.637 1.00 92.07 C ANISOU 1072 CG2 THR A 143 15050 11368 8565 315 506 -2127 C ATOM 1073 N ALA A 144 20.174 98.002 116.511 1.00 81.28 N ANISOU 1073 N ALA A 144 13002 9988 7892 -130 -381 -1847 N ATOM 1074 CA ALA A 144 20.323 97.041 115.424 1.00 76.57 C ANISOU 1074 CA ALA A 144 12023 9500 7568 -193 -356 -1649 C ATOM 1075 C ALA A 144 21.242 95.891 115.816 1.00 77.75 C ANISOU 1075 C ALA A 144 12174 9719 7650 -289 -572 -1518 C ATOM 1076 O ALA A 144 21.041 94.758 115.364 1.00 81.68 O ANISOU 1076 O ALA A 144 12463 10333 8239 -298 -466 -1358 O ATOM 1077 CB ALA A 144 20.847 97.737 114.168 1.00 72.32 C ANISOU 1077 CB ALA A 144 11205 8881 7392 -257 -472 -1641 C ATOM 1078 N ALA A 145 22.249 96.160 116.651 1.00 76.40 N ANISOU 1078 N ALA A 145 12231 9462 7335 -361 -892 -1583 N ATOM 1079 CA ALA A 145 23.113 95.090 117.135 1.00 79.96 C ANISOU 1079 CA ALA A 145 12697 9965 7717 -446 -1117 -1447 C ATOM 1080 C ALA A 145 22.368 94.151 118.074 1.00 92.88 C ANISOU 1080 C ALA A 145 14538 11728 9025 -374 -926 -1377 C ATOM 1081 O ALA A 145 22.640 92.945 118.088 1.00 99.35 O ANISOU 1081 O ALA A 145 15240 12635 9875 -417 -962 -1201 O ATOM 1082 CB ALA A 145 24.340 95.677 117.833 1.00 76.96 C ANISOU 1082 CB ALA A 145 12519 9448 7275 -546 -1541 -1527 C ATOM 1083 N ILE A 146 21.432 94.682 118.865 1.00 92.75 N ANISOU 1083 N ILE A 146 14822 11714 8703 -260 -709 -1503 N ATOM 1084 CA ILE A 146 20.615 93.831 119.725 1.00 91.49 C ANISOU 1084 CA ILE A 146 14842 11681 8238 -176 -464 -1411 C ATOM 1085 C ILE A 146 19.700 92.948 118.885 1.00 86.18 C ANISOU 1085 C ILE A 146 13830 11122 7794 -137 -147 -1244 C ATOM 1086 O ILE A 146 19.501 91.767 119.191 1.00 88.13 O ANISOU 1086 O ILE A 146 14042 11471 7975 -143 -68 -1067 O ATOM 1087 CB ILE A 146 19.817 94.690 120.723 1.00 96.46 C ANISOU 1087 CB ILE A 146 15873 12279 8497 -41 -264 -1591 C ATOM 1088 CG1 ILE A 146 20.761 95.386 121.706 1.00 95.49 C ANISOU 1088 CG1 ILE A 146 16151 12041 8090 -88 -627 -1758 C ATOM 1089 CG2 ILE A 146 18.793 93.844 121.468 1.00103.14 C ANISOU 1089 CG2 ILE A 146 16852 13267 9071 67 85 -1465 C ATOM 1090 CD1 ILE A 146 20.056 96.295 122.691 1.00 95.23 C ANISOU 1090 CD1 ILE A 146 16562 11955 7666 56 -446 -1975 C ATOM 1091 N ILE A 147 19.135 93.503 117.810 1.00 83.63 N ANISOU 1091 N ILE A 147 13252 10770 7753 -103 17 -1289 N ATOM 1092 CA ILE A 147 18.268 92.719 116.935 1.00 82.00 C ANISOU 1092 CA ILE A 147 12723 10652 7782 -78 271 -1142 C ATOM 1093 C ILE A 147 19.052 91.588 116.282 1.00 85.20 C ANISOU 1093 C ILE A 147 12872 11098 8403 -187 85 -984 C ATOM 1094 O ILE A 147 18.575 90.449 116.197 1.00 91.31 O ANISOU 1094 O ILE A 147 13516 11952 9225 -184 217 -826 O ATOM 1095 CB ILE A 147 17.605 93.630 115.885 1.00 73.07 C ANISOU 1095 CB ILE A 147 11387 9470 6906 -28 424 -1224 C ATOM 1096 CG1 ILE A 147 16.732 94.685 116.567 1.00 75.96 C ANISOU 1096 CG1 ILE A 147 11995 9783 7082 103 648 -1374 C ATOM 1097 CG2 ILE A 147 16.785 92.808 114.904 1.00 60.74 C ANISOU 1097 CG2 ILE A 147 9490 7985 5603 -20 619 -1074 C ATOM 1098 CD1 ILE A 147 16.161 95.715 115.613 1.00 74.45 C ANISOU 1098 CD1 ILE A 147 11622 9515 7149 153 762 -1457 C ATOM 1099 N SER A 148 20.269 91.880 115.819 1.00 80.97 N ANISOU 1099 N SER A 148 12254 10492 8019 -282 -217 -1019 N ATOM 1100 CA SER A 148 21.077 90.850 115.173 1.00 81.23 C ANISOU 1100 CA SER A 148 12041 10549 8275 -367 -375 -878 C ATOM 1101 C SER A 148 21.465 89.752 116.157 1.00 85.32 C ANISOU 1101 C SER A 148 12694 11112 8613 -400 -483 -748 C ATOM 1102 O SER A 148 21.497 88.571 115.794 1.00 91.98 O ANISOU 1102 O SER A 148 13349 12001 9598 -424 -459 -598 O ATOM 1103 CB SER A 148 22.320 91.476 114.542 1.00 78.73 C ANISOU 1103 CB SER A 148 11605 10140 8169 -450 -651 -926 C ATOM 1104 OG SER A 148 21.965 92.389 113.518 1.00 73.47 O ANISOU 1104 OG SER A 148 10785 9438 7692 -423 -544 -1008 O ATOM 1105 N CYS A 149 21.759 90.119 117.407 1.00 84.24 N ANISOU 1105 N CYS A 149 12897 10953 8159 -399 -612 -802 N ATOM 1106 CA CYS A 149 22.080 89.109 118.410 1.00 87.79 C ANISOU 1106 CA CYS A 149 13506 11451 8401 -427 -719 -661 C ATOM 1107 C CYS A 149 20.862 88.260 118.749 1.00 88.13 C ANISOU 1107 C CYS A 149 13565 11598 8322 -349 -385 -536 C ATOM 1108 O CYS A 149 20.971 87.037 118.899 1.00 94.21 O ANISOU 1108 O CYS A 149 14249 12412 9135 -381 -404 -350 O ATOM 1109 CB CYS A 149 22.636 89.772 119.669 1.00 94.44 C ANISOU 1109 CB CYS A 149 14748 12244 8891 -441 -951 -759 C ATOM 1110 SG CYS A 149 24.262 90.525 119.457 1.00101.67 S ANISOU 1110 SG CYS A 149 15627 13013 9989 -568 -1433 -843 S ATOM 1111 N LEU A 150 19.692 88.891 118.877 1.00 85.26 N ANISOU 1111 N LEU A 150 13297 11262 7837 -245 -74 -622 N ATOM 1112 CA LEU A 150 18.472 88.135 119.141 1.00 84.28 C ANISOU 1112 CA LEU A 150 13142 11227 7654 -170 269 -481 C ATOM 1113 C LEU A 150 18.120 87.223 117.975 1.00 80.85 C ANISOU 1113 C LEU A 150 12307 10808 7605 -205 355 -352 C ATOM 1114 O LEU A 150 17.590 86.126 118.183 1.00 89.25 O ANISOU 1114 O LEU A 150 13292 11923 8695 -201 491 -168 O ATOM 1115 CB LEU A 150 17.316 89.090 119.438 1.00 85.85 C ANISOU 1115 CB LEU A 150 13487 11433 7698 -41 594 -600 C ATOM 1116 CG LEU A 150 17.413 89.902 120.731 1.00 88.26 C ANISOU 1116 CG LEU A 150 14250 11725 7559 28 585 -735 C ATOM 1117 CD1 LEU A 150 16.320 90.955 120.777 1.00 88.37 C ANISOU 1117 CD1 LEU A 150 14351 11716 7509 168 915 -880 C ATOM 1118 CD2 LEU A 150 17.337 88.991 121.947 1.00 92.12 C ANISOU 1118 CD2 LEU A 150 14991 12303 7708 46 637 -568 C ATOM 1119 N LEU A 151 18.413 87.650 116.746 1.00 72.70 N ANISOU 1119 N LEU A 151 11029 9725 6869 -239 271 -443 N ATOM 1120 CA LEU A 151 18.140 86.810 115.587 1.00 72.74 C ANISOU 1120 CA LEU A 151 10692 9736 7211 -269 322 -348 C ATOM 1121 C LEU A 151 19.185 85.717 115.416 1.00 78.03 C ANISOU 1121 C LEU A 151 11251 10387 8009 -354 85 -235 C ATOM 1122 O LEU A 151 18.885 84.667 114.839 1.00 87.48 O ANISOU 1122 O LEU A 151 12236 11588 9414 -372 141 -121 O ATOM 1123 CB LEU A 151 18.053 87.666 114.326 1.00 71.38 C ANISOU 1123 CB LEU A 151 10327 9523 7272 -264 331 -477 C ATOM 1124 CG LEU A 151 16.781 88.509 114.245 1.00 70.91 C ANISOU 1124 CG LEU A 151 10279 9472 7193 -172 604 -546 C ATOM 1125 CD1 LEU A 151 16.908 89.558 113.163 1.00 65.56 C ANISOU 1125 CD1 LEU A 151 9470 8742 6697 -172 555 -677 C ATOM 1126 CD2 LEU A 151 15.571 87.621 113.996 1.00 72.18 C ANISOU 1126 CD2 LEU A 151 10262 9674 7490 -143 840 -403 C ATOM 1127 N TRP A 152 20.409 85.941 115.899 1.00 75.11 N ANISOU 1127 N TRP A 152 11013 9981 7544 -407 -191 -263 N ATOM 1128 CA TRP A 152 21.380 84.853 115.938 1.00 76.71 C ANISOU 1128 CA TRP A 152 11124 10160 7863 -475 -407 -128 C ATOM 1129 C TRP A 152 21.013 83.835 117.009 1.00 80.99 C ANISOU 1129 C TRP A 152 11805 10747 8220 -469 -351 50 C ATOM 1130 O TRP A 152 21.164 82.626 116.800 1.00 83.65 O ANISOU 1130 O TRP A 152 11982 11069 8732 -500 -383 202 O ATOM 1131 CB TRP A 152 22.788 85.398 116.174 1.00 77.35 C ANISOU 1131 CB TRP A 152 11279 10177 7932 -537 -736 -183 C ATOM 1132 CG TRP A 152 23.500 85.774 114.914 1.00 70.44 C ANISOU 1132 CG TRP A 152 10148 9245 7372 -566 -828 -254 C ATOM 1133 CD1 TRP A 152 23.894 87.023 114.536 1.00 65.91 C ANISOU 1133 CD1 TRP A 152 9580 8624 6838 -576 -907 -395 C ATOM 1134 CD2 TRP A 152 23.897 84.890 113.858 1.00 69.65 C ANISOU 1134 CD2 TRP A 152 9755 9123 7586 -579 -835 -180 C ATOM 1135 NE1 TRP A 152 24.516 86.973 113.312 1.00 65.36 N ANISOU 1135 NE1 TRP A 152 9233 8519 7082 -596 -947 -391 N ATOM 1136 CE2 TRP A 152 24.530 85.675 112.874 1.00 68.66 C ANISOU 1136 CE2 TRP A 152 9476 8954 7657 -591 -898 -273 C ATOM 1137 CE3 TRP A 152 23.780 83.512 113.651 1.00 64.49 C ANISOU 1137 CE3 TRP A 152 8962 8470 7069 -577 -790 -46 C ATOM 1138 CZ2 TRP A 152 25.045 85.129 111.700 1.00 71.72 C ANISOU 1138 CZ2 TRP A 152 9597 9316 8339 -588 -892 -240 C ATOM 1139 CZ3 TRP A 152 24.291 82.972 112.484 1.00 65.21 C ANISOU 1139 CZ3 TRP A 152 8795 8519 7464 -576 -805 -37 C ATOM 1140 CH2 TRP A 152 24.916 83.778 111.524 1.00 69.25 C ANISOU 1140 CH2 TRP A 152 9176 9002 8132 -575 -844 -135 C ATOM 1141 N GLY A 153 20.526 84.305 118.160 1.00 82.84 N ANISOU 1141 N GLY A 153 12347 11030 8098 -424 -257 38 N ATOM 1142 CA GLY A 153 20.066 83.390 119.191 1.00 87.53 C ANISOU 1142 CA GLY A 153 13089 11682 8488 -408 -155 230 C ATOM 1143 C GLY A 153 18.929 82.501 118.727 1.00 85.88 C ANISOU 1143 C GLY A 153 12655 11498 8476 -379 129 367 C ATOM 1144 O GLY A 153 18.817 81.352 119.162 1.00 85.62 O ANISOU 1144 O GLY A 153 12597 11475 8459 -401 146 576 O ATOM 1145 N ILE A 154 18.071 83.017 117.845 1.00 83.60 N ANISOU 1145 N ILE A 154 12197 11208 8360 -336 336 265 N ATOM 1146 CA ILE A 154 17.049 82.175 117.234 1.00 81.20 C ANISOU 1146 CA ILE A 154 11638 10902 8314 -328 546 388 C ATOM 1147 C ILE A 154 17.689 81.169 116.288 1.00 84.98 C ANISOU 1147 C ILE A 154 11853 11310 9126 -402 357 440 C ATOM 1148 O ILE A 154 17.324 79.988 116.274 1.00 91.78 O ANISOU 1148 O ILE A 154 12585 12146 10143 -426 404 612 O ATOM 1149 CB ILE A 154 16.001 83.044 116.516 1.00 76.73 C ANISOU 1149 CB ILE A 154 10957 10342 7855 -267 775 267 C ATOM 1150 CG1 ILE A 154 15.249 83.915 117.524 1.00 73.83 C ANISOU 1150 CG1 ILE A 154 10846 10032 7175 -170 1017 233 C ATOM 1151 CG2 ILE A 154 15.031 82.174 115.728 1.00 74.85 C ANISOU 1151 CG2 ILE A 154 10423 10078 7939 -279 920 385 C ATOM 1152 CD1 ILE A 154 14.215 84.818 116.893 1.00 68.69 C ANISOU 1152 CD1 ILE A 154 10077 9373 6649 -98 1246 127 C ATOM 1153 N THR A 155 18.660 81.618 115.487 1.00 80.65 N ANISOU 1153 N THR A 155 11223 10718 8702 -432 151 296 N ATOM 1154 CA THR A 155 19.359 80.707 114.587 1.00 81.86 C ANISOU 1154 CA THR A 155 11149 10800 9155 -480 -9 328 C ATOM 1155 C THR A 155 20.115 79.633 115.359 1.00 81.96 C ANISOU 1155 C THR A 155 11212 10780 9149 -522 -175 502 C ATOM 1156 O THR A 155 20.223 78.493 114.892 1.00 76.55 O ANISOU 1156 O THR A 155 10347 10028 8711 -546 -216 599 O ATOM 1157 CB THR A 155 20.313 81.491 113.684 1.00 79.24 C ANISOU 1157 CB THR A 155 10739 10436 8934 -491 -167 160 C ATOM 1158 OG1 THR A 155 19.593 82.543 113.029 1.00 78.31 O ANISOU 1158 OG1 THR A 155 10590 10345 8818 -452 -20 17 O ATOM 1159 CG2 THR A 155 20.926 80.581 112.629 1.00 75.51 C ANISOU 1159 CG2 THR A 155 10030 9891 8769 -513 -269 177 C ATOM 1160 N ILE A 156 20.635 79.974 116.540 1.00 83.54 N ANISOU 1160 N ILE A 156 11665 11017 9060 -530 -287 544 N ATOM 1161 CA ILE A 156 21.295 78.977 117.379 1.00 80.98 C ANISOU 1161 CA ILE A 156 11409 10667 8694 -571 -457 738 C ATOM 1162 C ILE A 156 20.308 77.889 117.783 1.00 79.49 C ANISOU 1162 C ILE A 156 11187 10488 8529 -563 -265 944 C ATOM 1163 O ILE A 156 20.539 76.698 117.546 1.00 81.20 O ANISOU 1163 O ILE A 156 11238 10627 8987 -595 -339 1085 O ATOM 1164 CB ILE A 156 21.931 79.644 118.613 1.00 81.81 C ANISOU 1164 CB ILE A 156 11837 10814 8435 -582 -627 737 C ATOM 1165 CG1 ILE A 156 23.058 80.596 118.202 1.00 79.31 C ANISOU 1165 CG1 ILE A 156 11510 10452 8172 -611 -874 565 C ATOM 1166 CG2 ILE A 156 22.447 78.590 119.583 1.00 81.65 C ANISOU 1166 CG2 ILE A 156 11913 10779 8333 -621 -793 973 C ATOM 1167 CD1 ILE A 156 24.293 79.903 117.683 1.00 79.32 C ANISOU 1167 CD1 ILE A 156 11294 10359 8484 -663 -1131 634 C ATOM 1168 N GLY A 157 19.181 78.288 118.378 1.00 78.75 N ANISOU 1168 N GLY A 157 11235 10476 8211 -514 -3 972 N ATOM 1169 CA GLY A 157 18.245 77.310 118.914 1.00 82.15 C ANISOU 1169 CA GLY A 157 11643 10919 8653 -508 195 1207 C ATOM 1170 C GLY A 157 17.680 76.376 117.860 1.00 81.63 C ANISOU 1170 C GLY A 157 11247 10763 9007 -534 265 1260 C ATOM 1171 O GLY A 157 17.475 75.188 118.117 1.00 88.69 O ANISOU 1171 O GLY A 157 12053 11602 10045 -567 274 1477 O ATOM 1172 N LEU A 158 17.422 76.898 116.659 1.00 77.84 N ANISOU 1172 N LEU A 158 10590 10256 8729 -523 300 1066 N ATOM 1173 CA LEU A 158 16.887 76.057 115.594 1.00 73.15 C ANISOU 1173 CA LEU A 158 9713 9566 8516 -550 331 1086 C ATOM 1174 C LEU A 158 17.898 75.015 115.132 1.00 73.79 C ANISOU 1174 C LEU A 158 9670 9531 8837 -594 92 1118 C ATOM 1175 O LEU A 158 17.506 73.938 114.669 1.00 75.96 O ANISOU 1175 O LEU A 158 9765 9702 9397 -623 97 1210 O ATOM 1176 CB LEU A 158 16.453 76.917 114.407 1.00 69.84 C ANISOU 1176 CB LEU A 158 9169 9150 8216 -525 393 867 C ATOM 1177 CG LEU A 158 15.376 77.972 114.652 1.00 70.14 C ANISOU 1177 CG LEU A 158 9276 9274 8099 -470 638 820 C ATOM 1178 CD1 LEU A 158 15.151 78.789 113.390 1.00 69.35 C ANISOU 1178 CD1 LEU A 158 9045 9163 8141 -453 636 612 C ATOM 1179 CD2 LEU A 158 14.082 77.322 115.115 1.00 69.96 C ANISOU 1179 CD2 LEU A 158 9174 9248 8162 -466 873 1031 C ATOM 1180 N THR A 159 19.192 75.310 115.250 1.00 73.47 N ANISOU 1180 N THR A 159 9713 9491 8712 -598 -120 1049 N ATOM 1181 CA THR A 159 20.239 74.454 114.711 1.00 74.74 C ANISOU 1181 CA THR A 159 9735 9536 9128 -620 -331 1058 C ATOM 1182 C THR A 159 21.137 73.844 115.779 1.00 77.84 C ANISOU 1182 C THR A 159 10236 9905 9436 -647 -513 1247 C ATOM 1183 O THR A 159 22.026 73.055 115.439 1.00 76.46 O ANISOU 1183 O THR A 159 9934 9618 9498 -657 -685 1286 O ATOM 1184 CB THR A 159 21.101 75.240 113.714 1.00 75.56 C ANISOU 1184 CB THR A 159 9772 9633 9304 -598 -436 832 C ATOM 1185 OG1 THR A 159 21.793 76.291 114.401 1.00 75.98 O ANISOU 1185 OG1 THR A 159 10007 9765 9095 -599 -534 785 O ATOM 1186 CG2 THR A 159 20.236 75.847 112.619 1.00 71.69 C ANISOU 1186 CG2 THR A 159 9185 9166 8886 -572 -278 659 C ATOM 1187 N VAL A 160 20.932 74.178 117.057 1.00 82.52 N ANISOU 1187 N VAL A 160 11066 10594 9694 -652 -480 1369 N ATOM 1188 CA VAL A 160 21.821 73.685 118.105 1.00 86.23 C ANISOU 1188 CA VAL A 160 11671 11050 10043 -682 -690 1554 C ATOM 1189 C VAL A 160 21.659 72.187 118.334 1.00 97.96 C ANISOU 1189 C VAL A 160 13037 12431 11750 -709 -704 1805 C ATOM 1190 O VAL A 160 22.569 71.544 118.871 1.00105.18 O ANISOU 1190 O VAL A 160 13975 13285 12704 -735 -925 1960 O ATOM 1191 CB VAL A 160 21.590 74.462 119.418 1.00 80.20 C ANISOU 1191 CB VAL A 160 11242 10422 8810 -671 -648 1607 C ATOM 1192 CG1 VAL A 160 20.278 74.046 120.070 1.00 79.01 C ANISOU 1192 CG1 VAL A 160 11165 10330 8525 -652 -362 1787 C ATOM 1193 CG2 VAL A 160 22.764 74.280 120.374 1.00 78.86 C ANISOU 1193 CG2 VAL A 160 11243 10241 8481 -708 -953 1735 C ATOM 1194 N HIS A 161 20.527 71.605 117.928 1.00 98.00 N ANISOU 1194 N HIS A 161 12904 12398 11933 -708 -492 1859 N ATOM 1195 CA HIS A 161 20.302 70.182 118.151 1.00 94.93 C ANISOU 1195 CA HIS A 161 12396 11889 11785 -741 -505 2107 C ATOM 1196 C HIS A 161 21.276 69.307 117.371 1.00 98.63 C ANISOU 1196 C HIS A 161 12661 12182 12632 -749 -722 2076 C ATOM 1197 O HIS A 161 21.478 68.147 117.742 1.00109.51 O ANISOU 1197 O HIS A 161 13974 13442 14195 -775 -812 2296 O ATOM 1198 CB HIS A 161 18.861 69.812 117.794 1.00 95.05 C ANISOU 1198 CB HIS A 161 12278 11878 11958 -748 -250 2160 C ATOM 1199 CG HIS A 161 18.513 70.039 116.355 1.00 96.21 C ANISOU 1199 CG HIS A 161 12226 11961 12366 -736 -210 1910 C ATOM 1200 ND1 HIS A 161 18.985 69.237 115.339 1.00 94.90 N ANISOU 1200 ND1 HIS A 161 11866 11627 12564 -743 -353 1825 N ATOM 1201 CD2 HIS A 161 17.731 70.973 115.764 1.00 96.46 C ANISOU 1201 CD2 HIS A 161 12240 12072 12340 -711 -48 1729 C ATOM 1202 CE1 HIS A 161 18.513 69.669 114.184 1.00 93.76 C ANISOU 1202 CE1 HIS A 161 11613 11470 12540 -726 -288 1600 C ATOM 1203 NE2 HIS A 161 17.749 70.721 114.413 1.00 93.94 N ANISOU 1203 NE2 HIS A 161 11728 11641 12325 -711 -113 1548 N ATOM 1204 N LEU A 162 21.887 69.835 116.308 1.00 92.11 N ANISOU 1204 N LEU A 162 11736 11331 11930 -718 -792 1818 N ATOM 1205 CA LEU A 162 22.840 69.061 115.521 1.00 88.74 C ANISOU 1205 CA LEU A 162 11123 10737 11855 -700 -958 1771 C ATOM 1206 C LEU A 162 24.145 68.805 116.259 1.00 94.11 C ANISOU 1206 C LEU A 162 11849 11382 12525 -707 -1204 1914 C ATOM 1207 O LEU A 162 24.947 67.988 115.795 1.00 96.38 O ANISOU 1207 O LEU A 162 11973 11512 13136 -685 -1336 1934 O ATOM 1208 CB LEU A 162 23.122 69.773 114.200 1.00 84.01 C ANISOU 1208 CB LEU A 162 10424 10141 11354 -653 -929 1471 C ATOM 1209 CG LEU A 162 21.935 69.809 113.238 1.00 83.40 C ANISOU 1209 CG LEU A 162 10261 10053 11375 -646 -743 1328 C ATOM 1210 CD1 LEU A 162 21.839 71.163 112.568 1.00 82.04 C ANISOU 1210 CD1 LEU A 162 10130 10005 11037 -617 -662 1089 C ATOM 1211 CD2 LEU A 162 22.055 68.703 112.202 1.00 80.28 C ANISOU 1211 CD2 LEU A 162 9681 9462 11361 -623 -787 1264 C ATOM 1212 N LEU A 163 24.378 69.480 117.383 1.00 97.19 N ANISOU 1212 N LEU A 163 12462 11905 12562 -733 -1279 2009 N ATOM 1213 CA LEU A 163 25.538 69.220 118.223 1.00 98.90 C ANISOU 1213 CA LEU A 163 12743 12087 12747 -755 -1552 2181 C ATOM 1214 C LEU A 163 25.283 68.143 119.270 1.00101.32 C ANISOU 1214 C LEU A 163 13118 12350 13031 -791 -1597 2509 C ATOM 1215 O LEU A 163 26.235 67.687 119.913 1.00 98.94 O ANISOU 1215 O LEU A 163 12836 11986 12769 -811 -1848 2691 O ATOM 1216 CB LEU A 163 25.984 70.511 118.920 1.00 95.67 C ANISOU 1216 CB LEU A 163 12570 11826 11953 -772 -1661 2110 C ATOM 1217 CG LEU A 163 26.473 71.644 118.016 1.00 94.62 C ANISOU 1217 CG LEU A 163 12372 11726 11855 -747 -1672 1826 C ATOM 1218 CD1 LEU A 163 26.697 72.916 118.821 1.00 99.63 C ANISOU 1218 CD1 LEU A 163 13272 12491 12091 -772 -1771 1761 C ATOM 1219 CD2 LEU A 163 27.746 71.234 117.294 1.00 88.67 C ANISOU 1219 CD2 LEU A 163 11376 10829 11486 -726 -1858 1806 C ATOM 1220 N LYS A 164 24.030 67.724 119.453 1.00103.22 N ANISOU 1220 N LYS A 164 13380 12612 13229 -802 -1366 2610 N ATOM 1221 CA LYS A 164 23.718 66.716 120.460 1.00108.38 C ANISOU 1221 CA LYS A 164 14095 13227 13857 -838 -1379 2952 C ATOM 1222 C LYS A 164 23.944 65.303 119.934 1.00108.56 C ANISOU 1222 C LYS A 164 13858 13017 14373 -843 -1459 3072 C ATOM 1223 O LYS A 164 24.510 64.460 120.639 1.00113.85 O ANISOU 1223 O LYS A 164 14532 13597 15128 -865 -1638 3338 O ATOM 1224 CB LYS A 164 22.277 66.884 120.941 1.00109.12 C ANISOU 1224 CB LYS A 164 14308 13439 13716 -846 -1076 3043 C ATOM 1225 N LYS A 165 23.524 65.028 118.701 1.00105.19 N ANISOU 1225 N LYS A 165 13217 12477 14272 -819 -1344 2877 N ATOM 1226 CA LYS A 165 23.644 63.684 118.152 1.00104.48 C ANISOU 1226 CA LYS A 165 12902 12142 14655 -816 -1409 2957 C ATOM 1227 C LYS A 165 25.107 63.329 117.910 1.00105.13 C ANISOU 1227 C LYS A 165 12879 12093 14974 -775 -1659 2938 C ATOM 1228 O LYS A 165 25.868 64.127 117.354 1.00 97.62 O ANISOU 1228 O LYS A 165 11912 11193 13988 -732 -1717 2713 O ATOM 1229 CB LYS A 165 22.850 63.572 116.852 1.00 98.49 C ANISOU 1229 CB LYS A 165 11981 11296 14147 -797 -1249 2714 C ATOM 1230 N LYS A 166 25.497 62.127 118.331 1.00109.48 N ANISOU 1230 N LYS A 166 13340 12464 15792 -786 -1801 3193 N ATOM 1231 CA LYS A 166 26.866 61.662 118.160 1.00104.34 C ANISOU 1231 CA LYS A 166 12558 11660 15426 -739 -2035 3218 C ATOM 1232 C LYS A 166 27.102 61.198 116.728 1.00 99.47 C ANISOU 1232 C LYS A 166 11717 10848 15231 -660 -1981 2959 C ATOM 1233 O LYS A 166 26.229 60.589 116.103 1.00101.78 O ANISOU 1233 O LYS A 166 11931 11024 15719 -661 -1847 2888 O ATOM 1234 CB LYS A 166 27.168 60.525 119.136 1.00102.51 C ANISOU 1234 CB LYS A 166 12310 11293 15345 -774 -2208 3601 C ATOM 1235 N MET A 167 28.292 61.485 116.218 1.00 96.59 N ANISOU 1235 N MET A 167 11253 10440 15006 -589 -2090 2825 N ATOM 1236 CA MET A 167 28.668 61.215 114.840 1.00 97.85 C ANISOU 1236 CA MET A 167 11234 10443 15503 -488 -2015 2555 C ATOM 1237 C MET A 167 30.058 60.595 114.828 1.00100.99 C ANISOU 1237 C MET A 167 11460 10656 16253 -413 -2197 2655 C ATOM 1238 O MET A 167 30.791 60.694 115.817 1.00105.22 O ANISOU 1238 O MET A 167 12025 11234 16722 -449 -2402 2893 O ATOM 1239 CB MET A 167 28.651 62.504 114.005 1.00100.58 C ANISOU 1239 CB MET A 167 11624 10963 15629 -455 -1881 2240 C ATOM 1240 CG MET A 167 27.313 63.232 113.989 1.00100.99 C ANISOU 1240 CG MET A 167 11827 11197 15346 -519 -1702 2137 C ATOM 1241 SD MET A 167 26.002 62.293 113.183 1.00102.75 S ANISOU 1241 SD MET A 167 11983 11260 15796 -526 -1547 2045 S ATOM 1242 CE MET A 167 26.669 62.131 111.529 1.00 98.43 C ANISOU 1242 CE MET A 167 11296 10559 15542 -396 -1499 1704 C ATOM 1243 N PRO A 168 30.446 59.932 113.724 1.00102.13 N ANISOU 1243 N PRO A 168 11431 10587 16785 -302 -2132 2480 N ATOM 1244 CA PRO A 168 29.693 59.615 112.504 1.00103.00 C ANISOU 1244 CA PRO A 168 11517 10598 17022 -249 -1939 2198 C ATOM 1245 C PRO A 168 28.798 58.392 112.669 1.00112.16 C ANISOU 1245 C PRO A 168 12662 11561 18395 -294 -1944 2322 C ATOM 1246 O PRO A 168 28.553 57.949 113.791 1.00118.09 O ANISOU 1246 O PRO A 168 13448 12307 19114 -381 -2053 2638 O ATOM 1247 CB PRO A 168 30.795 59.340 111.468 1.00101.23 C ANISOU 1247 CB PRO A 168 11125 10204 17132 -93 -1907 2013 C ATOM 1248 CG PRO A 168 32.081 59.792 112.107 1.00103.99 C ANISOU 1248 CG PRO A 168 11394 10614 17502 -77 -2064 2185 C ATOM 1249 CD PRO A 168 31.870 59.600 113.568 1.00105.01 C ANISOU 1249 CD PRO A 168 11613 10802 17484 -203 -2259 2531 C ATOM 1250 N ILE A 169 28.320 57.854 111.550 1.00113.17 N ANISOU 1250 N ILE A 169 12744 11518 18736 -236 -1836 2078 N ATOM 1251 CA ILE A 169 27.459 56.677 111.537 1.00115.19 C ANISOU 1251 CA ILE A 169 12968 11545 19253 -280 -1855 2158 C ATOM 1252 C ILE A 169 28.042 55.683 110.544 1.00119.85 C ANISOU 1252 C ILE A 169 13439 11817 20283 -145 -1864 1975 C ATOM 1253 O ILE A 169 28.208 56.007 109.362 1.00127.37 O ANISOU 1253 O ILE A 169 14406 12758 21229 -43 -1748 1638 O ATOM 1254 CB ILE A 169 26.007 57.029 111.170 1.00113.23 C ANISOU 1254 CB ILE A 169 12817 11394 18812 -367 -1730 2027 C ATOM 1255 CG1 ILE A 169 25.357 57.834 112.297 1.00110.39 C ANISOU 1255 CG1 ILE A 169 12571 11312 18058 -490 -1699 2252 C ATOM 1256 CG2 ILE A 169 25.210 55.770 110.873 1.00119.00 C ANISOU 1256 CG2 ILE A 169 13483 11833 19900 -401 -1767 2051 C ATOM 1257 CD1 ILE A 169 23.944 58.272 111.996 1.00111.16 C ANISOU 1257 CD1 ILE A 169 12737 11517 17984 -569 -1561 2152 C ATOM 1258 N GLN A 170 28.353 54.480 111.020 1.00118.35 N ANISOU 1258 N GLN A 170 13142 11362 20462 -135 -1995 2199 N ATOM 1259 CA GLN A 170 28.981 53.480 110.169 1.00112.89 C ANISOU 1259 CA GLN A 170 12339 10338 20217 10 -2005 2039 C ATOM 1260 C GLN A 170 27.972 52.896 109.188 1.00111.47 C ANISOU 1260 C GLN A 170 12212 9966 20175 9 -1945 1776 C ATOM 1261 O GLN A 170 26.831 52.593 109.549 1.00111.50 O ANISOU 1261 O GLN A 170 12253 9948 20165 -127 -1982 1896 O ATOM 1262 CB GLN A 170 29.593 52.368 111.020 1.00108.73 C ANISOU 1262 CB GLN A 170 11677 9569 20069 18 -2179 2377 C ATOM 1263 N ASN A 171 28.400 52.744 107.938 1.00110.09 N ANISOU 1263 N ASN A 171 12045 9648 20137 165 -1853 1423 N ATOM 1264 CA ASN A 171 27.563 52.158 106.896 1.00110.43 C ANISOU 1264 CA ASN A 171 12166 9477 20314 181 -1830 1129 C ATOM 1265 C ASN A 171 28.411 51.714 105.709 1.00118.98 C ANISOU 1265 C ASN A 171 13251 10335 21621 398 -1744 798 C ATOM 1266 O ASN A 171 28.072 51.985 104.556 1.00120.85 O ANISOU 1266 O ASN A 171 13621 10576 21721 462 -1645 437 O ATOM 1267 CB ASN A 171 26.493 53.151 106.436 1.00 95.16 C ANISOU 1267 CB ASN A 171 10374 7800 17983 86 -1746 946 C ATOM 1268 N ALA A 174 32.948 52.010 106.425 1.00123.97 N ANISOU 1268 N ALA A 174 13399 10953 22749 832 -1638 1156 N ATOM 1269 CA ALA A 174 32.961 53.432 106.100 1.00121.45 C ANISOU 1269 CA ALA A 174 13164 10994 21989 810 -1507 1021 C ATOM 1270 C ALA A 174 32.019 54.208 107.013 1.00120.62 C ANISOU 1270 C ALA A 174 13161 11179 21490 582 -1612 1206 C ATOM 1271 O ALA A 174 30.944 53.723 107.364 1.00120.11 O ANISOU 1271 O ALA A 174 13173 11053 21410 454 -1701 1279 O ATOM 1272 CB ALA A 174 32.584 53.646 104.643 1.00120.73 C ANISOU 1272 CB ALA A 174 13227 10892 21753 921 -1299 585 C ATOM 1273 N ASN A 175 32.429 55.415 107.394 1.00121.50 N ANISOU 1273 N ASN A 175 13270 11595 21300 538 -1595 1284 N ATOM 1274 CA ASN A 175 31.648 56.278 108.268 1.00122.25 C ANISOU 1274 CA ASN A 175 13478 11977 20993 348 -1669 1440 C ATOM 1275 C ASN A 175 31.130 57.478 107.487 1.00113.87 C ANISOU 1275 C ASN A 175 12554 11172 19541 336 -1503 1163 C ATOM 1276 O ASN A 175 31.868 58.092 106.711 1.00112.70 O ANISOU 1276 O ASN A 175 12374 11092 19357 453 -1371 982 O ATOM 1277 CB ASN A 175 32.481 56.753 109.462 1.00130.30 C ANISOU 1277 CB ASN A 175 14417 13137 21954 288 -1826 1765 C ATOM 1278 CG ASN A 175 32.891 55.616 110.378 1.00139.44 C ANISOU 1278 CG ASN A 175 15455 14067 23459 274 -2025 2093 C ATOM 1279 OD1 ASN A 175 32.959 54.460 109.961 1.00151.85 O ANISOU 1279 OD1 ASN A 175 16943 15334 25417 363 -2020 2055 O ATOM 1280 ND2 ASN A 175 33.163 55.940 111.637 1.00138.58 N ANISOU 1280 ND2 ASN A 175 15351 14095 23207 164 -2211 2417 N ATOM 1281 N LEU A 176 29.859 57.809 107.701 1.00104.47 N ANISOU 1281 N LEU A 176 11503 10116 18077 196 -1504 1153 N ATOM 1282 CA LEU A 176 29.205 58.924 107.034 1.00 95.86 C ANISOU 1282 CA LEU A 176 10542 9258 16623 168 -1369 919 C ATOM 1283 C LEU A 176 28.948 60.046 108.030 1.00 92.54 C ANISOU 1283 C LEU A 176 10188 9136 15838 36 -1409 1097 C ATOM 1284 O LEU A 176 28.588 59.794 109.183 1.00 91.40 O ANISOU 1284 O LEU A 176 10058 9014 15654 -76 -1525 1371 O ATOM 1285 CB LEU A 176 27.879 58.495 106.395 1.00 94.71 C ANISOU 1285 CB LEU A 176 10498 9023 16465 118 -1336 744 C ATOM 1286 CG LEU A 176 27.923 57.635 105.131 1.00 97.86 C ANISOU 1286 CG LEU A 176 10912 9156 17116 250 -1283 456 C ATOM 1287 CD1 LEU A 176 28.272 56.188 105.449 1.00106.89 C ANISOU 1287 CD1 LEU A 176 11950 9962 18700 292 -1396 587 C ATOM 1288 CD2 LEU A 176 26.599 57.718 104.389 1.00 93.42 C ANISOU 1288 CD2 LEU A 176 10484 8599 16414 182 -1263 242 C ATOM 1289 N CYS A 177 29.127 61.283 107.577 1.00 87.18 N ANISOU 1289 N CYS A 177 9561 8677 14886 55 -1305 941 N ATOM 1290 CA CYS A 177 28.863 62.473 108.386 1.00 89.48 C ANISOU 1290 CA CYS A 177 9941 9244 14813 -56 -1328 1050 C ATOM 1291 C CYS A 177 27.681 63.215 107.764 1.00 88.07 C ANISOU 1291 C CYS A 177 9889 9214 14360 -103 -1198 847 C ATOM 1292 O CYS A 177 27.851 64.057 106.881 1.00 82.00 O ANISOU 1292 O CYS A 177 9147 8553 13457 -45 -1085 632 O ATOM 1293 CB CYS A 177 30.093 63.367 108.473 1.00 91.29 C ANISOU 1293 CB CYS A 177 10109 9591 14988 -7 -1348 1068 C ATOM 1294 SG CYS A 177 29.790 64.951 109.290 1.00 90.41 S ANISOU 1294 SG CYS A 177 10137 9795 14419 -130 -1378 1130 S ATOM 1295 N SER A 178 26.478 62.901 108.240 1.00 90.50 N ANISOU 1295 N SER A 178 10261 9523 14602 -208 -1212 939 N ATOM 1296 CA SER A 178 25.269 63.527 107.725 1.00 95.21 C ANISOU 1296 CA SER A 178 10950 10239 14986 -260 -1107 784 C ATOM 1297 C SER A 178 24.158 63.393 108.754 1.00 97.14 C ANISOU 1297 C SER A 178 11240 10538 15132 -389 -1123 1006 C ATOM 1298 O SER A 178 24.091 62.406 109.493 1.00 94.21 O ANISOU 1298 O SER A 178 10822 10028 14945 -429 -1209 1230 O ATOM 1299 CB SER A 178 24.840 62.905 106.388 1.00 95.37 C ANISOU 1299 CB SER A 178 10963 10087 15187 -198 -1063 528 C ATOM 1300 OG SER A 178 23.502 63.246 106.062 1.00 93.14 O ANISOU 1300 OG SER A 178 10747 9874 14770 -276 -1017 445 O ATOM 1301 N SER A 179 23.305 64.415 108.805 1.00104.85 N ANISOU 1301 N SER A 179 12302 11715 15823 -445 -1026 956 N ATOM 1302 CA SER A 179 22.036 64.351 109.527 1.00113.57 C ANISOU 1302 CA SER A 179 13438 12869 16845 -549 -979 1125 C ATOM 1303 C SER A 179 20.992 63.888 108.520 1.00112.43 C ANISOU 1303 C SER A 179 13244 12596 16878 -567 -951 971 C ATOM 1304 O SER A 179 20.519 64.676 107.694 1.00120.50 O ANISOU 1304 O SER A 179 14302 13715 17769 -554 -881 763 O ATOM 1305 CB SER A 179 21.674 65.706 110.129 1.00118.75 C ANISOU 1305 CB SER A 179 14207 13791 17122 -585 -881 1151 C ATOM 1306 OG SER A 179 20.438 65.652 110.825 1.00122.23 O ANISOU 1306 OG SER A 179 14670 14281 17490 -667 -793 1324 O ATOM 1307 N PHE A 180 20.651 62.599 108.569 1.00106.98 N ANISOU 1307 N PHE A 180 12472 11672 16503 -599 -1030 1076 N ATOM 1308 CA PHE A 180 19.702 62.018 107.627 1.00103.39 C ANISOU 1308 CA PHE A 180 11970 11048 16266 -627 -1059 934 C ATOM 1309 C PHE A 180 18.307 62.604 107.823 1.00108.93 C ANISOU 1309 C PHE A 180 12667 11875 16849 -723 -969 1002 C ATOM 1310 O PHE A 180 17.462 62.011 108.506 1.00116.21 O ANISOU 1310 O PHE A 180 13515 12722 17918 -813 -964 1242 O ATOM 1311 CB PHE A 180 19.672 60.494 107.776 1.00100.25 C ANISOU 1311 CB PHE A 180 11479 10348 16263 -651 -1182 1062 C ATOM 1312 CG PHE A 180 21.016 59.838 107.593 1.00 95.54 C ANISOU 1312 CG PHE A 180 10866 9598 15837 -545 -1262 1008 C ATOM 1313 CD1 PHE A 180 21.492 59.545 106.325 1.00 91.85 C ANISOU 1313 CD1 PHE A 180 10419 8982 15498 -438 -1291 699 C ATOM 1314 CD2 PHE A 180 21.802 59.516 108.688 1.00 91.10 C ANISOU 1314 CD2 PHE A 180 10272 9036 15306 -542 -1305 1274 C ATOM 1315 CE1 PHE A 180 22.728 58.942 106.152 1.00 80.78 C ANISOU 1315 CE1 PHE A 180 8984 7429 14279 -321 -1331 656 C ATOM 1316 CE2 PHE A 180 23.041 58.912 108.521 1.00 84.65 C ANISOU 1316 CE2 PHE A 180 9409 8065 14691 -439 -1381 1243 C ATOM 1317 CZ PHE A 180 23.503 58.626 107.250 1.00 78.36 C ANISOU 1317 CZ PHE A 180 8611 7115 14048 -323 -1379 934 C ATOM 1318 N SER A 181 18.063 63.776 107.234 1.00106.97 N ANISOU 1318 N SER A 181 12481 11810 16352 -700 -887 812 N ATOM 1319 CA SER A 181 16.757 64.418 107.268 1.00108.78 C ANISOU 1319 CA SER A 181 12690 12150 16492 -772 -797 849 C ATOM 1320 C SER A 181 15.896 64.068 106.061 1.00107.51 C ANISOU 1320 C SER A 181 12477 11837 16535 -801 -887 663 C ATOM 1321 O SER A 181 14.679 64.284 106.103 1.00117.30 O ANISOU 1321 O SER A 181 13645 13098 17824 -879 -850 743 O ATOM 1322 CB SER A 181 16.915 65.944 107.362 1.00112.09 C ANISOU 1322 CB SER A 181 13204 12845 16539 -734 -670 766 C ATOM 1323 OG SER A 181 17.698 66.457 106.296 1.00113.87 O ANISOU 1323 OG SER A 181 13491 13102 16671 -649 -702 490 O ATOM 1324 N ILE A 182 16.496 63.529 104.993 1.00 89.49 N ANISOU 1324 N ILE A 182 10233 9395 14375 -735 -1007 421 N ATOM 1325 CA ILE A 182 15.728 63.086 103.831 1.00 81.59 C ANISOU 1325 CA ILE A 182 9221 8220 13559 -763 -1137 227 C ATOM 1326 C ILE A 182 15.100 61.719 104.035 1.00 87.71 C ANISOU 1326 C ILE A 182 9886 8709 14731 -850 -1274 364 C ATOM 1327 O ILE A 182 14.343 61.261 103.169 1.00 89.94 O ANISOU 1327 O ILE A 182 10151 8814 15209 -897 -1423 228 O ATOM 1328 CB ILE A 182 16.599 63.039 102.558 1.00 77.04 C ANISOU 1328 CB ILE A 182 8768 7578 12924 -642 -1197 -107 C ATOM 1329 CG1 ILE A 182 17.673 61.955 102.679 1.00 82.10 C ANISOU 1329 CG1 ILE A 182 9411 8020 13764 -567 -1249 -111 C ATOM 1330 CG2 ILE A 182 17.248 64.383 102.308 1.00 80.17 C ANISOU 1330 CG2 ILE A 182 9256 8243 12962 -560 -1060 -222 C ATOM 1331 CD1 ILE A 182 18.549 61.823 101.437 1.00 55.75 C ANISOU 1331 CD1 ILE A 182 6197 4600 10387 -425 -1268 -434 C ATOM 1332 N