HEADER MEMBRANE PROTEIN 11-DEC-19 6TOT TITLE CRYSTAL STRUCTURE OF THE OREXIN-1 RECEPTOR IN COMPLEX WITH LEMBOREXANT COMPND MOL_ID: 1; COMPND 2 MOLECULE: OREXIN RECEPTOR TYPE 1; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: OX1R,HYPOCRETIN RECEPTOR TYPE 1; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 OTHER_DETAILS: LEMBOREXANT BOUND IN THE ORTHOSTERIC SITE SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: HCRTR1; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS 7TM, GPCR, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR M.RAPPAS,A.ALI,K.A.BENNETT,J.D.BROWN,S.J.BUCKNELL,M.CONGREVE, AUTHOR 2 R.M.COOKE,G.CSEKE,C.DE GRAAF,A.S.DORE,J.C.ERREY,A.JAZAYERI, AUTHOR 3 F.H.MARSHALL,J.S.MASON,R.MOULD,J.C.PATEL,B.G.TEHAN,M.WEIR, AUTHOR 4 J.A.CHRISTOPHER REVDAT 4 29-JUL-20 6TOT 1 COMPND REMARK HETNAM SITE REVDAT 3 11-MAR-20 6TOT 1 JRNL REVDAT 2 29-JAN-20 6TOT 1 JRNL REVDAT 1 15-JAN-20 6TOT 0 JRNL AUTH M.RAPPAS,A.A.E.ALI,K.A.BENNETT,J.D.BROWN,S.J.BUCKNELL, JRNL AUTH 2 M.CONGREVE,R.M.COOKE,G.CSEKE,C.DE GRAAF,A.S.DORE,J.C.ERREY, JRNL AUTH 3 A.JAZAYERI,F.H.MARSHALL,J.S.MASON,R.MOULD,J.C.PATEL, JRNL AUTH 4 B.G.TEHAN,M.WEIR,J.A.CHRISTOPHER JRNL TITL COMPARISON OF OREXIN 1 AND OREXIN 2 LIGAND BINDING MODES JRNL TITL 2 USING X-RAY CRYSTALLOGRAPHY AND COMPUTATIONAL ANALYSIS. JRNL REF J.MED.CHEM. V. 63 1528 2020 JRNL REFN ISSN 0022-2623 JRNL PMID 31860301 JRNL DOI 10.1021/ACS.JMEDCHEM.9B01787 REMARK 2 REMARK 2 RESOLUTION. 2.22 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.11.7 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) : 2.22 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.02 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 63.9 REMARK 3 NUMBER OF REFLECTIONS : 35526 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.207 REMARK 3 R VALUE (WORKING SET) : 0.206 REMARK 3 FREE R VALUE : 0.239 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 1789 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) : 2.22 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.40 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 6.10 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) : 0.1978 REMARK 3 BIN FREE R VALUE : 0.2489 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 37 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 : 4826 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 357 REMARK 3 SOLVENT ATOMS : 43 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.74 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 4.22190 REMARK 3 B22 (A**2) : -1.61510 REMARK 3 B33 (A**2) : -2.60690 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.95430 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.340 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.294 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.226 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.320 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.236 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 : 0.919 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.892 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 5384 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 7333 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1863 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL REMARK 3 GENERAL PLANES : 809 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 5384 ; 20.000 ; HARMONIC 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 : 696 ; 5.000 ; SEMIHARMONIC 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 : 6015 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.00 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.60 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.82 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: {A|*} REMARK 3 ORIGIN FOR THE GROUP (A): 32.9949 -4.3913 99.0137 REMARK 3 T TENSOR REMARK 3 T11: -0.2612 T22: -0.1244 REMARK 3 T33: -0.0935 T12: 0.0134 REMARK 3 T13: -0.0949 T23: -0.112 REMARK 3 L TENSOR REMARK 3 L11: 0.2812 L22: 3.5754 REMARK 3 L33: 2.3151 L12: -0.3335 REMARK 3 L13: -0.5965 L23: 1.7035 REMARK 3 S TENSOR REMARK 3 S11: 0.0532 S12: 0.1022 S13: -0.1346 REMARK 3 S21: 0.1022 S22: 0.3738 S23: 0.473 REMARK 3 S31: -0.1346 S32: 0.473 S33: -0.4269 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: {B|*} REMARK 3 ORIGIN FOR THE GROUP (A): 27.9832 -26.6851 74.2895 REMARK 3 T TENSOR REMARK 3 T11: -0.0885 T22: -0.2256 REMARK 3 T33: -0.2878 T12: 0.0102 REMARK 3 T13: -0.0208 T23: -0.0071 REMARK 3 L TENSOR REMARK 3 L11: 1.3759 L22: 4.2332 REMARK 3 L33: 1.8937 L12: -0.2351 REMARK 3 L13: -0.3266 L23: 0.4813 REMARK 3 S TENSOR REMARK 3 S11: 0.0244 S12: -0.5302 S13: 0.1202 REMARK 3 S21: -0.5302 S22: 0.0999 S23: 0.0684 REMARK 3 S31: 0.1202 S32: 0.0684 S33: -0.1243 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 6TOT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-DEC-19. REMARK 100 THE DEPOSITION ID IS D_1292105813. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-NOV-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 3.0-6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.96861 REMARK 200 MONOCHROMATOR : SI (111) 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 : STARANISO REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35526 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.220 REMARK 200 RESOLUTION RANGE LOW (A) : 24.020 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 63.9 REMARK 200 DATA REDUNDANCY : 3.800 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.22 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40 REMARK 200 COMPLETENESS FOR SHELL (%) : 6.1 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 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: 6TO7 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 67.52 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.79 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRISODIUM CITRATE 50MM SODIUM REMARK 280 CHLORIDE 50MM LITHIUM SULPHATE 15-34% PEG400, PH 4.6, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 284K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 72.85750 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 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 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B 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 ALA A 25 REMARK 465 ALA A 26 REMARK 465 LEU A 189 REMARK 465 PRO A 190 REMARK 465 GLU A 191 REMARK 465 LEU A 192 REMARK 465 ALA A 193 REMARK 465 ALA A 194 REMARK 465 ARG A 195 REMARK 465 THR A 196 REMARK 465 GLY A 276 REMARK 465 ARG A 277 REMARK 465 GLN A 278 REMARK 465 ILE A 279 REMARK 465 PRO A 280 REMARK 465 GLY A 281 REMARK 465 THR A 282 REMARK 465 THR A 283 REMARK 465 SER A 284 REMARK 465 ALA A 285 REMARK 465 LEU A 377 REMARK 465 PRO A 378 REMARK 465 GLY A 379 REMARK 465 LEU A 380 REMARK 465 ALA A 381 REMARK 465 ALA A 382 REMARK 465 ALA A 383 REMARK 465 HIS A 384 REMARK 465 HIS A 385 REMARK 465 HIS A 386 REMARK 465 HIS A 387 REMARK 465 HIS A 388 REMARK 465 HIS A 389 REMARK 465 HIS A 390 REMARK 465 HIS A 391 REMARK 465 HIS A 392 REMARK 465 ALA B 25 REMARK 465 ALA B 26 REMARK 465 SER B 27 REMARK 465 GLU B 28 REMARK 465 ASP B 29 REMARK 465 GLU B 30 REMARK 465 PHE B 31 REMARK 465 LEU B 32 REMARK 465 ARG B 33 REMARK 465 TYR B 34 REMARK 465 LEU B 35 REMARK 465 TRP B 36 REMARK 465 ARG B 37 REMARK 465 ASP B 38 REMARK 465 TYR B 39 REMARK 465 LEU B 40 REMARK 465 TYR B 41 REMARK 465 PRO B 42 REMARK 465 PRO B 378 REMARK 465 GLY B 379 REMARK 465 LEU B 380 REMARK 465 ALA B 381 REMARK 465 ALA B 382 REMARK 465 ALA B 383 REMARK 465 HIS B 384 REMARK 465 HIS B 385 REMARK 465 HIS B 386 REMARK 465 HIS B 387 REMARK 465 HIS B 388 REMARK 465 HIS B 389 REMARK 465 HIS B 390 REMARK 465 HIS B 391 REMARK 465 HIS B 392 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 TYR A 39 -62.09 -140.24 REMARK 500 ILE A 108 -62.50 -91.95 REMARK 500 LEU A 152 -7.79 72.99 REMARK 500 TYR A 224 -75.01 -131.17 REMARK 500 PRO B 190 -39.63 -35.64 REMARK 500 TYR B 224 -71.94 -126.97 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 SOG A 407 REMARK 610 SOG B 405 REMARK 610 SOG B 407 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6TOD RELATED DB: PDB REMARK 900 RELATED ID: 6TOS RELATED DB: PDB REMARK 900 RELATED ID: 6TO7 RELATED DB: PDB DBREF 6TOT A 28 380 UNP O43613 OX1R_HUMAN 28 380 DBREF 6TOT B 28 380 UNP O43613 OX1R_HUMAN 28 380 SEQADV 6TOT ALA A 25 UNP O43613 EXPRESSION TAG SEQADV 6TOT ALA A 26 UNP O43613 EXPRESSION TAG SEQADV 6TOT SER A 27 UNP O43613 EXPRESSION TAG SEQADV 6TOT ALA A 46 UNP O43613 GLU 46 ENGINEERED MUTATION SEQADV 6TOT LEU A 85 UNP O43613 ILE 85 ENGINEERED MUTATION SEQADV 6TOT ALA A 95 UNP O43613 VAL 95 ENGINEERED MUTATION SEQADV 6TOT LEU A 162 UNP O43613 ARG 162 ENGINEERED MUTATION SEQADV 6TOT ALA A 194 UNP O43613 ASN 194 ENGINEERED MUTATION SEQADV 6TOT ALA A 198 UNP O43613 LEU 198 ENGINEERED MUTATION SEQADV 6TOT ALA A 211 UNP O43613 TYR 211 ENGINEERED MUTATION SEQADV 6TOT A UNP O43613 ALA 253 DELETION SEQADV 6TOT A UNP O43613 LEU 254 DELETION SEQADV 6TOT A UNP O43613 VAL 255 DELETION SEQADV 6TOT A UNP O43613 ARG 256 DELETION SEQADV 6TOT A UNP O43613 ASN 257 DELETION SEQADV 6TOT A UNP O43613 TRP 258 DELETION SEQADV 6TOT A UNP O43613 LYS 259 DELETION SEQADV 6TOT A UNP O43613 ARG 260 DELETION SEQADV 6TOT A UNP O43613 PRO 261 DELETION SEQADV 6TOT A UNP O43613 SER 262 DELETION SEQADV 6TOT A UNP O43613 ASP 263 DELETION SEQADV 6TOT A UNP O43613 GLN 264 DELETION SEQADV 6TOT A UNP O43613 LEU 265 DELETION SEQADV 6TOT A UNP O43613 GLY 266 DELETION SEQADV 6TOT A UNP O43613 ASP 267 DELETION SEQADV 6TOT A UNP O43613 LEU 268 DELETION SEQADV 6TOT A UNP O43613 GLU 269 DELETION SEQADV 6TOT A UNP O43613 GLN 270 DELETION SEQADV 6TOT A UNP O43613 GLY 271 DELETION SEQADV 6TOT A UNP O43613 LEU 272 DELETION SEQADV 6TOT A UNP O43613 SER 273 DELETION SEQADV 6TOT A UNP O43613 GLY 274 DELETION SEQADV 6TOT A UNP O43613 GLU 275 DELETION SEQADV 6TOT A UNP O43613 PRO 276 DELETION SEQADV 6TOT A UNP O43613 GLN 277 DELETION SEQADV 6TOT A UNP O43613 PRO 278 DELETION SEQADV 6TOT A UNP O43613 ARG 279 DELETION SEQADV 6TOT A UNP O43613 ALA 280 DELETION SEQADV 6TOT A UNP O43613 ARG 281 DELETION SEQADV 6TOT A UNP O43613 ALA 282 DELETION SEQADV 6TOT A UNP O43613 PHE 283 DELETION SEQADV 6TOT A UNP O43613 LEU 284 DELETION SEQADV 6TOT VAL A 304 UNP O43613 LEU 304 ENGINEERED MUTATION SEQADV 6TOT ALA A 339 UNP O43613 CYS 339 ENGINEERED MUTATION SEQADV 6TOT TRP A 375 UNP O43613 CYS 375 ENGINEERED MUTATION SEQADV 6TOT TRP A 376 UNP O43613 CYS 376 ENGINEERED MUTATION SEQADV 6TOT ALA A 381 UNP O43613 EXPRESSION TAG SEQADV 6TOT ALA A 382 UNP O43613 EXPRESSION TAG SEQADV 6TOT ALA A 383 UNP O43613 EXPRESSION TAG SEQADV 6TOT HIS A 384 UNP O43613 EXPRESSION TAG SEQADV 6TOT HIS A 385 UNP O43613 EXPRESSION TAG SEQADV 6TOT HIS A 386 UNP O43613 EXPRESSION TAG SEQADV 6TOT HIS A 387 UNP O43613 EXPRESSION TAG SEQADV 6TOT HIS A 388 UNP O43613 EXPRESSION TAG SEQADV 6TOT HIS A 389 UNP O43613 EXPRESSION TAG SEQADV 6TOT HIS A 390 UNP O43613 EXPRESSION TAG SEQADV 6TOT HIS A 391 UNP O43613 EXPRESSION TAG SEQADV 6TOT HIS A 392 UNP O43613 EXPRESSION TAG SEQADV 6TOT ALA B 25 UNP O43613 EXPRESSION TAG SEQADV 6TOT ALA B 26 UNP O43613 EXPRESSION TAG SEQADV 6TOT SER B 27 UNP O43613 EXPRESSION TAG SEQADV 6TOT ALA B 46 UNP O43613 GLU 46 ENGINEERED MUTATION SEQADV 6TOT LEU B 85 UNP O43613 ILE 85 ENGINEERED MUTATION SEQADV 6TOT ALA B 95 UNP O43613 VAL 95 ENGINEERED MUTATION SEQADV 6TOT LEU B 162 UNP O43613 ARG 162 ENGINEERED MUTATION SEQADV 6TOT ALA B 194 UNP O43613 ASN 194 ENGINEERED MUTATION SEQADV 6TOT ALA B 198 UNP O43613 LEU 198 ENGINEERED MUTATION SEQADV 6TOT ALA B 211 UNP O43613 TYR 211 ENGINEERED MUTATION SEQADV 6TOT B UNP O43613 ALA 253 DELETION SEQADV 6TOT B UNP O43613 LEU 254 DELETION SEQADV 6TOT B UNP O43613 VAL 255 DELETION SEQADV 6TOT B UNP O43613 ARG 256 DELETION SEQADV 6TOT B UNP O43613 ASN 257 DELETION SEQADV 6TOT B UNP O43613 TRP 258 DELETION SEQADV 6TOT B UNP O43613 LYS 259 DELETION SEQADV 6TOT B UNP O43613 ARG 260 DELETION SEQADV 6TOT B UNP O43613 PRO 261 DELETION SEQADV 6TOT B UNP O43613 SER 262 DELETION SEQADV 6TOT B UNP O43613 ASP 263 DELETION SEQADV 6TOT B UNP O43613 GLN 264 DELETION SEQADV 6TOT B UNP O43613 LEU 265 DELETION SEQADV 6TOT B UNP O43613 GLY 266 DELETION SEQADV 6TOT B UNP O43613 ASP 267 DELETION SEQADV 6TOT B UNP O43613 LEU 268 DELETION SEQADV 6TOT B UNP O43613 GLU 269 DELETION SEQADV 6TOT B UNP O43613 GLN 270 DELETION SEQADV 6TOT B UNP O43613 GLY 271 DELETION SEQADV 6TOT B UNP O43613 LEU 272 DELETION SEQADV 6TOT B UNP O43613 SER 273 DELETION SEQADV 6TOT B UNP O43613 GLY 274 DELETION SEQADV 6TOT B UNP O43613 GLU 275 DELETION SEQADV 6TOT B UNP O43613 PRO 276 DELETION SEQADV 6TOT B UNP O43613 GLN 277 DELETION SEQADV 6TOT B UNP O43613 PRO 278 DELETION SEQADV 6TOT B UNP O43613 ARG 279 DELETION SEQADV 6TOT B UNP O43613 ALA 280 DELETION SEQADV 6TOT B UNP O43613 ARG 281 DELETION SEQADV 6TOT B UNP O43613 ALA 282 DELETION SEQADV 6TOT B UNP O43613 PHE 283 DELETION SEQADV 6TOT B UNP O43613 LEU 284 DELETION SEQADV 6TOT VAL B 304 UNP O43613 LEU 304 ENGINEERED MUTATION SEQADV 6TOT ALA B 339 UNP O43613 CYS 339 ENGINEERED MUTATION SEQADV 6TOT TRP B 375 UNP O43613 CYS 375 ENGINEERED MUTATION SEQADV 6TOT TRP B 376 UNP O43613 CYS 376 ENGINEERED MUTATION SEQADV 6TOT ALA B 381 UNP O43613 EXPRESSION TAG SEQADV 6TOT ALA B 382 UNP O43613 EXPRESSION TAG SEQADV 6TOT ALA B 383 UNP O43613 EXPRESSION TAG SEQADV 6TOT HIS B 384 UNP O43613 EXPRESSION TAG SEQADV 6TOT HIS B 385 UNP O43613 EXPRESSION TAG SEQADV 6TOT HIS B 386 UNP O43613 EXPRESSION TAG SEQADV 6TOT HIS B 387 UNP O43613 EXPRESSION TAG SEQADV 6TOT HIS B 388 UNP O43613 EXPRESSION TAG SEQADV 6TOT HIS B 389 UNP O43613 EXPRESSION TAG SEQADV 6TOT HIS B 390 UNP O43613 EXPRESSION TAG SEQADV 6TOT HIS B 391 UNP O43613 EXPRESSION TAG SEQADV 6TOT HIS B 392 UNP O43613 EXPRESSION TAG SEQRES 1 A 336 ALA ALA SER GLU ASP GLU PHE LEU ARG TYR LEU TRP ARG SEQRES 2 A 336 ASP TYR LEU TYR PRO LYS GLN TYR ALA TRP VAL LEU ILE SEQRES 3 A 336 ALA ALA TYR VAL ALA VAL PHE VAL VAL ALA LEU VAL GLY SEQRES 4 A 336 ASN THR LEU VAL CYS LEU ALA VAL TRP ARG ASN HIS HIS SEQRES 5 A 336 MET ARG THR VAL THR ASN TYR PHE LEU VAL ASN LEU SER SEQRES 6 A 336 LEU ALA ASP VAL LEU ALA THR ALA ILE CYS LEU PRO ALA SEQRES 7 A 336 SER LEU LEU VAL ASP ILE THR GLU SER TRP LEU PHE GLY SEQRES 8 A 336 HIS ALA LEU CYS LYS VAL ILE PRO TYR LEU GLN ALA VAL SEQRES 9 A 336 SER VAL SER VAL ALA VAL LEU THR LEU SER PHE ILE ALA SEQRES 10 A 336 LEU ASP ARG TRP TYR ALA ILE CYS HIS PRO LEU LEU PHE SEQRES 11 A 336 LYS SER THR ALA ARG ARG ALA LEU GLY SER ILE LEU GLY SEQRES 12 A 336 ILE TRP ALA VAL SER LEU ALA ILE MET VAL PRO GLN ALA SEQRES 13 A 336 ALA VAL MET GLU CYS SER SER VAL LEU PRO GLU LEU ALA SEQRES 14 A 336 ALA ARG THR ARG ALA PHE SER VAL CYS ASP GLU ARG TRP SEQRES 15 A 336 ALA ASP ASP LEU ALA PRO LYS ILE TYR HIS SER CYS PHE SEQRES 16 A 336 PHE ILE VAL THR TYR LEU ALA PRO LEU GLY LEU MET ALA SEQRES 17 A 336 MET ALA TYR PHE GLN ILE PHE ARG LYS LEU TRP GLY ARG SEQRES 18 A 336 GLN ILE PRO GLY THR THR SER ALA GLU VAL LYS GLN MET SEQRES 19 A 336 ARG ALA ARG ARG LYS THR ALA LYS MET LEU MET VAL VAL SEQRES 20 A 336 VAL LEU VAL PHE ALA LEU CYS TYR LEU PRO ILE SER VAL SEQRES 21 A 336 LEU ASN VAL LEU LYS ARG VAL PHE GLY MET PHE ARG GLN SEQRES 22 A 336 ALA SER ASP ARG GLU ALA VAL TYR ALA ALA PHE THR PHE SEQRES 23 A 336 SER HIS TRP LEU VAL TYR ALA ASN SER ALA ALA ASN PRO SEQRES 24 A 336 ILE ILE TYR ASN PHE LEU SER GLY LYS PHE ARG GLU GLN SEQRES 25 A 336 PHE LYS ALA ALA PHE SER TRP TRP LEU PRO GLY LEU ALA SEQRES 26 A 336 ALA ALA HIS HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 1 B 336 ALA ALA SER GLU ASP GLU PHE LEU ARG TYR LEU TRP ARG SEQRES 2 B 336 ASP TYR LEU TYR PRO LYS GLN TYR ALA TRP VAL LEU ILE SEQRES 3 B 336 ALA ALA TYR VAL ALA VAL PHE VAL VAL ALA LEU VAL GLY SEQRES 4 B 336 ASN THR LEU VAL CYS LEU ALA VAL TRP ARG ASN HIS HIS SEQRES 5 B 336 MET ARG THR VAL THR ASN TYR PHE LEU VAL ASN LEU SER SEQRES 6 B 336 LEU ALA ASP VAL LEU ALA THR ALA ILE CYS LEU PRO ALA SEQRES 7 B 336 SER LEU LEU VAL ASP ILE THR GLU SER TRP LEU PHE GLY SEQRES 8 B 336 HIS ALA LEU CYS LYS VAL ILE PRO TYR LEU GLN ALA VAL SEQRES 9 B 336 SER VAL SER VAL ALA VAL LEU THR LEU SER PHE ILE ALA SEQRES 10 B 336 LEU ASP ARG TRP TYR ALA ILE CYS HIS PRO LEU LEU PHE SEQRES 11 B 336 LYS SER THR ALA ARG ARG ALA LEU GLY SER ILE LEU GLY SEQRES 12 B 336 ILE TRP ALA VAL SER LEU ALA ILE MET VAL PRO GLN ALA SEQRES 13 B 336 ALA VAL MET GLU CYS SER SER VAL LEU PRO GLU LEU ALA SEQRES 14 B 336 ALA ARG THR ARG ALA PHE SER VAL CYS ASP GLU ARG TRP SEQRES 15 B 336 ALA ASP ASP LEU ALA PRO LYS ILE TYR HIS SER CYS PHE SEQRES 16 B 336 PHE ILE VAL THR TYR LEU ALA PRO LEU GLY LEU MET ALA SEQRES 17 B 336 MET ALA TYR PHE GLN ILE PHE ARG LYS LEU TRP GLY ARG SEQRES 18 B 336 GLN ILE PRO GLY THR THR SER ALA GLU VAL LYS GLN MET SEQRES 19 B 336 ARG ALA ARG ARG LYS THR ALA LYS MET LEU MET VAL VAL SEQRES 20 B 336 VAL LEU VAL PHE ALA LEU CYS TYR LEU PRO ILE SER VAL SEQRES 21 B 336 LEU ASN VAL LEU LYS ARG VAL PHE GLY MET PHE ARG GLN SEQRES 22 B 336 ALA SER ASP ARG GLU ALA VAL TYR ALA ALA PHE THR PHE SEQRES 23 B 336 SER HIS TRP LEU VAL TYR ALA ASN SER ALA ALA ASN PRO SEQRES 24 B 336 ILE ILE TYR ASN PHE LEU SER GLY LYS PHE ARG GLU GLN SEQRES 25 B 336 PHE LYS ALA ALA PHE SER TRP TRP LEU PRO GLY LEU ALA SEQRES 26 B 336 ALA ALA HIS HIS HIS HIS HIS HIS HIS HIS HIS HET NRK A 401 50 HET PG4 A 402 13 HET SO4 A 403 5 HET SO4 A 404 5 HET SOG A 405 20 HET SOG A 406 20 HET SOG A 407 13 HET SOG A 408 20 HET PGW A 409 51 HET PGW A 410 51 HET NRK B 401 50 HET SO4 B 402 5 HET SO4 B 403 5 HET SOG B 404 20 HET SOG B 405 13 HET SOG B 406 20 HET SOG B 407 16 HET SOG B 408 20 HETNAM NRK (1~{R},2~{S})-2-[(2,4-DIMETHYLPYRIMIDIN-5-YL) HETNAM 2 NRK OXYMETHYL]-~{N}-(5-FLUORANYLPYRIDIN-2-YL)-2-(3- HETNAM 3 NRK FLUOROPHENYL)CYCLOPROPANE-1-CARBOXAMIDE HETNAM PG4 TETRAETHYLENE GLYCOL HETNAM SO4 SULFATE ION HETNAM SOG OCTYL 1-THIO-BETA-D-GLUCOPYRANOSIDE HETNAM PGW (1R)-2-{[(S)-{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY) HETNAM 2 PGW PHOSPHORYL]OXY}-1-[(HEXADECANOYLOXY)METHYL]ETHYL (9Z)- HETNAM 3 PGW OCTADEC-9-ENOATE HETSYN SOG 1-S-OCTYL-BETA-D-THIOGLUCOSIDE HETSYN PGW 1-PALMITOYL-2-OLEOYL-SN-GLYCERO-3-[PHOSPHO-(1- HETSYN 2 PGW GLYCEROL)]; PHOSPHATIDYLGLYCEROL FORMUL 3 NRK 2(C22 H20 F2 N4 O2) FORMUL 4 PG4 C8 H18 O5 FORMUL 5 SO4 4(O4 S 2-) FORMUL 7 SOG 9(C14 H28 O5 S) FORMUL 11 PGW 2(C40 H77 O10 P) FORMUL 21 HOH *43(H2 O) HELIX 1 AA1 SER A 27 TYR A 39 1 13 HELIX 2 AA2 TYR A 39 ASN A 74 1 36 HELIX 3 AA3 HIS A 75 ARG A 78 5 4 HELIX 4 AA4 THR A 79 GLU A 110 1 32 HELIX 5 AA5 PHE A 114 CYS A 149 1 36 HELIX 6 AA6 THR A 157 MET A 176 1 20 HELIX 7 AA7 MET A 176 VAL A 182 1 7 HELIX 8 AA8 ASP A 209 TYR A 224 1 16 HELIX 9 AA9 TYR A 224 TRP A 243 1 20 HELIX 10 AB1 VAL A 287 VAL A 323 1 37 HELIX 11 AB2 ASP A 332 SER A 362 1 31 HELIX 12 AB3 SER A 362 TRP A 376 1 15 HELIX 13 AB4 TYR B 45 ASN B 74 1 30 HELIX 14 AB5 HIS B 75 ARG B 78 5 4 HELIX 15 AB6 THR B 79 GLU B 110 1 32 HELIX 16 AB7 PHE B 114 CYS B 149 1 36 HELIX 17 AB8 THR B 157 MET B 176 1 20 HELIX 18 AB9 MET B 176 VAL B 182 1 7 HELIX 19 AC1 LEU B 189 ARG B 195 5 7 HELIX 20 AC2 ASP B 209 TYR B 224 1 16 HELIX 21 AC3 TYR B 224 TRP B 243 1 20 HELIX 22 AC4 THR B 251 VAL B 323 1 41 HELIX 23 AC5 ASP B 332 SER B 362 1 31 HELIX 24 AC6 SER B 362 LEU B 377 1 16 SHEET 1 AA1 2 MET A 183 SER A 186 0 SHEET 2 AA1 2 VAL A 201 GLU A 204 -1 O ASP A 203 N GLU A 184 SHEET 1 AA2 2 MET B 183 SER B 187 0 SHEET 2 AA2 2 SER B 200 GLU B 204 -1 O ASP B 203 N GLU B 184 SSBOND 1 CYS A 119 CYS A 202 1555 1555 2.05 SSBOND 2 CYS B 119 CYS B 202 1555 1555 2.06 CRYST1 59.725 145.715 71.703 90.00 112.25 90.00 P 1 21 1 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 0.016743 0.000000 0.006850 0.00000 SCALE2 0.000000 0.006863 0.000000 0.00000 SCALE3 0.000000 0.000000 0.015068 0.00000 ATOM 1 N SER A 27 4.128 16.875 132.041 1.00116.16 N ANISOU 1 N SER A 27 18767 10453 14915 118 5509 -1846 N ATOM 2 CA SER A 27 4.457 17.457 130.740 1.00115.53 C ANISOU 2 CA SER A 27 18275 10603 15017 235 5158 -1780 C ATOM 3 C SER A 27 5.948 17.324 130.401 1.00117.52 C ANISOU 3 C SER A 27 18653 10988 15011 230 4725 -1653 C ATOM 4 O SER A 27 6.286 17.198 129.223 1.00116.93 O ANISOU 4 O SER A 27 18253 11117 15057 289 4439 -1592 O ATOM 5 CB SER A 27 4.034 18.922 130.686 1.00119.38 C ANISOU 5 CB SER A 27 18646 11044 15668 344 5219 -1815 C ATOM 6 OG SER A 27 2.667 19.095 131.026 1.00128.23 O ANISOU 6 OG SER A 27 19630 12044 17049 362 5616 -1953 O ATOM 7 N GLU A 28 6.825 17.345 131.439 1.00112.68 N ANISOU 7 N GLU A 28 18514 10253 14047 163 4679 -1631 N ATOM 8 CA GLU A 28 8.294 17.251 131.370 1.00111.55 C ANISOU 8 CA GLU A 28 18538 10208 13638 151 4288 -1551 C ATOM 9 C GLU A 28 8.817 16.015 130.611 1.00112.21 C ANISOU 9 C GLU A 28 18446 10475 13713 143 4040 -1491 C ATOM 10 O GLU A 28 9.768 16.152 129.836 1.00111.68 O ANISOU 10 O GLU A 28 18227 10580 13628 173 3692 -1430 O ATOM 11 CB GLU A 28 8.917 17.331 132.781 1.00113.06 C ANISOU 11 CB GLU A 28 19291 10205 13462 90 4328 -1576 C ATOM 12 CG GLU A 28 8.935 18.737 133.372 1.00125.01 C ANISOU 12 CG GLU A 28 20993 11583 14921 101 4415 -1613 C ATOM 13 CD GLU A 28 8.832 18.879 134.884 1.00146.44 C ANISOU 13 CD GLU A 28 24244 14029 17368 45 4668 -1673 C ATOM 14 OE1 GLU A 28 9.306 17.976 135.612 1.00145.28 O ANISOU 14 OE1 GLU A 28 24452 13806 16943 2 4626 -1673 O ATOM 15 OE2 GLU A 28 8.290 19.912 135.342 1.00134.75 O ANISOU 15 OE2 GLU A 28 22852 12403 15943 53 4904 -1722 O ATOM 16 N ASP A 29 8.198 14.825 130.827 1.00105.84 N ANISOU 16 N ASP A 29 17669 9622 12922 94 4238 -1517 N ATOM 17 CA ASP A 29 8.573 13.560 130.166 1.00103.86 C ANISOU 17 CA ASP A 29 17279 9521 12663 82 4049 -1466 C ATOM 18 C ASP A 29 8.233 13.576 128.670 1.00101.52 C ANISOU 18 C ASP A 29 16436 9445 12691 143 3906 -1437 C ATOM 19 O ASP A 29 9.032 13.099 127.863 1.00 99.62 O ANISOU 19 O ASP A 29 16048 9380 12423 164 3592 -1367 O ATOM 20 CB ASP A 29 7.934 12.342 130.876 1.00106.09 C ANISOU 20 CB ASP A 29 17785 9657 12868 0 4351 -1513 C ATOM 21 CG ASP A 29 8.174 10.996 130.199 1.00120.81 C ANISOU 21 CG ASP A 29 19504 11657 14741 -15 4201 -1468 C ATOM 22 OD1 ASP A 29 9.356 10.663 129.928 1.00121.56 O ANISOU 22 OD1 ASP A 29 19665 11870 14652 19 3838 -1395 O ATOM 23 OD2 ASP A 29 7.183 10.272 129.951 1.00128.57 O ANISOU 23 OD2 ASP A 29 20303 12627 15921 -65 4452 -1519 O ATOM 24 N GLU A 30 7.047 14.128 128.317 1.00 95.10 N ANISOU 24 N GLU A 30 15337 8614 12182 183 4133 -1500 N ATOM 25 CA GLU A 30 6.550 14.282 126.944 1.00 93.46 C ANISOU 25 CA GLU A 30 14630 8586 12293 270 4013 -1494 C ATOM 26 C GLU A 30 7.477 15.208 126.146 1.00 92.15 C ANISOU 26 C GLU A 30 14367 8548 12099 349 3667 -1409 C ATOM 27 O GLU A 30 7.801 14.892 125.001 1.00 91.50 O ANISOU 27 O GLU A 30 14014 8644 12108 391 3417 -1351 O ATOM 28 CB GLU A 30 5.115 14.840 126.936 1.00 95.09 C ANISOU 28 CB GLU A 30 14604 8716 12809 320 4324 -1608 C ATOM 29 CG GLU A 30 4.055 13.840 127.367 1.00111.14 C ANISOU 29 CG GLU A 30 16588 10666 14973 234 4671 -1718 C ATOM 30 CD GLU A 30 2.871 14.430 128.113 1.00147.53 C ANISOU 30 CD GLU A 30 21201 15096 19758 229 5086 -1861 C ATOM 31 OE1 GLU A 30 2.194 15.322 127.551 1.00152.71 O ANISOU 31 OE1 GLU A 30 21546 15794 20684 350 5091 -1917 O ATOM 32 OE2 GLU A 30 2.612 13.991 129.258 1.00144.70 O ANISOU 32 OE2 GLU A 30 21171 14544 19264 109 5413 -1922 O ATOM 33 N PHE A 31 7.928 16.325 126.770 1.00 84.58 N ANISOU 33 N PHE A 31 13654 7483 11001 355 3668 -1407 N ATOM 34 CA PHE A 31 8.840 17.287 126.156 1.00 82.78 C ANISOU 34 CA PHE A 31 13391 7336 10725 400 3391 -1346 C ATOM 35 C PHE A 31 10.183 16.642 125.824 1.00 83.47 C ANISOU 35 C PHE A 31 13531 7558 10625 349 3068 -1279 C ATOM 36 O PHE A 31 10.666 16.803 124.699 1.00 82.17 O ANISOU 36 O PHE A 31 13136 7544 10542 388 2831 -1225 O ATOM 37 CB PHE A 31 9.019 18.549 127.029 1.00 84.48 C ANISOU 37 CB PHE A 31 13893 7387 10817 393 3495 -1377 C ATOM 38 CG PHE A 31 10.049 19.521 126.493 1.00 85.65 C ANISOU 38 CG PHE A 31 14052 7598 10894 407 3235 -1330 C ATOM 39 CD1 PHE A 31 9.759 20.340 125.408 1.00 88.25 C ANISOU 39 CD1 PHE A 31 14125 7986 11419 506 3166 -1302 C ATOM 40 CD2 PHE A 31 11.323 19.587 127.047 1.00 87.54 C ANISOU 40 CD2 PHE A 31 14561 7831 10870 321 3057 -1327 C ATOM 41 CE1 PHE A 31 10.723 21.205 124.888 1.00 88.97 C ANISOU 41 CE1 PHE A 31 14253 8115 11437 498 2960 -1264 C ATOM 42 CE2 PHE A 31 12.287 20.453 126.525 1.00 90.13 C ANISOU 42 CE2 PHE A 31 14875 8215 11155 307 2842 -1308 C ATOM 43 CZ PHE A 31 11.980 21.256 125.451 1.00 88.04 C ANISOU 43 CZ PHE A 31 14378 7993 11079 385 2814 -1273 C ATOM 44 N LEU A 32 10.762 15.886 126.788 1.00 78.50 N ANISOU 44 N LEU A 32 13213 6868 9745 271 3061 -1290 N ATOM 45 CA LEU A 32 12.039 15.174 126.622 1.00 77.48 C ANISOU 45 CA LEU A 32 13155 6857 9429 237 2754 -1251 C ATOM 46 C LEU A 32 11.948 14.071 125.570 1.00 78.58 C ANISOU 46 C LEU A 32 12994 7164 9698 255 2635 -1202 C ATOM 47 O LEU A 32 12.965 13.717 124.958 1.00 78.24 O ANISOU 47 O LEU A 32 12870 7264 9594 252 2350 -1162 O ATOM 48 CB LEU A 32 12.565 14.618 127.956 1.00 77.85 C ANISOU 48 CB LEU A 32 13638 6774 9168 185 2774 -1287 C ATOM 49 CG LEU A 32 13.051 15.661 128.975 1.00 83.77 C ANISOU 49 CG LEU A 32 14721 7380 9727 163 2785 -1338 C ATOM 50 CD1 LEU A 32 12.937 15.129 130.398 1.00 84.33 C ANISOU 50 CD1 LEU A 32 15253 7254 9536 131 2946 -1383 C ATOM 51 CD2 LEU A 32 14.475 16.130 128.672 1.00 85.93 C ANISOU 51 CD2 LEU A 32 14982 7770 9896 152 2433 -1344 C ATOM 52 N ARG A 33 10.730 13.541 125.346 1.00 72.46 N ANISOU 52 N ARG A 33 12043 6372 9117 269 2860 -1220 N ATOM 53 CA ARG A 33 10.493 12.518 124.330 1.00 70.69 C ANISOU 53 CA ARG A 33 11521 6298 9039 283 2772 -1186 C ATOM 54 C ARG A 33 10.479 13.136 122.928 1.00 71.94 C ANISOU 54 C ARG A 33 11318 6607 9408 362 2591 -1144 C ATOM 55 O ARG A 33 11.133 12.595 122.031 1.00 69.95 O ANISOU 55 O ARG A 33 10915 6507 9155 368 2351 -1088 O ATOM 56 CB ARG A 33 9.225 11.725 124.632 1.00 71.04 C ANISOU 56 CB ARG A 33 11509 6264 9220 253 3082 -1248 C ATOM 57 CG ARG A 33 9.457 10.668 125.703 1.00 85.61 C ANISOU 57 CG ARG A 33 13719 7990 10818 170 3196 -1263 C ATOM 58 CD ARG A 33 8.169 10.035 126.198 1.00105.60 C ANISOU 58 CD ARG A 33 16262 10391 13469 109 3584 -1347 C ATOM 59 NE ARG A 33 8.217 8.576 126.079 1.00124.84 N ANISOU 59 NE ARG A 33 18740 12854 15839 51 3586 -1334 N ATOM 60 CZ ARG A 33 8.677 7.757 127.021 1.00145.07 C ANISOU 60 CZ ARG A 33 21728 15284 18107 -4 3643 -1327 C ATOM 61 NH1 ARG A 33 9.125 8.243 128.174 1.00136.52 N ANISOU 61 NH1 ARG A 33 21069 14036 16766 -8 3693 -1336 N ATOM 62 NH2 ARG A 33 8.687 6.447 126.820 1.00132.46 N ANISOU 62 NH2 ARG A 33 20162 13707 16459 -47 3647 -1313 N ATOM 63 N TYR A 34 9.800 14.309 122.754 1.00 68.36 N ANISOU 63 N TYR A 34 10763 6097 9113 430 2699 -1171 N ATOM 64 CA TYR A 34 9.766 15.019 121.466 1.00 67.45 C ANISOU 64 CA TYR A 34 10375 6087 9167 526 2532 -1132 C ATOM 65 C TYR A 34 11.102 15.644 121.132 1.00 66.12 C ANISOU 65 C TYR A 34 10310 5968 8844 503 2288 -1075 C ATOM 66 O TYR A 34 11.482 15.596 119.973 1.00 64.49 O ANISOU 66 O TYR A 34 9914 5885 8702 539 2090 -1022 O ATOM 67 CB TYR A 34 8.608 16.017 121.363 1.00 70.35 C ANISOU 67 CB TYR A 34 10614 6369 9748 632 2711 -1186 C ATOM 68 CG TYR A 34 7.296 15.297 121.169 1.00 75.41 C ANISOU 68 CG TYR A 34 10999 7026 10628 670 2883 -1260 C ATOM 69 CD1 TYR A 34 6.402 15.142 122.227 1.00 77.65 C ANISOU 69 CD1 TYR A 34 11371 7170 10961 627 3208 -1359 C ATOM 70 CD2 TYR A 34 7.005 14.648 119.968 1.00 77.54 C ANISOU 70 CD2 TYR A 34 10950 7447 11065 729 2729 -1245 C ATOM 71 CE1 TYR A 34 5.233 14.398 122.085 1.00 79.71 C ANISOU 71 CE1 TYR A 34 11383 7446 11458 632 3391 -1456 C ATOM 72 CE2 TYR A 34 5.844 13.888 119.817 1.00 79.45 C ANISOU 72 CE2 TYR A 34 10942 7711 11534 744 2880 -1338 C ATOM 73 CZ TYR A 34 4.956 13.772 120.878 1.00 91.24 C ANISOU 73 CZ TYR A 34 12503 9068 13096 690 3219 -1450 C ATOM 74 OH TYR A 34 3.793 13.051 120.737 1.00 97.25 O ANISOU 74 OH TYR A 34 12995 9846 14109 686 3396 -1571 O ATOM 75 N LEU A 35 11.855 16.140 122.156 1.00 60.22 N ANISOU 75 N LEU A 35 9870 5124 7888 433 2302 -1098 N ATOM 76 CA LEU A 35 13.214 16.695 122.034 1.00 58.46 C ANISOU 76 CA LEU A 35 9758 4940 7514 380 2086 -1083 C ATOM 77 C LEU A 35 14.135 15.621 121.486 1.00 59.20 C ANISOU 77 C LEU A 35 9761 5190 7540 340 1851 -1050 C ATOM 78 O LEU A 35 14.975 15.893 120.622 1.00 57.32 O ANISOU 78 O LEU A 35 9417 5051 7312 326 1659 -1025 O ATOM 79 CB LEU A 35 13.723 17.137 123.415 1.00 58.92 C ANISOU 79 CB LEU A 35 10166 4864 7357 310 2150 -1143 C ATOM 80 CG LEU A 35 15.097 17.822 123.481 1.00 63.95 C ANISOU 80 CG LEU A 35 10926 5523 7849 241 1950 -1170 C ATOM 81 CD1 LEU A 35 15.047 19.226 122.900 1.00 62.90 C ANISOU 81 CD1 LEU A 35 10739 5345 7814 261 1981 -1164 C ATOM 82 CD2 LEU A 35 15.610 17.864 124.923 1.00 67.99 C ANISOU 82 CD2 LEU A 35 11788 5921 8126 179 1969 -1243 C ATOM 83 N TRP A 36 13.951 14.380 121.989 1.00 55.16 N ANISOU 83 N TRP A 36 9305 4690 6964 320 1887 -1055 N ATOM 84 CA TRP A 36 14.692 13.217 121.552 1.00 53.94 C ANISOU 84 CA TRP A 36 9079 4671 6745 298 1686 -1026 C ATOM 85 C TRP A 36 14.323 12.863 120.100 1.00 54.91 C ANISOU 85 C TRP A 36 8863 4930 7070 347 1609 -968 C ATOM 86 O TRP A 36 15.202 12.812 119.257 1.00 53.92 O ANISOU 86 O TRP A 36 8625 4921 6940 337 1400 -938 O ATOM 87 CB TRP A 36 14.470 12.026 122.507 1.00 52.75 C ANISOU 87 CB TRP A 36 9126 4459 6459 274 1779 -1046 C ATOM 88 CG TRP A 36 15.030 10.743 121.965 1.00 53.82 C ANISOU 88 CG TRP A 36 9171 4726 6553 272 1596 -1012 C ATOM 89 CD1 TRP A 36 14.330 9.719 121.396 1.00 56.50 C ANISOU 89 CD1 TRP A 36 9340 5121 7007 284 1658 -980 C ATOM 90 CD2 TRP A 36 16.417 10.431 121.783 1.00 53.91 C ANISOU 90 CD2 TRP A 36 9213 4841 6428 261 1313 -1016 C ATOM 91 NE1 TRP A 36 15.195 8.757 120.933 1.00 55.55 N ANISOU 91 NE1 TRP A 36 9179 5120 6806 283 1438 -950 N ATOM 92 CE2 TRP A 36 16.483 9.158 121.178 1.00 57.10 C ANISOU 92 CE2 TRP A 36 9493 5349 6852 275 1223 -975 C ATOM 93 CE3 TRP A 36 17.615 11.073 122.146 1.00 55.60 C ANISOU 93 CE3 TRP A 36 9550 5064 6509 237 1130 -1070 C ATOM 94 CZ2 TRP A 36 17.698 8.533 120.881 1.00 56.81 C ANISOU 94 CZ2 TRP A 36 9443 5428 6713 280 958 -980 C ATOM 95 CZ3 TRP A 36 18.819 10.462 121.829 1.00 57.32 C ANISOU 95 CZ3 TRP A 36 9726 5408 6647 236 863 -1091 C ATOM 96 CH2 TRP A 36 18.854 9.201 121.218 1.00 57.75 C ANISOU 96 CH2 TRP A 36 9655 5564 6723 265 779 -1044 C ATOM 97 N ARG A 37 13.032 12.642 119.821 1.00 50.83 N ANISOU 97 N ARG A 37 8187 4393 6733 399 1779 -966 N ATOM 98 CA ARG A 37 12.513 12.270 118.504 1.00 51.30 C ANISOU 98 CA ARG A 37 7934 4570 6989 461 1707 -927 C ATOM 99 C ARG A 37 12.825 13.310 117.400 1.00 56.84 C ANISOU 99 C ARG A 37 8509 5318 7772 520 1567 -888 C ATOM 100 O ARG A 37 13.393 12.960 116.363 1.00 55.51 O ANISOU 100 O ARG A 37 8207 5267 7618 525 1382 -839 O ATOM 101 CB ARG A 37 10.986 12.015 118.599 1.00 52.28 C ANISOU 101 CB ARG A 37 7915 4640 7309 507 1936 -977 C ATOM 102 CG ARG A 37 10.311 11.653 117.271 1.00 63.30 C ANISOU 102 CG ARG A 37 8976 6151 8924 587 1854 -963 C ATOM 103 CD ARG A 37 8.810 11.558 117.413 1.00 70.82 C ANISOU 103 CD ARG A 37 9760 7050 10100 635 2077 -1051 C ATOM 104 NE ARG A 37 8.406 10.200 117.776 1.00 84.30 N ANISOU 104 NE ARG A 37 11442 8768 11819 552 2197 -1091 N ATOM 105 CZ ARG A 37 7.267 9.885 118.386 1.00101.68 C ANISOU 105 CZ ARG A 37 13590 10885 14158 525 2472 -1196 C ATOM 106 NH1 ARG A 37 6.398 10.834 118.723 1.00 83.88 N ANISOU 106 NH1 ARG A 37 11281 8537 12054 588 2648 -1275 N ATOM 107 NH2 ARG A 37 6.992 8.620 118.677 1.00 92.26 N ANISOU 107 NH2 ARG A 37 12408 9690 12957 430 2591 -1231 N ATOM 108 N ASP A 38 12.466 14.582 117.657 1.00 53.98 N ANISOU 108 N ASP A 38 8220 4844 7445 564 1672 -910 N ATOM 109 CA ASP A 38 12.543 15.696 116.724 1.00 53.47 C ANISOU 109 CA ASP A 38 8095 4771 7450 637 1595 -879 C ATOM 110 C ASP A 38 13.914 16.388 116.594 1.00 57.08 C ANISOU 110 C ASP A 38 8701 5228 7758 555 1466 -864 C ATOM 111 O ASP A 38 14.127 17.098 115.608 1.00 55.22 O ANISOU 111 O ASP A 38 8423 4994 7564 597 1390 -829 O ATOM 112 CB ASP A 38 11.453 16.724 117.075 1.00 54.58 C ANISOU 112 CB ASP A 38 8256 4777 7705 735 1782 -920 C ATOM 113 CG ASP A 38 10.031 16.179 116.976 1.00 64.00 C ANISOU 113 CG ASP A 38 9235 5978 9106 827 1906 -966 C ATOM 114 OD1 ASP A 38 9.794 15.245 116.157 1.00 63.70 O ANISOU 114 OD1 ASP A 38 8982 6059 9161 852 1803 -949 O ATOM 115 OD2 ASP A 38 9.157 16.680 117.703 1.00 74.69 O ANISOU 115 OD2 ASP A 38 10624 7218 10537 870 2112 -1032 O ATOM 116 N TYR A 39 14.840 16.169 117.546 1.00 54.10 N ANISOU 116 N TYR A 39 8502 4844 7211 442 1440 -902 N ATOM 117 CA TYR A 39 16.131 16.855 117.520 1.00 52.55 C ANISOU 117 CA TYR A 39 8421 4647 6898 352 1329 -927 C ATOM 118 C TYR A 39 17.343 15.966 117.927 1.00 56.24 C ANISOU 118 C TYR A 39 8933 5211 7226 254 1167 -967 C ATOM 119 O TYR A 39 18.259 15.799 117.115 1.00 56.57 O ANISOU 119 O TYR A 39 8870 5353 7269 210 1012 -963 O ATOM 120 CB TYR A 39 16.049 18.162 118.374 1.00 52.12 C ANISOU 120 CB TYR A 39 8585 4433 6787 333 1469 -978 C ATOM 121 CG TYR A 39 17.384 18.846 118.534 1.00 52.35 C ANISOU 121 CG TYR A 39 8742 4452 6697 214 1373 -1037 C ATOM 122 CD1 TYR A 39 17.973 19.532 117.469 1.00 53.97 C ANISOU 122 CD1 TYR A 39 8889 4673 6944 183 1310 -1023 C ATOM 123 CD2 TYR A 39 18.104 18.739 119.720 1.00 52.49 C ANISOU 123 CD2 TYR A 39 8942 4444 6558 127 1339 -1121 C ATOM 124 CE1 TYR A 39 19.247 20.082 117.582 1.00 53.89 C ANISOU 124 CE1 TYR A 39 8966 4661 6849 47 1237 -1105 C ATOM 125 CE2 TYR A 39 19.383 19.278 119.841 1.00 53.15 C ANISOU 125 CE2 TYR A 39 9099 4538 6555 11 1227 -1207 C ATOM 126 CZ TYR A 39 19.944 19.959 118.775 1.00 60.65 C ANISOU 126 CZ TYR A 39 9958 5511 7577 -39 1189 -1206 C ATOM 127 OH TYR A 39 21.185 20.523 118.919 1.00 63.92 O ANISOU 127 OH TYR A 39 10429 5927 7930 -175 1110 -1319 O ATOM 128 N LEU A 40 17.378 15.447 119.172 1.00 52.44 N ANISOU 128 N LEU A 40 8621 4686 6616 228 1201 -1014 N ATOM 129 CA LEU A 40 18.524 14.667 119.671 1.00 52.37 C ANISOU 129 CA LEU A 40 8691 4751 6456 168 1022 -1068 C ATOM 130 C LEU A 40 18.833 13.375 118.880 1.00 55.76 C ANISOU 130 C LEU A 40 8938 5331 6916 185 872 -1026 C ATOM 131 O LEU A 40 19.987 13.179 118.499 1.00 56.38 O ANISOU 131 O LEU A 40 8954 5509 6958 139 685 -1065 O ATOM 132 CB LEU A 40 18.386 14.362 121.160 1.00 52.31 C ANISOU 132 CB LEU A 40 8958 4639 6281 164 1091 -1120 C ATOM 133 CG LEU A 40 18.369 15.544 122.102 1.00 56.15 C ANISOU 133 CG LEU A 40 9670 4977 6688 132 1202 -1182 C ATOM 134 CD1 LEU A 40 17.935 15.115 123.493 1.00 55.99 C ANISOU 134 CD1 LEU A 40 9936 4827 6509 147 1322 -1212 C ATOM 135 CD2 LEU A 40 19.722 16.247 122.144 1.00 59.85 C ANISOU 135 CD2 LEU A 40 10182 5478 7080 50 1024 -1274 C ATOM 136 N TYR A 41 17.826 12.522 118.613 1.00 50.99 N ANISOU 136 N TYR A 41 8237 4744 6392 245 960 -961 N ATOM 137 CA TYR A 41 18.000 11.302 117.812 1.00 50.06 C ANISOU 137 CA TYR A 41 7950 4759 6312 262 838 -916 C ATOM 138 C TYR A 41 18.485 11.627 116.364 1.00 52.62 C ANISOU 138 C TYR A 41 8055 5188 6752 256 719 -880 C ATOM 139 O TYR A 41 19.544 11.129 115.992 1.00 51.68 O ANISOU 139 O TYR A 41 7880 5171 6587 220 548 -900 O ATOM 140 CB TYR A 41 16.749 10.394 117.834 1.00 51.20 C ANISOU 140 CB TYR A 41 8040 4884 6531 309 983 -874 C ATOM 141 CG TYR A 41 16.836 9.247 116.849 1.00 53.72 C ANISOU 141 CG TYR A 41 8167 5336 6910 325 868 -825 C ATOM 142 CD1 TYR A 41 17.565 8.098 117.149 1.00 55.27 C ANISOU 142 CD1 TYR A 41 8441 5586 6971 309 745 -834 C ATOM 143 CD2 TYR A 41 16.256 9.341 115.583 1.00 54.75 C ANISOU 143 CD2 TYR A 41 8053 5530 7218 367 861 -774 C ATOM 144 CE1 TYR A 41 17.703 7.064 116.221 1.00 54.33 C ANISOU 144 CE1 TYR A 41 8155 5585 6903 322 639 -790 C ATOM 145 CE2 TYR A 41 16.389 8.314 114.649 1.00 55.65 C ANISOU 145 CE2 TYR A 41 8005 5763 7378 377 746 -731 C ATOM 146 CZ TYR A 41 17.109 7.173 114.976 1.00 63.02 C ANISOU 146 CZ TYR A 41 9012 6750 8183 348 647 -738 C ATOM 147 OH TYR A 41 17.235 6.147 114.064 1.00 66.65 O ANISOU 147 OH TYR A 41 9321 7319 8684 358 544 -697 O ATOM 148 N PRO A 42 17.781 12.459 115.547 1.00 49.41 N ANISOU 148 N PRO A 42 7544 4748 6483 299 801 -835 N ATOM 149 CA PRO A 42 18.300 12.774 114.195 1.00 49.75 C ANISOU 149 CA PRO A 42 7445 4860 6596 293 696 -801 C ATOM 150 C PRO A 42 19.715 13.320 113.976 1.00 55.74 C ANISOU 150 C PRO A 42 8262 5634 7281 192 601 -865 C ATOM 151 O PRO A 42 20.315 13.053 112.948 1.00 55.30 O ANISOU 151 O PRO A 42 8096 5660 7255 158 500 -857 O ATOM 152 CB PRO A 42 17.275 13.750 113.630 1.00 50.90 C ANISOU 152 CB PRO A 42 7559 4920 6861 378 809 -758 C ATOM 153 CG PRO A 42 16.420 14.152 114.745 1.00 54.99 C ANISOU 153 CG PRO A 42 8193 5325 7376 408 974 -790 C ATOM 154 CD PRO A 42 16.473 13.107 115.776 1.00 50.58 C ANISOU 154 CD PRO A 42 7706 4787 6727 369 989 -822 C ATOM 155 N LYS A 43 20.233 14.093 114.925 1.00 55.26 N ANISOU 155 N LYS A 43 8370 5492 7133 136 642 -942 N ATOM 156 CA LYS A 43 21.593 14.624 114.882 1.00 55.92 C ANISOU 156 CA LYS A 43 8498 5586 7162 24 561 -1041 C ATOM 157 C LYS A 43 22.642 13.584 115.328 1.00 60.26 C ANISOU 157 C LYS A 43 8991 6262 7644 -12 374 -1110 C ATOM 158 O LYS A 43 23.714 13.479 114.737 1.00 60.57 O ANISOU 158 O LYS A 43 8912 6383 7718 -80 273 -1160 O ATOM 159 CB LYS A 43 21.718 15.828 115.834 1.00 58.70 C ANISOU 159 CB LYS A 43 9054 5808 7440 -17 656 -1114 C ATOM 160 CG LYS A 43 20.827 16.991 115.459 1.00 72.57 C ANISOU 160 CG LYS A 43 10861 7454 9257 -41 783 -1101 C ATOM 161 CD LYS A 43 21.057 18.168 116.396 1.00 83.85 C ANISOU 161 CD LYS A 43 12371 8853 10634 -185 753 -1232 C ATOM 162 CE LYS A 43 22.387 18.847 116.189 1.00 95.38 C ANISOU 162 CE LYS A 43 13858 10227 12156 -239 859 -1223 C ATOM 163 NZ LYS A 43 22.461 19.550 114.882 1.00108.45 N ANISOU 163 NZ LYS A 43 15696 11711 13798 -192 1031 -1193 N ATOM 164 N GLN A 44 22.254 12.747 116.313 1.00 57.28 N ANISOU 164 N GLN A 44 8705 5889 7168 41 338 -1114 N ATOM 165 CA GLN A 44 23.035 11.615 116.826 1.00 57.02 C ANISOU 165 CA GLN A 44 8662 5957 7046 50 151 -1172 C ATOM 166 C GLN A 44 23.184 10.650 115.635 1.00 60.51 C ANISOU 166 C GLN A 44 8891 6526 7574 72 68 -1108 C ATOM 167 O GLN A 44 24.271 10.116 115.418 1.00 61.08 O ANISOU 167 O GLN A 44 8874 6701 7631 48 -99 -1181 O ATOM 168 CB GLN A 44 22.413 10.890 118.014 1.00 58.57 C ANISOU 168 CB GLN A 44 9059 6085 7110 120 186 -1157 C ATOM 169 CG GLN A 44 23.415 10.274 118.972 1.00 88.20 C ANISOU 169 CG GLN A 44 12955 9863 10694 136 -7 -1266 C ATOM 170 CD GLN A 44 22.744 9.998 120.296 1.00115.41 C ANISOU 170 CD GLN A 44 16697 13174 13978 189 85 -1260 C ATOM 171 OE1 GLN A 44 22.147 8.933 120.507 1.00113.01 O ANISOU 171 OE1 GLN A 44 16470 12851 13618 250 133 -1195 O ATOM 172 NE2 GLN A 44 22.803 10.966 121.210 1.00105.50 N ANISOU 172 NE2 GLN A 44 15634 11810 12641 159 133 -1331 N ATOM 173 N TYR A 45 22.092 10.448 114.862 1.00 55.30 N ANISOU 173 N TYR A 45 8143 5857 7010 123 181 -987 N ATOM 174 CA TYR A 45 22.038 9.619 113.664 1.00 54.45 C ANISOU 174 CA TYR A 45 7851 5852 6986 149 124 -916 C ATOM 175 C TYR A 45 22.985 10.202 112.603 1.00 58.78 C ANISOU 175 C TYR A 45 8279 6451 7603 76 66 -949 C ATOM 176 O TYR A 45 23.828 9.473 112.076 1.00 58.39 O ANISOU 176 O TYR A 45 8118 6508 7560 54 -59 -979 O ATOM 177 CB TYR A 45 20.584 9.542 113.147 1.00 55.35 C ANISOU 177 CB TYR A 45 7906 5925 7199 220 259 -809 C ATOM 178 CG TYR A 45 20.335 8.625 111.961 1.00 56.76 C ANISOU 178 CG TYR A 45 7910 6199 7457 257 201 -735 C ATOM 179 CD1 TYR A 45 20.860 8.918 110.702 1.00 58.43 C ANISOU 179 CD1 TYR A 45 8008 6460 7732 234 140 -713 C ATOM 180 CD2 TYR A 45 19.475 7.535 112.066 1.00 57.14 C ANISOU 180 CD2 TYR A 45 7925 6267 7521 309 234 -691 C ATOM 181 CE1 TYR A 45 20.621 8.095 109.607 1.00 57.26 C ANISOU 181 CE1 TYR A 45 7722 6389 7644 271 84 -647 C ATOM 182 CE2 TYR A 45 19.203 6.719 110.965 1.00 57.47 C ANISOU 182 CE2 TYR A 45 7808 6391 7638 338 180 -632 C ATOM 183 CZ TYR A 45 19.774 7.008 109.735 1.00 63.60 C ANISOU 183 CZ TYR A 45 8478 7222 8464 326 95 -607 C ATOM 184 OH TYR A 45 19.508 6.225 108.628 1.00 65.58 O ANISOU 184 OH TYR A 45 8595 7546 8778 358 37 -549 O ATOM 185 N ALA A 46 22.857 11.507 112.305 1.00 56.65 N ANISOU 185 N ALA A 46 8050 6093 7380 36 173 -952 N ATOM 186 CA ALA A 46 23.680 12.205 111.308 1.00 56.79 C ANISOU 186 CA ALA A 46 8007 6117 7454 -51 174 -987 C ATOM 187 C ALA A 46 25.172 12.199 111.663 1.00 62.30 C ANISOU 187 C ALA A 46 8668 6879 8123 -161 66 -1143 C ATOM 188 O ALA A 46 26.012 12.029 110.772 1.00 60.82 O ANISOU 188 O ALA A 46 8358 6758 7992 -227 24 -1185 O ATOM 189 CB ALA A 46 23.187 13.623 111.122 1.00 57.25 C ANISOU 189 CB ALA A 46 8179 6034 7538 -63 326 -964 C ATOM 190 N TRP A 47 25.495 12.353 112.964 1.00 60.98 N ANISOU 190 N TRP A 47 8605 6692 7873 -175 18 -1242 N ATOM 191 CA TRP A 47 26.868 12.329 113.443 1.00 62.24 C ANISOU 191 CA TRP A 47 8720 6918 8011 -258 -120 -1421 C ATOM 192 C TRP A 47 27.497 10.958 113.200 1.00 61.60 C ANISOU 192 C TRP A 47 8498 6980 7928 -210 -299 -1448 C ATOM 193 O TRP A 47 28.543 10.889 112.556 1.00 59.84 O ANISOU 193 O TRP A 47 8117 6838 7782 -287 -364 -1551 O ATOM 194 CB TRP A 47 26.965 12.720 114.923 1.00 63.55 C ANISOU 194 CB TRP A 47 9059 7021 8067 -255 -158 -1518 C ATOM 195 CG TRP A 47 28.374 13.065 115.303 1.00 66.96 C ANISOU 195 CG TRP A 47 9431 7504 8506 -356 -290 -1734 C ATOM 196 CD1 TRP A 47 28.984 14.280 115.162 1.00 70.44 C ANISOU 196 CD1 TRP A 47 9862 7890 9011 -501 -208 -1854 C ATOM 197 CD2 TRP A 47 29.395 12.150 115.738 1.00 67.75 C ANISOU 197 CD2 TRP A 47 9444 7725 8572 -322 -530 -1874 C ATOM 198 NE1 TRP A 47 30.305 14.194 115.536 1.00 71.01 N ANISOU 198 NE1 TRP A 47 9826 8050 9106 -571 -379 -2077 N ATOM 199 CE2 TRP A 47 30.592 12.893 115.875 1.00 72.85 C ANISOU 199 CE2 TRP A 47 10002 8396 9282 -451 -593 -2094 C ATOM 200 CE3 TRP A 47 29.409 10.777 116.054 1.00 69.40 C ANISOU 200 CE3 TRP A 47 9655 8014 8699 -189 -699 -1845 C ATOM 201 CZ2 TRP A 47 31.792 12.310 116.325 1.00 72.38 C ANISOU 201 CZ2 TRP A 47 9825 8453 9223 -434 -843 -2300 C ATOM 202 CZ3 TRP A 47 30.596 10.198 116.487 1.00 71.33 C ANISOU 202 CZ3 TRP A 47 9820 8362 8921 -160 -946 -2028 C ATOM 203 CH2 TRP A 47 31.768 10.961 116.626 1.00 72.26 C ANISOU 203 CH2 TRP A 47 9820 8516 9118 -274 -1028 -2258 C ATOM 204 N VAL A 48 26.840 9.873 113.697 1.00 56.45 N ANISOU 204 N VAL A 48 7909 6348 7192 -88 -357 -1362 N ATOM 205 CA VAL A 48 27.251 8.469 113.551 1.00 55.11 C ANISOU 205 CA VAL A 48 7654 6292 6993 -16 -517 -1365 C ATOM 206 C VAL A 48 27.405 8.078 112.063 1.00 56.76 C ANISOU 206 C VAL A 48 7667 6580 7321 -43 -498 -1303 C ATOM 207 O VAL A 48 28.380 7.423 111.711 1.00 57.39 O ANISOU 207 O VAL A 48 7612 6764 7430 -51 -630 -1388 O ATOM 208 CB VAL A 48 26.306 7.518 114.329 1.00 58.46 C ANISOU 208 CB VAL A 48 8239 6678 7297 102 -517 -1268 C ATOM 209 CG1 VAL A 48 26.581 6.047 114.004 1.00 57.78 C ANISOU 209 CG1 VAL A 48 8083 6690 7181 179 -651 -1244 C ATOM 210 CG2 VAL A 48 26.408 7.764 115.831 1.00 58.41 C ANISOU 210 CG2 VAL A 48 8459 6590 7142 132 -564 -1354 C ATOM 211 N LEU A 49 26.475 8.518 111.208 1.00 50.39 N ANISOU 211 N LEU A 49 6851 5715 6579 -50 -341 -1171 N ATOM 212 CA LEU A 49 26.482 8.268 109.773 1.00 49.98 C ANISOU 212 CA LEU A 49 6665 5708 6618 -69 -309 -1101 C ATOM 213 C LEU A 49 27.682 8.904 109.046 1.00 55.77 C ANISOU 213 C LEU A 49 7298 6463 7431 -196 -296 -1217 C ATOM 214 O LEU A 49 28.325 8.234 108.228 1.00 57.12 O ANISOU 214 O LEU A 49 7334 6719 7651 -216 -351 -1240 O ATOM 215 CB LEU A 49 25.154 8.758 109.165 1.00 49.95 C ANISOU 215 CB LEU A 49 6713 5614 6651 -23 -164 -952 C ATOM 216 CG LEU A 49 24.941 8.556 107.671 1.00 54.32 C ANISOU 216 CG LEU A 49 7179 6187 7274 -16 -137 -864 C ATOM 217 CD1 LEU A 49 25.057 7.101 107.301 1.00 54.14 C ANISOU 217 CD1 LEU A 49 7047 6276 7246 34 -248 -829 C ATOM 218 CD2 LEU A 49 23.607 9.101 107.234 1.00 56.70 C ANISOU 218 CD2 LEU A 49 7544 6395 7606 58 -32 -745 C ATOM 219 N ILE A 50 27.944 10.190 109.310 1.00 51.69 N ANISOU 219 N ILE A 50 6853 5857 6929 -291 -199 -1294 N ATOM 220 CA ILE A 50 29.031 10.947 108.699 1.00 51.64 C ANISOU 220 CA ILE A 50 6776 5841 7004 -443 -136 -1425 C ATOM 221 C ILE A 50 30.377 10.503 109.298 1.00 57.26 C ANISOU 221 C ILE A 50 7347 6667 7744 -495 -294 -1636 C ATOM 222 O ILE A 50 31.308 10.261 108.530 1.00 59.19 O ANISOU 222 O ILE A 50 7434 6978 8079 -574 -302 -1731 O ATOM 223 CB ILE A 50 28.781 12.496 108.727 1.00 54.07 C ANISOU 223 CB ILE A 50 7234 5994 7316 -531 45 -1434 C ATOM 224 CG1 ILE A 50 27.511 12.871 107.905 1.00 53.98 C ANISOU 224 CG1 ILE A 50 7344 5876 7291 -448 174 -1237 C ATOM 225 CG2 ILE A 50 29.999 13.285 108.214 1.00 53.35 C ANISOU 225 CG2 ILE A 50 7085 5878 7309 -719 139 -1603 C ATOM 226 CD1 ILE A 50 26.776 14.216 108.349 1.00 52.57 C ANISOU 226 CD1 ILE A 50 7363 5536 7076 -445 315 -1201 C ATOM 227 N ALA A 51 30.481 10.362 110.639 1.00 52.55 N ANISOU 227 N ALA A 51 6809 6090 7068 -440 -428 -1716 N ATOM 228 CA ALA A 51 31.713 9.876 111.272 1.00 52.07 C ANISOU 228 CA ALA A 51 6622 6139 7023 -447 -629 -1928 C ATOM 229 C ALA A 51 32.068 8.494 110.683 1.00 57.27 C ANISOU 229 C ALA A 51 7130 6924 7704 -362 -760 -1909 C ATOM 230 O ALA A 51 33.169 8.353 110.150 1.00 58.09 O ANISOU 230 O ALA A 51 7037 7112 7921 -435 -808 -2067 O ATOM 231 CB ALA A 51 31.548 9.779 112.783 1.00 52.45 C ANISOU 231 CB ALA A 51 6824 6167 6937 -355 -769 -1978 C ATOM 232 N ALA A 52 31.104 7.524 110.675 1.00 52.71 N ANISOU 232 N ALA A 52 6639 6351 7038 -224 -787 -1722 N ATOM 233 CA ALA A 52 31.296 6.169 110.129 1.00 51.80 C ANISOU 233 CA ALA A 52 6418 6339 6926 -136 -897 -1681 C ATOM 234 C ALA A 52 31.762 6.159 108.687 1.00 55.24 C ANISOU 234 C ALA A 52 6681 6814 7492 -228 -803 -1682 C ATOM 235 O ALA A 52 32.681 5.416 108.368 1.00 54.48 O ANISOU 235 O ALA A 52 6424 6822 7454 -218 -914 -1789 O ATOM 236 CB ALA A 52 30.038 5.333 110.278 1.00 52.32 C ANISOU 236 CB ALA A 52 6623 6372 6885 -10 -881 -1479 C ATOM 237 N TYR A 53 31.153 6.986 107.826 1.00 52.87 N ANISOU 237 N TYR A 53 6433 6422 7234 -309 -600 -1572 N ATOM 238 CA TYR A 53 31.528 7.095 106.412 1.00 52.97 C ANISOU 238 CA TYR A 53 6349 6434 7345 -403 -480 -1562 C ATOM 239 C TYR A 53 32.896 7.765 106.220 1.00 57.80 C ANISOU 239 C TYR A 53 6821 7063 8077 -567 -433 -1793 C ATOM 240 O TYR A 53 33.666 7.292 105.381 1.00 56.78 O ANISOU 240 O TYR A 53 6542 6996 8037 -619 -419 -1865 O ATOM 241 CB TYR A 53 30.457 7.843 105.616 1.00 53.78 C ANISOU 241 CB TYR A 53 6596 6408 7429 -418 -295 -1386 C ATOM 242 CG TYR A 53 29.478 6.951 104.882 1.00 54.51 C ANISOU 242 CG TYR A 53 6713 6514 7483 -304 -310 -1195 C ATOM 243 CD1 TYR A 53 29.778 6.443 103.620 1.00 56.11 C ANISOU 243 CD1 TYR A 53 6845 6745 7729 -328 -279 -1162 C ATOM 244 CD2 TYR A 53 28.220 6.676 105.414 1.00 54.80 C ANISOU 244 CD2 TYR A 53 6848 6524 7449 -183 -337 -1058 C ATOM 245 CE1 TYR A 53 28.878 5.631 102.933 1.00 54.90 C ANISOU 245 CE1 TYR A 53 6715 6604 7542 -227 -305 -1000 C ATOM 246 CE2 TYR A 53 27.310 5.867 104.732 1.00 55.48 C ANISOU 246 CE2 TYR A 53 6934 6625 7521 -91 -349 -909 C ATOM 247 CZ TYR A 53 27.639 5.363 103.484 1.00 60.65 C ANISOU 247 CZ TYR A 53 7519 7315 8212 -111 -344 -879 C ATOM 248 OH TYR A 53 26.741 4.610 102.782 1.00 62.80 O ANISOU 248 OH TYR A 53 7793 7598 8470 -24 -365 -744 O ATOM 249 N VAL A 54 33.202 8.856 106.989 1.00 55.15 N ANISOU 249 N VAL A 54 6531 6671 7755 -657 -395 -1922 N ATOM 250 CA VAL A 54 34.498 9.563 106.927 1.00 55.56 C ANISOU 250 CA VAL A 54 6438 6734 7938 -834 -340 -2179 C ATOM 251 C VAL A 54 35.639 8.622 107.390 1.00 60.82 C ANISOU 251 C VAL A 54 6869 7565 8676 -788 -571 -2391 C ATOM 252 O VAL A 54 36.626 8.459 106.662 1.00 61.28 O ANISOU 252 O VAL A 54 6727 7681 8877 -890 -528 -2548 O ATOM 253 CB VAL A 54 34.493 10.934 107.663 1.00 59.76 C ANISOU 253 CB VAL A 54 7087 7158 8460 -942 -246 -2268 C ATOM 254 CG1 VAL A 54 35.907 11.478 107.867 1.00 59.40 C ANISOU 254 CG1 VAL A 54 6855 7153 8562 -1118 -241 -2582 C ATOM 255 CG2 VAL A 54 33.638 11.958 106.919 1.00 59.75 C ANISOU 255 CG2 VAL A 54 7296 6984 8422 -1007 9 -2101 C ATOM 256 N ALA A 55 35.470 7.971 108.571 1.00 56.60 N ANISOU 256 N ALA A 55 6378 7093 8035 -624 -811 -2396 N ATOM 257 CA ALA A 55 36.432 7.012 109.138 1.00 56.07 C ANISOU 257 CA ALA A 55 6139 7169 7995 -522 -1078 -2582 C ATOM 258 C ALA A 55 36.747 5.890 108.142 1.00 61.27 C ANISOU 258 C ALA A 55 6646 7917 8716 -471 -1102 -2547 C ATOM 259 O ALA A 55 37.920 5.584 107.925 1.00 61.83 O ANISOU 259 O ALA A 55 6475 8089 8927 -503 -1187 -2771 O ATOM 260 CB ALA A 55 35.906 6.428 110.447 1.00 56.41 C ANISOU 260 CB ALA A 55 6361 7217 7856 -328 -1297 -2521 C ATOM 261 N VAL A 56 35.706 5.318 107.505 1.00 57.30 N ANISOU 261 N VAL A 56 6272 7375 8125 -399 -1019 -2282 N ATOM 262 CA VAL A 56 35.856 4.273 106.499 1.00 56.90 C ANISOU 262 CA VAL A 56 6115 7389 8113 -354 -1021 -2219 C ATOM 263 C VAL A 56 36.620 4.813 105.285 1.00 62.77 C ANISOU 263 C VAL A 56 6700 8121 9027 -543 -820 -2328 C ATOM 264 O VAL A 56 37.566 4.167 104.849 1.00 64.10 O ANISOU 264 O VAL A 56 6663 8385 9306 -547 -875 -2473 O ATOM 265 CB VAL A 56 34.508 3.588 106.146 1.00 59.62 C ANISOU 265 CB VAL A 56 6640 7689 8325 -243 -984 -1927 C ATOM 266 CG1 VAL A 56 34.538 2.947 104.762 1.00 59.09 C ANISOU 266 CG1 VAL A 56 6493 7644 8313 -264 -893 -1843 C ATOM 267 CG2 VAL A 56 34.131 2.558 107.207 1.00 59.07 C ANISOU 267 CG2 VAL A 56 6674 7658 8111 -51 -1197 -1876 C ATOM 268 N PHE A 57 36.252 6.016 104.797 1.00 58.73 N ANISOU 268 N PHE A 57 6299 7481 8533 -695 -580 -2274 N ATOM 269 CA PHE A 57 36.858 6.706 103.653 1.00 57.92 C ANISOU 269 CA PHE A 57 6132 7315 8561 -895 -332 -2360 C ATOM 270 C PHE A 57 38.368 6.919 103.845 1.00 63.69 C ANISOU 270 C PHE A 57 6592 8126 9482 -1026 -348 -2701 C ATOM 271 O PHE A 57 39.148 6.614 102.936 1.00 63.44 O ANISOU 271 O PHE A 57 6398 8126 9579 -1114 -247 -2811 O ATOM 272 CB PHE A 57 36.124 8.050 103.397 1.00 58.87 C ANISOU 272 CB PHE A 57 6483 7258 8625 -1005 -102 -2247 C ATOM 273 CG PHE A 57 36.639 8.897 102.258 1.00 59.46 C ANISOU 273 CG PHE A 57 6584 7216 8792 -1215 189 -2317 C ATOM 274 CD1 PHE A 57 36.261 8.633 100.947 1.00 61.78 C ANISOU 274 CD1 PHE A 57 6985 7438 9049 -1219 334 -2158 C ATOM 275 CD2 PHE A 57 37.486 9.972 102.498 1.00 61.33 C ANISOU 275 CD2 PHE A 57 6767 7396 9139 -1415 331 -2546 C ATOM 276 CE1 PHE A 57 36.738 9.414 99.891 1.00 62.59 C ANISOU 276 CE1 PHE A 57 7169 7403 9209 -1413 624 -2220 C ATOM 277 CE2 PHE A 57 37.973 10.748 101.440 1.00 64.09 C ANISOU 277 CE2 PHE A 57 7176 7612 9564 -1626 639 -2618 C ATOM 278 CZ PHE A 57 37.580 10.474 100.146 1.00 62.01 