CYS A 183 15.397 61.050 105.149 1.00 96.04 N ANISOU 1332 N CYS A 183 10870 9704 15918 -878 -1249 636 N ATOM 1333 CA CYS A 183 14.817 59.756 105.484 1.00104.26 C ANISOU 1333 CA CYS A 183 11787 10469 17358 -969 -1367 823 C ATOM 1334 C CYS A 183 13.801 59.860 106.616 1.00101.28 C ANISOU 1334 C CYS A 183 11281 10176 17023 -1085 -1255 1186 C ATOM 1335 O CYS A 183 13.375 58.835 107.163 1.00103.81 O ANISOU 1335 O CYS A 183 11480 10298 17665 -1167 -1313 1428 O ATOM 1336 CB CYS A 183 15.924 58.759 105.843 1.00115.47 C ANISOU 1336 CB CYS A 183 13212 11712 18949 -908 -1431 883 C ATOM 1337 SG CYS A 183 16.838 58.096 104.423 1.00123.83 S ANISOU 1337 SG CYS A 183 14377 12527 20145 -777 -1577 481 S ATOM 1338 N HIS A 184 13.402 61.075 106.976 1.00101.85 N ANISOU 1338 N HIS A 184 11378 10531 16788 -1086 -1082 1234 N ATOM 1339 CA HIS A 184 12.389 61.300 107.995 1.00103.13 C ANISOU 1339 CA HIS A 184 11434 10796 16957 -1171 -925 1559 C ATOM 1340 C HIS A 184 11.086 61.691 107.310 1.00100.50 C ANISOU 1340 C HIS A 184 10995 10448 16743 -1240 -940 1496 C ATOM 1341 O HIS A 184 11.066 62.610 106.483 1.00 96.94 O ANISOU 1341 O HIS A 184 10620 10121 16094 -1194 -945 1241 O ATOM 1342 CB HIS A 184 12.833 62.389 108.975 1.00104.17 C ANISOU 1342 CB HIS A 184 11679 11238 16663 -1113 -711 1666 C ATOM 1343 CG HIS A 184 12.032 62.428 110.241 1.00113.15 C ANISOU 1343 CG HIS A 184 12748 12468 17775 -1173 -519 2034 C ATOM 1344 ND1 HIS A 184 10.667 62.234 110.264 1.00117.63 N ANISOU 1344 ND1 HIS A 184 13141 12964 18590 -1262 -456 2202 N ATOM 1345 CD2 HIS A 184 12.404 62.630 111.527 1.00115.88 C ANISOU 1345 CD2 HIS A 184 13185 12970 17875 -1151 -370 2276 C ATOM 1346 CE1 HIS A 184 10.233 62.318 111.509 1.00119.67 C ANISOU 1346 CE1 HIS A 184 13380 13337 18754 -1281 -240 2537 C ATOM 1347 NE2 HIS A 184 11.267 62.558 112.295 1.00118.60 N ANISOU 1347 NE2 HIS A 184 13424 13344 18295 -1214 -189 2580 N ATOM 1348 N THR A 185 10.009 60.981 107.640 1.00102.27 N ANISOU 1348 N THR A 185 11031 10511 17317 -1354 -957 1746 N ATOM 1349 CA THR A 185 8.702 61.307 107.091 1.00100.56 C ANISOU 1349 CA THR A 185 10670 10264 17275 -1432 -982 1742 C ATOM 1350 C THR A 185 8.232 62.662 107.614 1.00 98.36 C ANISOU 1350 C THR A 185 10399 10292 16682 -1395 -715 1827 C ATOM 1351 O THR A 185 8.743 63.186 108.607 1.00 92.74 O ANISOU 1351 O THR A 185 9789 9790 15658 -1331 -502 1953 O ATOM 1352 CB THR A 185 7.677 60.228 107.445 1.00102.00 C ANISOU 1352 CB THR A 185 10613 10195 17946 -1568 -1047 2043 C ATOM 1353 OG1 THR A 185 7.619 60.065 108.867 1.00102.48 O ANISOU 1353 OG1 THR A 185 10620 10351 17967 -1578 -808 2430 O ATOM 1354 CG2 THR A 185 8.048 58.899 106.804 1.00105.29 C ANISOU 1354 CG2 THR A 185 11025 10266 18714 -1608 -1344 1922 C ATOM 1355 N PHE A 186 7.248 63.234 106.923 1.00 98.43 N ANISOU 1355 N PHE A 186 10307 10313 16780 -1433 -745 1749 N ATOM 1356 CA PHE A 186 6.734 64.546 107.298 1.00 97.44 C ANISOU 1356 CA PHE A 186 10177 10450 16398 -1388 -499 1805 C ATOM 1357 C PHE A 186 6.114 64.496 108.690 1.00 94.70 C ANISOU 1357 C PHE A 186 9714 10181 16087 -1410 -212 2204 C ATOM 1358 O PHE A 186 5.156 63.753 108.925 1.00 97.15 O ANISOU 1358 O PHE A 186 9797 10323 16791 -1509 -214 2464 O ATOM 1359 CB PHE A 186 5.703 65.018 106.272 1.00106.42 C ANISOU 1359 CB PHE A 186 11186 11539 17708 -1436 -617 1686 C ATOM 1360 CG PHE A 186 5.326 66.470 106.406 1.00113.02 C ANISOU 1360 CG PHE A 186 12042 12631 18269 -1368 -398 1666 C ATOM 1361 CD1 PHE A 186 4.425 66.884 107.373 1.00119.51 C ANISOU 1361 CD1 PHE A 186 12716 13554 19140 -1372 -113 1965 C ATOM 1362 CD2 PHE A 186 5.867 67.420 105.555 1.00112.79 C ANISOU 1362 CD2 PHE A 186 12178 12732 17946 -1291 -464 1355 C ATOM 1363 CE1 PHE A 186 4.078 68.214 107.497 1.00120.53 C ANISOU 1363 CE1 PHE A 186 12868 13895 19033 -1295 94 1934 C ATOM 1364 CE2 PHE A 186 5.521 68.752 105.672 1.00114.16 C ANISOU 1364 CE2 PHE A 186 12365 13116 17894 -1229 -274 1339 C ATOM 1365 CZ PHE A 186 4.626 69.150 106.644 1.00117.72 C ANISOU 1365 CZ PHE A 186 12673 13652 18403 -1228 1 1618 C ATOM 1366 N GLN A 187 6.661 65.279 109.613 1.00 95.88 N ANISOU 1366 N GLN A 187 10027 10578 15827 -1317 32 2259 N ATOM 1367 CA GLN A 187 6.117 65.369 110.966 1.00 99.15 C ANISOU 1367 CA GLN A 187 10392 11103 16179 -1310 343 2618 C ATOM 1368 C GLN A 187 6.153 66.832 111.399 1.00 94.94 C ANISOU 1368 C GLN A 187 10008 10854 15211 -1201 596 2544 C ATOM 1369 O GLN A 187 6.249 67.746 110.572 1.00 92.01 O ANISOU 1369 O GLN A 187 9693 10562 14707 -1158 532 2267 O ATOM 1370 CB GLN A 187 6.876 64.444 111.932 1.00106.74 C ANISOU 1370 CB GLN A 187 11442 12021 17095 -1317 354 2826 C ATOM 1371 CG GLN A 187 6.778 62.950 111.619 1.00113.54 C ANISOU 1371 CG GLN A 187 12140 12572 18426 -1424 122 2937 C ATOM 1372 CD GLN A 187 5.410 62.348 111.918 1.00121.96 C ANISOU 1372 CD GLN A 187 12918 13493 19929 -1529 216 3279 C ATOM 1373 OE1 GLN A 187 4.384 63.028 111.874 1.00128.91 O ANISOU 1373 OE1 GLN A 187 13661 14451 20866 -1533 381 3349 O ATOM 1374 NE2 GLN A 187 5.395 61.056 112.225 1.00122.34 N ANISOU 1374 NE2 GLN A 187 12852 13313 20319 -1614 111 3509 N ATOM 1375 N TRP A 188 6.080 67.061 112.713 1.00 97.92 N ANISOU 1375 N TRP A 188 10468 11380 15356 -1152 886 2794 N ATOM 1376 CA TRP A 188 5.986 68.424 113.231 1.00 97.11 C ANISOU 1376 CA TRP A 188 10514 11523 14859 -1044 1148 2740 C ATOM 1377 C TRP A 188 7.258 69.218 112.956 1.00 84.78 C ANISOU 1377 C TRP A 188 9221 10093 12900 -969 1025 2417 C ATOM 1378 O TRP A 188 7.197 70.342 112.444 1.00 81.03 O ANISOU 1378 O TRP A 188 8796 9724 12267 -913 1055 2198 O ATOM 1379 CB TRP A 188 5.677 68.400 114.730 1.00106.17 C ANISOU 1379 CB TRP A 188 11736 12790 15813 -1000 1482 3073 C ATOM 1380 CG TRP A 188 5.705 69.760 115.365 1.00107.36 C ANISOU 1380 CG TRP A 188 12100 13180 15512 -874 1747 2994 C ATOM 1381 CD1 TRP A 188 6.534 70.185 116.362 1.00109.72 C ANISOU 1381 CD1 TRP A 188 12710 13645 15334 -796 1845 2991 C ATOM 1382 CD2 TRP A 188 4.873 70.877 115.032 1.00107.92 C ANISOU 1382 CD2 TRP A 188 12097 13332 15576 -812 1925 2896 C ATOM 1383 NE1 TRP A 188 6.265 71.495 116.676 1.00110.92 N ANISOU 1383 NE1 TRP A 188 13001 13968 15176 -687 2076 2881 N ATOM 1384 CE2 TRP A 188 5.250 71.944 115.873 1.00108.03 C ANISOU 1384 CE2 TRP A 188 12396 13553 15099 -689 2142 2826 C ATOM 1385 CE3 TRP A 188 3.843 71.078 114.107 1.00108.27 C ANISOU 1385 CE3 TRP A 188 11862 13281 15993 -848 1904 2866 C ATOM 1386 CZ2 TRP A 188 4.634 73.191 115.815 1.00105.45 C ANISOU 1386 CZ2 TRP A 188 12079 13331 14656 -594 2358 2720 C ATOM 1387 CZ3 TRP A 188 3.235 72.318 114.051 1.00107.49 C ANISOU 1387 CZ3 TRP A 188 11758 13297 15786 -756 2113 2782 C ATOM 1388 CH2 TRP A 188 3.631 73.358 114.900 1.00105.47 C ANISOU 1388 CH2 TRP A 188 11786 13239 15050 -626 2349 2707 C ATOM 1389 N HIS A 189 8.423 68.656 113.299 1.00 79.79 N ANISOU 1389 N HIS A 189 8744 9444 12126 -970 884 2402 N ATOM 1390 CA HIS A 189 9.684 69.353 113.047 1.00 76.95 C ANISOU 1390 CA HIS A 189 8606 9191 11441 -906 755 2125 C ATOM 1391 C HIS A 189 9.869 69.641 111.562 1.00 73.22 C ANISOU 1391 C HIS A 189 8069 8650 11102 -912 548 1808 C ATOM 1392 O HIS A 189 10.382 70.701 111.185 1.00 73.24 O ANISOU 1392 O HIS A 189 8196 8776 10855 -850 538 1579 O ATOM 1393 CB HIS A 189 10.857 68.531 113.584 1.00 80.79 C ANISOU 1393 CB HIS A 189 9213 9631 11854 -916 607 2195 C ATOM 1394 CG HIS A 189 12.203 69.124 113.291 1.00 83.43 C ANISOU 1394 CG HIS A 189 9728 10042 11930 -861 452 1939 C ATOM 1395 ND1 HIS A 189 12.941 68.784 112.177 1.00 82.04 N ANISOU 1395 ND1 HIS A 189 9506 9749 11918 -866 219 1713 N ATOM 1396 CD2 HIS A 189 12.952 70.021 113.977 1.00 84.50 C ANISOU 1396 CD2 HIS A 189 10088 10349 11671 -800 497 1884 C ATOM 1397 CE1 HIS A 189 14.081 69.451 112.185 1.00 80.74 C ANISOU 1397 CE1 HIS A 189 9499 9685 11495 -810 145 1551 C ATOM 1398 NE2 HIS A 189 14.113 70.208 113.267 1.00 82.27 N ANISOU 1398 NE2 HIS A 189 9855 10047 11358 -778 289 1648 N ATOM 1399 N GLU A 190 9.453 68.707 110.703 1.00 71.18 N ANISOU 1399 N GLU A 190 7627 8187 11229 -987 376 1796 N ATOM 1400 CA GLU A 190 9.556 68.930 109.265 1.00 74.80 C ANISOU 1400 CA GLU A 190 8053 8578 11791 -989 177 1500 C ATOM 1401 C GLU A 190 8.598 70.018 108.801 1.00 74.63 C ANISOU 1401 C GLU A 190 7959 8649 11746 -972 282 1429 C ATOM 1402 O GLU A 190 8.917 70.769 107.872 1.00 72.92 O ANISOU 1402 O GLU A 190 7808 8487 11413 -934 190 1173 O ATOM 1403 CB GLU A 190 9.297 67.625 108.509 1.00 75.29 C ANISOU 1403 CB GLU A 190 7967 8378 12261 -1072 -50 1498 C ATOM 1404 CG GLU A 190 10.428 66.604 108.610 1.00 79.71 C ANISOU 1404 CG GLU A 190 8605 8816 12867 -1068 -203 1480 C ATOM 1405 CD GLU A 190 10.595 66.033 110.008 1.00 89.86 C ANISOU 1405 CD GLU A 190 9904 10116 14124 -1083 -81 1796 C ATOM 1406 OE1 GLU A 190 9.607 66.028 110.773 1.00 91.96 O ANISOU 1406 OE1 GLU A 190 10070 10413 14458 -1122 103 2062 O ATOM 1407 OE2 GLU A 190 11.717 65.597 110.344 1.00 92.18 O ANISOU 1407 OE2 GLU A 190 10306 10389 14329 -1052 -161 1792 O ATOM 1408 N ALA A 191 7.425 70.116 109.433 1.00 76.47 N ANISOU 1408 N ALA A 191 8051 8899 12105 -995 483 1669 N ATOM 1409 CA ALA A 191 6.516 71.220 109.144 1.00 71.56 C ANISOU 1409 CA ALA A 191 7351 8370 11467 -963 616 1632 C ATOM 1410 C ALA A 191 7.102 72.546 109.611 1.00 70.14 C ANISOU 1410 C ALA A 191 7386 8409 10854 -855 783 1510 C ATOM 1411 O ALA A 191 6.974 73.564 108.922 1.00 63.09 O ANISOU 1411 O ALA A 191 6508 7585 9878 -814 771 1328 O ATOM 1412 CB ALA A 191 5.160 70.969 109.801 1.00 64.82 C ANISOU 1412 CB ALA A 191 6277 7474 10879 -1000 829 1949 C ATOM 1413 N MET A 192 7.739 72.553 110.786 1.00 72.05 N ANISOU 1413 N MET A 192 7802 8752 10820 -811 922 1614 N ATOM 1414 CA MET A 192 8.473 73.736 111.220 1.00 74.19 C ANISOU 1414 CA MET A 192 8309 9202 10676 -719 1016 1470 C ATOM 1415 C MET A 192 9.564 74.097 110.222 1.00 75.49 C ANISOU 1415 C MET A 192 8570 9371 10743 -708 778 1176 C ATOM 1416 O MET A 192 9.770 75.277 109.916 1.00 81.10 O ANISOU 1416 O MET A 192 9368 10184 11260 -651 808 1002 O ATOM 1417 CB MET A 192 9.079 73.506 112.605 1.00 85.83 C ANISOU 1417 CB MET A 192 9976 10758 11876 -690 1130 1629 C ATOM 1418 CG MET A 192 8.179 73.881 113.768 1.00101.25 C ANISOU 1418 CG MET A 192 11961 12808 13702 -636 1468 1852 C ATOM 1419 SD MET A 192 9.043 73.715 115.343 1.00115.62 S ANISOU 1419 SD MET A 192 14087 14741 15103 -595 1557 2000 S ATOM 1420 CE MET A 192 7.867 74.468 116.463 1.00119.58 C ANISOU 1420 CE MET A 192 14654 15371 15409 -495 2002 2187 C ATOM 1421 N PHE A 193 10.270 73.090 109.701 1.00 74.10 N ANISOU 1421 N PHE A 193 8373 9073 10709 -756 555 1126 N ATOM 1422 CA PHE A 193 11.335 73.345 108.737 1.00 68.73 C ANISOU 1422 CA PHE A 193 7773 8390 9950 -732 361 865 C ATOM 1423 C PHE A 193 10.804 74.055 107.498 1.00 64.52 C ANISOU 1423 C PHE A 193 7166 7858 9490 -725 308 683 C ATOM 1424 O PHE A 193 11.442 74.981 106.983 1.00 64.76 O ANISOU 1424 O PHE A 193 7296 7976 9333 -675 276 495 O ATOM 1425 CB PHE A 193 12.016 72.029 108.358 1.00 66.39 C ANISOU 1425 CB PHE A 193 7445 7934 9847 -772 161 855 C ATOM 1426 CG PHE A 193 13.049 72.164 107.274 1.00 56.23 C ANISOU 1426 CG PHE A 193 6222 6625 8517 -734 -7 598 C ATOM 1427 CD1 PHE A 193 14.346 72.545 107.578 1.00 55.21 C ANISOU 1427 CD1 PHE A 193 6228 6576 8171 -682 -31 529 C ATOM 1428 CD2 PHE A 193 12.727 71.894 105.952 1.00 52.46 C ANISOU 1428 CD2 PHE A 193 5670 6042 8220 -750 -143 437 C ATOM 1429 CE1 PHE A 193 15.300 72.664 106.583 1.00 55.02 C ANISOU 1429 CE1 PHE A 193 6241 6533 8132 -639 -148 319 C ATOM 1430 CE2 PHE A 193 13.677 72.013 104.953 1.00 53.81 C ANISOU 1430 CE2 PHE A 193 5917 6202 8326 -699 -259 211 C ATOM 1431 CZ PHE A 193 14.965 72.399 105.268 1.00 55.25 C ANISOU 1431 CZ PHE A 193 6210 6469 8312 -640 -243 160 C ATOM 1432 N LEU A 194 9.635 73.638 107.007 1.00 66.11 N ANISOU 1432 N LEU A 194 7187 7956 9977 -780 283 753 N ATOM 1433 CA LEU A 194 9.063 74.282 105.829 1.00 72.06 C ANISOU 1433 CA LEU A 194 7870 8704 10807 -780 200 602 C ATOM 1434 C LEU A 194 8.560 75.685 106.153 1.00 73.54 C ANISOU 1434 C LEU A 194 8073 9039 10830 -721 397 608 C ATOM 1435 O LEU A 194 8.700 76.603 105.337 1.00 70.88 O ANISOU 1435 O LEU A 194 7776 8760 10394 -686 344 438 O ATOM 1436 CB LEU A 194 7.935 73.424 105.256 1.00 75.74 C ANISOU 1436 CB LEU A 194 8130 8997 11651 -868 79 689 C ATOM 1437 CG LEU A 194 8.328 72.051 104.706 1.00 76.20 C ANISOU 1437 CG LEU A 194 8175 8866 11911 -927 -155 638 C ATOM 1438 CD1 LEU A 194 7.147 71.399 104.005 1.00 79.17 C ANISOU 1438 CD1 LEU A 194 8357 9061 12663 -1021 -319 690 C ATOM 1439 CD2 LEU A 194 9.516 72.162 103.763 1.00 73.89 C ANISOU 1439 CD2 LEU A 194 8053 8587 11437 -873 -307 363 C ATOM 1440 N LEU A 195 7.978 75.871 107.342 1.00 71.27 N ANISOU 1440 N LEU A 195 7763 8808 10508 -701 635 808 N ATOM 1441 CA LEU A 195 7.468 77.186 107.718 1.00 64.06 C ANISOU 1441 CA LEU A 195 6875 8017 9448 -627 848 808 C ATOM 1442 C LEU A 195 8.593 78.186 107.953 1.00 66.44 C ANISOU 1442 C LEU A 195 7411 8446 9388 -555 867 637 C ATOM 1443 O LEU A 195 8.427 79.379 107.670 1.00 69.67 O ANISOU 1443 O LEU A 195 7849 8923 9699 -501 929 532 O ATOM 1444 CB LEU A 195 6.587 77.072 108.964 1.00 55.16 C ANISOU 1444 CB LEU A 195 5686 6913 8358 -605 1130 1065 C ATOM 1445 CG LEU A 195 5.240 76.371 108.771 1.00 57.35 C ANISOU 1445 CG LEU A 195 5678 7067 9046 -670 1162 1272 C ATOM 1446 CD1 LEU A 195 4.486 76.250 110.089 1.00 59.47 C ANISOU 1446 CD1 LEU A 195 5897 7372 9326 -633 1492 1552 C ATOM 1447 CD2 LEU A 195 4.404 77.108 107.736 1.00 51.57 C ANISOU 1447 CD2 LEU A 195 4784 6305 8506 -669 1098 1192 C ATOM 1448 N GLU A 196 9.739 77.727 108.461 1.00 63.11 N ANISOU 1448 N GLU A 196 7142 8042 8794 -558 798 618 N ATOM 1449 CA GLU A 196 10.896 78.598 108.641 1.00 67.17 C ANISOU 1449 CA GLU A 196 7857 8652 9010 -508 768 464 C ATOM 1450 C GLU A 196 11.460 79.111 107.322 1.00 64.41 C ANISOU 1450 C GLU A 196 7500 8298 8675 -504 599 251 C ATOM 1451 O GLU A 196 12.309 80.007 107.339 1.00 67.70 O ANISOU 1451 O GLU A 196 8048 8787 8889 -464 580 129 O ATOM 1452 CB GLU A 196 11.990 77.864 109.418 1.00 77.71 C ANISOU 1452 CB GLU A 196 9322 9985 10217 -523 693 518 C ATOM 1453 CG GLU A 196 11.641 77.579 110.869 1.00 83.68 C ANISOU 1453 CG GLU A 196 10161 10782 10850 -512 870 727 C ATOM 1454 CD GLU A 196 12.572 76.564 111.503 1.00 87.39 C ANISOU 1454 CD GLU A 196 10713 11217 11275 -547 753 826 C ATOM 1455 OE1 GLU A 196 13.590 76.208 110.870 1.00 91.17 O ANISOU 1455 OE1 GLU A 196 11189 11644 11807 -567 545 714 O ATOM 1456 OE2 GLU A 196 12.282 76.117 112.633 1.00 87.84 O ANISOU 1456 OE2 GLU A 196 10833 11295 11248 -547 878 1030 O ATOM 1457 N PHE A 197 11.016 78.564 106.192 1.00 58.08 N ANISOU 1457 N PHE A 197 6558 7408 8102 -544 470 210 N ATOM 1458 CA PHE A 197 11.430 79.021 104.873 1.00 58.08 C ANISOU 1458 CA PHE A 197 6564 7408 8097 -533 326 24 C ATOM 1459 C PHE A 197 10.336 79.753 104.115 1.00 65.03 C ANISOU 1459 C PHE A 197 7334 8291 9083 -530 341 2 C ATOM 1460 O PHE A 197 10.642 80.674 103.355 1.00 70.92 O ANISOU 1460 O PHE A 197 8125 9089 9732 -497 298 -126 O ATOM 1461 CB PHE A 197 11.910 77.834 104.025 1.00 55.80 C ANISOU 1461 CB PHE A 197 6248 7009 7945 -570 134 -43 C ATOM 1462 CG PHE A 197 12.091 78.159 102.566 1.00 49.13 C ANISOU 1462 CG PHE A 197 5412 6155 7100 -554 1 -219 C ATOM 1463 CD1 PHE A 197 13.236 78.802 102.123 1.00 48.68 C ANISOU 1463 CD1 PHE A 197 5465 6169 6861 -502 -18 -351 C ATOM 1464 CD2 PHE A 197 11.119 77.817 101.638 1.00 47.82 C ANISOU 1464 CD2 PHE A 197 5147 5905 7118 -595 -114 -239 C ATOM 1465 CE1 PHE A 197 13.406 79.101 100.782 1.00 48.47 C ANISOU 1465 CE1 PHE A 197 5463 6146 6809 -479 -113 -493 C ATOM 1466 CE2 PHE A 197 11.283 78.117 100.296 1.00 46.67 C ANISOU 1466 CE2 PHE A 197 5046 5759 6928 -576 -244 -397 C ATOM 1467 CZ PHE A 197 12.429 78.757 99.869 1.00 45.35 C ANISOU 1467 CZ PHE A 197 5002 5678 6551 -513 -227 -521 C ATOM 1468 N PHE A 198 9.072 79.371 104.306 1.00 67.09 N ANISOU 1468 N PHE A 198 7438 8490 9562 -565 396 146 N ATOM 1469 CA PHE A 198 7.989 79.964 103.531 1.00 64.91 C ANISOU 1469 CA PHE A 198 7025 8194 9443 -570 373 148 C ATOM 1470 C PHE A 198 7.544 81.310 104.088 1.00 68.93 C ANISOU 1470 C PHE A 198 7541 8795 9854 -497 583 179 C ATOM 1471 O PHE A 198 7.138 82.185 103.315 1.00 70.79 O ANISOU 1471 O PHE A 198 7729 9045 10126 -476 544 119 O ATOM 1472 CB PHE A 198 6.808 78.997 103.462 1.00 60.55 C ANISOU 1472 CB PHE A 198 6267 7515 9224 -644 324 305 C ATOM 1473 CG PHE A 198 6.996 77.892 102.465 1.00 63.05 C ANISOU 1473 CG PHE A 198 6565 7706 9685 -715 52 222 C ATOM 1474 CD1 PHE A 198 7.404 78.175 101.172 1.00 66.70 C ANISOU 1474 CD1 PHE A 198 7108 8170 10068 -708 -142 30 C ATOM 1475 CD2 PHE A 198 6.783 76.571 102.821 1.00 63.65 C ANISOU 1475 CD2 PHE A 198 6561 7655 9967 -783 -4 336 C ATOM 1476 CE1 PHE A 198 7.582 77.162 100.248 1.00 66.67 C ANISOU 1476 CE1 PHE A 198 7126 8042 10163 -758 -383 -71 C ATOM 1477 CE2 PHE A 198 6.962 75.553 101.901 1.00 58.70 C ANISOU 1477 CE2 PHE A 198 5939 6888 9478 -842 -263 236 C ATOM 1478 CZ PHE A 198 7.363 75.849 100.613 1.00 55.73 C ANISOU 1478 CZ PHE A 198 5666 6514 8995 -824 -450 19 C ATOM 1479 N LEU A 199 7.601 81.498 105.406 1.00 70.61 N ANISOU 1479 N LEU A 199 7829 9063 9938 -453 802 270 N ATOM 1480 CA LEU A 199 7.348 82.830 105.954 1.00 72.69 C ANISOU 1480 CA LEU A 199 8153 9403 10064 -367 1003 254 C ATOM 1481 C LEU A 199 8.380 83.843 105.476 1.00 71.84 C ANISOU 1481 C LEU A 199 8202 9356 9738 -331 915 62 C ATOM 1482 O LEU A 199 7.980 84.936 105.040 1.00 80.71 O ANISOU 1482 O LEU A 199 9292 10493 10880 -287 951 12 O ATOM 1483 CB LEU A 199 7.277 82.768 107.484 1.00 80.54 C ANISOU 1483 CB LEU A 199 9247 10442 10911 -319 1250 373 C ATOM 1484 CG LEU A 199 6.231 81.837 108.095 1.00101.44 C ANISOU 1484 CG LEU A 199 11733 13037 13774 -343 1395 607 C ATOM 1485 CD1 LEU A 199 6.241 81.968 109.608 1.00110.74 C ANISOU 1485 CD1 LEU A 199 13064 14284 14727 -273 1670 712 C ATOM 1486 CD2 LEU A 199 4.850 82.132 107.533 1.00108.32 C ANISOU 1486 CD2 LEU A 199 12346 13846 14963 -339 1456 702 C ATOM 1487 N PRO A 200 9.691 83.567 105.513 1.00 61.09 N ANISOU 1487 N PRO A 200 6991 8022 8200 -348 800 -33 N ATOM 1488 CA PRO A 200 10.637 84.509 104.892 1.00 59.96 C ANISOU 1488 CA PRO A 200 6949 7921 7911 -325 706 -190 C ATOM 1489 C PRO A 200 10.454 84.640 103.394 1.00 63.93 C ANISOU 1489 C PRO A 200 7354 8399 8536 -345 552 -260 C ATOM 1490 O PRO A 200 10.658 85.731 102.849 1.00 71.78 O ANISOU 1490 O PRO A 200 8379 9426 9470 -313 538 -338 O ATOM 1491 CB PRO A 200 12.008 83.912 105.240 1.00 58.85 C ANISOU 1491 CB PRO A 200 6938 7794 7628 -347 609 -234 C ATOM 1492 CG PRO A 200 11.760 83.083 106.448 1.00 60.62 C ANISOU 1492 CG PRO A 200 7191 8009 7834 -359 707 -100 C ATOM 1493 CD PRO A 200 10.399 82.504 106.247 1.00 60.14 C ANISOU 1493 CD PRO A 200 6950 7893 8008 -382 771 22 C ATOM 1494 N LEU A 201 10.082 83.558 102.706 1.00 62.29 N ANISOU 1494 N LEU A 201 7047 8127 8494 -400 425 -232 N ATOM 1495 CA LEU A 201 9.845 83.648 101.270 1.00 63.13 C ANISOU 1495 CA LEU A 201 7096 8209 8683 -417 260 -303 C ATOM 1496 C LEU A 201 8.680 84.579 100.966 1.00 63.76 C ANISOU 1496 C LEU A 201 7057 8285 8883 -398 305 -249 C ATOM 1497 O LEU A 201 8.734 85.363 100.012 1.00 70.45 O ANISOU 1497 O LEU A 201 7915 9155 9696 -381 222 -314 O ATOM 1498 CB LEU A 201 9.588 82.259 100.691 1.00 60.16 C ANISOU 1498 CB LEU A 201 6656 7738 8463 -481 99 -295 C ATOM 1499 CG LEU A 201 9.243 82.217 99.202 1.00 56.86 C ANISOU 1499 CG LEU A 201 6212 7282 8112 -503 -102 -374 C ATOM 1500 CD1 LEU A 201 10.386 82.768 98.364 1.00 44.49 C ANISOU 1500 CD1 LEU A 201 4791 5785 6328 -457 -153 -517 C ATOM 1501 CD2 LEU A 201 8.897 80.799 98.782 1.00 64.69 C ANISOU 1501 CD2 LEU A 201 7154 8149 9275 -569 -272 -374 C ATOM 1502 N GLY A 202 7.620 84.511 101.771 1.00 60.49 N ANISOU 1502 N GLY A 202 6522 7839 8622 -395 448 -111 N ATOM 1503 CA GLY A 202 6.487 85.395 101.555 1.00 59.73 C ANISOU 1503 CA GLY A 202 6285 7727 8683 -364 511 -40 C ATOM 1504 C GLY A 202 6.806 86.841 101.878 1.00 54.31 C ANISOU 1504 C GLY A 202 5692 7102 7841 -281 650 -100 C ATOM 1505 O GLY A 202 6.358 87.755 101.180 1.00 54.89 O ANISOU 1505 O GLY A 202 5701 7168 7989 -255 612 -107 O ATOM 1506 N ILE A 203 7.587 87.070 102.936 1.00 54.26 N ANISOU 1506 N ILE A 203 5846 7144 7626 -241 791 -143 N ATOM 1507 CA ILE A 203 7.944 88.431 103.325 1.00 55.41 C ANISOU 1507 CA ILE A 203 6104 7323 7626 -167 903 -217 C ATOM 1508 C ILE A 203 8.837 89.072 102.270 1.00 55.01 C ANISOU 1508 C ILE A 203 6121 7296 7486 -179 734 -333 C ATOM 1509 O ILE A 203 8.621 90.219 101.863 1.00 52.00 O ANISOU 1509 O ILE A 203 5720 6906 7132 -137 748 -355 O ATOM 1510 CB ILE A 203 8.618 88.433 104.708 1.00 52.56 C ANISOU 1510 CB ILE A 203 5927 6996 7046 -134 1046 -243 C ATOM 1511 CG1 ILE A 203 7.630 87.986 105.786 1.00 49.80 C ANISOU 1511 CG1 ILE A 203 5524 6634 6765 -99 1269 -107 C ATOM 1512 CG2 ILE A 203 9.171 89.811 105.029 1.00 39.16 C ANISOU 1512 CG2 ILE A 203 4378 5311 5189 -71 1102 -355 C ATOM 1513 CD1 ILE A 203 8.237 87.903 107.168 1.00 41.90 C ANISOU 1513 CD1 ILE A 203 4736 5674 5509 -65 1400 -119 C ATOM 1514 N ILE A 204 9.855 88.340 101.811 1.00 57.58 N ANISOU 1514 N ILE A 204 6518 7645 7714 -229 588 -394 N ATOM 1515 CA ILE A 204 10.787 88.895 100.835 1.00 57.75 C ANISOU 1515 CA ILE A 204 6602 7696 7643 -232 464 -483 C ATOM 1516 C ILE A 204 10.085 89.157 99.508 1.00 65.58 C ANISOU 1516 C ILE A 204 7491 8675 8754 -241 348 -462 C ATOM 1517 O ILE A 204 10.299 90.197 98.874 1.00 69.12 O ANISOU 1517 O ILE A 204 7955 9139 9168 -215 320 -485 O ATOM 1518 CB ILE A 204 12.000 87.962 100.667 1.00 54.64 C ANISOU 1518 CB ILE A 204 6293 7323 7144 -267 366 -539 C ATOM 1519 CG1 ILE A 204 12.821 87.929 101.957 1.00 51.93 C ANISOU 1519 CG1 ILE A 204 6065 6993 6674 -260 443 -551 C ATOM 1520 CG2 ILE A 204 12.865 88.408 99.498 1.00 55.09 C ANISOU 1520 CG2 ILE A 204 6389 7411 7132 -262 263 -605 C ATOM 1521 CD1 ILE A 204 14.025 87.023 101.889 1.00 54.89 C ANISOU 1521 CD1 ILE A 204 6495 7374 6985 -288 350 -584 C ATOM 1522 N LEU A 205 9.230 88.229 99.070 1.00 67.08 N ANISOU 1522 N LEU A 205 7573 8825 9089 -282 260 -408 N ATOM 1523 CA LEU A 205 8.510 88.431 97.816 1.00 67.69 C ANISOU 1523 CA LEU A 205 7566 8881 9273 -299 107 -383 C ATOM 1524 C LEU A 205 7.551 89.611 97.911 1.00 71.29 C ANISOU 1524 C LEU A 205 7908 9314 9864 -255 187 -303 C ATOM 1525 O LEU A 205 7.431 90.399 96.965 1.00 72.93 O ANISOU 1525 O LEU A 205 8103 9529 10077 -244 91 -297 O ATOM 1526 CB LEU A 205 7.758 87.158 97.426 1.00 63.38 C ANISOU 1526 CB LEU A 205 6928 8271 8884 -363 -35 -344 C ATOM 1527 CG LEU A 205 8.606 86.006 96.883 1.00 62.37 C ANISOU 1527 CG LEU A 205 6913 8138 8647 -399 -171 -442 C ATOM 1528 CD1 LEU A 205 7.731 84.804 96.568 1.00 67.94 C ANISOU 1528 CD1 LEU A 205 7523 8745 9548 -468 -328 -404 C ATOM 1529 CD2 LEU A 205 9.384 86.444 95.653 1.00 63.83 C ANISOU 1529 CD2 LEU A 205 7225 8378 8651 -376 -281 -538 C ATOM 1530 N PHE A 206 6.858 89.752 99.044 1.00 71.39 N ANISOU 1530 N PHE A 206 7843 9295 9989 -222 375 -231 N ATOM 1531 CA PHE A 206 5.941 90.874 99.215 1.00 70.47 C ANISOU 1531 CA PHE A 206 7612 9140 10023 -159 487 -158 C ATOM 1532 C PHE A 206 6.698 92.194 99.279 1.00 70.08 C ANISOU 1532 C PHE A 206 7686 9114 9826 -101 552 -238 C ATOM 1533 O PHE A 206 6.308 93.177 98.637 1.00 73.16 O ANISOU 1533 O PHE A 206 8012 9477 10309 -70 511 -205 O ATOM 1534 CB PHE A 206 5.095 90.676 100.474 1.00 70.00 C ANISOU 1534 CB PHE A 206 7460 9042 10094 -117 721 -66 C ATOM 1535 CG PHE A 206 4.268 91.874 100.843 1.00 71.91 C ANISOU 1535 CG PHE A 206 7609 9237 10478 -23 899 -9 C ATOM 1536 CD1 PHE A 206 3.068 92.128 100.201 1.00 70.02 C ANISOU 1536 CD1 PHE A 206 7139 8930 10534 -19 841 118 C ATOM 1537 CD2 PHE A 206 4.690 92.747 101.834 1.00 72.42 C ANISOU 1537 CD2 PHE A 206 7817 9308 10392 65 1110 -85 C ATOM 1538 CE1 PHE A 206 2.306 93.230 100.536 1.00 67.13 C ANISOU 1538 CE1 PHE A 206 6671 8505 10331 82 1018 177 C ATOM 1539 CE2 PHE A 206 3.933 93.851 102.173 1.00 71.01 C ANISOU 1539 CE2 PHE A 206 7564 9066 10349 168 1287 -50 C ATOM 1540 CZ PHE A 206 2.739 94.092 101.524 1.00 71.13 C ANISOU 1540 CZ PHE A 206 7331 9014 10679 182 1255 86 C ATOM 1541 N CYS A 207 7.785 92.236 100.053 1.00 65.40 N ANISOU 1541 N CYS A 207 7264 8558 9025 -89 633 -332 N ATOM 1542 CA CYS A 207 8.576 93.458 100.149 1.00 56.16 C ANISOU 1542 CA CYS A 207 6209 7388 7739 -48 666 -409 C ATOM 1543 C CYS A 207 9.194 93.818 98.806 1.00 55.83 C ANISOU 1543 C CYS A 207 6180 7376 7656 -81 487 -423 C ATOM 1544 O CYS A 207 9.201 94.989 98.412 1.00 58.35 O ANISOU 1544 O CYS A 207 6490 7666 8013 -47 483 -412 O ATOM 1545 CB CYS A 207 9.658 93.303 101.216 1.00 49.37 C ANISOU 1545 CB CYS A 207 5527 6554 6679 -48 736 -499 C ATOM 1546 SG CYS A 207 9.016 93.223 102.903 1.00 56.61 S ANISOU 1546 SG CYS A 207 6498 7443 7570 16 982 -487 S ATOM 1547 N SER A 208 9.713 92.822 98.084 1.00 58.57 N ANISOU 1547 N SER A 208 6555 7773 7925 -137 351 -441 N ATOM 1548 CA SER A 208 10.277 93.089 96.766 1.00 65.28 C ANISOU 1548 CA SER A 208 7438 8663 8704 -154 209 -446 C ATOM 1549 C SER A 208 9.222 93.650 95.822 1.00 62.35 C ANISOU 1549 C SER A 208 6955 8265 8471 -146 116 -357 C ATOM 1550 O SER A 208 9.515 94.530 95.004 1.00 61.53 O ANISOU 1550 O SER A 208 6872 8175 8332 -133 59 -329 O ATOM 1551 CB SER A 208 10.893 91.815 96.190 1.00 67.38 C ANISOU 1551 CB SER A 208 7765 8974 8862 -198 102 -494 C ATOM 1552 OG SER A 208 11.926 91.329 97.029 1.00 68.79 O ANISOU 1552 OG SER A 208 8031 9170 8938 -203 173 -557 O ATOM 1553 N ALA A 209 7.984 93.163 95.927 1.00 62.22 N ANISOU 1553 N ALA A 209 6806 8203 8631 -157 93 -290 N ATOM 1554 CA ALA A 209 6.916 93.675 95.076 1.00 64.54 C ANISOU 1554 CA ALA A 209 6969 8457 9095 -154 -23 -186 C ATOM 1555 C ALA A 209 6.583 95.120 95.425 1.00 67.75 C ANISOU 1555 C ALA A 209 7315 8811 9616 -85 98 -135 C ATOM 1556 O ALA A 209 6.488 95.976 94.539 1.00 71.13 O ANISOU 1556 O ALA A 209 7722 9232 10072 -73 0 -75 O ATOM 1557 CB ALA A 209 5.675 92.788 95.198 1.00 64.05 C ANISOU 1557 CB ALA A 209 6747 8338 9249 -189 -81 -108 C ATOM 1558 N ARG A 210 6.414 95.412 96.717 1.00 62.96 N ANISOU 1558 N ARG A 210 6694 8161 9066 -32 313 -159 N ATOM 1559 CA ARG A 210 6.052 96.764 97.132 1.00 63.07 C ANISOU 1559 CA ARG A 210 6664 8099 9200 49 445 -134 C ATOM 1560 C ARG A 210 7.171 97.759 96.845 1.00 67.95 C ANISOU 1560 C ARG A 210 7417 8725 9676 58 422 -195 C ATOM 1561 O ARG A 210 6.905 98.891 96.425 1.00 73.67 O ANISOU 1561 O ARG A 210 8088 9387 10516 98 406 -137 O ATOM 1562 CB ARG A 210 5.694 96.776 98.618 1.00 63.67 C ANISOU 1562 CB ARG A 210 6745 8129 9316 116 698 -171 C ATOM 1563 CG ARG A 210 4.457 95.965 98.973 1.00 71.25 C ANISOU 1563 CG ARG A 210 7530 9063 10480 120 769 -67 C ATOM 1564 CD ARG A 210 3.175 96.653 98.521 1.00 81.49 C ANISOU 1564 CD ARG A 210 8601 10271 12092 170 767 72 C ATOM 1565 NE ARG A 210 2.937 97.907 99.233 1.00 87.20 N ANISOU 1565 NE ARG A 210 9329 10909 12894 290 984 50 N ATOM 1566 CZ ARG A 210 3.092 99.115 98.698 1.00 90.16 C ANISOU 1566 CZ ARG A 210 9711 11228 13318 328 929 48 C ATOM 1567 NH1 ARG A 210 3.481 99.240 97.436 1.00 90.81 N ANISOU 1567 NH1 ARG A 210 9796 11348 13359 256 674 87 N ATOM 1568 NH2 ARG A 210 2.853 100.199 99.424 1.00 89.61 N ANISOU 1568 NH2 ARG A 210 9656 11057 13334 445 1134 11 N ATOM 1569 N ILE A 211 8.426 97.361 97.066 1.00 61.16 N ANISOU 1569 N ILE A 211 6712 7927 8597 20 415 -293 N ATOM 1570 CA ILE A 211 9.543 98.274 96.839 1.00 54.83 C ANISOU 1570 CA ILE A 211 6013 7121 7698 20 393 -330 C ATOM 1571 C ILE A 211 9.670 98.604 95.356 1.00 62.16 C ANISOU 1571 C ILE A 211 6908 8087 8623 -6 235 -236 C ATOM 1572 O ILE A 211 9.752 99.776 94.970 1.00 74.75 O ANISOU 1572 O ILE A 211 8484 9628 10291 18 222 -180 O ATOM 1573 CB ILE A 211 10.848 97.682 97.398 1.00 51.71 C ANISOU 1573 CB ILE A 211 5761 6779 7109 -19 407 -432 C ATOM 1574 CG1 ILE A 211 10.802 97.631 98.925 1.00 49.55 C ANISOU 1574 CG1 ILE A 211 5560 6459 6807 14 554 -518 C ATOM 1575 CG2 ILE A 211 12.045 98.493 96.930 1.00 54.73 C ANISOU 1575 CG2 ILE A 211 6208 7158 7428 -37 354 -434 C ATOM 1576 CD1 ILE A 211 11.972 96.888 99.535 1.00 50.69 C ANISOU 1576 CD1 ILE A 211 5831 6653 6776 -31 538 -598 C ATOM 1577 N ILE A 212 9.688 97.576 94.505 1.00 65.75 N ANISOU 1577 N ILE A 212 7372 8627 8984 -53 112 -218 N ATOM 1578 CA ILE A 212 9.787 97.802 93.065 1.00 68.78 C ANISOU 1578 CA ILE A 212 7766 9059 9309 -70 -38 -132 C ATOM 1579 C ILE A 212 8.591 98.602 92.569 1.00 72.65 C ANISOU 1579 C ILE A 212 8125 9484 9996 -44 -111 -6 C ATOM 1580 O ILE A 212 8.730 99.507 91.737 1.00 74.17 O ANISOU 1580 O ILE A 212 8318 9672 10191 -34 -178 90 O ATOM 1581 CB ILE A 212 9.918 96.458 92.323 1.00 68.66 C ANISOU 1581 CB ILE A 212 7815 9130 9144 -113 -159 -166 C ATOM 1582 CG1 ILE A 212 11.239 95.775 92.686 1.00 66.81 C ANISOU 1582 CG1 ILE A 212 7699 8951 8734 -127 -84 -271 C ATOM 1583 CG2 ILE A 212 9.812 96.657 90.818 1.00 69.24 C ANISOU 1583 CG2 ILE A 212 7927 9254 9128 -121 -323 -78 C ATOM 1584 CD1 ILE A 212 11.346 94.356 92.185 1.00 66.42 C ANISOU 1584 CD1 ILE A 212 7716 8956 8565 -155 -174 -333 C ATOM 1585 N TRP A 213 7.399 98.289 93.080 1.00 74.77 N ANISOU 1585 N TRP A 213 8263 9692 10452 -31 -94 18 N ATOM 1586 CA TRP A 213 6.203 99.026 92.688 1.00 74.48 C ANISOU 1586 CA TRP A 213 8065 9577 10659 -1 -160 153 C ATOM 1587 C TRP A 213 6.306 100.495 93.081 1.00 69.31 C ANISOU 1587 C TRP A 213 7383 8828 10125 67 -38 182 C ATOM 1588 O TRP A 213 5.964 101.383 92.292 1.00 72.93 O ANISOU 1588 O TRP A 213 7776 9244 10691 84 -136 307 O ATOM 1589 CB TRP A 213 4.972 98.376 93.321 1.00 83.02 C ANISOU 1589 CB TRP A 213 8985 10601 11958 7 -121 182 C ATOM 1590 CG TRP A 213 3.656 98.834 92.776 1.00 96.37 C ANISOU 1590 CG TRP A 213 10473 12211 13934 24 -236 345 C ATOM 1591 CD1 TRP A 213 3.446 99.748 91.785 1.00101.75 C ANISOU 1591 CD1 TRP A 213 11116 12867 14677 33 -385 466 C ATOM 1592 CD2 TRP A 213 2.360 98.392 93.195 1.00102.23 C ANISOU 1592 CD2 TRP A 213 11001 12877 14963 34 -216 429 C ATOM 1593 NE1 TRP A 213 2.099 99.905 91.564 1.00105.46 N ANISOU 1593 NE1 TRP A 213 11362 13248 15462 47 -479 615 N ATOM 1594 CE2 TRP A 213 1.410 99.083 92.417 1.00107.54 C ANISOU 1594 CE2 TRP A 213 11503 13476 15882 48 -372 597 C ATOM 1595 CE3 TRP A 213 1.910 97.479 94.155 1.00 98.64 C ANISOU 1595 CE3 TRP A 213 10472 12407 14599 31 -78 401 C ATOM 1596 CZ2 TRP A 213 0.039 98.889 92.567 1.00108.46 C ANISOU 1596 CZ2 TRP A 213 11357 13497 16356 59 -398 736 C ATOM 1597 CZ3 TRP A 213 0.548 97.289 94.303 1.00100.05 C ANISOU 1597 CZ3 TRP A 213 10394 12496 15124 43 -82 544 C ATOM 1598 CH2 TRP A 213 -0.372 97.991 93.513 1.00104.15 C ANISOU 1598 CH2 TRP A 213 10727 12936 15910 57 -243 708 C ATOM 1599 N SER A 214 6.793 100.773 94.293 1.00 62.69 N ANISOU 1599 N SER A 214 6607 7945 9266 106 159 66 N ATOM 1600 CA SER A 214 6.883 102.155 94.753 1.00 57.94 C ANISOU 1600 CA SER A 214 6001 7224 8788 173 266 62 C ATOM 1601 C SER A 214 8.018 102.910 94.070 1.00 63.77 C ANISOU 1601 C SER A 214 6836 7976 9416 142 188 86 C ATOM 1602 O SER A 214 7.887 104.110 93.802 1.00 68.26 O ANISOU 1602 O SER A 214 7356 8445 10136 180 179 164 O ATOM 1603 CB SER A 214 7.062 102.195 96.271 1.00 57.00 C ANISOU 1603 CB SER A 214 5961 7048 8650 225 480 -86 C ATOM 1604 OG SER A 214 6.001 101.525 96.931 1.00 63.53 O ANISOU 1604 OG SER A 214 6689 7863 9586 262 591 -79 O ATOM 1605 N LEU A 215 9.131 102.235 93.779 1.00 59.64 N ANISOU 1605 N LEU A 215 6435 7566 8658 79 142 34 N ATOM 1606 CA LEU A 215 10.272 102.921 93.182 1.00 56.89 C ANISOU 1606 CA LEU A 215 6159 7230 8227 52 100 77 C ATOM 1607 C LEU A 215 10.061 103.187 91.696 1.00 63.56 C ANISOU 1607 C LEU A 215 6967 8129 9055 36 -46 249 C ATOM 1608 O LEU A 215 10.432 104.257 91.200 1.00 70.88 O ANISOU 1608 O LEU A 215 7883 9004 10045 42 -68 356 O ATOM 1609 CB LEU A 215 11.550 102.115 93.407 1.00 57.18 C ANISOU 1609 CB LEU A 215 6318 7361 8049 3 124 -20 C ATOM 1610 CG LEU A 215 12.052 102.105 94.852 1.00 59.58 C ANISOU 1610 CG LEU A 215 6690 7600 8346 9 237 -171 C ATOM 1611 CD1 LEU A 215 13.354 101.333 94.969 1.00 68.38 C ANISOU 1611 CD1 LEU A 215 7898 8800 9283 -43 230 -234 C ATOM 1612 CD2 LEU A 215 12.219 103.525 95.366 1.00 53.10 C ANISOU 1612 CD2 LEU A 215 5873 6626 7678 40 279 -180 C ATOM 1613 N ARG A 216 9.477 102.233 90.967 1.00 64.65 N ANISOU 1613 N ARG A 216 7097 8362 9106 14 -161 284 N ATOM 1614 CA ARG A 216 9.138 102.495 89.573 1.00 72.35 C ANISOU 1614 CA ARG A 216 8063 9384 10044 3 -327 448 C ATOM 1615 C ARG A 216 8.083 103.583 89.447 1.00 80.67 C ANISOU 1615 C ARG A 216 8968 10313 11370 44 -378 585 C ATOM 1616 O ARG A 216 7.977 104.213 88.389 1.00 82.95 O ANISOU 1616 O ARG A 216 9249 10611 11657 42 -502 752 O ATOM 1617 CB ARG A 216 8.655 101.218 88.883 1.00 73.08 C ANISOU 1617 CB ARG A 216 8197 9578 9991 -33 -475 431 C ATOM 1618 CG ARG A 216 9.699 100.117 88.811 1.00 82.64 C ANISOU 1618 CG ARG A 216 9561 10904 10935 -61 -435 306 C ATOM 1619 CD ARG A 216 9.430 99.172 87.653 1.00 94.89 C ANISOU 1619 CD ARG A 216 11210 12551 12293 -88 -618 319 C ATOM 1620 NE ARG A 216 9.858 99.740 86.377 1.00107.79 N ANISOU 1620 NE ARG A 216 12946 14256 13754 -77 -692 449 N ATOM 1621 CZ ARG A 216 11.063 99.555 85.846 1.00116.65 C ANISOU 1621 CZ ARG A 216 14216 15476 14631 -65 -609 434 C ATOM 1622 NH1 ARG A 216 11.963 98.813 86.479 1.00117.22 N ANISOU 1622 NH1 ARG A 216 14336 15577 14624 -65 -469 291 N ATOM 1623 NH2 ARG A 216 11.370 100.110 84.681 1.00119.77 N ANISOU 1623 NH2 ARG A 216 14704 15939 14865 -47 -656 579 N ATOM 1624 N GLN A 217 7.305 103.817 90.505 1.00 80.78 N ANISOU 1624 N GLN A 217 8866 10209 11618 91 -273 529 N ATOM 1625 CA GLN A 217 6.363 104.929 90.503 1.00 81.37 C ANISOU 1625 CA GLN A 217 8786 10139 11992 150 -283 652 C ATOM 1626 C GLN A 217 7.096 106.261 90.623 1.00 82.47 C ANISOU 1626 C GLN A 217 8956 10176 12204 178 -209 682 C ATOM 1627 O GLN A 217 6.815 107.204 89.874 1.00 84.75 O ANISOU 1627 O GLN A 217 9174 10399 12628 194 -303 854 O ATOM 1628 CB GLN A 217 5.354 104.759 91.640 1.00 84.22 C ANISOU 1628 CB GLN A 217 9019 10400 12579 211 -145 579 C ATOM 1629 CG GLN A 217 4.225 105.776 91.632 1.00 96.70 C ANISOU 1629 CG GLN A 217 10408 11822 14512 290 -141 711 C ATOM 1630 CD GLN A 217 3.271 105.578 90.471 1.00103.96 C ANISOU 1630 CD GLN A 217 11193 12767 15542 259 -384 909 C ATOM 1631 OE1 GLN A 217 3.023 104.451 90.043 1.00106.42 O ANISOU 1631 OE1 GLN A 217 11516 13186 15732 194 -520 909 O ATOM 1632 NE2 GLN A 217 2.731 106.676 89.954 1.00105.72 N ANISOU 1632 NE2 GLN A 217 11291 12875 16002 304 -463 1081 N ATOM 1633 N ARG A 218 8.046 106.353 91.560 1.00 79.43 N ANISOU 1633 N ARG A 218 8673 9764 11741 178 -62 524 N ATOM 1634 CA ARG A 218 8.807 107.589 91.723 1.00 78.20 C ANISOU 1634 CA ARG A 218 8549 9488 11677 189 -17 542 C ATOM 1635 C ARG A 218 9.559 107.946 90.448 1.00 82.99 C ANISOU 1635 C ARG A 218 9188 10168 12178 136 -135 718 C ATOM 1636 O ARG A 218 9.586 109.113 90.040 1.00 89.04 O ANISOU 1636 O ARG A 218 9899 10821 13112 152 -171 858 O ATOM 1637 CB ARG A 218 9.784 107.463 92.892 1.00 75.59 C ANISOU 1637 CB ARG A 218 8341 9128 11252 177 109 341 C ATOM 1638 CG ARG A 218 9.141 107.233 94.249 1.00 80.00 C ANISOU 1638 CG ARG A 218 8909 9609 11879 242 255 168 C ATOM 1639 CD ARG A 218 10.214 107.143 95.326 1.00 87.81 C ANISOU 1639 CD ARG A 218 10054 10574 12737 219 333 -17 C ATOM 1640 NE ARG A 218 9.678 106.775 96.633 1.00 94.89 N ANISOU 1640 NE ARG A 218 11004 11428 13622 281 482 -182 N ATOM 1641 CZ ARG A 218 10.427 106.562 97.710 1.00 95.34 C ANISOU 1641 CZ ARG A 218 11216 11469 13538 269 543 -353 C ATOM 1642 NH1 ARG A 218 11.746 106.681 97.635 1.00 90.31 N ANISOU 1642 NH1 ARG A 218 10668 10844 12801 191 453 -378 N ATOM 1643 NH2 ARG A 218 9.861 106.231 98.862 1.00 99.27 N ANISOU 1643 NH2 ARG A 218 11779 11938 14001 336 692 -483 N ATOM 1644 N GLN A 219 10.178 106.954 89.806 1.00 81.27 N ANISOU 1644 N GLN A 219 9064 10132 11683 80 -182 719 N ATOM 1645 CA GLN A 219 10.888 107.216 88.560 1.00 84.78 C ANISOU 1645 CA GLN A 219 9559 10666 11988 45 -257 894 C ATOM 1646 C GLN A 219 9.927 107.639 87.457 1.00 80.47 C ANISOU 1646 C GLN A 219 8945 10122 11506 62 -414 1104 C ATOM 1647 O GLN A 219 10.265 108.488 86.623 1.00 85.27 O ANISOU 1647 O GLN A 219 9552 10717 12130 56 -461 1299 O ATOM 1648 CB GLN A 219 11.679 105.980 88.135 1.00 93.12 C ANISOU 1648 CB GLN A 219 10743 11911 12727 5 -249 830 C ATOM 1649 CG GLN A 219 12.531 106.206 86.902 1.00107.32 C ANISOU 1649 CG GLN A 219 12615 13813 14349 -13 -270 1004 C ATOM 1650 CD GLN A 219 12.942 104.913 86.236 1.00121.53 C ANISOU 1650 CD GLN A 219 14551 15800 15825 -25 -280 951 C ATOM 1651 OE1 GLN A 219 13.433 103.993 86.888 1.00127.86 O ANISOU 1651 OE1 GLN A 219 15398 16644 16540 -36 -203 777 O ATOM 1652 NE2 GLN A 219 12.733 104.832 84.927 1.00127.44 N ANISOU 1652 NE2 GLN A 219 15379 16653 16387 -17 -382 1100 N ATOM 1653 N ALA A 220 8.724 107.060 87.435 1.00 72.67 N ANISOU 1653 N ALA A 220 7894 9146 10571 78 -507 1087 N ATOM 1654 CA ALA A 220 7.745 107.445 86.425 1.00 74.80 C ANISOU 1654 CA ALA A 220 8088 9405 10929 88 -697 1294 C ATOM 1655 C ALA A 220 7.229 108.859 86.652 1.00 70.71 C ANISOU 1655 C ALA A 220 7418 8688 10762 140 -684 1420 C ATOM 1656 O ALA A 220 6.822 109.529 85.697 1.00 70.73 O ANISOU 1656 O ALA A 220 7371 8667 10837 145 -832 1646 O ATOM 1657 CB ALA A 220 6.585 106.451 86.409 1.00 50.08 C ANISOU 1657 CB ALA A 220 4896 6309 7821 82 -820 1250 C ATOM 1658 N ASP A 221 7.237 109.328 87.903 1.00 62.55 N ANISOU 1658 N ASP A 221 6323 7502 9940 186 -514 1277 N ATOM 1659 CA ASP A 221 6.808 110.692 88.192 1.00 67.05 C ANISOU 1659 CA ASP A 221 6766 7854 10855 250 -482 1365 C ATOM 1660 C ASP A 221 7.894 111.707 87.847 1.00 69.97 C ANISOU 1660 C ASP A 221 7192 8164 11230 224 -466 1467 C ATOM 1661 O ASP A 221 7.590 112.795 87.345 1.00 68.78 O ANISOU 1661 O ASP A 221 6949 7885 11300 250 -538 1661 O ATOM 1662 CB ASP A 221 6.403 110.816 89.663 1.00 64.96 C ANISOU 1662 CB ASP A 221 6451 7440 10790 323 -294 1155 C ATOM 1663 CG ASP A 221 5.117 110.072 89.982 1.00 75.17 C ANISOU 1663 CG ASP A 221 7624 8746 12191 365 -291 1123 C ATOM 1664 OD1 ASP A 221 4.504 109.502 89.054 1.00 80.43 O ANISOU 1664 OD1 ASP A 221 8233 9517 12811 328 -472 1263 O ATOM 1665 OD2 ASP A 221 4.718 110.057 91.167 1.00 81.18 O ANISOU 1665 OD2 ASP A 221 8351 9408 13086 436 -109 965 O ATOM 1666 N LEU A 222 9.160 111.371 88.110 1.00 70.26 N ANISOU 1666 N LEU A 222 7359 8279 11056 171 -378 1357 N ATOM 1667 CA LEU A 222 10.260 112.254 87.730 1.00 73.29 C ANISOU 1667 CA LEU A 222 7774 8611 11462 133 -366 1481 C ATOM 1668 C LEU A 222 10.312 112.441 86.220 1.00 83.10 C ANISOU 1668 C LEU A 222 9025 9968 12583 106 -494 1769 C ATOM 1669 O LEU A 222 10.421 113.569 85.724 1.00 89.64 O ANISOU 1669 O LEU A 222 9790 10680 13591 108 -537 1979 O ATOM 1670 CB LEU A 222 11.587 111.692 88.244 1.00 75.53 C ANISOU 1670 CB LEU A 222 8174 8974 11551 78 -261 1327 C ATOM 1671 CG LEU A 222 11.956 111.968 89.701 1.00 79.86 C ANISOU 1671 CG LEU A 222 8743 9360 12238 89 -156 1091 C ATOM 1672 CD1 LEU A 222 13.140 111.114 90.128 1.00 76.18 C ANISOU 1672 CD1 LEU A 222 8385 9012 11547 29 -93 952 C ATOM 1673 CD2 LEU A 222 12.266 113.443 89.893 1.00 86.95 C ANISOU 1673 CD2 LEU A 222 9585 10017 13437 95 -165 1169 C ATOM 1674 N GLU A 223 10.234 111.340 85.471 1.00 89.51 N ANISOU 1674 N GLU A 223 9930 11000 13080 82 -561 1783 N ATOM 1675 CA GLU A 223 10.284 111.429 84.016 1.00 95.29 C ANISOU 1675 CA GLU A 223 10721 11860 13625 63 -683 2042 C ATOM 1676 C GLU A 223 9.030 112.079 83.446 1.00 93.87 C ANISOU 1676 C GLU A 223 10428 11591 13645 96 -865 2239 C ATOM 1677 O GLU A 223 9.080 112.658 82.356 1.00 96.05 O ANISOU 1677 O GLU A 223 10726 11899 13868 88 -969 2507 O ATOM 1678 CB GLU A 223 10.490 110.039 83.416 1.00101.90 C ANISOU 1678 CB GLU A 223 11721 12938 14060 40 -715 1965 C ATOM 1679 CG GLU A 223 11.839 109.430 83.752 1.00111.01 C ANISOU 1679 CG GLU A 223 12978 14188 15013 13 -539 1827 C ATOM 1680 CD GLU A 223 11.956 107.986 83.311 1.00119.81 C ANISOU 1680 CD GLU A 223 14248 15506 15767 6 -559 1707 C ATOM 1681 OE1 GLU A 223 10.921 107.389 82.948 1.00122.45 O ANISOU 1681 OE1 GLU A 223 14607 15888 16031 12 -722 1687 O ATOM 1682 OE2 GLU A 223 13.084 107.447 83.326 1.00122.60 O ANISOU 1682 OE2 GLU A 223 14693 15957 15932 -4 -420 1637 O ATOM 1683 N ASP A 224 7.903 111.997 84.158 1.00 92.52 N ANISOU 1683 N ASP A 224 10131 11307 13716 138 -900 2131 N ATOM 1684 CA ASP A 224 6.691 112.662 83.688 1.00 96.29 C ANISOU 1684 CA ASP A 224 10460 11672 14453 176 -1071 2331 C ATOM 1685 C ASP A 224 6.805 114.175 83.832 1.00 92.99 C ANISOU 1685 C ASP A 224 9927 11030 14377 212 -1030 2481 C ATOM 1686 O ASP A 224 6.364 114.923 82.951 1.00 87.45 O ANISOU 1686 O ASP A 224 9158 10276 13792 221 -1185 2757 O ATOM 1687 CB ASP A 224 5.471 112.137 84.446 1.00106.27 C ANISOU 1687 CB ASP A 224 11590 12868 15921 219 -1087 2189 C ATOM 1688 CG ASP A 224 4.176 112.329 83.676 1.00121.78 C ANISOU 1688 CG ASP A 224 13416 14791 18064 237 -1331 2410 C ATOM 1689 OD1 ASP A 224 3.847 111.460 82.841 1.00127.47 O ANISOU 1689 OD1 ASP A 224 14215 15673 18544 188 -1529 2465 O ATOM 1690 OD2 ASP A 224 3.491 113.348 83.901 1.00126.63 O ANISOU 1690 OD2 ASP A 224 13845 15199 19068 301 -1338 2527 O ATOM 1691 N ASN A 225 7.395 114.645 84.934 1.00 92.19 N ANISOU 1691 N ASN A 225 9809 10780 14440 232 -840 2305 N ATOM 1692 CA ASN A 225 7.614 116.079 85.103 1.00 90.04 C ANISOU 1692 CA ASN A 225 9446 10267 14498 260 -808 2423 C ATOM 1693 C ASN A 225 8.639 116.597 84.102 1.00 94.45 C ANISOU 1693 C ASN A 225 10074 10889 14924 196 -846 2671 C ATOM 1694 O ASN A 225 8.440 117.647 83.480 1.00 96.39 O ANISOU 1694 O ASN A 225 10233 11008 15381 207 -937 2936 O ATOM 1695 CB ASN A 225 8.062 116.383 86.533 1.00 79.77 C ANISOU 1695 CB ASN A 225 8154 8792 13364 289 -621 2145 C ATOM 1696 CG ASN A 225 6.958 116.177 87.549 1.00 75.89 C ANISOU 1696 CG ASN A 225 7577 8189 13069 381 -545 1946 C ATOM 1697 OD1 ASN A 225 5.778 116.360 87.247 1.00 76.83 O ANISOU 1697 OD1 ASN A 225 7553 8248 13392 441 -629 2068 O ATOM 1698 ND2 ASN A 225 7.336 115.797 88.764 1.00 74.67 N ANISOU 1698 ND2 ASN A 225 7506 8004 12859 396 -383 1652 N ATOM 1699 N TRP A 226 9.749 115.873 83.939 1.00 97.49 N ANISOU 1699 N TRP A 226 10605 11462 14974 133 -764 2605 N ATOM 1700 CA TRP A 226 10.771 116.288 82.984 1.00105.23 C ANISOU 1700 CA TRP A 226 11645 12520 15817 80 -756 2855 C ATOM 1701 C TRP A 226 10.251 116.238 81.554 1.00114.21 C ANISOU 1701 C TRP A 226 12826 13805 16763 80 -922 3151 C ATOM 1702 O TRP A 226 10.663 117.049 80.716 1.00121.41 O ANISOU 1702 O TRP A 226 13732 14700 17700 62 -949 3450 O ATOM 1703 CB TRP A 226 12.013 115.409 83.137 1.00104.18 C ANISOU 1703 CB TRP A 226 11643 12561 15378 29 -613 2714 C ATOM 1704 CG TRP A 226 13.210 115.892 82.373 1.00112.22 C ANISOU 1704 CG TRP A 226 12691 13628 16317 -18 -541 2958 C ATOM 1705 CD1 TRP A 226 14.021 116.940 82.697 1.00114.14 C ANISOU 1705 CD1 TRP A 226 12842 13679 16846 -53 -475 3054 C ATOM 1706 CD2 TRP A 226 13.740 115.334 81.165 1.00119.89 C ANISOU 1706 CD2 TRP A 226 13795 14850 16906 -32 -517 3142 C ATOM 1707 NE1 TRP A 226 15.021 117.073 81.764 1.00117.12 N ANISOU 1707 NE1 TRP A 226 13256 14175 17071 -92 -400 3314 N ATOM 1708 CE2 TRP A 226 14.872 116.098 80.813 1.00121.92 C ANISOU 1708 CE2 TRP A 226 14011 15062 17249 -70 -405 3369 C ATOM 1709 CE3 TRP A 226 13.365 114.266 80.345 1.00124.65 C ANISOU 1709 CE3 TRP A 226 14557 15701 17104 -12 -578 3136 C ATOM 1710 CZ2 TRP A 226 15.630 115.829 79.674 1.00128.20 C ANISOU 1710 CZ2 TRP A 226 14916 16066 17727 -76 -315 3600 C ATOM 1711 CZ3 TRP A 226 14.119 113.999 79.216 1.00129.58 C ANISOU 1711 CZ3 TRP A 226 15321 16526 17387 -14 -506 3335 C ATOM 1712 CH2 TRP A 226 15.239 114.778 78.891 1.00131.52 C ANISOU 1712 CH2 TRP A 226 15519 16736 17714 -39 -356 3571 C ATOM 1713 N GLU A 227 9.347 115.302 81.255 1.00115.62 N ANISOU 1713 N GLU A 227 13054 14124 16752 97 -1048 3082 N ATOM 1714 CA GLU A 227 8.740 115.260 79.928 1.00115.77 C ANISOU 1714 CA GLU A 227 13132 14266 16588 96 -1258 3350 C ATOM 1715 C GLU A 227 7.874 116.488 79.687 1.00114.12 C ANISOU 1715 C GLU A 227 12748 13847 16767 129 -1405 3602 C ATOM 1716 O GLU A 227 8.053 117.197 78.691 1.00119.73 O ANISOU 1716 O GLU A 227 13483 14570 17441 117 -1491 3925 O ATOM 1717 CB GLU A 227 7.918 113.981 79.760 1.00120.87 C ANISOU 1717 CB GLU A 227 13858 15070 17000 95 -1398 3199 C ATOM 1718 CG GLU A 227 7.069 113.954 78.497 1.00133.52 C ANISOU 1718 CG GLU A 227 15512 16759 18459 92 -1683 3453 C ATOM 1719 CD GLU A 227 6.256 112.682 78.368 1.00141.18 C ANISOU 1719 CD GLU A 227 16553 17853 19235 78 -1854 3292 C ATOM 1720 OE1 GLU A 227 6.707 111.634 78.878 1.00142.38 O ANISOU 1720 OE1 GLU A 227 16803 18110 19187 63 -1728 3020 O ATOM 1721 OE2 GLU A 227 5.163 112.729 77.764 1.00145.25 O ANISOU 1721 OE2 GLU A 227 17017 18348 19824 77 -2132 3447 O ATOM 1722 N THR A 228 6.937 116.764 80.599 1.00105.41 N ANISOU 1722 N THR A 228 11463 12541 16045 180 -1419 3470 N ATOM 1723 CA THR A 228 6.061 117.919 80.446 1.00 98.49 C ANISOU 1723 CA THR A 228 10397 11437 15589 230 -1546 3695 C ATOM 1724 C THR A 228 6.835 119.230 80.384 1.00 96.15 C ANISOU 1724 C THR A 228 10051 10963 15520 224 -1464 3882 C ATOM 1725 O THR A 228 6.298 120.231 79.897 1.00 96.99 O ANISOU 1725 O THR A 228 10033 10911 15910 252 -1596 4157 O ATOM 1726 CB THR A 228 5.047 117.971 81.591 1.00 92.18 C ANISOU 1726 CB THR A 228 9412 10439 15174 306 -1500 3484 C ATOM 1727 OG1 THR A 228 5.741 117.991 82.845 1.00 89.39 O ANISOU 1727 OG1 THR A 228 9079 9988 14895 320 -1250 3186 O ATOM 1728 CG2 THR A 228 4.123 116.758 81.545 1.00 86.03 C ANISOU 1728 CG2 THR A 228 8632 9808 14246 305 -1617 3371 C ATOM 1729 N LEU A 229 8.082 119.250 80.853 1.00 92.04 N ANISOU 1729 N LEU A 229 9612 10451 14908 184 -1267 3754 N ATOM 1730 CA LEU A 229 8.877 120.471 80.787 1.00 88.80 C ANISOU 1730 CA LEU A 229 9143 9857 14740 163 -1204 3942 C ATOM 1731 C LEU A 229 9.479 120.667 79.397 1.00 96.07 C ANISOU 1731 C LEU A 229 10158 10945 15400 111 -1263 4314 C ATOM 1732 O LEU A 229 9.257 121.700 78.756 1.00103.26 O ANISOU 1732 O LEU A 229 10981 11726 16528 118 -1368 4642 O ATOM 1733 CB LEU A 229 9.968 120.448 81.862 1.00 78.67 C ANISOU 1733 CB LEU A 229 7891 8494 13504 132 -999 3675 C ATOM 1734 CG LEU A 229 9.488 120.791 83.275 1.00 78.32 C ANISOU 1734 CG LEU A 229 7753 8188 13815 194 -929 3371 C ATOM 1735 CD1 LEU A 229 10.655 120.847 84.248 1.00 75.57 C ANISOU 1735 CD1 LEU A 229 7464 7755 13494 149 -776 3138 C ATOM 1736 CD2 LEU A 229 8.729 122.110 83.270 1.00 89.71 C ANISOU 1736 CD2 LEU A 229 9027 9324 15735 258 -1016 3543 C ATOM 1737 N ASN A 230 10.246 119.683 78.915 1.00 95.16 N ANISOU 1737 N ASN A 230 10227 11114 14815 69 -1184 4275 N ATOM 1738 CA ASN A 230 10.826 119.785 77.578 1.00105.95 C ANISOU 1738 CA ASN A 230 11717 12665 15875 38 -1201 4621 C ATOM 1739 C ASN A 230 9.742 119.819 76.509 1.00113.51 C ANISOU 1739 C ASN A 230 12714 13704 16710 64 -1457 4874 C ATOM 1740 O ASN A 230 9.839 120.579 75.537 1.00117.95 O ANISOU 1740 O ASN A 230 13288 14266 17261 56 -1533 5254 O ATOM 1741 CB ASN A 230 11.775 118.617 77.319 1.00108.79 C ANISOU 1741 CB ASN A 230 12278 13310 15747 13 -1046 4490 C ATOM 1742 CG ASN A 230 12.710 118.359 78.475 1.00111.14 C ANISOU 1742 CG ASN A 230 12534 13540 16155 -13 -835 4197 C ATOM 1743 OD1 ASN A 230 13.275 119.286 79.057 1.00111.10 O ANISOU 1743 OD1 ASN A 230 12393 13312 16507 -39 -755 4233 O ATOM 1744 ND2 ASN A 230 12.866 117.093 78.829 1.00109.03 N ANISOU 1744 ND2 ASN A 230 12384 13448 15593 -10 -768 3904 N ATOM 1745 N ASP A 231 8.702 118.997 76.671 1.00112.34 N ANISOU 1745 N ASP A 231 12583 13620 16480 90 -1608 4683 N ATOM 1746 CA ASP A 231 7.629 118.957 75.684 1.00114.54 C ANISOU 1746 CA ASP A 231 12895 13968 16657 104 -1901 4911 C ATOM 1747 C ASP A 231 6.944 120.313 75.566 1.00111.20 C ANISOU 1747 C ASP A 231 12258 13281 16713 132 -2042 5201 C ATOM 1748 O ASP A 231 6.673 120.784 74.456 1.00112.28 O ANISOU 1748 O ASP A 231 12440 13462 16758 126 -2229 5565 O ATOM 1749 CB ASP A 231 6.616 117.870 76.049 1.00118.34 C ANISOU 1749 CB ASP A 231 13378 14514 17071 118 -2042 4642 C ATOM 1750 CG ASP A 231 6.059 117.153 74.832 1.00125.28 C ANISOU 1750 CG ASP A 231 14449 15615 17536 99 -2314 4784 C ATOM 1751 OD1 ASP A 231 6.757 117.104 73.798 1.00130.13 O ANISOU 1751 OD1 ASP A 231 15287 16417 17741 81 -2306 4982 O ATOM 1752 OD2 ASP A 231 4.921 116.640 74.908 1.00127.77 O ANISOU 1752 OD2 ASP A 231 14698 15911 17938 105 -2538 4703 O ATOM 1753 N ASN A 232 6.679 120.967 76.701 1.00109.34 N ANISOU 1753 N ASN A 232 11800 12760 16984 170 -1951 5048 N ATOM 1754 CA ASN A 232 5.976 122.246 76.665 1.00113.97 C ANISOU 1754 CA ASN A 232 12169 13061 18074 213 -2075 5296 C ATOM 1755 C ASN A 232 6.827 123.348 76.041 1.00112.38 C ANISOU 1755 C ASN A 232 11968 12778 17952 181 -2029 5645 C ATOM 1756 O ASN A 232 6.284 124.254 75.398 1.00110.52 O ANISOU 1756 O ASN A 232 11628 12410 17953 199 -2207 5993 O ATOM 1757 CB ASN A 232 5.536 122.651 78.073 1.00114.06 C ANISOU 1757 CB ASN A 232 11976 12780 18584 279 -1953 5012 C ATOM 1758 CG ASN A 232 4.113 122.208 78.397 1.00112.50 C ANISOU 1758 CG ASN A 232 11643 12534 18568 343 -2095 4899 C ATOM 1759 OD1 ASN A 232 3.210 122.315 77.566 1.00113.63 O ANISOU 1759 OD1 ASN A 232 11723 12694 18756 353 -2354 5162 O ATOM 1760 ND2 ASN A 232 3.909 121.718 79.617 1.00109.84 N ANISOU 1760 ND2 ASN A 232 11254 12130 18349 386 -1927 4524 N ATOM 1761 N LEU A 233 8.151 123.292 76.219 1.00107.66 N ANISOU 1761 N LEU A 233 11468 12248 17192 131 -1798 5581 N ATOM 1762 CA LEU A 233 9.020 124.302 75.622 1.00104.27 C ANISOU 1762 CA LEU A 233 11020 11741 16856 91 -1737 5936 C ATOM 1763 C LEU A 233 8.981 124.224 74.102 1.00109.63 C ANISOU 1763 C LEU A 233 11857 12658 17140 73 -1877 6341 C ATOM 1764 O LEU A 233 8.945 125.255 73.419 1.00114.82 O ANISOU 1764 O LEU A 233 12444 13199 17984 67 -1967 6744 O ATOM 1765 CB LEU A 233 10.451 124.136 76.139 1.00100.95 C ANISOU 1765 CB LEU A 233 10653 11353 16348 37 -1464 5781 C ATOM 1766 CG LEU A 233 10.716 124.602 77.575 1.00 99.31 C ANISOU 1766 CG LEU A 233 10297 10848 16590 41 -1343 5470 C ATOM 1767 CD1 LEU A 233 12.188 124.461 77.941 1.00 99.99 C ANISOU 1767 CD1 LEU A 233 10430 10972 16590 -30 -1122 5380 C ATOM 1768 CD2 LEU A 233 10.262 126.041 77.749 1.00102.33 C ANISOU 1768 CD2 LEU A 233 10475 10858 17549 69 -1440 5664 C ATOM 1769 N LYS A 234 8.971 123.004 73.560 1.00109.76 N ANISOU 1769 N LYS A 234 12103 13000 16599 67 -1904 6237 N ATOM 1770 CA LYS A 234 8.834 122.819 72.119 1.00111.73 C ANISOU 1770 CA LYS A 234 12558 13490 16402 61 -2062 6578 C ATOM 1771 C LYS A 234 7.533 123.416 71.607 1.00116.89 C ANISOU 1771 C LYS A 234 13109 14020 17285 87 -2402 6840 C ATOM 1772 O LYS A 234 7.460 123.857 70.453 1.00126.45 O ANISOU 1772 O LYS A 234 14425 15328 18292 71 -2519 7166 O ATOM 1773 CB LYS A 234 8.898 121.332 71.779 1.00107.48 C ANISOU 1773 CB LYS A 234 12293 13282 15264 61 -2061 6339 C ATOM 1774 N VAL A 235 6.498 123.430 72.448 1.00113.93 N ANISOU 1774 N VAL A 235 12530 13445 17312 123 -2525 6622 N ATOM 1775 CA VAL A 235 5.265 124.129 72.106 1.00119.29 C ANISOU 1775 CA VAL A 235 13046 13962 18316 145 -2801 6809 C ATOM 1776 C VAL A 235 5.503 125.633 72.078 1.00123.85 C ANISOU 1776 C VAL A 235 13446 14292 19318 132 -2714 7006 C ATOM 1777 O VAL A 235 5.071 126.330 71.153 1.00131.95 O ANISOU 1777 O VAL A 235 14464 15319 20351 107 -2867 7264 O ATOM 1778 CB VAL A 235 4.142 123.751 73.091 1.00120.37 C ANISOU 1778 CB VAL A 235 12982 13936 18818 202 -2903 6535 C ATOM 1779 CG1 VAL A 235 3.002 124.755 73.021 1.00122.85 C ANISOU 1779 CG1 VAL A 235 13055 14013 19608 217 -3057 6634 C ATOM 1780 CG2 VAL A 235 3.639 122.342 72.814 1.00122.34 C ANISOU 1780 CG2 VAL A 235 13400 14446 18637 186 -3065 6358 C ATOM 1781 N ILE A 236 6.220 126.151 73.080 1.00123.86 N ANISOU 1781 N ILE A 236 13313 14073 19677 143 -2479 6883 N ATOM 1782 CA ILE A 236 6.456 127.590 73.158 1.00124.51 C ANISOU 1782 CA ILE A 236 13214 13891 20205 125 -2408 7029 C ATOM 1783 C ILE A 236 7.305 128.055 71.983 1.00133.42 C ANISOU 1783 C ILE A 236 14473 15181 21038 58 -2360 7373 C ATOM 1784 O ILE A 236 7.044 129.108 71.388 1.00130.24 O ANISOU 1784 O ILE A 236 13973 14672 20839 37 -2444 7617 O ATOM 1785 CB ILE A 236 7.110 127.952 74.504 1.00113.69 C ANISOU 1785 CB ILE A 236 11711 12249 19237 143 -2185 6780 C ATOM 1786 CG1 ILE A 236 6.278 127.415 75.667 1.00109.03 C ANISOU 1786 CG1 ILE A 236 11020 11517 18887 229 -2199 6428 C ATOM 1787 CG2 ILE A 236 7.277 129.459 74.623 1.00 97.44 C ANISOU 1787 CG2 ILE A 236 9463 9894 17667 121 -2144 6899 C ATOM 1788 CD1 ILE A 236 6.974 127.511 77.005 1.00107.56 C ANISOU 1788 CD1 ILE A 236 10784 11115 18967 252 -1978 6119 C ATOM 1789 N GLU A 237 8.330 127.276 71.628 1.00145.44 N ANISOU 1789 N GLU A 237 16215 16965 22080 31 -2207 7400 N ATOM 1790 CA GLU A 237 9.184 127.635 70.501 1.00155.59 C ANISOU 1790 CA GLU A 237 17640 18429 23050 -16 -2111 7717 C ATOM 1791 C GLU A 237 8.414 127.594 69.187 1.00164.47 C ANISOU 1791 C GLU A 237 18922 19745 23825 -11 -2347 7952 C ATOM 1792 O GLU A 237 8.626 128.440 68.311 1.00172.16 O ANISOU 1792 O GLU A 237 19906 20727 24782 -37 -2352 8257 O ATOM 1793 CB GLU A 237 10.393 126.703 70.448 1.00151.66 C ANISOU 1793 CB GLU A 237 17343 18177 22103 -30 -1866 7663 C ATOM 1794 CG GLU A 237 11.247 126.726 71.703 1.00150.95 C ANISOU 1794 CG GLU A 237 17111 17901 22342 -48 -1642 7444 C ATOM 1795 CD GLU A 237 12.377 125.719 71.655 1.00150.78 C ANISOU 1795 CD GLU A 237 17274 18132 21885 -62 -1403 7386 C ATOM 1796 OE1 GLU A 237 12.413 124.910 70.705 1.00152.40 O ANISOU 1796 OE1 GLU A 237 17733 18663 21510 -42 -1408 7473 O ATOM 1797 OE2 GLU A 237 13.229 125.738 72.566 1.00148.92 O ANISOU 1797 OE2 GLU A 237 16935 17766 21880 -92 -1209 7221 O ATOM 1798 N LYS A 238 7.519 126.622 69.031 1.00158.06 N ANISOU 1798 N LYS A 238 18236 19079 22739 18 -2559 7815 N ATOM 1799 CA LYS A 238 6.702 126.504 67.832 1.00157.89 C ANISOU 1799 CA LYS A 238 18381 19222 22388 17 -2832 7997 C ATOM 1800 C LYS A 238 5.381 127.255 67.942 1.00160.20 C ANISOU 1800 C LYS A 238 18432 19274 23162 22 -3096 8040 C ATOM 1801 O LYS A 238 4.517 127.091 67.075 1.00163.39 O ANISOU 1801 O LYS A 238 18942 19782 23357 18 -3373 8155 O ATOM 1802 CB LYS A 238 6.430 125.030 67.523 1.00151.81 C ANISOU 1802 CB LYS A 238 17889 18736 21056 34 -2954 7819 C ATOM 1803 N ALA A 239 5.204 128.067 68.981 1.00156.11 N ANISOU 1803 N ALA A 239 17601 18434 23281 35 -3016 7941 N ATOM 1804 CA ALA A 239 3.938 128.760 69.173 1.00154.45 C ANISOU 1804 CA ALA A 239 17142 17983 23557 51 -3225 7957 C ATOM 1805 C ALA A 239 3.819 129.937 68.214 1.00160.52 C ANISOU 1805 C ALA A 239 17863 18689 24437 19 -3324 8320 C ATOM 1806 O ALA A 239 4.798 130.633 67.931 1.00161.41 O ANISOU 1806 O ALA A 239 17993 18788 24546 -10 -3150 8507 O ATOM 1807 CB ALA A 239 3.803 129.244 70.615 1.00148.83 C ANISOU 1807 CB ALA A 239 16142 16941 23463 93 -3076 7703 C ATOM 1808 N ASP A 240 2.604 130.152 67.708 1.00165.43 N ANISOU 1808 N ASP A 240 18413 19267 25174 18 -3612 8428 N ATOM 1809 CA ASP A 240 2.299 131.302 66.866 1.00170.41 C ANISOU 1809 CA ASP A 240 18963 19805 25980 -9 -3743 8771 C ATOM 1810 C ASP A 240 1.182 132.159 67.449 1.00169.55 C ANISOU 1810 C ASP A 240 18506 19367 26549 10 -3858 8743 C ATOM 1811 O ASP A 240 0.691 133.069 66.770 1.00172.42 O ANISOU 1811 O ASP A 240 18772 19636 27103 -12 -4017 9021 O ATOM 1812 CB ASP A 240 1.934 130.847 65.448 1.00175.92 C ANISOU 1812 CB ASP A 240 19944 20778 26121 -33 -4003 8999 C ATOM 1813 CG ASP A 240 0.674 130.003 65.408 1.00178.37 C ANISOU 1813 CG ASP A 240 20263 21138 26371 -27 -4300 8849 C ATOM 1814 OD1 ASP A 240 0.300 129.435 66.455 1.00176.75 O ANISOU 1814 OD1 ASP A 240 19916 20841 26401 0 -4253 8539 O ATOM 1815 OD2 ASP A 240 0.061 129.902 64.323 1.00182.17 O ANISOU 1815 OD2 ASP A 240 20896 21747 26573 -50 -4586 9042 O ATOM 1816 N ASN A 241 0.767 131.891 68.685 1.00168.92 N ANISOU 1816 N ASN A 241 18241 19110 26831 58 -3769 8418 N ATOM 1817 CA ASN A 241 -0.279 132.647 69.354 1.00169.64 C ANISOU 1817 CA ASN A 241 18006 18883 27567 96 -3820 8349 C ATOM 1818 C ASN A 241 0.263 133.246 70.644 1.00156.81 C ANISOU 1818 C ASN A 241 16205 16981 26394 144 -3531 8118 C ATOM 1819 O ASN A 241 1.144 132.673 71.293 1.00154.31 O ANISOU 1819 O ASN A 241 15998 16726 25906 158 -3326 7901 O ATOM 1820 CB ASN A 241 -1.497 131.764 69.666 1.00178.60 C ANISOU 1820 CB ASN A 241 19074 20038 28748 126 -3986 8156 C ATOM 1821 CG ASN A 241 -2.254 131.348 68.420 1.00188.43 C ANISOU 1821 CG ASN A 241 20449 21484 29661 72 -4331 8381 C ATOM 1822 OD1 ASN A 241 -1.809 131.587 67.298 1.00192.23 O ANISOU 1822 OD1 ASN A 241 21125 22128 29784 25 -4435 8663 O ATOM 1823 ND2 ASN A 241 -3.407 130.717 68.612 1.00191.53 N ANISOU 1823 ND2 ASN A 241 20741 21861 30170 80 -4510 8254 N ATOM 1824 N ALA A 242 -0.274 134.410 71.012 1.00146.90 N ANISOU 1824 N ALA A 242 14684 15412 25718 171 -3524 8158 N ATOM 1825 CA ALA A 242 0.145 135.050 72.255 1.00139.89 C ANISOU 1825 CA ALA A 242 13645 14231 25277 225 -3273 7911 C ATOM 1826 C ALA A 242 -0.459 134.363 73.473 1.00139.67 C ANISOU 1826 C ALA A 242 13539 14105 25423 314 -3163 7518 C ATOM 1827 O ALA A 242 0.118 134.421 74.565 1.00114.50 O ANISOU 1827 O ALA A 242 10341 10767 22395 363 -2933 7235 O ATOM 1828 CB ALA A 242 -0.233 136.530 72.236 1.00139.32 C ANISOU 1828 CB ALA A 242 13331 13849 25754 232 -3300 8071 C ATOM 1829 N ALA A 243 -1.608 133.709 73.310 1.00138.53 N ANISOU 1829 N ALA A 243 13344 14040 25250 335 -3326 7495 N ATOM 1830 CA ALA A 243 -2.275 133.035 74.417 1.00130.96 C ANISOU 1830 CA ALA A 243 12294 13000 24465 422 -3214 7148 C ATOM 1831 C ALA A 243 -1.776 131.615 74.645 1.00123.68 C ANISOU 1831 C ALA A 243 11586 12341 23066 418 -3165 6949 C ATOM 1832 O ALA A 243 -1.900 131.101 75.762 1.00108.06 O ANISOU 1832 O ALA A 243 9567 10286 21204 496 -2988 6623 O ATOM 1833 CB ALA A 243 -3.787 133.014 74.185 1.00132.92 C ANISOU 1833 CB ALA A 243 12346 13187 24970 439 -3402 7224 C ATOM 1834 N GLN A 244 -1.205 130.976 73.620 1.00120.03 N ANISOU 1834 N GLN A 244 11359 12185 22060 337 -3304 7134 N ATOM 1835 CA GLN A 244 -0.688 129.621 73.786 1.00124.31 C ANISOU 1835 CA GLN A 244 12115 12983 22135 331 -3262 6953 C ATOM 1836 C GLN A 244 0.462 129.574 74.781 1.00122.88 C ANISOU 1836 C GLN A 244 11995 12729 21964 366 -2968 6718 C ATOM 1837 O GLN A 244 0.603 128.591 75.521 1.00117.17 O ANISOU 1837 O GLN A 244 11336 12080 21103 406 -2865 6448 O ATOM 1838 CB GLN A 244 -0.237 129.056 72.440 1.00135.27 C ANISOU 1838 CB GLN A 244 13773 14705 22918 245 -3448 7202 C ATOM 1839 CG GLN A 244 -1.368 128.602 71.532 1.00144.04 C ANISOU 1839 CG GLN A 244 14902 15950 23876 208 -3776 7343 C ATOM 1840 CD GLN A 244 -0.860 128.052 70.207 1.00146.31 C ANISOU 1840 CD GLN A 244 15512 16566 23511 137 -3946 7556 C ATOM 1841 OE1 GLN A 244 0.114 128.554 69.644 1.00143.45 O ANISOU 1841 OE1 GLN A 244 15289 16277 22937 108 -3853 7750 O ATOM 1842 NE2 GLN A 244 -1.516 127.011 69.709 1.00149.29 N ANISOU 1842 NE2 GLN A 244 16018 17138 23566 110 -4186 7512 N ATOM 1843 N VAL A 245 1.289 130.620 74.819 1.00128.69 N ANISOU 1843 N VAL A 245 12708 13312 22878 345 -2843 6818 N ATOM 1844 CA VAL A 245 2.447 130.600 75.705 1.00122.69 C ANISOU 1844 CA VAL A 245 12015 12472 22128 357 -2593 6608 C ATOM 1845 C VAL A 245 2.036 130.831 77.154 1.00118.47 C ANISOU 1845 C VAL A 245 11327 11643 22043 460 -2422 6249 C ATOM 1846 O VAL A 245 2.729 130.384 78.075 1.00106.73 O ANISOU 1846 O VAL A 245 9921 10122 20508 491 -2240 5979 O ATOM 1847 CB VAL A 245 3.494 131.631 75.248 1.00120.06 C ANISOU 1847 CB VAL A 245 11700 12068 21848 286 -2528 6835 C ATOM 1848 CG1 VAL A 245 3.892 131.373 73.801 1.00124.22 C ANISOU 1848 CG1 VAL A 245 12404 12906 21889 201 -2658 7188 C ATOM 1849 CG2 VAL A 245 2.963 133.046 75.414 1.00114.42 C ANISOU 1849 CG2 VAL A 245 10757 11031 21689 308 -2550 6908 C ATOM 1850 N LYS A 246 0.916 131.520 77.389 1.00126.36 N ANISOU 1850 N LYS A 246 12116 12426 23471 520 -2467 6234 N ATOM 1851 CA LYS A 246 0.457 131.724 78.759 1.00127.33 C ANISOU 1851 CA LYS A 246 12115 12280 23984 636 -2274 5881 C ATOM 1852 C LYS A 246 -0.011 130.414 79.380 1.00132.11 C ANISOU 1852 C LYS A 246 12761 13025 24409 700 -2219 5623 C ATOM 1853 O LYS A 246 0.223 130.162 80.568 1.00132.53 O ANISOU 1853 O LYS A 246 12841 12961 24552 782 -2004 5287 O ATOM 1854 CB LYS A 246 -0.663 132.764 78.793 1.00129.06 C ANISOU 1854 CB LYS A 246 12095 12248 24695 690 -2318 5952 C ATOM 1855 CG LYS A 246 -1.039 133.224 80.193 1.00130.49 C ANISOU 1855 CG LYS A 246 12170 12120 25290 821 -2081 5598 C ATOM 1856 CD LYS A 246 -2.436 133.824 80.226 1.00140.42 C ANISOU 1856 CD LYS A 246 13185 13199 26968 892 -2116 5653 C ATOM 1857 CE LYS A 246 -2.729 134.472 81.572 1.00144.21 C ANISOU 1857 CE LYS A 246 13584 13356 27854 1033 -1854 5316 C ATOM 1858 NZ LYS A 246 -2.330 133.602 82.714 1.00140.96 N ANISOU 1858 NZ LYS A 246 13322 12980 27259 1110 -1630 4928 N ATOM 1859 N ASP A 247 -0.672 129.565 78.590 1.00126.49 N ANISOU 1859 N ASP A 247 12064 12560 23437 