C ANISOU 278 CZ PHE A 57 7055 7264 9244 -1620 789 -2447 C ATOM 279 N VAL A 58 38.774 7.431 105.027 1.00 61.45 N ANISOU 279 N VAL A 58 6255 7874 9221 -1037 -476 -2880 N ATOM 280 CA VAL A 58 40.174 7.710 105.347 1.00 61.43 C ANISOU 280 CA VAL A 58 5973 7954 9413 -1156 -523 -3240 C ATOM 281 C VAL A 58 40.961 6.401 105.449 1.00 64.85 C ANISOU 281 C VAL A 58 6156 8560 9922 -1010 -771 -3380 C ATOM 282 O VAL A 58 41.909 6.218 104.689 1.00 66.49 O ANISOU 282 O VAL A 58 6128 8818 10315 -1116 -676 -3566 O ATOM 283 CB VAL A 58 40.343 8.647 106.585 1.00 65.90 C ANISOU 283 CB VAL A 58 6569 8499 9970 -1200 -610 -3397 C ATOM 284 CG1 VAL A 58 41.817 8.856 106.935 1.00 65.70 C ANISOU 284 CG1 VAL A 58 6217 8578 10168 -1312 -696 -3805 C ATOM 285 CG2 VAL A 58 39.654 9.997 106.368 1.00 65.55 C ANISOU 285 CG2 VAL A 58 6768 8271 9868 -1358 -331 -3277 C ATOM 286 N VAL A 59 40.524 5.475 106.322 1.00 58.88 N ANISOU 286 N VAL A 59 5479 7878 9016 -764 -1064 -3281 N ATOM 287 CA VAL A 59 41.153 4.166 106.569 1.00 57.34 C ANISOU 287 CA VAL A 59 5113 7829 8843 -573 -1340 -3387 C ATOM 288 C VAL A 59 41.233 3.314 105.279 1.00 62.98 C ANISOU 288 C VAL A 59 5743 8570 9615 -572 -1223 -3294 C ATOM 289 O VAL A 59 42.250 2.661 105.053 1.00 62.56 O ANISOU 289 O VAL A 59 5431 8631 9708 -535 -1326 -3503 O ATOM 290 CB VAL A 59 40.471 3.448 107.767 1.00 59.50 C ANISOU 290 CB VAL A 59 5596 8121 8890 -319 -1628 -3253 C ATOM 291 CG1 VAL A 59 40.973 2.024 107.951 1.00 58.45 C ANISOU 291 CG1 VAL A 59 5360 8109 8739 -97 -1901 -3318 C ATOM 292 CG2 VAL A 59 40.666 4.255 109.056 1.00 59.14 C ANISOU 292 CG2 VAL A 59 5605 8059 8807 -320 -1768 -3410 C ATOM 293 N ALA A 60 40.208 3.373 104.409 1.00 61.14 N ANISOU 293 N ALA A 60 5719 8231 9281 -615 -1008 -3003 N ATOM 294 CA ALA A 60 40.230 2.659 103.131 1.00 61.24 C ANISOU 294 CA ALA A 60 5688 8248 9332 -629 -879 -2906 C ATOM 295 C ALA A 60 41.197 3.338 102.136 1.00 69.03 C ANISOU 295 C ALA A 60 6491 9205 10533 -870 -613 -3111 C ATOM 296 O ALA A 60 41.891 2.630 101.416 1.00 69.14 O ANISOU 296 O ALA A 60 6325 9284 10663 -874 -587 -3211 O ATOM 297 CB ALA A 60 38.834 2.564 102.540 1.00 61.37 C ANISOU 297 CB ALA A 60 5987 8158 9174 -592 -757 -2558 C ATOM 298 N LEU A 61 41.266 4.696 102.106 1.00 67.70 N ANISOU 298 N LEU A 61 6377 8926 10418 -1076 -398 -3183 N ATOM 299 CA LEU A 61 42.166 5.406 101.184 1.00 68.12 C ANISOU 299 CA LEU A 61 6297 8919 10667 -1333 -97 -3387 C ATOM 300 C LEU A 61 43.613 5.224 101.558 1.00 73.22 C ANISOU 300 C LEU A 61 6559 9704 11559 -1385 -198 -3782 C ATOM 301 O LEU A 61 44.427 4.907 100.692 1.00 72.06 O ANISOU 301 O LEU A 61 6216 9583 11579 -1481 -54 -3935 O ATOM 302 CB LEU A 61 41.839 6.905 101.067 1.00 68.20 C ANISOU 302 CB LEU A 61 6506 8754 10655 -1540 173 -3362 C ATOM 303 CG LEU A 61 40.797 7.307 100.024 1.00 72.99 C ANISOU 303 CG LEU A 61 7451 9179 11104 -1582 420 -3057 C ATOM 304 CD1 LEU A 61 40.745 8.805 99.890 1.00 73.26 C ANISOU 304 CD1 LEU A 61 7661 9032 11141 -1794 696 -3096 C ATOM 305 CD2 LEU A 61 41.089 6.692 98.651 1.00 74.41 C ANISOU 305 CD2 LEU A 61 7615 9330 11328 -1632 596 -3020 C ATOM 306 N VAL A 62 43.933 5.419 102.852 1.00 71.68 N ANISOU 306 N VAL A 62 6254 9595 11387 -1313 -451 -3959 N ATOM 307 CA VAL A 62 45.284 5.259 103.382 1.00 72.16 C ANISOU 307 CA VAL A 62 5932 9803 11684 -1325 -618 -4365 C ATOM 308 C VAL A 62 45.721 3.788 103.281 1.00 77.13 C ANISOU 308 C VAL A 62 6376 10583 12347 -1101 -861 -4407 C ATOM 309 O VAL A 62 46.740 3.508 102.653 1.00 77.38 O ANISOU 309 O VAL A 62 6109 10682 12610 -1184 -777 -4656 O ATOM 310 CB VAL A 62 45.444 5.855 104.806 1.00 76.08 C ANISOU 310 CB VAL A 62 6402 10340 12163 -1280 -858 -4531 C ATOM 311 CG1 VAL A 62 46.873 5.680 105.322 1.00 75.90 C ANISOU 311 CG1 VAL A 62 5960 10480 12400 -1275 -1067 -4983 C ATOM 312 CG2 VAL A 62 45.056 7.331 104.824 1.00 75.84 C ANISOU 312 CG2 VAL A 62 6555 10150 12111 -1517 -587 -4501 C ATOM 313 N GLY A 63 44.911 2.883 103.833 1.00 73.45 N ANISOU 313 N GLY A 63 6108 10150 11650 -833 -1124 -4158 N ATOM 314 CA GLY A 63 45.160 1.447 103.846 1.00 73.15 C ANISOU 314 CA GLY A 63 5975 10232 11588 -588 -1374 -4152 C ATOM 315 C GLY A 63 45.409 0.806 102.496 1.00 78.24 C ANISOU 315 C GLY A 63 6528 10877 12325 -643 -1173 -4109 C ATOM 316 O GLY A 63 46.397 0.085 102.330 1.00 78.67 O ANISOU 316 O GLY A 63 6297 11048 12546 -568 -1285 -4340 O ATOM 317 N ASN A 64 44.513 1.044 101.526 1.00 74.39 N ANISOU 317 N ASN A 64 6287 10254 11725 -757 -887 -3819 N ATOM 318 CA ASN A 64 44.626 0.446 100.196 1.00 73.85 C ANISOU 318 CA ASN A 64 6194 10159 11705 -808 -684 -3745 C ATOM 319 C ASN A 64 45.778 1.000 99.372 1.00 77.87 C ANISOU 319 C ASN A 64 6440 10655 12492 -1058 -400 -4043 C ATOM 320 O ASN A 64 46.260 0.289 98.499 1.00 77.55 O ANISOU 320 O ASN A 64 6275 10642 12548 -1061 -307 -4094 O ATOM 321 CB ASN A 64 43.305 0.514 99.426 1.00 72.53 C ANISOU 321 CB ASN A 64 6388 9850 11321 -829 -503 -3357 C ATOM 322 CG ASN A 64 42.253 -0.416 99.971 1.00 82.15 C ANISOU 322 CG ASN A 64 7813 11097 12304 -579 -753 -3083 C ATOM 323 OD1 ASN A 64 42.395 -1.642 99.964 1.00 74.57 O ANISOU 323 OD1 ASN A 64 6792 10225 11315 -400 -932 -3067 O ATOM 324 ND2 ASN A 64 41.166 0.141 100.454 1.00 72.37 N ANISOU 324 ND2 ASN A 64 6830 9773 10894 -564 -754 -2871 N ATOM 325 N THR A 65 46.223 2.246 99.631 1.00 75.63 N ANISOU 325 N THR A 65 6078 10319 12339 -1276 -243 -4247 N ATOM 326 CA THR A 65 47.377 2.824 98.922 1.00 76.16 C ANISOU 326 CA THR A 65 5881 10362 12692 -1543 57 -4575 C ATOM 327 C THR A 65 48.652 2.173 99.473 1.00 80.14 C ANISOU 327 C THR A 65 5932 11065 13452 -1445 -191 -4969 C ATOM 328 O THR A 65 49.556 1.840 98.705 1.00 79.42 O ANISOU 328 O THR A 65 5581 11008 13587 -1542 -27 -5193 O ATOM 329 CB THR A 65 47.393 4.366 98.973 1.00 87.70 C ANISOU 329 CB THR A 65 7438 11682 14201 -1822 334 -4661 C ATOM 330 OG1 THR A 65 47.166 4.802 100.309 1.00 88.56 O ANISOU 330 OG1 THR A 65 7564 11843 14241 -1729 67 -4693 O ATOM 331 CG2 THR A 65 46.356 4.997 98.045 1.00 87.80 C ANISOU 331 CG2 THR A 65 7874 11475 14012 -1945 658 -4325 C ATOM 332 N LEU A 66 48.674 1.928 100.805 1.00 76.74 N ANISOU 332 N LEU A 66 5431 10759 12968 -1226 -601 -5043 N ATOM 333 CA LEU A 66 49.753 1.253 101.527 1.00 76.14 C ANISOU 333 CA LEU A 66 4970 10874 13084 -1055 -938 -5398 C ATOM 334 C LEU A 66 49.905 -0.213 101.097 1.00 80.25 C ANISOU 334 C LEU A 66 5418 11487 13586 -819 -1096 -5336 C ATOM 335 O LEU A 66 51.009 -0.743 101.162 1.00 80.46 O ANISOU 335 O LEU A 66 5071 11651 13851 -740 -1241 -5674 O ATOM 336 CB LEU A 66 49.555 1.340 103.048 1.00 75.95 C ANISOU 336 CB LEU A 66 4998 10923 12936 -855 -1345 -5439 C ATOM 337 CG LEU A 66 49.775 2.689 103.735 1.00 80.47 C ANISOU 337 CG LEU A 66 5528 11455 13591 -1053 -1288 -5634 C ATOM 338 CD1 LEU A 66 49.794 2.514 105.234 1.00 80.40 C ANISOU 338 CD1 LEU A 66 5534 11540 13472 -807 -1747 -5723 C ATOM 339 CD2 LEU A 66 51.073 3.360 103.292 1.00 83.63 C ANISOU 339 CD2 LEU A 66 5509 11892 14376 -1327 -1064 -6087 C ATOM 340 N VAL A 67 48.811 -0.868 100.667 1.00 76.52 N ANISOU 340 N VAL A 67 5290 10939 12843 -703 -1072 -4924 N ATOM 341 CA VAL A 67 48.864 -2.242 100.158 1.00 76.01 C ANISOU 341 CA VAL A 67 5204 10935 12739 -502 -1177 -4833 C ATOM 342 C VAL A 67 49.678 -2.190 98.847 1.00 82.44 C ANISOU 342 C VAL A 67 5793 11725 13806 -721 -818 -5010 C ATOM 343 O VAL A 67 50.663 -2.922 98.708 1.00 82.02 O ANISOU 343 O VAL A 67 5419 11789 13955 -627 -916 -5272 O ATOM 344 CB VAL A 67 47.459 -2.892 99.963 1.00 78.57 C ANISOU 344 CB VAL A 67 5955 11174 12724 -360 -1208 -4362 C ATOM 345 CG1 VAL A 67 47.565 -4.260 99.289 1.00 78.24 C ANISOU 345 CG1 VAL A 67 5894 11176 12657 -199 -1256 -4279 C ATOM 346 CG2 VAL A 67 46.730 -3.027 101.289 1.00 78.19 C ANISOU 346 CG2 VAL A 67 6120 11146 12443 -143 -1544 -4220 C ATOM 347 N CYS A 68 49.296 -1.268 97.931 1.00 80.53 N ANISOU 347 N CYS A 68 5728 11319 13553 -1010 -399 -4887 N ATOM 348 CA CYS A 68 49.939 -1.045 96.634 1.00 81.07 C ANISOU 348 CA CYS A 68 5679 11308 13817 -1261 17 -5022 C ATOM 349 C CYS A 68 51.410 -0.695 96.788 1.00 88.60 C ANISOU 349 C CYS A 68 6150 12360 15155 -1400 77 -5533 C ATOM 350 O CYS A 68 52.226 -1.129 95.976 1.00 89.03 O ANISOU 350 O CYS A 68 5969 12436 15422 -1473 260 -5732 O ATOM 351 CB CYS A 68 49.191 0.018 95.836 1.00 80.99 C ANISOU 351 CB CYS A 68 6017 11079 13677 -1522 413 -4794 C ATOM 352 SG CYS A 68 47.488 -0.431 95.413 1.00 84.68 S ANISOU 352 SG CYS A 68 7010 11429 13736 -1370 375 -4229 S ATOM 353 N LEU A 69 51.743 0.077 97.845 1.00 86.58 N ANISOU 353 N LEU A 69 5739 12163 14996 -1435 -81 -5758 N ATOM 354 CA LEU A 69 53.101 0.497 98.185 1.00 86.76 C ANISOU 354 CA LEU A 69 5277 12294 15395 -1561 -77 -6279 C ATOM 355 C LEU A 69 53.939 -0.652 98.771 1.00 91.16 C ANISOU 355 C LEU A 69 5458 13070 16110 -1260 -493 -6547 C ATOM 356 O LEU A 69 55.110 -0.764 98.434 1.00 90.55 O ANISOU 356 O LEU A 69 4952 13074 16377 -1348 -395 -6949 O ATOM 357 CB LEU A 69 53.065 1.703 99.149 1.00 87.03 C ANISOU 357 CB LEU A 69 5314 12310 15442 -1681 -139 -6405 C ATOM 358 CG LEU A 69 52.885 3.096 98.517 1.00 91.91 C ANISOU 358 CG LEU A 69 6116 12724 16083 -2068 352 -6380 C ATOM 359 CD1 LEU A 69 52.377 4.098 99.541 1.00 92.35 C ANISOU 359 CD1 LEU A 69 6328 12744 16019 -2102 224 -6342 C ATOM 360 CD2 LEU A 69 54.195 3.610 97.924 1.00 94.60 C ANISOU 360 CD2 LEU A 69 6064 13055 16824 -2382 709 -6842 C ATOM 361 N ALA A 70 53.335 -1.502 99.631 1.00 89.38 N ANISOU 361 N ALA A 70 5403 12926 15631 -903 -943 -6334 N ATOM 362 CA ALA A 70 53.949 -2.679 100.276 1.00 90.03 C ANISOU 362 CA ALA A 70 5243 13191 15775 -550 -1395 -6519 C ATOM 363 C ALA A 70 54.484 -3.716 99.275 1.00 95.91 C ANISOU 363 C ALA A 70 5809 13974 16658 -489 -1282 -6582 C ATOM 364 O ALA A 70 55.473 -4.395 99.560 1.00 95.61 O ANISOU 364 O ALA A 70 5391 14090 16845 -307 -1527 -6924 O ATOM 365 CB ALA A 70 52.933 -3.352 101.186 1.00 90.76 C ANISOU 365 CB ALA A 70 5710 13288 15487 -222 -1785 -6170 C ATOM 366 N VAL A 71 53.788 -3.869 98.138 1.00 93.56 N ANISOU 366 N VAL A 71 5805 13534 16209 -616 -937 -6246 N ATOM 367 CA VAL A 71 54.112 -4.805 97.062 1.00 93.71 C ANISOU 367 CA VAL A 71 5745 13552 16308 -587 -772 -6237 C ATOM 368 C VAL A 71 55.163 -4.165 96.140 1.00101.83 C ANISOU 368 C VAL A 71 6432 14547 17711 -923 -332 -6600 C ATOM 369 O VAL A 71 56.087 -4.853 95.710 1.00101.05 O ANISOU 369 O VAL A 71 5996 14536 17863 -869 -312 -6874 O ATOM 370 CB VAL A 71 52.809 -5.254 96.333 1.00 96.36 C ANISOU 370 CB VAL A 71 6583 13744 16287 -561 -632 -5711 C ATOM 371 CG1 VAL A 71 53.096 -6.118 95.106 1.00 95.94 C ANISOU 371 CG1 VAL A 71 6491 13660 16301 -574 -405 -5686 C ATOM 372 CG2 VAL A 71 51.885 -5.993 97.297 1.00 95.84 C ANISOU 372 CG2 VAL A 71 6802 13720 15894 -228 -1060 -5415 C ATOM 373 N TRP A 72 55.048 -2.841 95.890 1.00102.79 N ANISOU 373 N TRP A 72 6640 14537 17879 -1266 21 -6624 N ATOM 374 CA TRP A 72 55.977 -2.072 95.059 1.00104.94 C ANISOU 374 CA TRP A 72 6648 14738 18487 -1633 496 -6965 C ATOM 375 C TRP A 72 57.354 -1.909 95.737 1.00110.33 C ANISOU 375 C TRP A 72 6725 15601 19593 -1641 339 -7553 C ATOM 376 O TRP A 72 58.388 -2.009 95.064 1.00110.86 O ANISOU 376 O TRP A 72 6425 15693 20004 -1793 600 -7910 O ATOM 377 CB TRP A 72 55.381 -0.699 94.676 1.00104.96 C ANISOU 377 CB TRP A 72 6979 14526 18374 -1976 900 -6801 C ATOM 378 CG TRP A 72 56.257 0.086 93.741 1.00107.11 C ANISOU 378 CG TRP A 72 7067 14680 18952 -2375 1449 -7118 C ATOM 379 CD1 TRP A 72 56.445 -0.141 92.407 1.00110.27 C ANISOU 379 CD1 TRP A 72 7559 14942 19395 -2546 1882 -7083 C ATOM 380 CD2 TRP A 72 57.142 1.159 94.094 1.00107.47 C ANISOU 380 CD2 TRP A 72 6785 14732 19317 -2652 1626 -7558 C ATOM 381 NE1 TRP A 72 57.372 0.742 91.902 1.00109.97 N ANISOU 381 NE1 TRP A 72 7296 14811 19678 -2922 2345 -7464 N ATOM 382 CE2 TRP A 72 57.815 1.552 92.914 1.00111.67 C ANISOU 382 CE2 TRP A 72 7239 15115 20076 -3001 2202 -7767 C ATOM 383 CE3 TRP A 72 57.420 1.841 95.293 1.00109.39 C ANISOU 383 CE3 TRP A 72 6811 15082 19672 -2649 1365 -7802 C ATOM 384 CZ2 TRP A 72 58.753 2.595 92.899 1.00111.63 C ANISOU 384 CZ2 TRP A 72 6933 15063 20417 -3358 2541 -8218 C ATOM 385 CZ3 TRP A 72 58.348 2.878 95.279 1.00111.29 C ANISOU 385 CZ3 TRP A 72 6742 15288 20257 -2996 1675 -8249 C ATOM 386 CH2 TRP A 72 59.004 3.245 94.094 1.00112.08 C ANISOU 386 CH2 TRP A 72 6757 15238 20590 -3352 2264 -8457 C ATOM 387 N ARG A 73 57.369 -1.667 97.062 1.00106.23 N ANISOU 387 N ARG A 73 6101 15206 19055 -1474 -88 -7668 N ATOM 388 CA ARG A 73 58.617 -1.500 97.796 1.00105.82 C ANISOU 388 CA ARG A 73 5484 15334 19390 -1452 -303 -8233 C ATOM 389 C ARG A 73 59.302 -2.838 98.110 1.00108.58 C ANISOU 389 C ARG A 73 5504 15884 19867 -1070 -728 -8441 C ATOM 390 O ARG A 73 60.530 -2.914 97.998 1.00110.11 O ANISOU 390 O ARG A 73 5160 16199 20478 -1116 -710 -8948 O ATOM 391 CB ARG A 73 58.441 -0.620 99.040 1.00107.31 C ANISOU 391 CB ARG A 73 5696 15558 19520 -1452 -566 -8312 C ATOM 392 CG ARG A 73 58.962 0.799 98.796 1.00124.25 C ANISOU 392 CG ARG A 73 7678 17605 21925 -1903 -131 -8606 C ATOM 393 CD ARG A 73 58.235 1.868 99.594 1.00140.35 C ANISOU 393 CD ARG A 73 10013 19563 23752 -1993 -193 -8445 C ATOM 394 NE ARG A 73 58.589 3.215 99.134 1.00149.62 N ANISOU 394 NE ARG A 73 11127 20593 25127 -2452 309 -8657 N ATOM 395 CZ ARG A 73 58.217 4.345 99.732 1.00164.41 C ANISOU 395 CZ ARG A 73 13175 22383 26910 -2615 348 -8630 C ATOM 396 NH1 ARG A 73 57.480 4.311 100.837 1.00148.00 N ANISOU 396 NH1 ARG A 73 11332 20355 24548 -2357 -86 -8405 N ATOM 397 NH2 ARG A 73 58.587 5.518 99.235 1.00147.27 N ANISOU 397 NH2 ARG A 73 10963 20064 24927 -3040 839 -8834 N ATOM 398 N ASN A 74 58.532 -3.888 98.453 1.00102.05 N ANISOU 398 N ASN A 74 4993 15084 18698 -704 -1083 -8071 N ATOM 399 CA ASN A 74 59.081 -5.216 98.749 1.00101.05 C ANISOU 399 CA ASN A 74 4636 15120 18636 -311 -1492 -8221 C ATOM 400 C ASN A 74 58.881 -6.215 97.583 1.00104.77 C ANISOU 400 C ASN A 74 5244 15528 19037 -267 -1264 -7991 C ATOM 401 O ASN A 74 57.756 -6.653 97.312 1.00103.94 O ANISOU 401 O ASN A 74 5626 15312 18554 -186 -1242 -7496 O ATOM 402 CB ASN A 74 58.527 -5.745 100.086 1.00 99.59 C ANISOU 402 CB ASN A 74 4689 15013 18139 95 -2091 -8044 C ATOM 403 CG ASN A 74 59.111 -7.050 100.605 1.00118.76 C ANISOU 403 CG ASN A 74 6918 17599 20606 543 -2584 -8223 C ATOM 404 OD1 ASN A 74 59.735 -7.849 99.889 1.00110.68 O ANISOU 404 OD1 ASN A 74 5648 16627 19777 617 -2507 -8378 O ATOM 405 ND2 ASN A 74 58.887 -7.310 101.883 1.00110.55 N ANISOU 405 ND2 ASN A 74 6023 16625 19357 868 -3105 -8194 N ATOM 406 N HIS A 75 59.992 -6.591 96.921 1.00102.01 N ANISOU 406 N HIS A 75 4445 15250 19062 -315 -1104 -8375 N ATOM 407 CA HIS A 75 60.006 -7.526 95.790 1.00102.37 C ANISOU 407 CA HIS A 75 4555 15243 19098 -286 -869 -8236 C ATOM 408 C HIS A 75 59.702 -8.990 96.177 1.00105.61 C ANISOU 408 C HIS A 75 5123 15733 19270 183 -1326 -8030 C ATOM 409 O HIS A 75 59.239 -9.758 95.326 1.00105.11 O ANISOU 409 O HIS A 75 5317 15584 19038 220 -1158 -7735 O ATOM 410 CB HIS A 75 61.320 -7.426 95.006 1.00103.76 C ANISOU 410 CB HIS A 75 4192 15465 19769 -493 -534 -8740 C ATOM 411 CG HIS A 75 61.505 -6.151 94.235 1.00107.98 C ANISOU 411 CG HIS A 75 4689 15849 20488 -1001 69 -8862 C ATOM 412 ND1 HIS A 75 61.216 -4.913 94.791 1.00110.38 N ANISOU 412 ND1 HIS A 75 5076 16102 20760 -1222 124 -8876 N ATOM 413 CD2 HIS A 75 62.034 -5.960 93.003 1.00110.35 C ANISOU 413 CD2 HIS A 75 4872 16037 21020 -1318 634 -9010 C ATOM 414 CE1 HIS A 75 61.544 -4.019 93.870 1.00110.07 C ANISOU 414 CE1 HIS A 75 4992 15913 20916 -1661 718 -9014 C ATOM 415 NE2 HIS A 75 62.046 -4.601 92.780 1.00110.34 N ANISOU 415 NE2 HIS A 75 4912 15901 21112 -1738 1049 -9103 N ATOM 416 N HIS A 76 59.938 -9.373 97.453 1.00101.34 N ANISOU 416 N HIS A 76 4465 15341 18697 539 -1898 -8180 N ATOM 417 CA HIS A 76 59.639 -10.728 97.941 1.00100.73 C ANISOU 417 CA HIS A 76 4591 15319 18364 1000 -2349 -7990 C ATOM 418 C HIS A 76 58.127 -10.913 98.094 1.00101.74 C ANISOU 418 C HIS A 76 5370 15307 17981 1055 -2383 -7388 C ATOM 419 O HIS A 76 57.625 -12.035 98.002 1.00101.52 O ANISOU 419 O HIS A 76 5624 15251 17698 1315 -2542 -7111 O ATOM 420 CB HIS A 76 60.375 -11.019 99.258 1.00102.01 C ANISOU 420 CB HIS A 76 4468 15660 18633 1367 -2946 -8351 C ATOM 421 CG HIS A 76 61.863 -10.985 99.119 1.00105.69 C ANISOU 421 CG HIS A 76 4258 16281 19619 1363 -2964 -8969 C ATOM 422 ND1 HIS A 76 62.572 -9.804 99.242 1.00107.62 N ANISOU 422 ND1 HIS A 76 4091 16579 20219 1065 -2802 -9378 N ATOM 423 CD2 HIS A 76 62.726 -11.981 98.817 1.00107.61 C ANISOU 423 CD2 HIS A 76 4173 16627 20087 1607 -3096 -9241 C ATOM 424 CE1 HIS A 76 63.839 -10.120 99.034 1.00107.10 C ANISOU 424 CE1 HIS A 76 3441 16654 20597 1134 -2845 -9900 C ATOM 425 NE2 HIS A 76 63.983 -11.420 98.785 1.00107.48 N ANISOU 425 NE2 HIS A 76 3512 16740 20586 1468 -3031 -9840 N ATOM 426 N MET A 77 57.408 -9.785 98.285 1.00 96.07 N ANISOU 426 N MET A 77 4879 14493 17129 793 -2207 -7203 N ATOM 427 CA MET A 77 55.951 -9.699 98.414 1.00 94.70 C ANISOU 427 CA MET A 77 5281 14181 16519 782 -2182 -6670 C ATOM 428 C MET A 77 55.241 -9.748 97.048 1.00 94.75 C ANISOU 428 C MET A 77 5565 14029 16407 541 -1708 -6328 C ATOM 429 O MET A 77 54.019 -9.839 97.012 1.00 93.49 O ANISOU 429 O MET A 77 5863 13757 15900 548 -1681 -5889 O ATOM 430 CB MET A 77 55.555 -8.412 99.156 1.00 97.00 C ANISOU 430 CB MET A 77 5667 14437 16752 607 -2185 -6655 C ATOM 431 CG MET A 77 55.885 -8.446 100.622 1.00100.73 C ANISOU 431 CG MET A 77 6038 15031 17204 889 -2706 -6867 C ATOM 432 SD MET A 77 54.932 -7.238 101.558 1.00105.10 S ANISOU 432 SD MET A 77 6913 15498 17521 751 -2741 -6665 S ATOM 433 CE MET A 77 53.468 -8.156 101.788 1.00101.67 C ANISOU 433 CE MET A 77 7094 14952 16584 980 -2875 -6090 C ATOM 434 N ARG A 78 56.003 -9.697 95.932 1.00 88.39 N ANISOU 434 N ARG A 78 4487 13209 15887 333 -1339 -6540 N ATOM 435 CA ARG A 78 55.467 -9.709 94.572 1.00 85.78 C ANISOU 435 CA ARG A 78 4413 12718 15461 99 -880 -6263 C ATOM 436 C ARG A 78 55.081 -11.119 94.136 1.00 86.36 C ANISOU 436 C ARG A 78 4699 12780 15333 351 -992 -6009 C ATOM 437 O ARG A 78 55.605 -11.644 93.151 1.00 87.36 O ANISOU 437 O ARG A 78 4695 12890 15609 303 -760 -6105 O ATOM 438 CB ARG A 78 56.438 -9.023 93.597 1.00 84.16 C ANISOU 438 CB ARG A 78 3875 12474 15627 -245 -407 -6600 C ATOM 439 CG ARG A 78 56.686 -7.551 93.927 1.00 90.96 C ANISOU 439 CG ARG A 78 4601 13307 16653 -545 -228 -6809 C ATOM 440 CD ARG A 78 57.609 -6.897 92.923 1.00 96.47 C ANISOU 440 CD ARG A 78 5010 13938 17707 -909 287 -7141 C ATOM 441 NE ARG A 78 57.767 -5.460 93.157 1.00 98.77 N ANISOU 441 NE ARG A 78 5243 14164 18122 -1229 515 -7303 N ATOM 442 CZ ARG A 78 58.405 -4.636 92.331 1.00112.64 C ANISOU 442 CZ ARG A 78 6846 15812 20141 -1611 1028 -7554 C ATOM 443 NH1 ARG A 78 58.944 -5.093 91.208 1.00101.40 N ANISOU 443 NH1 ARG A 78 5309 14332 18887 -1724 1375 -7674 N ATOM 444 NH2 ARG A 78 58.501 -3.346 92.615 1.00102.06 N ANISOU 444 NH2 ARG A 78 5489 14403 18887 -1891 1218 -7688 N ATOM 445 N THR A 79 54.149 -11.729 94.885 1.00 79.73 N ANISOU 445 N THR A 79 4204 11940 14150 614 -1334 -5689 N ATOM 446 CA THR A 79 53.600 -13.075 94.648 1.00 77.98 C ANISOU 446 CA THR A 79 4257 11693 13680 865 -1477 -5407 C ATOM 447 C THR A 79 52.279 -12.963 93.854 1.00 78.83 C ANISOU 447 C THR A 79 4833 11631 13486 692 -1204 -4940 C ATOM 448 O THR A 79 51.733 -11.861 93.734 1.00 78.52 O ANISOU 448 O THR A 79 4935 11506 13395 445 -998 -4821 O ATOM 449 CB THR A 79 53.443 -13.847 95.991 1.00 82.90 C ANISOU 449 CB THR A 79 4975 12406 14118 1263 -2013 -5381 C ATOM 450 OG1 THR A 79 52.312 -13.365 96.718 1.00 77.03 O ANISOU 450 OG1 THR A 79 4592 11595 13082 1252 -2119 -5083 O ATOM 451 CG2 THR A 79 54.695 -13.768 96.880 1.00 83.31 C ANISOU 451 CG2 THR A 79 4577 12622 14455 1442 -2328 -5858 C ATOM 452 N VAL A 80 51.770 -14.092 93.320 1.00 73.71 N ANISOU 452 N VAL A 80 4427 10934 12647 829 -1212 -4690 N ATOM 453 CA VAL A 80 50.519 -14.145 92.542 1.00 72.45 C ANISOU 453 CA VAL A 80 4699 10624 12206 704 -999 -4266 C ATOM 454 C VAL A 80 49.329 -13.654 93.400 1.00 75.13 C ANISOU 454 C VAL A 80 5352 10921 12274 725 -1160 -3987 C ATOM 455 O VAL A 80 48.563 -12.802 92.940 1.00 74.50 O ANISOU 455 O VAL A 80 5478 10732 12098 497 -922 -3789 O ATOM 456 CB VAL A 80 50.291 -15.536 91.872 1.00 75.57 C ANISOU 456 CB VAL A 80 5261 10988 12463 870 -1018 -4096 C ATOM 457 CG1 VAL A 80 48.893 -15.666 91.272 1.00 74.80 C ANISOU 457 CG1 VAL A 80 5615 10752 12053 786 -887 -3663 C ATOM 458 CG2 VAL A 80 51.350 -15.810 90.807 1.00 75.41 C ANISOU 458 CG2 VAL A 80 4970 10974 12709 778 -754 -4343 C ATOM 459 N THR A 81 49.234 -14.137 94.663 1.00 70.56 N ANISOU 459 N THR A 81 4805 10421 11582 1001 -1558 -3998 N ATOM 460 CA THR A 81 48.200 -13.746 95.633 1.00 69.66 C ANISOU 460 CA THR A 81 4972 10272 11225 1048 -1730 -3774 C ATOM 461 C THR A 81 48.264 -12.246 95.876 1.00 72.95 C ANISOU 461 C THR A 81 5281 10676 11760 809 -1592 -3881 C ATOM 462 O THR A 81 47.242 -11.573 95.755 1.00 72.58 O ANISOU 462 O THR A 81 5493 10530 11555 658 -1448 -3627 O ATOM 463 CB THR A 81 48.374 -14.499 96.975 1.00 77.55 C ANISOU 463 CB THR A 81 6000 11351 12115 1392 -2172 -3848 C ATOM 464 OG1 THR A 81 48.568 -15.889 96.749 1.00 81.41 O ANISOU 464 OG1 THR A 81 6550 11850 12531 1623 -2295 -3812 O ATOM 465 CG2 THR A 81 47.207 -14.313 97.908 1.00 75.28 C ANISOU 465 CG2 THR A 81 6064 11000 11541 1450 -2319 -3585 C ATOM 466 N ASN A 82 49.464 -11.722 96.203 1.00 70.38 N ANISOU 466 N ASN A 82 4566 10450 11724 776 -1633 -4271 N ATOM 467 CA ASN A 82 49.665 -10.303 96.509 1.00 70.51 C ANISOU 467 CA ASN A 82 4449 10460 11882 548 -1510 -4426 C ATOM 468 C ASN A 82 49.396 -9.376 95.318 1.00 75.77 C ANISOU 468 C ASN A 82 5190 10996 12603 196 -1044 -4332 C ATOM 469 O ASN A 82 48.878 -8.281 95.546 1.00 75.50 O ANISOU 469 O ASN A 82 5280 10892 12515 24 -933 -4251 O ATOM 470 CB ASN A 82 51.018 -10.050 97.139 1.00 67.03 C ANISOU 470 CB ASN A 82 3561 10160 11749 601 -1677 -4890 C ATOM 471 CG ASN A 82 51.132 -10.555 98.572 1.00 82.21 C ANISOU 471 CG ASN A 82 5483 12183 13570 931 -2170 -4977 C ATOM 472 OD1 ASN A 82 50.177 -11.096 99.165 1.00 69.17 O ANISOU 472 OD1 ASN A 82 4190 10486 11604 1120 -2374 -4683 O ATOM 473 ND2 ASN A 82 52.316 -10.384 99.175 1.00 72.98 N ANISOU 473 ND2 ASN A 82 3918 11144 12666 1009 -2371 -5402 N ATOM 474 N TYR A 83 49.651 -9.831 94.060 1.00 72.01 N ANISOU 474 N TYR A 83 4694 10468 12197 102 -775 -4316 N ATOM 475 CA TYR A 83 49.326 -9.043 92.864 1.00 71.22 C ANISOU 475 CA TYR A 83 4749 10213 12097 -208 -334 -4197 C ATOM 476 C TYR A 83 47.798 -8.925 92.734 1.00 72.74 C ANISOU 476 C TYR A 83 5399 10285 11954 -212 -320 -3758 C ATOM 477 O TYR A 83 47.284 -7.843 92.427 1.00 72.48 O ANISOU 477 O TYR A 83 5537 10135 11869 -425 -94 -3652 O ATOM 478 CB TYR A 83 49.948 -9.652 91.599 1.00 72.94 C ANISOU 478 CB TYR A 83 4873 10396 12445 -280 -72 -4282 C ATOM 479 CG TYR A 83 51.382 -9.242 91.321 1.00 76.33 C ANISOU 479 CG TYR A 83 4871 10875 13254 -438 131 -4726 C ATOM 480 CD1 TYR A 83 52.056 -9.710 90.196 1.00 78.70 C ANISOU 480 CD1 TYR A 83 5060 11133 13709 -534 419 -4850 C ATOM 481 CD2 TYR A 83 52.063 -8.379 92.174 1.00 77.65 C ANISOU 481 CD2 TYR A 83 4739 11127 13637 -504 49 -5039 C ATOM 482 CE1 TYR A 83 53.366 -9.320 89.922 1.00 79.47 C ANISOU 482 CE1 TYR A 83 4746 11269 14180 -701 643 -5282 C ATOM 483 CE2 TYR A 83 53.379 -7.995 91.918 1.00 78.87 C ANISOU 483 CE2 TYR A 83 4467 11330 14170 -667 248 -5480 C ATOM 484 CZ TYR A 83 54.030 -8.474 90.794 1.00 86.87 C ANISOU 484 CZ TYR A 83 5359 12299 15347 -767 552 -5606 C ATOM 485 OH TYR A 83 55.332 -8.102 90.545 1.00 88.34 O ANISOU 485 OH TYR A 83 5103 12530 15931 -941 775 -6067 O ATOM 486 N PHE A 84 47.067 -10.024 93.024 1.00 66.68 N ANISOU 486 N PHE A 84 4829 9544 10964 30 -571 -3521 N ATOM 487 CA PHE A 84 45.608 -9.998 92.998 1.00 64.72 C ANISOU 487 CA PHE A 84 4971 9199 10420 45 -589 -3138 C ATOM 488 C PHE A 84 45.070 -9.144 94.163 1.00 66.61 C ANISOU 488 C PHE A 84 5282 9446 10580 54 -743 -3096 C ATOM 489 O PHE A 84 44.076 -8.455 93.978 1.00 66.41 O ANISOU 489 O PHE A 84 5506 9316 10411 -56 -624 -2871 O ATOM 490 CB PHE A 84 45.002 -11.409 93.006 1.00 65.81 C ANISOU 490 CB PHE A 84 5288 9354 10361 276 -784 -2926 C ATOM 491 CG PHE A 84 45.019 -12.190 91.713 1.00 66.67 C ANISOU 491 CG PHE A 84 5474 9405 10451 243 -599 -2838 C ATOM 492 CD1 PHE A 84 44.406 -11.690 90.570 1.00 68.87 C ANISOU 492 CD1 PHE A 84 5969 9546 10653 43 -307 -2659 C ATOM 493 CD2 PHE A 84 45.568 -13.468 91.662 1.00 68.24 C ANISOU 493 CD2 PHE A 84 5574 9676 10679 435 -736 -2917 C ATOM 494 CE1 PHE A 84 44.410 -12.421 89.380 1.00 69.37 C ANISOU 494 CE1 PHE A 84 6132 9545 10681 18 -144 -2578 C ATOM 495 CE2 PHE A 84 45.570 -14.199 90.473 1.00 70.07 C ANISOU 495 CE2 PHE A 84 5892 9846 10884 404 -560 -2834 C ATOM 496 CZ PHE A 84 44.993 -13.669 89.340 1.00 68.25 C ANISOU 496 CZ PHE A 84 5869 9480 10582 190 -264 -2666 C ATOM 497 N LEU A 85 45.752 -9.129 95.327 1.00 62.11 N ANISOU 497 N LEU A 85 4494 8994 10111 183 -1000 -3329 N ATOM 498 CA LEU A 85 45.342 -8.283 96.461 1.00 61.78 C ANISOU 498 CA LEU A 85 4515 8955 10002 186 -1140 -3320 C ATOM 499 C LEU A 85 45.481 -6.764 96.156 1.00 65.54 C ANISOU 499 C LEU A 85 4943 9356 10603 -104 -860 -3411 C ATOM 500 O LEU A 85 44.697 -5.958 96.675 1.00 65.58 O ANISOU 500 O LEU A 85 5134 9299 10484 -157 -860 -3269 O ATOM 501 CB LEU A 85 46.048 -8.669 97.784 1.00 61.60 C ANISOU 501 CB LEU A 85 4304 9067 10036 412 -1508 -3556 C ATOM 502 CG LEU A 85 45.713 -10.059 98.388 1.00 65.19 C ANISOU 502 CG LEU A 85 4915 9561 10292 727 -1822 -3429 C ATOM 503 CD1 LEU A 85 46.580 -10.351 99.609 1.00 64.70 C ANISOU 503 CD1 LEU A 85 4675 9615 10292 958 -2187 -3703 C ATOM 504 CD2 LEU A 85 44.233 -10.190 98.751 1.00 65.02 C ANISOU 504 CD2 LEU A 85 5291 9443 9969 771 -1851 -3063 C ATOM 505 N VAL A 86 46.443 -6.392 95.282 1.00 61.40 N ANISOU 505 N VAL A 86 4191 8821 10317 -295 -597 -3642 N ATOM 506 CA VAL A 86 46.674 -5.016 94.814 1.00 60.77 C ANISOU 506 CA VAL A 86 4089 8639 10361 -595 -267 -3745 C ATOM 507 C VAL A 86 45.506 -4.608 93.920 1.00 64.53 C ANISOU 507 C VAL A 86 4955 8942 10622 -713 -29 -3398 C ATOM 508 O VAL A 86 45.034 -3.472 93.994 1.00 64.86 O ANISOU 508 O VAL A 86 5153 8882 10610 -859 106 -3326 O ATOM 509 CB VAL A 86 48.030 -4.875 94.074 1.00 64.26 C ANISOU 509 CB VAL A 86 4201 9100 11115 -769 -19 -4095 C ATOM 510 CG1 VAL A 86 48.190 -3.490 93.442 1.00 63.94 C ANISOU 510 CG1 VAL A 86 4214 8912 11171 -1104 386 -4173 C ATOM 511 CG2 VAL A 86 49.185 -5.152 95.016 1.00 63.98 C ANISOU 511 CG2 VAL A 86 3748 9245 11318 -647 -281 -4477 C ATOM 512 N ASN A 87 45.044 -5.547 93.076 1.00 60.24 N ANISOU 512 N ASN A 87 4574 8362 9953 -635 6 -3192 N ATOM 513 CA ASN A 87 43.915 -5.339 92.179 1.00 59.26 C ANISOU 513 CA ASN A 87 4816 8083 9616 -703 179 -2870 C ATOM 514 C ASN A 87 42.614 -5.203 92.987 1.00 63.17 C ANISOU 514 C ASN A 87 5546 8568 9888 -578 -30 -2607 C ATOM 515 O ASN A 87 41.735 -4.433 92.600 1.00 63.09 O ANISOU 515 O ASN A 87 5790 8428 9752 -673 108 -2418 O ATOM 516 CB ASN A 87 43.835 -6.474 91.180 1.00 57.01 C ANISOU 516 CB ASN A 87 4611 7783 9267 -632 224 -2753 C ATOM 517 CG ASN A 87 42.874 -6.209 90.062 1.00 69.78 C ANISOU 517 CG ASN A 87 6582 9230 10700 -727 432 -2482 C ATOM 518 OD1 ASN A 87 43.045 -5.267 89.296 1.00 67.55 O ANISOU 518 OD1 ASN A 87 6405 8808 10452 -935 732 -2517 O ATOM 519 ND2 ASN A 87 41.851 -7.040 89.938 1.00 53.09 N ANISOU 519 ND2 ASN A 87 4672 7114 8384 -572 274 -2217 N ATOM 520 N LEU A 88 42.507 -5.933 94.120 1.00 58.99 N ANISOU 520 N LEU A 88 4940 8164 9311 -362 -357 -2611 N ATOM 521 CA LEU A 88 41.357 -5.855 95.017 1.00 58.45 C ANISOU 521 CA LEU A 88 5074 8087 9049 -245 -545 -2400 C ATOM 522 C LEU A 88 41.329 -4.456 95.684 1.00 65.24 C ANISOU 522 C LEU A 88 5929 8906 9952 -371 -490 -2481 C ATOM 523 O LEU A 88 40.263 -3.858 95.791 1.00 64.70 O ANISOU 523 O LEU A 88 6090 8750 9742 -394 -455 -2277 O ATOM 524 CB LEU A 88 41.372 -7.027 96.032 1.00 57.68 C ANISOU 524 CB LEU A 88 4929 8107 8881 10 -877 -2408 C ATOM 525 CG LEU A 88 40.402 -7.008 97.241 1.00 60.78 C ANISOU 525 CG LEU A 88 5503 8497 9092 141 -1084 -2255 C ATOM 526 CD1 LEU A 88 38.944 -6.848 96.827 1.00 59.81 C ANISOU 526 CD1 LEU A 88 5667 8266 8791 107 -984 -1946 C ATOM 527 CD2 LEU A 88 40.572 -8.246 98.083 1.00 61.95 C ANISOU 527 CD2 LEU A 88 5642 8733 9163 387 -1373 -2283 C ATOM 528 N SER A 89 42.507 -3.918 96.047 1.00 64.37 N ANISOU 528 N SER A 89 5551 8853 10052 -462 -464 -2791 N ATOM 529 CA SER A 89 42.698 -2.574 96.616 1.00 64.82 C ANISOU 529 CA SER A 89 5572 8872 10184 -611 -385 -2920 C ATOM 530 C SER A 89 42.396 -1.407 95.651 1.00 70.37 C ANISOU 530 C SER A 89 6448 9404 10887 -854 -22 -2842 C ATOM 531 O SER A 89 42.004 -0.335 96.105 1.00 70.70 O ANISOU 531 O SER A 89 6603 9366 10895 -954 56 -2818 O ATOM 532 CB SER A 89 44.127 -2.415 97.133 1.00 66.95 C ANISOU 532 CB SER A 89 5476 9255 10705 -649 -452 -3310 C ATOM 533 OG SER A 89 44.375 -3.306 98.206 1.00 74.49 O ANISOU 533 OG SER A 89 6316 10351 11636 -400 -820 -3388 O ATOM 534 N LEU A 90 42.609 -1.613 94.330 1.00 66.85 N ANISOU 534 N LEU A 90 6045 8889 10467 -943 204 -2810 N ATOM 535 CA LEU A 90 42.339 -0.627 93.279 1.00 66.15 C ANISOU 535 CA LEU A 90 6177 8611 10346 -1154 555 -2731 C ATOM 536 C LEU A 90 40.830 -0.534 92.987 1.00 69.58 C ANISOU 536 C LEU A 90 6975 8938 10525 -1075 522 -2380 C ATOM 537 O LEU A 90 40.306 0.548 92.744 1.00 69.28 O ANISOU 537 O LEU A 90 7143 8758 10424 -1192 689 -2309 O ATOM 538 CB LEU A 90 43.058 -1.050 91.986 1.00 65.96 C ANISOU 538 CB LEU A 90 6108 8548 10404 -1238 772 -2800 C ATOM 539 CG LEU A 90 44.595 -1.067 91.975 1.00 70.15 C ANISOU 539 CG LEU A 90 6584 8959 11112 -1520 1161 -3034 C ATOM 540 CD1 LEU A 90 45.163 -1.648 90.672 1.00 69.70 C ANISOU 540 CD1 LEU A 90 6163 9003 11316 -1623 1149 -3401 C ATOM 541 CD2 LEU A 90 45.140 0.339 92.205 1.00 71.37 C ANISOU 541 CD2 LEU A 90 6707 9081 11330 -1569 1353 -3086 C ATOM 542 N ALA A 91 40.131 -1.679 93.103 1.00 66.01 N ANISOU 542 N ALA A 91 6594 8553 9934 -871 299 -2179 N ATOM 543 CA ALA A 91 38.679 -1.797 92.980 1.00 65.05 C ANISOU 543 CA ALA A 91 6756 8362 9598 -769 222 -1877 C ATOM 544 C ALA A 91 38.121 -1.064 94.209 1.00 69.58 C ANISOU 544 C ALA A 91 7356 8951 10130 -726 90 -1852 C ATOM 545 O ALA A 91 37.159 -0.311 94.080 1.00 70.23 O ANISOU 545 O ALA A 91 7665 8921 10097 -741 150 -1685 O ATOM 546 CB ALA A 91 38.181 -3.232 92.961 1.00 65.33 C ANISOU 546 CB ALA A 91 6801 8484 9537 -579 19 -1733 C ATOM 547 N ASP A 92 38.756 -1.264 95.390 1.00 65.58 N ANISOU 547 N ASP A 92 6626 8575 9715 -665 -93 -2030 N ATOM 548 CA ASP A 92 38.393 -0.650 96.673 1.00 64.92 C ANISOU 548 CA ASP A 92 6556 8514 9597 -620 -231 -2042 C ATOM 549 C ASP A 92 38.595 0.866 96.637 1.00 67.51 C ANISOU 549 C ASP A 92 6936 8730 9985 -812 -22 -2131 C ATOM 550 O ASP A 92 37.769 1.593 97.171 1.00 67.64 O ANISOU 550 O ASP A 92 7114 8681 9904 -798 -37 -2015 O ATOM 551 CB ASP A 92 39.196 -1.273 97.836 1.00 66.88 C ANISOU 551 CB ASP A 92 6569 8917 9924 -503 -483 -2244 C ATOM 552 CG ASP A 92 38.828 -2.693 98.280 1.00 77.65 C ANISOU 552 CG ASP A 92 7950 10373 11179 -276 -733 -2138 C ATOM 553 OD1 ASP A 92 37.798 -3.242 97.777 1.00 75.51 O ANISOU 553 OD1 ASP A 92 7867 10055 10768 -211 -720 -1893 O ATOM 554 OD2 ASP A 92 39.578 -3.267 99.122 1.00 85.05 O ANISOU 554 OD2 ASP A 92 8721 11424 12168 -158 -947 -2312 O ATOM 555 N VAL A 93 39.670 1.338 95.990 1.00 63.38 N ANISOU 555 N VAL A 93 6286 8172 9622 -998 194 -2341 N ATOM 556 CA VAL A 93 39.973 2.764 95.830 1.00 62.91 C ANISOU 556 CA VAL A 93 6292 7984 9629 -1213 445 -2450 C ATOM 557 C VAL A 93 38.972 3.405 94.853 1.00 66.62 C ANISOU 557 C VAL A 93 7118 8258 9938 -1263 649 -2203 C ATOM 558 O VAL A 93 38.551 4.534 95.080 1.00 65.99 O ANISOU 558 O VAL A 93 7207 8062 9806 -1336 750 -2163 O ATOM 559 CB VAL A 93 41.469 3.000 95.477 1.00 66.79 C ANISOU 559 CB VAL A 93 6520 8495 10360 -1408 630 -2783 C ATOM 560 CG1 VAL A 93 41.722 4.399 94.916 1.00 66.63 C ANISOU 560 CG1 VAL A 93 6642 8289 10387 -1668 983 -2866 C ATOM 561 CG2 VAL A 93 42.345 2.759 96.699 1.00 66.58 C ANISOU 561 CG2 VAL A 93 6161 8647 10491 -1351 392 -3054 C ATOM 562 N LEU A 94 38.558 2.668 93.797 1.00 63.66 N ANISOU 562 N LEU A 94 6870 7845 9474 -1205 688 -2038 N ATOM 563 CA LEU A 94 37.551 3.129 92.828 1.00 63.21 C ANISOU 563 CA LEU A 94 7165 7607 9244 -1206 825 -1801 C ATOM 564 C LEU A 94 36.207 3.402 93.569 1.00 65.00 C ANISOU 564 C LEU A 94 7543 7826 9326 -1051 641 -1594 C ATOM 565 O LEU A 94 35.634 4.476 93.423 1.00 64.89 O ANISOU 565 O LEU A 94 7762 7663 9232 -1093 758 -1510 O ATOM 566 CB LEU A 94 37.380 2.092 91.676 1.00 63.07 C ANISOU 566 CB LEU A 94 7225 7580 9158 -1143 840 -1680 C ATOM 567 CG LEU A 94 36.203 2.285 90.686 1.00 67.68 C ANISOU 567 CG LEU A 94 8170 8005 9541 -1078 887 -1418 C ATOM 568 CD1 LEU A 94 36.330 3.595 89.890 1.00 68.24 C ANISOU 568 CD1 LEU A 94 8522 7842 9561 -1242 1188 -1431 C ATOM 569 CD2 LEU A 94 36.065 1.096 89.739 1.00 67.79 C ANISOU 569 CD2 LEU A 94 8220 8041 9495 -1001 850 -1321 C ATOM 570 N ALA A 95 35.755 2.439 94.392 1.00 59.58 N ANISOU 570 N ALA A 95 6730 7293 8614 -876 370 -1530 N ATOM 571 CA ALA A 95 34.543 2.528 95.195 1.00 57.78 C ANISOU 571 CA ALA A 95 6603 7075 8275 -732 203 -1364 C ATOM 572 C ALA A 95 34.644 3.617 96.289 1.00 60.06 C ANISOU 572 C ALA A 95 6875 7345 8600 -788 208 -1463 C ATOM 573 O ALA A 95 33.690 4.365 96.485 1.00 58.19 O ANISOU 573 O ALA A 95 6820 7015 8274 -750 223 -1334 O ATOM 574 CB ALA A 95 34.254 1.181 95.825 1.00 57.91 C ANISOU 574 CB ALA A 95 6494 7244 8265 -563 -44 -1312 C ATOM 575 N THR A 96 35.793 3.707 96.990 1.00 57.28 N ANISOU 575 N THR A 96 6302 7079 8382 -870 188 -1702 N ATOM 576 CA THR A 96 35.990 4.669 98.083 1.00 57.81 C ANISOU 576 CA THR A 96 6339 7138 8488 -926 174 -1823 C ATOM 577 C THR A 96 36.076 6.120 97.577 1.00 63.86 C ANISOU 577 C THR A 96 7272 7726 9265 -1108 445 -1856 C ATOM 578 O THR A 96 35.449 6.999 98.179 1.00 64.69 O ANISOU 578 O THR A 96 7517 7756 9306 -1100 453 -1798 O ATOM 579 CB THR A 96 37.177 4.249 98.966 1.00 61.64 C ANISOU 579 CB THR A 96 6533 7777 9112 -936 31 -2084 C ATOM 580 OG1 THR A 96 36.879 2.940 99.464 1.00 65.98 O ANISOU 580 OG1 THR A 96 7014 8455 9600 -736 -222 -2010 O ATOM 581 CG2 THR A 96 37.426 5.204 100.158 1.00 54.41 C ANISOU 581 CG2 THR A 96 5583 6860 8231 -988 -15 -2229 C ATOM 582 N ALA A 97 36.816 6.367 96.484 1.00 60.08 N ANISOU 582 N ALA A 97 6807 7164 8857 -1269 681 -1948 N ATOM 583 CA ALA A 97 36.978 7.714 95.958 1.00 60.80 C ANISOU 583 CA ALA A 97 7094 7060 8948 -1456 971 -1994 C ATOM 584 C ALA A 97 35.728 8.316 95.311 1.00 65.83 C ANISOU 584 C ALA A 97 8101 7514 9397 -1385 1051 -1734 C ATOM 585 O ALA A 97 35.382 9.461 95.612 1.00 65.43 O ANISOU 585 O ALA A 97 8225 7337 9298 -1434 1148 -1718 O ATOM 586 CB ALA A 97 38.156 7.773 94.985 1.00 61.61 C ANISOU 586 CB ALA A 97 7124 7108 9179 -1661 1230 -2184 C ATOM 587 N ILE A 98 35.066 7.560 94.421 1.00 62.77 N ANISOU 587 N ILE A 98 7834 7111 8905 -1263 1003 -1544 N ATOM 588 CA ILE A 98 33.961 8.067 93.608 1.00 62.21 C ANISOU 588 CA ILE A 98 8112 6862 8661 -1181 1065 -1322 C ATOM 589 C ILE A 98 32.594 7.749 94.150 1.00 63.89 C ANISOU 589 C ILE A 98 8368 7133 8776 -956 822 -1124 C ATOM 590 O ILE A 98 31.728 8.612 94.139 1.00 64.79 O ANISOU 590 O ILE A 98 8710 7114 8793 -895 849 -1010 O ATOM 591 CB ILE A 98 34.107 7.566 92.129 1.00 65.73 C ANISOU 591 CB ILE A 98 8707 7222 9047 -1201 1187 -1257 C ATOM 592 CG1 ILE A 98 35.562 7.717 91.573 1.00 65.92 C ANISOU 592 CG1 ILE A 98 8646 7202 9198 -1441 1456 -1483 C ATOM 593 CG2 ILE A 98 33.077 8.208 91.187 1.00 67.39 C ANISOU 593 CG2 ILE A 98 9322 7216 9066 -1119 1258 -1057 C ATOM 594 CD1 ILE A 98 36.242 9.195 91.662 1.00 70.22 C ANISOU 594 CD1 ILE A 98 9319 7568 9794 -1675 1761 -1651 C ATOM 595 N CYS A 99 32.379 6.513 94.571 1.00 58.43 N ANISOU 595 N CYS A 99 7470 6622 8109 -831 600 -1087 N ATOM 596 CA CYS A 99 31.075 6.016 94.987 1.00 56.74 C ANISOU 596 CA CYS A 99 7278 6464 7816 -632 393 -912 C ATOM 597 C CYS A 99 30.741 6.249 96.457 1.00 56.33 C ANISOU 597 C CYS A 99 7126 6487 7790 -579 273 -942 C ATOM 598 O CYS A 99 29.570 6.466 96.753 1.00 55.32 O ANISOU 598 O CYS A 99 7100 6324 7597 -456 200 -811 O ATOM 599 CB CYS A 99 30.932 4.544 94.607 1.00 57.23 C ANISOU 599 CB CYS A 99 7221 6650 7871 -534 247 -848 C ATOM 600 SG CYS A 99 31.608 4.133 92.972 1.00 61.07 S ANISOU 600 SG CYS A 99 7799 7065 8341 -618 399 -853 S ATOM 601 N LEU A 100 31.724 6.179 97.377 1.00 51.13 N ANISOU 601 N LEU A 100 6272 5929 7227 -660 243 -1121 N ATOM 602 CA LEU A 100 31.445 6.375 98.807 1.00 50.30 C ANISOU 602 CA LEU A 100 6105 5884 7124 -606 123 -1156 C ATOM 603 C LEU A 100 30.816 7.763 99.103 1.00 57.68 C ANISOU 603 C LEU A 100 7232 6670 8012 -629 232 -1113 C ATOM 604 O LEU A 100 29.828 7.788 99.849 1.00 58.36 O ANISOU 604 O LEU A 100 7366 6762 8046 -509 137 -1015 O ATOM 605 CB LEU A 100 32.668 6.086 99.705 1.00 49.07 C ANISOU 605 CB LEU A 100 5724 5852 7068 -675 47 -1377 C ATOM 606 CG LEU A 100 32.454 6.232 101.214 1.00 52.05 C ANISOU 606 CG LEU A 100 6068 6284 7424 -610 -96 -1424 C ATOM 607 CD1 LEU A 100 33.260 5.237 101.987 1.00 50.98 C ANISOU 607 CD1 LEU A 100 5731 6305 7335 -562 -285 -1568 C ATOM 608 CD2 LEU A 100 32.804 7.649 101.697 1.00 55.06 C ANISOU 608 CD2 LEU A 100 6513 6569 7838 -741 29 -1541 C ATOM 609 N PRO A 101 31.343 8.915 98.577 1.00 54.64 N ANISOU 609 N PRO A 101 6972 6144 7646 -781 443 -1189 N ATOM 610 CA PRO A 101 30.695 10.221 98.884 1.00 53.29 C ANISOU 610 CA PRO A 101 7011 5821 7416 -783 542 -1140 C ATOM 611 C PRO A 101 29.252 10.290 98.386 1.00 56.21 C ANISOU 611 C PRO A 101 7571 6106 7680 -608 499 -921 C ATOM 612 O PRO A 101 28.375 10.703 99.132 1.00 54.97 O ANISOU 612 O PRO A 101 7469 5926 7492 -510 443 -858 O ATOM 613 CB PRO A 101 31.577 11.243 98.165 1.00 54.85 C ANISOU 613 CB PRO A 101 7334 5866 7639 -984 798 -1255 C ATOM 614 CG PRO A 101 32.843 10.528 97.827 1.00 59.46 C ANISOU 614 CG PRO A 101 7696 6557 8338 -1111 824 -1425 C ATOM 615 CD PRO A 101 32.505 9.091 97.673 1.00 55.33 C ANISOU 615 CD PRO A 101 7035 6185 7802 -960 625 -1326 C ATOM 616 N ALA A 102 29.006 9.805 97.147 1.00 53.93 N ANISOU 616 N ALA A 102 7364 5782 7345 -559 508 -821 N ATOM 617 CA ALA A 102 27.700 9.738 96.472 1.00 52.96 C ANISOU 617 CA ALA A 102 7399 5590 7132 -380 435 -637 C ATOM 618 C ALA A 102 26.669 8.945 97.275 1.00 55.14 C ANISOU 618 C ALA A 102 7527 5997 7425 -219 235 -559 C ATOM 619 O ALA A 102 25.527 9.391 97.383 1.00 55.68 O ANISOU 619 O ALA A 102 7696 6001 7460 -88 194 -466 O ATOM 620 CB ALA A 102 27.859 9.134 95.081 1.00 53.16 C ANISOU 620 CB ALA A 102 7499 5586 7112 -374 454 -579 C ATOM 621 N SER A 103 27.080 7.789 97.854 1.00 48.60 N ANISOU 621 N SER A 103 6473 5342 6652 -228 123 -611 N ATOM 622 CA SER A 103 26.238 6.941 98.688 1.00 47.64 C ANISOU 622 CA SER A 103 6229 5332 6540 -104 -33 -557 C ATOM 623 C SER A 103 25.887 7.636 99.972 1.00 51.24 C ANISOU 623 C SER A 103 6698 5767 7003 -91 -24 -591 C ATOM 624 O SER A 103 24.728 7.596 100.368 1.00 52.03 O ANISOU 624 O SER A 103 6818 5857 7095 27 -73 -511 O ATOM 625 CB SER A 103 26.917 5.612 98.993 1.00 50.57 C ANISOU 625 CB SER A 103 6410 5861 6942 -121 -136 -614 C ATOM 626 OG SER A 103 26.675 4.682 97.956 1.00 56.08 O ANISOU 626 OG SER A 103 7094 6592 7623 -68 -187 -533 O ATOM 627 N LEU A 104 26.877 8.283 100.619 1.00 46.88 N ANISOU 627 N LEU A 104 6134 5205 6475 -218 45 -724 N ATOM 628 CA LEU A 104 26.697 9.042 101.845 1.00 46.68 C ANISOU 628 CA LEU A 104 6145 5146 6446 -226 64 -775 C ATOM 629 C LEU A 104 25.596 10.112 101.737 1.00 52.77 C ANISOU 629 C LEU A 104 7102 5765 7182 -154 150 -679 C ATOM 630 O LEU A 104 24.738 10.187 102.617 1.00 52.84 O ANISOU 630 O LEU A 104 7128 5764 7185 -65 122 -641 O ATOM 631 CB LEU A 104 28.054 9.647 102.288 1.00 46.78 C ANISOU 631 CB LEU A 104 6117 5159 6498 -393 130 -956 C ATOM 632 CG LEU A 104 28.037 10.792 103.344 1.00 51.16 C ANISOU 632 CG LEU A 104 6759 5636 7042 -442 192 -1030 C ATOM 633 CD1 LEU A 104 27.565 10.308 104.734 1.00 50.82 C ANISOU 633 CD1 LEU A 104 6671 5669 6970 -350 63 -1032 C ATOM 634 CD2 LEU A 104 29.383 11.457 103.433 1.00 53.54 C ANISOU 634 CD2 LEU A 104 7018 5922 7401 -629 280 -1222 C ATOM 635 N LEU A 105 25.608 10.912 100.644 1.00 49.92 N ANISOU 635 N LEU A 105 6897 5277 6793 -182 259 -643 N ATOM 636 CA LEU A 105 24.607 11.936 100.395 1.00 50.32 C ANISOU 636 CA LEU A 105 7156 5166 6797 -89 324 -556 C ATOM 637 C LEU A 105 23.191 11.438 100.039 1.00 52.57 C ANISOU 637 C LEU A 105 7418 5473 7082 114 202 -431 C ATOM 638 O LEU A 105 22.218 12.101 100.392 1.00 53.08 O ANISOU 638 O LEU A 105 7554 5465 7148 215 212 -398 O ATOM 639 CB LEU A 105 25.045 12.890 99.278 1.00 51.61 C ANISOU 639 CB LEU A 105 7540 5168 6903 -158 468 -549 C ATOM 640 CG LEU A 105 26.278 13.792 99.526 1.00 58.09 C ANISOU 640 CG LEU A 105 8526 5842 7705 -308 660 -647 C ATOM 641 CD1 LEU A 105 26.629 14.543 98.259 1.00 59.45 C ANISOU 641 CD1 LEU A 105 9023 5790 7776 -260 781 -568 C ATOM 642 CD2 LEU A 105 26.042 14.860 100.646 1.00 60.31 C ANISOU 642 CD2 LEU A 105 8788 6119 8006 -290 656 -686 C ATOM 643 N VAL A 106 23.083 10.261 99.362 1.00 47.47 N ANISOU 643 N VAL A 106 6666 4925 6447 171 92 -377 N ATOM 644 CA VAL A 106 21.802 9.612 99.033 1.00 46.44 C ANISOU 644 CA VAL A 106 6471 4833 6341 345 -32 -289 C ATOM 645 C VAL A 106 21.298 9.103 100.412 1.00 51.45 C ANISOU 645 C VAL A 106 6947 5568 7036 368 -71 -320 C ATOM 646 O VAL A 106 20.142 9.312 100.758 1.00 50.11 O ANISOU 646 O VAL A 106 6763 5370 6905 487 -90 -290 O ATOM 647 CB VAL A 106 21.825 8.470 97.985 1.00 50.18 C ANISOU 647 CB VAL A 106 6877 5382 6807 374 -129 -240 C ATOM 648 CG1 VAL A 106 20.426 7.889 97.774 1.00 49.34 C ANISOU 648 CG1 VAL A 106 6688 5314 6743 544 -258 -176 C ATOM 649 CG2 VAL A 106 22.432 8.932 96.652 1.00 50.00 C ANISOU 649 CG2 VAL A 106 7049 5244 6706 335 -65 -217 C ATOM 650 N ASP A 107 22.195 8.501 101.217 1.00 49.52 N ANISOU 650 N ASP A 107 6600 5424 6794 257 -75 -392 N ATOM 651 CA ASP A 107 21.872 8.008 102.551 1.00 50.50 C ANISOU 651 CA ASP A 107 6635 5616 6937 270 -100 -426 C ATOM 652 C ASP A 107 21.419 9.149 103.505 1.00 57.59 C ANISOU 652 C ASP A 107 7631 6416 7835 284 -11 -452 C ATOM 653 O ASP A 107 20.686 8.878 104.463 1.00 57.54 O ANISOU 653 O ASP A 107 7590 6426 7849 335 -7 -455 O ATOM 654 CB ASP A 107 23.025 7.150 103.135 1.00 52.30 C ANISOU 654 CB ASP A 107 6773 5956 7143 174 -152 -505 C ATOM 655 CG ASP A 107 23.131 5.687 102.628 1.00 62.58 C ANISOU 655 CG ASP A 107 7960 7372 8448 198 -252 -474 C ATOM 656 OD1 ASP A 107 22.242 5.248 101.830 1.00 61.39 O ANISOU 656 OD1 ASP A 107 7784 7221 8319 280 -284 -390 O ATOM 657 OD2 ASP A 107 24.086 4.978 103.045 1.00 65.05 O ANISOU 657 OD2 ASP A 107 8207 7770 8740 145 -309 -543 O ATOM 658 N ILE A 108 21.790 10.420 103.193 1.00 56.26 N ANISOU 658 N ILE A 108 7605 6129 7643 239 80 -470 N ATOM 659 CA ILE A 108 21.390 11.618 103.955 1.00 56.73 C ANISOU 659 CA ILE A 108 7784 6075 7695 254 175 -493 C ATOM 660 C ILE A 108 20.088 12.241 103.380 1.00 60.82 C ANISOU 660 C ILE A 108 8380 6489 8239 416 188 -412 C ATOM 661 O ILE A 108 19.085 12.337 104.097 1.00 60.48 O ANISOU 661 O ILE A 108 8306 6432 8243 508 203 -407 O ATOM 662 CB ILE A 108 22.526 12.692 104.077 1.00 59.44 C ANISOU 662 CB ILE A 108 8253 6334 7998 107 280 -578 C ATOM 663 CG1 ILE A 108 23.763 12.167 104.827 1.00 59.31 C ANISOU 663 CG1 ILE A 108 8133 6425 7977 -33 242 -697 C ATOM 664 CG2 ILE A 108 22.006 13.983 104.738 1.00 59.41 C ANISOU 664 CG2 ILE A 108 8404 6190 7978 135 387 -587 C ATOM 665 CD1 ILE A 108 25.039 13.056 104.619 1.00 60.83 C ANISOU 665 CD1 ILE A 108 8392 6557 8165 -206 341 -812 C ATOM 666 N THR A 109 20.133 12.700 102.113 1.00 56.83 N ANISOU 666 N THR A 109 7991 5901 7702 454 187 -362 N ATOM 667 CA THR A 109 19.026 13.405 101.448 1.00 56.36 C ANISOU 667 CA THR A 109 8045 5722 7646 631 171 -298 C ATOM 668 C THR A 109 17.906 12.496 100.941 1.00 60.36 C ANISOU 668 C THR A 109 8403 6305 8224 793 32 -250 C ATOM 669 O THR A 109 16.765 12.949 100.866 1.00 60.69 O ANISOU 669 O THR A 109 8459 6283 8315 961 0 -235 O ATOM 670 CB THR A 109 19.550 14.276 100.296 1.00 60.52 C ANISOU 670 CB THR A 109 8818 6100 8079 615 228 -268 C ATOM 671 OG1 THR A 109 20.136 13.441 99.297 1.00 58.65 O ANISOU 671 OG1 THR A 109 8548 5925 7813 566 170 -244 O ATOM 672 CG2 THR A 109 20.549 15.330 100.751 1.00 59.06 C ANISOU 672 CG2 THR A 109 8792 5811 7838 450 394 -335 C ATOM 673 N GLU A 110 18.236 11.243 100.554 1.00 56.19 N ANISOU 673 N GLU A 110 7732 5909 7708 747 -53 -238 N ATOM 674 CA GLU A 110 17.328 10.243 99.956 1.00 55.50 C ANISOU 674 CA GLU A 110 7496 5904 7686 868 -188 -206 C ATOM 675 C GLU A 110 16.874 10.729 98.558 1.00 58.91 C ANISOU 675 C GLU A 110 8074 6234 8075 1012 -275 -151 C ATOM 676 O GLU A 110 15.757 10.463 98.117 1.00 58.96 O ANISOU 676 O GLU A 110 7999 6256 8149 1176 -397 -143 O ATOM 677 CB GLU A 110 16.158 9.906 100.908 1.00 56.79 C ANISOU 677 CB GLU A 110 7491 6117 7970 949 -189 -244 C ATOM 678 CG GLU A 110 16.571 9.226 102.195 1.00 69.50 C ANISOU 678 CG GLU A 110 8900 7872 9634 892 -224 -264 C ATOM 679 CD GLU A 110 17.332 7.915 102.114 1.00 91.30 C ANISOU 679 CD GLU A 110 11654 10711 12326 725 -184 -281 C ATOM 680 OE1 GLU A 110 16.990 7.075 101.248 1.00 95.03 O ANISOU 680 OE1 GLU A 110 12170 11163 12773 653 -94 -324 O ATOM 681 OE2 GLU A 110 18.286 7.739 102.905 1.00 72.33 O ANISOU 681 OE2 GLU A 110 9203 8386 9891 678 -255 -260 O ATOM 682 N SER A 111 17.772 11.461 97.878 1.00 54.97 N ANISOU 682 N SER A 111 7806 5621 7460 947 -207 -127 N ATOM 683 CA SER A 111 17.602 12.065 96.554 1.00 54.78 C ANISOU 683 CA SER A 111 8023 5453 7338 1061 -254 -72 C ATOM 684 C SER A 111 18.970 12.104 95.848 1.00 57.24 C ANISOU 684 C SER A 111 8500 5712 7536 890 -151 -63 C ATOM 685 O SER A 111 20.000 11.820 96.464 1.00 56.09 O ANISOU 685 O SER A 111 8260 5643 7409 696 -49 -116 O ATOM 686 CB SER A 111 17.026 13.475 96.662 1.00 58.91 C ANISOU 686 CB SER A 111 8756 5800 7829 1191 -209 -67 C ATOM 687 OG SER A 111 17.961 14.395 97.205 1.00 67.87 O ANISOU 687 OG SER A 111 10047 6840 8903 1032 -19 -95 O ATOM 688 N TRP A 112 18.980 12.482 94.573 1.00 53.95 N ANISOU 688 N TRP A 112 8339 5156 7004 967 -173 -9 N ATOM 689 CA TRP A 112 20.205 12.517 93.782 1.00 53.76 C ANISOU 689 CA TRP A 112 8494 5057 6874 805 -46 -8 C ATOM 690 C TRP A 112 20.574 13.950 93.459 1.00 60.36 C ANISOU 690 C TRP A 112 9692 5654 7588 781 121 -5 C ATOM 691 O TRP A 112 19.752 14.681 92.914 1.00 61.63 O ANISOU 691 O TRP A 112 10090 5659 7667 979 55 49 O ATOM 692 CB TRP A 112 20.048 11.639 92.527 1.00 51.15 C ANISOU 692 CB TRP A 112 8205 4745 6485 882 -174 48 C ATOM 693 CG TRP A 112 21.307 11.464 91.752 1.00 51.03 C ANISOU 693 CG TRP A 112 8331 4676 6383 702 -31 38 C ATOM 694 CD1 TRP A 112 21.623 12.051 90.566 1.00 53.61 C ANISOU 694 CD1 TRP A 112 9025 4796 6550 710 56 76 C ATOM 695 CD2 TRP A 112 22.396 10.589 92.074 1.00 50.77 C ANISOU 695 CD2 TRP A 112 8079 4791 6420 496 47 -26 C ATOM 696 NE1 TRP A 112 22.852 11.612 90.134 1.00 53.32 N ANISOU 696 NE1 TRP A 112 8996 4769 6493 502 209 35 N ATOM 697 CE2 TRP A 112 23.350 10.711 91.039 1.00 54.40 C ANISOU 697 CE2 TRP A 112 8759 5131 6779 375 194 -33 C ATOM 698 CE3 TRP A 112 22.641 9.672 93.116 1.00 51.68 C ANISOU 698 CE3 TRP A 112 7849 5120 6666 415 0 -81 C ATOM 699 CZ2 TRP A 112 24.554 9.996 91.041 1.00 53.36 C ANISOU 699 CZ2 TRP A 112 8473 5099 6700 175 298 -108 C ATOM 700 CZ3 TRP A 112 23.830 8.958 93.113 1.00 52.71 C ANISOU 700 CZ3 TRP A 112 7852 5346 6831 238 76 -147 C ATOM 701 CH2 TRP A 112 24.769 9.121 92.084 1.00 53.47 C ANISOU 701 CH2 TRP A 112 8131 5334 6852 121 221 -166 C ATOM 702 N LEU A 113 21.803 14.362 93.816 1.00 58.53 N ANISOU 702 N LEU A 113 9505 5386 7348 544 334 -77 N ATOM 703 CA LEU A 113 22.255 15.745 93.643 1.00 59.56 C ANISOU 703 CA LEU A 113 9975 5281 7374 474 539 -96 C ATOM 704 C LEU A 113 23.431 15.952 92.647 1.00 66.09 C ANISOU 704 C LEU A 113 11048 5966 8096 288 745 -125 C ATOM 705 O LEU A 113 24.000 17.049 92.604 1.00 66.64 O ANISOU 705 O LEU A 113 11383 5843 8094 168 966 -169 O ATOM 706 CB LEU A 113 22.614 16.339 95.029 1.00 59.79 C ANISOU 706 CB LEU A 113 9878 5348 7491 342 652 -187 C ATOM 707 CG LEU A 113 21.556 16.253 96.152 1.00 64.89 C ANISOU 707 CG LEU A 113 10308 6110 8239 489 510 -176 C ATOM 708 CD1 LEU A 113 22.179 16.532 97.506 1.00 65.12 C ANISOU 708 CD1 LEU A 113 10183 6210 8348 316 615 -280 C ATOM 709 CD2 LEU A 113 20.386 17.206 95.910 1.00 67.15 C ANISOU 709 CD2 LEU A 113 10824 6227 8462 728 458 -108 C ATOM 710 N PHE A 114 23.763 14.932 91.833 1.00 63.32 N ANISOU 710 N PHE A 114 10628 5693 7735 261 691 -106 N ATOM 711 CA PHE A 114 24.894 14.949 90.895 1.00 63.15 C ANISOU 711 CA PHE A 114 10800 5558 7637 72 900 -147 C ATOM 712 C PHE A 114 24.478 14.926 89.418 1.00 67.91 C ANISOU 712 C PHE A 114 11761 5985 8058 217 859 -42 C ATOM 713 O PHE A 114 25.328 14.721 88.539 1.00 67.38 O ANISOU 713 O PHE A 114 11852 5828 7921 75 1021 -66 O ATOM 714 CB PHE A 114 25.859 13.778 91.194 1.00 65.05 C ANISOU 714 CB PHE A 114 10673 6024 8017 -111 909 -239 C ATOM 715 CG PHE A 114 26.212 13.578 92.647 1.00 66.93 C ANISOU 715 CG PHE A 114 10551 6457 8421 -212 883 -342 C ATOM 716 CD1 PHE A 114 27.247 14.296 93.234 1.00 70.21 C ANISOU 716 CD1 PHE A 114 10953 6831 8894 -435 1094 -484 C ATOM 717 CD2 PHE A 114 25.515 12.663 93.428 1.00 70.24 C ANISOU 717 CD2 PHE A 114 10662 7092 8934 -87 653 -309 C ATOM 718 CE1 PHE A 114 27.563 14.126 94.585 1.00 71.44 C ANISOU 718 CE1 PHE A 114 10803 7157 9183 -509 1043 -586 C ATOM 719 CE2 PHE A 114 25.827 12.493 94.783 1.00 73.61 C ANISOU 719 CE2 PHE A 114 10815 7672 9482 -166 628 -400 C ATOM 720 CZ PHE A 114 26.857 13.219 95.349 1.00 71.64 C ANISOU 720 CZ PHE A 114 10564 7382 9275 -368 807 -537 C ATOM 721 N GLY A 115 23.188 15.113 89.154 1.00 65.46 N ANISOU 721 N GLY A 115 11573 5624 7676 501 639 61 N ATOM 722 CA GLY A 115 22.668 15.134 87.788 1.00 66.11 C ANISOU 722 CA GLY A 115 12019 5532 7569 687 545 158 C ATOM 723 C GLY A 115 22.534 13.800 87.079 1.00 72.57 C ANISOU 723 C GLY A 115 12686 6491 8396 739 372 195 C ATOM 724 O GLY A 115 22.980 12.764 87.582 1.00 72.49 O ANISOU 724 O GLY A 115 12289 6714 8538 608 351 145 O ATOM 725 N HIS A 116 21.910 13.839 85.883 1.00 71.30 N ANISOU 725 N HIS A 116 12865 6171 8055 944 240 280 N ATOM 726 CA HIS A 116 21.590 12.712 84.999 1.00 72.14 C ANISOU 726 CA HIS A 116 12930 6356 8121 1045 45 326 C ATOM 727 C HIS A 116 22.763 11.831 84.575 1.00 73.00 C ANISOU 727 C HIS A 116 12959 6532 8247 801 216 289 C ATOM 728 O HIS A 116 22.610 10.610 84.554 1.00 74.09 O ANISOU 728 O HIS A 116 12794 6877 8479 812 59 290 O ATOM 729 CB HIS A 116 20.859 13.210 83.750 1.00 74.68 C