660 -2419 5771 N ATOM 1860 CA ASP A 247 -1.134 128.279 79.097 1.00120.11 C ANISOU 1860 CA ASP A 247 11280 11897 22459 706 -2392 5549 C ATOM 1861 C ASP A 247 -0.015 127.247 79.150 1.00121.11 C ANISOU 1861 C ASP A 247 11641 12257 22117 670 -2342 5452 C ATOM 1862 O ASP A 247 -0.053 126.343 79.991 1.00108.24 O ANISOU 1862 O ASP A 247 10035 10672 20417 731 -2220 5178 O ATOM 1863 CB ASP A 247 -2.286 127.755 78.238 1.00127.24 C ANISOU 1863 CB ASP A 247 12107 12957 23281 662 -2656 5730 C ATOM 1864 CG ASP A 247 -3.550 128.582 78.385 1.00140.73 C ANISOU 1864 CG ASP A 247 13548 14425 25496 711 -2677 5785 C ATOM 1865 OD1 ASP A 247 -3.751 129.180 79.462 1.00143.97 O ANISOU 1865 OD1 ASP A 247 13832 14574 26296 816 -2435 5571 O ATOM 1866 OD2 ASP A 247 -4.345 128.630 77.423 1.00146.87 O ANISOU 1866 OD2 ASP A 247 14255 15272 26276 647 -2937 6038 O ATOM 1867 N ALA A 248 0.981 127.361 78.268 1.00136.86 N ANISOU 1867 N ALA A 248 13804 14403 23792 575 -2417 5680 N ATOM 1868 CA ALA A 248 2.075 126.395 78.267 1.00 90.07 C ANISOU 1868 CA ALA A 248 8100 8703 17420 539 -2355 5614 C ATOM 1869 C ALA A 248 2.956 126.555 79.499 1.00116.23 C ANISOU 1869 C ALA A 248 11441 11841 20879 580 -2080 5316 C ATOM 1870 O ALA A 248 3.387 125.560 80.094 1.00120.29 O ANISOU 1870 O ALA A 248 12095 12539 21071 551 -1928 4983 O ATOM 1871 CB ALA A 248 2.903 126.536 76.991 1.00 91.40 C ANISOU 1871 CB ALA A 248 8442 9079 17205 430 -2461 5945 C ATOM 1872 N LEU A 249 3.240 127.799 79.896 1.00109.71 N ANISOU 1872 N LEU A 249 10523 10717 20445 599 -1983 5324 N ATOM 1873 CA LEU A 249 4.011 128.025 81.114 1.00 99.45 C ANISOU 1873 CA LEU A 249 9264 9212 19310 634 -1755 5013 C ATOM 1874 C LEU A 249 3.250 127.578 82.354 1.00 93.75 C ANISOU 1874 C LEU A 249 8487 8395 18739 748 -1603 4609 C ATOM 1875 O LEU A 249 3.870 127.262 83.376 1.00 86.10 O ANISOU 1875 O LEU A 249 7636 7412 17667 745 -1402 4244 O ATOM 1876 CB LEU A 249 4.390 129.501 81.241 1.00101.30 C ANISOU 1876 CB LEU A 249 9417 9144 19928 615 -1712 5080 C ATOM 1877 CG LEU A 249 5.744 129.937 80.680 1.00103.03 C ANISOU 1877 CG LEU A 249 9733 9402 20011 490 -1707 5288 C ATOM 1878 CD1 LEU A 249 5.712 130.047 79.167 1.00102.30 C ANISOU 1878 CD1 LEU A 249 9651 9544 19674 404 -1876 5715 C ATOM 1879 CD2 LEU A 249 6.167 131.253 81.310 1.00112.72 C ANISOU 1879 CD2 LEU A 249 10881 10281 21666 484 -1626 5188 C ATOM 1880 N THR A 250 1.917 127.552 82.287 1.00 96.46 N ANISOU 1880 N THR A 250 8656 8687 19306 835 -1684 4662 N ATOM 1881 CA THR A 250 1.123 127.118 83.431 1.00 92.65 C ANISOU 1881 CA THR A 250 8096 8108 19000 964 -1517 4331 C ATOM 1882 C THR A 250 1.405 125.659 83.770 1.00 88.70 C ANISOU 1882 C THR A 250 7760 7934 18008 905 -1430 4062 C ATOM 1883 O THR A 250 1.599 125.304 84.939 1.00 81.36 O ANISOU 1883 O THR A 250 6908 6968 17039 951 -1200 3688 O ATOM 1884 CB THR A 250 -0.364 127.325 83.145 1.00 90.60 C ANISOU 1884 CB THR A 250 7623 7814 18988 1005 -1602 4435 C ATOM 1885 OG1 THR A 250 -0.604 128.701 82.823 1.00 92.57 O ANISOU 1885 OG1 THR A 250 7758 7838 19575 997 -1642 4600 O ATOM 1886 CG2 THR A 250 -1.193 126.939 84.357 1.00 88.65 C ANISOU 1886 CG2 THR A 250 7284 7463 18936 1140 -1379 4110 C ATOM 1887 N LYS A 251 1.426 124.794 82.752 1.00 86.95 N ANISOU 1887 N LYS A 251 7613 8035 17391 801 -1616 4242 N ATOM 1888 CA LYS A 251 1.750 123.391 82.977 1.00 86.12 C ANISOU 1888 CA LYS A 251 7676 8240 16807 733 -1549 3996 C ATOM 1889 C LYS A 251 3.193 123.215 83.428 1.00 77.02 C ANISOU 1889 C LYS A 251 6742 7168 15353 655 -1374 3782 C ATOM 1890 O LYS A 251 3.487 122.314 84.221 1.00 74.44 O ANISOU 1890 O LYS A 251 6527 6966 14791 645 -1220 3462 O ATOM 1891 CB LYS A 251 1.488 122.582 81.707 1.00 88.75 C ANISOU 1891 CB LYS A 251 8067 8869 16784 644 -1809 4238 C ATOM 1892 N MET A 252 4.101 124.063 82.943 1.00 81.31 N ANISOU 1892 N MET A 252 7334 7636 15925 597 -1403 3973 N ATOM 1893 CA MET A 252 5.493 123.981 83.375 1.00 84.60 C ANISOU 1893 CA MET A 252 7920 8097 16128 519 -1251 3801 C ATOM 1894 C MET A 252 5.643 124.400 84.830 1.00 90.64 C ANISOU 1894 C MET A 252 8682 8599 17160 589 -1056 3449 C ATOM 1895 O MET A 252 6.344 123.743 85.607 1.00 73.19 O ANISOU 1895 O MET A 252 6615 6484 14712 553 -917 3150 O ATOM 1896 CB MET A 252 6.373 124.855 82.484 1.00 85.28 C ANISOU 1896 CB MET A 252 8021 8139 16243 440 -1328 4133 C ATOM 1897 CG MET A 252 6.427 124.425 81.038 1.00 93.89 C ANISOU 1897 CG MET A 252 9179 9515 16979 370 -1492 4474 C ATOM 1898 SD MET A 252 7.506 125.509 80.093 1.00 96.91 S ANISOU 1898 SD MET A 252 9573 9831 17417 288 -1525 4884 S ATOM 1899 CE MET A 252 8.929 125.552 81.178 1.00 93.56 C ANISOU 1899 CE MET A 252 9225 9316 17007 229 -1292 4578 C ATOM 1900 N ARG A 253 4.997 125.504 85.213 1.00 92.45 N ANISOU 1900 N ARG A 253 8761 8486 17878 695 -1050 3480 N ATOM 1901 CA ARG A 253 5.099 125.987 86.585 1.00 88.42 C ANISOU 1901 CA ARG A 253 8282 7698 17615 780 -868 3134 C ATOM 1902 C ARG A 253 4.537 124.968 87.568 1.00 83.98 C ANISOU 1902 C ARG A 253 7773 7248 16887 853 -706 2787 C ATOM 1903 O ARG A 253 5.101 124.760 88.647 1.00 82.22 O ANISOU 1903 O ARG A 253 7699 6983 16560 859 -550 2450 O ATOM 1904 CB ARG A 253 4.380 127.329 86.719 1.00 95.76 C ANISOU 1904 CB ARG A 253 9040 8234 19112 903 -889 3244 C ATOM 1905 CG ARG A 253 4.837 128.166 87.899 1.00 99.86 C ANISOU 1905 CG ARG A 253 9637 8409 19897 964 -749 2946 C ATOM 1906 CD ARG A 253 3.992 129.418 88.041 1.00106.75 C ANISOU 1906 CD ARG A 253 10337 8880 21343 1112 -753 3033 C ATOM 1907 NE ARG A 253 4.595 130.386 88.953 1.00108.56 N ANISOU 1907 NE ARG A 253 10666 8754 21829 1145 -674 2793 N ATOM 1908 CZ ARG A 253 4.506 130.322 90.278 1.00105.57 C ANISOU 1908 CZ ARG A 253 10423 8222 21468 1254 -482 2369 C ATOM 1909 NH1 ARG A 253 3.841 129.330 90.854 1.00100.09 N ANISOU 1909 NH1 ARG A 253 9763 7723 20545 1335 -321 2153 N ATOM 1910 NH2 ARG A 253 5.085 131.251 91.027 1.00106.94 N ANISOU 1910 NH2 ARG A 253 10720 8114 21799 1251 -450 2138 N ATOM 1911 N ALA A 254 3.426 124.319 87.209 1.00 78.06 N ANISOU 1911 N ALA A 254 6902 6639 16117 902 -754 2878 N ATOM 1912 CA ALA A 254 2.910 123.238 88.039 1.00 74.24 C ANISOU 1912 CA ALA A 254 6454 6292 15460 954 -603 2596 C ATOM 1913 C ALA A 254 3.859 122.046 88.057 1.00 87.61 C ANISOU 1913 C ALA A 254 8352 8304 16631 825 -584 2448 C ATOM 1914 O ALA A 254 3.972 121.361 89.079 1.00 81.37 O ANISOU 1914 O ALA A 254 7667 7568 15681 850 -413 2136 O ATOM 1915 CB ALA A 254 1.528 122.811 87.549 1.00 81.19 C ANISOU 1915 CB ALA A 254 7129 7241 16480 1017 -695 2772 C ATOM 1916 N ALA A 255 4.552 121.789 86.947 1.00 82.83 N ANISOU 1916 N ALA A 255 7809 7906 15755 697 -744 2674 N ATOM 1917 CA ALA A 255 5.507 120.687 86.916 1.00 80.35 C ANISOU 1917 CA ALA A 255 7683 7879 14968 586 -713 2543 C ATOM 1918 C ALA A 255 6.749 121.010 87.736 1.00 89.12 C ANISOU 1918 C ALA A 255 8934 8891 16036 544 -586 2331 C ATOM 1919 O ALA A 255 7.303 120.130 88.406 1.00 93.60 O ANISOU 1919 O ALA A 255 9638 9598 16327 508 -483 2079 O ATOM 1920 CB ALA A 255 5.886 120.360 85.472 1.00 78.00 C ANISOU 1920 CB ALA A 255 7425 7821 14390 482 -894 2847 C ATOM 1921 N ALA A 256 7.199 122.267 87.698 1.00 95.12 N ANISOU 1921 N ALA A 256 9657 9397 17089 543 -613 2438 N ATOM 1922 CA ALA A 256 8.366 122.663 88.479 1.00 92.93 C ANISOU 1922 CA ALA A 256 9499 8985 16826 493 -537 2248 C ATOM 1923 C ALA A 256 8.075 122.647 89.973 1.00 95.85 C ANISOU 1923 C ALA A 256 9946 9185 17289 589 -382 1859 C ATOM 1924 O ALA A 256 8.975 122.376 90.776 1.00 95.53 O ANISOU 1924 O ALA A 256 10059 9147 17090 538 -319 1618 O ATOM 1925 CB ALA A 256 8.843 124.048 88.046 1.00 92.92 C ANISOU 1925 CB ALA A 256 9422 8721 17164 465 -626 2476 C ATOM 1926 N LEU A 257 6.833 122.936 90.367 1.00100.33 N ANISOU 1926 N LEU A 257 10412 9601 18109 733 -315 1803 N ATOM 1927 CA LEU A 257 6.468 122.883 91.777 1.00 95.51 C ANISOU 1927 CA LEU A 257 9892 8843 17552 848 -127 1441 C ATOM 1928 C LEU A 257 6.239 121.455 92.254 1.00 95.59 C ANISOU 1928 C LEU A 257 9983 9135 17201 846 -19 1255 C ATOM 1929 O LEU A 257 6.490 121.152 93.425 1.00 95.62 O ANISOU 1929 O LEU A 257 10146 9105 17078 881 124 942 O ATOM 1930 CB LEU A 257 5.220 123.729 92.030 1.00 91.86 C ANISOU 1930 CB LEU A 257 9277 8105 17519 1023 -54 1462 C ATOM 1931 CG LEU A 257 5.368 125.229 91.771 1.00 90.92 C ANISOU 1931 CG LEU A 257 9085 7639 17821 1052 -141 1602 C ATOM 1932 CD1 LEU A 257 4.014 125.913 91.818 1.00 92.27 C ANISOU 1932 CD1 LEU A 257 9062 7575 18421 1233 -75 1679 C ATOM 1933 CD2 LEU A 257 6.328 125.860 92.767 1.00 92.23 C ANISOU 1933 CD2 LEU A 257 9449 7565 18027 1039 -95 1317 C ATOM 1934 N ASP A 258 5.765 120.570 91.373 1.00 98.75 N ANISOU 1934 N ASP A 258 10288 9801 17431 802 -98 1445 N ATOM 1935 CA ASP A 258 5.608 119.170 91.755 1.00 99.15 C ANISOU 1935 CA ASP A 258 10409 10111 17151 783 -17 1287 C ATOM 1936 C ASP A 258 6.961 118.503 91.962 1.00 94.28 C ANISOU 1936 C ASP A 258 9988 9665 16168 656 -24 1152 C ATOM 1937 O ASP A 258 7.112 117.654 92.848 1.00 96.75 O ANISOU 1937 O ASP A 258 10422 10078 16261 660 93 908 O ATOM 1938 CB ASP A 258 4.802 118.417 90.696 1.00109.22 C ANISOU 1938 CB ASP A 258 11543 11601 18353 757 -144 1524 C ATOM 1939 CG ASP A 258 3.353 118.858 90.639 1.00122.43 C ANISOU 1939 CG ASP A 258 12996 13120 20402 886 -132 1643 C ATOM 1940 OD1 ASP A 258 2.823 119.308 91.676 1.00128.53 O ANISOU 1940 OD1 ASP A 258 13741 13683 21410 1020 60 1465 O ATOM 1941 OD2 ASP A 258 2.744 118.753 89.554 1.00127.48 O ANISOU 1941 OD2 ASP A 258 13493 13844 21101 859 -315 1918 O ATOM 1942 N ALA A 259 7.957 118.876 91.156 1.00103.12 N ANISOU 1942 N ALA A 259 11130 10816 17234 547 -153 1327 N ATOM 1943 CA ALA A 259 9.276 118.266 91.279 1.00112.24 C ANISOU 1943 CA ALA A 259 12435 12125 18086 430 -157 1234 C ATOM 1944 C ALA A 259 9.976 118.684 92.565 1.00115.28 C ANISOU 1944 C ALA A 259 12958 12317 18526 436 -79 952 C ATOM 1945 O ALA A 259 10.806 117.930 93.087 1.00117.71 O ANISOU 1945 O ALA A 259 13398 12750 18576 369 -52 788 O ATOM 1946 CB ALA A 259 10.134 118.622 90.065 1.00 59.52 C ANISOU 1946 CB ALA A 259 5724 5519 11373 324 -285 1525 C ATOM 1947 N GLN A 260 9.664 119.872 93.090 1.00116.83 N ANISOU 1947 N GLN A 260 13136 12198 19055 518 -58 890 N ATOM 1948 CA GLN A 260 10.275 120.309 94.343 1.00117.91 C ANISOU 1948 CA GLN A 260 13440 12127 19233 530 -11 597 C ATOM 1949 C GLN A 260 9.841 119.420 95.502 1.00122.92 C ANISOU 1949 C GLN A 260 14214 12848 19644 606 148 295 C ATOM 1950 O GLN A 260 10.669 118.976 96.305 1.00131.22 O ANISOU 1950 O GLN A 260 15441 13938 20480 550 155 84 O ATOM 1951 CB GLN A 260 9.918 121.768 94.630 1.00117.43 C ANISOU 1951 CB GLN A 260 13345 11688 19584 621 -20 580 C ATOM 1952 CG GLN A 260 10.636 122.782 93.759 1.00116.99 C ANISOU 1952 CG GLN A 260 13192 11485 19775 527 -185 841 C ATOM 1953 CD GLN A 260 10.502 124.199 94.287 1.00118.08 C ANISOU 1953 CD GLN A 260 13341 11204 20319 603 -206 754 C ATOM 1954 OE1 GLN A 260 10.932 125.158 93.646 1.00119.94 O ANISOU 1954 OE1 GLN A 260 13479 11261 20829 544 -335 974 O ATOM 1955 NE2 GLN A 260 9.906 124.336 95.466 1.00115.95 N ANISOU 1955 NE2 GLN A 260 13201 10766 20088 741 -71 434 N ATOM 1956 N LYS A 261 8.538 119.151 95.606 1.00119.97 N ANISOU 1956 N LYS A 261 13751 12500 19331 733 276 291 N ATOM 1957 CA LYS A 261 8.019 118.342 96.701 1.00122.15 C ANISOU 1957 CA LYS A 261 14140 12851 19422 819 461 39 C ATOM 1958 C LYS A 261 8.316 116.857 96.537 1.00129.72 C ANISOU 1958 C LYS A 261 15131 14143 20015 725 453 44 C ATOM 1959 O LYS A 261 8.158 116.103 97.504 1.00131.04 O ANISOU 1959 O LYS A 261 15420 14386 19983 766 589 -163 O ATOM 1960 CB LYS A 261 6.509 118.557 96.836 1.00118.25 C ANISOU 1960 CB LYS A 261 13500 12262 19169 989 618 69 C ATOM 1961 N ALA A 262 8.751 116.421 95.353 1.00135.18 N ANISOU 1961 N ALA A 262 15731 15028 20605 607 305 273 N ATOM 1962 CA ALA A 262 8.968 114.998 95.118 1.00142.10 C ANISOU 1962 CA ALA A 262 16635 16203 21153 530 297 277 C ATOM 1963 C ALA A 262 10.304 114.525 95.679 1.00159.62 C ANISOU 1963 C ALA A 262 19031 18494 23122 432 272 121 C ATOM 1964 O ALA A 262 10.409 113.391 96.158 1.00162.70 O ANISOU 1964 O ALA A 262 19503 19056 23259 412 329 0 O ATOM 1965 CB ALA A 262 8.885 114.694 93.623 1.00137.07 C ANISOU 1965 CB ALA A 262 15863 15740 20478 460 155 565 C ATOM 1966 N THR A 263 11.327 115.367 95.627 1.00178.59 N ANISOU 1966 N THR A 263 21479 20758 25621 366 176 139 N ATOM 1967 CA THR A 263 12.659 114.969 96.072 1.00182.42 C ANISOU 1967 CA THR A 263 22095 21296 25919 260 119 30 C ATOM 1968 C THR A 263 12.664 114.696 97.571 1.00182.90 C ANISOU 1968 C THR A 263 22348 21288 25858 309 205 -279 C ATOM 1969 O THR A 263 12.313 115.589 98.354 1.00193.39 O ANISOU 1969 O THR A 263 23757 22374 27347 394 250 -429 O ATOM 1970 CB THR A 263 13.677 116.054 95.729 1.00185.02 C ANISOU 1970 CB THR A 263 22401 21448 26451 180 -12 136 C ATOM 1971 OG1 THR A 263 13.285 117.291 96.333 1.00188.80 O ANISOU 1971 OG1 THR A 263 22911 21615 27209 257 -9 34 O ATOM 1972 CG2 THR A 263 13.767 116.236 94.220 1.00187.42 C ANISOU 1972 CG2 THR A 263 22537 21854 26821 129 -78 467 C ATOM 1973 N PRO A 264 13.048 113.490 98.018 1.00154.83 N ANISOU 1973 N PRO A 264 18886 17929 22014 266 233 -382 N ATOM 1974 CA PRO A 264 13.092 113.129 99.437 1.00140.01 C ANISOU 1974 CA PRO A 264 17213 16014 19971 307 308 -654 C ATOM 1975 C PRO A 264 14.443 113.428 100.079 1.00132.37 C ANISOU 1975 C PRO A 264 16397 14940 18960 211 164 -777 C ATOM 1976 O PRO A 264 15.423 112.761 99.748 1.00126.30 O ANISOU 1976 O PRO A 264 15604 14315 18070 97 68 -702 O ATOM 1977 CB PRO A 264 12.817 111.621 99.417 1.00132.99 C ANISOU 1977 CB PRO A 264 16313 15398 18821 295 384 -646 C ATOM 1978 CG PRO A 264 13.198 111.159 98.017 1.00133.22 C ANISOU 1978 CG PRO A 264 16181 15604 18831 205 290 -407 C ATOM 1979 CD PRO A 264 13.484 112.374 97.164 1.00142.21 C ANISOU 1979 CD PRO A 264 17216 16600 20220 179 192 -238 C ATOM 1980 N MET A 277 22.549 118.218 96.916 1.00145.54 N ANISOU 1980 N MET A 277 17360 15729 22210 -639 -935 325 N ATOM 1981 CA MET A 277 21.165 118.642 96.745 1.00143.76 C ANISOU 1981 CA MET A 277 17180 15469 21975 -506 -821 277 C ATOM 1982 C MET A 277 20.994 120.111 97.116 1.00149.42 C ANISOU 1982 C MET A 277 17925 15802 23047 -500 -946 218 C ATOM 1983 O MET A 277 19.953 120.711 96.844 1.00152.71 O ANISOU 1983 O MET A 277 18329 16131 23563 -395 -868 237 O ATOM 1984 CB MET A 277 20.228 117.773 97.587 1.00140.65 C ANISOU 1984 CB MET A 277 16980 15210 21252 -393 -711 -10 C ATOM 1985 N LYS A 278 22.023 120.685 97.744 1.00151.80 N ANISOU 1985 N LYS A 278 18260 15857 23560 -613 -1158 147 N ATOM 1986 CA LYS A 278 21.969 122.098 98.108 1.00147.90 C ANISOU 1986 CA LYS A 278 17804 14961 23431 -621 -1309 80 C ATOM 1987 C LYS A 278 21.955 122.985 96.870 1.00146.08 C ANISOU 1987 C LYS A 278 17326 14643 23535 -648 -1290 447 C ATOM 1988 O LYS A 278 21.270 124.014 96.844 1.00145.57 O ANISOU 1988 O LYS A 278 17269 14327 23715 -579 -1305 433 O ATOM 1989 CB LYS A 278 23.148 122.455 99.013 1.00141.87 C ANISOU 1989 CB LYS A 278 17126 13949 22829 -758 -1584 -65 C ATOM 1990 N ASP A 279 22.704 122.606 95.834 1.00145.71 N ANISOU 1990 N ASP A 279 17064 14795 23502 -738 -1245 786 N ATOM 1991 CA ASP A 279 22.689 123.349 94.582 1.00147.20 C ANISOU 1991 CA ASP A 279 17029 14947 23951 -759 -1200 1173 C ATOM 1992 C ASP A 279 21.553 122.929 93.660 1.00147.11 C ANISOU 1992 C ASP A 279 16983 15198 23713 -633 -993 1312 C ATOM 1993 O ASP A 279 21.371 123.549 92.608 1.00145.83 O ANISOU 1993 O ASP A 279 16664 15017 23728 -631 -956 1633 O ATOM 1994 CB ASP A 279 24.027 123.189 93.856 1.00146.21 C ANISOU 1994 CB ASP A 279 16695 14911 23949 -903 -1220 1500 C ATOM 1995 N PHE A 280 20.788 121.901 94.024 1.00148.44 N ANISOU 1995 N PHE A 280 17290 15603 23508 -533 -874 1093 N ATOM 1996 CA PHE A 280 19.658 121.454 93.219 1.00145.21 C ANISOU 1996 CA PHE A 280 16850 15426 22898 -421 -716 1204 C ATOM 1997 C PHE A 280 18.322 121.984 93.715 1.00144.12 C ANISOU 1997 C PHE A 280 16794 15120 22844 -284 -688 1020 C ATOM 1998 O PHE A 280 17.401 122.157 92.910 1.00150.55 O ANISOU 1998 O PHE A 280 17520 15998 23683 -206 -620 1198 O ATOM 1999 CB PHE A 280 19.607 119.923 93.178 1.00141.32 C ANISOU 1999 CB PHE A 280 16424 15301 21971 -400 -597 1120 C ATOM 2000 N ARG A 281 18.191 122.241 95.018 1.00135.31 N ANISOU 2000 N ARG A 281 15851 13790 21770 -245 -739 674 N ATOM 2001 CA ARG A 281 16.955 122.822 95.532 1.00125.07 C ANISOU 2001 CA ARG A 281 14631 12305 20585 -95 -679 497 C ATOM 2002 C ARG A 281 16.810 124.275 95.097 1.00125.21 C ANISOU 2002 C ARG A 281 14534 11993 21048 -88 -767 667 C ATOM 2003 O ARG A 281 15.716 124.709 94.716 1.00126.92 O ANISOU 2003 O ARG A 281 14679 12150 21396 30 -692 748 O ATOM 2004 CB ARG A 281 16.915 122.708 97.056 1.00117.15 C ANISOU 2004 CB ARG A 281 13879 11161 19470 -45 -689 75 C ATOM 2005 N HIS A 282 17.903 125.041 95.143 1.00121.43 N ANISOU 2005 N HIS A 282 14019 11282 20836 -215 -937 741 N ATOM 2006 CA HIS A 282 17.885 126.422 94.677 1.00118.04 C ANISOU 2006 CA HIS A 282 13463 10525 20863 -228 -1037 939 C ATOM 2007 C HIS A 282 17.805 126.527 93.160 1.00117.32 C ANISOU 2007 C HIS A 282 13135 10600 20842 -260 -992 1402 C ATOM 2008 O HIS A 282 17.546 127.620 92.646 1.00122.89 O ANISOU 2008 O HIS A 282 13720 11064 21910 -247 -1049 1611 O ATOM 2009 CB HIS A 282 19.124 127.164 95.181 1.00118.12 C ANISOU 2009 CB HIS A 282 13492 10228 21159 -374 -1254 894 C ATOM 2010 N GLY A 283 18.028 125.428 92.436 1.00113.48 N ANISOU 2010 N GLY A 283 12597 10508 20012 -297 -894 1567 N ATOM 2011 CA GLY A 283 17.862 125.455 90.994 1.00111.46 C ANISOU 2011 CA GLY A 283 12168 10436 19747 -307 -841 1987 C ATOM 2012 C GLY A 283 16.411 125.546 90.572 1.00111.89 C ANISOU 2012 C GLY A 283 12196 10532 19786 -165 -775 2039 C ATOM 2013 O GLY A 283 16.096 126.160 89.548 1.00114.27 O ANISOU 2013 O GLY A 283 12357 10805 20256 -157 -798 2378 O ATOM 2014 N PHE A 284 15.509 124.938 91.345 1.00107.08 N ANISOU 2014 N PHE A 284 11709 9987 18991 -51 -694 1726 N ATOM 2015 CA PHE A 284 14.086 125.094 91.069 1.00102.99 C ANISOU 2015 CA PHE A 284 11137 9460 18534 91 -639 1766 C ATOM 2016 C PHE A 284 13.587 126.475 91.468 1.00101.19 C ANISOU 2016 C PHE A 284 10871 8810 18767 169 -693 1727 C ATOM 2017 O PHE A 284 12.619 126.973 90.883 1.00 99.42 O ANISOU 2017 O PHE A 284 10525 8517 18735 259 -691 1912 O ATOM 2018 CB PHE A 284 13.284 124.011 91.787 1.00104.45 C ANISOU 2018 CB PHE A 284 11438 9835 18415 188 -515 1469 C ATOM 2019 CG PHE A 284 13.304 122.682 91.091 1.00108.50 C ANISOU 2019 CG PHE A 284 11947 10760 18520 149 -464 1574 C ATOM 2020 CD1 PHE A 284 12.609 122.495 89.908 1.00111.32 C ANISOU 2020 CD1 PHE A 284 12188 11290 18818 174 -480 1863 C ATOM 2021 CD2 PHE A 284 14.011 121.616 91.623 1.00109.11 C ANISOU 2021 CD2 PHE A 284 12147 11036 18275 89 -419 1378 C ATOM 2022 CE1 PHE A 284 12.623 121.272 89.264 1.00112.73 C ANISOU 2022 CE1 PHE A 284 12392 11827 18613 140 -451 1934 C ATOM 2023 CE2 PHE A 284 14.029 120.390 90.985 1.00108.81 C ANISOU 2023 CE2 PHE A 284 12113 11351 17877 61 -374 1459 C ATOM 2024 CZ PHE A 284 13.334 120.218 89.803 1.00109.92 C ANISOU 2024 CZ PHE A 284 12157 11655 17953 87 -389 1726 C ATOM 2025 N ASP A 285 14.220 127.103 92.462 1.00100.52 N ANISOU 2025 N ASP A 285 10895 8427 18873 141 -757 1483 N ATOM 2026 CA ASP A 285 13.916 128.499 92.760 1.00 92.83 C ANISOU 2026 CA ASP A 285 9891 7013 18367 202 -830 1459 C ATOM 2027 C ASP A 285 14.187 129.376 91.548 1.00 79.34 C ANISOU 2027 C ASP A 285 7972 5203 16971 127 -937 1911 C ATOM 2028 O ASP A 285 13.356 130.208 91.166 1.00121.47 O ANISOU 2028 O ASP A 285 13195 10339 22619 220 -951 2063 O ATOM 2029 CB ASP A 285 14.736 128.977 93.959 1.00 90.52 C ANISOU 2029 CB ASP A 285 9777 6421 18198 153 -927 1129 C ATOM 2030 CG ASP A 285 14.153 128.530 95.278 1.00109.81 C ANISOU 2030 CG ASP A 285 12453 8836 20433 285 -814 668 C ATOM 2031 OD1 ASP A 285 13.184 127.741 95.263 1.00116.73 O ANISOU 2031 OD1 ASP A 285 13330 9954 21070 400 -644 620 O ATOM 2032 OD2 ASP A 285 14.658 128.973 96.331 1.00121.25 O ANISOU 2032 OD2 ASP A 285 14092 10016 21963 272 -900 362 O ATOM 2033 N ILE A 286 15.354 129.198 90.926 1.00 78.87 N ANISOU 2033 N ILE A 286 7847 5278 16840 -38 -1003 2150 N ATOM 2034 CA ILE A 286 15.669 129.942 89.713 1.00 95.65 C ANISOU 2034 CA ILE A 286 9777 7351 19216 -113 -1076 2622 C ATOM 2035 C ILE A 286 14.778 129.491 88.565 1.00 90.92 C ANISOU 2035 C ILE A 286 9081 7047 18415 -47 -1005 2917 C ATOM 2036 O ILE A 286 14.429 130.291 87.688 1.00 94.17 O ANISOU 2036 O ILE A 286 9348 7348 19083 -34 -1063 3266 O ATOM 2037 CB ILE A 286 17.161 129.784 89.368 1.00 80.63 C ANISOU 2037 CB ILE A 286 7825 5538 17275 -296 -1123 2809 C ATOM 2038 CG1 ILE A 286 18.025 130.107 90.589 1.00 81.38 C ANISOU 2038 CG1 ILE A 286 8026 5347 17546 -372 -1236 2485 C ATOM 2039 CG2 ILE A 286 17.537 130.677 88.196 1.00 83.18 C ANISOU 2039 CG2 ILE A 286 7945 5763 17897 -373 -1182 3311 C ATOM 2040 CD1 ILE A 286 19.506 129.904 90.362 1.00 81.38 C ANISOU 2040 CD1 ILE A 286 7951 5419 17552 -553 -1291 2656 C ATOM 2041 N LEU A 287 14.389 128.215 88.550 1.00 91.66 N ANISOU 2041 N LEU A 287 9260 7508 18059 -6 -900 2789 N ATOM 2042 CA LEU A 287 13.529 127.717 87.482 1.00 90.90 C ANISOU 2042 CA LEU A 287 9095 7690 17754 49 -872 3044 C ATOM 2043 C LEU A 287 12.139 128.337 87.564 1.00 93.33 C ANISOU 2043 C LEU A 287 9327 7795 18339 197 -893 3037 C ATOM 2044 O LEU A 287 11.628 128.873 86.574 1.00 83.43 O ANISOU 2044 O LEU A 287 7940 6520 17241 217 -967 3391 O ATOM 2045 CB LEU A 287 13.450 126.192 87.545 1.00 81.11 C ANISOU 2045 CB LEU A 287 7968 6848 16001 52 -774 2872 C ATOM 2046 CG LEU A 287 12.714 125.496 86.400 1.00 72.72 C ANISOU 2046 CG LEU A 287 6870 6105 14656 84 -776 3117 C ATOM 2047 CD1 LEU A 287 13.367 125.822 85.065 1.00 79.43 C ANISOU 2047 CD1 LEU A 287 7648 7064 15467 -4 -824 3564 C ATOM 2048 CD2 LEU A 287 12.677 123.995 86.630 1.00 74.08 C ANISOU 2048 CD2 LEU A 287 7166 6617 14364 85 -690 2893 C ATOM 2049 N VAL A 288 11.515 128.282 88.743 1.00101.69 N ANISOU 2049 N VAL A 288 10468 8701 19467 308 -822 2649 N ATOM 2050 CA VAL A 288 10.185 128.863 88.912 1.00 79.60 C ANISOU 2050 CA VAL A 288 7583 5694 16968 469 -806 2626 C ATOM 2051 C VAL A 288 10.235 130.375 88.729 1.00101.45 C ANISOU 2051 C VAL A 288 10237 8047 20262 483 -909 2810 C ATOM 2052 O VAL A 288 9.340 130.971 88.115 1.00 85.08 O ANISOU 2052 O VAL A 288 8008 5861 18457 566 -959 3056 O ATOM 2053 CB VAL A 288 9.606 128.472 90.286 1.00 78.76 C ANISOU 2053 CB VAL A 288 7608 5510 16806 596 -662 2162 C ATOM 2054 CG1 VAL A 288 8.319 129.231 90.563 1.00 83.91 C ANISOU 2054 CG1 VAL A 288 8156 5881 17843 780 -612 2129 C ATOM 2055 CG2 VAL A 288 9.362 126.972 90.348 1.00 88.19 C ANISOU 2055 CG2 VAL A 288 8876 7109 17523 592 -567 2040 C ATOM 2056 N GLY A 289 11.284 131.017 89.246 1.00 98.77 N ANISOU 2056 N GLY A 289 9964 7463 20101 395 -963 2708 N ATOM 2057 CA GLY A 289 11.398 132.460 89.109 1.00 87.59 C ANISOU 2057 CA GLY A 289 8444 5647 19189 391 -1073 2862 C ATOM 2058 C GLY A 289 11.511 132.907 87.665 1.00105.79 C ANISOU 2058 C GLY A 289 10562 8094 21540 302 -1166 3369 C ATOM 2059 O GLY A 289 10.977 133.952 87.284 1.00110.27 O ANISOU 2059 O GLY A 289 10994 8522 22381 336 -1221 3514 O ATOM 2060 N GLN A 290 12.211 132.123 86.840 1.00 99.70 N ANISOU 2060 N GLN A 290 9790 7607 20484 192 -1174 3647 N ATOM 2061 CA GLN A 290 12.303 132.451 85.422 1.00104.65 C ANISOU 2061 CA GLN A 290 10276 8414 21072 120 -1238 4132 C ATOM 2062 C GLN A 290 10.978 132.224 84.708 1.00105.65 C ANISOU 2062 C GLN A 290 10329 8690 21125 230 -1260 4310 C ATOM 2063 O GLN A 290 10.688 132.899 83.713 1.00106.26 O ANISOU 2063 O GLN A 290 10276 8809 21288 206 -1341 4647 O ATOM 2064 CB GLN A 290 13.414 131.636 84.762 1.00109.02 C ANISOU 2064 CB GLN A 290 10876 9256 21290 -13 -1204 4357 C ATOM 2065 CG GLN A 290 14.815 132.147 85.054 1.00118.34 C ANISOU 2065 CG GLN A 290 12040 10308 22617 -158 -1219 4346 C ATOM 2066 CD GLN A 290 15.895 131.186 84.595 1.00121.61 C ANISOU 2066 CD GLN A 290 12502 11034 22670 -272 -1136 4488 C ATOM 2067 OE1 GLN A 290 16.036 130.091 85.138 1.00118.48 O ANISOU 2067 OE1 GLN A 290 12236 10874 21905 -266 -1052 4178 O ATOM 2068 NE2 GLN A 290 16.661 131.590 83.588 1.00124.88 N ANISOU 2068 NE2 GLN A 290 12804 11549 23094 -370 -1129 4890 N ATOM 2069 N ILE A 291 10.165 131.283 85.194 1.00107.84 N ANISOU 2069 N ILE A 291 10678 9082 21216 340 -1194 4073 N ATOM 2070 CA ILE A 291 8.831 131.098 84.633 1.00110.38 C ANISOU 2070 CA ILE A 291 10902 9500 21539 450 -1240 4224 C ATOM 2071 C ILE A 291 7.936 132.275 84.998 1.00110.76 C ANISOU 2071 C ILE A 291 10820 9251 22013 544 -1253 4138 C ATOM 2072 O ILE A 291 7.144 132.750 84.175 1.00116.31 O ANISOU 2072 O ILE A 291 11380 9988 22823 562 -1343 4403 O ATOM 2073 CB ILE A 291 8.234 129.758 85.103 1.00 84.36 C ANISOU 2073 CB ILE A 291 7702 6500 17851 507 -1141 3918 C ATOM 2074 CG1 ILE A 291 9.116 128.593 84.649 1.00 81.66 C ANISOU 2074 CG1 ILE A 291 7497 6570 16959 381 -1108 3932 C ATOM 2075 CG2 ILE A 291 6.821 129.582 84.570 1.00 85.27 C ANISOU 2075 CG2 ILE A 291 7688 6682 18027 615 -1213 4076 C ATOM 2076 CD1 ILE A 291 8.665 127.243 85.165 1.00 78.70 C ANISOU 2076 CD1 ILE A 291 7226 6469 16208 421 -1014 3620 C ATOM 2077 N ASP A 292 8.058 132.773 86.232 1.00109.62 N ANISOU 2077 N ASP A 292 10738 8815 22097 601 -1164 3759 N ATOM 2078 CA ASP A 292 7.269 133.929 86.649 1.00112.85 C ANISOU 2078 CA ASP A 292 11047 8934 22897 698 -1152 3648 C ATOM 2079 C ASP A 292 7.632 135.168 85.840 1.00119.48 C ANISOU 2079 C ASP A 292 11752 9657 23987 600 -1281 3963 C ATOM 2080 O ASP A 292 6.764 135.993 85.532 1.00127.15 O ANISOU 2080 O ASP A 292 12574 10504 25233 661 -1322 4083 O ATOM 2081 CB ASP A 292 7.466 134.190 88.142 1.00113.95 C ANISOU 2081 CB ASP A 292 11336 8800 23160 775 -1032 3161 C ATOM 2082 CG ASP A 292 6.931 133.066 89.006 1.00115.34 C ANISOU 2082 CG ASP A 292 11632 9073 23120 898 -875 2839 C ATOM 2083 OD1 ASP A 292 5.910 132.457 88.623 1.00116.97 O ANISOU 2083 OD1 ASP A 292 11736 9454 23252 982 -841 2947 O ATOM 2084 OD2 ASP A 292 7.529 132.793 90.068 1.00116.58 O ANISOU 2084 OD2 ASP A 292 11982 9133 23181 906 -794 2480 O ATOM 2085 N ASP A 293 8.912 135.319 85.490 1.00121.58 N ANISOU 2085 N ASP A 293 12054 9960 24178 448 -1340 4110 N ATOM 2086 CA ASP A 293 9.324 136.458 84.675 1.00130.10 C ANISOU 2086 CA ASP A 293 12992 10952 25487 351 -1452 4436 C ATOM 2087 C ASP A 293 8.712 136.382 83.282 1.00129.32 C ANISOU 2087 C ASP A 293 12766 11093 25275 333 -1535 4880 C ATOM 2088 O ASP A 293 8.153 137.365 82.784 1.00141.11 O ANISOU 2088 O ASP A 293 14107 12462 27046 347 -1614 5077 O ATOM 2089 CB ASP A 293 10.849 136.525 84.596 1.00137.15 C ANISOU 2089 CB ASP A 293 13933 11867 26310 192 -1476 4510 C ATOM 2090 CG ASP A 293 11.485 136.914 85.916 1.00142.04 C ANISOU 2090 CG ASP A 293 14662 12195 27112 187 -1460 4097 C ATOM 2091 OD1 ASP A 293 10.864 137.692 86.671 1.00145.43 O ANISOU 2091 OD1 ASP A 293 15093 12335 27829 289 -1458 3844 O ATOM 2092 OD2 ASP A 293 12.607 136.443 86.198 1.00141.32 O ANISOU 2092 OD2 ASP A 293 14664 12165 26867 81 -1454 4023 O ATOM 2093 N ALA A 294 8.806 135.217 82.638 1.00119.13 N ANISOU 2093 N ALA A 294 11552 10147 23567 301 -1529 5038 N ATOM 2094 CA ALA A 294 8.157 135.037 81.346 1.00119.52 C ANISOU 2094 CA ALA A 294 11528 10442 23443 290 -1629 5423 C ATOM 2095 C ALA A 294 6.640 135.002 81.471 1.00123.42 C ANISOU 2095 C ALA A 294 11932 10889 24074 420 -1665 5347 C ATOM 2096 O ALA A 294 5.943 135.225 80.474 1.00124.58 O ANISOU 2096 O ALA A 294 11978 11143 24212 412 -1788 5655 O ATOM 2097 CB ALA A 294 8.661 133.761 80.673 1.00115.27 C ANISOU 2097 CB ALA A 294 11127 10283 22386 231 -1617 5577 C ATOM 2098 N LEU A 295 6.116 134.728 82.668 1.00121.17 N ANISOU 2098 N LEU A 295 11679 10449 23911 539 -1554 4948 N ATOM 2099 CA LEU A 295 4.672 134.782 82.875 1.00117.12 C ANISOU 2099 CA LEU A 295 11049 9867 23585 668 -1552 4869 C ATOM 2100 C LEU A 295 4.159 136.212 82.765 1.00104.43 C ANISOU 2100 C LEU A 295 9269 7979 22430 695 -1602 4969 C ATOM 2101 O LEU A 295 3.066 136.446 82.236 1.00106.47 O ANISOU 2101 O LEU A 295 9378 8250 22828 739 -1682 5145 O ATOM 2102 CB LEU A 295 4.315 134.182 84.235 1.00108.36 C ANISOU 2102 CB LEU A 295 10023 8660 22488 798 -1376 4413 C ATOM 2103 CG LEU A 295 2.956 133.494 84.350 1.00 97.77 C ANISOU 2103 CG LEU A 295 8597 7420 21131 916 -1343 4348 C ATOM 2104 CD1 LEU A 295 2.866 132.342 83.364 1.00 95.84 C ANISOU 2104 CD1 LEU A 295 8379 7546 20488 849 -1472 4598 C ATOM 2105 CD2 LEU A 295 2.723 133.006 85.772 1.00 96.06 C ANISOU 2105 CD2 LEU A 295 8475 7094 20931 1049 -1126 3889 C ATOM 2106 N LYS A 296 4.933 137.181 83.261 1.00105.90 N ANISOU 2106 N LYS A 296 9471 7904 22864 663 -1570 4860 N ATOM 2107 CA LYS A 296 4.577 138.582 83.061 1.00118.82 C ANISOU 2107 CA LYS A 296 10943 9274 24930 675 -1636 4990 C ATOM 2108 C LYS A 296 4.766 138.995 81.608 1.00117.53 C ANISOU 2108 C LYS A 296 10669 9262 24725 553 -1805 5489 C ATOM 2109 O LYS A 296 3.972 139.775 81.070 1.00115.40 O ANISOU 2109 O LYS A 296 10231 8895 24723 575 -1897 5702 O ATOM 2110 CB LYS A 296 5.404 139.483 83.978 1.00111.30 C ANISOU 2110 CB LYS A 296 10051 8001 24238 666 -1583 4731 C ATOM 2111 CG LYS A 296 4.721 139.843 85.288 1.00125.00 C ANISOU 2111 CG LYS A 296 11825 9444 26225 831 -1444 4298 C ATOM 2112 CD LYS A 296 5.223 141.178 85.824 1.00128.73 C ANISOU 2112 CD LYS A 296 12295 9550 27067 824 -1469 4167 C ATOM 2113 CE LYS A 296 6.728 141.169 86.040 1.00126.42 C ANISOU 2113 CE LYS A 296 12136 9245 26653 684 -1517 4104 C ATOM 2114 NZ LYS A 296 7.222 142.490 86.519 1.00121.71 N ANISOU 2114 NZ LYS A 296 11528 8285 26430 665 -1579 3990 N ATOM 2115 N LEU A 297 5.815 138.489 80.956 1.00115.28 N ANISOU 2115 N LEU A 297 10481 9216 24104 427 -1838 5687 N ATOM 2116 CA LEU A 297 6.020 138.806 79.547 1.00125.59 C ANISOU 2116 CA LEU A 297 11717 10701 25302 322 -1971 6165 C ATOM 2117 C LEU A 297 4.945 138.175 78.672 1.00134.68 C ANISOU 2117 C LEU A 297 12840 12099 26232 351 -2080 6382 C ATOM 2118 O LEU A 297 4.614 138.718 77.613 1.00115.81 O ANISOU 2118 O LEU A 297 10354 9765 23882 306 -2218 6746 O ATOM 2119 CB LEU A 297 7.409 138.350 79.099 1.00123.80 C ANISOU 2119 CB LEU A 297 11614 10687 24738 196 -1938 6310 C ATOM 2120 N ALA A 298 4.387 137.038 79.098 1.00131.39 N ANISOU 2120 N ALA A 298 12508 11826 25587 423 -2035 6167 N ATOM 2121 CA ALA A 298 3.328 136.398 78.324 1.00129.73 C ANISOU 2121 CA ALA A 298 12269 11840 25184 445 -2167 6347 C ATOM 2122 C ALA A 298 2.006 137.145 78.449 1.00133.86 