ANISOU 729 CB HIS A 116 13747 6428 8201 1303 -91 410 C ATOM 730 CG HIS A 116 19.496 13.757 84.025 1.00 80.17 C ANISOU 730 CG HIS A 116 14453 7103 8905 1613 -356 436 C ATOM 731 ND1 HIS A 116 19.316 15.063 84.467 1.00 83.39 N ANISOU 731 ND1 HIS A 116 15076 7342 9266 1670 -257 434 N ATOM 732 CD2 HIS A 116 18.282 13.175 83.872 1.00 83.34 C ANISOU 732 CD2 HIS A 116 14677 7625 9364 1877 -705 449 C ATOM 733 CE1 HIS A 116 18.006 15.220 84.597 1.00 83.43 C ANISOU 733 CE1 HIS A 116 15013 7378 9308 1976 -552 446 C ATOM 734 NE2 HIS A 116 17.341 14.109 84.257 1.00 83.63 N ANISOU 734 NE2 HIS A 116 14788 7581 9408 2106 -828 446 N ATOM 735 N ALA A 117 23.900 12.436 84.190 1.00 66.22 N ANISOU 735 N ALA A 117 12379 5486 7296 585 542 248 N ATOM 736 CA ALA A 117 25.091 11.729 83.710 1.00 64.67 C ANISOU 736 CA ALA A 117 12135 5319 7118 346 745 190 C ATOM 737 C ALA A 117 25.725 10.829 84.765 1.00 66.55 C ANISOU 737 C ALA A 117 11821 5857 7608 169 755 92 C ATOM 738 O ALA A 117 25.901 9.643 84.505 1.00 66.34 O ANISOU 738 O ALA A 117 11582 5986 7637 148 667 91 O ATOM 739 CB ALA A 117 26.109 12.716 83.167 1.00 65.23 C ANISOU 739 CB ALA A 117 12620 5106 7059 145 1123 139 C ATOM 740 N LEU A 118 26.020 11.373 85.958 1.00 62.18 N ANISOU 740 N LEU A 118 11053 5380 7193 62 840 12 N ATOM 741 CA LEU A 118 26.609 10.649 87.085 1.00 61.57 C ANISOU 741 CA LEU A 118 10488 5569 7336 -82 828 -90 C ATOM 742 C LEU A 118 25.653 9.638 87.730 1.00 65.24 C ANISOU 742 C LEU A 118 10603 6280 7905 90 516 -37 C ATOM 743 O LEU A 118 26.109 8.771 88.477 1.00 64.40 O ANISOU 743 O LEU A 118 10133 6389 7946 -1 477 -104 O ATOM 744 CB LEU A 118 27.187 11.617 88.122 1.00 62.13 C ANISOU 744 CB LEU A 118 10487 5620 7499 -239 1005 -199 C ATOM 745 CG LEU A 118 28.370 12.487 87.645 1.00 67.31 C ANISOU 745 CG LEU A 118 11394 6070 8111 -486 1366 -306 C ATOM 746 CD1 LEU A 118 28.662 13.602 88.639 1.00 66.93 C ANISOU 746 CD1 LEU A 118 11332 5970 8129 -600 1508 -401 C ATOM 747 CD2 LEU A 118 29.617 11.640 87.363 1.00 69.14 C ANISOU 747 CD2 LEU A 118 11413 6407 8452 -699 1508 -430 C ATOM 748 N CYS A 119 24.345 9.717 87.416 1.00 62.78 N ANISOU 748 N CYS A 119 10407 5930 7518 339 295 70 N ATOM 749 CA CYS A 119 23.336 8.750 87.869 1.00 63.21 C ANISOU 749 CA CYS A 119 10156 6191 7670 498 18 108 C ATOM 750 C CYS A 119 23.554 7.430 87.107 1.00 65.91 C ANISOU 750 C CYS A 119 10409 6631 8002 485 -62 128 C ATOM 751 O CYS A 119 23.247 6.350 87.616 1.00 64.58 O ANISOU 751 O CYS A 119 9922 6669 7946 511 -211 121 O ATOM 752 CB CYS A 119 21.925 9.302 87.668 1.00 64.33 C ANISOU 752 CB CYS A 119 10445 6247 7752 762 -178 181 C ATOM 753 SG CYS A 119 20.588 8.150 88.098 1.00 68.62 S ANISOU 753 SG CYS A 119 10620 7021 8433 949 -493 199 S ATOM 754 N LYS A 120 24.121 7.514 85.893 1.00 61.71 N ANISOU 754 N LYS A 120 10182 5938 7327 431 59 147 N ATOM 755 CA LYS A 120 24.445 6.307 85.150 1.00 60.69 C ANISOU 755 CA LYS A 120 9994 5886 7181 399 16 159 C ATOM 756 C LYS A 120 25.862 5.838 85.489 1.00 63.04 C ANISOU 756 C LYS A 120 10095 6275 7583 150 229 55 C ATOM 757 O LYS A 120 26.053 4.660 85.776 1.00 62.54 O ANISOU 757 O LYS A 120 9740 6404 7619 122 143 32 O ATOM 758 CB LYS A 120 24.227 6.492 83.642 1.00 62.25 C ANISOU 758 CB LYS A 120 10626 5864 7162 497 9 235 C ATOM 759 CG LYS A 120 22.800 6.115 83.250 1.00 61.60 C ANISOU 759 CG LYS A 120 10565 5810 7030 768 -319 314 C ATOM 760 CD LYS A 120 22.421 6.539 81.856 1.00 56.18 C ANISOU 760 CD LYS A 120 10360 4880 6104 914 -373 385 C ATOM 761 CE LYS A 120 21.795 5.414 81.080 1.00 72.85 C ANISOU 761 CE LYS A 120 12431 7072 8178 1046 -620 423 C ATOM 762 NZ LYS A 120 20.425 5.100 81.552 1.00 83.85 N ANISOU 762 NZ LYS A 120 13571 8611 9680 1262 -941 424 N ATOM 763 N VAL A 121 26.823 6.781 85.550 1.00 57.21 N ANISOU 763 N VAL A 121 9498 5404 6837 -24 501 -24 N ATOM 764 CA VAL A 121 28.249 6.532 85.761 1.00 56.00 C ANISOU 764 CA VAL A 121 9178 5305 6793 -268 729 -161 C ATOM 765 C VAL A 121 28.586 5.978 87.151 1.00 58.60 C ANISOU 765 C VAL A 121 9053 5887 7323 -324 646 -253 C ATOM 766 O VAL A 121 29.299 4.982 87.218 1.00 57.86 O ANISOU 766 O VAL A 121 8725 5937 7321 -402 646 -321 O ATOM 767 CB VAL A 121 29.110 7.791 85.415 1.00 59.65 C ANISOU 767 CB VAL A 121 9931 5533 7199 -448 1059 -241 C ATOM 768 CG1 VAL A 121 30.603 7.554 85.666 1.00 59.84 C ANISOU 768 CG1 VAL A 121 9732 5626 7377 -708 1296 -424 C ATOM 769 CG2 VAL A 121 28.883 8.240 83.974 1.00 58.81 C ANISOU 769 CG2 VAL A 121 10332 5150 6863 -395 1161 -151 C ATOM 770 N ILE A 122 28.154 6.639 88.243 1.00 55.46 N ANISOU 770 N ILE A 122 8557 5529 6984 -286 587 -265 N ATOM 771 CA ILE A 122 28.526 6.245 89.608 1.00 54.53 C ANISOU 771 CA ILE A 122 8072 5617 7029 -340 521 -361 C ATOM 772 C ILE A 122 27.935 4.868 89.999 1.00 57.77 C ANISOU 772 C ILE A 122 8226 6234 7490 -214 277 -306 C ATOM 773 O ILE A 122 28.747 4.023 90.378 1.00 57.68 O ANISOU 773 O ILE A 122 7979 6365 7571 -294 272 -394 O ATOM 774 CB ILE A 122 28.249 7.376 90.624 1.00 58.06 C ANISOU 774 CB ILE A 122 8531 6023 7505 -343 548 -390 C ATOM 775 CG1 ILE A 122 29.251 8.523 90.369 1.00 58.20 C ANISOU 775 CG1 ILE A 122 8732 5868 7514 -539 835 -501 C ATOM 776 CG2 ILE A 122 28.296 6.872 92.100 1.00 59.25 C ANISOU 776 CG2 ILE A 122 8341 6384 7788 -340 417 -458 C ATOM 777 CD1 ILE A 122 28.896 9.908 90.995 1.00 66.42 C ANISOU 777 CD1 ILE A 122 9931 6779 8526 -539 910 -505 C ATOM 778 N PRO A 123 26.615 4.545 89.869 1.00 53.92 N ANISOU 778 N PRO A 123 7772 5765 6951 -27 81 -182 N ATOM 779 CA PRO A 123 26.162 3.179 90.209 1.00 52.76 C ANISOU 779 CA PRO A 123 7388 5801 6858 53 -105 -153 C ATOM 780 C PRO A 123 26.868 2.082 89.389 1.00 53.83 C ANISOU 780 C PRO A 123 7487 5984 6980 -4 -86 -166 C ATOM 781 O PRO A 123 27.125 0.988 89.915 1.00 52.85 O ANISOU 781 O PRO A 123 7132 6020 6928 -13 -164 -203 O ATOM 782 CB PRO A 123 24.648 3.238 89.938 1.00 54.41 C ANISOU 782 CB PRO A 123 7681 5977 7017 244 -276 -43 C ATOM 783 CG PRO A 123 24.295 4.669 90.139 1.00 58.87 C ANISOU 783 CG PRO A 123 8426 6395 7545 276 -208 -35 C ATOM 784 CD PRO A 123 25.457 5.382 89.481 1.00 54.98 C ANISOU 784 CD PRO A 123 8143 5759 6990 125 15 -83 C ATOM 785 N TYR A 124 27.224 2.396 88.129 1.00 48.45 N ANISOU 785 N TYR A 124 7059 5151 6200 -43 33 -144 N ATOM 786 CA TYR A 124 27.965 1.508 87.224 1.00 48.84 C ANISOU 786 CA TYR A 124 7120 5210 6227 -111 95 -164 C ATOM 787 C TYR A 124 29.376 1.206 87.778 1.00 51.97 C ANISOU 787 C TYR A 124 7289 5706 6752 -276 230 -316 C ATOM 788 O TYR A 124 29.746 0.046 87.899 1.00 52.51 O ANISOU 788 O TYR A 124 7163 5913 6877 -274 159 -346 O ATOM 789 CB TYR A 124 28.029 2.120 85.810 1.00 50.60 C ANISOU 789 CB TYR A 124 7720 5208 6296 -127 230 -115 C ATOM 790 CG TYR A 124 29.036 1.483 84.884 1.00 52.38 C ANISOU 790 CG TYR A 124 7997 5403 6504 -243 381 -164 C ATOM 791 CD1 TYR A 124 28.786 0.245 84.294 1.00 55.22 C ANISOU 791 CD1 TYR A 124 8314 5838 6829 -172 253 -108 C ATOM 792 CD2 TYR A 124 30.237 2.120 84.583 1.00 52.11 C ANISOU 792 CD2 TYR A 124 8056 5253 6490 -433 671 -278 C ATOM 793 CE1 TYR A 124 29.713 -0.350 83.437 1.00 55.92 C ANISOU 793 CE1 TYR A 124 8457 5892 6900 -276 403 -156 C ATOM 794 CE2 TYR A 124 31.184 1.520 83.754 1.00 52.72 C ANISOU 794 CE2 TYR A 124 8161 5300 6570 -548 835 -342 C ATOM 795 CZ TYR A 124 30.907 0.295 83.166 1.00 58.95 C ANISOU 795 CZ TYR A 124 8920 6164 7315 -461 698 -273 C ATOM 796 OH TYR A 124 31.819 -0.293 82.333 1.00 58.22 O ANISOU 796 OH TYR A 124 8867 6032 7221 -568 868 -336 O ATOM 797 N LEU A 125 30.139 2.242 88.124 1.00 47.25 N ANISOU 797 N LEU A 125 6713 5036 6205 -410 413 -424 N ATOM 798 CA LEU A 125 31.474 2.114 88.708 1.00 46.62 C ANISOU 798 CA LEU A 125 6395 5047 6270 -564 530 -606 C ATOM 799 C LEU A 125 31.474 1.325 90.026 1.00 50.33 C ANISOU 799 C LEU A 125 6543 5734 6846 -498 332 -653 C ATOM 800 O LEU A 125 32.398 0.537 90.243 1.00 51.25 O ANISOU 800 O LEU A 125 6446 5969 7059 -545 326 -769 O ATOM 801 CB LEU A 125 32.110 3.507 88.913 1.00 46.57 C ANISOU 801 CB LEU A 125 6484 4911 6300 -721 756 -720 C ATOM 802 CG LEU A 125 32.555 4.245 87.628 1.00 51.34 C ANISOU 802 CG LEU A 125 7412 5281 6815 -845 1032 -731 C ATOM 803 CD1 LEU A 125 33.212 5.560 87.952 1.00 50.62 C ANISOU 803 CD1 LEU A 125 7397 5064 6772 -1017 1269 -862 C ATOM 804 CD2 LEU A 125 33.480 3.367 86.740 1.00 51.80 C ANISOU 804 CD2 LEU A 125 7418 5353 6909 -938 1155 -807 C ATOM 805 N GLN A 126 30.459 1.535 90.904 1.00 45.10 N ANISOU 805 N GLN A 126 5863 5112 6162 -383 176 -572 N ATOM 806 CA GLN A 126 30.356 0.820 92.183 1.00 44.65 C ANISOU 806 CA GLN A 126 5568 5226 6170 -313 3 -604 C ATOM 807 C GLN A 126 30.058 -0.648 91.929 1.00 46.81 C ANISOU 807 C GLN A 126 5758 5606 6423 -218 -139 -538 C ATOM 808 O GLN A 126 30.687 -1.494 92.558 1.00 46.37 O ANISOU 808 O GLN A 126 5513 5677 6427 -212 -212 -622 O ATOM 809 CB GLN A 126 29.293 1.449 93.104 1.00 46.19 C ANISOU 809 CB GLN A 126 5798 5410 6343 -228 -84 -536 C ATOM 810 CG GLN A 126 29.488 1.160 94.596 1.00 46.77 C ANISOU 810 CG GLN A 126 5680 5612 6480 -206 -190 -616 C ATOM 811 CD GLN A 126 29.150 -0.245 95.032 1.00 62.89 C ANISOU 811 CD GLN A 126 7600 7783 8512 -103 -356 -576 C ATOM 812 OE1 GLN A 126 29.926 -0.911 95.738 1.00 61.36 O ANISOU 812 OE1 GLN A 126 7258 7695 8361 -105 -422 -677 O ATOM 813 NE2 GLN A 126 28.011 -0.750 94.604 1.00 48.55 N ANISOU 813 NE2 GLN A 126 5853 5954 6639 -5 -428 -442 N ATOM 814 N ALA A 127 29.121 -0.951 90.989 1.00 41.98 N ANISOU 814 N ALA A 127 5297 4934 5719 -137 -185 -399 N ATOM 815 CA ALA A 127 28.804 -2.318 90.563 1.00 40.67 C ANISOU 815 CA ALA A 127 5085 4846 5524 -62 -300 -336 C ATOM 816 C ALA A 127 30.027 -3.012 89.931 1.00 44.21 C ANISOU 816 C ALA A 127 5472 5323 6003 -143 -213 -422 C ATOM 817 O ALA A 127 30.248 -4.194 90.197 1.00 45.82 O ANISOU 817 O ALA A 127 5539 5640 6229 -100 -307 -439 O ATOM 818 CB ALA A 127 27.644 -2.313 89.589 1.00 41.20 C ANISOU 818 CB ALA A 127 5336 4824 5492 26 -359 -201 C ATOM 819 N VAL A 128 30.818 -2.285 89.115 1.00 39.91 N ANISOU 819 N VAL A 128 5040 4665 5461 -262 -19 -484 N ATOM 820 CA VAL A 128 32.048 -2.774 88.457 1.00 39.99 C ANISOU 820 CA VAL A 128 4992 4681 5523 -362 116 -593 C ATOM 821 C VAL A 128 33.073 -3.121 89.529 1.00 46.29 C ANISOU 821 C VAL A 128 5501 5624 6463 -396 85 -764 C ATOM 822 O VAL A 128 33.744 -4.141 89.427 1.00 47.14 O ANISOU 822 O VAL A 128 5470 5821 6620 -382 54 -830 O ATOM 823 CB VAL A 128 32.615 -1.748 87.418 1.00 42.54 C ANISOU 823 CB VAL A 128 5530 4819 5816 -503 376 -636 C ATOM 824 CG1 VAL A 128 34.106 -1.931 87.163 1.00 41.65 C ANISOU 824 CG1 VAL A 128 5276 4722 5825 -651 566 -825 C ATOM 825 CG2 VAL A 128 31.840 -1.794 86.111 1.00 42.16 C ANISOU 825 CG2 VAL A 128 5789 4627 5604 -447 388 -483 C ATOM 826 N SER A 129 33.195 -2.277 90.551 1.00 43.95 N ANISOU 826 N SER A 129 5125 5346 6228 -427 80 -841 N ATOM 827 CA SER A 129 34.139 -2.517 91.639 1.00 44.29 C ANISOU 827 CA SER A 129 4908 5522 6398 -440 15 -1018 C ATOM 828 C SER A 129 33.797 -3.783 92.431 1.00 48.17 C ANISOU 828 C SER A 129 5283 6154 6864 -284 -219 -974 C ATOM 829 O SER A 129 34.715 -4.470 92.873 1.00 48.99 O ANISOU 829 O SER A 129 5199 6364 7049 -260 -287 -1112 O ATOM 830 CB SER A 129 34.279 -1.289 92.543 1.00 47.65 C ANISOU 830 CB SER A 129 5306 5923 6876 -508 54 -1108 C ATOM 831 OG SER A 129 33.165 -1.073 93.396 1.00 53.79 O ANISOU 831 OG SER A 129 6148 6711 7578 -402 -87 -987 O ATOM 832 N VAL A 130 32.491 -4.106 92.583 1.00 43.94 N ANISOU 832 N VAL A 130 4865 5609 6219 -176 -335 -796 N ATOM 833 CA VAL A 130 32.021 -5.314 93.299 1.00 43.67 C ANISOU 833 CA VAL A 130 4774 5677 6142 -42 -522 -741 C ATOM 834 C VAL A 130 32.421 -6.543 92.490 1.00 46.91 C ANISOU 834 C VAL A 130 5158 6125 6541 -13 -536 -735 C ATOM 835 O VAL A 130 32.978 -7.496 93.031 1.00 47.18 O ANISOU 835 O VAL A 130 5076 6254 6597 57 -638 -807 O ATOM 836 CB VAL A 130 30.486 -5.283 93.577 1.00 47.21 C ANISOU 836 CB VAL A 130 5346 6091 6502 37 -599 -577 C ATOM 837 CG1 VAL A 130 30.000 -6.595 94.202 1.00 46.43 C ANISOU 837 CG1 VAL A 130 5218 6071 6354 148 -744 -527 C ATOM 838 CG2 VAL A 130 30.109 -4.087 94.446 1.00 46.63 C ANISOU 838 CG2 VAL A 130 5295 5980 6443 19 -583 -592 C ATOM 839 N SER A 131 32.136 -6.493 91.186 1.00 42.77 N ANISOU 839 N SER A 131 4766 5513 5971 -57 -434 -651 N ATOM 840 CA SER A 131 32.463 -7.508 90.194 1.00 41.71 C ANISOU 840 CA SER A 131 4649 5385 5813 -49 -412 -634 C ATOM 841 C SER A 131 33.967 -7.791 90.173 1.00 44.90 C ANISOU 841 C SER A 131 4882 5845 6332 -100 -341 -819 C ATOM 842 O SER A 131 34.350 -8.946 90.152 1.00 46.95 O ANISOU 842 O SER A 131 5067 6176 6597 -31 -413 -845 O ATOM 843 CB SER A 131 31.979 -7.058 88.823 1.00 43.93 C ANISOU 843 CB SER A 131 5141 5533 6016 -101 -297 -532 C ATOM 844 OG SER A 131 32.194 -8.066 87.853 1.00 49.32 O ANISOU 844 OG SER A 131 5868 6212 6661 -91 -278 -506 O ATOM 845 N VAL A 132 34.812 -6.764 90.219 1.00 40.23 N ANISOU 845 N VAL A 132 4221 5222 5842 -217 -201 -961 N ATOM 846 CA VAL A 132 36.267 -6.939 90.234 1.00 40.30 C ANISOU 846 CA VAL A 132 4022 5290 5999 -277 -125 -1180 C ATOM 847 C VAL A 132 36.663 -7.616 91.544 1.00 46.34 C ANISOU 847 C VAL A 132 4587 6202 6817 -150 -342 -1282 C ATOM 848 O VAL A 132 37.380 -8.602 91.501 1.00 47.45 O ANISOU 848 O VAL A 132 4600 6420 7008 -82 -403 -1373 O ATOM 849 CB VAL A 132 37.050 -5.615 89.966 1.00 44.12 C ANISOU 849 CB VAL A 132 4477 5692 6594 -459 104 -1332 C ATOM 850 CG1 VAL A 132 38.548 -5.772 90.240 1.00 44.11 C ANISOU 850 CG1 VAL A 132 4190 5780 6790 -515 153 -1607 C ATOM 851 CG2 VAL A 132 36.820 -5.111 88.546 1.00 43.41 C ANISOU 851 CG2 VAL A 132 4635 5431 6429 -574 336 -1244 C ATOM 852 N ALA A 133 36.152 -7.121 92.695 1.00 43.64 N ANISOU 852 N ALA A 133 4248 5886 6446 -103 -462 -1261 N ATOM 853 CA ALA A 133 36.407 -7.644 94.043 1.00 42.37 C ANISOU 853 CA ALA A 133 3967 5835 6295 29 -678 -1345 C ATOM 854 C ALA A 133 36.112 -9.157 94.102 1.00 47.47 C ANISOU 854 C ALA A 133 4654 6534 6848 186 -828 -1258 C ATOM 855 O ALA A 133 36.990 -9.936 94.463 1.00 47.30 O ANISOU 855 O ALA A 133 4497 6596 6879 280 -938 -1394 O ATOM 856 CB ALA A 133 35.576 -6.876 95.075 1.00 42.06 C ANISOU 856 CB ALA A 133 4017 5774 6192 47 -748 -1274 C ATOM 857 N VAL A 134 34.917 -9.563 93.648 1.00 44.90 N ANISOU 857 N VAL A 134 4513 6153 6395 211 -824 -1048 N ATOM 858 CA VAL A 134 34.429 -10.946 93.603 1.00 45.23 C ANISOU 858 CA VAL A 134 4635 6217 6333 329 -930 -943 C ATOM 859 C VAL A 134 35.309 -11.823 92.693 1.00 48.27 C ANISOU 859 C VAL A 134 4950 6627 6765 339 -886 -1011 C ATOM 860 O VAL A 134 35.767 -12.877 93.125 1.00 47.97 O ANISOU 860 O VAL A 134 4867 6650 6711 465 -1011 -1065 O ATOM 861 CB VAL A 134 32.948 -10.925 93.153 1.00 50.69 C ANISOU 861 CB VAL A 134 5510 6833 6916 310 -899 -736 C ATOM 862 CG1 VAL A 134 32.480 -12.277 92.667 1.00 51.32 C ANISOU 862 CG1 VAL A 134 5675 6914 6908 378 -946 -635 C ATOM 863 CG2 VAL A 134 32.057 -10.439 94.269 1.00 50.96 C ANISOU 863 CG2 VAL A 134 5602 6858 6902 343 -968 -680 C ATOM 864 N LEU A 135 35.530 -11.390 91.439 1.00 44.04 N ANISOU 864 N LEU A 135 4432 6028 6273 214 -705 -1008 N ATOM 865 CA LEU A 135 36.354 -12.112 90.484 1.00 43.64 C ANISOU 865 CA LEU A 135 4329 5981 6270 202 -622 -1075 C ATOM 866 C LEU A 135 37.821 -12.213 90.922 1.00 49.34 C ANISOU 866 C LEU A 135 4802 6791 7153 228 -642 -1324 C ATOM 867 O LEU A 135 38.459 -13.226 90.671 1.00 49.60 O ANISOU 867 O LEU A 135 4762 6870 7215 309 -678 -1393 O ATOM 868 CB LEU A 135 36.240 -11.487 89.091 1.00 43.63 C ANISOU 868 CB LEU A 135 4448 5866 6262 54 -401 -1021 C ATOM 869 CG LEU A 135 34.952 -11.742 88.291 1.00 48.04 C ANISOU 869 CG LEU A 135 5248 6339 6665 59 -402 -801 C ATOM 870 CD1 LEU A 135 34.980 -10.969 86.988 1.00 48.70 C ANISOU 870 CD1 LEU A 135 5482 6292 6729 -74 -195 -772 C ATOM 871 CD2 LEU A 135 34.764 -13.233 87.967 1.00 47.83 C ANISOU 871 CD2 LEU A 135 5265 6345 6565 155 -486 -736 C ATOM 872 N THR A 136 38.350 -11.182 91.592 1.00 47.32 N ANISOU 872 N THR A 136 4409 6561 7009 167 -628 -1472 N ATOM 873 CA THR A 136 39.729 -11.191 92.075 1.00 47.35 C ANISOU 873 CA THR A 136 4141 6658 7190 192 -670 -1744 C ATOM 874 C THR A 136 39.882 -12.276 93.137 1.00 50.03 C ANISOU 874 C THR A 136 4433 7096 7481 418 -948 -1782 C ATOM 875 O THR A 136 40.833 -13.048 93.071 1.00 51.19 O ANISOU 875 O THR A 136 4423 7311 7717 512 -1010 -1938 O ATOM 876 CB THR A 136 40.150 -9.782 92.538 1.00 56.43 C ANISOU 876 CB THR A 136 5176 7802 8463 59 -589 -1892 C ATOM 877 OG1 THR A 136 40.100 -8.907 91.414 1.00 52.64 O ANISOU 877 OG1 THR A 136 4784 7205 8013 -143 -306 -1860 O ATOM 878 CG2 THR A 136 41.544 -9.747 93.129 1.00 54.40 C ANISOU 878 CG2 THR A 136 4607 7651 8410 85 -658 -2205 C ATOM 879 N LEU A 137 38.926 -12.347 94.080 1.00 44.42 N ANISOU 879 N LEU A 137 3880 6378 6619 509 -1102 -1639 N ATOM 880 CA LEU A 137 38.877 -13.323 95.156 1.00 43.39 C ANISOU 880 CA LEU A 137 3798 6300 6388 722 -1350 -1640 C ATOM 881 C LEU A 137 38.758 -14.753 94.601 1.00 49.68 C ANISOU 881 C LEU A 137 4693 7089 7094 833 -1384 -1549 C ATOM 882 O LEU A 137 39.453 -15.648 95.085 1.00 51.07 O ANISOU 882 O LEU A 137 4815 7321 7269 1009 -1551 -1660 O ATOM 883 CB LEU A 137 37.720 -13.009 96.109 1.00 42.93 C ANISOU 883 CB LEU A 137 3935 6199 6179 750 -1430 -1485 C ATOM 884 CG LEU A 137 37.851 -11.759 96.979 1.00 47.44 C ANISOU 884 CG LEU A 137 4435 6780 6808 691 -1453 -1583 C ATOM 885 CD1 LEU A 137 36.524 -11.378 97.548 1.00 47.32 C ANISOU 885 CD1 LEU A 137 4632 6697 6652 677 -1452 -1394 C ATOM 886 CD2 LEU A 137 38.841 -11.949 98.096 1.00 49.43 C ANISOU 886 CD2 LEU A 137 4557 7116 7109 839 -1671 -1801 C ATOM 887 N SER A 138 37.907 -14.949 93.571 1.00 45.91 N ANISOU 887 N SER A 138 4366 6537 6540 737 -1236 -1359 N ATOM 888 CA SER A 138 37.675 -16.205 92.845 1.00 45.02 C ANISOU 888 CA SER A 138 4367 6399 6339 799 -1227 -1256 C ATOM 889 C SER A 138 38.988 -16.713 92.265 1.00 51.67 C ANISOU 889 C SER A 138 5026 7291 7315 838 -1196 -1439 C ATOM 890 O SER A 138 39.372 -17.842 92.558 1.00 52.12 O ANISOU 890 O SER A 138 5093 7380 7330 1008 -1329 -1478 O ATOM 891 CB SER A 138 36.663 -15.986 91.721 1.00 45.18 C ANISOU 891 CB SER A 138 4541 6332 6292 657 -1061 -1066 C ATOM 892 OG SER A 138 35.374 -15.735 92.255 1.00 45.70 O ANISOU 892 OG SER A 138 4765 6358 6243 648 -1104 -906 O ATOM 893 N PHE A 139 39.717 -15.853 91.522 1.00 50.46 N ANISOU 893 N PHE A 139 4707 7137 7328 686 -1016 -1568 N ATOM 894 CA PHE A 139 41.021 -16.171 90.930 1.00 51.89 C ANISOU 894 CA PHE A 139 4676 7361 7680 688 -937 -1779 C ATOM 895 C PHE A 139 42.098 -16.419 91.989 1.00 57.10 C ANISOU 895 C PHE A 139 5100 8134 8460 856 -1144 -2027 C ATOM 896 O PHE A 139 43.042 -17.150 91.712 1.00 57.30 O ANISOU 896 O PHE A 139 4976 8208 8589 951 -1167 -2184 O ATOM 897 CB PHE A 139 41.464 -15.100 89.922 1.00 54.67 C ANISOU 897 CB PHE A 139 4941 7657 8172 456 -653 -1860 C ATOM 898 CG PHE A 139 40.710 -15.042 88.605 1.00 58.20 C ANISOU 898 CG PHE A 139 5621 7981 8511 320 -445 -1663 C ATOM 899 CD1 PHE A 139 39.345 -15.333 88.544 1.00 62.09 C ANISOU 899 CD1 PHE A 139 6374 8418 8798 350 -515 -1403 C ATOM 900 CD2 PHE A 139 41.343 -14.621 87.442 1.00 62.26 C ANISOU 900 CD2 PHE A 139 6102 8425 9129 157 -174 -1753 C ATOM 901 CE1 PHE A 139 38.639 -15.222 87.344 1.00 63.10 C ANISOU 901 CE1 PHE A 139 6715 8433 8825 241 -359 -1240 C ATOM 902 CE2 PHE A 139 40.633 -14.514 86.237 1.00 65.42 C ANISOU 902 CE2 PHE A 139 6760 8694 9401 46 1 -1572 C ATOM 903 CZ PHE A 139 39.288 -14.815 86.199 1.00 63.24 C ANISOU 903 CZ PHE A 139 6732 8376 8921 99 -113 -1319 C ATOM 904 N ILE A 140 41.949 -15.852 93.206 1.00 54.36 N ANISOU 904 N ILE A 140 4731 7826 8095 911 -1311 -2069 N ATOM 905 CA ILE A 140 42.893 -16.122 94.298 1.00 54.36 C ANISOU 905 CA ILE A 140 4547 7928 8179 1104 -1560 -2302 C ATOM 906 C ILE A 140 42.638 -17.540 94.808 1.00 59.19 C ANISOU 906 C ILE A 140 5340 8539 8610 1359 -1781 -2212 C ATOM 907 O ILE A 140 43.590 -18.322 94.913 1.00 60.40 O ANISOU 907 O ILE A 140 5355 8753 8839 1535 -1914 -2390 O ATOM 908 CB ILE A 140 42.858 -15.072 95.444 1.00 57.12 C ANISOU 908 CB ILE A 140 4845 8308 8549 1088 -1676 -2384 C ATOM 909 CG1 ILE A 140 43.406 -13.712 94.971 1.00 57.20 C ANISOU 909 CG1 ILE A 140 4634 8324 8774 848 -1459 -2545 C ATOM 910 CG2 ILE A 140 43.647 -15.576 96.659 1.00 57.21 C ANISOU 910 CG2 ILE A 140 4751 8409 8576 1344 -1999 -2589 C ATOM 911 CD1 ILE A 140 43.118 -12.516 95.920 1.00 60.81 C ANISOU 911 CD1 ILE A 140 5099 8779 9227 775 -1507 -2569 C ATOM 912 N ALA A 141 41.350 -17.869 95.095 1.00 54.63 N ANISOU 912 N ALA A 141 5076 7882 7799 1375 -1806 -1946 N ATOM 913 CA ALA A 141 40.899 -19.173 95.584 1.00 54.25 C ANISOU 913 CA ALA A 141 5273 7796 7545 1579 -1967 -1826 C ATOM 914 C ALA A 141 41.331 -20.258 94.625 1.00 59.10 C ANISOU 914 C ALA A 141 5875 8404 8176 1637 -1910 -1832 C ATOM 915 O ALA A 141 41.906 -21.267 95.049 1.00 59.48 O ANISOU 915 O ALA A 141 5948 8472 8181 1866 -2090 -1919 O ATOM 916 CB ALA A 141 39.388 -19.186 95.732 1.00 54.93 C ANISOU 916 CB ALA A 141 5654 7786 7430 1501 -1904 -1554 C ATOM 917 N LEU A 142 41.121 -20.006 93.324 1.00 55.61 N ANISOU 917 N LEU A 142 5402 7928 7799 1439 -1662 -1754 N ATOM 918 CA LEU A 142 41.449 -20.902 92.216 1.00 55.48 C ANISOU 918 CA LEU A 142 5390 7889 7801 1446 -1552 -1743 C ATOM 919 C LEU A 142 42.935 -21.229 92.187 1.00 60.32 C ANISOU 919 C LEU A 142 5724 8586 8607 1572 -1615 -2024 C ATOM 920 O LEU A 142 43.307 -22.397 92.069 1.00 60.27 O ANISOU 920 O LEU A 142 5762 8579 8559 1744 -1695 -2050 O ATOM 921 CB LEU A 142 41.010 -20.226 90.904 1.00 55.45 C ANISOU 921 CB LEU A 142 5407 7824 7836 1189 -1272 -1634 C ATOM 922 CG LEU A 142 40.935 -21.068 89.659 1.00 59.52 C ANISOU 922 CG LEU A 142 6022 8282 8312 1154 -1128 -1551 C ATOM 923 CD1 LEU A 142 39.836 -22.133 89.765 1.00 58.76 C ANISOU 923 CD1 LEU A 142 6220 8122 7985 1236 -1211 -1329 C ATOM 924 CD2 LEU A 142 40.740 -20.184 88.459 1.00 61.29 C ANISOU 924 CD2 LEU A 142 6251 8443 8595 914 -865 -1502 C ATOM 925 N ASP A 143 43.774 -20.192 92.337 1.00 58.24 N ANISOU 925 N ASP A 143 5171 8394 8562 1491 -1581 -2248 N ATOM 926 CA ASP A 143 45.227 -20.274 92.347 1.00 58.40 C ANISOU 926 CA ASP A 143 4854 8509 8824 1582 -1629 -2569 C ATOM 927 C ASP A 143 45.696 -21.125 93.521 1.00 61.60 C ANISOU 927 C ASP A 143 5255 8977 9174 1908 -1979 -2690 C ATOM 928 O ASP A 143 46.473 -22.055 93.315 1.00 61.31 O ANISOU 928 O ASP A 143 5120 8974 9203 2085 -2058 -2827 O ATOM 929 CB ASP A 143 45.833 -18.869 92.413 1.00 61.04 C ANISOU 929 CB ASP A 143 4908 8895 9390 1397 -1515 -2775 C ATOM 930 CG ASP A 143 47.305 -18.856 92.083 1.00 80.80 C ANISOU 930 CG ASP A 143 7025 11485 12192 1416 -1470 -3126 C ATOM 931 OD1 ASP A 143 48.124 -18.855 93.027 1.00 83.20 O ANISOU 931 OD1 ASP A 143 7101 11892 12618 1589 -1716 -3379 O ATOM 932 OD2 ASP A 143 47.640 -18.861 90.881 1.00 89.53 O ANISOU 932 OD2 ASP A 143 8056 12549 13411 1263 -1191 -3162 O ATOM 933 N ARG A 144 45.176 -20.847 94.733 1.00 57.31 N ANISOU 933 N ARG A 144 4855 8433 8489 1998 -2186 -2629 N ATOM 934 CA ARG A 144 45.508 -21.596 95.942 1.00 56.98 C ANISOU 934 CA ARG A 144 4893 8419 8340 2318 -2533 -2721 C ATOM 935 C ARG A 144 45.055 -23.043 95.837 1.00 61.31 C ANISOU 935 C ARG A 144 5749 8884 8661 2502 -2602 -2547 C ATOM 936 O ARG A 144 45.820 -23.943 96.174 1.00 61.29 O ANISOU 936 O ARG A 144 5718 8910 8659 2775 -2813 -2697 O ATOM 937 CB ARG A 144 44.954 -20.908 97.213 1.00 57.19 C ANISOU 937 CB ARG A 144 5060 8432 8236 2343 -2696 -2671 C ATOM 938 CG ARG A 144 45.471 -19.487 97.494 1.00 61.11 C ANISOU 938 CG ARG A 144 5261 9010 8949 2192 -2671 -2872 C ATOM 939 CD ARG A 144 46.968 -19.404 97.725 1.00 61.94 C ANISOU 939 CD ARG A 144 4975 9242 9317 2325 -2835 -3258 C ATOM 940 NE ARG A 144 47.719 -19.472 96.466 1.00 60.32 N ANISOU 940 NE ARG A 144 4488 9075 9356 2198 -2601 -3393 N ATOM 941 CZ ARG A 144 48.919 -20.024 96.340 1.00 74.62 C ANISOU 941 CZ ARG A 144 6015 10973 11365 2366 -2712 -3681 C ATOM 942 NH1 ARG A 144 49.533 -20.541 97.397 1.00 68.06 N ANISOU 942 NH1 ARG A 144 5138 10206 10515 2687 -3088 -3870 N ATOM 943 NH2 ARG A 144 49.516 -20.067 95.153 1.00 56.46 N ANISOU 943 NH2 ARG A 144 3485 8688 9278 2223 -2451 -3789 N ATOM 944 N TRP A 145 43.842 -23.267 95.304 1.00 57.50 N ANISOU 944 N TRP A 145 5551 8299 7998 2352 -2419 -2249 N ATOM 945 CA TRP A 145 43.290 -24.604 95.082 1.00 56.26 C ANISOU 945 CA TRP A 145 5703 8047 7626 2471 -2430 -2069 C ATOM 946 C TRP A 145 44.166 -25.407 94.125 1.00 59.89 C ANISOU 946 C TRP A 145 6017 8531 8206 2545 -2370 -2185 C ATOM 947 O TRP A 145 44.529 -26.527 94.463 1.00 60.69 O ANISOU 947 O TRP A 145 6246 8608 8207 2803 -2541 -2222 O ATOM 948 CB TRP A 145 41.855 -24.509 94.575 1.00 54.07 C ANISOU 948 CB TRP A 145 5680 7671 7192 2250 -2222 -1771 C ATOM 949 CG TRP A 145 41.096 -25.797 94.641 1.00 54.05 C ANISOU 949 CG TRP A 145 6035 7559 6943 2356 -2248 -1583 C ATOM 950 CD1 TRP A 145 40.540 -26.368 95.751 1.00 56.76 C ANISOU 950 CD1 TRP A 145 6683 7823 7059 2513 -2404 -1499 C ATOM 951 CD2 TRP A 145 40.732 -26.631 93.531 1.00 53.30 C ANISOU 951 CD2 TRP A 145 6057 7401 6792 2285 -2085 -1454 C ATOM 952 NE1 TRP A 145 39.863 -27.515 95.403 1.00 56.11 N ANISOU 952 NE1 TRP A 145 6893 7632 6793 2536 -2335 -1332 N ATOM 953 CE2 TRP A 145 39.949 -27.690 94.041 1.00 57.20 C ANISOU 953 CE2 TRP A 145 6914 7784 7035 2397 -2149 -1300 C ATOM 954 CE3 TRP A 145 40.985 -26.581 92.147 1.00 53.81 C ANISOU 954 CE3 TRP A 145 5979 7480 6987 2132 -1880 -1457 C ATOM 955 CZ2 TRP A 145 39.384 -28.668 93.211 1.00 55.94 C ANISOU 955 CZ2 TRP A 145 6952 7540 6764 2347 -2020 -1153 C ATOM 956 CZ3 TRP A 145 40.456 -27.572 91.331 1.00 54.87 C ANISOU 956 CZ3 TRP A 145 6320 7530 6999 2103 -1771 -1308 C ATOM 957 CH2 TRP A 145 39.655 -28.592 91.859 1.00 55.34 C ANISOU 957 CH2 TRP A 145 6715 7492 6821 2205 -1845 -1160 C ATOM 958 N TYR A 146 44.559 -24.837 92.970 1.00 55.57 N ANISOU 958 N TYR A 146 5223 8022 7870 2333 -2127 -2255 N ATOM 959 CA TYR A 146 45.467 -25.548 92.060 1.00 54.98 C ANISOU 959 CA TYR A 146 4992 7967 7932 2393 -2043 -2391 C ATOM 960 C TYR A 146 46.901 -25.663 92.613 1.00 63.69 C ANISOU 960 C TYR A 146 5770 9183 9246 2624 -2250 -2738 C ATOM 961 O TYR A 146 47.577 -26.640 92.326 1.00 64.45 O ANISOU 961 O TYR A 146 5818 9286 9383 2809 -2306 -2846 O ATOM 962 CB TYR A 146 45.471 -24.941 90.654 1.00 54.19 C ANISOU 962 CB TYR A 146 4769 7847 7974 2095 -1698 -2365 C ATOM 963 CG TYR A 146 44.288 -25.375 89.821 1.00 54.31 C ANISOU 963 CG TYR A 146 5107 7745 7783 1954 -1527 -2062 C ATOM 964 CD1 TYR A 146 44.223 -26.653 89.280 1.00 55.53 C ANISOU 964 CD1 TYR A 146 5438 7839 7824 2063 -1515 -1980 C ATOM 965 CD2 TYR A 146 43.232 -24.501 89.562 1.00 54.90 C ANISOU 965 CD2 TYR A 146 5308 7768 7782 1718 -1386 -1871 C ATOM 966 CE1 TYR A 146 43.133 -27.062 88.515 1.00 54.31 C ANISOU 966 CE1 TYR A 146 5569 7579 7486 1929 -1371 -1723 C ATOM 967 CE2 TYR A 146 42.143 -24.895 88.784 1.00 55.14 C ANISOU 967 CE2 TYR A 146 5613 7699 7639 1600 -1256 -1620 C ATOM 968 CZ TYR A 146 42.102 -26.177 88.261 1.00 59.79 C ANISOU 968 CZ TYR A 146 6364 8234 8121 1700 -1250 -1552 C ATOM 969 OH TYR A 146 41.041 -26.594 87.503 1.00 60.35 O ANISOU 969 OH TYR A 146 6694 8210 8026 1583 -1137 -1326 O ATOM 970 N ALA A 147 47.379 -24.685 93.392 1.00 62.36 N ANISOU 970 N ALA A 147 5370 9103 9221 2622 -2373 -2928 N ATOM 971 CA ALA A 147 48.735 -24.788 93.928 1.00 62.57 C ANISOU 971 CA ALA A 147 5062 9246 9465 2851 -2600 -3289 C ATOM 972 C ALA A 147 48.852 -25.860 95.013 1.00 69.01 C ANISOU 972 C ALA A 147 6091 10046 10083 3243 -2978 -3307 C ATOM 973 O ALA A 147 49.770 -26.672 94.952 1.00 71.93 O ANISOU 973 O ALA A 147 6326 10457 10547 3490 -3121 -3507 O ATOM 974 CB ALA A 147 49.211 -23.448 94.450 1.00 63.18 C ANISOU 974 CB ALA A 147 4834 9419 9753 2728 -2627 -3503 C ATOM 975 N ILE A 148 47.906 -25.891 95.958 1.00 64.43 N ANISOU 975 N ILE A 148 5869 9390 9222 3302 -3120 -3097 N ATOM 976 CA ILE A 148 47.866 -26.786 97.113 1.00 63.74 C ANISOU 976 CA ILE A 148 6077 9249 8891 3655 -3463 -3085 C ATOM 977 C ILE A 148 47.148 -28.128 96.850 1.00 70.15 C ANISOU 977 C ILE A 148 7315 9918 9421 3763 -3425 -2833 C ATOM 978 O ILE A 148 47.716 -29.170 97.172 1.00 71.30 O ANISOU 978 O ILE A 148 7561 10039 9490 4084 -3644 -2931 O ATOM 979 CB ILE A 148 47.251 -26.019 98.321 1.00 66.18 C ANISOU 979 CB ILE A 148 6558 9536 9050 3643 -3609 -3017 C ATOM 980 CG1 ILE A 148 48.068 -24.755 98.641 1.00 66.24 C ANISOU 980 CG1 ILE A 148 6142 9685 9343 3560 -3674 -3300 C ATOM 981 CG2 ILE A 148 47.081 -26.916 99.554 1.00 67.13 C ANISOU 981 CG2 ILE A 148 7074 9563 8870 3996 -3940 -2978 C ATOM 982 CD1 ILE A 148 47.305 -23.637 99.388 1.00 75.83 C ANISOU 982 CD1 ILE A 148 7461 10879 10472 3385 -3655 -3191 C ATOM 983 N CYS A 149 45.908 -28.113 96.312 1.00 67.63 N ANISOU 983 N CYS A 149 7254 9500 8944 3509 -3163 -2523 N ATOM 984 CA CYS A 149 45.101 -29.326 96.112 1.00 67.14 C ANISOU 984 CA CYS A 149 7609 9292 8609 3571 -3107 -2281 C ATOM 985 C CYS A 149 45.444 -30.124 94.852 1.00 71.73 C ANISOU 985 C CYS A 149 8120 9863 9272 3548 -2936 -2281 C ATOM 986 O CYS A 149 45.474 -31.348 94.924 1.00 70.65 O ANISOU 986 O CYS A 149 8236 9640 8969 3765 -3025 -2237 O ATOM 987 CB CYS A 149 43.612 -29.007 96.175 1.00 67.02 C ANISOU 987 CB CYS A 149 7888 9177 8399 3328 -2930 -1984 C ATOM 988 SG CYS A 149 43.064 -28.369 97.779 1.00 71.14 S ANISOU 988 SG CYS A 149 8614 9664 8753 3392 -3122 -1951 S ATOM 989 N HIS A 150 45.653 -29.457 93.704 1.00 68.97 N ANISOU 989 N HIS A 150 7476 9580 9152 3284 -2677 -2316 N ATOM 990 CA HIS A 150 45.929 -30.135 92.437 1.00 68.35 C ANISOU 990 CA HIS A 150 7350 9476 9143 3230 -2479 -2306 C ATOM 991 C HIS A 150 47.186 -29.560 91.737 1.00 73.36 C ANISOU 991 C HIS A 150 7511 10232 10128 3176 -2382 -2594 C ATOM 992 O HIS A 150 47.064 -28.912 90.689 1.00 71.44 O ANISOU 992 O HIS A 150 7134 9994 10015 2887 -2092 -2559 O ATOM 993 CB HIS A 150 44.668 -30.098 91.546 1.00 68.93 C ANISOU 993 CB HIS A 150 7652 9455 9084 2934 -2200 -2011 C ATOM 994 CG HIS A 150 43.458 -30.694 92.205 1.00 72.34 C ANISOU 994 CG HIS A 150 8513 9767 9206 2969 -2266 -1765 C ATOM 995 ND1 HIS A 150 43.241 -32.065 92.220 1.00 74.35 N ANISOU 995 ND1 HIS A 150 9082 9913 9256 3140 -2315 -1671 N ATOM 996 CD2 HIS A 150 42.483 -30.095 92.923 1.00 73.77 C ANISOU 996 CD2 HIS A 150 8850 9916 9263 2862 -2284 -1623 C ATOM 997 CE1 HIS A 150 42.116 -32.244 92.897 1.00 73.54 C ANISOU 997 CE1 HIS A 150 9314 9710 8916 3106 -2336 -1476 C ATOM 998 NE2 HIS A 150 41.625 -31.090 93.344 1.00 73.58 N ANISOU 998 NE2 HIS A 150 9230 9760 8965 2944 -2319 -1443 N ATOM 999 N PRO A 151 48.407 -29.769 92.318 1.00 73.24 N ANISOU 999 N PRO A 151 7244 10310 10274 3453 -2621 -2897 N ATOM 1000 CA PRO A 151 49.629 -29.195 91.717 1.00 73.84 C ANISOU 1000 CA PRO A 151 6831 10505 10720 3389 -2515 -3213 C ATOM 1001 C PRO A 151 50.083 -29.782 90.390 1.00 81.45 C ANISOU 1001 C PRO A 151 7701 11441 11806 3319 -2257 -3252 C ATOM 1002 O PRO A 151 49.710 -30.906 90.034 1.00 82.67 O ANISOU 1002 O PRO A 151 8149 11496 11764 3418 -2238 -3082 O ATOM 1003 CB PRO A 151 50.696 -29.413 92.793 1.00 75.03 C ANISOU 1003 CB PRO A 151 6771 10754 10982 3747 -2890 -3525 C ATOM 1004 CG PRO A 151 49.975 -29.833 94.012 1.00 79.16 C ANISOU 1004 CG PRO A 151 7694 11205 11180 3957 -3179 -3354 C ATOM 1005 CD PRO A 151 48.741 -30.503 93.555 1.00 75.00 C ANISOU 1005 CD PRO A 151 7615 10526 10356 3841 -3002 -2987 C ATOM 1006 N LEU A 152 50.929 -29.001 89.671 1.00 78.87 N ANISOU 1006 N LEU A 152 6966 11193 11809 3137 -2040 -3491 N ATOM 1007 CA LEU A 152 51.578 -29.312 88.383 1.00 79.01 C ANISOU 1007 CA LEU A 152 6812 11194 12015 3035 -1748 -3603 C ATOM 1008 C LEU A 152 50.629 -29.287 87.146 1.00 83.38 C ANISOU 1008 C LEU A 152 7652 11616 12414 2729 -1393 -3299 C ATOM 1009 O LEU A 152 51.133 -29.333 86.022 1.00 83.35 O ANISOU 1009 O LEU A 152 7523 11582 12563 2593 -1106 -3387 O ATOM 1010 CB LEU A 152 52.381 -30.641 88.431 1.00 79.09 C ANISOU 1010 CB LEU A 152 6783 11214 12055 3388 -1924 -3761 C ATOM 1011 CG LEU A 152 53.296 -30.870 89.665 1.00 83.70 C ANISOU 1011 CG LEU A 152 7140 11913 12749 3765 -2341 -4060 C ATOM 1012 CD1 LEU A 152 53.575 -32.340 89.887 1.00 83.23 C ANISOU 1012 CD1 LEU A 152 7266 11806 12551 4151 -2570 -4072 C ATOM 1013 CD2 LEU A 152 54.578 -30.045 89.598 1.00 86.53 C ANISOU 1013 CD2 LEU A 152 6915 12419 13543 3717 -2298 -4487 C ATOM 1014 N LEU A 153 49.292 -29.151 87.331 1.00 79.78 N ANISOU 1014 N LEU A 153 7562 11079 11672 2613 -1402 -2967 N ATOM 1015 CA LEU A 153 48.351 -29.090 86.193 1.00 79.44 C ANISOU 1015 CA LEU A 153 7786 10917 11481 2342 -1110 -2696 C ATOM 1016 C LEU A 153 48.428 -27.758 85.429 1.00 80.27 C ANISOU 1016 C LEU A 153 7723 11018 11756 2008 -808 -2743 C ATOM 1017 O LEU A 153 48.606 -27.763 84.206 1.00 79.34 O ANISOU 1017 O LEU A 153 7620 10830 11696 1838 -512 -2740 O ATOM 1018 CB LEU A 153 46.885 -29.359 86.608 1.00 79.86 C ANISOU 1018 CB LEU A 153 8251 10887 11203 2323 -1215 -2358 C ATOM 1019 CG LEU A 153 46.553 -30.622 87.399 1.00 84.73 C ANISOU 1019 CG LEU A 153 9136 11465 11592 2610 -1477 -2261 C ATOM 1020 CD1 LEU A 153 45.111 -30.590 87.829 1.00 84.91 C ANISOU 1020 CD1 LEU A 153 9510 11409 11342 2521 -1520 -1965 C ATOM 1021 CD2 LEU A 153 46.834 -31.889 86.596 1.00 86.74 C ANISOU 1021 CD2 LEU A 153 9510 11650 11797 2721 -1400 -2251 C ATOM 1022 N PHE A 154 48.268 -26.625 86.146 1.00 74.70 N ANISOU 1022 N PHE A 154 6900 10372 11110 1915 -873 -2780 N ATOM 1023 CA PHE A 154 48.313 -25.295 85.540 1.00 74.11 C ANISOU 1023 CA PHE A 154 6701 10280 11179 1607 -596 -2825 C ATOM 1024 C PHE A 154 49.422 -24.473 86.154 1.00 82.47 C ANISOU 1024 C PHE A 154 7336 11458 12539 1615 -640 -3167 C ATOM 1025 O PHE A 154 49.571 -24.461 87.377 1.00 82.46 O ANISOU 1025 O PHE A 154 7236 11550 12543 1806 -948 -3255 O ATOM 1026 CB PHE A 154 46.950 -24.565 85.664 1.00 74.43 C ANISOU 1026 CB PHE A 154 7027 10254 11001 1435 -580 -2530 C ATOM 1027 CG PHE A 154 45.812 -25.275 84.963 1.00 73.90 C ANISOU 1027 CG PHE A 154 7348 10068 10662 1392 -520 -2218 C ATOM 1028 CD1 PHE A 154 45.630 -25.148 83.591 1.00 74.62 C ANISOU 1028 CD1 PHE A 154 7569 10052 10731 1186 -223 -2133 C ATOM 1029 CD2 PHE A 154 44.946 -26.099 85.671 1.00 73.99 C ANISOU 1029 CD2 PHE A 154 7608 10067 10439 1555 -755 -2026 C ATOM 1030 CE1 PHE A 154 44.603 -25.834 82.939 1.00 74.47 C ANISOU 1030 CE1 PHE A 154 7897 9930 10469 1155 -194 -1868 C ATOM 1031 CE2 PHE A 154 43.915 -26.779 85.018 1.00 75.70 C ANISOU 1031 CE2 PHE A 154 8155 10178 10428 1502 -696 -1768 C ATOM 1032 CZ PHE A 154 43.757 -26.648 83.656 1.00 73.32 C ANISOU 1032 CZ PHE A 154 7953 9787 10118 1308 -431 -1696 C ATOM 1033 N LYS A 155 50.213 -23.799 85.308 1.00 82.27 N ANISOU 1033 N LYS A 155 7073 11421 12764 1404 -326 -3373 N ATOM 1034 CA LYS A 155 51.310 -22.937 85.760 1.00 83.60 C ANISOU 1034 CA LYS A 155 6807 11696 13259 1359 -309 -3734 C ATOM 1035 C LYS A 155 50.751 -21.577 86.191 1.00 90.15 C ANISOU 1035 C LYS A 155 7676 12517 14062 1152 -273 -3660 C ATOM 1036 O LYS A 155 49.858 -21.037 85.528 1.00 89.59 O ANISOU 1036 O LYS A 155 7889 12325 13826 932 -62 -3409 O ATOM 1037 CB LYS A 155 52.360 -22.757 84.648 1.00 86.30 C ANISOU 1037 CB LYS A 155 6895 12008 13889 1185 65 -3997 C ATOM 1038 CG LYS A 155 53.783 -23.055 85.091 1.00102.62 C ANISOU 1038 CG LYS A 155 8488 14214 16289 1378 -57 -4421 C ATOM 1039 CD LYS A 155 54.749 -23.036 83.914 1.00112.93 C ANISOU 1039 CD LYS A 155 9562 15473 17875 1201 351 -4675 C ATOM 1040 CE LYS A 155 56.140 -23.456 84.323 1.00124.33 C ANISOU 1040 CE LYS A 155 10508 17062 19670 1416 216 -5116 C ATOM 1041 NZ LYS A 155 57.080 -23.461 83.170 1.00132.41 N ANISOU 1041 NZ LYS A 155 11289 18034 20989 1231 647 -5385 N ATOM 1042 N SER A 156 51.267 -21.036 87.306 1.00 88.83 N ANISOU 1042 N SER A 156 7233 12472 14047 1240 -494 -3882 N ATOM 1043 CA SER A 156 50.847 -19.736 87.818 1.00 89.86 C ANISOU 1043 CA SER A 156 7370 12601 14172 1062 -475 -3848 C ATOM 1044 C SER A 156 52.025 -18.811 88.059 1.00 95.46 C ANISOU 1044 C SER A 156 7632 13398 15240 951 -387 -4251 C ATOM 1045 O SER A 156 52.791 -18.992 89.007 1.00 95.41 O ANISOU 1045 O SER A 156 7325 13529 15395 1160 -673 -4521 O ATOM 1046 CB SER A 156 49.988 -19.880 89.068 1.00 95.00 C ANISOU 1046 CB SER A 156 8219 13291 14584 1256 -848 -3659 C ATOM 1047 OG SER A 156 48.645 -20.186 88.726 1.00106.83 O ANISOU 1047 OG SER A 156 10148 14679 15764 1228 -823 -3267 O ATOM 1048 N THR A 157 52.168 -17.821 87.171 1.00 92.94 N ANISOU 1048 N THR A 157 7284 12986 15043 618 17 -4302 N ATOM 1049 CA THR A 157 53.220 -16.809 87.212 1.00 92.65 C ANISOU 1049 CA THR A 157 6851 12996 15354 430 203 -4683 C ATOM 1050 C THR A 157 52.633 -15.411 87.396 1.00 96.32 C ANISOU 1050 C THR A 157 7448 13391 15758 178 337 -4582 C ATOM 1051 O THR A 157 51.424 -15.225 87.274 1.00 94.81 O ANISOU 1051 O THR A 157 7657 13100 15267 132 337 -4217 O ATOM 1052 CB THR A 157 54.109 -16.914 85.970 1.00 99.74 C ANISOU 1052 CB THR A 157 7578 13829 16490 252 615 -4898 C ATOM 1053 OG1 THR A 157 53.286 -16.889 84.802 1.00 98.66 O ANISOU 1053 OG1 THR A 157 7863 13504 16120 65 928 -4580 O ATOM 1054 CG2 THR A 157 54.984 -18.164 85.982 1.00 98.87 C ANISOU 1054 CG2 THR A 157 7206 13823 16538 519 459 -5116 C ATOM 1055 N ALA A 158 53.500 -14.438 87.714 1.00 94.87 N ANISOU 1055 N ALA A 158 6915 13262 15871 23 441 -4926 N ATOM 1056 CA ALA A 158 53.170 -13.030 87.931 1.00 95.15 C ANISOU 1056 CA ALA A 158 7018 13232 15902 -227 591 -4907 C ATOM 1057 C ALA A 158 52.667 -12.360 86.646 1.00100.54 C ANISOU 1057 C ALA A 158 8027 13699 16475 -544 1062 -4713 C ATOM 1058 O ALA A 158 51.723 -11.572 86.711 1.00101.22 O ANISOU 1058 O ALA A 158 8419 13687 16354 -659 1105 -4464 O ATOM 1059 CB ALA A 158 54.385 -12.296 88.468 1.00 95.78 C ANISOU 1059 CB ALA A 158 6607 13420 16364 -322 617 -5377 C ATOM 1060 N ARG A 159 53.291 -12.674 85.488 1.00 96.90 N ANISOU 1060 N ARG A 159 7519 13155 16145 -672 1410 -4831 N ATOM 1061 CA ARG A 159 52.913 -12.155 84.170 1.00 96.84 C ANISOU 1061 CA ARG A 159 7856 12919 16019 -952 1868 -4666 C ATOM 1062 C ARG A 159 51.498 -12.654 83.817 1.00100.10 C ANISOU 1062 C ARG A 159 8778 13237 16018 -844 1742 -4186 C ATOM 1063 O ARG A 159 50.692 -11.883 83.291 1.00 99.50 O ANISOU 1063 O ARG A 159 9067 12995 15742 -1016 1932 -3954 O ATOM 1064 CB ARG A 159 53.964 -12.572 83.111 1.00 98.89 C ANISOU 1064 CB ARG A 159 7937 13123 16515 -1069 2233 -4924 C ATOM 1065 CG ARG A 159 53.528 -12.436 81.647 1.00113.65 C ANISOU 1065 CG ARG A 159 10243 14743 18194 -1283 2661 -4709 C ATOM 1066 CD ARG A 159 54.329 -11.401 80.883 1.00129.29 C ANISOU 1066 CD ARG A 159 12170 16563 20389 -1648 3201 -4970 C ATOM 1067 NE ARG A 159 53.965 -11.386 79.464 1.00142.32 N ANISOU 1067 NE ARG A 159 14279 17960 21836 -1823 3599 -4770 N ATOM 1068 CZ ARG A 159 54.657 -10.768 78.509 1.00158.73 C ANISOU 1068 CZ ARG A 159 16405 19849 24058 -2132 4138 -4971 C ATOM 1069 NH1 ARG A 159 55.772 -10.107 78.807 1.00143.37 N ANISOU 1069 NH1 ARG A 159 14038 17946 22490 -2322 4363 -5396 N ATOM 1070 NH2 ARG A 159 54.247 -10.813 77.249 1.00147.36 N ANISOU 1070 NH2 ARG A 159 15442 18165 22383 -2258 4461 -4761 N ATOM 1071 N ARG A 160 51.200 -13.933 84.144 1.00 96.11 N ANISOU 1071 N ARG A 160 8292 12834 15391 -551 1413 -4053 N ATOM 1072 CA ARG A 160 49.896 -14.574 83.928 1.00 95.21 C ANISOU 1072 CA ARG A 160 8603 12657 14915 -425 1251 -3637 C ATOM 1073 C ARG A 160 48.840 -14.034 84.901 1.00 96.01 C ANISOU 1073 C ARG A 160 8869 12790 14822 -360 979 -3417 C ATOM 1074 O ARG A 160 47.646 -14.099 84.598 1.00 95.52 O ANISOU 1074 O ARG A 160 9181 12635 14478 -353 943 -3082 O ATOM 1075 CB ARG A 160 50.005 -16.103 84.043 1.00 96.43 C ANISOU 1075 CB ARG A 160 8710 12906 15024 -145 1005 -3605 C ATOM 1076 CG ARG A 160 50.554 -16.767 82.793 1.00110.04 C ANISOU 1076 CG ARG A 160 10459 14541 16810 -209 1297 -3670 C ATOM 1077 CD ARG A 160 50.695 -18.263 82.982 1.00122.70 C ANISOU 1077 CD ARG A 160 12006 16237 18375 81 1043 -3656 C ATOM 1078 NE ARG A 160 50.830 -18.956 81.700 1.00132.38 N ANISOU 1078 NE ARG A 160 13398 17346 19556 25 1307 -3601 N ATOM 1079 CZ ARG A 160 49.822 -19.510 81.033 1.00145.85 C ANISOU 1079 CZ ARG A 160 15514 18941 20961 43 1308 -3269 C ATOM 1080 NH1 ARG A 160 48.587 -19.465 81.521 1.00131.47 N ANISOU 1080 NH1 ARG A 160 13961 17117 18874 112 1068 -2970 N ATOM 1081 NH2 ARG A 160 50.041 -20.118 79.874 1.00132.50 N ANISOU 1081 NH2 ARG A 160 13964 17140 19241 -12 1553 -3249 N ATOM 1082 N ALA A 161 49.281 -13.516 86.071 1.00 90.37 N ANISOU 1082 N ALA A 161 7868 12204 14264 -310 785 -3619 N ATOM 1083 CA ALA A 161 48.408 -12.901 87.074 1.00 89.09 C ANISOU 1083 CA ALA A 161 7831 12070 13950 -263 552 -3457 C ATOM 1084 C ALA A 161 47.934 -11.541 86.544 1.00 90.62 C ANISOU 1084 C ALA A 161 8238 12107 14087 -541 850 -3360 C ATOM 1085 O ALA A 161 46.764 -11.209 86.714 1.00 90.45 O ANISOU 1085 O ALA A 161 8518 12023 13827 -530 763 -3072 O ATOM 1086 CB ALA A 161 49.143 -12.735 88.397 1.00 89.71 C ANISOU 1086 CB ALA A 161 7549 12317 14221 -137 281 -3735 C ATOM 1087 N LEU A 162 48.828 -10.794 85.851 1.00 85.24 N ANISOU 1087 N LEU A 162 7419 11346 13621 -789 1217 -3602 N ATOM 1088 CA LEU A 162 48.548 -9.504 85.213 1.00 84.44 C ANISOU 1088 CA LEU A 162 7548 11062 13475 -1069 1560 -3546 C ATOM 1089 C LEU A 162 47.539 -9.681 84.071 1.00 85.34 C ANISOU 1089 C LEU A 162 8134 10993 13297 -1109 1710 -3205 C ATOM 1090 O LEU A 162 46.685 -8.816 83.871 1.00 85.86 O ANISOU 1090 O LEU A 162 8513 10926 13184 -1208 1791 -3006 O ATOM 1091 CB LEU A 162 49.851 -8.878 84.686 1.00 85.01 C ANISOU 1091 CB LEU A 162 7361 11081 13856 -1321 1947 -3916 C ATOM 1092 CG LEU A 162 49.744 -7.518 83.972 1.00 90.71 C ANISOU 1092 CG LEU A 162 8333 11583 14549 -1636 2364 -3907 C ATOM 1093 CD1 LEU A 162 50.658 -6.496 84.606 1.00 91.10 C ANISOU 1093 CD1 LEU A 162 8046 11676 14892 -1816 2489 -4264 C ATOM 1094 CD2 LEU A 162 50.071 -7.655 82.491 1.00 94.36 C ANISOU 1094 CD2 LEU A 162 9008 11850 14994 -1812 2792 -3909 C ATOM 1095 N GLY A 163 47.658 -10.791 83.343 1.00 78.52 N ANISOU 1095 N GLY A 163 7319 10122 12391 -1021 1732 -3155 N ATOM 1096 CA GLY A 163 46.774 -11.149 82.239 1.00 76.87 C ANISOU 1096 CA GLY A 163 7538 9755 11913 -1032 1838 -2857 C ATOM 1097 C GLY A 163 45.372 -11.425 82.732 1.00 77.34 C ANISOU 1097 C GLY A 163 7842 9845 11700 -856 1507 -2526 C ATOM 1098 O GLY A 163 44.398 -10.973 82.128 1.00 77.06 O ANISOU 1098 O GLY A 163 8176 9662 11440 -915 1577 -2283 O ATOM 1099 N SER A 164 45.275 -12.153 83.858 1.00 71.53 N ANISOU 1099 N SER A 164 6901 9293 10985 -636 1147 -2532 N ATOM 1100 CA SER A 164 44.026 -12.470 84.545 1.00 70.34 C ANISOU 1100 CA SER A 164 6924 9188 10612 -467 830 -2263 C ATOM 1101 C SER A 164 43.429 -11.180 85.111 1.00 71.54 C ANISOU 1101 C SER A 164 7163 9301 10717 -556 819 -2197 C ATOM 1102 O SER A 164 42.230 -10.975 84.961 1.00 71.56 O ANISOU 1102 O SER A 164 7454 9229 10507 -536 752 -1938 O ATOM 1103 CB SER A 164 44.271 -13.466 85.674 1.00 74.38 C ANISOU 1103 CB SER A 164 7203 9883 11175 -226 493 -2336 C ATOM 1104 OG SER A 164 44.905 -14.649 85.211 1.00 84.90 O ANISOU 1104 OG SER A 164 8439 11254 12566 -127 499 -2421 O ATOM 1105 N ILE A 165 44.275 -10.294 85.713 1.00 65.85 N ANISOU 1105 N ILE A 165 6191 8624 10205 -659 893 -2447 N ATOM 1106 CA ILE A 165 43.901 -8.995 86.301 1.00 64.75 C ANISOU 1106 CA ILE A 165 6101 8446 10055 -761 910 -2434 C ATOM 1107 C ILE A 165 43.224 -8.093 85.248 1.00 68.88 C ANISOU 1107 C ILE A 165 6995 8754 10424 -935 1180 -2259 C ATOM 1108 O ILE A 165 42.197 -7.480 85.541 1.00 67.64 O ANISOU 1108 O ILE A 165 7048 8544 10108 -915 1090 -2066 O ATOM 1109 CB ILE A 165 45.120 -8.337 87.032 1.00 66.94 C ANISOU 1109 CB ILE A 165 6006 8811 10616 -852 959 -2786 C ATOM 1110 CG1 ILE A 165 45.210 -8.848 88.483 1.00 66.56 C ANISOU 1110 CG1 ILE A 165 5719 8957 10612 -631 569 -2861 C ATOM 1111 CG2 ILE A 165 45.112 -6.793 86.985 1.00 66.52 C ANISOU 1111 CG2 ILE A 165 6040 8635 10601 -1083 1199 -2842 C ATOM 1112 CD1 ILE A 165 46.593 -8.709 89.161 1.00 69.51 C ANISOU 1112 CD1 ILE A 165 5658 9464 11288 -638 529 -3253 C ATOM 1113 N LEU A 166 43.773 -8.069 84.020 1.00 66.20 N ANISOU 1113 N LEU A 166 6754 8280 10118 -1087 1504 -2328 N ATOM 1114 CA LEU A 166 43.247 -7.314 82.881 1.00 65.67 C ANISOU 1114 CA LEU A 166 7090 7979 9882 -1238 1776 -2176 C ATOM 1115 C LEU A 166 41.926 -7.926 82.399 1.00 66.60 C ANISOU 1115 C LEU A 166 7538 8048 9719 -1089 1596 -1849 C ATOM 1116 O LEU A 166 41.025 -7.197 81.998 1.00 66.31 O ANISOU 1116 O LEU A 166 7829 7868 9498 -1118 1632 -1665 O ATOM 1117 CB LEU A 166 44.287 -7.293 81.741 1.00 66.05 C ANISOU 1117 CB LEU A 166 7157 7896 10043 -1430 2174 -2359 C ATOM 1118 CG LEU A 166 45.044 -5.968 81.525 1.00 71.94 C ANISOU 1118 CG LEU A 166 7904 8501 10928 -1698 2544 -2571 C ATOM 1119 CD1 LEU A 166 46.030 -5.690 82.646 1.00 73.14 C ANISOU 1119 CD1 LEU A 166 7575 8828 11385 -1737 2488 -2886 C ATOM 1120 CD2 LEU A 166 45.811 -5.992 80.235 1.00 74.47 C ANISOU 1120 CD2 LEU A 166 8361 8641 11292 -1890 2970 -2691 C ATOM 1121 N GLY A 167 41.834 -9.253 82.473 1.00 61.43 N ANISOU 1121 N GLY A 167 6784 7513 9043 -923 1395 -1798 N ATOM 1122 CA GLY A 167 40.668 -10.040 82.083 1.00 60.11 C ANISOU 1122 CA GLY A 167 6867 7327 8646 -779 1206 -1527 C ATOM 1123 C GLY A 167 39.487 -9.762 82.976 1.00 62.59 C ANISOU 1123 C GLY A 167 7239 7699 8845 -663 933 -1353 C ATOM 1124 O GLY A 167 38.373 -9.574 82.486 1.00 63.38 O ANISOU 1124 O GLY A 167 7630 7700 8751 -633 883 -1141 O ATOM 1125 N ILE A 168 39.747 -9.696 84.294 1.00 57.13 N ANISOU 1125 N ILE A 168 6270 7160 8277 -596 758 -1458 N ATOM 1126 CA ILE A 168 38.800 -9.357 85.357 1.00 55.58 C ANISOU 1126 CA ILE A 168 6084 7026 8008 -499 523 -1339 C ATOM 1127 C ILE A 168 38.155 -7.970 85.067 1.00 58.47 C ANISOU 1127 C ILE A 168 6685 7244 8289 -608 649 -1246 C ATOM 1128 O ILE A 168 36.931 -7.828 85.162 1.00 58.72 O ANISOU 1128 O ILE A 168 6898 7244 8169 -528 509 -1050 O ATOM 1129 CB ILE A 168 39.527 -9.431 86.749 1.00 58.16 C ANISOU 1129 CB ILE A 168 6079 7521 8499 -430 362 -1525 C ATOM 1130 CG1 ILE A 168 39.843 -10.906 87.127 1.00 58.00 C ANISOU 1130 CG1 ILE A 168 5906 7633 8498 -257 165 -1559 C ATOM 1131 CG2 ILE A 168 38.728 -8.723 87.882 1.00 58.00 C ANISOU 1131 CG2 ILE A 168 6081 7533 8425 -380 192 -1443 C ATOM 1132 CD1 ILE A 168 40.794 -11.123 88.359 1.00 61.61 C ANISOU 1132 CD1 ILE A 168 6040 8245 9125 -166 6 -1790 C ATOM 1133 N TRP A 169 38.975 -6.966 84.690 1.00 53.70 N ANISOU 1133 N TRP A 169 6083 6538 7783 -790 922 -1399 N ATOM 1134 CA TRP A 169 38.499 -5.605 84.371 1.00 51.93 C ANISOU 1134 CA TRP A 169 6113 6145 7473 -900 1075 -1332 C ATOM 1135 C TRP A 169 37.638 -5.569 83.114 1.00 54.70 C ANISOU 1135 C TRP A 169 6862 6317 7604 -889 1144 -1125 C ATOM 1136 O TRP A 169 36.541 -5.014 83.156 1.00 55.30 O ANISOU 1136 O TRP A 169 7150 6324 7538 -827 1043 -959 O ATOM 1137 CB TRP A 169 39.648 -4.598 84.295 1.00 49.82 C ANISOU 1137 CB TRP A 169 5757 5801 7370 -1113 1375 -1568 C ATOM 1138 CG TRP A 169 40.103 -4.177 85.649 1.00 50.01 C ANISOU 1138 CG TRP A 169 5472 5967 7564 -1117 1264 -1734 C ATOM 1139 CD1 TRP A 169 41.123 -4.716 86.371 1.00 52.59 C ANISOU 1139 CD1 TRP A 169 5419 6463 8098 -1098 1187 -1963 C ATOM 1140 CD2 TRP A 169 39.501 -3.178 86.485 1.00 50.03 C ANISOU 1140 CD2 TRP A 169 5525 5956 7528 -1113 1179 -1682 C ATOM 1141 NE1 TRP A 169 41.203 -4.114 87.599 1.00 52.37 N ANISOU 1141 NE1 TRP A 169 5215 6526 8157 -1085 1052 -2059 N ATOM 1142 CE2 TRP A 169 40.229 -3.152 87.694 1.00 53.64 C ANISOU 1142 CE2 TRP A 169 5634 6575 8171 -1105 1061 -1888 C ATOM 1143 CE3 TRP A 169 38.417 -2.292 86.327 1.00 51.08 C ANISOU 1143 CE3 TRP A 169 5969 5953 7488 -1102 1184 -1489 C ATOM 1144 CZ2 TRP A 169 39.899 -2.295 88.751 1.00 52.44 C ANISOU 1144 CZ2 TRP A 169 5448 6449 8027 -1100 959 -1898 C ATOM 1145 CZ3 TRP A 169 38.092 -1.443 87.377 1.00 52.34 C ANISOU 1145 CZ3 TRP A 169 6077 6140 7668 -1094 1092 -1500 C ATOM 1146 CH2 TRP A 169 38.825 -1.452 88.572 1.00 52.78 C ANISOU 1146 CH2 TRP A 169 5798 6355 7901 -1100 989 -1698 C ATOM 1147 N ALA A 170 38.089 -6.219 82.029 1.00 48.81 N ANISOU 1147 N ALA A 170 6217 5502 6827 -930 1291 -1138 N ATOM 1148 CA ALA A 170 37.331 -6.311 80.788 1.00 47.20 C ANISOU 1148 CA ALA A 170 6406 5126 6400 -905 1336 -955 C ATOM 1149 C ALA A 170 35.963 -6.959 81.042 1.00 49.61 C ANISOU 1149 C ALA A 170 6774 5512 6565 -707 1000 -742 C ATOM 1150 O ALA A 170 34.967 -6.480 80.515 1.00 49.46 O ANISOU 1150 O ALA A 170 7055 5367 6370 -657 947 -585 O ATOM 1151 CB ALA A 170 38.115 -7.101 79.748 1.00 47.52 C ANISOU 1151 CB ALA A 170 6496 5108 6451 -973 1531 -1025 C ATOM 1152 N VAL A 171 35.905 -8.021 81.868 1.00 45.67 N ANISOU 1152 N VAL A 171 5997 5212 6143 -592 777 -751 N ATOM 1153 CA VAL A 171 34.649 -8.725 82.163 1.00 44.99 C ANISOU 1153 CA VAL A 171 5944 5203 5946 -427 489 -577 C ATOM 1154 C VAL A 171 33.730 -7.836 83.034 1.00 48.57 C ANISOU 1154 C VAL A 171 6401 5672 6380 -376 351 -506 C ATOM 1155 O VAL A 171 32.589 -7.576 82.633 1.00 48.53 O ANISOU 1155 O VAL A 171 6610 5591 6240 -306 250 -358 O ATOM 1156 CB VAL A 171 34.870 -10.165 82.739 1.00 48.16 C ANISOU 1156 CB VAL A 171 6103 5781 6416 -327 324 -608 C ATOM 1157 CG1 VAL A 171 33.564 -10.797 83.216 1.00 47.39 C ANISOU 1157 CG1 VAL A 171 6027 5756 6224 -185 59 -453 C ATOM 1158 CG2 VAL A 171 35.553 -11.067 81.724 1.00 47.65 C ANISOU 1158 CG2 VAL A 171 6085 5679 6339 -356 448 -648 C ATOM 1159 N SER A 172 34.239 -7.341 84.179 1.00 43.96 N ANISOU 1159 N SER A 172 5588 5178 5936 -408 350 -624 N ATOM 1160 CA SER A 172 33.483 -6.458 85.075 1.00 44.76 C ANISOU 1160 CA SER A 172 5684 5291 6033 -371 247 -577 C ATOM 1161 C SER A 172 32.953 -5.195 84.375 1.00 49.72 C ANISOU 1161 C SER A 172 6608 5730 6553 -419 364 -500 C ATOM 1162 O SER A 172 31.798 -4.823 84.580 1.00 48.74 O ANISOU 1162 O SER A 172 6588 5584 6348 -324 221 -378 O ATOM 1163 CB SER A 172 34.327 -6.080 86.279 1.00 49.26 C ANISOU 1163 CB SER A 172 5985 5966 6764 -418 258 -744 C ATOM 1164 OG SER A 172 34.707 -7.248 86.989 1.00 58.80 O ANISOU 1164 OG SER A 172 6960 7338 8044 -332 108 -805 O ATOM 1165 N LEU A 173 33.769 -4.577 83.503 1.00 47.78 N ANISOU 1165 N LEU A 173 6518 5336 6300 -559 628 -576 N ATOM 1166 CA LEU A 173 33.336 -3.405 82.745 1.00 47.68 C ANISOU 1166 CA LEU A 173 6854 5109 6155 -599 758 -504 C ATOM 1167 C LEU A 173 32.168 -3.729 81.782 1.00 51.37 C ANISOU 1167 C LEU A 173 7617 5481 6421 -465 618 -318 C ATOM 1168 O LEU A 173 31.229 -2.947 81.694 1.00 52.66 O ANISOU 1168 O LEU A 173 7988 5545 6477 -387 540 -218 O ATOM 1169 CB LEU A 173 34.511 -2.714 82.024 1.00 47.82 C ANISOU 1169 CB LEU A 173 7004 4964 6201 -797 1111 -639 C ATOM 1170 CG LEU A 173 35.572 -1.977 82.899 1.00 53.04 C ANISOU 1170 CG LEU A 173 7424 5671 7059 -952 1279 -847 C ATOM 1171 CD1 LEU A 173 36.773 -1.551 82.061 