C ANISOU 2122 C ALA A 298 12583 12143 26137 530 -2227 6352 C ATOM 2123 O ALA A 298 1.215 137.165 77.499 1.00138.52 O ANISOU 2123 O ALA A 298 13091 12850 26691 507 -2400 6637 O ATOM 2124 CB ALA A 298 3.159 134.944 78.764 1.00129.02 C ANISOU 2124 CB ALA A 298 12314 11964 24745 491 -2107 6114 C ATOM 2125 N ASN A 299 1.749 137.763 79.604 1.00136.34 N ANISOU 2125 N ASN A 299 12819 12137 26848 629 -2086 6040 N ATOM 2126 CA ASN A 299 0.504 138.489 79.813 1.00143.54 C ANISOU 2126 CA ASN A 299 13527 12821 28189 725 -2101 6026 C ATOM 2127 C ASN A 299 0.513 139.869 79.170 1.00143.68 C ANISOU 2127 C ASN A 299 13392 12649 28550 675 -2216 6316 C ATOM 2128 O ASN A 299 -0.556 140.471 79.014 1.00147.58 O ANISOU 2128 O ASN A 299 13698 12997 29378 731 -2277 6415 O ATOM 2129 CB ASN A 299 0.215 138.618 81.312 1.00148.67 C ANISOU 2129 CB ASN A 299 14182 13208 29099 869 -1878 5568 C ATOM 2130 CG ASN A 299 0.109 137.273 82.003 1.00147.74 C ANISOU 2130 CG ASN A 299 14197 13266 28673 930 -1752 5280 C ATOM 2131 OD1 ASN A 299 -0.120 136.247 81.362 1.00145.03 O ANISOU 2131 OD1 ASN A 299 13889 13220 27997 884 -1849 5424 O ATOM 2132 ND2 ASN A 299 0.272 137.271 83.321 1.00148.67 N ANISOU 2132 ND2 ASN A 299 14402 13198 28889 1034 -1540 4865 N ATOM 2133 N GLU A 300 1.684 140.383 78.792 1.00139.91 N ANISOU 2133 N GLU A 300 12976 12165 28018 571 -2242 6467 N ATOM 2134 CA GLU A 300 1.793 141.680 78.139 1.00147.11 C ANISOU 2134 CA GLU A 300 13740 12908 29246 514 -2352 6766 C ATOM 2135 C GLU A 300 1.853 141.559 76.619 1.00150.82 C ANISOU 2135 C GLU A 300 14210 13658 29438 401 -2541 7244 C ATOM 2136 O GLU A 300 2.244 142.516 75.942 1.00156.24 O ANISOU 2136 O GLU A 300 14813 14268 30286 329 -2625 7540 O ATOM 2137 CB GLU A 300 3.018 142.433 78.661 1.00151.88 C ANISOU 2137 CB GLU A 300 14387 13307 30013 466 -2271 6653 C ATOM 2138 CG GLU A 300 2.982 142.709 80.153 1.00153.42 C ANISOU 2138 CG GLU A 300 14615 13194 30485 579 -2108 6174 C ATOM 2139 CD GLU A 300 4.256 143.363 80.656 1.00152.32 C ANISOU 2139 CD GLU A 300 14542 12864 30471 514 -2068 6051 C ATOM 2140 OE1 GLU A 300 5.059 143.822 79.817 1.00152.99 O ANISOU 2140 OE1 GLU A 300 14582 13010 30535 386 -2162 6376 O ATOM 2141 OE2 GLU A 300 4.456 143.417 81.889 1.00149.19 O ANISOU 2141 OE2 GLU A 300 14244 12256 30186 589 -1946 5631 O ATOM 2142 N GLY A 301 1.475 140.405 76.072 1.00148.32 N ANISOU 2142 N GLY A 301 13997 13661 28696 389 -2613 7323 N ATOM 2143 CA GLY A 301 1.486 140.205 74.634 1.00150.20 C ANISOU 2143 CA GLY A 301 14286 14181 28602 295 -2799 7746 C ATOM 2144 C GLY A 301 2.854 140.121 74.002 1.00151.20 C ANISOU 2144 C GLY A 301 14569 14498 28382 188 -2764 7943 C ATOM 2145 O GLY A 301 2.964 140.229 72.776 1.00151.66 O ANISOU 2145 O GLY A 301 14670 14750 28203 116 -2896 8324 O ATOM 2146 N LYS A 302 3.904 139.933 74.801 1.00149.85 N ANISOU 2146 N LYS A 302 14487 14279 28171 178 -2585 7699 N ATOM 2147 CA LYS A 302 5.268 139.844 74.286 1.00147.57 C ANISOU 2147 CA LYS A 302 14322 14158 27588 77 -2519 7875 C ATOM 2148 C LYS A 302 5.501 138.421 73.785 1.00138.95 C ANISOU 2148 C LYS A 302 13459 13461 25874 57 -2510 7901 C ATOM 2149 O LYS A 302 6.142 137.591 74.433 1.00129.00 O ANISOU 2149 O LYS A 302 12328 12284 24402 62 -2374 7651 O ATOM 2150 CB LYS A 302 6.273 140.246 75.359 1.00146.99 C ANISOU 2150 CB LYS A 302 14235 13852 27762 65 -2357 7603 C ATOM 2151 N VAL A 303 4.976 138.148 72.588 1.00141.87 N ANISOU 2151 N VAL A 303 13892 14074 25939 35 -2671 8212 N ATOM 2152 CA VAL A 303 5.082 136.809 72.011 1.00139.94 C ANISOU 2152 CA VAL A 303 13886 14206 25078 23 -2695 8241 C ATOM 2153 C VAL A 303 6.543 136.449 71.773 1.00143.98 C ANISOU 2153 C VAL A 303 14563 14905 25236 -42 -2523 8311 C ATOM 2154 O VAL A 303 6.994 135.347 72.106 1.00142.58 O ANISOU 2154 O VAL A 303 14550 14911 24715 -34 -2420 8118 O ATOM 2155 CB VAL A 303 4.262 136.713 70.712 1.00141.66 C ANISOU 2155 CB VAL A 303 14162 14626 25037 7 -2929 8568 C ATOM 2156 CG1 VAL A 303 4.038 135.256 70.337 1.00135.69 C ANISOU 2156 CG1 VAL A 303 13644 14208 23704 18 -2997 8496 C ATOM 2157 CG2 VAL A 303 2.945 137.455 70.855 1.00147.21 C ANISOU 2157 CG2 VAL A 303 14633 15082 26219 51 -3094 8585 C ATOM 2158 N LYS A 304 7.307 137.377 71.197 1.00152.30 N ANISOU 2158 N LYS A 304 15562 15914 26393 -108 -2479 8595 N ATOM 2159 CA LYS A 304 8.709 137.105 70.912 1.00145.01 C ANISOU 2159 CA LYS A 304 14763 15165 25170 -170 -2295 8696 C ATOM 2160 C LYS A 304 9.594 137.323 72.132 1.00137.64 C ANISOU 2160 C LYS A 304 13736 14002 24558 -188 -2122 8409 C ATOM 2161 O LYS A 304 10.637 136.672 72.256 1.00135.62 O ANISOU 2161 O LYS A 304 13597 13901 24032 -223 -1958 8350 O ATOM 2162 CB LYS A 304 9.188 137.978 69.752 1.00146.92 C ANISOU 2162 CB LYS A 304 14978 15466 25379 -231 -2307 9138 C ATOM 2163 N GLU A 305 9.198 138.220 73.039 1.00134.71 N ANISOU 2163 N GLU A 305 13167 13262 24754 -162 -2159 8220 N ATOM 2164 CA GLU A 305 10.001 138.495 74.224 1.00130.17 C ANISOU 2164 CA GLU A 305 12527 12442 24489 -178 -2031 7923 C ATOM 2165 C GLU A 305 9.776 137.481 75.338 1.00126.13 C ANISOU 2165 C GLU A 305 12120 11923 23882 -114 -1965 7490 C ATOM 2166 O GLU A 305 10.601 137.399 76.254 1.00124.82 O ANISOU 2166 O GLU A 305 11970 11632 23824 -136 -1852 7238 O ATOM 2167 CB GLU A 305 9.711 139.905 74.743 1.00133.22 C ANISOU 2167 CB GLU A 305 12692 12426 25498 -169 -2098 7878 C ATOM 2168 N ALA A 306 8.685 136.717 75.288 1.00127.42 N ANISOU 2168 N ALA A 306 12349 12210 23855 -37 -2044 7401 N ATOM 2169 CA ALA A 306 8.493 135.622 76.231 1.00107.55 C ANISOU 2169 CA ALA A 306 9941 9734 21189 26 -1973 7027 C ATOM 2170 C ALA A 306 9.000 134.294 75.687 1.00124.11 C ANISOU 2170 C ALA A 306 12250 12214 22694 -4 -1921 7095 C ATOM 2171 O ALA A 306 9.443 133.443 76.468 1.00119.20 O ANISOU 2171 O ALA A 306 11728 11631 21933 9 -1810 6822 O ATOM 2172 CB ALA A 306 7.015 135.489 76.611 1.00107.44 C ANISOU 2172 CB ALA A 306 9856 9625 21342 134 -2071 6860 C ATOM 2173 N GLN A 307 8.940 134.095 74.367 1.00125.30 N ANISOU 2173 N GLN A 307 12485 12644 22478 -39 -1999 7445 N ATOM 2174 CA GLN A 307 9.540 132.906 73.771 1.00123.98 C ANISOU 2174 CA GLN A 307 12545 12846 21718 -65 -1929 7520 C ATOM 2175 C GLN A 307 11.051 132.902 73.963 1.00124.25 C ANISOU 2175 C GLN A 307 12613 12906 21692 -137 -1718 7531 C ATOM 2176 O GLN A 307 11.661 131.842 74.149 1.00121.48 O ANISOU 2176 O GLN A 307 12412 12750 20994 -144 -1597 7410 O ATOM 2177 CB GLN A 307 9.193 132.825 72.283 1.00130.81 C ANISOU 2177 CB GLN A 307 13521 13985 22194 -81 -2055 7888 C ATOM 2178 CG GLN A 307 7.805 132.279 71.978 1.00138.14 C ANISOU 2178 CG GLN A 307 14493 15009 22985 -22 -2277 7856 C ATOM 2179 CD GLN A 307 7.462 132.362 70.501 1.00147.14 C ANISOU 2179 CD GLN A 307 15754 16378 23775 -46 -2437 8219 C ATOM 2180 OE1 GLN A 307 8.029 133.170 69.765 1.00152.95 O ANISOU 2180 OE1 GLN A 307 16476 17119 24518 -93 -2395 8517 O ATOM 2181 NE2 GLN A 307 6.531 131.523 70.060 1.00148.30 N ANISOU 2181 NE2 GLN A 307 16026 16711 23612 -14 -2629 8193 N ATOM 2182 N ALA A 308 11.673 134.084 73.920 1.00127.59 N ANISOU 2182 N ALA A 308 12881 13129 22468 -194 -1678 7678 N ATOM 2183 CA ALA A 308 13.116 134.172 74.115 1.00125.24 C ANISOU 2183 CA ALA A 308 12571 12831 22182 -271 -1493 7699 C ATOM 2184 C ALA A 308 13.491 133.958 75.576 1.00125.68 C ANISOU 2184 C ALA A 308 12593 12661 22500 -271 -1426 7288 C ATOM 2185 O ALA A 308 14.493 133.298 75.874 1.00130.52 O ANISOU 2185 O ALA A 308 13280 13380 22933 -315 -1280 7198 O ATOM 2186 CB ALA A 308 13.629 135.523 73.620 1.00128.94 C ANISOU 2186 CB ALA A 308 12864 13145 22981 -334 -1497 7989 C ATOM 2187 N ALA A 309 12.701 134.510 76.501 1.00132.18 N ANISOU 2187 N ALA A 309 13312 13168 23742 -217 -1525 7029 N ATOM 2188 CA ALA A 309 12.966 134.295 77.919 1.00132.63 C ANISOU 2188 CA ALA A 309 13379 13004 24012 -202 -1470 6607 C ATOM 2189 C ALA A 309 12.803 132.830 78.298 1.00126.01 C ANISOU 2189 C ALA A 309 12717 12374 22788 -155 -1408 6389 C ATOM 2190 O ALA A 309 13.444 132.357 79.244 1.00122.38 O ANISOU 2190 O ALA A 309 12315 11841 22343 -175 -1320 6109 O ATOM 2191 CB ALA A 309 12.047 135.173 78.768 1.00101.72 C ANISOU 2191 CB ALA A 309 9347 8727 20576 -127 -1565 6368 C ATOM 2192 N ALA A 310 11.954 132.098 77.572 1.00120.79 N ANISOU 2192 N ALA A 310 12144 11968 21783 -99 -1473 6511 N ATOM 2193 CA ALA A 310 11.805 130.667 77.806 1.00124.94 C ANISOU 2193 CA ALA A 310 12836 12719 21918 -57 -1432 6340 C ATOM 2194 C ALA A 310 13.030 129.880 77.362 1.00131.57 C ANISOU 2194 C ALA A 310 13808 13833 22349 -134 -1282 6460 C ATOM 2195 O ALA A 310 13.204 128.735 77.792 1.00132.65 O ANISOU 2195 O ALA A 310 14074 14143 22185 -122 -1203 6220 O ATOM 2196 CB ALA A 310 10.561 130.144 77.087 1.00126.61 C ANISOU 2196 CB ALA A 310 13096 13128 21881 15 -1580 6447 C ATOM 2197 N GLU A 311 13.876 130.461 76.508 1.00137.56 N ANISOU 2197 N GLU A 311 14531 14676 23059 -212 -1215 6770 N ATOM 2198 CA GLU A 311 15.100 129.783 76.100 1.00133.39 C ANISOU 2198 CA GLU A 311 14104 14401 22177 -274 -1029 6883 C ATOM 2199 C GLU A 311 16.174 129.861 77.175 1.00125.56 C ANISOU 2199 C GLU A 311 13037 13214 21454 -342 -913 6657 C ATOM 2200 O GLU A 311 17.050 128.990 77.234 1.00123.06 O ANISOU 2200 O GLU A 311 12808 13080 20868 -380 -758 6619 O ATOM 2201 CB GLU A 311 15.616 130.372 74.787 1.00144.24 C ANISOU 2201 CB GLU A 311 15461 15942 23403 -316 -974 7297 C ATOM 2202 CG GLU A 311 14.617 130.265 73.650 1.00154.31 C ANISOU 2202 CG GLU A 311 16846 17425 24361 -260 -1109 7526 C ATOM 2203 CD GLU A 311 14.158 128.840 73.416 1.00159.07 C ANISOU 2203 CD GLU A 311 17681 18331 24429 -204 -1125 7421 C ATOM 2204 OE1 GLU A 311 14.933 128.051 72.836 1.00161.68 O ANISOU 2204 OE1 GLU A 311 18175 18955 24300 -215 -960 7510 O ATOM 2205 OE2 GLU A 311 13.026 128.505 73.824 1.00160.44 O ANISOU 2205 OE2 GLU A 311 17864 18443 24652 -143 -1299 7239 O ATOM 2206 N GLN A 312 16.126 130.887 78.028 1.00123.36 N ANISOU 2206 N GLN A 312 12606 12566 21699 -360 -994 6493 N ATOM 2207 CA GLN A 312 16.980 130.905 79.208 1.00118.60 C ANISOU 2207 CA GLN A 312 11965 11749 21348 -419 -943 6202 C ATOM 2208 C GLN A 312 16.647 129.763 80.156 1.00108.37 C ANISOU 2208 C GLN A 312 10814 10484 19878 -372 -922 5826 C ATOM 2209 O GLN A 312 17.468 129.422 81.015 1.00101.51 O ANISOU 2209 O GLN A 312 9964 9576 19028 -429 -855 5547 O ATOM 2210 CB GLN A 312 16.851 132.245 79.935 1.00116.95 C ANISOU 2210 CB GLN A 312 11603 11136 21697 -430 -1065 6063 C ATOM 2211 N LEU A 313 15.462 129.162 80.019 1.00106.82 N ANISOU 2211 N LEU A 313 10708 10456 19424 -270 -975 5695 N ATOM 2212 CA LEU A 313 15.109 128.011 80.840 1.00108.68 C ANISOU 2212 CA LEU A 313 11073 10858 19361 -221 -928 5228 C ATOM 2213 C LEU A 313 15.815 126.739 80.384 1.00101.84 C ANISOU 2213 C LEU A 313 10343 10400 17952 -257 -789 5209 C ATOM 2214 O LEU A 313 15.904 125.781 81.159 1.00 91.65 O ANISOU 2214 O LEU A 313 9148 9228 16446 -247 -726 4830 O ATOM 2215 CB LEU A 313 13.592 127.804 80.844 1.00115.01 C ANISOU 2215 CB LEU A 313 11893 11682 20125 -105 -1035 5121 C ATOM 2216 CG LEU A 313 12.748 128.644 81.814 1.00114.50 C ANISOU 2216 CG LEU A 313 11731 11229 20545 -25 -1115 4907 C ATOM 2217 CD1 LEU A 313 12.798 130.129 81.485 1.00122.82 C ANISOU 2217 CD1 LEU A 313 12628 11931 22108 -39 -1212 5232 C ATOM 2218 CD2 LEU A 313 11.313 128.158 81.817 1.00104.79 C ANISOU 2218 CD2 LEU A 313 10507 10087 19220 91 -1180 4793 C ATOM 2219 N LYS A 314 16.314 126.704 79.147 1.00105.99 N ANISOU 2219 N LYS A 314 10888 11137 18247 -291 -728 5612 N ATOM 2220 CA LYS A 314 17.105 125.567 78.693 1.00108.65 C ANISOU 2220 CA LYS A 314 11355 11834 18094 -314 -562 5603 C ATOM 2221 C LYS A 314 18.512 125.586 79.274 1.00113.64 C ANISOU 2221 C LYS A 314 11914 12387 18876 -403 -423 5538 C ATOM 2222 O LYS A 314 19.083 124.522 79.543 1.00109.42 O ANISOU 2222 O LYS A 314 11470 12066 18037 -411 -300 5321 O ATOM 2223 CB LYS A 314 17.166 125.539 77.166 1.00114.02 C ANISOU 2223 CB LYS A 314 12108 12766 18450 -302 -521 6055 C ATOM 2224 CG LYS A 314 15.935 124.943 76.504 1.00118.40 C ANISOU 2224 CG LYS A 314 12810 13534 18642 -220 -654 6053 C ATOM 2225 CD LYS A 314 16.137 124.810 75.004 1.00125.36 C ANISOU 2225 CD LYS A 314 13822 14692 19117 -209 -606 6474 C ATOM 2226 CE LYS A 314 15.069 123.925 74.394 1.00127.99 C ANISOU 2226 CE LYS A 314 14351 15281 18998 -140 -750 6400 C ATOM 2227 NZ LYS A 314 15.210 123.836 72.917 1.00132.35 N ANISOU 2227 NZ LYS A 314 15076 16094 19117 -121 -731 6803 N ATOM 2228 N THR A 315 19.074 126.775 79.490 1.00122.10 N ANISOU 2228 N THR A 315 12813 13138 20442 -475 -458 5725 N ATOM 2229 CA THR A 315 20.431 126.871 80.012 1.00120.61 C ANISOU 2229 CA THR A 315 12525 12844 20457 -576 -363 5703 C ATOM 2230 C THR A 315 20.482 126.660 81.519 1.00125.54 C ANISOU 2230 C THR A 315 13166 13276 21257 -593 -442 5204 C ATOM 2231 O THR A 315 21.520 126.240 82.042 1.00135.34 O ANISOU 2231 O THR A 315 14384 14535 22504 -663 -371 5078 O ATOM 2232 CB THR A 315 21.050 128.227 79.659 1.00113.41 C ANISOU 2232 CB THR A 315 11412 11640 20038 -660 -393 6110 C ATOM 2233 OG1 THR A 315 20.286 129.277 80.265 1.00113.92 O ANISOU 2233 OG1 THR A 315 11406 11353 20524 -641 -593 5973 O ATOM 2234 CG2 THR A 315 21.075 128.428 78.149 1.00113.58 C ANISOU 2234 CG2 THR A 315 11434 11929 19794 -627 -295 6540 C ATOM 2235 N THR A 316 19.387 126.933 82.234 1.00124.70 N ANISOU 2235 N THR A 316 13103 12987 21291 -525 -582 4927 N ATOM 2236 CA THR A 316 19.393 126.736 83.681 1.00123.52 C ANISOU 2236 CA THR A 316 13007 12663 21262 -527 -642 4450 C ATOM 2237 C THR A 316 19.183 125.272 84.057 1.00122.18 C ANISOU 2237 C THR A 316 12999 12810 20614 -477 -556 4119 C ATOM 2238 O THR A 316 19.776 124.791 85.027 1.00123.18 O ANISOU 2238 O THR A 316 13174 12911 20720 -517 -546 3817 O ATOM 2239 CB THR A 316 18.332 127.616 84.349 1.00125.90 C ANISOU 2239 CB THR A 316 13298 12629 21908 -456 -784 4277 C ATOM 2240 OG1 THR A 316 18.267 127.312 85.749 1.00124.36 O ANISOU 2240 OG1 THR A 316 13204 12305 21742 -437 -816 3794 O ATOM 2241 CG2 THR A 316 16.969 127.394 83.726 1.00127.31 C ANISOU 2241 CG2 THR A 316 13516 12959 21896 -338 -800 4347 C ATOM 2242 N ARG A 317 18.355 124.541 83.304 1.00118.02 N ANISOU 2242 N ARG A 317 12561 12573 19708 -397 -515 4176 N ATOM 2243 CA ARG A 317 18.090 123.154 83.669 1.00111.64 C ANISOU 2243 CA ARG A 317 11899 12039 18480 -352 -451 3862 C ATOM 2244 C ARG A 317 19.271 122.253 83.337 1.00104.84 C ANISOU 2244 C ARG A 317 11075 11434 17326 -408 -304 3913 C ATOM 2245 O ARG A 317 19.509 121.264 84.041 1.00109.92 O ANISOU 2245 O ARG A 317 11804 12196 17764 -407 -257 3606 O ATOM 2246 CB ARG A 317 16.815 122.647 82.992 1.00116.91 C ANISOU 2246 CB ARG A 317 12644 12907 18869 -258 -487 3898 C ATOM 2247 CG ARG A 317 16.905 122.449 81.483 1.00123.88 C ANISOU 2247 CG ARG A 317 13559 14048 19459 -256 -448 4284 C ATOM 2248 CD ARG A 317 16.012 121.292 81.046 1.00124.98 C ANISOU 2248 CD ARG A 317 13846 14482 19160 -187 -471 4172 C ATOM 2249 NE ARG A 317 15.378 121.533 79.753 1.00130.26 N ANISOU 2249 NE ARG A 317 14545 15269 19681 -154 -556 4515 N ATOM 2250 CZ ARG A 317 15.935 121.251 78.580 1.00135.84 C ANISOU 2250 CZ ARG A 317 15342 16214 20057 -165 -478 4802 C ATOM 2251 NH1 ARG A 317 17.147 120.718 78.528 1.00137.50 N ANISOU 2251 NH1 ARG A 317 15595 16565 20082 -203 -288 4792 N ATOM 2252 NH2 ARG A 317 15.278 121.506 77.457 1.00138.58 N ANISOU 2252 NH2 ARG A 317 15741 16656 20257 -133 -586 5106 N ATOM 2253 N ASN A 318 20.026 122.577 82.283 1.00100.49 N ANISOU 2253 N ASN A 318 10453 10965 16763 -451 -217 4309 N ATOM 2254 CA ASN A 318 21.235 121.815 81.981 1.00 98.57 C ANISOU 2254 CA ASN A 318 10216 10934 16302 -493 -44 4381 C ATOM 2255 C ASN A 318 22.273 121.991 83.083 1.00 99.05 C ANISOU 2255 C ASN A 318 10176 10786 16674 -585 -61 4207 C ATOM 2256 O ASN A 318 22.866 121.018 83.561 1.00 99.76 O ANISOU 2256 O ASN A 318 10313 11012 16577 -596 13 3995 O ATOM 2257 CB ASN A 318 21.814 122.241 80.629 1.00101.72 C ANISOU 2257 CB ASN A 318 10552 11444 16654 -508 82 4873 C ATOM 2258 CG ASN A 318 20.908 121.883 79.455 1.00104.58 C ANISOU 2258 CG ASN A 318 11062 12064 16610 -419 91 5046 C ATOM 2259 OD1 ASN A 318 19.981 121.082 79.583 1.00109.84 O ANISOU 2259 OD1 ASN A 318 11874 12873 16988 -352 22 4790 O ATOM 2260 ND2 ASN A 318 21.187 122.474 78.298 1.00102.62 N ANISOU 2260 ND2 ASN A 318 10779 11872 16340 -422 167 5495 N ATOM 2261 N ALA A 319 22.485 123.234 83.518 1.00100.20 N ANISOU 2261 N ALA A 319 10184 10578 17308 -652 -183 4289 N ATOM 2262 CA ALA A 319 23.485 123.510 84.544 1.00101.35 C ANISOU 2262 CA ALA A 319 10238 10489 17783 -754 -251 4140 C ATOM 2263 C ALA A 319 23.038 123.055 85.928 1.00111.74 C ANISOU 2263 C ALA A 319 11687 11714 19056 -731 -367 3638 C ATOM 2264 O ALA A 319 23.876 122.637 86.737 1.00116.68 O ANISOU 2264 O ALA A 319 12310 12304 19719 -796 -392 3447 O ATOM 2265 CB ALA A 319 23.821 125.000 84.560 1.00 91.84 C ANISOU 2265 CB ALA A 319 8861 8908 17127 -838 -373 4378 C ATOM 2266 N TYR A 320 21.740 123.108 86.218 1.00115.02 N ANISOU 2266 N TYR A 320 12213 12095 19393 -637 -433 3436 N ATOM 2267 CA TYR A 320 21.246 122.945 87.584 1.00117.31 C ANISOU 2267 CA TYR A 320 12625 12238 19710 -605 -531 2989 C ATOM 2268 C TYR A 320 20.411 121.693 87.814 1.00107.28 C ANISOU 2268 C TYR A 320 11513 11243 18006 -509 -457 2722 C ATOM 2269 O TYR A 320 20.545 121.060 88.865 1.00101.05 O ANISOU 2269 O TYR A 320 10827 10459 17109 -510 -473 2389 O ATOM 2270 CB TYR A 320 20.417 124.173 87.993 1.00124.97 C ANISOU 2270 CB TYR A 320 13581 12859 21044 -564 -661 2933 C ATOM 2271 CG TYR A 320 21.219 125.242 88.714 1.00135.95 C ANISOU 2271 CG TYR A 320 14903 13860 22894 -662 -809 2899 C ATOM 2272 CD1 TYR A 320 21.849 126.269 88.016 1.00139.61 C ANISOU 2272 CD1 TYR A 320 15185 14138 23721 -747 -855 3275 C ATOM 2273 CD2 TYR A 320 21.352 125.217 90.095 1.00141.17 C ANISOU 2273 CD2 TYR A 320 15688 14328 23621 -673 -915 2495 C ATOM 2274 CE1 TYR A 320 22.584 127.238 88.679 1.00144.55 C ANISOU 2274 CE1 TYR A 320 15741 14381 24799 -850 -1021 3241 C ATOM 2275 CE2 TYR A 320 22.086 126.181 90.766 1.00144.83 C ANISOU 2275 CE2 TYR A 320 16115 14418 24498 -770 -1090 2442 C ATOM 2276 CZ TYR A 320 22.699 127.188 90.053 1.00147.75 C ANISOU 2276 CZ TYR A 320 16288 14592 25259 -862 -1151 2812 C ATOM 2277 OH TYR A 320 23.431 128.152 90.708 1.00154.39 O ANISOU 2277 OH TYR A 320 17082 15035 26545 -971 -1354 2764 O ATOM 2278 N ILE A 321 19.561 121.302 86.870 1.00101.87 N ANISOU 2278 N ILE A 321 10852 10781 17073 -432 -392 2867 N ATOM 2279 CA ILE A 321 18.540 120.275 87.104 1.00 97.15 C ANISOU 2279 CA ILE A 321 10383 10383 16148 -340 -360 2623 C ATOM 2280 C ILE A 321 18.990 118.904 86.603 1.00105.77 C ANISOU 2280 C ILE A 321 11547 11827 16813 -346 -246 2624 C ATOM 2281 O ILE A 321 18.956 117.922 87.344 1.00111.69 O ANISOU 2281 O ILE A 321 12394 12683 17361 -330 -217 2336 O ATOM 2282 CB ILE A 321 17.196 120.696 86.461 1.00 86.53 C ANISOU 2282 CB ILE A 321 9016 9026 14834 -252 -407 2756 C ATOM 2283 CG1 ILE A 321 16.814 122.116 86.895 1.00 84.52 C ANISOU 2283 CG1 ILE A 321 8675 8396 15041 -237 -506 2778 C ATOM 2284 CG2 ILE A 321 16.073 119.736 86.838 1.00 82.46 C ANISOU 2284 CG2 ILE A 321 8599 8661 14071 -164 -393 2501 C ATOM 2285 CD1 ILE A 321 16.388 122.240 88.347 1.00 80.14 C ANISOU 2285 CD1 ILE A 321 8195 7624 14630 -189 -533 2380 C ATOM 2286 N GLN A 322 19.419 118.819 85.339 1.00107.26 N ANISOU 2286 N GLN A 322 11701 12196 16858 -360 -170 2951 N ATOM 2287 CA GLN A 322 19.688 117.528 84.702 1.00107.66 C ANISOU 2287 CA GLN A 322 11848 12582 16477 -337 -52 2957 C ATOM 2288 C GLN A 322 20.649 116.669 85.508 1.00107.14 C ANISOU 2288 C GLN A 322 11806 12572 16329 -378 17 2732 C ATOM 2289 O GLN A 322 20.562 115.438 85.463 1.00108.91 O ANISOU 2289 O GLN A 322 12138 13024 16217 -341 82 2581 O ATOM 2290 CB GLN A 322 20.253 117.736 83.288 1.00116.14 C ANISOU 2290 CB GLN A 322 12889 13803 17435 -345 49 3358 C ATOM 2291 CG GLN A 322 20.385 116.449 82.472 1.00121.77 C ANISOU 2291 CG GLN A 322 13742 14860 17667 -295 175 3368 C ATOM 2292 CD GLN A 322 21.086 116.675 81.144 1.00129.63 C ANISOU 2292 CD GLN A 322 14727 15997 18528 -291 317 3760 C ATOM 2293 OE1 GLN A 322 21.875 117.608 81.006 1.00131.37 O ANISOU 2293 OE1 GLN A 322 14799 16071 19043 -348 366 4014 O ATOM 2294 NE2 GLN A 322 20.794 115.831 80.157 1.00133.39 N ANISOU 2294 NE2 GLN A 322 15371 16751 18561 -222 384 3817 N ATOM 2295 N LYS A 323 21.571 117.293 86.246 1.00106.68 N ANISOU 2295 N LYS A 323 11649 12296 16588 -458 -19 2712 N ATOM 2296 CA LYS A 323 22.498 116.526 87.073 1.00107.03 C ANISOU 2296 CA LYS A 323 11705 12371 16590 -505 9 2510 C ATOM 2297 C LYS A 323 21.778 115.829 88.222 1.00104.47 C ANISOU 2297 C LYS A 323 11515 12045 16133 -466 -58 2115 C ATOM 2298 O LYS A 323 22.057 114.661 88.520 1.00106.57 O ANISOU 2298 O LYS A 323 11854 12485 16154 -456 0 1952 O ATOM 2299 CB LYS A 323 23.600 117.441 87.607 1.00113.26 C ANISOU 2299 CB LYS A 323 12352 12896 17787 -612 -65 2592 C ATOM 2300 CG LYS A 323 24.740 116.711 88.288 1.00114.44 C ANISOU 2300 CG LYS A 323 12475 13076 17932 -674 -52 2466 C ATOM 2301 CD LYS A 323 25.206 115.543 87.440 1.00114.68 C ANISOU 2301 CD LYS A 323 12515 13427 17630 -630 147 2578 C ATOM 2302 CE LYS A 323 26.680 115.257 87.655 1.00116.73 C ANISOU 2302 CE LYS A 323 12637 13673 18043 -705 197 2662 C ATOM 2303 NZ LYS A 323 27.532 116.373 87.156 1.00120.36 N ANISOU 2303 NZ LYS A 323 12887 13962 18883 -785 209 3013 N ATOM 2304 N TYR A 324 20.852 116.527 88.885 1.00102.85 N ANISOU 2304 N TYR A 324 11344 11638 16096 -436 -165 1966 N ATOM 2305 CA TYR A 324 20.139 115.914 90.001 1.00 98.85 C ANISOU 2305 CA TYR A 324 10966 11126 15467 -388 -195 1611 C ATOM 2306 C TYR A 324 19.115 114.895 89.519 1.00 93.22 C ANISOU 2306 C TYR A 324 10330 10662 14425 -305 -128 1562 C ATOM 2307 O TYR A 324 18.778 113.963 90.258 1.00 83.83 O ANISOU 2307 O TYR A 324 9238 9560 13053 -276 -108 1311 O ATOM 2308 CB TYR A 324 19.463 116.987 90.854 1.00101.12 C ANISOU 2308 CB TYR A 324 11272 11112 16036 -361 -295 1466 C ATOM 2309 CG TYR A 324 19.055 116.502 92.230 1.00100.16 C ANISOU 2309 CG TYR A 324 11295 10939 15823 -323 -311 1096 C ATOM 2310 CD1 TYR A 324 19.984 116.416 93.260 1.00100.80 C ANISOU 2310 CD1 TYR A 324 11438 10913 15946 -392 -382 913 C ATOM 2311 CD2 TYR A 324 17.742 116.134 92.501 1.00 98.09 C ANISOU 2311 CD2 TYR A 324 11101 10731 15436 -219 -258 946 C ATOM 2312 CE1 TYR A 324 19.620 115.975 94.520 1.00102.37 C ANISOU 2312 CE1 TYR A 324 11798 11075 16024 -352 -393 588 C ATOM 2313 CE2 TYR A 324 17.367 115.691 93.760 1.00 97.01 C ANISOU 2313 CE2 TYR A 324 11101 10555 15203 -175 -239 632 C ATOM 2314 CZ TYR A 324 18.311 115.615 94.764 1.00100.97 C ANISOU 2314 CZ TYR A 324 11694 10963 15706 -240 -304 452 C ATOM 2315 OH TYR A 324 17.947 115.177 96.018 1.00102.95 O ANISOU 2315 OH TYR A 324 12109 11184 15824 -192 -283 151 O ATOM 2316 N LEU A 325 18.609 115.055 88.294 1.00 95.29 N ANISOU 2316 N LEU A 325 10556 11034 14617 -271 -108 1807 N ATOM 2317 CA LEU A 325 17.713 114.053 87.727 1.00 95.30 C ANISOU 2317 CA LEU A 325 10633 11269 14307 -207 -82 1778 C ATOM 2318 C LEU A 325 18.450 112.749 87.454 1.00 94.92 C ANISOU 2318 C LEU A 325 10657 11466 13942 -222 9 1732 C ATOM 2319 O LEU A 325 17.924 111.663 87.722 1.00 95.74 O ANISOU 2319 O LEU A 325 10847 11704 13824 -188 18 1544 O ATOM 2320 CB LEU A 325 17.079 114.582 86.443 1.00 99.46 C ANISOU 2320 CB LEU A 325 11123 11845 14824 -176 -119 2068 C ATOM 2321 CG LEU A 325 16.101 115.745 86.581 1.00104.96 C ANISOU 2321 CG LEU A 325 11740 12314 15827 -139 -215 2128 C ATOM 2322 CD1 LEU A 325 16.054 116.515 85.282 1.00109.98 C ANISOU 2322 CD1 LEU A 325 12314 12961 16511 -142 -254 2497 C ATOM 2323 CD2 LEU A 325 14.720 115.233 86.951 1.00104.48 C ANISOU 2323 CD2 LEU A 325 11711 12281 15707 -64 -258 1951 C ATOM 2324 N MET A 326 19.670 112.837 86.917 1.00 95.95 N ANISOU 2324 N MET A 326 10740 11645 14073 -268 86 1914 N ATOM 2325 CA MET A 326 20.443 111.635 86.622 1.00 93.87 C ANISOU 2325 CA MET A 326 10532 11597 13535 -266 198 1881 C ATOM 2326 C MET A 326 20.963 110.974 87.892 1.00 89.93 C ANISOU 2326 C MET A 326 10052 11055 13062 -298 191 1610 C ATOM 2327 O MET A 326 21.068 109.743 87.948 1.00 89.26 O ANISOU 2327 O MET A 326 10046 11138 12732 -274 247 1478 O ATOM 2328 CB MET A 326 21.602 111.975 85.683 1.00100.28 C ANISOU 2328 CB MET A 326 11267 12464 14372 -292 317 2180 C ATOM 2329 CG MET A 326 21.168 112.498 84.319 1.00110.54 C ANISOU 2329 CG MET A 326 12582 13847 15571 -254 340 2476 C ATOM 2330 SD MET A 326 22.539 113.088 83.303 1.00119.40 S ANISOU 2330 SD MET A 326 13593 15002 16770 -282 515 2871 S ATOM 2331 CE MET A 326 23.539 111.608 83.176 1.00119.42 C ANISOU 2331 CE MET A 326 13661 15234 16480 -246 708 2767 C ATOM 2332 N ASP A 327 21.293 111.765 88.917 1.00 89.13 N ANISOU 2332 N ASP A 327 9893 10722 13251 -353 109 1525 N ATOM 2333 CA ASP A 327 21.746 111.186 90.178 1.00 92.82 C ANISOU 2333 CA ASP A 327 10403 11139 13724 -385 71 1270 C ATOM 2334 C ASP A 327 20.625 110.418 90.867 1.00 93.19 C ANISOU 2334 C ASP A 327 10575 11244 13588 -327 51 1008 C ATOM 2335 O ASP A 327 20.849 109.325 91.401 1.00 93.34 O ANISOU 2335 O ASP A 327 10660 11368 13437 -326 75 845 O ATOM 2336 CB ASP A 327 22.289 112.280 91.098 1.00 96.19 C ANISOU 2336 CB ASP A 327 10774 11286 14487 -457 -46 1229 C ATOM 2337 CG ASP A 327 23.562 112.914 90.568 1.00105.15 C ANISOU 2337 CG ASP A 327 11754 12347 15850 -534 -35 1490 C ATOM 2338 OD1 ASP A 327 24.332 112.219 89.872 1.00107.74 O ANISOU 2338 OD1 ASP A 327 12029 12853 16055 -536 87 1633 O ATOM 2339 OD2 ASP A 327 23.793 114.110 90.848 1.00110.37 O ANISOU 2339 OD2 ASP A 327 12342 12761 16830 -590 -139 1557 O ATOM 2340 N ARG A 328 19.410 110.972 90.865 1.00 94.39 N ANISOU 2340 N ARG A 328 10744 11321 13797 -276 13 985 N ATOM 2341 CA ARG A 328 18.287 110.294 91.504 1.00 89.92 C ANISOU 2341 CA ARG A 328 10266 10799 13101 -217 14 771 C ATOM 2342 C ARG A 328 17.812 109.109 90.673 1.00 80.59 C ANISOU 2342 C ARG A 328 9122 9861 11638 -181 60 801 C ATOM 2343 O ARG A 328 17.433 108.070 91.225 1.00 72.05 O ANISOU 2343 O ARG A 328 8109 8867 10401 -162 78 623 O ATOM 2344 CB ARG A 328 17.145 111.283 91.744 1.00100.13 C ANISOU 2344 CB ARG A 328 11537 11920 14589 -163 -26 755 C ATOM 2345 CG ARG A 328 15.936 110.682 92.444 1.00113.48 C ANISOU 2345 CG ARG A 328 13286 13635 16196 -93 4 560 C ATOM 2346 CD ARG A 328 15.198 111.718 93.271 1.00127.52 C ANISOU 2346 CD ARG A 328 15063 15175 18213 -37 -1 459 C ATOM 2347 NE ARG A 328 16.095 112.393 94.208 1.00141.31 N ANISOU 2347 NE ARG A 328 16870 16731 20092 -79 -39 340 N ATOM 2348 CZ ARG A 328 16.481 111.884 95.376 1.00148.18 C ANISOU 2348 CZ ARG A 328 17862 17586 20855 -92 -30 113 C ATOM 2349 NH1 ARG A 328 16.055 110.686 95.763 1.00149.03 N ANISOU 2349 NH1 ARG A 328 18033 17860 20733 -63 39 -8 N ATOM 2350 NH2 ARG A 328 17.299 112.573 96.160 1.00150.62 N ANISOU 2350 NH2 ARG A 328 18234 17704 21291 -140 -109 14 N ATOM 2351 N HIS A 329 17.824 109.245 89.343 1.00 80.34 N ANISOU 2351 N HIS A 329 9059 9933 11532 -172 70 1028 N ATOM 2352 CA HIS A 329 17.451 108.126 88.484 1.00 78.30 C ANISOU 2352 CA HIS A 329 8872 9896 10984 -140 89 1046 C ATOM 2353 C HIS A 329 18.414 106.957 88.644 1.00 80.24 C ANISOU 2353 C HIS A 329 9173 10272 11043 -156 168 947 C ATOM 2354 O HIS A 329 18.008 105.797 88.518 1.00 80.35 O ANISOU 2354 O HIS A 329 9266 10419 10843 -130 170 837 O ATOM 2355 CB HIS A 329 17.396 108.575 87.023 1.00 81.18 C ANISOU 2355 CB HIS A 329 9230 10343 11273 -125 82 1315 C ATOM 2356 CG HIS A 329 17.113 107.465 86.058 1.00 90.82 C ANISOU 2356 CG HIS A 329 10562 11780 12165 -90 83 1327 C ATOM 2357 ND1 HIS A 329 18.109 106.699 85.492 1.00 93.86 N ANISOU 2357 ND1 HIS A 329 11018 12317 12329 -84 193 1355 N ATOM 2358 CD2 HIS A 329 15.946 106.995 85.556 1.00 93.14 C ANISOU 2358 CD2 HIS A 329 10915 12149 12325 -59 -22 1310 C ATOM 2359 CE1 HIS A 329 17.569 105.803 84.685 1.00 94.04 C ANISOU 2359 CE1 HIS A 329 11166 12496 12070 -45 156 1333 C ATOM 2360 NE2 HIS A 329 16.257 105.962 84.706 1.00 92.82 N ANISOU 2360 NE2 HIS A 329 11004 12297 11967 -38 7 1309 N ATOM 2361 N ALA A 330 19.688 107.239 88.920 1.00 80.22 N ANISOU 2361 N ALA A 330 9118 10216 11146 -201 221 991 N ATOM 2362 CA ALA A 330 20.640 106.166 89.183 1.00 70.55 C ANISOU 2362 CA ALA A 330 7919 9088 9798 -212 292 902 C ATOM 2363 C ALA A 330 20.472 105.610 90.592 1.00 66.81 C ANISOU 2363 C ALA A 330 7486 8551 9350 -230 241 650 C ATOM 2364 O ALA A 330 20.615 104.401 90.805 1.00 68.06 O ANISOU 2364 O ALA A 330 7701 8817 9342 -217 272 530 O ATOM 2365 CB ALA A 330 22.069 106.664 88.970 1.00 67.26 C ANISOU 2365 CB ALA A 330 7399 8629 9528 -255 361 1069 C ATOM 2366 N LYS A 331 20.173 106.477 91.563 1.00 66.88 N ANISOU 2366 N LYS A 331 7479 8378 9555 -254 167 568 N ATOM 2367 CA LYS A 331 19.908 106.011 92.920 1.00 71.67 C ANISOU 2367 CA LYS A 331 8158 8927 10147 -258 129 334 C ATOM 2368 C LYS A 331 18.695 105.088 92.955 1.00 77.68 C ANISOU 2368 C LYS A 331 8984 9795 10735 -203 150 223 C ATOM 2369 O LYS A 331 18.686 104.086 93.680 1.00 77.45 O ANISOU 2369 O LYS A 331 9017 9819 10592 -203 161 75 O ATOM 2370 CB LYS A 331 19.709 107.210 93.849 1.00 75.25 C ANISOU 2370 CB LYS A 331 8616 9157 10819 -273 58 262 C ATOM 2371 CG LYS A 331 19.067 106.888 95.189 1.00 83.67 C ANISOU 2371 CG LYS A 331 9793 10164 11835 -248 45 25 C ATOM 2372 CD LYS A 331 19.980 106.059 96.074 1.00 91.87 C ANISOU 2372 CD LYS A 331 10895 11232 12781 -293 15 -96 C ATOM 2373 CE LYS A 331 19.355 105.847 97.443 1.00 97.37 C ANISOU 2373 CE LYS A 331 11727 11863 13406 -264 10 -315 C ATOM 2374 NZ LYS A 331 18.036 105.166 97.347 1.00 97.92 N ANISOU 2374 NZ LYS A 331 11815 12038 13352 -191 105 -358 N ATOM 2375 N ILE A 332 17.666 105.406 92.167 1.00 82.28 N ANISOU 2375 N ILE A 332 9544 10402 11315 -162 140 313 N ATOM 2376 CA ILE A 332 16.488 104.548 92.094 1.00 78.82 C ANISOU 2376 CA ILE A 332 9138 10053 10757 -121 135 239 C ATOM 2377 C ILE A 332 16.824 103.236 91.396 1.00 77.18 C ANISOU 2377 C ILE A 332 8980 10024 10320 -123 151 238 C ATOM 2378 O ILE A 332 16.412 102.157 91.841 1.00 79.67 O ANISOU 2378 O ILE A 332 9339 10396 10536 -116 152 110 O ATOM 2379 CB ILE A 332 15.335 105.288 91.389 1.00 82.00 C ANISOU 2379 CB ILE A 332 9484 10418 11255 -83 86 359 C ATOM 2380 CG1 ILE A 332 14.812 106.429 92.265 1.00 86.51 C ANISOU 2380 CG1 ILE A 332 10014 10791 12066 -58 90 313 C ATOM 2381 CG2 ILE A 332 14.211 104.327 91.030 1.00 78.81 C ANISOU 2381 CG2 ILE A 332 9090 10116 10738 -56 46 329 C ATOM 2382 CD1 ILE A 