1.00 53.25 C ANISOU 1171 CD1 LEU A 173 7549 5543 7138 -1165 1654 -1007 C ATOM 1172 CD2 LEU A 173 34.989 -0.750 83.634 1.00 53.84 C ANISOU 1172 CD2 LEU A 173 7595 5723 7138 -942 1240 -812 C ATOM 1173 N ALA A 174 32.190 -4.900 81.135 1.00 46.74 N ANISOU 1173 N ALA A 174 7031 4934 5792 -425 562 -283 N ATOM 1174 CA ALA A 174 31.163 -5.358 80.192 1.00 46.16 C ANISOU 1174 CA ALA A 174 7212 4786 5541 -303 413 -134 C ATOM 1175 C ALA A 174 29.843 -5.842 80.842 1.00 50.36 C ANISOU 1175 C ALA A 174 7615 5452 6069 -136 95 -33 C ATOM 1176 O ALA A 174 28.786 -5.343 80.472 1.00 50.99 O ANISOU 1176 O ALA A 174 7897 5442 6034 -32 -32 64 O ATOM 1177 CB ALA A 174 31.733 -6.434 79.283 1.00 46.67 C ANISOU 1177 CB ALA A 174 7322 4839 5570 -339 491 -150 C ATOM 1178 N ILE A 175 29.899 -6.775 81.817 1.00 46.60 N ANISOU 1178 N ILE A 175 6814 5175 5718 -109 -26 -69 N ATOM 1179 CA ILE A 175 28.719 -7.355 82.482 1.00 46.30 C ANISOU 1179 CA ILE A 175 6642 5259 5692 19 -282 4 C ATOM 1180 C ILE A 175 27.895 -6.337 83.314 1.00 48.43 C ANISOU 1180 C ILE A 175 6880 5530 5990 76 -369 30 C ATOM 1181 O ILE A 175 26.734 -6.625 83.633 1.00 47.89 O ANISOU 1181 O ILE A 175 6760 5518 5917 183 -560 91 O ATOM 1182 CB ILE A 175 29.061 -8.632 83.326 1.00 49.55 C ANISOU 1182 CB ILE A 175 6768 5852 6205 29 -358 -44 C ATOM 1183 CG1 ILE A 175 29.815 -8.283 84.636 1.00 49.52 C ANISOU 1183 CG1 ILE A 175 6525 5949 6342 -17 -310 -151 C ATOM 1184 CG2 ILE A 175 29.810 -9.718 82.477 1.00 48.72 C ANISOU 1184 CG2 ILE A 175 6695 5744 6070 -7 -282 -68 C ATOM 1185 CD1 ILE A 175 30.028 -9.508 85.579 1.00 49.44 C ANISOU 1185 CD1 ILE A 175 6282 6102 6403 32 -421 -191 C ATOM 1186 N MET A 176 28.479 -5.164 83.642 1.00 42.98 N ANISOU 1186 N MET A 176 6222 4771 5336 -2 -217 -28 N ATOM 1187 CA MET A 176 27.810 -4.127 84.437 1.00 42.05 C ANISOU 1187 CA MET A 176 6092 4641 5245 43 -271 -12 C ATOM 1188 C MET A 176 27.150 -3.033 83.596 1.00 48.17 C ANISOU 1188 C MET A 176 7191 5224 5888 99 -258 60 C ATOM 1189 O MET A 176 26.445 -2.193 84.156 1.00 48.40 O ANISOU 1189 O MET A 176 7231 5230 5929 163 -321 82 O ATOM 1190 CB MET A 176 28.733 -3.527 85.513 1.00 43.26 C ANISOU 1190 CB MET A 176 6065 4848 5523 -62 -147 -127 C ATOM 1191 CG MET A 176 29.074 -4.506 86.626 1.00 45.44 C ANISOU 1191 CG MET A 176 6034 5316 5915 -56 -236 -190 C ATOM 1192 SD MET A 176 27.631 -5.367 87.335 1.00 48.51 S ANISOU 1192 SD MET A 176 6310 5821 6300 92 -486 -97 S ATOM 1193 CE MET A 176 28.451 -6.541 88.357 1.00 45.45 C ANISOU 1193 CE MET A 176 5668 5600 6002 78 -524 -184 C ATOM 1194 N VAL A 177 27.304 -3.092 82.258 1.00 45.63 N ANISOU 1194 N VAL A 177 7151 4758 5428 95 -194 100 N ATOM 1195 CA VAL A 177 26.645 -2.186 81.319 1.00 45.93 C ANISOU 1195 CA VAL A 177 7561 4592 5300 183 -213 175 C ATOM 1196 C VAL A 177 25.082 -2.288 81.465 1.00 51.30 C ANISOU 1196 C VAL A 177 8210 5320 5960 383 -513 250 C ATOM 1197 O VAL A 177 24.464 -1.223 81.555 1.00 52.03 O ANISOU 1197 O VAL A 177 8446 5313 6010 470 -556 277 O ATOM 1198 CB VAL A 177 27.164 -2.340 79.849 1.00 49.27 C ANISOU 1198 CB VAL A 177 8327 4837 5557 140 -80 198 C ATOM 1199 CG1 VAL A 177 26.333 -1.506 78.873 1.00 47.88 C ANISOU 1199 CG1 VAL A 177 8578 4440 5174 276 -156 284 C ATOM 1200 CG2 VAL A 177 28.636 -1.951 79.750 1.00 48.95 C ANISOU 1200 CG2 VAL A 177 8321 4720 5557 -68 255 96 C ATOM 1201 N PRO A 178 24.425 -3.495 81.565 1.00 48.56 N ANISOU 1201 N PRO A 178 7665 5123 5663 453 -709 268 N ATOM 1202 CA PRO A 178 22.956 -3.526 81.770 1.00 48.46 C ANISOU 1202 CA PRO A 178 7580 5159 5671 622 -968 301 C ATOM 1203 C PRO A 178 22.493 -2.708 82.980 1.00 52.15 C ANISOU 1203 C PRO A 178 7881 5679 6255 654 -986 276 C ATOM 1204 O PRO A 178 21.433 -2.082 82.915 1.00 51.23 O ANISOU 1204 O PRO A 178 7833 5511 6122 800 -1134 296 O ATOM 1205 CB PRO A 178 22.667 -5.018 81.988 1.00 49.95 C ANISOU 1205 CB PRO A 178 7520 5519 5938 618 -1086 288 C ATOM 1206 CG PRO A 178 23.745 -5.700 81.298 1.00 53.80 C ANISOU 1206 CG PRO A 178 8099 5981 6363 510 -947 285 C ATOM 1207 CD PRO A 178 24.955 -4.873 81.468 1.00 49.61 C ANISOU 1207 CD PRO A 178 7637 5375 5837 383 -698 246 C ATOM 1208 N GLN A 179 23.314 -2.693 84.060 1.00 49.68 N ANISOU 1208 N GLN A 179 7360 5460 6055 526 -840 223 N ATOM 1209 CA GLN A 179 23.079 -1.936 85.290 1.00 50.73 C ANISOU 1209 CA GLN A 179 7345 5638 6291 528 -823 192 C ATOM 1210 C GLN A 179 23.065 -0.448 84.992 1.00 58.14 C ANISOU 1210 C GLN A 179 8541 6398 7150 557 -741 208 C ATOM 1211 O GLN A 179 22.145 0.248 85.445 1.00 59.26 O ANISOU 1211 O GLN A 179 8672 6522 7322 667 -835 218 O ATOM 1212 CB GLN A 179 24.144 -2.263 86.369 1.00 51.85 C ANISOU 1212 CB GLN A 179 7259 5899 6542 385 -690 120 C ATOM 1213 CG GLN A 179 23.907 -1.582 87.722 1.00 55.30 C ANISOU 1213 CG GLN A 179 7548 6387 7076 384 -680 83 C ATOM 1214 CD GLN A 179 22.595 -1.988 88.378 1.00 71.35 C ANISOU 1214 CD GLN A 179 9424 8509 9178 497 -847 103 C ATOM 1215 OE1 GLN A 179 22.265 -3.170 88.489 1.00 69.09 O ANISOU 1215 OE1 GLN A 179 8997 8328 8926 511 -935 104 O ATOM 1216 NE2 GLN A 179 21.824 -1.016 88.849 1.00 57.94 N ANISOU 1216 NE2 GLN A 179 7746 6762 7507 572 -876 107 N ATOM 1217 N ALA A 180 24.068 0.041 84.211 1.00 54.42 N ANISOU 1217 N ALA A 180 8317 5782 6577 458 -552 202 N ATOM 1218 CA ALA A 180 24.159 1.456 83.831 1.00 53.35 C ANISOU 1218 CA ALA A 180 8493 5440 6338 467 -433 216 C ATOM 1219 C ALA A 180 22.953 1.854 82.991 1.00 56.41 C ANISOU 1219 C ALA A 180 9142 5699 6593 679 -626 293 C ATOM 1220 O ALA A 180 22.387 2.920 83.206 1.00 57.38 O ANISOU 1220 O ALA A 180 9392 5723 6687 778 -658 309 O ATOM 1221 CB ALA A 180 25.448 1.724 83.076 1.00 53.92 C ANISOU 1221 CB ALA A 180 8785 5373 6329 301 -167 181 C ATOM 1222 N ALA A 181 22.528 0.963 82.086 1.00 51.81 N ANISOU 1222 N ALA A 181 8621 5126 5937 761 -777 331 N ATOM 1223 CA ALA A 181 21.394 1.121 81.166 1.00 50.85 C ANISOU 1223 CA ALA A 181 8733 4899 5687 980 -1011 384 C ATOM 1224 C ALA A 181 20.044 1.376 81.848 1.00 55.05 C ANISOU 1224 C ALA A 181 9072 5516 6328 1162 -1247 371 C ATOM 1225 O ALA A 181 19.298 2.221 81.369 1.00 55.96 O ANISOU 1225 O ALA A 181 9429 5488 6344 1345 -1375 394 O ATOM 1226 CB ALA A 181 21.301 -0.094 80.247 1.00 51.04 C ANISOU 1226 CB ALA A 181 8781 4964 5649 1001 -1126 403 C ATOM 1227 N VAL A 182 19.724 0.660 82.953 1.00 50.78 N ANISOU 1227 N VAL A 182 8115 5193 5986 1118 -1298 325 N ATOM 1228 CA VAL A 182 18.438 0.825 83.639 1.00 49.77 C ANISOU 1228 CA VAL A 182 7775 5149 5987 1268 -1487 291 C ATOM 1229 C VAL A 182 18.402 2.071 84.571 1.00 53.33 C ANISOU 1229 C VAL A 182 8224 5549 6491 1275 -1384 278 C ATOM 1230 O VAL A 182 17.316 2.486 84.957 1.00 52.18 O ANISOU 1230 O VAL A 182 7986 5417 6423 1429 -1529 250 O ATOM 1231 CB VAL A 182 17.936 -0.466 84.367 1.00 53.52 C ANISOU 1231 CB VAL A 182 7851 5845 6638 1229 -1578 241 C ATOM 1232 CG1 VAL A 182 17.686 -1.600 83.375 1.00 52.77 C ANISOU 1232 CG1 VAL A 182 7777 5783 6490 1261 -1723 247 C ATOM 1233 CG2 VAL A 182 18.872 -0.916 85.494 1.00 53.41 C ANISOU 1233 CG2 VAL A 182 7616 5955 6723 1031 -1382 220 C ATOM 1234 N MET A 183 19.561 2.658 84.936 1.00 50.43 N ANISOU 1234 N MET A 183 7945 5124 6093 1110 -1136 281 N ATOM 1235 CA MET A 183 19.619 3.807 85.850 1.00 49.37 C ANISOU 1235 CA MET A 183 7813 4940 6005 1093 -1023 261 C ATOM 1236 C MET A 183 19.044 5.038 85.210 1.00 57.74 C ANISOU 1236 C MET A 183 9214 5791 6935 1267 -1080 296 C ATOM 1237 O MET A 183 19.419 5.392 84.087 1.00 57.01 O ANISOU 1237 O MET A 183 9485 5517 6658 1288 -1036 340 O ATOM 1238 CB MET A 183 21.044 4.088 86.334 1.00 50.93 C ANISOU 1238 CB MET A 183 8017 5126 6207 864 -752 232 C ATOM 1239 CG MET A 183 21.694 2.928 87.057 1.00 54.17 C ANISOU 1239 CG MET A 183 8104 5737 6742 714 -708 185 C ATOM 1240 SD MET A 183 20.719 2.239 88.419 1.00 57.74 S ANISOU 1240 SD MET A 183 8170 6395 7374 773 -851 152 S ATOM 1241 CE MET A 183 20.651 3.662 89.553 1.00 53.71 C ANISOU 1241 CE MET A 183 7675 5822 6913 765 -743 120 C ATOM 1242 N GLU A 184 18.109 5.674 85.920 1.00 58.00 N ANISOU 1242 N GLU A 184 9147 5835 7056 1401 -1173 274 N ATOM 1243 CA GLU A 184 17.428 6.872 85.474 1.00 59.66 C ANISOU 1243 CA GLU A 184 9653 5854 7161 1605 -1257 296 C ATOM 1244 C GLU A 184 17.304 7.877 86.597 1.00 65.17 C ANISOU 1244 C GLU A 184 10286 6533 7945 1596 -1149 268 C ATOM 1245 O GLU A 184 17.071 7.508 87.748 1.00 63.47 O ANISOU 1245 O GLU A 184 9719 6487 7908 1535 -1137 219 O ATOM 1246 CB GLU A 184 16.048 6.521 84.903 1.00 61.64 C ANISOU 1246 CB GLU A 184 9848 6135 7437 1867 -1578 278 C ATOM 1247 CG GLU A 184 16.116 5.676 83.644 1.00 76.82 C ANISOU 1247 CG GLU A 184 12203 7854 9131 2038 -1710 328 C ATOM 1248 CD GLU A 184 16.891 6.285 82.492 1.00100.36 C ANISOU 1248 CD GLU A 184 15311 10829 11994 1921 -1671 367 C ATOM 1249 OE1 GLU A 184 17.357 7.436 82.641 1.00101.11 O ANISOU 1249 OE1 GLU A 184 15775 10740 11902 1822 -1474 419 O ATOM 1250 OE2 GLU A 184 17.033 5.616 81.443 1.00 94.60 O ANISOU 1250 OE2 GLU A 184 14319 10268 11358 1919 -1818 337 O ATOM 1251 N CYS A 185 17.485 9.155 86.245 1.00 65.35 N ANISOU 1251 N CYS A 185 10682 6328 7819 1653 -1056 300 N ATOM 1252 CA CYS A 185 17.381 10.317 87.124 1.00 66.62 C ANISOU 1252 CA CYS A 185 10882 6413 8017 1664 -945 281 C ATOM 1253 C CYS A 185 15.992 10.913 86.886 1.00 74.15 C ANISOU 1253 C CYS A 185 11917 7289 8966 1982 -1188 278 C ATOM 1254 O CYS A 185 15.722 11.425 85.795 1.00 73.73 O ANISOU 1254 O CYS A 185 12245 7041 8730 2162 -1291 320 O ATOM 1255 CB CYS A 185 18.486 11.312 86.793 1.00 66.99 C ANISOU 1255 CB CYS A 185 11317 6241 7897 1521 -678 307 C ATOM 1256 SG CYS A 185 18.881 12.449 88.135 1.00 70.83 S ANISOU 1256 SG CYS A 185 11757 6693 8463 1387 -449 259 S ATOM 1257 N SER A 186 15.086 10.762 87.857 1.00 74.28 N ANISOU 1257 N SER A 186 11579 7459 9187 2062 -1291 216 N ATOM 1258 CA SER A 186 13.706 11.222 87.703 1.00 76.37 C ANISOU 1258 CA SER A 186 11833 7682 9500 2370 -1534 179 C ATOM 1259 C SER A 186 13.367 12.387 88.623 1.00 84.10 C ANISOU 1259 C SER A 186 12830 8586 10537 2433 -1443 153 C ATOM 1260 O SER A 186 13.592 12.292 89.829 1.00 83.64 O ANISOU 1260 O SER A 186 12504 8650 10626 2271 -1291 116 O ATOM 1261 CB SER A 186 12.735 10.071 87.944 1.00 81.78 C ANISOU 1261 CB SER A 186 12085 8593 10395 2439 -1740 100 C ATOM 1262 OG SER A 186 13.103 8.922 87.200 1.00 97.76 O ANISOU 1262 OG SER A 186 14074 10697 12372 2359 -1809 122 O ATOM 1263 N SER A 187 12.778 13.462 88.062 1.00 83.96 N ANISOU 1263 N SER A 187 13141 8360 10398 2689 -1551 167 N ATOM 1264 CA SER A 187 12.376 14.649 88.826 1.00 85.28 C ANISOU 1264 CA SER A 187 13372 8426 10603 2788 -1480 143 C ATOM 1265 C SER A 187 11.137 14.413 89.715 1.00 91.61 C ANISOU 1265 C SER A 187 13740 9396 11672 2929 -1620 37 C ATOM 1266 O SER A 187 10.979 15.108 90.725 1.00 91.98 O ANISOU 1266 O SER A 187 13708 9432 11809 2907 -1487 6 O ATOM 1267 CB SER A 187 12.171 15.847 87.904 1.00 89.65 C ANISOU 1267 CB SER A 187 14450 8687 10925 3033 -1553 191 C ATOM 1268 OG SER A 187 12.159 17.066 88.633 1.00101.95 O ANISOU 1268 OG SER A 187 16153 10110 12472 3056 -1399 189 O ATOM 1269 N VAL A 188 10.265 13.440 89.343 1.00 88.93 N ANISOU 1269 N VAL A 188 13121 9206 11464 3063 -1872 -32 N ATOM 1270 CA VAL A 188 9.043 13.094 90.092 1.00134.71 C ANISOU 1270 CA VAL A 188 18478 15166 17541 3182 -1993 -162 C ATOM 1271 C VAL A 188 8.592 11.647 89.797 1.00154.47 C ANISOU 1271 C VAL A 188 20630 17874 20187 3153 -2156 -231 C ATOM 1272 O VAL A 188 8.813 11.127 88.704 1.00113.84 O ANISOU 1272 O VAL A 188 15633 12709 14910 3182 -2296 -190 O ATOM 1273 CB VAL A 188 7.890 14.140 89.917 1.00139.00 C ANISOU 1273 CB VAL A 188 19113 15581 18120 3542 -2187 -234 C ATOM 1274 CG1 VAL A 188 7.215 14.047 88.545 1.00138.86 C ANISOU 1274 CG1 VAL A 188 19252 15494 18016 3848 -2539 -264 C ATOM 1275 CG2 VAL A 188 6.865 14.046 91.048 1.00138.80 C ANISOU 1275 CG2 VAL A 188 18642 15698 18399 3588 -2174 -374 C ATOM 1276 N ARG A 197 9.587 22.172 96.375 1.00 98.79 N ANISOU 1276 N ARG A 197 15073 9605 12859 3189 -606 -153 N ATOM 1277 CA ARG A 197 10.974 22.043 95.919 1.00 98.49 C ANISOU 1277 CA ARG A 197 15279 9517 12627 2918 -461 -66 C ATOM 1278 C ARG A 197 11.165 20.713 95.158 1.00101.26 C ANISOU 1278 C ARG A 197 15442 10035 12996 2855 -609 -48 C ATOM 1279 O ARG A 197 11.015 19.632 95.747 1.00100.63 O ANISOU 1279 O ARG A 197 14951 10188 13095 2738 -630 -97 O ATOM 1280 CB ARG A 197 11.969 22.166 97.099 1.00 99.99 C ANISOU 1280 CB ARG A 197 15407 9753 12833 2577 -173 -76 C ATOM 1281 CG ARG A 197 12.019 23.554 97.746 1.00113.15 C ANISOU 1281 CG ARG A 197 17179 11291 14520 2623 -26 -111 C ATOM 1282 CD ARG A 197 13.035 23.668 98.870 1.00125.69 C ANISOU 1282 CD ARG A 197 18987 12780 15989 2327 252 -97 C ATOM 1283 NE ARG A 197 12.980 24.996 99.489 1.00138.63 N ANISOU 1283 NE ARG A 197 21022 14151 17502 2449 356 -82 N ATOM 1284 CZ ARG A 197 13.664 25.365 100.570 1.00149.65 C ANISOU 1284 CZ ARG A 197 22653 15412 18797 2236 604 -88 C ATOM 1285 NH1 ARG A 197 14.464 24.500 101.186 1.00136.63 N ANISOU 1285 NH1 ARG A 197 20864 13881 17169 1897 758 -122 N ATOM 1286 NH2 ARG A 197 13.550 26.599 101.045 1.00129.83 N ANISOU 1286 NH2 ARG A 197 20520 12642 16165 2368 693 -74 N ATOM 1287 N ALA A 198 11.468 20.804 93.837 1.00 96.52 N ANISOU 1287 N ALA A 198 15176 9298 12198 2939 -704 21 N ATOM 1288 CA ALA A 198 11.650 19.650 92.942 1.00 95.37 C ANISOU 1288 CA ALA A 198 14932 9271 12033 2906 -851 45 C ATOM 1289 C ALA A 198 12.978 18.926 93.179 1.00 96.06 C ANISOU 1289 C ALA A 198 14934 9469 12097 2532 -650 74 C ATOM 1290 O ALA A 198 14.034 19.568 93.197 1.00 96.41 O ANISOU 1290 O ALA A 198 15255 9376 12000 2340 -422 109 O ATOM 1291 CB ALA A 198 11.534 20.090 91.488 1.00 96.18 C ANISOU 1291 CB ALA A 198 15479 9157 11909 3131 -1006 107 C ATOM 1292 N PHE A 199 12.929 17.594 93.375 1.00 88.90 N ANISOU 1292 N PHE A 199 13639 8804 11334 2431 -728 44 N ATOM 1293 CA PHE A 199 14.141 16.819 93.637 1.00 86.91 C ANISOU 1293 CA PHE A 199 13273 8674 11076 2108 -569 57 C ATOM 1294 C PHE A 199 14.266 15.551 92.783 1.00 87.29 C ANISOU 1294 C PHE A 199 13198 8848 11120 2085 -711 78 C ATOM 1295 O PHE A 199 13.331 14.747 92.702 1.00 87.29 O ANISOU 1295 O PHE A 199 12931 8986 11251 2224 -911 41 O ATOM 1296 CB PHE A 199 14.280 16.498 95.136 1.00 88.38 C ANISOU 1296 CB PHE A 199 13124 9026 11430 1929 -440 -4 C ATOM 1297 CG PHE A 199 13.279 15.514 95.694 1.00 89.53 C ANISOU 1297 CG PHE A 199 12859 9375 11782 2007 -576 -64 C ATOM 1298 CD1 PHE A 199 12.028 15.938 96.123 1.00 92.23 C ANISOU 1298 CD1 PHE A 199 13085 9705 12255 2222 -657 -122 C ATOM 1299 CD2 PHE A 199 13.601 14.168 95.823 1.00 90.90 C ANISOU 1299 CD2 PHE A 199 12766 9743 12028 1857 -600 -75 C ATOM 1300 CE1 PHE A 199 11.108 15.028 96.645 1.00 92.74 C ANISOU 1300 CE1 PHE A 199 12765 9945 12526 2268 -743 -200 C ATOM 1301 CE2 PHE A 199 12.681 13.262 96.348 1.00 93.44 C ANISOU 1301 CE2 PHE A 199 12736 10231 12537 1908 -690 -139 C ATOM 1302 CZ PHE A 199 11.442 13.698 96.755 1.00 91.53 C ANISOU 1302 CZ PHE A 199 12375 9971 12431 2102 -750 -206 C ATOM 1303 N SER A 200 15.438 15.374 92.162 1.00 80.27 N ANISOU 1303 N SER A 200 12499 7907 10092 1897 -590 123 N ATOM 1304 CA SER A 200 15.722 14.198 91.346 1.00 78.53 C ANISOU 1304 CA SER A 200 12197 7791 9850 1848 -689 146 C ATOM 1305 C SER A 200 16.050 12.979 92.210 1.00 77.92 C ANISOU 1305 C SER A 200 11704 7968 9936 1654 -658 103 C ATOM 1306 O SER A 200 16.553 13.119 93.326 1.00 77.13 O ANISOU 1306 O SER A 200 11471 7929 9906 1485 -499 65 O ATOM 1307 CB SER A 200 16.862 14.479 90.372 1.00 82.18 C ANISOU 1307 CB SER A 200 13028 8088 10109 1716 -542 197 C ATOM 1308 OG SER A 200 16.398 15.122 89.196 1.00 93.08 O ANISOU 1308 OG SER A 200 14814 9245 11307 1940 -647 250 O ATOM 1309 N VAL A 201 15.720 11.785 91.705 1.00 71.80 N ANISOU 1309 N VAL A 201 10740 7329 9210 1692 -819 104 N ATOM 1310 CA VAL A 201 16.042 10.508 92.349 1.00 70.26 C ANISOU 1310 CA VAL A 201 10202 7355 9140 1523 -800 71 C ATOM 1311 C VAL A 201 16.710 9.593 91.336 1.00 71.46 C ANISOU 1311 C VAL A 201 10405 7541 9207 1442 -834 108 C ATOM 1312 O VAL A 201 16.286 9.524 90.177 1.00 71.21 O ANISOU 1312 O VAL A 201 10537 7433 9086 1592 -982 143 O ATOM 1313 CB VAL A 201 14.903 9.800 93.140 1.00 73.21 C ANISOU 1313 CB VAL A 201 10214 7893 9710 1609 -917 10 C ATOM 1314 CG1 VAL A 201 14.428 10.643 94.319 1.00 72.60 C ANISOU 1314 CG1 VAL A 201 10072 7789 9724 1639 -826 -36 C ATOM 1315 CG2 VAL A 201 13.739 9.399 92.239 1.00 72.99 C ANISOU 1315 CG2 VAL A 201 10132 7878 9721 1836 -1163 -6 C ATOM 1316 N CYS A 202 17.785 8.943 91.758 1.00 65.25 N ANISOU 1316 N CYS A 202 9499 6855 8437 1216 -700 94 N ATOM 1317 CA CYS A 202 18.512 8.012 90.913 1.00 64.08 C ANISOU 1317 CA CYS A 202 9371 6751 8225 1120 -706 118 C ATOM 1318 C CYS A 202 18.061 6.603 91.332 1.00 65.08 C ANISOU 1318 C CYS A 202 9160 7086 8480 1113 -824 93 C ATOM 1319 O CYS A 202 18.258 6.192 92.478 1.00 64.59 O ANISOU 1319 O CYS A 202 8874 7148 8519 1007 -760 50 O ATOM 1320 CB CYS A 202 20.015 8.203 91.079 1.00 64.57 C ANISOU 1320 CB CYS A 202 9507 6787 8239 886 -485 94 C ATOM 1321 SG CYS A 202 21.027 7.278 89.900 1.00 68.52 S ANISOU 1321 SG CYS A 202 10093 7292 8650 769 -444 113 S ATOM 1322 N ASP A 203 17.362 5.925 90.422 1.00 58.90 N ANISOU 1322 N ASP A 203 8368 6326 7686 1240 -1003 113 N ATOM 1323 CA ASP A 203 16.820 4.598 90.611 1.00 57.57 C ANISOU 1323 CA ASP A 203 7917 6327 7628 1242 -1118 84 C ATOM 1324 C ASP A 203 16.739 3.871 89.268 1.00 57.74 C ANISOU 1324 C ASP A 203 8035 6338 7565 1300 -1254 118 C ATOM 1325 O ASP A 203 16.833 4.497 88.212 1.00 55.51 O ANISOU 1325 O ASP A 203 8049 5903 7141 1386 -1290 162 O ATOM 1326 CB ASP A 203 15.431 4.667 91.297 1.00 59.98 C ANISOU 1326 CB ASP A 203 8011 6690 8089 1381 -1224 26 C ATOM 1327 CG ASP A 203 14.995 3.377 91.998 1.00 77.16 C ANISOU 1327 CG ASP A 203 9869 9041 10408 1315 -1245 -28 C ATOM 1328 OD1 ASP A 203 15.797 2.395 92.018 1.00 77.58 O ANISOU 1328 OD1 ASP A 203 9869 9176 10431 1171 -1191 -11 O ATOM 1329 OD2 ASP A 203 13.859 3.346 92.533 1.00 86.20 O ANISOU 1329 OD2 ASP A 203 10825 10230 11697 1405 -1302 -96 O ATOM 1330 N GLU A 204 16.589 2.538 89.322 1.00 53.44 N ANISOU 1330 N GLU A 204 7269 5941 7094 1249 -1318 96 N ATOM 1331 CA GLU A 204 16.454 1.682 88.152 1.00 52.55 C ANISOU 1331 CA GLU A 204 7211 5838 6917 1293 -1453 117 C ATOM 1332 C GLU A 204 15.070 1.861 87.533 1.00 56.16 C ANISOU 1332 C GLU A 204 7667 6262 7408 1518 -1689 83 C ATOM 1333 O GLU A 204 14.075 1.982 88.252 1.00 56.43 O ANISOU 1333 O GLU A 204 7487 6359 7597 1598 -1750 14 O ATOM 1334 CB GLU A 204 16.630 0.209 88.544 1.00 53.16 C ANISOU 1334 CB GLU A 204 7041 6082 7077 1171 -1442 92 C ATOM 1335 CG GLU A 204 17.995 -0.168 89.072 1.00 52.00 C ANISOU 1335 CG GLU A 204 6876 5982 6899 978 -1257 107 C ATOM 1336 CD GLU A 204 18.105 -1.614 89.508 1.00 64.77 C ANISOU 1336 CD GLU A 204 8281 7746 8582 888 -1260 83 C ATOM 1337 OE1 GLU A 204 17.121 -2.369 89.336 1.00 53.98 O ANISOU 1337 OE1 GLU A 204 6787 6441 7283 953 -1387 56 O ATOM 1338 OE2 GLU A 204 19.181 -1.995 90.021 1.00 53.95 O ANISOU 1338 OE2 GLU A 204 6876 6424 7197 756 -1137 80 O ATOM 1339 N ARG A 205 15.006 1.854 86.210 1.00 51.95 N ANISOU 1339 N ARG A 205 7369 5632 6735 1622 -1822 117 N ATOM 1340 CA ARG A 205 13.756 1.981 85.479 1.00 52.78 C ANISOU 1340 CA ARG A 205 7497 5701 6855 1860 -2091 71 C ATOM 1341 C ARG A 205 13.504 0.670 84.740 1.00 58.06 C ANISOU 1341 C ARG A 205 8072 6460 7529 1851 -2237 47 C ATOM 1342 O ARG A 205 14.357 0.202 83.976 1.00 58.30 O ANISOU 1342 O ARG A 205 8291 6449 7412 1761 -2183 112 O ATOM 1343 CB ARG A 205 13.766 3.192 84.533 1.00 52.77 C ANISOU 1343 CB ARG A 205 7912 5479 6660 2033 -2162 123 C ATOM 1344 CG ARG A 205 12.493 3.345 83.708 1.00 70.06 C ANISOU 1344 CG ARG A 205 10152 7621 8847 2319 -2486 63 C ATOM 1345 CD ARG A 205 12.300 4.777 83.240 1.00 95.34 C ANISOU 1345 CD ARG A 205 13725 10603 11896 2525 -2545 97 C ATOM 1346 NE ARG A 205 11.803 5.635 84.320 1.00112.92 N ANISOU 1346 NE ARG A 205 15786 12846 14272 2583 -2494 48 N ATOM 1347 CZ ARG A 205 11.919 6.958 84.351 1.00128.74 C ANISOU 1347 CZ ARG A 205 18078 14669 16167 2684 -2431 88 C ATOM 1348 NH1 ARG A 205 11.430 7.648 85.372 1.00117.25 N ANISOU 1348 NH1 ARG A 205 16448 13241 14862 2732 -2383 36 N ATOM 1349 NH2 ARG A 205 12.526 7.602 83.360 1.00114.39 N ANISOU 1349 NH2 ARG A 205 16750 12629 14084 2731 -2397 177 N ATOM 1350 N TRP A 206 12.330 0.081 85.004 1.00 53.95 N ANISOU 1350 N TRP A 206 7248 6060 7190 1933 -2403 -60 N ATOM 1351 CA TRP A 206 11.883 -1.190 84.472 1.00 53.06 C ANISOU 1351 CA TRP A 206 6983 6050 7129 1921 -2546 -115 C ATOM 1352 C TRP A 206 10.559 -1.053 83.728 1.00 61.97 C ANISOU 1352 C TRP A 206 8069 7162 8315 2167 -2863 -222 C ATOM 1353 O TRP A 206 9.570 -0.589 84.296 1.00 62.79 O ANISOU 1353 O TRP A 206 7964 7301 8593 2286 -2943 -326 O ATOM 1354 CB TRP A 206 11.797 -2.224 85.606 1.00 50.17 C ANISOU 1354 CB TRP A 206 6255 5857 6951 1737 -2407 -173 C ATOM 1355 CG TRP A 206 13.124 -2.531 86.240 1.00 49.74 C ANISOU 1355 CG TRP A 206 6244 5826 6829 1519 -2147 -84 C ATOM 1356 CD1 TRP A 206 13.557 -2.135 87.473 1.00 52.21 C ANISOU 1356 CD1 TRP A 206 6471 6164 7202 1415 -1949 -73 C ATOM 1357 CD2 TRP A 206 14.200 -3.294 85.662 1.00 48.96 C ANISOU 1357 CD2 TRP A 206 6283 5726 6593 1392 -2071 -9 C ATOM 1358 NE1 TRP A 206 14.829 -2.616 87.710 1.00 50.91 N ANISOU 1358 NE1 TRP A 206 6368 6023 6953 1241 -1776 -7 N ATOM 1359 CE2 TRP A 206 15.250 -3.328 86.613 1.00 51.92 C ANISOU 1359 CE2 TRP A 206 6624 6137 6968 1224 -1840 31 C ATOM 1360 CE3 TRP A 206 14.367 -3.983 84.445 1.00 49.45 C ANISOU 1360 CE3 TRP A 206 6491 5761 6538 1409 -2181 16 C ATOM 1361 CZ2 TRP A 206 16.450 -4.017 86.383 1.00 50.10 C ANISOU 1361 CZ2 TRP A 206 6474 5921 6641 1083 -1720 86 C ATOM 1362 CZ3 TRP A 206 15.558 -4.667 84.221 1.00 50.19 C ANISOU 1362 CZ3 TRP A 206 6680 5863 6529 1256 -2037 82 C ATOM 1363 CH2 TRP A 206 16.583 -4.673 85.180 1.00 50.47 C ANISOU 1363 CH2 TRP A 206 6654 5939 6583 1100 -1812 111 C ATOM 1364 N ALA A 207 10.542 -1.472 82.458 1.00 61.63 N ANISOU 1364 N ALA A 207 8222 7066 8131 2250 -3050 -210 N ATOM 1365 CA ALA A 207 9.355 -1.462 81.603 1.00 62.74 C ANISOU 1365 CA ALA A 207 8344 7190 8305 2497 -3397 -325 C ATOM 1366 C ALA A 207 8.311 -2.499 82.058 1.00 68.75 C ANISOU 1366 C ALA A 207 8640 8141 9343 2460 -3495 -497 C ATOM 1367 O ALA A 207 7.119 -2.289 81.827 1.00 69.42 O ANISOU 1367 O ALA A 207 8562 8248 9565 2662 -3751 -649 O ATOM 1368 CB ALA A 207 9.754 -1.729 80.160 1.00 63.71 C ANISOU 1368 CB ALA A 207 8834 7197 8176 2568 -3546 -259 C ATOM 1369 N ASP A 208 8.756 -3.609 82.699 1.00 65.49 N ANISOU 1369 N ASP A 208 8020 7853 9013 2205 -3288 -487 N ATOM 1370 CA ASP A 208 7.883 -4.687 83.185 1.00 65.12 C ANISOU 1370 CA ASP A 208 7564 7964 9212 2119 -3313 -645 C ATOM 1371 C ASP A 208 8.328 -5.263 84.552 1.00 67.64 C ANISOU 1371 C ASP A 208 7669 8381 9650 1866 -2990 -625 C ATOM 1372 O ASP A 208 9.475 -5.073 84.960 1.00 67.18 O ANISOU 1372 O ASP A 208 7782 8285 9459 1743 -2774 -482 O ATOM 1373 CB ASP A 208 7.773 -5.803 82.125 1.00 67.15 C ANISOU 1373 CB ASP A 208 7856 8251 9406 2102 -3481 -681 C ATOM 1374 CG ASP A 208 9.069 -6.556 81.882 1.00 78.75 C ANISOU 1374 CG ASP A 208 9536 9702 10682 1907 -3293 -525 C ATOM 1375 OD1 ASP A 208 9.848 -6.132 80.994 1.00 79.49 O ANISOU 1375 OD1 ASP A 208 10002 9668 10532 1966 -3323 -401 O ATOM 1376 OD2 ASP A 208 9.309 -7.564 82.585 1.00 84.29 O ANISOU 1376 OD2 ASP A 208 10044 10505 11475 1700 -3105 -535 O ATOM 1377 N ASP A 209 7.419 -5.995 85.225 1.00 62.21 N ANISOU 1377 N ASP A 209 6619 7811 9209 1790 -2960 -784 N ATOM 1378 CA ASP A 209 7.638 -6.616 86.530 1.00 61.20 C ANISOU 1378 CA ASP A 209 6303 7757 9192 1568 -2668 -789 C ATOM 1379 C ASP A 209 8.577 -7.820 86.497 1.00 60.87 C ANISOU 1379 C ASP A 209 6352 7748 9030 1368 -2526 -697 C ATOM 1380 O ASP A 209 9.195 -8.119 87.521 1.00 61.00 O ANISOU 1380 O ASP A 209 6354 7785 9039 1209 -2280 -638 O ATOM 1381 CB ASP A 209 6.295 -7.077 87.136 1.00 63.91 C ANISOU 1381 CB ASP A 209 6257 8191 9835 1544 -2666 -1009 C ATOM 1382 CG ASP A 209 5.276 -6.013 87.472 1.00 83.15 C ANISOU 1382 CG ASP A 209 8522 10616 12454 1720 -2755 -1138 C ATOM 1383 OD1 ASP A 209 5.681 -4.848 87.718 1.00 86.18 O ANISOU 1383 OD1 ASP A 209 9080 10921 12745 1816 -2723 -1036 O ATOM 1384 OD2 ASP A 209 4.074 -6.346 87.524 1.00 93.32 O ANISOU 1384 OD2 ASP A 209 9493 11972 13992 1754 -2843 -1353 O ATOM 1385 N LEU A 210 8.635 -8.548 85.363 1.00 53.77 N ANISOU 1385 N LEU A 210 5543 6849 8038 1385 -2687 -696 N ATOM 1386 CA LEU A 210 9.437 -9.770 85.231 1.00 52.36 C ANISOU 1386 CA LEU A 210 5444 6698 7753 1212 -2570 -624 C ATOM 1387 C LEU A 210 10.947 -9.526 85.162 1.00 53.23 C ANISOU 1387 C LEU A 210 5842 6745 7637 1154 -2431 -434 C ATOM 1388 O LEU A 210 11.684 -10.152 85.920 1.00 52.59 O ANISOU 1388 O LEU A 210 5750 6698 7533 998 -2224 -380 O ATOM 1389 CB LEU A 210 8.949 -10.614 84.036 1.00 52.50 C ANISOU 1389 CB LEU A 210 5463 6732 7752 1249 -2788 -698 C ATOM 1390 CG LEU A 210 9.429 -12.074 83.941 1.00 56.59 C ANISOU 1390 CG LEU A 210 5992 7291 8218 1067 -2678 -676 C ATOM 1391 CD1 LEU A 210 9.123 -12.881 85.219 1.00 56.68 C ANISOU 1391 CD1 LEU A 210 5762 7375 8399 887 -2448 -757 C ATOM 1392 CD2 LEU A 210 8.913 -12.741 82.681 1.00 55.00 C ANISOU 1392 CD2 LEU A 210 5821 7092 7985 1123 -2917 -752 C ATOM 1393 N ALA A 211 11.398 -8.628 84.264 1.00 48.97 N ANISOU 