332 13.674 107.205 91.638 1.00 88.13 C ANISOU 2382 CD1 ILE A 332 10135 10932 12416 -13 42 443 C ATOM 2383 N LYS A 333 17.582 103.304 90.298 1.00 75.35 N ANISOU 2383 N LYS A 333 8750 9876 10006 -126 176 383 N ATOM 2384 CA LYS A 333 17.920 102.095 89.553 1.00 74.09 C ANISOU 2384 CA LYS A 333 8663 9875 9614 -108 209 371 C ATOM 2385 C LYS A 333 18.754 101.137 90.395 1.00 74.72 C ANISOU 2385 C LYS A 333 8762 9970 9658 -125 260 232 C ATOM 2386 O LYS A 333 18.590 99.915 90.304 1.00 83.12 O ANISOU 2386 O LYS A 333 9890 11120 10571 -107 261 134 O ATOM 2387 CB LYS A 333 18.662 102.463 88.267 1.00 73.59 C ANISOU 2387 CB LYS A 333 8608 9891 9462 -91 269 564 C ATOM 2388 CG LYS A 333 19.018 101.274 87.391 1.00 80.20 C ANISOU 2388 CG LYS A 333 9552 10886 10033 -49 325 544 C ATOM 2389 CD LYS A 333 19.843 101.703 86.189 1.00 91.35 C ANISOU 2389 CD LYS A 333 10984 12379 11346 -17 432 747 C ATOM 2390 CE LYS A 333 20.241 100.510 85.335 1.00 98.17 C ANISOU 2390 CE LYS A 333 11985 13391 11924 46 516 704 C ATOM 2391 NZ LYS A 333 21.125 100.912 84.206 1.00106.42 N ANISOU 2391 NZ LYS A 333 13058 14522 12855 95 672 911 N ATOM 2392 N ARG A 334 19.654 101.671 91.223 1.00 68.58 N ANISOU 2392 N ARG A 334 7930 9095 9033 -163 280 224 N ATOM 2393 CA ARG A 334 20.462 100.808 92.078 1.00 67.85 C ANISOU 2393 CA ARG A 334 7849 9006 8925 -184 298 110 C ATOM 2394 C ARG A 334 19.635 100.217 93.215 1.00 67.13 C ANISOU 2394 C ARG A 334 7812 8881 8812 -188 251 -65 C ATOM 2395 O ARG A 334 19.909 99.096 93.660 1.00 69.26 O ANISOU 2395 O ARG A 334 8118 9199 8999 -190 260 -159 O ATOM 2396 CB ARG A 334 21.662 101.589 92.621 1.00 72.18 C ANISOU 2396 CB ARG A 334 8320 9445 9659 -235 292 168 C ATOM 2397 CG ARG A 334 22.577 100.794 93.544 1.00 81.09 C ANISOU 2397 CG ARG A 334 9447 10560 10803 -265 276 75 C ATOM 2398 CD ARG A 334 23.958 101.429 93.637 1.00 93.32 C ANISOU 2398 CD ARG A 334 10885 12026 12546 -316 267 193 C ATOM 2399 NE ARG A 334 24.749 101.177 92.436 1.00100.32 N ANISOU 2399 NE ARG A 334 11696 13012 13410 -281 397 358 N ATOM 2400 CZ ARG A 334 25.651 100.206 92.326 1.00101.43 C ANISOU 2400 CZ ARG A 334 11799 13218 13524 -260 470 368 C ATOM 2401 NH1 ARG A 334 25.884 99.397 93.351 1.00101.22 N ANISOU 2401 NH1 ARG A 334 11796 13165 13501 -282 398 233 N ATOM 2402 NH2 ARG A 334 26.324 100.046 91.194 1.00102.48 N ANISOU 2402 NH2 ARG A 334 11874 13438 13626 -207 626 521 N ATOM 2403 N ALA A 335 18.614 100.938 93.683 1.00 64.03 N ANISOU 2403 N ALA A 335 7422 8406 8503 -181 216 -99 N ATOM 2404 CA ALA A 335 17.772 100.412 94.752 1.00 64.71 C ANISOU 2404 CA ALA A 335 7554 8464 8568 -171 211 -242 C ATOM 2405 C ALA A 335 16.880 99.284 94.250 1.00 63.44 C ANISOU 2405 C ALA A 335 7408 8408 8290 -146 209 -264 C ATOM 2406 O ALA A 335 16.665 98.293 94.959 1.00 55.02 O ANISOU 2406 O ALA A 335 6377 7363 7167 -150 219 -362 O ATOM 2407 CB ALA A 335 16.934 101.535 95.361 1.00 59.46 C ANISOU 2407 CB ALA A 335 6882 7671 8041 -150 209 -265 C ATOM 2408 N ILE A 336 16.346 99.418 93.033 1.00 61.51 N ANISOU 2408 N ILE A 336 7141 8218 8012 -126 179 -167 N ATOM 2409 CA ILE A 336 15.556 98.340 92.445 1.00 59.84 C ANISOU 2409 CA ILE A 336 6953 8090 7694 -114 133 -190 C ATOM 2410 C ILE A 336 16.439 97.134 92.155 1.00 66.06 C ANISOU 2410 C ILE A 336 7804 8963 8331 -117 152 -243 C ATOM 2411 O ILE A 336 16.041 95.985 92.385 1.00 70.21 O ANISOU 2411 O ILE A 336 8359 9514 8804 -121 127 -329 O ATOM 2412 CB ILE A 336 14.839 98.834 91.175 1.00 61.18 C ANISOU 2412 CB ILE A 336 7108 8291 7848 -96 58 -68 C ATOM 2413 CG1 ILE A 336 13.857 99.956 91.517 1.00 65.73 C ANISOU 2413 CG1 ILE A 336 7598 8762 8616 -82 38 -13 C ATOM 2414 CG2 ILE A 336 14.122 97.684 90.479 1.00 63.23 C ANISOU 2414 CG2 ILE A 336 7414 8625 7987 -94 -34 -100 C ATOM 2415 CD1 ILE A 336 13.101 100.491 90.321 1.00 63.47 C ANISOU 2415 CD1 ILE A 336 7282 8493 8341 -68 -63 130 C ATOM 2416 N THR A 337 17.650 97.375 91.648 1.00 66.82 N ANISOU 2416 N THR A 337 7912 9094 8383 -112 207 -181 N ATOM 2417 CA THR A 337 18.589 96.284 91.411 1.00 62.54 C ANISOU 2417 CA THR A 337 7415 8617 7729 -97 256 -226 C ATOM 2418 C THR A 337 18.945 95.565 92.706 1.00 59.53 C ANISOU 2418 C THR A 337 7025 8192 7403 -124 263 -335 C ATOM 2419 O THR A 337 19.141 94.344 92.706 1.00 60.46 O ANISOU 2419 O THR A 337 7182 8345 7446 -111 267 -408 O ATOM 2420 CB THR A 337 19.852 96.820 90.730 1.00 56.55 C ANISOU 2420 CB THR A 337 6633 7889 6963 -79 347 -109 C ATOM 2421 OG1 THR A 337 19.495 97.463 89.500 1.00 53.61 O ANISOU 2421 OG1 THR A 337 6290 7569 6511 -51 346 12 O ATOM 2422 CG2 THR A 337 20.830 95.692 90.433 1.00 57.09 C ANISOU 2422 CG2 THR A 337 6736 8019 6937 -43 428 -149 C ATOM 2423 N PHE A 338 19.011 96.298 93.819 1.00 61.19 N ANISOU 2423 N PHE A 338 7199 8315 7734 -157 254 -350 N ATOM 2424 CA PHE A 338 19.382 95.679 95.087 1.00 61.41 C ANISOU 2424 CA PHE A 338 7244 8304 7785 -183 246 -439 C ATOM 2425 C PHE A 338 18.288 94.750 95.599 1.00 62.93 C ANISOU 2425 C PHE A 338 7471 8506 7935 -180 228 -522 C ATOM 2426 O PHE A 338 18.576 93.640 96.062 1.00 59.32 O ANISOU 2426 O PHE A 338 7038 8062 7440 -187 224 -576 O ATOM 2427 CB PHE A 338 19.697 96.755 96.124 1.00 56.51 C ANISOU 2427 CB PHE A 338 6618 7582 7272 -215 223 -447 C ATOM 2428 CG PHE A 338 19.873 96.219 97.512 1.00 52.53 C ANISOU 2428 CG PHE A 338 6169 7037 6753 -240 195 -540 C ATOM 2429 CD1 PHE A 338 21.039 95.567 97.872 1.00 50.69 C ANISOU 2429 CD1 PHE A 338 5930 6807 6523 -265 165 -540 C ATOM 2430 CD2 PHE A 338 18.870 96.362 98.457 1.00 49.22 C ANISOU 2430 CD2 PHE A 338 5808 6575 6318 -232 206 -611 C ATOM 2431 CE1 PHE A 338 21.205 95.069 99.151 1.00 47.11 C ANISOU 2431 CE1 PHE A 338 5542 6318 6040 -291 117 -608 C ATOM 2432 CE2 PHE A 338 19.030 95.865 99.736 1.00 49.05 C ANISOU 2432 CE2 PHE A 338 5866 6526 6245 -249 189 -683 C ATOM 2433 CZ PHE A 338 20.200 95.219 100.083 1.00 46.70 C ANISOU 2433 CZ PHE A 338 5576 6236 5933 -283 130 -680 C ATOM 2434 N ILE A 339 17.027 95.182 95.532 1.00 62.58 N ANISOU 2434 N ILE A 339 7411 8443 7925 -169 217 -514 N ATOM 2435 CA ILE A 339 15.953 94.365 96.087 1.00 51.71 C ANISOU 2435 CA ILE A 339 6034 7060 6554 -170 214 -563 C ATOM 2436 C ILE A 339 15.663 93.167 95.190 1.00 57.51 C ANISOU 2436 C ILE A 339 6775 7851 7225 -169 159 -573 C ATOM 2437 O ILE A 339 15.159 92.138 95.660 1.00 58.05 O ANISOU 2437 O ILE A 339 6842 7909 7305 -183 145 -614 O ATOM 2438 CB ILE A 339 14.694 95.220 96.322 1.00 54.60 C ANISOU 2438 CB ILE A 339 6351 7373 7023 -150 233 -535 C ATOM 2439 CG1 ILE A 339 13.691 94.461 97.194 1.00 63.31 C ANISOU 2439 CG1 ILE A 339 7434 8456 8166 -149 272 -565 C ATOM 2440 CG2 ILE A 339 14.061 95.626 94.998 1.00 53.36 C ANISOU 2440 CG2 ILE A 339 6145 7241 6890 -137 168 -454 C ATOM 2441 CD1 ILE A 339 14.249 94.049 98.541 1.00 66.29 C ANISOU 2441 CD1 ILE A 339 7884 8815 8486 -159 332 -628 C ATOM 2442 N MET A 340 15.983 93.266 93.898 1.00 61.99 N ANISOU 2442 N MET A 340 7364 8470 7719 -151 126 -537 N ATOM 2443 CA MET A 340 15.781 92.131 93.004 1.00 70.40 C ANISOU 2443 CA MET A 340 8480 9576 8694 -142 60 -575 C ATOM 2444 C MET A 340 16.784 91.019 93.285 1.00 76.87 C ANISOU 2444 C MET A 340 9341 10403 9463 -135 97 -644 C ATOM 2445 O MET A 340 16.411 89.842 93.351 1.00 87.24 O ANISOU 2445 O MET A 340 10677 11697 10774 -144 47 -707 O ATOM 2446 CB MET A 340 15.876 92.578 91.545 1.00 78.38 C ANISOU 2446 CB MET A 340 9542 10646 9593 -111 26 -519 C ATOM 2447 CG MET A 340 14.645 93.301 91.024 1.00 91.08 C ANISOU 2447 CG MET A 340 11113 12242 11249 -119 -69 -447 C ATOM 2448 SD MET A 340 14.801 93.755 89.285 1.00107.17 S ANISOU 2448 SD MET A 340 13250 14361 13109 -83 -128 -365 S ATOM 2449 CE MET A 340 13.170 94.416 88.949 1.00112.98 C ANISOU 2449 CE MET A 340 13912 15055 13962 -108 -289 -276 C ATOM 2450 N VAL A 341 18.062 91.370 93.458 1.00 68.46 N ANISOU 2450 N VAL A 341 8272 9349 8391 -121 176 -622 N ATOM 2451 CA VAL A 341 19.073 90.339 93.669 1.00 62.70 C ANISOU 2451 CA VAL A 341 7560 8617 7645 -105 212 -669 C ATOM 2452 C VAL A 341 18.896 89.676 95.029 1.00 64.06 C ANISOU 2452 C VAL A 341 7711 8734 7894 -145 187 -709 C ATOM 2453 O VAL A 341 19.212 88.492 95.191 1.00 74.10 O ANISOU 2453 O VAL A 341 9000 9987 9167 -138 177 -756 O ATOM 2454 CB VAL A 341 20.491 90.919 93.493 1.00 55.01 C ANISOU 2454 CB VAL A 341 6551 7659 6691 -83 297 -604 C ATOM 2455 CG1 VAL A 341 20.657 91.501 92.096 1.00 45.83 C ANISOU 2455 CG1 VAL A 341 5419 6561 5434 -35 349 -539 C ATOM 2456 CG2 VAL A 341 20.791 91.968 94.549 1.00 60.99 C ANISOU 2456 CG2 VAL A 341 7248 8366 7558 -131 289 -557 C ATOM 2457 N VAL A 342 18.380 90.406 96.021 1.00 57.34 N ANISOU 2457 N VAL A 342 6836 7852 7099 -179 186 -689 N ATOM 2458 CA VAL A 342 18.092 89.792 97.314 1.00 54.22 C ANISOU 2458 CA VAL A 342 6447 7417 6738 -209 179 -713 C ATOM 2459 C VAL A 342 16.990 88.750 97.170 1.00 56.60 C ANISOU 2459 C VAL A 342 6740 7705 7058 -217 144 -735 C ATOM 2460 O VAL A 342 17.038 87.683 97.793 1.00 63.56 O ANISOU 2460 O VAL A 342 7628 8558 7964 -233 132 -749 O ATOM 2461 CB VAL A 342 17.726 90.869 98.352 1.00 50.40 C ANISOU 2461 CB VAL A 342 5971 6901 6278 -224 208 -698 C ATOM 2462 CG1 VAL A 342 17.206 90.227 99.631 1.00 44.28 C ANISOU 2462 CG1 VAL A 342 5227 6098 5500 -242 228 -710 C ATOM 2463 CG2 VAL A 342 18.932 91.747 98.651 1.00 52.45 C ANISOU 2463 CG2 VAL A 342 6242 7141 6546 -234 201 -684 C ATOM 2464 N ALA A 343 15.989 89.034 96.337 1.00 54.37 N ANISOU 2464 N ALA A 343 6437 7434 6789 -212 108 -724 N ATOM 2465 CA ALA A 343 14.929 88.060 96.105 1.00 50.56 C ANISOU 2465 CA ALA A 343 5929 6920 6361 -232 38 -735 C ATOM 2466 C ALA A 343 15.414 86.913 95.227 1.00 53.72 C ANISOU 2466 C ALA A 343 6387 7314 6708 -219 -31 -802 C ATOM 2467 O ALA A 343 15.094 85.748 95.488 1.00 51.97 O ANISOU 2467 O ALA A 343 6159 7038 6550 -243 -80 -828 O ATOM 2468 CB ALA A 343 13.716 88.746 95.477 1.00 41.43 C ANISOU 2468 CB ALA A 343 4720 5762 5259 -236 -13 -691 C ATOM 2469 N ILE A 344 16.193 87.220 94.187 1.00 54.03 N ANISOU 2469 N ILE A 344 6490 7402 6638 -176 -23 -827 N ATOM 2470 CA ILE A 344 16.660 86.175 93.281 1.00 53.48 C ANISOU 2470 CA ILE A 344 6504 7323 6492 -139 -62 -910 C ATOM 2471 C ILE A 344 17.624 85.236 93.996 1.00 65.49 C ANISOU 2471 C ILE A 344 8020 8803 8060 -127 -10 -941 C ATOM 2472 O ILE A 344 17.532 84.010 93.859 1.00 79.08 O ANISOU 2472 O ILE A 344 9776 10460 9812 -124 -67 -1008 O ATOM 2473 CB ILE A 344 17.296 86.799 92.026 1.00 53.09 C ANISOU 2473 CB ILE A 344 6534 7347 6293 -78 -21 -910 C ATOM 2474 CG1 ILE A 344 16.230 87.500 91.186 1.00 61.05 C ANISOU 2474 CG1 ILE A 344 7564 8383 7249 -92 -119 -875 C ATOM 2475 CG2 ILE A 344 18.006 85.738 91.201 1.00 49.77 C ANISOU 2475 CG2 ILE A 344 6223 6916 5773 -13 -7 -1008 C ATOM 2476 CD1 ILE A 344 16.781 88.209 89.970 1.00 64.29 C ANISOU 2476 CD1 ILE A 344 8063 8875 7491 -33 -74 -844 C ATOM 2477 N VAL A 345 18.557 85.792 94.774 1.00 61.39 N ANISOU 2477 N VAL A 345 7457 8304 7565 -125 77 -888 N ATOM 2478 CA VAL A 345 19.501 84.958 95.513 1.00 53.77 C ANISOU 2478 CA VAL A 345 6471 7294 6663 -118 103 -892 C ATOM 2479 C VAL A 345 18.763 84.068 96.504 1.00 50.94 C ANISOU 2479 C VAL A 345 6092 6871 6394 -170 44 -886 C ATOM 2480 O VAL A 345 19.087 82.884 96.658 1.00 56.13 O ANISOU 2480 O VAL A 345 6754 7464 7110 -162 18 -915 O ATOM 2481 CB VAL A 345 20.559 85.832 96.212 1.00 48.20 C ANISOU 2481 CB VAL A 345 5717 6612 5984 -123 162 -822 C ATOM 2482 CG1 VAL A 345 21.261 85.051 97.314 1.00 52.66 C ANISOU 2482 CG1 VAL A 345 6253 7123 6634 -141 142 -799 C ATOM 2483 CG2 VAL A 345 21.569 86.346 95.200 1.00 44.26 C ANISOU 2483 CG2 VAL A 345 5213 6157 5447 -63 242 -805 C ATOM 2484 N PHE A 346 17.752 84.617 97.180 1.00 44.87 N ANISOU 2484 N PHE A 346 5291 6109 5647 -218 37 -837 N ATOM 2485 CA PHE A 346 17.005 83.828 98.154 1.00 46.30 C ANISOU 2485 CA PHE A 346 5443 6236 5915 -264 14 -799 C ATOM 2486 C PHE A 346 16.291 82.659 97.487 1.00 55.85 C ANISOU 2486 C PHE A 346 6647 7375 7200 -277 -76 -842 C ATOM 2487 O PHE A 346 16.176 81.577 98.073 1.00 66.54 O ANISOU 2487 O PHE A 346 7979 8655 8648 -304 -106 -820 O ATOM 2488 CB PHE A 346 16.008 84.719 98.894 1.00 42.74 C ANISOU 2488 CB PHE A 346 4958 5807 5474 -292 64 -735 C ATOM 2489 CG PHE A 346 15.299 84.031 100.026 1.00 41.82 C ANISOU 2489 CG PHE A 346 4809 5647 5432 -328 90 -665 C ATOM 2490 CD1 PHE A 346 14.098 83.374 99.814 1.00 46.81 C ANISOU 2490 CD1 PHE A 346 5370 6228 6188 -359 52 -631 C ATOM 2491 CD2 PHE A 346 15.827 84.051 101.306 1.00 47.72 C ANISOU 2491 CD2 PHE A 346 5599 6402 6128 -335 145 -617 C ATOM 2492 CE1 PHE A 346 13.440 82.745 100.854 1.00 50.18 C ANISOU 2492 CE1 PHE A 346 5751 6614 6702 -392 102 -534 C ATOM 2493 CE2 PHE A 346 15.174 83.424 102.353 1.00 50.82 C ANISOU 2493 CE2 PHE A 346 5979 6766 6563 -361 192 -530 C ATOM 2494 CZ PHE A 346 13.979 82.770 102.126 1.00 49.62 C ANISOU 2494 CZ PHE A 346 5737 6566 6549 -388 188 -480 C ATOM 2495 N VAL A 347 15.819 82.851 96.257 1.00 50.93 N ANISOU 2495 N VAL A 347 6051 6761 6538 -262 -140 -901 N ATOM 2496 CA VAL A 347 15.063 81.802 95.577 1.00 54.98 C ANISOU 2496 CA VAL A 347 6578 7188 7124 -284 -271 -956 C ATOM 2497 C VAL A 347 15.998 80.735 95.019 1.00 61.17 C ANISOU 2497 C VAL A 347 7448 7915 7881 -235 -297 -1061 C ATOM 2498 O VAL A 347 15.913 79.558 95.386 1.00 58.55 O ANISOU 2498 O VAL A 347 7100 7476 7670 -257 -352 -1074 O ATOM 2499 CB VAL A 347 14.170 82.407 94.479 1.00 51.89 C ANISOU 2499 CB VAL A 347 6205 6822 6689 -290 -366 -978 C ATOM 2500 CG1 VAL A 347 13.549 81.308 93.634 1.00 56.42 C ANISOU 2500 CG1 VAL A 347 6828 7293 7317 -313 -547 -1062 C ATOM 2501 CG2 VAL A 347 13.085 83.267 95.104 1.00 55.03 C ANISOU 2501 CG2 VAL A 347 6486 7241 7183 -334 -342 -864 C ATOM 2502 N ILE A 348 16.916 81.130 94.132 1.00 59.73 N ANISOU 2502 N ILE A 348 7351 7792 7553 -159 -241 -1128 N ATOM 2503 CA ILE A 348 17.742 80.155 93.427 1.00 59.47 C ANISOU 2503 CA ILE A 348 7413 7699 7484 -86 -238 -1243 C ATOM 2504 C ILE A 348 18.725 79.422 94.330 1.00 62.40 C ANISOU 2504 C ILE A 348 7730 8013 7967 -67 -169 -1214 C ATOM 2505 O ILE A 348 19.359 78.462 93.880 1.00 65.66 O ANISOU 2505 O ILE A 348 8201 8346 8402 -2 -163 -1305 O ATOM 2506 CB ILE A 348 18.511 80.832 92.275 1.00 62.33 C ANISOU 2506 CB ILE A 348 7874 8151 7656 5 -148 -1294 C ATOM 2507 CG1 ILE A 348 19.590 81.760 92.834 1.00 66.12 C ANISOU 2507 CG1 ILE A 348 8274 8717 8133 29 8 -1193 C ATOM 2508 CG2 ILE A 348 17.547 81.591 91.371 1.00 60.82 C ANISOU 2508 CG2 ILE A 348 7746 8019 7343 -16 -237 -1301 C ATOM 2509 CD1 ILE A 348 20.428 82.438 91.772 1.00 70.01 C ANISOU 2509 CD1 ILE A 348 8830 9294 8474 118 129 -1201 C ATOM 2510 N CYS A 349 18.873 79.840 95.586 1.00 60.97 N ANISOU 2510 N CYS A 349 7450 7862 7853 -116 -124 -1093 N ATOM 2511 CA CYS A 349 19.760 79.155 96.521 1.00 61.12 C ANISOU 2511 CA CYS A 349 7419 7826 7980 -109 -94 -1041 C ATOM 2512 C CYS A 349 19.031 78.193 97.447 1.00 67.60 C ANISOU 2512 C CYS A 349 8194 8549 8941 -180 -174 -982 C ATOM 2513 O CYS A 349 19.533 77.096 97.706 1.00 80.04 O ANISOU 2513 O CYS A 349 9758 10022 10631 -162 -200 -985 O ATOM 2514 CB CYS A 349 20.537 80.169 97.369 1.00 59.64 C ANISOU 2514 CB CYS A 349 7177 7722 7762 -119 -20 -939 C ATOM 2515 SG CYS A 349 21.852 81.052 96.496 1.00 58.08 S ANISOU 2515 SG CYS A 349 6981 7599 7486 -35 90 -957 S ATOM 2516 N PHE A 350 17.855 78.570 97.952 1.00 62.88 N ANISOU 2516 N PHE A 350 7559 7976 8358 -253 -200 -913 N ATOM 2517 CA PHE A 350 17.194 77.802 98.997 1.00 59.02 C ANISOU 2517 CA PHE A 350 7009 7412 8002 -320 -234 -809 C ATOM 2518 C PHE A 350 15.904 77.123 98.560 1.00 58.06 C ANISOU 2518 C PHE A 350 6856 7197 8009 -372 -337 -823 C ATOM 2519 O PHE A 350 15.522 76.120 99.171 1.00 65.19 O ANISOU 2519 O PHE A 350 7704 7994 9071 -419 -381 -748 O ATOM 2520 CB PHE A 350 16.902 78.706 100.204 1.00 57.63 C ANISOU 2520 CB PHE A 350 6804 7327 7766 -357 -148 -683 C ATOM 2521 CG PHE A 350 18.124 79.391 100.750 1.00 62.96 C ANISOU 2521 CG PHE A 350 7513 8073 8336 -326 -92 -663 C ATOM 2522 CD1 PHE A 350 19.306 78.691 100.926 1.00 62.18 C ANISOU 2522 CD1 PHE A 350 7416 7925 8287 -296 -118 -660 C ATOM 2523 CD2 PHE A 350 18.096 80.740 101.066 1.00 69.19 C ANISOU 2523 CD2 PHE A 350 8323 8961 9004 -326 -29 -646 C ATOM 2524 CE1 PHE A 350 20.434 79.318 101.423 1.00 69.17 C ANISOU 2524 CE1 PHE A 350 8309 8860 9112 -278 -99 -625 C ATOM 2525 CE2 PHE A 350 19.221 81.373 101.563 1.00 68.85 C ANISOU 2525 CE2 PHE A 350 8309 8961 8891 -311 -15 -629 C ATOM 2526 CZ PHE A 350 20.391 80.662 101.741 1.00 70.27 C ANISOU 2526 CZ PHE A 350 8476 9093 9130 -292 -58 -612 C ATOM 2527 N LEU A 351 15.235 77.625 97.527 1.00 55.40 N ANISOU 2527 N LEU A 351 6542 6884 7622 -371 -394 -900 N ATOM 2528 CA LEU A 351 13.989 77.025 97.061 1.00 60.99 C ANISOU 2528 CA LEU A 351 7209 7489 8476 -433 -536 -908 C ATOM 2529 C LEU A 351 14.189 75.659 96.402 1.00 58.75 C ANISOU 2529 C LEU A 351 6986 7043 8291 -425 -674 -1024 C ATOM 2530 O LEU A 351 13.390 74.749 96.661 1.00 53.95 O ANISOU 2530 O LEU A 351 6305 6299 7894 -497 -782 -972 O ATOM 2531 CB LEU A 351 13.270 77.964 96.090 1.00 66.26 C ANISOU 2531 CB LEU A 351 7896 8222 9059 -434 -594 -954 C ATOM 2532 CG LEU A 351 11.917 77.470 95.571 1.00 69.63 C ANISOU 2532 CG LEU A 351 8261 8537 9657 -510 -781 -947 C ATOM 2533 CD1 LEU A 351 10.936 77.281 96.718 1.00 68.72 C ANISOU 2533 CD1 LEU A 351 7967 8378 9764 -587 -737 -760 C ATOM 2534 CD2 LEU A 351 11.357 78.428 94.533 1.00 72.58 C ANISOU 2534 CD2 LEU A 351 8671 8980 9927 -503 -863 -990 C ATOM 2535 N PRO A 352 15.201 75.464 95.537 1.00 58.50 N ANISOU 2535 N PRO A 352 7086 7008 8133 -336 -669 -1178 N ATOM 2536 CA PRO A 352 15.340 74.143 94.895 1.00 64.28 C ANISOU 2536 CA PRO A 352 7899 7563 8961 -314 -796 -1313 C ATOM 2537 C PRO A 352 15.467 72.992 95.879 1.00 65.71 C ANISOU 2537 C PRO A 352 7993 7603 9372 -352 -812 -1225 C ATOM 2538 O PRO A 352 14.868 71.930 95.664 1.00 57.46 O ANISOU 2538 O PRO A 352 6944 6377 8512 -400 -970 -1264 O ATOM 2539 CB PRO A 352 16.607 74.306 94.043 1.00 61.92 C ANISOU 2539 CB PRO A 352 7742 7315 8468 -184 -698 -1460 C ATOM 2540 CG PRO A 352 16.666 75.747 93.748 1.00 53.16 C ANISOU 2540 CG PRO A 352 6644 6395 7158 -164 -603 -1426 C ATOM 2541 CD PRO A 352 16.187 76.418 94.996 1.00 52.73 C ANISOU 2541 CD PRO A 352 6438 6416 7180 -246 -546 -1240 C ATOM 2542 N SER A 353 16.230 73.170 96.959 1.00 67.21 N ANISOU 2542 N SER A 353 8116 7859 9561 -337 -672 -1097 N ATOM 2543 CA SER A 353 16.336 72.110 97.955 1.00 62.36 C ANISOU 2543 CA SER A 353 7421 7118 9154 -376 -691 -979 C ATOM 2544 C SER A 353 15.017 71.894 98.685 1.00 57.89 C ANISOU 2544 C SER A 353 6734 6506 8756 -494 -745 -815 C ATOM 2545 O SER A 353 14.715 70.767 99.094 1.00 58.50 O ANISOU 2545 O SER A 353 6750 6419 9060 -545 -825 -742 O ATOM 2546 CB SER A 353 17.450 72.434 98.949 1.00 64.81 C ANISOU 2546 CB SER A 353 7703 7521 9402 -338 -557 -868 C ATOM 2547 OG SER A 353 17.615 71.388 99.888 1.00 69.63 O ANISOU 2547 OG SER A 353 8247 8009 10200 -371 -587 -739 O ATOM 2548 N VAL A 354 14.216 72.950 98.845 1.00 57.62 N ANISOU 2548 N VAL A 354 6652 6603 8638 -534 -692 -743 N ATOM 2549 CA VAL A 354 12.936 72.821 99.538 1.00 59.83 C ANISOU 2549 CA VAL A 354 6794 6845 9093 -631 -701 -567 C ATOM 2550 C VAL A 354 11.960 71.994 98.710 1.00 63.79 C ANISOU 2550 C VAL A 354 7254 7166 9816 -698 -909 -624 C ATOM 2551 O VAL A 354 11.270 71.111 99.233 1.00 64.02 O ANISOU 2551 O VAL A 354 7164 7054 10106 -778 -970 -489 O ATOM 2552 CB VAL A 354 12.361 74.212 99.864 1.00 48.79 C ANISOU 2552 CB VAL A 354 5355 5621 7561 -635 -574 -489 C ATOM 2553 CG1 VAL A 354 10.898 74.104 100.264 1.00 49.61 C ANISOU 2553 CG1 VAL A 354 5298 5671 7878 -721 -583 -326 C ATOM 2554 CG2 VAL A 354 13.165 74.869 100.972 1.00 42.97 C ANISOU 2554 CG2 VAL A 354 4654 5023 6651 -594 -394 -402 C ATOM 2555 N VAL A 355 11.887 72.268 97.406 1.00 62.92 N ANISOU 2555 N VAL A 355 7246 7052 9609 -669 -1034 -816 N ATOM 2556 CA VAL A 355 10.980 71.523 96.537 1.00 65.63 C ANISOU 2556 CA VAL A 355 7582 7213 10142 -736 -1281 -895 C ATOM 2557 C VAL A 355 11.351 70.045 96.520 1.00 65.33 C ANISOU 2557 C VAL A 355 7577 6951 10294 -745 -1400 -956 C ATOM 2558 O VAL A 355 10.478 69.170 96.572 1.00 59.78 O ANISOU 2558 O VAL A 355 6775 6056 9884 -843 -1568 -893 O ATOM 2559 CB VAL A 355 10.980 72.127 95.121 1.00 63.42 C ANISOU 2559 CB VAL A 355 7460 6986 9653 -689 -1397 -1102 C ATOM 2560 CG1 VAL A 355 10.145 71.277 94.175 1.00 62.99 C ANISOU 2560 CG1 VAL A 355 7443 6723 9768 -757 -1701 -1215 C ATOM 2561 CG2 VAL A 355 10.459 73.555 95.157 1.00 61.94 C ANISOU 2561 CG2 VAL A 355 7208 6987 9338 -693 -1304 -1013 C ATOM 2562 N VAL A 356 12.649 69.743 96.461 1.00 62.42 N ANISOU 2562 N VAL A 356 7332 6588 9798 -642 -1314 -1068 N ATOM 2563 CA VAL A 356 13.079 68.348 96.452 1.00 58.88 C ANISOU 2563 CA VAL A 356 6915 5911 9544 -631 -1412 -1130 C ATOM 2564 C VAL A 356 12.739 67.674 97.776 1.00 55.81 C ANISOU 2564 C VAL A 356 6345 5437 9424 -718 -1376 -872 C ATOM 2565 O VAL A 356 12.280 66.526 97.799 1.00 61.16 O ANISOU 2565 O VAL A 356 6966 5880 10393 -786 -1535 -846 O ATOM 2566 CB VAL A 356 14.581 68.248 96.130 1.00 57.22 C ANISOU 2566 CB VAL A 356 6850 5731 9159 -485 -1296 -1283 C ATOM 2567 CG1 VAL A 356 15.058 66.813 96.279 1.00 66.91 C ANISOU 2567 CG1 VAL A 356 8087 6713 10625 -464 -1372 -1321 C ATOM 2568 CG2 VAL A 356 14.852 68.749 94.722 1.00 56.81 C ANISOU 2568 CG2 VAL A 356 6995 5738 8853 -395 -1327 -1533 C ATOM 2569 N ARG A 357 12.940 68.373 98.896 1.00 53.70 N ANISOU 2569 N ARG A 357 5994 5351 9061 -719 -1173 -673 N ATOM 2570 CA ARG A 357 12.579 67.797 100.188 1.00 60.95 C ANISOU 2570 CA ARG A 357 6762 6211 10186 -795 -1117 -405 C ATOM 2571 C ARG A 357 11.075 67.580 100.311 1.00 70.89 C ANISOU 2571 C ARG A 357 7859 7377 11699 -920 -1205 -256 C ATOM 2572 O ARG A 357 10.642 66.648 100.997 1.00 76.83 O ANISOU 2572 O ARG A 357 8486 7977 12730 -997 -1237 -69 O ATOM 2573 CB ARG A 357 13.078 68.681 101.330 1.00 61.32 C ANISOU 2573 CB ARG A 357 6796 6479 10021 -762 -890 -243 C ATOM 2574 CG ARG A 357 14.583 68.636 101.542 1.00 71.75 C ANISOU 2574 CG ARG A 357 8218 7847 11196 -665 -825 -304 C ATOM 2575 CD ARG A 357 14.946 69.015 102.970 1.00 85.25 C ANISOU 2575 CD ARG A 357 9900 9690 12799 -672 -673 -82 C ATOM 2576 NE ARG A 357 16.390 69.028 103.189 1.00 97.49 N ANISOU 2576 NE ARG A 357 11525 11279 14238 -589 -643 -121 N ATOM 2577 CZ ARG A 357 16.964 69.150 104.381 1.00107.13 C ANISOU 2577 CZ ARG A 357 12749 12578 15376 -590 -572 54 C ATOM 2578 NH1 ARG A 357 16.216 69.266 105.470 1.00117.46 N ANISOU 2578 NH1 ARG A 357 14019 13946 16665 -656 -495 272 N ATOM 2579 NH2 ARG A 357 18.286 69.153 104.486 1.00105.77 N ANISOU 2579 NH2 ARG A 357 12622 12423 15143 -520 -579 19 N ATOM 2580 N ILE A 358 10.267 68.422 99.663 1.00 69.73 N ANISOU 2580 N ILE A 358 7694 7310 11489 -943 -1245 -314 N ATOM 2581 CA ILE A 358 8.823 68.211 99.677 1.00 67.50 C ANISOU 2581 CA ILE A 358 7228 6920 11498 -1062 -1351 -168 C ATOM 2582 C ILE A 358 8.457 66.988 98.847 1.00 62.82 C ANISOU 2582 C ILE A 358 6637 6038 11191 -1130 -1652 -283 C ATOM 2583 O ILE A 358 7.583 66.199 99.228 1.00 61.43 O ANISOU 2583 O ILE A 358 6283 5681 11375 -1243 -1748 -103 O ATOM 2584 CB ILE A 358 8.093 69.475 99.186 1.00 51.51 C ANISOU 2584 CB ILE A 358 5174 5051 9347 -1062 -1330 -192 C ATOM 2585 CG1 ILE A 358 8.175 70.577 100.242 1.00 82.31 C ANISOU 2585 CG1 ILE A 358 9032 9188 13055 -1015 -1029 -29 C ATOM 2586 CG2 ILE A 358 6.641 69.168 98.853 1.00 53.70 C ANISOU 2586 CG2 ILE A 358 5263 5174 9968 -1184 -1516 -87 C ATOM 2587 CD1 ILE A 358 7.397 71.820 99.881 1.00 49.19 C ANISOU 2587 CD1 ILE A 358 4781 5126 8784 -1010 -987 -23 C ATOM 2588 N ARG A 359 9.126 66.802 97.707 1.00 66.31 N ANISOU 2588 N ARG A 359 7288 6423 11483 -1061 -1801 -581 N ATOM 2589 CA ARG A 359 8.870 65.629 96.880 1.00 75.67 C ANISOU 2589 CA ARG A 359 8530 7316 12904 -1110 -2099 -737 C ATOM 2590 C ARG A 359 9.236 64.340 97.605 1.00 75.82 C ANISOU 2590 C ARG A 359 8486 7126 13196 -1135 -2109 -632 C ATOM 2591 O ARG A 359 8.581 63.310 97.409 1.00 81.63 O ANISOU 2591 O ARG A 359 9147 7586 14281 -1234 -2342 -615 O ATOM 2592 CB ARG A 359 9.636 65.749 95.560 1.00 87.88 C ANISOU 2592 CB ARG A 359 10356 8866 14166 -998 -2201 -1088 C ATOM 2593 CG ARG A 359 9.489 64.558 94.624 1.00106.27 C ANISOU 2593 CG ARG A 359 12814 10888 16677 -1022 -2511 -1308 C ATOM 2594 CD ARG A 359 9.661 64.976 93.168 1.00121.42 C ANISOU 2594 CD ARG A 359 15002 12841 18292 -944 -2652 -1624 C ATOM 2595 NE ARG A 359 10.960 65.593 92.905 1.00129.57 N ANISOU 2595 NE ARG A 359 16217 14076 18937 -772 -2406 -1766 N ATOM 2596 CZ ARG A 359 11.949 65.007 92.236 1.00135.18 C ANISOU 2596 CZ ARG A 359 17155 14692 19517 -640 -2399 -2016 C ATOM 2597 NH1 ARG A 359 11.792 63.782 91.752 1.00140.88 N ANISOU 2597 NH1 ARG A 359 17977 15108 20443 -658 -2635 -2181 N ATOM 2598 NH2 ARG A 359 13.094 65.649 92.044 1.00130.64 N ANISOU 2598 NH2 ARG A 359 16701 14312 18626 -488 -2150 -2099 N ATOM 2599 N ILE A 360 10.266 64.376 98.455 1.00 73.41 N ANISOU 2599 N ILE A 360 8202 6934 12758 -1053 -1879 -548 N ATOM 2600 CA ILE A 360 10.635 63.189 99.219 1.00 74.13 C ANISOU 2600 CA ILE A 360 8223 6834 13109 -1074 -1884 -412 C ATOM 2601 C ILE A 360 9.605 62.914 100.309 1.00 73.30 C ANISOU 2601 C ILE A 360 7868 6685 13297 -1208 -1839 -54 C ATOM 2602 O ILE A 360 9.291 61.755 100.608 1.00 86.02 O ANISOU 2602 O ILE A 360 9372 8042 15268 -1288 -1963 69 O ATOM 2603 CB ILE A 360 12.054 63.342 99.796 1.00 80.67 C ANISOU 2603 CB ILE A 360 9143 7797 13713 -949 -1677 -411 C ATOM 2604 CG1 ILE A 360 13.071 63.543 98.671 1.00 56.31 C ANISOU 2604 CG1 ILE A 360 6279 4734 10382 -808 -1697 -746 C ATOM 2605 CG2 ILE A 360 12.435 62.123 100.620 1.00 58.43 C ANISOU 2605 CG2 ILE A 360 6246 4780 11175 -971 -1695 -243 C ATOM 2606 CD1 ILE A 360 14.504 63.653 99.147 1.00 55.02 C ANISOU 2606 CD1 ILE A 360 6175 4674 10056 -684 -1515 -743 C ATOM 2607 N PHE A 361 9.060 63.972 100.919 1.00 62.66 N ANISOU 2607 N PHE A 361 6422 5575 11811 -1227 -1646 126 N ATOM 2608 CA PHE A 361 7.996 63.793 101.905 1.00 67.74 C ANISOU 2608 CA PHE A 361 6825 6191 12721 -1339 -1561 474 C ATOM 2609 C PHE A 361 6.802 63.068 101.300 1.00 73.01 C ANISOU 2609 C PHE A 361 7337 6592 13812 -1474 -1828 503 C ATOM 2610 O PHE A 361 6.147 62.262 101.972 1.00 66.70 O ANISOU 2610 O PHE A 361 6337 5626 13378 -1578 -1843 774 O ATOM 2611 CB PHE A 361 7.562 65.148 102.465 1.00 64.75 C ANISOU 2611 CB PHE A 361 6394 6102 12108 -1314 -1308 607 C ATOM 2612 CG PHE A 361 8.562 65.771 103.392 1.00 63.71 C ANISOU 2612 CG PHE A 361 6377 6204 11627 -1213 -1049 663 C ATOM 2613 CD1 PHE A 361 9.347 64.984 104.217 1.00 62.85 C ANISOU 2613 CD1 PHE A 361 6298 6037 11544 -1197 -998 786 C ATOM 2614 CD2 PHE A 361 8.717 67.147 103.440 1.00 63.83 C ANISOU 2614 CD2 PHE A 361 6471 6480 11302 -1140 -879 599 C ATOM 2615 CE1 PHE A 361 10.269 65.557 105.073 1.00 69.94 C ANISOU 2615 CE1 PHE A 361 7309 7140 12125 -1114 -803 841 C ATOM 2616 CE2 PHE A 361 9.638 67.727 104.293 1.00 61.77 C ANISOU 2616 CE2 PHE A 361 6326 6413 10732 -1058 -679 641 C ATOM 2617 CZ PHE A 361 10.415 66.930 105.109 1.00 67.26 C ANISOU 2617 CZ PHE A 361 7056 7053 11447 -1048 -651 761 C ATOM 2618 N TRP A 362 6.506 63.340 100.028 1.00 78.35 N ANISOU 2618 N TRP A 362 8103 7219 14449 -1479 -2054 239 N ATOM 2619 CA TRP A 362 5.377 62.691 99.372 1.00 83.45 C ANISOU 2619 CA TRP A 362 8615 7597 15494 -1616 -2366 244 C ATOM 2620 C TRP A 362 5.685 61.229 99.068 1.00 83.26 C ANISOU 2620 C TRP A 362 8643 7234 15757 -1657 -2615 144 C ATOM 2621 O TRP A 362 4.854 60.347 99.315 1.00 86.94 O ANISOU 2621 O TRP A 362 8907 7446 16681 -1794 -2773 334 O ATOM 2622 CB TRP A 362 5.014 63.450 98.095 1.00 89.70 C ANISOU 2622 CB TRP A 362 9523 8444 16117 -1605 -2560 -12 C ATOM 2623 CG TRP A 362 3.840 62.880 97.366 1.00102.76 C ANISOU 2623 CG TRP A 362 11051 9826 18165 -1754 -2928 -17 C ATOM 2624 CD1 TRP A 362 3.858 62.220 96.171 1.00109.20 C ANISOU 2624 CD1 TRP A 362 12047 10410 19034 -1776 -3298 -312 C ATOM 2625 CD2 TRP A 362 2.471 62.913 97.786 1.00112.42 C ANISOU 2625 CD2 TRP A 362 11950 10984 19782 -1889 -2963 294 C ATOM 2626 NE1 TRP A 362 2.584 61.842 95.820 1.00116.37 N ANISOU 2626 NE1 TRP A 362 12815 11199 20201 -1842 -3510 -187 N ATOM 2627 CE2 TRP A 362 1.714 62.255 96.795 1.00119.61 C ANISOU 2627 CE2 TRP A 362 12905 11702 20841 -1909 -3311 187 C ATOM 2628 CE3 TRP A 362 1.811 63.434 98.903 1.00115.72 C ANISOU 2628 CE3 TRP A 362 12087 11541 20340 -1926 -2669 662 C ATOM 2629 CZ2 TRP A 362 0.332 62.106 96.888 1.00126.15 C ANISOU 2629 CZ2 TRP A 362 13482 12456 21995 -1975 -3398 443 C ATOM 2630 CZ3 TRP A 362 0.439 63.284 98.993 1.00123.81 C ANISOU 2630 CZ3 TRP A 362 12868 12496 21679 -1977 -2726 909 C ATOM 2631 CH2 TRP A 362 -0.286 62.625 97.992 1.00127.67 C ANISOU 2631 CH2 TRP A 362 13385 12778 22346 -2004 -3097 803 C ATOM 2632 N LEU A 363 6.882 60.952 98.543 1.00 77.77 N ANISOU 2632 N LEU A 363 8210 6517 14823 -1535 -2644 -146 N ATOM 2633 CA LEU A 363 7.226 59.583 98.171 1.00 78.79 C ANISOU 2633 CA LEU A 363 8417 6305 15216 -1550 -2877 -283 C ATOM 2634 C LEU A 363 7.339 58.673 99.387 1.00 86.00 C ANISOU 2634 C LEU A 363 9150 7087 16439 -1601 -2771 31 C ATOM 2635 O LEU A 363 7.006 57.485 99.300 1.00 99.45 O ANISOU 2635 O LEU A 363 10782 8456 18550 -1689 -2998 62 O ATOM 2636 CB LEU A 363 8.526 59.567 97.369 1.00 76.42 C ANISOU 2636 CB LEU A 363 8431 6030 14578 -1378 -2871 -651 C ATOM 2637 CG LEU A 363 8.424 60.154 95.960 1.00 84.70 C ANISOU 2637 CG LEU A 363 9704 7124 15354 -1329 -3042 -996 C ATOM 2638 CD1 LEU A 363 9.786 60.182 95.290 1.00 83.59 C ANISOU 2638 CD1 LEU A 363 9859 7037 14866 -1138 -2952 -1314 C ATOM 2639 CD2 LEU A 363 7.427 59.364 95.124 1.00 96.85 C ANISOU 2639 CD2 LEU A 363 11244 8333 17220 -1459 -3454 -1114 C ATOM 2640 N LEU A 364 7.810 59.198 100.521 1.00 81.20 N ANISOU 2640 N LEU A 364 8482 6732 15639 -1546 -2442 267 N ATOM 2641 CA LEU A 364 7.819 58.401 101.744 1.00 86.31 C ANISOU 2641 CA LEU A 364 8960 7280 16555 -1602 -2334 613 C ATOM 2642 C LEU A 364 6.401 58.087 102.200 1.00 91.78 C ANISOU 2642 C LEU A 364 9362 7845 17667 -1774 -2387 938 C ATOM 2643 O LEU A 364 6.136 56.999 102.726 1.00 94.68 O ANISOU 2643 O LEU A 364 9582 7973 18418 -1856 -2457 1161 O ATOM 2644 CB LEU A 364 8.585 59.132 102.846 1.00 82.54 C ANISOU 2644 CB LEU A 364 8513 7119 15729 -1508 -1990 788 C ATOM 2645 CG LEU A 364 10.108 59.149 102.736 1.00 76.39 C ANISOU 2645 CG LEU A 364 7952 6413 14660 -1353 -1925 581 C ATOM 2646 CD1 LEU A 364 10.708 60.037 103.814 1.00 72.84 C ANISOU 2646 CD1 LEU A 364 7526 6286 13864 -1284 -1626 762 C ATOM 2647 CD2 LEU A 364 10.657 57.736 102.837 1.00 75.42 C ANISOU 2647 CD2 LEU A 364 7827 5976 14854 -1354 -2069 595 C ATOM 2648 N HIS A 365 5.479 59.028 102.002 1.00 89.17 N ANISOU 2648 N HIS A 365 8932 7672 17277 -1818 -2345 984 N ATOM 2649 CA HIS A 365 4.087 58.817 102.376 1.00 89.24 C ANISOU 2649 CA HIS A 365 8651 7598 17657 -1943 -2363 1296 C ATOM 2650 C HIS A 365 3.333 58.002 101.331 1.00 90.69 C ANISOU 2650 C HIS A 365 8833 7547 18077 -1961 -2724 1142 C ATOM 2651 O HIS A 365 2.367 57.309 101.671 1.00 85.04 O ANISOU 2651 O HIS A 365 7907 6711 17695 -2012 -2778 1397 O ATOM 2652 CB HIS A 365 3.410 60.171 102.600 1.00 81.18 C ANISOU 2652 CB HIS A 365 7516 6845 16483 -1956 -2153 1416 C ATOM 2653 CG HIS A 365 1.935 60.083 102.830 1.00 92.57 C ANISOU 2653 CG HIS A 365 8691 8262 18217 -2008 -2142 1697 C ATOM 2654 ND1 HIS A 365 1.011 60.461 101.880 1.00 96.10 N ANISOU 2654 ND1 HIS A 365 9092 8686 18735 -2024 -2348 1581 N ATOM 2655 CD2 HIS A 365 1.222 59.666 103.903 1.00 98.31 C ANISOU 2655 CD2 HIS A 365 9188 8986 19178 -2031 -1944 2098 C ATOM 2656 CE1 HIS A 365 -0.207 60.279 102.356 1.00101.77 C ANISOU 2656 CE1 HIS A 365 9546 9373 19749 -2056 -2283 1899 C ATOM 2657 NE2 HIS A 365 -0.107 59.796 103.582 1.00101.14 N ANISOU 2657 NE2 HIS A 365 9351 9309 19768 -2056 -2028 2211 N ATOM 2658 N THR A 366 3.764 58.053 100.070 1.00 92.27 N ANISOU 2658 N THR A 366 9274 7679 18104 -1914 -2972 735 N ATOM 2659 CA THR A 366 3.078 57.362 98.984 1.00 90.94 C ANISOU 2659 CA THR A 366 9153 7302 18099 -1927 -3331 560 C ATOM 2660 C THR A 366 3.621 55.954 98.752 1.00 96.35 C ANISOU 2660 C THR A 366 9947 7711 18950 -1894 -3519 433 C ATOM 2661 O THR A 366 2.847 54.996 98.660 1.00100.46 O ANISOU 2661 O THR A 366 10342 8022 19805 -1942 -3719 542 O ATOM 2662 CB THR A 366 3.183 58.180 97.690 1.00 92.04 C ANISOU 2662 CB THR A 366 9524 7529 17919 -1883 -3497 194 C ATOM 2663 OG1 THR A 366 2.412 59.381 97.816 1.00 95.12 O ANISOU 2663 OG1 THR A 366 9768 8136 18239 -1924 -3379 339 O ATOM 2664 CG2 THR A 366 2.676 57.376 96.502 1.00 97.79 C ANISOU 2664 CG2 THR A 366 10373 8028 18754 -1884 -3884 -26 C ATOM 2665 N SER A 367 4.945 55.810 98.654 1.00 95.90 N ANISOU 2665 N SER A 367 10112 7639 18686 -1804 -3457 206 N ATOM 2666 CA SER A 367 5.552 54.537 98.295 1.00 97.17 C ANISOU 2666 CA SER A 367 10407 7538 18975 -1746 -3629 32 C ATOM 2667 C SER A 367 6.220 53.813 99.455 1.00101.56 C ANISOU 2667 C SER A 367 10855 8020 19711 -1736 -3453 276 C ATOM 2668 O SER A 367 6.467 52.608 99.343 1.00107.29 O ANISOU 2668 O SER A 367 11607 8503 20655 -1709 -3601 228 O ATOM 2669 CB SER A 367 6.587 54.738 97.178 1.00 90.92 C ANISOU 2669 CB SER A 367 9968 6741 17837 -1618 -3707 -433 C ATOM 2670 OG SER A 367 5.965 55.164 95.978 1.00 82.23 O ANISOU 2670 OG SER A 367 9006 5667 16572 -1620 -3924 -672 O ATOM 2671 N GLY A 368 6.516 54.501 100.554 1.00 96.09 N ANISOU 2671 N GLY A 368 10052 7530 18930 -1757 -3152 541 N ATOM 2672 CA GLY A 368 7.156 53.817 101.659 1.00 99.00 C ANISOU 2672 CA GLY A 368 10337 7835 19442 -1746 -3000 795 C ATOM 2673 C GLY A 368 8.628 53.541 101.385 1.00 98.37 C ANISOU 2673 C GLY A 368 10488 7674 19216 -1622 -2993 530 C ATOM 2674 O GLY A 368 9.268 54.166 100.534 1.00 97.71 O ANISOU 2674 O GLY A 368 10625 7652 18850 -1538 -3012 181 O ATOM 2675 N THR A 369 9.167 52.571 102.128 1.00103.59 N ANISOU 2675 N THR A 369 11085 8191 20082 -1600 -2958 713 N ATOM 2676 CA THR A 369 10.586 52.239 102.052 1.00106.16 C ANISOU 2676 CA THR A 369 11583 8427 20327 -1472 -2923 532 C ATOM 2677 C THR A 369 10.809 50.756 101.772 1.00111.56 C ANISOU 2677 C THR A 369 12276 8805 21305 -1421 -3114 454 C ATOM 2678 O THR A 369 11.840 50.198 102.158 1.00113.68 O ANISOU 2678 O THR A 369 12580 8976 21637 -1334 -3056 477 O ATOM 2679 CB THR A 369 11.313 52.648 103.333 1.00103.92 C ANISOU 2679 CB THR A 369 11232 8293 19961 -1471 -2663 845 C ATOM 2680 OG1 THR A 369 10.641 52.088 104.468 1.00107.86 O ANISOU 2680 OG1 THR A 369 11501 8788 20693 -1569 -2597 1293 O ATOM 2681 CG2 THR A 369 11.354 54.163 103.465 1.00100.23 C ANISOU 2681 CG2 THR A 369 10824 8255 19002 -1425 -2430 827 C ATOM 2682 N GLN A 370 9.859 50.102 101.102 1.00117.05 N ANISOU 2682 N GLN A 370 12936 9342 22197 -1474 -3352 366 N ATOM 2683 CA GLN A 370 10.063 48.714 100.695 1.00119.42 C ANISOU 2683 CA GLN A 370 13270 9338 22766 -1425 -3556 241 C ATOM 2684 C GLN A 370 10.991 48.636 99.488 1.00110.70 C ANISOU 2684 C GLN A 370 12474 8138 21450 -1270 -3633 -249 C ATOM 2685 O GLN A 370 12.033 47.973 99.529 1.00117.12 O ANISOU 2685 O GLN A 370 13366 8809 22323 -1153 -3595 -344 O ATOM 2686 CB GLN A 370 8.720 48.044 100.383 1.00134.06 C ANISOU 2686 CB GLN A 370 14982 11041 24912 -1537 -3803 319 C ATOM 2687 CG GLN A 370 7.717 48.040 101.529 1.00146.53 C ANISOU 2687 CG GLN A 370 16242 12703 26730 -1672 -3711 811 C ATOM 2688 CD GLN A 370 6.891 49.312 101.595 1.00151.29 C ANISOU 2688 CD GLN A 370 16775 13569 27141 -1745 -3596 914 C ATOM 2689 OE1 GLN A 370 7.266 50.341 101.033 1.00151.05 O ANISOU 2689 OE1 GLN A 370 16923 13704 26765 -1699 -3531 668 O ATOM 2690 NE2 GLN A 370 5.755 49.244 102.279 1.00154.44 N ANISOU 2690 NE2 GLN A 370 16904 14003 27774 -1852 -3561 1284 N ATOM 2691 N ASN A 371 10.622 49.311 98.403 1.00103.93 N ANISOU 2691 N ASN A 371 11793 7360 20335 -1256 -3728 -553 N ATOM 2692 CA ASN A 371 11.443 49.406 97.204 1.00105.06 C ANISOU 2692 CA ASN A 371 12258 7462 20197 -1097 -3761 -1018 C ATOM 2693 C ASN A 371 12.181 50.740 97.222 1.00110.13 C ANISOU 2693 C ASN A 371 13009 8372 20465 -1022 -3523 -1107 C ATOM 2694 O ASN A 371 11.550 51.803 97.250 1.00107.95 O ANISOU 2694 O ASN A 371 12687 8314 20016 -1107 -3484 -1036 O ATOM 2695 CB ASN A 371 10.583 49.278 95.947 1.00106.74 C ANISOU 2695 CB ASN A 371 12627 7598 20331 -1124 -4032 -1294 C ATOM 2696 CG ASN A 371 11.394 49.378 94.669 1.00108.68 C ANISOU 2696 CG ASN A 371 13239 7820 20233 -950 -4042 -1770 C ATOM 2697 OD1 ASN A 371 12.601 49.141 94.665 1.00104.70 O ANISOU 2697 OD1 ASN A 371 12856 7266 19658 -795 -3881 -1909 O ATOM 2698 ND2 ASN A 371 10.730 49.731 93.574 1.00114.54 N ANISOU 2698 ND2 ASN A 371 14160 8601 20758 -968 -4223 -2004 N ATOM 2699 N CYS A 372 13.513 50.681 97.207 1.00111.57 N ANISOU 2699 N CYS A 372 13320 8529 20542 -858 -3363 -1253 N ATOM 2700 CA CYS A 372 14.335 51.883 97.276 1.00107.35 C ANISOU 2700 CA CYS A 372 12872 8224 19693 -770 -3134 -1326 C ATOM 2701 C CYS A 372 14.536 52.564 95.929 1.00109.01 C ANISOU 2701 C CYS A 372 13372 8532 19514 -654 -3146 -1748 C ATOM 2702 O CYS A 372 14.892 53.747 95.902 1.00103.53 O ANISOU 2702 O CYS A 372 12726 8110 18500 -607 -2969 -1783 O ATOM 2703 CB CYS A 372 15.712 51.559 97.867 1.00106.23 C ANISOU 2703 CB CYS A 372 12716 8016 19631 -628 -2949 -1270 C ATOM 2704 SG CYS A 372 15.769 51.302 99.664 1.00108.11 S ANISOU 2704 SG CYS A 372 12640 8270 20166 -748 -2843 -713 S ATOM 2705 N GLU A 373 14.321 51.856 94.816 1.00122.35 N ANISOU 2705 N GLU A 373 15261 10063 21163 -595 -3326 -2044 N ATOM 2706 CA GLU A 373 14.586 52.425 93.498 1.00126.03 C ANISOU 2706 CA GLU A 373 16041 10627 21217 -465 -3319 -2437 C ATOM 2707 C GLU A 373 13.688 53.611 93.169 1.00125.43 C ANISOU 2707 C GLU A 373 15974 10793 20889 -575 -3381 -2429 C ATOM 2708 O GLU A 373 13.971 54.329 92.203 1.00135.11 O ANISOU 2708 O GLU A 373 17446 12164 21725 -469 -3333 -2706 O ATOM 2709 CB GLU A 373 14.439 51.349 92.419 1.00129.58 C ANISOU 2709 CB GLU A 373 16716 10843 21678 -399 -3515 -2725 C ATOM 2710 CG GLU A 373 15.368 51.533 91.223 1.00130.57 C ANISOU 2710 CG GLU A 373 17198 11001 21410 -173 -3386 -3133 C ATOM 2711 CD GLU A 373 16.828 51.290 91.570 1.00129.04 C ANISOU 2711 CD GLU A 373 17012 10760 21259 27 -3104 -3169 C ATOM 2712 OE1 GLU A 373 17.097 50.618 92.587 1.00128.02 O ANISOU 2712 OE1 GLU A 373 16649 10489 21504 -8 -3080 -2922 O ATOM 2713 OE2 GLU A 373 17.707 51.773 90.825 1.00128.99 O ANISOU 2713 OE2 GLU A 373 17233 10862 20917 224 -2899 -3425 O ATOM 2714 N VAL A 374 12.622 53.836 93.941 1.00117.26 N ANISOU 2714 N VAL A 374 14675 9813 20064 -775 -3467 -2105 N ATOM 2715 CA VAL A 374 11.792 55.016 93.742 1.00110.38 C ANISOU 2715 CA VAL A 374 13772 9179 18990 -877 -3498 -2058 C ATOM 2716 C VAL A 374 12.541 56.289 94.112 1.00100.29 C ANISOU 2716 C VAL A 374 12497 8200 17411 -805 -3211 -2028 C ATOM 2717 O VAL A 374 12.167 57.380 93.665 1.00 96.75 O ANISOU 2717 O VAL A 374 12103 8008 16650 -815 -3179 -2073 O ATOM 2718 CB VAL A 374 10.491 54.892 94.560 1.00112.15 C ANISOU 2718 CB VAL A 374 13680 9390 19544 -1087 -3608 -1681 C ATOM 2719 CG1 VAL A 374 9.438 55.868 94.053 1.00114.45 C ANISOU 2719 CG1 VAL A 374 13955 9863 19669 -1181 -3714 -1676 C ATOM 2720 CG2 VAL A 374 9.973 53.462 94.517 1.00115.75 C ANISOU 2720 CG2 VAL A 374 14068 9555 20356 -1135 -3830 -1628 C ATOM 2721 N TYR A 375 13.604 56.176 94.908 1.00 99.10 N ANISOU 2721 N TYR A 375 12275 8125 17252 -700 -2950 -1894 N ATOM 2722 CA TYR A 375 14.342 57.327 95.411 1.00 94.12 C ANISOU 2722 CA TYR A 375 11605 7883 16274 -612 -2625 -1769 C ATOM 2723 C TYR A 375 15.687 57.520 94.721 1.00 86.97 C ANISOU 2723 C TYR A 375 10918 7051 15075 -386 -2443 -2038 C ATOM 2724 O TYR A 375 16.493 58.334 95.183 1.00 80.57 O ANISOU 2724 O TYR A 375 10061 6516 14035 -303 -2180 -1929 O ATOM 2725 CB TYR A 375 14.553 57.194 96.922 1.00 68.68 C ANISOU 2725 CB TYR A 375 8128 4727 13240 -672 -2467 -1375 C ATOM 2726 CG TYR A 375 13.283 56.984 97.714 1.00 69.30 C ANISOU 2726 CG TYR A 375 7971 4743 13616 -880 -2582 -1061 C ATOM 2727 CD1 TYR A 375 12.796 55.707 97.961 1.00 72.23 C ANISOU 2727 CD1 TYR A 375 8237 4757 14450 -981 -2789 -964 C ATOM 2728 CD2 TYR A 375 12.574 58.064 98.221 1.00 78.95 C ANISOU 2728 CD2 TYR A 375 9068 6252 14679 -968 -2468 -851 C ATOM 2729 CE1 TYR A 375 11.637 55.513 98.687 1.00 80.51 C ANISOU 2729 CE1 TYR A 375 9047 5746 15798 -1170 -2869 -646 C ATOM 2730 CE2 TYR A 375 11.415 57.879 98.948 1.00 75.34 C ANISOU 2730 CE2 TYR A 375 8381 5739 14506 -1141 -2531 -547 C ATOM 2731 CZ TYR A 375 10.952 56.603 99.178 1.00 79.52 C ANISOU 2731 CZ TYR A 375 8795 5922 15498 -1244 -2726 -435 C ATOM 2732 OH TYR A 375 9.797 56.419 99.902 1.00 88.37 O ANISOU 2732 OH TYR A 375 9663 6985 16927 -1416 -2766 -102 O ATOM 2733 N ARG A 376 15.954 56.795 93.632 1.00 92.69 N ANISOU 2733 N ARG A 376 11881 7529 15809 -279 -2572 -2384 N ATOM 2734 CA ARG A 376 17.258 56.901 92.983 1.00 97.85 C ANISOU 2734 CA ARG A 376 12731 8235 16213 -43 -2358 -2626 C ATOM 2735 C ARG A 376 17.442 58.270 92.338 1.00 95.65 C ANISOU 2735 C ARG A 376 12578 8309 15454 28 -2194 -2723 C ATOM 2736 O ARG A 376 18.390 58.998 92.653 1.00 93.62 O ANISOU 2736 O ARG A 376 12269 8296 15005 134 -1913 -2633 O ATOM 2737 CB ARG A 376 17.431 55.793 91.944 1.00110.70 C ANISOU 2737 CB ARG A 376 14615 9501 17943 67 -2522 -2992 C ATOM 2738 CG ARG A 376 18.823 55.777 91.330 1.00120.97 C ANISOU 2738 CG ARG A 376 16100 10826 19036 335 -2256 -3222 C ATOM 2739 CD ARG A 376 18.937 54.809 90.168 1.00133.14 C ANISOU 2739 CD ARG A 376 17953 12056 20579 466 -2383 -3615 C ATOM 2740 NE ARG A 376 20.316 54.701 89.698 1.00142.23 N ANISOU 2740 NE ARG A 376 19245 13205 21593 741 -2082 -3803 N ATOM 2741 CZ ARG A 376 20.904 55.582 88.893 1.00151.44 C ANISOU 2741 CZ ARG A 376 20600 14607 22335 904 -1853 -3975 C ATOM 2742 NH1 ARG A 376 20.236 56.644 88.464 1.00157.29 N ANISOU 2742 NH1 ARG A 376 21419 15619 22724 814 -1903 -3976 N ATOM 2743 NH2 ARG A 376 22.164 55.401 88.519 1.00153.44 N ANISOU 2743 NH2 ARG A 376 20943 14837 22521 1159 -1555 -4112 N ATOM 2744 N SER A 377 16.540 58.636 91.424 1.00 95.22 N ANISOU 2744 N SER A 377 12686 8273 15219 -35 -2385 -2895 N ATOM 2745 CA SER A 377 16.669 59.913 90.731 1.00 94.08 C ANISOU 2745 CA SER A 377 12676 8446 14624 32 -2249 -2984 C ATOM 2746 C SER A 377 16.415 61.091 91.662 1.00 96.51 C ANISOU 2746 C SER A 377 12741 9079 14849 -73 -2103 -2661 C ATOM 2747 O SER A 377 16.945 62.184 91.434 1.00 95.85 O ANISOU 2747 O SER A 377 12702 9278 14437 12 -1891 -2661 O ATOM 2748 CB SER A 377 15.710 59.964 89.543 1.00 95.92 C ANISOU 2748 CB SER A 377 13146 8600 14699 -20 -2533 -3230 C ATOM 2749 OG SER A 377 14.363 59.875 89.975 1.00 99.54 O ANISOU 2749 OG SER A 377 13426 8979 15417 -249 -2808 -3054 O ATOM 2750 N VAL A 378 15.614 60.893 92.711 1.00 97.15 N ANISOU 2750 N VAL A 378 12571 9116 15224 -250 -2201 -2381 N ATOM 2751 CA VAL A 378 15.303 61.991 93.620 1.00 89.03 C ANISOU 2751 CA VAL A 378 11337 8380 14110 -340 -2057 -2088 C ATOM 2752 C VAL A 378 16.512 62.330 94.482 1.00 93.86 C ANISOU 2752 C VAL A 378 11853 9157 14653 -243 -1769 -1935 C ATOM 2753 O VAL A 378 16.757 63.501 94.798 1.00 99.86 O ANISOU 2753 O VAL A 378 12563 10204 15175 -231 -1591 -1824 O ATOM 2754 CB VAL A 378 14.076 61.641 94.480 1.00 84.35 C ANISOU 2754 CB VAL A 378 10514 7687 13850 -543 -2218 -1827 C ATOM 2755 CG1 VAL A 378 13.578 62.875 95.209 1.00 76.89 C ANISOU 2755 CG1 VAL A 378 9404 7041 12769 -621 -2073 -1577 C ATOM 2756 CG2 VAL A 378 12.979 61.039 93.619 1.00 93.47 C ANISOU 2756 CG2 VAL A 378 11746 8597 15171 -643 -2556 -1983 C ATOM 2757 N ASP A 379 17.282 61.315 94.882 1.00 87.53 N ANISOU 2757 N ASP A 379 11019 8161 14077 -177 -1740 -1921 N ATOM 2758 CA ASP A 379 18.482 61.567 95.673 1.00 82.58 C ANISOU 2758 CA ASP A 379 10296 7665 13416 -86 -1507 -1771 C ATOM 2759 C ASP A 379 19.510 62.358 94.876 1.00 72.15 C ANISOU 2759 C ASP A 379 9116 6524 11775 87 -1307 -1951 C ATOM 2760 O ASP A 379 20.203 63.221 95.428 1.00 56.74 O ANISOU 2760 O ASP A 379 7076 4800 9682 119 -1120 -1805 O ATOM 2761 CB ASP A 379 19.078 60.247 96.160 1.00 88.72 C ANISOU 2761 CB ASP A 379 11009 8164 14536 -43 -1543 -1723 C ATOM 2762 CG ASP A 379 18.283 59.634 97.293 1.00 90.28 C ANISOU 2762 CG ASP A 379 11012 8245 15045 -214 -1669 -1433 C ATOM 2763 OD1 ASP A 379 17.290 60.254 97.726 1.00 91.04 O ANISOU 2763 OD1 ASP A 379 11018 8486 15087 -355 -1701 -1269 O ATOM 2764 OD2 ASP A 379 18.652 58.534 97.752 1.00 91.16 O ANISOU 2764 OD2 ASP A 379 11055 8117 15465 -200 -1723 -1355 O ATOM 2765 N LEU A 380 19.625 62.075 93.576 1.00 68.99 N ANISOU 2765 N LEU A 380 8943 6015 11254 199 -1344 -2262 N ATOM 2766 CA LEU A 380 20.529 62.850 92.733 1.00 70.22 C ANISOU 2766 CA LEU A 380 9242 6350 11091 367 -1131 -2419 C ATOM 2767 C LEU A 380 20.100 64.310 92.674 1.00 74.00 C ANISOU 2767 C LEU A 380 9704 7143 11272 299 -1070 -2331 C ATOM 2768 O LEU A 380 20.943 65.214 92.672 1.00 71.57 O ANISOU 2768 O LEU A 380 9372 7048 10773 384 -852 -2281 O ATOM 2769 CB LEU A 380 20.587 62.245 91.330 1.00 71.27 C ANISOU 2769 CB LEU A 380 9662 6305 11113 500 -1188 -2775 C ATOM 2770 CG LEU A 380 21.527 62.918 90.328 1.00 78.15 C ANISOU 2770 CG LEU A 380 10712 7337 11644 698 -940 -2948 C ATOM 2771 CD1 LEU A 380 22.964 62.887 90.828 1.00 77.28 C ANISOU 2771 CD1 LEU A 380 10460 7263 11641 843 -662 -2838 C ATOM 2772 CD2 LEU A 380 21.419 62.260 88.960 1.00 67.07 C ANISOU 2772 CD2 LEU A 380 9640 5746 10096 824 -1018 -3311 C ATOM 2773 N ALA A 381 18.790 64.559 92.640 1.00 70.71 N ANISOU 2773 N ALA A 381 9280 6743 10846 143 -1266 -2297 N ATOM 2774 CA ALA A 381 18.302 65.933 92.626 1.00 61.12 C ANISOU 2774 CA ALA A 381 8033 5803 9386 77 -1218 -2202 C ATOM 2775 C ALA A 381 18.585 66.636 93.947 1.00 63.15 C ANISOU 2775 C ALA A 381 8068 6243 9684 17 -1070 -1912 C ATOM 2776 O ALA A 381 18.863 67.841 93.965 1.00 62.93 O ANISOU 2776 O ALA A 381 8024 6454 9432 37 -928 -1852 O ATOM 2777 CB ALA A 381 16.807 65.959 92.314 1.00 59.51 C ANISOU 2777 CB ALA A 381 7844 5545 9223 -73 -1473 -2215 C ATOM 2778 N PHE A 382 18.523 65.903 95.062 1.00 61.93 N ANISOU 2778 N PHE A 382 7754 5970 9805 -56 -1109 -1729 N ATOM 2779 CA PHE A 382 18.711 66.531 96.366 1.00 65.86 C ANISOU 2779 CA PHE A 382 8078 6634 10311 -119 -994 -1458 C ATOM 2780 C PHE A 382 20.125 67.082 96.514 1.00 65.94 C ANISOU 2780 C PHE A 382 8081 6779 10193 4 -795 -1440 C ATOM 2781 O PHE A 382 20.313 68.247 96.883 1.00 72.83 O ANISOU 2781 O PHE A 382 8912 7875 10886 -12 -686 -1339 O ATOM 2782 CB PHE A 382 18.399 65.538 97.485 1.00 51.48 C ANISOU 2782 CB PHE A 382 6114 4649 8796 -212 -1078 -1257 C ATOM 2783 CG PHE A 382 18.691 66.070 98.860 1.00 58.95 C ANISOU 2783 CG PHE A 382 6925 5754 9719 -261 -965 -985 C ATOM 2784 CD1 PHE A 382 17.872 67.029 99.435 1.00 66.21 C ANISOU 2784 CD1 PHE A 382 7786 6857 10514 -357 -925 -840 C ATOM 2785 CD2 PHE A 382 19.786 65.617 99.576 1.00 58.33 C ANISOU 2785 CD2 PHE A 382 6790 5632 9741 -204 -906 -877 C ATOM 2786 CE1 PHE A 382 18.140 67.524 100.699 1.00 70.11 C ANISOU 2786 CE1 PHE A 382 8200 7490 10947 -392 -824 -613 C ATOM 2787 CE2 PHE A 382 20.059 66.106 100.840 1.00 64.62 C ANISOU 2787 CE2 PHE A 382 7497 6571 10486 -252 -835 -635 C ATOM 2788 CZ PHE A 382 19.235 67.062 101.402 1.00 70.18 C ANISOU 2788 CZ PHE A 382 8178 7460 11029 -344 -792 -514 C ATOM 2789 N PHE A 383 21.136 66.258 96.229 1.00 66.17 N ANISOU 2789 N PHE A 383 8142 6660 10339 128 -750 -1533 N ATOM 2790 CA PHE A 383 22.515 66.717 96.354 1.00 69.63 C ANISOU 2790 CA PHE A 383 8537 7203 10716 246 -566 -1495 C ATOM 2791 C PHE A 383 22.891 67.719 95.271 1.00 69.37 C ANISOU 2791 C PHE A 383 8619 7337 10400 344 -426 -1646 C ATOM 2792 O PHE A 383 23.855 68.472 95.449 1.00 57.03 O ANISOU 2792 O PHE A 383 6989 5916 8764 405 -273 -1566 O ATOM 2793 CB PHE A 383 23.472 65.524 96.335 1.00 66.65 C ANISOU 2793 CB PHE A 383 8137 6602 10586 364 -542 -1538 C ATOM 2794 CG PHE A 383 23.339 64.626 97.534 1.00 65.01 C ANISOU 2794 CG PHE A 383 7791 6246 10665 274 -659 -1333 C ATOM 2795 CD1 PHE A 383 23.851 65.010 98.763 1.00 60.23 C ANISOU 2795 CD1 PHE A 383 7038 5752 10094 223 -628 -1074 C ATOM 2796 CD2 PHE A 383 22.700 63.400 97.435 1.00 65.64 C ANISOU 2796 CD2 PHE A 383 7897 6067 10976 239 -814 -1391 C ATOM 2797 CE1 PHE A 383 23.729 64.190 99.870 1.00 57.03 C ANISOU 2797 CE1 PHE A 383 6524 5221 9922 144 -735 -864 C ATOM 2798 CE2 PHE A 383 22.576 62.574 98.538 1.00 62.47 C ANISOU 2798 CE2 PHE A 383 7363 5527 10846 155 -913 -1172 C ATOM 2799 CZ PHE A 383 23.091 62.970 99.757 1.00 61.08 C ANISOU 2799 CZ PHE A 383 7051 5483 10675 110 -866 -902 C ATOM 2800 N ILE A 384 22.157 67.751 94.157 1.00 74.93 N ANISOU 2800 N ILE A 384 9495 8023 10954 356 -490 -1847 N ATOM 2801 CA ILE A 384 22.365 68.801 93.164 1.00 71.42 C ANISOU 2801 CA ILE A 384 9168 7759 10209 431 -367 -1954 C ATOM 2802 C ILE A 384 21.857 70.135 93.695 1.00 77.74 C ANISOU 2802 C ILE A 384 9881 8790 10868 316 -359 -1789 C ATOM 2803 O ILE A 384 22.578 71.140 93.687 1.00 82.01 O ANISOU 2803 O ILE A 384 10381 9501 11276 362 -203 -1723 O ATOM 2804 CB ILE A 384 21.694 68.426 91.831 1.00 63.92 C ANISOU 2804 CB ILE A 384 8456 6719 9113 474 -470 -2212 C ATOM 2805 CG1 ILE A 384 22.552 67.414 91.069 1.00 59.98 C ANISOU 2805 CG1 ILE A 384 8094 6034 8660 654 -385 -2418 C ATOM 2806 CG2 ILE A 384 21.454 69.666 90.981 1.00 59.95 C ANISOU 2806 CG2 ILE A 384 8064 6431 8282 489 -409 -2259 C ATOM 2807 CD1 ILE A 384 21.958 66.988 89.744 1.00 60.78 C ANISOU 2807 CD1 ILE A 384 8479 6028 8584 708 -501 -2701 C ATOM 2808 N THR A 385 20.611 70.164 94.178 1.00 75.31 N ANISOU 2808 N THR A 385 9529 8473 10610 167 -521 -1714 N ATOM 2809 CA THR A 385 20.077 71.382 94.777 1.00 64.33 C ANISOU 2809 CA THR A 385 8052 7278 9113 68 -500 -1557 C ATOM 2810 C THR A 385 20.755 71.716 96.097 1.00 68.32 C ANISOU 2810 C THR A 385 8406 7858 9694 40 -410 -1351 C ATOM 2811 O THR A 385 20.613 72.841 96.586 1.00 79.11 O ANISOU 2811 O THR A 385 9723 9392 10945 -11 -357 -1242 O ATOM 2812 CB THR A 385 18.569 71.259 95.003 1.00 57.46 C ANISOU 2812 CB THR A 385 7151 6363 8320 -71 -672 -1510 C ATOM 2813 OG1 THR A 385 18.311 70.258 95.997 1.00 53.03 O ANISOU 2813 OG1 THR A 385 6479 5653 8016 -143 -747 -1388 O ATOM 2814 CG2 THR A 385 17.865 70.887 93.706 1.00 60.06 C ANISOU 2814 CG2 THR A 385 7635 6596 8588 -59 -821 -1714 C ATOM 2815 N LEU A 386 21.478 70.764 96.687 1.00 67.58 N ANISOU 2815 N LEU A 386 8249 7634 9793 72 -409 -1297 N ATOM 2816 CA LEU A 386 22.211 71.057 97.912 1.00 71.15 C ANISOU 2816 CA LEU A 386 8579 8152 10303 47 -357 -1100 C ATOM 2817 C LEU A 386 23.400 71.965 97.631 1.00 69.32 C ANISOU 2817 C LEU A 386 8331 8049 9960 137 -215 -1103 C ATOM 2818 O LEU A 386 23.752 72.812 98.460 1.00 65.93 O ANISOU 2818 O LEU A 386 7830 7740 9479 90 -189 -961 O ATOM 2819 CB LEU A 386 22.661 69.758 98.575 1.00 74.14 C ANISOU 2819 CB LEU A 386 8890 8344 10938 57 -417 -1023 C ATOM 2820 CG LEU A 386 22.945 69.841 100.073 1.00 74.21 C ANISOU 2820 CG LEU A 386 8790 8395 11013 -18 -442 -781 C ATOM 2821 CD1 LEU A 386 21.732 70.389 100.807 1.00 71.25 C ANISOU 2821 CD1 LEU A 386 8414 8122 10538 -148 -480 -667 C ATOM 2822 CD2 LEU A 386 23.331 68.475 100.613 1.00 81.04 C ANISOU 2822 CD2 LEU A 386 9591 9056 12145 -6 -518 -697 C ATOM 2823 N SER A 387 24.035 71.806 96.465 1.00 68.12 N ANISOU 2823 N SER A 387 8248 7863 9771 267 -120 -1260 N ATOM 2824 CA SER A 387 25.092 72.733 96.078 1.00 65.85 C ANISOU 2824 CA SER A 387 7930 7700 9390 351 38 -1245 C ATOM 2825 C SER A 387 24.526 74.108 95.749 1.00 63.33 C ANISOU 2825 C SER A 387 7657 7568 8838 298 65 -1243 C ATOM 2826 O SER A 387 25.231 75.114 95.889 1.00 70.41 O ANISOU 2826 O SER A 387 8486 8582 9682 309 154 -1156 O ATOM 2827 CB SER A 387 25.881 72.176 94.893 1.00 64.59 C ANISOU 2827 CB SER A 387 7842 7458 9242 522 174 -1403 C ATOM 2828 OG SER A 387 25.050 71.996 93.761 1.00 67.15 O ANISOU 2828 OG SER A 387 8353 7761 9399 551 148 -1600 O ATOM 2829 N PHE A 388 23.265 74.173 95.312 1.00 58.32 N ANISOU 2829 N PHE A 388 7123 6944 8090 238 -25 -1327 N ATOM 2830 CA PHE A 388 22.603 75.466 95.160 1.00 57.55 C ANISOU 2830 CA PHE A 388 7047 7008 7812 176 -21 -1296 C ATOM 2831 C PHE A 388 22.527 76.197 96.493 1.00 56.60 C ANISOU 2831 C PHE A 388 6816 6968 7722 76 -42 -1120 C ATOM 2832 O PHE A 388 22.668 77.424 96.548 1.00 57.88 O ANISOU 2832 O PHE A 388 6959 7259 7773 59 14 -1067 O ATOM 2833 CB PHE A 388 21.201 75.282 94.576 1.00 55.18 C ANISOU 2833 CB PHE A 388 6844 6679 7444 118 -149 -1391 C ATOM 2834 CG PHE A 388 21.181 75.052 93.092 1.00 61.67 C ANISOU 2834 CG PHE A 388 7832 7475 8126 212 -140 -1578 C ATOM 2835 CD1 PHE A 388 21.446 73.799 92.566 1.00 63.42 C ANISOU 2835 CD1 PHE A 388 8144 7533 8421 291 -168 -1722 C ATOM 2836 CD2 PHE A 388 20.878 76.087 92.223 1.00 65.60 C ANISOU 2836 CD2 PHE A 388 8413 8106 8407 227 -110 -1611 C ATOM 2837 CE1 PHE A 388 21.422 73.585 91.200 1.00 61.66 C ANISOU 2837 CE1 PHE A 388 8118 7283 8026 388 -161 -1914 C ATOM 2838 CE2 PHE A 388 20.852 75.879 90.856 1.00 70.97 C ANISOU 2838 CE2 PHE A 388 9280 8771 8912 317 -108 -1778 C ATOM 2839 CZ PHE A 388 21.123 74.626 90.344 1.00 67.09 C ANISOU 2839 CZ PHE A 388 8906 8122 8466 400 -132 -1939 C ATOM 2840 N THR A 389 22.299 75.456 97.581 1.00 54.38 N ANISOU 2840 N THR A 389 6475 6603 7583 11 -123 -1028 N ATOM 2841 CA THR A 389 22.279 76.063 98.907 1.00 59.05 C ANISOU 2841 CA THR A 389 7002 7266 8169 -71 -140 -869 C ATOM 2842 C THR A 389 23.639 76.651 99.259 1.00 64.46 C ANISOU 2842 C THR A 389 7627 8003 8863 -33 -85 -797 C ATOM 2843 O THR A 389 23.725 77.711 99.890 1.00 68.96 O ANISOU 2843 O THR A 389 8185 8671 9347 -82 -83 -720 O ATOM 2844 CB THR A 389 21.856 75.026 99.948 1.00 60.65 C ANISOU 2844 CB THR A 389 7169 7364 8511 -135 -226 -768 C ATOM 2845 OG1 THR A 389 20.553 74.525 99.622 1.00 67.68 O ANISOU 2845 OG1 THR A 389 8086 8195 9436 -183 -286 -812 O ATOM 2846 CG2 THR A 389 21.825 75.638 101.340 1.00 59.95 C ANISOU 2846 CG2 THR A 389 7056 7356 8365 -208 -235 -607 C ATOM 2847 N TYR A 390 24.712 75.982 98.846 1.00 60.58 N ANISOU 2847 N TYR A 390 7094 7430 8494 57 -45 -823 N ATOM 2848 CA TYR A 390 26.057 76.466 99.113 1.00 61.19 C ANISOU 2848 CA TYR A 390 7076 7535 8640 95 -1 -736 C ATOM 2849 C TYR A 390 26.469 77.611 98.196 1.00 58.27 C ANISOU 2849 C TYR A 390 6706 7272 8161 145 118 -777 C ATOM 2850 O TYR A 390 27.531 78.202 98.414 1.00 55.00 O ANISOU 2850 O TYR A 390 6193 6885 7821 160 149 -685 O ATOM 2851 CB TYR A 390 27.053 75.309 98.994 1.00 65.04 C ANISOU 2851 CB TYR A 390 7488 7882 9341 187 19 -728 C ATOM 2852 CG TYR A 390 26.715 74.135 99.887 1.00 69.01 C ANISOU 2852 CG TYR A 390 7980 8261 9979 139 -104 -664 C ATOM 2853 CD1 TYR A 390 26.286 74.332 101.194 1.00 70.87 C ANISOU 2853 CD1 TYR A 390 8216 8533 10178 23 -220 -524 C ATOM 2854 CD2 TYR A 390 26.806 72.831 99.417 1.00 66.90 C ANISOU 2854 CD2 TYR A 390 7716 7832 9870 215 -98 -740 C ATOM 2855 CE1 TYR A 390 25.971 73.261 102.014 1.00 72.67 C ANISOU 2855 CE1 TYR A 390 8435 8653 10524 -20 -320 -435 C ATOM 2856 CE2 TYR A 390 26.490 71.754 100.229 1.00 68.25 C ANISOU 2856 CE2 TYR A 390 7867 7875 10191 167 -215 -660 C ATOM 2857 CZ TYR A 390 26.074 71.976 101.526 1.00 68.88 C ANISOU 2857 CZ TYR A 390 7935 8007 10231 46 -322 -494 C ATOM 2858 OH TYR A 390 25.761 70.906 102.333 1.00 67.01 O ANISOU 2858 OH TYR A 390 7678 7647 10138 -2 -426 -385 O ATOM 2859 N MET A 391 25.658 77.947 97.189 1.00 59.48 N ANISOU 2859 N MET A 391 6961 7481 8157 164 170 -893 N ATOM 2860 CA MET A 391 25.970 79.075 96.318 1.00 65.39 C ANISOU 2860 CA MET A 391 7719 8337 8788 206 283 -907 C ATOM 2861 C MET A 391 25.825 80.423 97.011 1.00 67.65 C ANISOU 2861 C MET A 391 7970 8721 9014 113 242 -809 C ATOM 2862 O MET A 391 26.276 81.431 96.458 1.00 74.95 O ANISOU 2862 O MET A 391 8868 9718 9891 138 325 -780 O ATOM 2863 CB MET A 391 25.076 79.060 95.078 1.00 64.96 C ANISOU 2863 CB MET A 391 7805 8315 8563 245 317 -1047 C ATOM 2864 CG MET A 391 25.639 78.303 93.894 1.00 72.37 C ANISOU 2864 CG MET A 391 8812 9199 9486 385 436 -1163 C ATOM 2865 SD MET A 391 24.840 78.815 92.363 1.00 80.65 S ANISOU 2865 SD MET A 391 10048 10335 10260 431 478 -1293 S ATOM 2866 CE MET A 391 23.118 78.719 92.843 1.00 80.25 C ANISOU 2866 CE MET A 391 10049 10266 10176 289 255 -1324 C ATOM 2867 N ASN A 392 25.213 80.472 98.197 1.00 62.36 N ANISOU 2867 N ASN A 392 7306 8045 8343 15 125 -755 N ATOM 2868 CA ASN A 392 24.942 81.753 98.837 1.00 65.99 C ANISOU 2868 CA ASN A 392 7770 8581 8721 -61 89 -696 C ATOM 2869 C ASN A 392 26.203 82.455 99.324 1.00 61.31 C ANISOU 2869 C ASN A 392 7086 7991 8218 -72 72 -596 C ATOM 2870 O ASN A 392 26.124 83.627 99.705 1.00 60.34 O ANISOU 2870 O ASN A 392 6973 7915 8039 -125 42 -563 O ATOM 2871 CB ASN A 392 23.968 81.566 100.004 1.00 70.44 C ANISOU 2871 CB ASN A 392 8386 9136 9243 -145 -1 -666 C ATOM 2872 CG ASN A 392 24.661 81.149 101.288 1.00 73.36 C ANISOU 2872 CG ASN A 392 8727 9456 9692 -183 -93 -565 C ATOM 2873 OD1 ASN A 392 25.058 81.991 102.094 1.00 71.92 O ANISOU 2873 OD1 ASN A 392 8552 9301 9474 -230 -150 -505 O ATOM 2874 ND2 ASN A 392 24.800 79.844 101.489 1.00 75.52 N ANISOU 2874 ND2 ASN A 392 8978 9645 10073 -166 -127 -545 N ATOM 2875 N VAL A 393 27.355 81.782 99.321 1.00 59.65 N ANISOU 2875 N VAL A 393 6778 7715 8172 -22 81 -545 N ATOM 2876 CA VAL A 393 28.590 82.449 99.720 1.00 63.86 C ANISOU 2876 CA VAL A 393 7192 8234 8838 -38 44 -431 C ATOM 2877 C VAL A 393 29.232 83.203 98.564 1.00 69.34 C ANISOU 2877 C VAL A 393 7809 8970 9568 28 192 -417 C ATOM 2878 O VAL A 393 30.001 84.143 98.800 1.00 73.40 O ANISOU 2878 O VAL A 393 8226 9484 10177 -10 159 -319 O ATOM 2879 CB VAL A 393 29.598 81.452 100.314 1.00 57.96 C ANISOU 2879 CB VAL A 393 6337 7386 8299 -18 -27 -345 C ATOM 2880 CG1 VAL A 393 29.077 80.895 101.628 1.00 56.49 C ANISOU 2880 CG1 VAL A 393 6228 7166 8068 -99 -192 -312 C ATOM 2881 CG2 VAL A 393 29.889 80.334 99.326 1.00 50.58 C ANISOU 2881 CG2 VAL A 393 5364 6395 7457 106 115 -403 C ATOM 2882 N MET A 394 28.940 82.824 97.320 1.00 66.69 N ANISOU 2882 N MET A 394 7522 8663 9154 123 349 -505 N ATOM 2883 CA MET A 394 29.461 83.537 96.164 1.00 74.22 C ANISOU 2883 CA MET A 394 8432 9673 10096 196 518 -479 C ATOM 2884 C MET A 394 28.437 84.468 95.528 1.00 79.48 C ANISOU 2884 C MET A 394 9215 10434 10550 170 545 -535 C ATOM 2885 O MET A 394 28.785 85.201 94.596 1.00 84.33 O ANISOU 2885 O MET A 394 9806 11105 11131 219 677 -491 O ATOM 2886 CB MET A 394 29.973 82.546 95.113 1.00 76.86 C ANISOU 2886 CB MET A 394 8764 9977 10463 343 697 -533 C ATOM 2887 CG MET A 394 28.908 81.622 94.564 1.00 80.15 C ANISOU 2887 CG MET A 394 9359 10385 10710 383 697 -704 C ATOM 2888 SD MET A 394 29.561 80.537 93.285 1.00 88.78 S ANISOU 2888 SD MET A 394 10494 11425 11811 573 913 -800 S ATOM 2889 CE MET A 394 30.060 81.739 92.056 1.00 86.42 C ANISOU 2889 CE MET A 394 10193 11251 11392 650 1137 -732 C ATOM 2890 N LEU A 395 27.192 84.458 96.004 1.00 75.14 N ANISOU 2890 N LEU A 395 8778 9899 9873 99 431 -609 N ATOM 2891 CA LEU A 395 26.167 85.373 95.519 1.00 70.43 C ANISOU 2891 CA LEU A 395 8269 9378 9115 69 433 -644 C ATOM 2892 C LEU A 395 25.876 86.510 96.488 1.00 65.80 C ANISOU 2892 C LEU A 395 7665 8797 8538 -31 332 -588 C ATOM 2893 O LEU A 395 25.420 87.574 96.055 1.00 57.04 O ANISOU 2893 O LEU A 395 6579 7736 7358 -46 353 -574 O ATOM 2894 CB LEU A 395 24.869 84.612 95.229 1.00 66.31 C ANISOU 2894 CB LEU A 395 7871 8855 8467 70 387 -762 C ATOM 2895 CG LEU A 395 24.977 83.507 94.177 1.00 70.33 C ANISOU 2895 CG LEU A 395 8450 9341 8932 170 461 -859 C ATOM 2896 CD1 LEU A 395 23.610 82.906 93.877 1.00 72.00 C ANISOU 2896 CD1 LEU A 395 8780 9536 9041 147 367 -969 C ATOM 2897 CD2 LEU A 395 25.629 84.038 92.910 1.00 69.55 C ANISOU 2897 CD2 LEU A 395 8367 9307 8752 264 621 -840 C ATOM 2898 N ASP A 396 26.118 86.309 97.783 1.00 66.11 N ANISOU 2898 N ASP A 396 7680 8782 8656 -93 217 -558 N ATOM 2899 CA ASP A 396 26.014 87.415 98.728 1.00 73.94 C ANISOU 2899 CA ASP A 396 8683 9765 9645 -175 122 -520 C ATOM 2900 C ASP A 396 26.964 88.573 98.424 1.00 80.42 C ANISOU 2900 C ASP A 396 9407 10577 10570 -186 137 -432 C ATOM 2901 O ASP A 396 26.593 89.719 98.734 1.00 81.20 O ANISOU 2901 O ASP A 396 9540 10673 10638 -238 89 -429 O ATOM 2902 CB ASP A 396 26.236 86.902 100.160 1.00 80.39 C ANISOU 2902 CB ASP A 396 9521 10525 10498 -232 -13 -500 C ATOM 2903 CG ASP A 396 25.008 86.215 100.736 1.00 90.42 C ANISOU 2903 CG ASP A 396 10900 11805 11652 -249 -32 -560 C ATOM 2904 OD1 ASP A 396 23.958 86.197 100.060 1.00 93.44 O ANISOU 2904 OD1 ASP A 396 11324 12227 11952 -227 38 -620 O ATOM 2905 OD2 ASP A 396 25.096 85.690 101.866 1.00 94.42 O ANISOU 2905 OD2 ASP A 396 11442 12274 12157 -288 -123 -531 O ATOM 2906 N PRO A 397 28.167 88.369 97.869 1.00 78.01 N ANISOU 2906 N PRO A 397 8974 10255 10412 -140 205 -350 N ATOM 2907 CA PRO A 397 28.949 89.527 97.402 1.00 76.57 C ANISOU 2907 CA PRO A 397 8680 10066 10347 -150 246 -241 C ATOM 2908 C PRO A 397 28.196 90.431 96.442 1.00 73.69 C ANISOU 2908 C PRO A 397 8373 9768 9857 -131 343 -252 C ATOM 2909 O PRO A 397 28.410 91.651 96.459 1.00 75.69 O ANISOU 2909 O PRO A 397 8578 9998 10184 -179 314 -179 O ATOM 2910 CB PRO A 397 30.159 88.869 96.729 1.00 76.86 C ANISOU 2910 CB PRO A 397 8571 10089 10543 -68 374 -153 C ATOM 2911 CG PRO A 397 30.363 87.631 97.508 1.00 74.04 C ANISOU 2911 CG PRO A 397 8214 9679 10238 -64 289 -189 C ATOM 2912 CD PRO A 397 28.987 87.142 97.877 1.00 73.69 C ANISOU 2912 CD PRO A 397 8349 9666 9982 -85 232 -327 C ATOM 2913 N VAL A 398 27.321 89.875 95.602 1.00 67.48 N ANISOU 2913 N VAL A 398 7689 9053 8898 -67 435 -336 N ATOM 2914 CA VAL A 398 26.512 90.710 94.720 1.00 60.81 C ANISOU 2914 CA VAL A 398 6908 8271 7926 -54 492 -337 C ATOM 2915 C VAL A 398 25.513 91.528 95.527 1.00 60.78 C ANISOU 2915 C VAL A 398 6966 8242 7885 -133 370 -378 C ATOM 2916 O VAL A 398 25.199 92.670 95.167 1.00 64.21 O ANISOU 2916 O VAL A 398 7398 8683 8317 -150 378 -331 O ATOM 2917 CB VAL A 398 25.807 89.843 93.661 1.00 53.65 C ANISOU 2917 CB VAL A 398 6112 7432 6840 26 574 -423 C ATOM 2918 CG1 VAL A 398 25.069 90.719 92.661 1.00 44.92 C ANISOU 2918 CG1 VAL A 398 5071 6393 5604 41 613 -397 C ATOM 2919 CG2 VAL A 398 26.811 88.949 92.956 1.00 57.53 C ANISOU 2919 CG2 VAL A 398 6568 7932 7359 124 714 -409 C ATOM 2920 N VAL A 399 24.999 90.969 96.624 1.00 55.46 N ANISOU 2920 N VAL A 399 6350 7534 7189 -173 271 -458 N ATOM 2921 CA VAL A 399 24.104 91.727 97.493 1.00 55.98 C ANISOU 2921 CA VAL A 399 6482 7570 7218 -228 190 -500 C ATOM 2922 C VAL A 399 24.847 92.894 98.133 1.00 59.71 C ANISOU 2922 C VAL A 399 6912 7968 7807 -285 114 -444 C ATOM 2923 O VAL A 399 24.316 94.007 98.234 1.00 61.28 O ANISOU 2923 O VAL A 399 7142 8138 8005 -307 95 -450 O ATOM 2924 CB VAL A 399 23.475 90.801 98.551 1.00 54.07 C ANISOU 2924 CB VAL A 399 6316 7312 6917 -249 131 -575 C ATOM 2925 CG1 VAL A 399 22.688 91.610 99.571 1.00 51.74 C ANISOU 2925 CG1 VAL A 399 6099 6981 6579 -289 81 -613 C ATOM 2926 CG2 VAL A 399 22.582 89.770 97.885 1.00 56.13 C ANISOU 2926 CG2 VAL A 399 6611 7620 7097 -207 180 -628 C ATOM 2927 N TYR A 400 26.090 92.663 98.564 1.00 64.03 N ANISOU 2927 N TYR A 400 7381 8466 8480 -310 56 -387 N ATOM 2928 CA TYR A 400 26.864 93.729 99.193 1.00 67.83 C ANISOU 2928 CA TYR A 400 7817 8854 9101 -379 -61 -333 C ATOM 2929 C TYR A 400 27.171 94.846 98.203 1.00 69.98 C ANISOU 2929 C TYR A 400 7994 9118 9477 -374 9 -233 C ATOM 2930 O TYR A 400 27.179 96.027 98.570 1.00 65.47 O ANISOU 2930 O TYR A 400 7429 8463 8982 -428 -76 -221 O ATOM 2931 CB TYR A 400 28.165 93.171 99.772 1.00 68.75 C ANISOU 2931 CB TYR A 400 7840 8913 9369 -410 -160 -266 C ATOM 2932 CG TYR A 400 28.004 91.953 100.655 1.00 74.22 C ANISOU 2932 CG TYR A 400 8610 9614 9977 -410 -227 -328 C ATOM 2933 CD1 TYR A 400 26.930 91.831 101.528 1.00 78.03 C ANISOU 2933 CD1 TYR A 400 9261 10107 10279 -427 -271 -433 C ATOM 2934 CD2 TYR A 400 28.934 90.923 100.613 1.00 77.60 C ANISOU 2934 CD2 TYR A 400 8932 10031 10520 -387 -230 -263 C ATOM 2935 CE1 TYR A 400 26.790 90.712 102.334 1.00 84.45 C ANISOU 2935 CE1 TYR A 400 10141 10927 11020 -429 -322 -460 C ATOM 2936 CE2 TYR A 400 28.803 89.805 101.411 1.00 78.72 C ANISOU 2936 CE2 TYR A 400 9138 10169 10604 -389 -298 -298 C ATOM 2937 CZ TYR A 400 27.731 89.703 102.268 1.00 83.21 C ANISOU 2937 CZ TYR A 400 9879 10754 10983 -414 -347 -390 C ATOM 2938 OH TYR A 400 27.607 88.586 103.062 1.00 83.58 O ANISOU 2938 OH TYR A 400 9986 10796 10976 -418 -407 -396 O ATOM 2939 N TYR A 401 27.421 94.489 96.942 1.00 73.44 N ANISOU 2939 N TYR A 401 8356 9635 9911 -305 168 -159 N ATOM 2940 CA TYR A 401 27.849 95.475 95.955 1.00 73.64 C ANISOU 2940 CA TYR A 401 8282 9662 10034 -295 257 -24 C ATOM 2941 C TYR A 401 26.763 96.515 95.699 1.00 70.15 C ANISOU 2941 C TYR A 401 7921 9220 9513 -306 249 -49 C ATOM 2942 O TYR A 401 27.032 97.722 95.697 1.00 77.13 O ANISOU 2942 O TYR A 401 8746 10024 10536 -352 206 34 O ATOM 2943 CB TYR A 401 28.243 94.769 94.658 1.00 81.13 C ANISOU 2943 CB TYR A 401 9182 10712 10933 -198 455 46 C ATOM 2944 CG TYR A 401 28.719 95.702 93.572 1.00 91.24 C ANISOU 2944 CG TYR A 401 10367 12012 12289 -175 584 216 C ATOM 2945 CD1 TYR A 401 30.031 96.158 93.548 1.00 91.69 C ANISOU 2945 CD1 TYR A 401 10234 12001 12601 -200 612 385 C ATOM 2946 CD2 TYR A 401 27.859 96.123 92.567 1.00 95.96 C ANISOU 2946 CD2 TYR A 401 11053 12690 12717 -131 670 229 C ATOM 2947 CE1 TYR A 401 30.470 97.012 92.555 1.00 93.60 C ANISOU 2947 CE1 TYR A 401 10376 12260 12927 -179 751 571 C ATOM 2948 CE2 TYR A 401 28.288 96.976 91.571 1.00 99.34 C ANISOU 2948 CE2 TYR A 401 11405 13142 13199 -108 794 408 C ATOM 2949 CZ TYR A 401 29.595 97.418 91.569 1.00 97.33 C ANISOU 2949 CZ TYR A 401 10960 12823 13197 -130 848 582 C ATOM 2950 OH TYR A 401 30.024 98.268 90.576 1.00 97.79 O ANISOU 2950 OH TYR A 401 10930 12903 13322 -108 992 790 O ATOM 2951 N PHE A 402 25.529 96.068 95.484 1.00 60.34 N ANISOU 2951 N PHE A 402 6798 8048 8080 -266 280 -151 N ATOM 2952 CA PHE A 402 24.430 96.975 95.179 1.00 59.74 C ANISOU 2952 CA PHE A 402 6779 7971 7951 -264 276 -161 C ATOM 2953 C PHE A 402 23.752 97.539 96.421 1.00 59.75 C ANISOU 2953 C PHE A 402 6854 7878 7972 -311 164 -264 C ATOM 2954 O PHE A 402 22.765 98.271 96.289 1.00 60.26 O ANISOU 2954 O PHE A 402 6957 7922 8017 -299 166 -281 O ATOM 2955 CB PHE A 402 23.389 96.269 94.306 1.00 58.91 C ANISOU 2955 CB PHE A 402 6750 7974 7661 -202 344 -205 C ATOM 2956 CG PHE A 402 23.907 95.862 92.959 1.00 65.51 C ANISOU 2956 CG PHE A 402 7566 8902 8422 -138 466 -120 C ATOM 2957 CD1 PHE A 402 23.949 96.771 91.915 1.00 64.15 C ANISOU 2957 CD1 PHE A 402 7368 8760 8246 -118 531 14 C ATOM 2958 CD2 PHE A 402 24.352 94.570 92.735 1.00 75.15 C ANISOU 2958 CD2 PHE A 402 8808 10176 9572 -91 524 -170 C ATOM 2959 CE1 PHE A 402 24.426 96.399 90.673 1.00 69.58 C ANISOU 2959 CE1 PHE A 402 8070 9544 8824 -45 667 95 C ATOM 2960 CE2 PHE A 402 24.829 94.192 91.495 1.00 75.03 C ANISOU 2960 CE2 PHE A 402 8804 10240 9462 -12 661 -109 C ATOM 2961 CZ PHE A 402 24.867 95.107 90.463 1.00 75.16 C ANISOU 2961 CZ PHE A 402 8814 10302 9440 13 740 23 C ATOM 2962 N SER A 403 24.253 97.227 97.618 1.00 59.45 N ANISOU 2962 N SER A 403 6844 7776 7966 -354 68 -330 N ATOM 2963 CA SER A 403 23.613 97.725 98.832 1.00 63.01 C ANISOU 2963 CA SER A 403 7409 8143 8389 -382 -19 -442 C ATOM 2964 C SER A 403 23.834 99.222 98.999 1.00 77.34 C ANISOU 2964 C SER A 403 9211 9829 10345 -420 -89 -415 C ATOM 2965 O SER A 403 22.928 99.946 99.428 1.00 84.76 O ANISOU 2965 O SER A 403 10237 10707 11262 -406 -94 -492 O ATOM 2966 CB SER A 403 24.141 96.972 100.051 1.00 57.52 C ANISOU 2966 CB SER A 403 6778 7420 7657 -417 -117 -509 C ATOM 2967 OG SER A 403 25.499 97.296 100.301 1.00 57.53 O ANISOU 2967 OG SER A 403 6701 7341 7817 -477 -232 -439 O ATOM 2968 N SER A 404 25.027 99.701 98.667 1.00 77.41 N ANISOU 2968 N SER A 404 9103 9781 10528 -466 -139 -300 N ATOM 2969 CA SER A 404 25.384 101.096 98.854 1.00 75.58 C ANISOU 2969 CA SER A 404 8843 9397 10477 -519 -236 -262 C ATOM 2970 C SER A 404 26.357 101.488 97.756 1.00 79.07 C ANISOU 2970 C SER A 404 9097 9841 11104 -537 -185 -59 C ATOM 2971 O SER A 404 27.121 100.639 97.279 1.00 78.77 O ANISOU 2971 O SER A 404 8962 9890 11077 -522 -116 27 O ATOM 2972 CB SER A 404 26.012 101.330 100.237 1.00 81.53 C ANISOU 2972 CB SER A 404 9679 10011 11288 -592 -436 -355 C ATOM 2973 OG SER A 404 26.385 102.685 100.419 1.00 92.55 O ANISOU 2973 OG SER A 404 11055 11230 12880 -651 -559 -332 O ATOM 2974 N PRO A 405 26.349 102.752 97.324 1.00 83.13 N ANISOU 2974 N PRO A 405 9554 10257 11775 -560 -199 32 N ATOM 2975 CA PRO A 405 27.345 103.204 96.341 1.00 77.40 C ANISOU 2975 CA PRO A 405 8638 9521 11250 -583 -140 258 C ATOM 2976 C PRO A 405 28.770 103.226 96.871 1.00 70.82 C ANISOU 2976 C PRO A 405 7677 8580 10653 -666 -266 336 C ATOM 2977 O PRO A 405 29.689 103.525 96.101 1.00 71.57 O ANISOU 2977 O PRO A 405 7582 8663 10947 -684 -197 549 O ATOM 2978 CB PRO A 405 26.866 104.621 95.988 1.00 78.06 C ANISOU 2978 CB PRO A 405 8708 9489 11461 -598 -160 324 C ATOM 2979 CG PRO A 405 26.058 105.050 97.169 1.00 80.49 C ANISOU 2979 CG PRO A 405 9186 9676 11720 -610 -294 109 C ATOM 2980 CD PRO A 405 25.375 103.807 97.649 1.00 79.29 C ANISOU 2980 CD PRO A 405 9165 9662 11299 -554 -243 -53 C ATOM 2981 N SER A 406 28.985 102.922 98.154 1.00 70.71 N ANISOU 2981 N SER A 406 7755 8486 10627 -718 -450 188 N ATOM 2982 CA SER A 406 30.340 102.895 98.694 1.00 80.22 C ANISOU 2982 CA SER A 406 8831 9578 12071 -806 -615 270 C ATOM 2983 C SER A 406 31.129 101.698 98.180 1.00 79.99 C ANISOU 2983 C SER A 406 8657 9679 12056 -764 -487 385 C ATOM 2984 O SER A 406 32.362 101.757 98.103 1.00 84.42 O ANISOU 2984 O SER A 406 9015 10168 12892 -816 -539 549 O ATOM 2985 CB SER A 406 30.297 102.881 100.223 1.00 88.40 C ANISOU 2985 CB SER A 406 10044 10496 13047 -869 -870 75 C ATOM 2986 OG SER A 406 29.705 104.064 100.729 1.00 93.69 O ANISOU 2986 OG SER A 406 10852 11013 13733 -900 -988 -38 O ATOM 2987 N PHE A 407 30.443 100.604 97.830 1.00 76.09 N ANISOU 2987 N PHE A 407 8254 9360 11295 -668 -322 304 N ATOM 2988 CA PHE A 407 31.154 99.438 97.308 1.00 74.32 C ANISOU 2988 CA PHE A 407 7912 9245 11082 -611 -186 392 C ATOM 2989 C PHE A 407 31.742 99.693 95.926 1.00 70.35 C ANISOU 2989 C PHE A 407 7227 8800 10705 -559 35 610 C ATOM 2990 O PHE A 407 32.946 99.447 95.739 1.00 63.16 O ANISOU 2990 O PHE A 407 6115 7858 10025 -565 73 770 O ATOM 2991 CB PHE A 407 30.236 98.212 97.328 1.00 73.86 C ANISOU 2991 CB PHE A 407 8013 9329 10719 -528 -93 234 C ATOM 2992 CG PHE A 407 30.118 97.568 98.678 1.00 72.38 C ANISOU 2992 CG PHE A 407 7947 9102 10454 -568 -273 88 C ATOM 2993 CD1 PHE A 407 29.256 98.080 99.634 1.00 70.98 C ANISOU 2993 CD1 PHE A 407 7954 8865 10150 -607 -406 -65 C ATOM 2994 CD2 PHE A 407 30.873 96.450 98.991 1.00 67.44 C ANISOU 2994 CD2 PHE A 407 7254 8494 9878 -558 -296 112 C ATOM 2995 CE1 PHE A 407 29.149 97.487 100.877 1.00 68.90 C ANISOU 2995 CE1 PHE A 407 7824 8575 9779 -637 -553 -184 C ATOM 2996 CE2 PHE A 407 30.770 95.854 100.231 1.00 65.90 C ANISOU 2996 CE2 PHE A 407 7177 8264 9598 -596 -468 2 C ATOM 2997 CZ PHE A 407 29.908 96.373 101.175 1.00 66.76 C ANISOU 2997 CZ PHE A 407 7488 8329 9549 -637 -594 -143 C ATOM 2998 N PRO A 408 30.988 100.173 94.927 1.00 71.15 N ANISOU 2998 N PRO A 408 7380 8982 10673 -503 191 647 N ATOM 2999 CA PRO A 408 31.640 100.501 93.649 1.00 79.03 C ANISOU 2999 CA PRO A 408 8216 10030 11780 -456 405 883 C ATOM 3000 C PRO A 408 32.629 101.643 93.769 1.00 91.69 C ANISOU 3000 C PRO A 408 9612 11470 13758 -553 318 1085 C ATOM 3001 O PRO A 408 33.573 101.719 92.974 1.00100.34 O ANISOU 3001 O PRO A 408 10508 12582 15034 -525 488 1317 O ATOM 3002 CB PRO A 408 30.462 100.861 92.734 1.00 74.29 C ANISOU 3002 CB PRO A 408 7758 9535 10933 -393 522 863 C ATOM 3003 CG PRO A 408 29.398 101.311 93.660 1.00 70.92 C ANISOU 3003 CG PRO A 408 7486 9031 10427 -447 328 673 C ATOM 3004 CD PRO A 408 29.539 100.446 94.876 1.00 65.12 C ANISOU 3004 CD PRO A 408 6812 8265 9666 -477 187 503 C ATOM 3005 N ASN A 409 32.448 102.532 94.749 1.00 92.32 N ANISOU 3005 N ASN A 409 9733 11379 13967 -663 61 1005 N ATOM 3006 CA ASN A 409 33.415 103.600 94.967 1.00100.30 C ANISOU 3006 CA ASN A 409 10546 12196 15369 -774 -76 1182 C ATOM 3007 C ASN A 409 34.700 103.095 95.606 1.00 99.36 C ANISOU 3007 C ASN A 409 10246 11990 15516 -834 -200 1256 C ATOM 3008 O ASN A 409 35.729 103.770 95.510 1.00106.98 O ANISOU 3008 O ASN A 409 10973 12815 16859 -913 -259 1473 O ATOM 3009 CB ASN A 409 32.805 104.707 95.827 1.00106.93 C ANISOU 3009 CB ASN A 409 11515 12855 16256 -866 -330 1045 C ATOM 3010 CG ASN A 409 31.778 105.526 95.073 1.00112.96 C ANISOU 3010 CG ASN A 409 12366 13649 16904 -822 -218 1062 C ATOM 3011 OD1 ASN A 409 31.762 105.538 93.842 1.00117.49 O ANISOU 3011 OD1 ASN A 409 12860 14346 17435 -752 18 1243 O ATOM 3012 ND2 ASN A 409 30.915 106.216 95.808 1.00117.75 N ANISOU 3012 ND2 ASN A 409 13145 14140 17456 -854 -383 880 N ATOM 3013 N PHE A 410 34.667 101.930 96.257 1.00 90.22 N ANISOU 3013 N PHE A 410 9181 10899 14198 -804 -251 1100 N ATOM 3014 CA PHE A 410 35.903 101.341 96.760 1.00 84.96 C ANISOU 3014 CA PHE A 410 8325 10163 13794 -846 -355 1197 C ATOM 3015 C PHE A 410 36.776 100.851 95.613 1.00 79.16 C ANISOU 3015 C PHE A 410 7342 9522 13213 -754 -49 1442 C ATOM 3016 O PHE A 410 37.984 101.112 95.583 1.00 79.55 O ANISOU 3016 O PHE A 410 7109 9458 13657 -808 -80 1668 O ATOM 3017 CB PHE A 410 35.597 100.197 97.728 1.00 82.49 C ANISOU 3017 CB PHE A 410 8182 9899 13263 -830 -481 983 C ATOM 3018 CG PHE A 410 36.811 99.400 98.129 1.00 77.10 C ANISOU 3018 CG PHE A 410 7300 9166 12830 -850 -562 1095 C ATOM 3019 CD1 PHE A 410 37.659 99.857 99.124 1.00 74.78 C ANISOU 3019 CD1 PHE A 410 6903 8675 12835 -989 -900 1147 C ATOM 3020 CD2 PHE A 410 37.101 98.192 97.514 1.00 79.40 C ANISOU 3020 CD2 PHE A 410 7509 9591 13067 -726 -317 1145 C ATOM 3021 CE1 PHE A 410 38.775 99.127 99.497 1.00 76.74 C ANISOU 3021 CE1 PHE A 410 6947 8867 13344 -1010 -998 1271 C ATOM 3022 CE2 PHE A 410 38.215 97.458 97.883 1.00 81.28 C ANISOU 3022 CE2 PHE A 410 7544 9769 13568 -734 -386 1259 C ATOM 3023 CZ PHE A 410 39.052 97.926 98.875 1.00 76.76 C ANISOU 3023 CZ PHE A 410 6846 9005 13312 -878 -730 1334 C ATOM 3024 N PHE A 411 36.181 100.132 94.658 1.00 76.44 N ANISOU 3024 N PHE A 411 7101 9376 12566 -609 252 1402 N ATOM 3025 CA PHE A 411 36.962 99.626 93.535 1.00 76.99 C ANISOU 3025 CA PHE A 411 6982 9544 12726 -493 580 1611 C ATOM 3026 C PHE A 411 37.305 100.731 92.545 1.00 87.34 C ANISOU 3026 C PHE A 411 8136 10837 14213 -497 752 1874 C ATOM 3027 O PHE A 411 38.328 100.648 91.855 1.00 91.02 O ANISOU 3027 O PHE A 411 8355 11311 14916 -443 977 2126 O ATOM 3028 CB PHE A 411 36.208 98.496 92.835 1.00 71.91 C ANISOU 3028 CB PHE A 411 6540 9103 11679 -337 820 1461 C ATOM 3029 CG PHE A 411 35.892 97.333 93.732 1.00 72.14 C ANISOU 3029 CG PHE A 411 6704 9148 11560 -327 679 1234 C ATOM 3030 CD1 PHE A 411 36.861 96.393 94.040 1.00 72.68 C ANISOU 3030 CD1 PHE A 411 6614 9182 11819 -294 694 1288 C ATOM 3031 CD2 PHE A 411 34.624 97.179 94.265 1.00 71.86 C ANISOU 3031 CD2 PHE A 411 6937 9151 11214 -347 539 987 C ATOM 3032 CE1 PHE A 411 36.573 95.323 94.866 1.00 72.78 C ANISOU 3032 CE1 PHE A 411 6748 9200 11704 -287 557 1102 C ATOM 3033 CE2 PHE A 411 34.328 96.113 95.091 1.00 72.58 C ANISOU 3033 CE2 PHE A 411 7145 9255 11176 -341 422 807 C ATOM 3034 CZ PHE A 411 35.303 95.182 95.392 1.00 75.99 C ANISOU 3034 CZ PHE A 411 7431 9653 11789 -313 424 865 C ATOM 3035 N SER A 412 36.471 101.772 92.457 1.00 91.39 N ANISOU 3035 N SER A 412 8776 11319 14628 -553 666 1837 N ATOM 3036 CA SER A 412 36.775 102.882 91.559 1.00 96.57 C ANISOU 3036 CA SER A 412 9282 11941 15469 -568 808 2108 C ATOM 3037 C SER A 412 37.943 103.708 92.084 1.00105.24 C ANISOU 3037 C SER A 412 10080 12812 17095 -709 628 2325 C ATOM 3038 O SER A 412 38.821 104.110 91.312 1.00117.73 O ANISOU 3038 O SER A 412 11402 14372 18957 -696 827 2638 O ATOM 3039 CB SER A 412 35.538 103.758 91.362 1.00 91.19 C ANISOU 3039 CB SER A 412 8811 11268 14567 -589 742 2012 C ATOM 3040 OG SER A 412 35.250 104.505 92.530 1.00 90.53 O ANISOU 3040 OG SER A 412 8784 10991 14622 -726 394 1870 O ATOM 3041 N THR A 413 37.971 103.974 93.391 1.00104.89 N ANISOU 3041 N THR A 413 10070 12588 17194 -845 247 2169 N ATOM 3042 CA THR A 413 39.106 104.666 93.988 1.00106.29 C ANISOU 3042 CA THR A 413 9975 12526 17886 -994 9 2352 C ATOM 3043 C THR A 413 40.327 103.766 94.128 1.00107.19 C ANISOU 3043 C THR A 413 9829 12631 18265 -975 54 2495 C ATOM 3044 O THR A 413 41.451 104.275 94.192 1.00111.45 O ANISOU 3044 O THR A 413 10048 13004 19295 -1068 -28 2757 O ATOM 3045 CB THR A 413 38.725 105.238 95.356 1.00100.89 C ANISOU 3045 CB THR A 413 9458 11645 17230 -1140 -437 2116 C ATOM 3046 OG1 THR A 413 38.223 104.190 96.196 1.00 91.33 O ANISOU 3046 OG1 THR A 413 8480 10521 15702 -1103 -548 1830 O ATOM 3047 CG2 THR A 413 37.662 106.318 95.204 1.00101.18 C ANISOU 3047 CG2 THR A 413 9689 11637 17116 -1162 -478 2020 C ATOM 3048 N LEU A 414 40.133 102.446 94.181 1.00105.81 N ANISOU 3048 N LEU A 414 9771 12618 17814 -858 175 2341 N ATOM 3049 CA LEU A 414 41.273 101.536 94.159 1.00105.81 C ANISOU 3049 CA LEU A 414 9513 12619 18073 -808 276 2495 C ATOM 3050 C LEU A 414 41.903 101.491 92.774 1.00110.29 C ANISOU 3050 C LEU A 414 9850 13290 18766 -677 729 2795 C ATOM 3051 O LEU A 414 43.131 101.424 92.646 1.00115.08 O ANISOU 3051 O LEU A 414 10165 13804 19757 -666 794 3041 O ATOM 3052 CB LEU A 414 40.840 100.138 94.607 1.00 99.63 C ANISOU 3052 CB LEU A 414 8932 11961 16963 -716 276 2241 C ATOM 3053 CG LEU A 414 41.906 99.051 94.774 1.00 98.72 C ANISOU 3053 CG LEU A 414 8585 11831 17094 -657 334 2349 C ATOM 3054 CD1 LEU A 414 41.554 98.151 95.947 1.00 97.24 C ANISOU 3054 CD1 LEU A 414 8590 11630 16726 -689 51 2092 C ATOM 3055 CD2 LEU A 414 42.058 98.222 93.506 1.00 97.92 C ANISOU 3055 CD2 LEU A 414 8434 11912 16859 -446 823 2440 C ATOM 3056 N ILE A 415 41.078 101.529 91.725 1.00113.43 N ANISOU 3056 N ILE A 415 10441 13873 18784 -554 1033 2761 N ATOM 3057 CA ILE A 415 41.611 101.547 90.369 1.00120.66 C ANISOU 3057 CA ILE A 415 11192 14902 19753 -418 1482 3043 C ATOM 3058 C ILE A 415 42.092 102.937 89.971 1.00126.25 C ANISOU 3058 C ILE A 415 11717 15476 20775 -505 1475 3335 C ATOM 3059 O ILE A 415 42.823 103.070 88.981 1.00130.76 O ANISOU 3059 O ILE A 415 12197 16081 21406 -384 1771 3574 O ATOM 3060 CB ILE A 415 40.566 101.022 89.368 1.00122.05 C ANISOU 3060 CB ILE A 415 11691 15325 19360 -247 1780 2889 C ATOM 3061 CG1 ILE A 415 41.256 100.333 88.189 1.00128.80 C ANISOU 3061 CG1 ILE A 415 12433 16323 20184 -49 2261 3082 C ATOM 3062 CG2 ILE A 415 39.666 102.147 88.880 1.00121.96 C ANISOU 3062 CG2 ILE A 415 11838 15337 19164 -294 1758 2910 C ATOM 3063 CD1 ILE A 415 42.041 99.098 88.581 1.00130.93 C ANISOU 3063 CD1 ILE A 415 12567 16576 20604 31 2319 3040 C ATOM 3064 N ASN A 416 41.705 103.977 90.717 1.00125.82 N ANISOU 3064 N ASN A 416 11678 15255 20875 -690 1118 3285 N ATOM 3065 CA ASN A 416 42.266 105.304 90.482 1.00127.90 C ANISOU 3065 CA ASN A 416 11816 15337 21445 -762 1031 3523 C ATOM 3066 C ASN A 416 43.765 105.315 90.744 1.00137.47 C ANISOU 3066 C ASN A 416 12786 16369 23075 -762 945 3720 C ATOM 3067 O ASN A 416 44.522 106.006 90.051 1.00143.33 O ANISOU 3067 O ASN A 416 13375 17039 24046 -721 1082 4005 O ATOM 3068 CB ASN A 416 41.563 106.339 91.362 1.00124.84 C ANISOU 3068 CB ASN A 416 11519 14770 21146 -955 631 3382 C ATOM 3069 CG ASN A 416 40.269 106.844 90.754 1.00126.40 C ANISOU 3069 CG ASN A 416 11935 15086 21003 -931 750 3306 C ATOM 3070 OD1 ASN A 416 39.801 106.326 89.740 1.00130.52 O ANISOU 3070 OD1 ASN A 416 12588 15844 21159 -770 1097 3320 O ATOM 3071 ND2 ASN A 416 39.681 107.860 91.376 1.00124.29 N ANISOU 3071 ND2 ASN A 416 11784 14646 20797 -1059 436 3188 N ATOM 3072 N ARG A 417 44.213 104.552 91.742 1.00141.13 N ANISOU 3072 N ARG A 417 13211 16756 23655 -804 712 3589 N ATOM 3073 CA ARG A 417 45.633 104.428 92.036 1.00150.68 C ANISOU 3073 CA ARG A 417 14190 17794 25266 -798 620 3779 C ATOM 3074 C ARG A 417 46.375 103.601 90.995 1.00155.07 C ANISOU 3074 C ARG A 417 14628 18484 25809 -593 1072 3968 C ATOM 3075 O ARG A 417 47.611 103.622 90.983 1.00163.92 O ANISOU 3075 O ARG A 417 15527 19460 27298 -565 1074 4194 O ATOM 3076 CB ARG A 417 45.815 103.813 93.425 1.00154.66 C ANISOU 3076 CB ARG A 417 14721 18185 25858 -902 222 3579 C ATOM 3077 CG ARG A 417 44.902 104.422 94.480 1.00155.36 C ANISOU 3077 CG ARG A 417 15007 18179 25844 -1080 -198 3320 C ATOM 3078 CD ARG A 417 44.849 103.572 95.740 1.00155.49 C ANISOU 3078 CD ARG A 417 15120 18159 25800 -1149 -524 3085 C ATOM 3079 NE ARG A 417 43.758 103.977 96.623 1.00154.32 N ANISOU 3079 NE ARG A 417 15223 17975 25437 -1284 -843 2796 N ATOM 3080 CZ ARG A 417 43.884 104.848 97.619 1.00158.49 C ANISOU 3080 CZ ARG A 417 15837 18271 26111 -1434 -1282 2712 C ATOM 3081 NH1 ARG A 417 45.058 105.412 97.866 1.00164.23 N ANISOU 3081 NH1 ARG A 417 16397 18781 27220 -1476 -1474 2909 N ATOM 3082 NH2 ARG A 417 42.834 105.156 98.369 1.00156.61 N ANISOU 3082 NH2 ARG A 417 15863 18008 25632 -1533 -1528 2427 N ATOM 3083 N CYS A 418 45.654 102.882 90.136 1.00153.57 N ANISOU 3083 N CYS A 418 14592 18552 25207 -445 1446 3875 N ATOM 3084 CA CYS A 418 46.242 102.086 89.060 1.00152.27 C ANISOU 3084 CA CYS A 418 14380 18524 24951 -229 1904 4012 C ATOM 3085 C CYS A 418 47.260 101.080 89.591 1.00147.96 C ANISOU 3085 C CYS A 418 13680 17888 24650 -180 1861 4028 C ATOM 3086 O CYS A 418 46.909 100.157 90.326 1.00140.80 O ANISOU 3086 O CYS A 418 12854 17018 23624 -196 1719 3797 O ATOM 3087 CB CYS A 418 46.891 102.999 88.014 1.00154.43 C ANISOU 3087 CB CYS A 418 14527 18762 25389 -164 2146 4342 C ATOM 3088 SG CYS A 418 47.399 102.164 86.493 1.00154.84 S ANISOU 3088 SG CYS A 418 14601 19014 25218 120 2757 4491 S TER 3089 CYS A 418 HETATM 3090 C1 OLA A 501 33.871 89.861 113.640 1.00112.97 C ANISOU 3090 C1 OLA A 501 14498 13789 14637 -1141 -2970 -38 C HETATM 3091 O1 OLA A 501 34.216 89.053 112.758 1.00110.70 O ANISOU 3091 O1 OLA A 501 13934 13546 14583 -1079 -2768 66 O HETATM 3092 O2 OLA A 501 32.982 89.626 114.480 1.00111.41 O ANISOU 3092 O2 OLA A 501 14606 13659 14067 -1120 -2958 -110 O HETATM 3093 C2 OLA A 501 34.562 91.213 113.684 1.00116.02 C ANISOU 3093 C2 OLA A 501 14859 14031 15192 -1235 -3220 -74 C HETATM 3094 C3 OLA A 501 33.633 92.376 113.540 1.00115.42 C ANISOU 3094 C3 OLA A 501 15153 13946 14755 -1240 -3238 -290 C HETATM 3095 C4 OLA A 501 34.358 93.677 113.256 1.00111.46 C ANISOU 3095 C4 OLA A 501 14570 13331 14450 -1284 -3276 -365 C HETATM 3096 C5 OLA A 501 35.143 94.222 114.419 1.00116.62 C ANISOU 3096 C5 OLA A 501 15315 13793 15204 -1420 -3753 -365 C HETATM 3097 C6 OLA A 501 35.997 95.416 114.074 1.00119.52 C ANISOU 3097 C6 OLA A 501 15491 14015 15906 -1482 -3816 -369 C HETATM 3098 C7 OLA A 501 37.081 95.125 113.045 1.00120.48 C ANISOU 3098 C7 OLA A 501 15172 14058 16547 -1546 -3931 -122 C HETATM 3099 C8 OLA A 501 38.089 94.117 113.493 1.00117.83 C ANISOU 3099 C8 OLA A 501 14810 13678 16282 -1613 -4267 22 C HETATM 3100 C9 OLA A 501 38.919 93.578 112.373 1.00111.81 C ANISOU 3100 C9 OLA A 501 13575 12905 16001 -1606 -4195 279 C HETATM 3101 C1 OLA A 502 1.470 63.384 104.412 1.00108.79 C ANISOU 3101 C1 OLA A 502 10624 11082 19629 -1877 -1271 2030 C HETATM 3102 O1 OLA A 502 1.942 63.145 105.545 1.00109.85 O ANISOU 3102 O1 OLA A 502 10789 11304 19645 -1834 -1011 2234 O HETATM 3103 O2 OLA A 502 0.228 63.385 104.264 1.00111.68 O ANISOU 3103 O2 OLA A 502 10731 11353 20350 -1959 -1325 2206 O HETATM 3104 C2 OLA A 502 2.378 63.670 103.238 1.00100.88 C ANISOU 3104 C2 OLA A 502 9911 10106 18313 -1807 -1507 1584 C HETATM 3105 C3 OLA A 502 2.620 65.171 103.119 1.00 94.69 C ANISOU 3105 C3 OLA A 502 9257 9636 17084 -1688 -1311 1445 C HETATM 3106 C4 OLA A 502 3.893 65.459 102.332 1.00 95.33 C ANISOU 3106 C4 OLA A 502 9659 9802 16759 -1583 -1418 1062 C HETATM 3107 C5 OLA A 502 4.296 66.927 102.419 1.00 95.91 C ANISOU 3107 C5 OLA A 502 9865 10189 16388 -1462 -1188 964 C HETATM 3108 C6 OLA A 502 3.101 67.864 102.290 1.00 96.96 C ANISOU 3108 C6 OLA A 502 9814 10402 16624 -1488 -1123 1078 C HETATM 3109 C7 OLA A 502 3.364 68.941 101.242 1.00 94.20 C ANISOU 3109 C7 OLA A 502 9624 10189 15979 -1419 -1215 797 C HETATM 3110 C8 OLA A 502 3.062 70.322 101.812 1.00 90.64 C ANISOU 3110 C8 OLA A 502 9130 9983 15327 -1341 -914 900 C HETATM 3111 C9 OLA A 502 3.711 70.437 103.170 1.00 87.52 C ANISOU 3111 C9 OLA A 502 8804 9734 14714 -1268 -582 1042 C HETATM 3112 C10 OLA A 502 3.219 71.419 104.146 1.00 90.28 C ANISOU 3112 C10 OLA A 502 9078 10264 14962 -1206 -240 1232 C HETATM 3113 C11 OLA A 502 2.894 72.828 103.712 1.00 90.39 C ANISOU 3113 C11 OLA A 502 9102 10426 14817 -1138 -166 1134 C HETATM 3114 C12 OLA A 502 2.421 73.623 104.923 1.00 89.85 C ANISOU 3114 C12 OLA A 502 8967 10506 14666 -1064 221 1346 C HETATM 3115 C13 OLA A 502 3.555 73.815 105.924 1.00 84.00 C ANISOU 3115 C13 OLA A 502 8471 9918 13528 -978 427 1317 C HETATM 3116 C14 OLA A 502 3.233 73.170 107.269 1.00 84.21 C ANISOU 3116 C14 OLA A 502 8424 9935 13637 -986 672 1616 C HETATM 3117 C15 OLA A 502 1.783 73.396 107.683 1.00 82.79 C ANISOU 3117 C15 OLA A 502 7972 9729 13757 -994 890 1885 C HETATM 3118 C16 OLA A 502 1.570 73.032 109.148 1.00 81.97 C ANISOU 3118 C16 OLA A 502 7856 9675 13616 -962 1224 2182 C HETATM 3119 C17 OLA A 502 0.133 73.299 109.581 1.00 83.60 C ANISOU 3119 C17 OLA A 502 7777 9859 14127 -948 1496 2466 C HETATM 3120 C18 OLA A 502 0.054 73.530 111.086 1.00 87.14 C ANISOU 3120 C18 OLA A 502 8322 10449 14338 -845 1934 2690 C HETATM 3121 C11 OLA A 503 12.434 90.185 111.237 1.00 72.74 C HETATM 3122 C12 OLA A 503 12.114 88.877 110.589 1.00 73.10 C HETATM 3123 C13 OLA A 503 12.208 87.680 111.517 1.00 73.31 C HETATM 3124 C14 OLA A 503 11.864 86.364 110.868 1.00 73.17 C HETATM 3125 C15 OLA A 503 11.963 85.176 111.791 1.00 73.36 C HETATM 3126 C16 OLA A 503 11.635 83.856 111.142 1.00 73.83 C HETATM 3127 C17 OLA A 503 11.764 82.670 112.056 1.00 73.44 C HETATM 3128 C11 OLA A 504 26.868 90.111 116.482 1.00 68.98 C HETATM 3129 C12 OLA A 504 27.167 88.833 115.766 1.00 69.14 C HETATM 3130 C13 OLA A 504 27.029 87.590 116.625 1.00 69.76 C HETATM 3131 C14 OLA A 504 27.213 86.295 115.873 1.00 69.98 C HETATM 3132 C15 OLA A 504 27.033 85.058 116.718 1.00 70.28 C HETATM 3133 C16 OLA A 504 26.972 83.771 115.933 1.00 69.66 C HETATM 3134 C17 OLA A 504 28.204 83.463 115.125 1.00 68.79 C HETATM 3135 C1 OLA A 505 29.606 93.090 90.942 1.00 57.43 C HETATM 3136 C2 OLA A 505 29.684 91.689 91.522 1.00 58.36 C HETATM 3137 C3 OLA A 505 30.965 91.376 92.222 1.00 59.69 C HETATM 3138 C4 OLA A 505 30.994 91.872 93.656 1.00 60.75 C HETATM 3139 C5 OLA A 505 32.328 91.687 94.328 1.00 61.51 C HETATM 3140 C6 OLA A 505 32.293 91.727 95.833 1.00 61.33 C HETATM 3141 C7 OLA A 505 31.978 93.091 96.427 1.00 60.38 C HETATM 3142 C8 OLA A 505 32.057 93.131 97.919 1.00 59.83 C HETATM 3143 C1 OLA A 506 8.938 89.993 92.759 1.00 90.81 C HETATM 3144 O1 OLA A 506 8.823 91.096 92.176 1.00 91.38 O HETATM 3145 O2 OLA A 506 9.963 89.788 93.448 1.00 89.86 O HETATM 3146 C2 OLA A 506 7.876 88.921 92.617 1.00 90.78 C HETATM 3147 C3 OLA A 506 6.525 89.380 93.164 1.00 90.67 C HETATM 3148 C4 OLA A 506 6.030 88.438 94.257 1.00 90.96 C HETATM 3149 C5 OLA A 506 4.507 88.273 94.261 1.00 90.79 C HETATM 3150 C6 OLA A 506 3.814 89.073 95.367 1.00 90.35 C HETATM 3151 C7 OLA A 506 4.024 88.473 96.757 1.00 89.79 C HETATM 3152 C8 OLA A 506 2.718 88.064 97.428 1.00 89.27 C HETATM 3153 C9 OLA A 506 3.030 87.127 98.580 1.00 88.69 C HETATM 3154 C10 OLA A 506 2.964 85.791 98.523 1.00 88.35 C HETATM 3155 C11 OLA A 506 2.546 84.994 97.300 1.00 87.90 C HETATM 3156 C12 OLA A 506 3.760 84.533 96.503 1.00 87.16 C HETATM 3157 C13 OLA A 506 3.358 83.522 95.434 1.00 86.65 C HETATM 3158 C14 OLA A 506 3.478 84.112 94.032 1.00 86.31 C HETATM 3159 C18 OLC A 507 1.568 84.585 110.343 1.00 80.51 C HETATM 3160 C10 OLC A 507 1.736 91.265 108.770 1.00 86.07 C HETATM 3161 C9 OLC A 507 2.170 92.479 108.986 1.00 86.31 C HETATM 3162 C17 OLC A 507 0.167 84.468 109.794 1.00 81.36 C HETATM 3163 C11 OLC A 507 0.568 90.914 107.902 1.00 85.89 C HETATM 3164 C8 OLC A 507 1.625 93.715 108.342 1.00 86.65 C HETATM 3165 C24 OLC A 507 4.092 103.815 108.252 1.00 95.57 C HETATM 3166 C16 OLC A 507 -0.852 85.283 110.548 1.00 82.85 C HETATM 3167 C12 OLC A 507 0.259 89.449 107.878 1.00 85.39 C HETATM 3168 C7 OLC A 507 2.258 94.978 108.837 1.00 86.61 C HETATM 3169 C15 OLC A 507 -0.572 86.766 110.575 1.00 83.63 C HETATM 3170 C13 OLC A 507 -0.062 88.858 109.240 1.00 84.90 C HETATM 3171 C6 OLC A 507 3.688 95.212 108.366 1.00 86.41 C HETATM 3172 C14 OLC A 507 -0.425 87.394 109.210 1.00 84.27 C HETATM 3173 C5 OLC A 507 3.826 95.496 106.888 1.00 86.50 C HETATM 3174 C4 OLC A 507 2.812 96.470 106.340 1.00 86.96 C HETATM 3175 C3 OLC A 507 2.480 97.621 107.273 1.00 87.97 C HETATM 3176 C2 OLC A 507 3.519 98.694 107.276 1.00 89.32 C HETATM 3177 C21 OLC A 507 2.666 101.846 108.961 1.00 93.73 C HETATM 3178 C1 OLC A 507 3.349 99.666 108.409 1.00 90.57 C HETATM 3179 C22 OLC A 507 2.697 103.240 108.377 1.00 95.08 C HETATM 3180 O19 OLC A 507 3.385 99.374 109.574 1.00 90.04 O HETATM 3181 O25 OLC A 507 4.064 105.179 107.841 1.00 95.61 O HETATM 3182 O23 OLC A 507 2.054 103.230 107.104 1.00 95.17 O HETATM 3183 O20 OLC A 507 3.147 100.907 107.976 1.00 92.24 O CONECT 48 1337 CONECT 54 2704 CONECT 717 1294 CONECT 1294 717 CONECT 1337 48 CONECT 2704 54 CONECT 3090 3091 3092 3093 CONECT 3091 3090 CONECT 3092 3090 CONECT 3093 3090 3094 CONECT 3094 3093 3095 CONECT 3095 3094 3096 CONECT 3096 3095 3097 CONECT 3097 3096 3098 CONECT 3098 3097 3099 CONECT 3099 3098 3100 CONECT 3100 3099 CONECT 3101 3102 3103 3104 CONECT 3102 3101 CONECT 3103 3101 CONECT 3104 3101 3105 CONECT 3105 3104 3106 CONECT 3106 3105 3107 CONECT 3107 3106 3108 CONECT 3108 3107 3109 CONECT 3109 3108 3110 CONECT 3110 3109 3111 CONECT 3111 3110 3112 CONECT 3112 3111 3113 CONECT 3113 3112 3114 CONECT 3114 3113 3115 CONECT 3115 3114 3116 CONECT 3116 3115 3117 CONECT 3117 3116 3118 CONECT 3118 3117 3119 CONECT 3119 3118 3120 CONECT 3120 3119 CONECT 3121 3122 CONECT 3122 3121 3123 CONECT 3123 3122 3124 CONECT 3124 3123 3125 CONECT 3125 3124 3126 CONECT 3126 3125 3127 CONECT 3127 3126 CONECT 3128 3129 CONECT 3129 3128 3130 CONECT 3130 3129 3131 CONECT 3131 3130 3132 CONECT 3132 3131 3133 CONECT 3133 3132 3134 CONECT 3134 3133 CONECT 3135 3136 CONECT 3136 3135 3137 CONECT 3137 3136 3138 CONECT 3138 3137 3139 CONECT 3139 3138 3140 CONECT 3140 3139 3141 CONECT 3141 3140 3142 CONECT 3142 3141 CONECT 3143 3144 3145 3146 CONECT 3144 3143 CONECT 3145 3143 CONECT 3146 3143 3147 CONECT 3147 3146 3148 CONECT 3148 3147 3149 CONECT 3149 3148 3150 CONECT 3150 3149 3151 CONECT 3151 3150 3152 CONECT 3152 3151 3153 CONECT 3153 3152 3154 CONECT 3154 3153 3155 CONECT 3155 3154 3156 CONECT 3156 3155 3157 CONECT 3157 3156 3158 CONECT 3158 3157 CONECT 3159 3162 CONECT 3160 3161 3163 CONECT 3161 3160 3164 CONECT 3162 3159 3166 CONECT 3163 3160 3167 CONECT 3164 3161 3168 CONECT 3165 3179 3181 CONECT 3166 3162 3169 CONECT 3167 3163 3170 CONECT 3168 3164 3171 CONECT 3169 3166 3172 CONECT 3170 3167 3172 CONECT 3171 3168 3173 CONECT 3172 3169 3170 CONECT 3173 3171 3174 CONECT 3174 3173 3175 CONECT 3175 3174 3176 CONECT 3176 3175 3178 CONECT 3177 3179 3183 CONECT 3178 3176 3180 3183 CONECT 3179 3165 3177 3182 CONECT 3180 3178 CONECT 3181 3165 CONECT 3182 3179 CONECT 3183 3177 3178 MASTER 326 0 7 16 2 0 0 6 3182 1 100 34 END