1393 N ALA A 211 5565 6106 6934 1282 -2540 -348 N ATOM 1394 CA ALA A 211 12.805 -8.239 84.044 1.00 47.62 C ANISOU 1394 CA ALA A 211 5674 5858 6563 1233 -2406 -194 C ATOM 1395 C ALA A 211 13.611 -7.924 85.346 1.00 48.73 C ANISOU 1395 C ALA A 211 5764 6022 6730 1111 -2154 -141 C ATOM 1396 O ALA A 211 14.649 -8.578 85.522 1.00 47.37 O ANISOU 1396 O ALA A 211 5650 5870 6479 982 -2010 -77 O ATOM 1397 CB ALA A 211 12.889 -7.085 83.055 1.00 48.11 C ANISOU 1397 CB ALA A 211 6017 5783 6477 1401 -2540 -142 C ATOM 1398 N PRO A 212 13.161 -7.028 86.292 1.00 43.58 N ANISOU 1398 N PRO A 212 4997 5371 6189 1150 -2102 -178 N ATOM 1399 CA PRO A 212 13.937 -6.818 87.545 1.00 42.48 C ANISOU 1399 CA PRO A 212 4824 5253 6062 1032 -1878 -136 C ATOM 1400 C PRO A 212 14.128 -8.088 88.378 1.00 45.95 C ANISOU 1400 C PRO A 212 5117 5784 6556 880 -1747 -160 C ATOM 1401 O PRO A 212 15.210 -8.286 88.931 1.00 44.42 O ANISOU 1401 O PRO A 212 4989 5599 6289 783 -1604 -100 O ATOM 1402 CB PRO A 212 13.121 -5.763 88.311 1.00 43.99 C ANISOU 1402 CB PRO A 212 4908 5429 6379 1117 -1876 -194 C ATOM 1403 CG PRO A 212 11.777 -5.781 87.698 1.00 48.21 C ANISOU 1403 CG PRO A 212 5318 5973 7025 1253 -2082 -300 C ATOM 1404 CD PRO A 212 11.958 -6.167 86.270 1.00 44.17 C ANISOU 1404 CD PRO A 212 4976 5424 6382 1313 -2251 -266 C ATOM 1405 N LYS A 213 13.092 -8.969 88.427 1.00 43.57 N ANISOU 1405 N LYS A 213 4631 5543 6382 863 -1801 -260 N ATOM 1406 CA LYS A 213 13.129 -10.264 89.128 1.00 43.57 C ANISOU 1406 CA LYS A 213 4529 5604 6423 722 -1673 -292 C ATOM 1407 C LYS A 213 14.171 -11.204 88.525 1.00 45.46 C ANISOU 1407 C LYS A 213 4914 5847 6511 653 -1657 -213 C ATOM 1408 O LYS A 213 14.960 -11.791 89.274 1.00 43.42 O ANISOU 1408 O LYS A 213 4688 5608 6203 559 -1513 -176 O ATOM 1409 CB LYS A 213 11.753 -10.947 89.143 1.00 46.41 C ANISOU 1409 CB LYS A 213 4667 6008 6957 708 -1724 -437 C ATOM 1410 CG LYS A 213 10.703 -10.144 89.895 1.00 52.75 C ANISOU 1410 CG LYS A 213 5286 6813 7942 761 -1702 -542 C ATOM 1411 CD LYS A 213 9.357 -10.828 89.857 1.00 52.15 C ANISOU 1411 CD LYS A 213 4962 6783 8069 739 -1747 -718 C ATOM 1412 CE LYS A 213 8.338 -9.974 90.542 1.00 55.81 C ANISOU 1412 CE LYS A 213 5230 7247 8730 800 -1719 -837 C ATOM 1413 NZ LYS A 213 7.013 -10.627 90.570 1.00 78.10 N ANISOU 1413 NZ LYS A 213 7770 10117 11787 762 -1736 -1044 N ATOM 1414 N ILE A 214 14.183 -11.349 87.178 1.00 41.26 N ANISOU 1414 N ILE A 214 4486 5290 5900 713 -1809 -192 N ATOM 1415 CA ILE A 214 15.179 -12.197 86.511 1.00 40.31 C ANISOU 1415 CA ILE A 214 4517 5164 5637 654 -1785 -120 C ATOM 1416 C ILE A 214 16.562 -11.586 86.709 1.00 43.49 C ANISOU 1416 C ILE A 214 5069 5530 5926 634 -1670 -25 C ATOM 1417 O ILE A 214 17.465 -12.284 87.163 1.00 44.67 O ANISOU 1417 O ILE A 214 5240 5707 6027 551 -1554 4 O ATOM 1418 CB ILE A 214 14.848 -12.473 85.022 1.00 43.32 C ANISOU 1418 CB ILE A 214 5000 5511 5949 720 -1968 -126 C ATOM 1419 CG1 ILE A 214 13.581 -13.335 84.887 1.00 44.48 C ANISOU 1419 CG1 ILE A 214 4964 5710 6224 708 -2072 -248 C ATOM 1420 CG2 ILE A 214 16.030 -13.117 84.279 1.00 42.36 C ANISOU 1420 CG2 ILE A 214 5073 5360 5662 667 -1918 -39 C ATOM 1421 CD1 ILE A 214 12.849 -13.139 83.527 1.00 51.21 C ANISOU 1421 CD1 ILE A 214 5875 6529 7055 835 -2326 -297 C ATOM 1422 N TYR A 215 16.702 -10.274 86.437 1.00 38.77 N ANISOU 1422 N TYR A 215 4570 4867 5295 712 -1699 6 N ATOM 1423 CA TYR A 215 17.967 -9.546 86.561 1.00 37.95 C ANISOU 1423 CA TYR A 215 4601 4717 5102 681 -1579 71 C ATOM 1424 C TYR A 215 18.586 -9.605 87.960 1.00 43.02 C ANISOU 1424 C TYR A 215 5142 5413 5792 601 -1430 61 C ATOM 1425 O TYR A 215 19.755 -9.945 88.068 1.00 44.07 O ANISOU 1425 O TYR A 215 5325 5557 5862 536 -1337 84 O ATOM 1426 CB TYR A 215 17.860 -8.085 86.074 1.00 37.93 C ANISOU 1426 CB TYR A 215 4741 4613 5057 776 -1622 95 C ATOM 1427 CG TYR A 215 19.165 -7.336 86.253 1.00 38.47 C ANISOU 1427 CG TYR A 215 4935 4629 5052 714 -1466 138 C ATOM 1428 CD1 TYR A 215 20.244 -7.565 85.403 1.00 39.76 C ANISOU 1428 CD1 TYR A 215 5261 4744 5101 658 -1396 175 C ATOM 1429 CD2 TYR A 215 19.357 -6.468 87.335 1.00 38.19 C ANISOU 1429 CD2 TYR A 215 4837 4597 5076 694 -1372 123 C ATOM 1430 CE1 TYR A 215 21.473 -6.942 85.609 1.00 39.92 C ANISOU 1430 CE1 TYR A 215 5356 4724 5088 579 -1232 181 C ATOM 1431 CE2 TYR A 215 20.581 -5.835 87.545 1.00 38.13 C ANISOU 1431 CE2 TYR A 215 4916 4550 5022 619 -1227 135 C ATOM 1432 CZ TYR A 215 21.632 -6.069 86.672 1.00 44.71 C ANISOU 1432 CZ TYR A 215 5887 5339 5760 559 -1155 156 C ATOM 1433 OH TYR A 215 22.840 -5.453 86.840 1.00 46.83 O ANISOU 1433 OH TYR A 215 6215 5569 6009 471 -998 137 O ATOM 1434 N HIS A 216 17.827 -9.261 89.013 1.00 38.72 N ANISOU 1434 N HIS A 216 4461 4895 5354 612 -1409 15 N ATOM 1435 CA HIS A 216 18.344 -9.255 90.371 1.00 37.51 C ANISOU 1435 CA HIS A 216 4249 4776 5227 550 -1281 3 C ATOM 1436 C HIS A 216 18.579 -10.657 90.934 1.00 40.69 C ANISOU 1436 C HIS A 216 4606 5236 5619 480 -1227 -13 C ATOM 1437 O HIS A 216 19.456 -10.817 91.783 1.00 41.11 O ANISOU 1437 O HIS A 216 4678 5307 5634 441 -1144 -10 O ATOM 1438 CB HIS A 216 17.493 -8.381 91.271 1.00 38.16 C ANISOU 1438 CB HIS A 216 4243 4847 5410 586 -1258 -38 C ATOM 1439 CG HIS A 216 17.719 -6.931 90.972 1.00 41.83 C ANISOU 1439 CG HIS A 216 4802 5242 5850 645 -1268 -11 C ATOM 1440 ND1 HIS A 216 18.870 -6.277 91.394 1.00 43.57 N ANISOU 1440 ND1 HIS A 216 5102 5440 6013 598 -1170 12 N ATOM 1441 CD2 HIS A 216 16.984 -6.077 90.217 1.00 43.78 C ANISOU 1441 CD2 HIS A 216 5095 5428 6112 749 -1370 -11 C ATOM 1442 CE1 HIS A 216 18.766 -5.045 90.928 1.00 43.32 C ANISOU 1442 CE1 HIS A 216 5170 5327 5963 657 -1188 30 C ATOM 1443 NE2 HIS A 216 17.632 -4.868 90.246 1.00 43.53 N ANISOU 1443 NE2 HIS A 216 5192 5323 6024 761 -1311 23 N ATOM 1444 N SER A 217 17.920 -11.685 90.379 1.00 37.78 N ANISOU 1444 N SER A 217 4202 4887 5266 468 -1283 -32 N ATOM 1445 CA SER A 217 18.199 -13.084 90.741 1.00 37.04 C ANISOU 1445 CA SER A 217 4113 4825 5135 403 -1226 -40 C ATOM 1446 C SER A 217 19.587 -13.479 90.164 1.00 42.47 C ANISOU 1446 C SER A 217 4916 5516 5706 394 -1219 12 C ATOM 1447 O SER A 217 20.432 -13.995 90.896 1.00 42.25 O ANISOU 1447 O SER A 217 4916 5508 5632 371 -1151 12 O ATOM 1448 CB SER A 217 17.109 -13.998 90.212 1.00 38.88 C ANISOU 1448 CB SER A 217 4280 5068 5423 381 -1279 -88 C ATOM 1449 OG SER A 217 15.885 -13.694 90.858 1.00 47.08 O ANISOU 1449 OG SER A 217 5182 6109 6598 378 -1259 -165 O ATOM 1450 N CYS A 218 19.844 -13.158 88.877 1.00 39.74 N ANISOU 1450 N CYS A 218 4647 5141 5313 421 -1286 46 N ATOM 1451 CA CYS A 218 21.138 -13.409 88.244 1.00 40.28 C ANISOU 1451 CA CYS A 218 4818 5200 5288 404 -1253 80 C ATOM 1452 C CYS A 218 22.238 -12.619 88.935 1.00 43.08 C ANISOU 1452 C CYS A 218 5171 5556 5640 393 -1168 71 C ATOM 1453 O CYS A 218 23.306 -13.173 89.204 1.00 42.44 O ANISOU 1453 O CYS A 218 5097 5504 5526 372 -1117 56 O ATOM 1454 CB CYS A 218 21.091 -13.078 86.758 1.00 40.92 C ANISOU 1454 CB CYS A 218 5018 5221 5309 431 -1319 113 C ATOM 1455 SG CYS A 218 19.958 -14.112 85.818 1.00 45.41 S ANISOU 1455 SG CYS A 218 5593 5789 5870 447 -1448 103 S ATOM 1456 N PHE A 219 21.966 -11.317 89.209 1.00 37.76 N ANISOU 1456 N PHE A 219 4488 4851 5008 413 -1161 68 N ATOM 1457 CA PHE A 219 22.891 -10.392 89.836 1.00 35.98 C ANISOU 1457 CA PHE A 219 4260 4619 4792 392 -1083 46 C ATOM 1458 C PHE A 219 23.444 -10.996 91.114 1.00 40.93 C ANISOU 1458 C PHE A 219 4813 5309 5430 377 -1047 4 C ATOM 1459 O PHE A 219 24.655 -11.175 91.209 1.00 41.65 O ANISOU 1459 O PHE A 219 4902 5423 5500 357 -1010 -31 O ATOM 1460 CB PHE A 219 22.266 -8.998 90.066 1.00 36.41 C ANISOU 1460 CB PHE A 219 4322 4622 4888 421 -1083 48 C ATOM 1461 CG PHE A 219 23.313 -7.965 90.428 1.00 36.51 C ANISOU 1461 CG PHE A 219 4362 4609 4901 382 -991 20 C ATOM 1462 CD1 PHE A 219 23.708 -7.782 91.757 1.00 37.94 C ANISOU 1462 CD1 PHE A 219 4461 4834 5120 362 -950 -29 C ATOM 1463 CD2 PHE A 219 23.933 -7.202 89.440 1.00 37.35 C ANISOU 1463 CD2 PHE A 219 4593 4637 4963 357 -936 31 C ATOM 1464 CE1 PHE A 219 24.700 -6.857 92.087 1.00 37.88 C ANISOU 1464 CE1 PHE A 219 4462 4808 5125 316 -873 -78 C ATOM 1465 CE2 PHE A 219 24.904 -6.253 89.775 1.00 38.97 C ANISOU 1465 CE2 PHE A 219 4814 4812 5183 297 -827 -18 C ATOM 1466 CZ PHE A 219 25.305 -6.117 91.089 1.00 37.03 C ANISOU 1466 CZ PHE A 219 4450 4627 4992 275 -804 -79 C ATOM 1467 N PHE A 220 22.556 -11.378 92.045 1.00 36.53 N ANISOU 1467 N PHE A 220 4206 4770 4903 390 -1058 -5 N ATOM 1468 CA PHE A 220 22.877 -12.000 93.332 1.00 35.61 C ANISOU 1468 CA PHE A 220 4077 4685 4768 391 -1029 -40 C ATOM 1469 C PHE A 220 23.662 -13.311 93.198 1.00 40.00 C ANISOU 1469 C PHE A 220 4672 5271 5255 399 -1042 -46 C ATOM 1470 O PHE A 220 24.628 -13.501 93.919 1.00 39.15 O ANISOU 1470 O PHE A 220 4572 5187 5115 423 -1042 -88 O ATOM 1471 CB PHE A 220 21.573 -12.228 94.137 1.00 36.87 C ANISOU 1471 CB PHE A 220 4213 4830 4968 389 -1006 -47 C ATOM 1472 CG PHE A 220 21.736 -12.990 95.426 1.00 37.52 C ANISOU 1472 CG PHE A 220 4346 4910 4999 391 -961 -75 C ATOM 1473 CD1 PHE A 220 22.421 -12.436 96.500 1.00 41.49 C ANISOU 1473 CD1 PHE A 220 4878 5412 5474 413 -945 -107 C ATOM 1474 CD2 PHE A 220 21.173 -14.245 95.582 1.00 37.91 C ANISOU 1474 CD2 PHE A 220 4442 4945 5018 372 -931 -76 C ATOM 1475 CE1 PHE A 220 22.569 -13.148 97.703 1.00 42.45 C ANISOU 1475 CE1 PHE A 220 5099 5512 5519 436 -918 -134 C ATOM 1476 CE2 PHE A 220 21.294 -14.942 96.796 1.00 40.65 C ANISOU 1476 CE2 PHE A 220 4897 5260 5289 382 -876 -99 C ATOM 1477 CZ PHE A 220 22.020 -14.404 97.833 1.00 39.25 C ANISOU 1477 CZ PHE A 220 4772 5077 5065 424 -880 -124 C ATOM 1478 N ILE A 221 23.231 -14.222 92.307 1.00 39.17 N ANISOU 1478 N ILE A 221 4593 5162 5127 389 -1065 -15 N ATOM 1479 CA ILE A 221 23.896 -15.502 92.099 1.00 39.67 C ANISOU 1479 CA ILE A 221 4709 5243 5122 402 -1072 -18 C ATOM 1480 C ILE A 221 25.326 -15.307 91.560 1.00 42.65 C ANISOU 1480 C ILE A 221 5079 5640 5484 414 -1070 -42 C ATOM 1481 O ILE A 221 26.241 -15.943 92.058 1.00 44.02 O ANISOU 1481 O ILE A 221 5261 5842 5624 455 -1079 -84 O ATOM 1482 CB ILE A 221 23.007 -16.494 91.253 1.00 43.70 C ANISOU 1482 CB ILE A 221 5255 5736 5615 375 -1089 14 C ATOM 1483 CG1 ILE A 221 21.627 -16.713 91.938 1.00 44.38 C ANISOU 1483 CG1 ILE A 221 5361 5801 5699 355 -1049 -3 C ATOM 1484 CG2 ILE A 221 23.661 -17.890 91.055 1.00 43.86 C ANISOU 1484 CG2 ILE A 221 5339 5762 5565 385 -1099 25 C ATOM 1485 CD1 ILE A 221 21.643 -17.237 93.253 1.00 49.84 C ANISOU 1485 CD1 ILE A 221 5981 6478 6478 327 -1028 -21 C ATOM 1486 N VAL A 222 25.514 -14.417 90.605 1.00 38.36 N ANISOU 1486 N VAL A 222 4531 5076 4970 383 -1053 -29 N ATOM 1487 CA VAL A 222 26.783 -14.176 89.921 1.00 38.59 C ANISOU 1487 CA VAL A 222 4558 5104 5000 365 -1007 -65 C ATOM 1488 C VAL A 222 27.774 -13.320 90.732 1.00 43.36 C ANISOU 1488 C VAL A 222 5081 5735 5658 361 -973 -149 C ATOM 1489 O VAL A 222 28.983 -13.547 90.645 1.00 44.13 O ANISOU 1489 O VAL A 222 5129 5862 5777 362 -947 -225 O ATOM 1490 CB VAL A 222 26.472 -13.598 88.502 1.00 42.26 C ANISOU 1490 CB VAL A 222 5107 5502 5448 327 -981 -17 C ATOM 1491 CG1 VAL A 222 27.660 -12.879 87.867 1.00 41.58 C ANISOU 1491 CG1 VAL A 222 5038 5382 5377 279 -880 -65 C ATOM 1492 CG2 VAL A 222 25.934 -14.695 87.575 1.00 41.90 C ANISOU 1492 CG2 VAL A 222 5138 5440 5342 335 -1025 34 C ATOM 1493 N THR A 223 27.287 -12.357 91.501 1.00 39.65 N ANISOU 1493 N THR A 223 4588 5256 5222 356 -975 -151 N ATOM 1494 CA THR A 223 28.166 -11.485 92.279 1.00 39.44 C ANISOU 1494 CA THR A 223 4489 5250 5247 343 -949 -239 C ATOM 1495 C THR A 223 28.354 -11.948 93.713 1.00 43.31 C ANISOU 1495 C THR A 223 4948 5788 5721 406 -1017 -289 C ATOM 1496 O THR A 223 29.281 -11.488 94.382 1.00 42.36 O ANISOU 1496 O THR A 223 4759 5699 5638 413 -1029 -388 O ATOM 1497 CB THR A 223 27.666 -10.045 92.260 1.00 43.28 C ANISOU 1497 CB THR A 223 4996 5682 5769 299 -900 -220 C ATOM 1498 OG1 THR A 223 26.360 -10.022 92.833 1.00 40.04 O ANISOU 1498 OG1 THR A 223 4610 5259 5347 334 -944 -159 O ATOM 1499 CG2 THR A 223 27.690 -9.424 90.861 1.00 42.17 C ANISOU 1499 CG2 THR A 223 4937 5466 5620 247 -828 -184 C ATOM 1500 N TYR A 224 27.472 -12.815 94.199 1.00 39.83 N ANISOU 1500 N TYR A 224 4570 5341 5221 449 -1058 -233 N ATOM 1501 CA TYR A 224 27.564 -13.224 95.576 1.00 40.48 C ANISOU 1501 CA TYR A 224 4686 5437 5258 513 -1108 -273 C ATOM 1502 C TYR A 224 27.498 -14.756 95.795 1.00 44.60 C ANISOU 1502 C TYR A 224 5301 5956 5689 578 -1148 -255 C ATOM 1503 O TYR A 224 28.521 -15.356 96.117 1.00 44.77 O ANISOU 1503 O TYR A 224 5326 6008 5675 654 -1212 -322 O ATOM 1504 CB TYR A 224 26.506 -12.468 96.433 1.00 41.74 C ANISOU 1504 CB TYR A 224 4877 5557 5426 495 -1077 -244 C ATOM 1505 CG TYR A 224 26.665 -12.685 97.924 1.00 44.37 C ANISOU 1505 CG TYR A 224 5282 5881 5694 556 -1114 -291 C ATOM 1506 CD1 TYR A 224 26.082 -13.784 98.557 1.00 46.16 C ANISOU 1506 CD1 TYR A 224 5641 6070 5830 597 -1110 -262 C ATOM 1507 CD2 TYR A 224 27.414 -11.803 98.702 1.00 45.08 C ANISOU 1507 CD2 TYR A 224 5338 5988 5804 572 -1147 -374 C ATOM 1508 CE1 TYR A 224 26.251 -14.003 99.924 1.00 47.78 C ANISOU 1508 CE1 TYR A 224 5971 6239 5942 664 -1140 -304 C ATOM 1509 CE2 TYR A 224 27.580 -12.007 100.073 1.00 45.64 C ANISOU 1509 CE2 TYR A 224 5509 6039 5792 644 -1201 -422 C ATOM 1510 CZ TYR A 224 27.008 -13.115 100.674 1.00 53.98 C ANISOU 1510 CZ TYR A 224 6727 7045 6737 696 -1198 -382 C ATOM 1511 OH TYR A 224 27.175 -13.326 102.014 1.00 55.58 O ANISOU 1511 OH TYR A 224 7084 7203 6829 776 -1247 -426 O ATOM 1512 N LEU A 225 26.307 -15.366 95.678 1.00 40.84 N ANISOU 1512 N LEU A 225 4900 5439 5179 553 -1112 -180 N ATOM 1513 CA LEU A 225 26.071 -16.756 96.039 1.00 40.21 C ANISOU 1513 CA LEU A 225 4946 5329 5003 597 -1118 -164 C ATOM 1514 C LEU A 225 26.955 -17.788 95.337 1.00 42.59 C ANISOU 1514 C LEU A 225 5267 5654 5260 646 -1160 -176 C ATOM 1515 O LEU A 225 27.554 -18.594 96.051 1.00 41.85 O ANISOU 1515 O LEU A 225 5270 5551 5081 741 -1211 -214 O ATOM 1516 CB LEU A 225 24.591 -17.143 95.916 1.00 40.77 C ANISOU 1516 CB LEU A 225 5064 5350 5078 529 -1044 -106 C ATOM 1517 CG LEU A 225 24.190 -18.440 96.695 1.00 45.49 C ANISOU 1517 CG LEU A 225 5835 5882 5567 551 -1003 -102 C ATOM 1518 CD1 LEU A 225 24.318 -18.245 98.195 1.00 45.82 C ANISOU 1518 CD1 LEU A 225 5995 5879 5537 605 -993 -137 C ATOM 1519 CD2 LEU A 225 22.800 -18.879 96.339 1.00 45.39 C ANISOU 1519 CD2 LEU A 225 5825 5827 5593 457 -915 -75 C ATOM 1520 N ALA A 226 27.027 -17.816 93.990 1.00 38.14 N ANISOU 1520 N ALA A 226 4642 5107 4741 596 -1141 -147 N ATOM 1521 CA ALA A 226 27.880 -18.821 93.335 1.00 36.57 C ANISOU 1521 CA ALA A 226 4469 4924 4504 642 -1164 -164 C ATOM 1522 C ALA A 226 29.386 -18.603 93.606 1.00 41.01 C ANISOU 1522 C ALA A 226 4946 5539 5097 719 -1218 -268 C ATOM 1523 O ALA A 226 30.020 -19.574 94.020 1.00 41.95 O ANISOU 1523 O ALA A 226 5126 5661 5150 824 -1278 -310 O ATOM 1524 CB ALA A 226 27.588 -18.933 91.843 1.00 36.76 C ANISOU 1524 CB ALA A 226 4477 4938 4552 570 -1123 -112 C ATOM 1525 N PRO A 227 29.991 -17.382 93.452 1.00 36.94 N ANISOU 1525 N PRO A 227 4296 5059 4681 677 -1200 -327 N ATOM 1526 CA PRO A 227 31.436 -17.252 93.747 1.00 36.08 C ANISOU 1526 CA PRO A 227 4074 5007 4629 743 -1250 -464 C ATOM 1527 C PRO A 227 31.831 -17.609 95.177 1.00 39.89 C ANISOU 1527 C PRO A 227 4598 5505 5052 875 -1372 -537 C ATOM 1528 O PRO A 227 32.769 -18.380 95.365 1.00 38.13 O ANISOU 1528 O PRO A 227 4361 5313 4814 991 -1458 -625 O ATOM 1529 CB PRO A 227 31.757 -15.779 93.425 1.00 37.04 C ANISOU 1529 CB PRO A 227 4068 5141 4865 642 -1179 -513 C ATOM 1530 CG PRO A 227 30.625 -15.268 92.687 1.00 40.38 C ANISOU 1530 CG PRO A 227 4556 5509 5277 545 -1099 -392 C ATOM 1531 CD PRO A 227 29.425 -16.091 92.992 1.00 36.76 C ANISOU 1531 CD PRO A 227 4221 5018 4727 573 -1132 -290 C ATOM 1532 N LEU A 228 31.125 -17.068 96.179 1.00 39.68 N ANISOU 1532 N LEU A 228 4640 5450 4986 869 -1386 -507 N ATOM 1533 CA LEU A 228 31.453 -17.342 97.589 1.00 41.81 C ANISOU 1533 CA LEU A 228 5001 5713 5172 998 -1505 -573 C ATOM 1534 C LEU A 228 31.197 -18.774 98.001 1.00 46.45 C ANISOU 1534 C LEU A 228 5801 6242 5606 1108 -1550 -529 C ATOM 1535 O LEU A 228 32.002 -19.323 98.749 1.00 48.26 O ANISOU 1535 O LEU A 228 6097 6475 5764 1265 -1683 -616 O ATOM 1536 CB LEU A 228 30.782 -16.362 98.551 1.00 42.99 C ANISOU 1536 CB LEU A 228 5190 5832 5313 955 -1486 -557 C ATOM 1537 CG LEU A 228 31.154 -14.910 98.315 1.00 49.17 C ANISOU 1537 CG LEU A 228 5791 6659 6233 863 -1450 -620 C ATOM 1538 CD1 LEU A 228 30.092 -14.039 98.803 1.00 50.20 C ANISOU 1538 CD1 LEU A 228 5974 6742 6359 787 -1379 -551 C ATOM 1539 CD2 LEU A 228 32.518 -14.557 98.930 1.00 52.29 C ANISOU 1539 CD2 LEU A 228 6070 7118 6680 944 -1572 -795 C ATOM 1540 N GLY A 229 30.154 -19.396 97.450 1.00 41.76 N ANISOU 1540 N GLY A 229 5312 5593 4965 1035 -1449 -410 N ATOM 1541 CA GLY A 229 29.853 -20.804 97.697 1.00 41.03 C ANISOU 1541 CA GLY A 229 5438 5426 4726 1110 -1453 -365 C ATOM 1542 C GLY A 229 30.973 -21.682 97.188 1.00 45.66 C ANISOU 1542 C GLY A 229 6003 6046 5298 1226 -1536 -426 C ATOM 1543 O GLY A 229 31.443 -22.564 97.914 1.00 47.54 O ANISOU 1543 O GLY A 229 6409 6243 5412 1385 -1632 -465 O ATOM 1544 N LEU A 230 31.449 -21.405 95.948 1.00 41.07 N ANISOU 1544 N LEU A 230 5232 5531 4842 1158 -1497 -442 N ATOM 1545 CA LEU A 230 32.574 -22.106 95.311 1.00 40.70 C ANISOU 1545 CA LEU A 230 5118 5524 4821 1249 -1547 -517 C ATOM 1546 C LEU A 230 33.873 -21.861 96.087 1.00 48.11 C ANISOU 1546 C LEU A 230 5952 6525 5803 1403 -1699 -682 C ATOM 1547 O LEU A 230 34.655 -22.787 96.282 1.00 49.55 O ANISOU 1547 O LEU A 230 6187 6708 5932 1569 -1805 -754 O ATOM 1548 CB LEU A 230 32.740 -21.689 93.825 1.00 39.96 C ANISOU 1548 CB LEU A 230 4861 5469 4853 1117 -1438 -504 C ATOM 1549 CG LEU A 230 31.735 -22.289 92.821 1.00 42.52 C ANISOU 1549 CG LEU A 230 5294 5736 5125 1013 -1334 -371 C ATOM 1550 CD1 LEU A 230 31.646 -21.457 91.556 1.00 40.84 C ANISOU 1550 CD1 LEU A 230 4961 5540 5015 871 -1234 -347 C ATOM 1551 CD2 LEU A 230 32.054 -23.751 92.520 1.00 43.74 C ANISOU 1551 CD2 LEU A 230 5577 5856 5187 1108 -1354 -365 C ATOM 1552 N MET A 231 34.074 -20.625 96.573 1.00 45.36 N ANISOU 1552 N MET A 231 5463 6224 5547 1357 -1720 -752 N ATOM 1553 CA MET A 231 35.243 -20.257 97.364 1.00 45.38 C ANISOU 1553 CA MET A 231 5342 6292 5610 1487 -1876 -932 C ATOM 1554 C MET A 231 35.264 -20.997 98.705 1.00 49.57 C ANISOU 1554 C MET A 231 6105 6767 5962 1688 -2045 -954 C ATOM 1555 O MET A 231 36.291 -21.573 99.040 1.00 49.04 O ANISOU 1555 O MET A 231 6017 6731 5885 1879 -2211 -1089 O ATOM 1556 CB MET A 231 35.322 -18.728 97.554 1.00 47.65 C ANISOU 1556 CB MET A 231 5452 6626 6027 1363 -1837 -992 C ATOM 1557 CG MET A 231 35.845 -17.995 96.334 1.00 50.96 C ANISOU 1557 CG MET A 231 5633 7099 6631 1217 -1705 -1049 C ATOM 1558 SD MET A 231 36.213 -16.266 96.711 1.00 55.83 S ANISOU 1558 SD MET A 231 6057 7760 7397 1098 -1672 -1166 S ATOM 1559 CE MET A 231 34.753 -15.448 96.026 1.00 52.17 C ANISOU 1559 CE MET A 231 5697 7220 6905 900 -1480 -959 C ATOM 1560 N ALA A 232 34.133 -21.008 99.455 1.00 47.35 N ANISOU 1560 N ALA A 232 6060 6393 5538 1653 -1999 -830 N ATOM 1561 CA ALA A 232 34.016 -21.696 100.750 1.00 47.32 C ANISOU 1561 CA ALA A 232 6355 6296 5328 1827 -2119 -832 C ATOM 1562 C ALA A 232 34.393 -23.181 100.631 1.00 54.11 C ANISOU 1562 C ALA A 232 7398 7102 6058 1998 -2192 -831 C ATOM 1563 O ALA A 232 35.089 -23.714 101.502 1.00 53.05 O ANISOU 1563 O ALA A 232 7408 6940 5809 2226 -2385 -927 O ATOM 1564 CB ALA A 232 32.611 -21.545 101.314 1.00 47.45 C ANISOU 1564 CB ALA A 232 6592 6204 5233 1712 -1979 -690 C ATOM 1565 N MET A 233 33.991 -23.829 99.516 1.00 52.57 N ANISOU 1565 N MET A 233 7199 6892 5882 1901 -2053 -734 N ATOM 1566 CA MET A 233 34.310 -25.241 99.252 1.00 51.83 C ANISOU 1566 CA MET A 233 7277 6742 5674 2041 -2093 -723 C ATOM 1567 C MET A 233 35.769 -25.442 98.886 1.00 58.05 C ANISOU 1567 C MET A 233 7858 7628 6570 2204 -2247 -888 C ATOM 1568 O MET A 233 36.337 -26.486 99.228 1.00 59.78 O ANISOU 1568 O MET A 233 8246 7799 6669 2424 -2379 -939 O ATOM 1569 CB MET A 233 33.404 -25.817 98.166 1.00 53.77 C ANISOU 1569 CB MET A 233 7569 6944 5917 1872 -1896 -582 C ATOM 1570 CG MET A 233 31.996 -26.047 98.637 1.00 57.65 C ANISOU 1570 CG MET A 233 8314 7313 6278 1758 -1757 -450 C ATOM 1571 SD MET A 233 30.914 -26.723 97.363 1.00 62.46 S ANISOU 1571 SD MET A 233 8952 7878 6901 1561 -1553 -319 S ATOM 1572 CE MET A 233 30.783 -25.357 96.260 1.00 58.64 C ANISOU 1572 CE MET A 233 8106 7524 6652 1368 -1488 -313 C ATOM 1573 N ALA A 234 36.368 -24.469 98.174 1.00 55.11 N ANISOU 1573 N ALA A 234 7131 7382 6426 2097 -2217 -979 N ATOM 1574 CA ALA A 234 37.778 -24.499 97.766 1.00 55.71 C ANISOU 1574 CA ALA A 234 6945 7563 6660 2213 -2324 -1170 C ATOM 1575 C ALA A 234 38.690 -24.323 98.984 1.00 62.07 C ANISOU 1575 C ALA A 234 7725 8405 7452 2440 -2583 -1356 C ATOM 1576 O ALA A 234 39.645 -25.087 99.141 1.00 61.22 O ANISOU 1576 O ALA A 234 7605 8317 7337 2670 -2754 -1491 O ATOM 1577 CB ALA A 234 38.056 -23.406 96.746 1.00 56.14 C ANISOU 1577 CB ALA A 234 6666 7712 6951 2001 -2177 -1219 C ATOM 1578 N TYR A 235 38.379 -23.336 99.860 1.00 60.52 N ANISOU 1578 N TYR A 235 7534 8213 7247 2390 -2623 -1367 N ATOM 1579 CA TYR A 235 39.162 -23.093 101.065 1.00 61.78 C ANISOU 1579 CA TYR A 235 7693 8401 7379 2599 -2883 -1545 C ATOM 1580 C TYR A 235 39.028 -24.225 102.077 1.00 67.79 C ANISOU 1580 C TYR A 235 8861 9035 7860 2860 -3057 -1509 C ATOM 1581 O TYR A 235 40.002 -24.514 102.765 1.00 68.64 O ANISOU 1581 O TYR A 235 8972 9168 7941 3122 -3324 -1689 O ATOM 1582 CB TYR A 235 38.883 -21.714 101.682 1.00 63.42 C ANISOU 1582 CB TYR A 235 7806 8640 7651 2464 -2865 -1569 C ATOM 1583 CG TYR A 235 39.613 -20.611 100.943 1.00 65.73 C ANISOU 1583 CG TYR A 235 7673 9068 8233 2306 -2794 -1717 C ATOM 1584 CD1 TYR A 235 41.006 -20.527 100.972 1.00 67.36 C ANISOU 1584 CD1 TYR A 235 7596 9386 8613 2438 -2964 -1984 C ATOM 1585 CD2 TYR A 235 38.917 -19.677 100.173 1.00 66.27 C ANISOU 1585 CD2 TYR A 235 7631 9143 8407 2026 -2546 -1604 C ATOM 1586 CE1 TYR A 235 41.688 -19.546 100.254 1.00 67.63 C ANISOU 1586 CE1 TYR A 235 7248 9527 8922 2268 -2854 -2136 C ATOM 1587 CE2 TYR A 235 39.591 -18.692 99.449 1.00 67.16 C ANISOU 1587 CE2 TYR A 235 7404 9350 8765 1873 -2447 -1737 C ATOM 1588 CZ TYR A 235 40.978 -18.638 99.486 1.00 76.01 C ANISOU 1588 CZ TYR A 235 8248 10572 10059 1980 -2584 -2004 C ATOM 1589 OH TYR A 235 41.664 -17.682 98.779 1.00 79.19 O ANISOU 1589 OH TYR A 235 8323 11053 10712 1808 -2452 -2155 O ATOM 1590 N PHE A 236 37.871 -24.909 102.122 1.00 64.82 N ANISOU 1590 N PHE A 236 8832 8517 7281 2797 -2906 -1296 N ATOM 1591 CA PHE A 236 37.677 -26.058 102.995 1.00 65.42 C ANISOU 1591 CA PHE A 236 9353 8436 7068 3019 -3016 -1246 C ATOM 1592 C PHE A 236 38.586 -27.212 102.544 1.00 70.28 C ANISOU 1592 C PHE A 236 9977 9059 7668 3244 -3146 -1331 C ATOM 1593 O PHE A 236 39.115 -27.940 103.391 1.00 70.51 O ANISOU 1593 O PHE A 236 10264 9011 7516 3540 -3375 -1411 O ATOM 1594 CB PHE A 236 36.199 -26.486 103.054 1.00 67.97 C ANISOU 1594 CB PHE A 236 10013 8602 7211 2853 -2773 -1017 C ATOM 1595 CG PHE A 236 35.971 -27.788 103.795 1.00 70.68 C ANISOU 1595 CG PHE A 236 10852 8754 7249 3053 -2825 -959 C ATOM 1596 CD1 PHE A 236 36.006 -27.833 105.187 1.00 74.45 C ANISOU 1596 CD1 PHE A 236 11671 9113 7504 3241 -2980 -996 C ATOM 1597 CD2 PHE A 236 35.769 -28.979 103.098 1.00 73.05 C ANISOU 1597 CD2 PHE A 236 11307 8978 7470 3063 -2722 -873 C ATOM 1598 CE1 PHE A 236 35.837 -29.047 105.867 1.00 75.41 C ANISOU 1598 CE1 PHE A 236 12304 9031 7318 3437 -3020 -945 C ATOM 1599 CE2 PHE A 236 35.602 -30.191 103.782 1.00 75.90 C ANISOU 1599 CE2 PHE A 236 12159 9143 7536 3251 -2759 -825 C ATOM 1600 CZ PHE A 236 35.623 -30.214 105.160 1.00 74.03 C ANISOU 1600 CZ PHE A 236 12280 8777 7071 3435 -2899 -858 C ATOM 1601 N GLN A 237 38.781 -27.373 101.218 1.00 66.17 N ANISOU 1601 N GLN A 237 9196 8620 7326 3119 -3006 -1320 N ATOM 1602 CA GLN A 237 39.669 -28.415 100.689 1.00 65.33 C ANISOU 1602 CA GLN A 237 9061 8528 7235 3317 -3104 -1410 C ATOM 1603 C GLN A 237 41.118 -28.076 100.988 1.00 71.66 C ANISOU 1603 C GLN A 237 9562 9463 8204 3536 -3372 -1686 C ATOM 1604 O GLN A 237 41.892 -28.969 101.339 1.00 72.79 O ANISOU 1604 O GLN A 237 9819 9577 8262 3842 -3593 -1802 O ATOM 1605 CB GLN A 237 39.455 -28.639 99.197 1.00 65.81 C ANISOU 1605 CB GLN A 237 8944 8627 7433 3111 -2865 -1324 C ATOM 1606 CG GLN A 237 38.082 -29.198 98.906 1.00 65.57 C ANISOU 1606 CG GLN A 237 9224 8460 7229 2939 -2641 -1083 C ATOM 1607 CD GLN A 237 38.078 -30.197 97.796 1.00 71.92 C ANISOU 1607 CD GLN A 237 10063 9233 8030 2916 -2521 -1021 C ATOM 1608 OE1 GLN A 237 38.658 -29.987 96.723 1.00 68.40 O ANISOU 1608 OE1 GLN A 237 9313 8890 7784 2841 -2457 -1087 O ATOM 1609 NE2 GLN A 237 37.402 -31.310 98.042 1.00 58.53 N ANISOU 1609 NE2 GLN A 237 8764 7377 6097 2967 -2469 -894 N ATOM 1610 N ILE A 238 41.471 -26.780 100.880 1.00 69.03 N ANISOU 1610 N ILE A 238 8852 9267 8108 3386 -3357 -1805 N ATOM 1611 CA ILE A 238 42.790 -26.230 101.197 1.00 69.46 C ANISOU 1611 CA ILE A 238 8563 9463 8368 3539 -3589 -2098 C ATOM 1612 C ILE A 238 43.061 -26.452 102.687 1.00 76.23 C ANISOU 1612 C ILE A 238 9685 10257 9020 3841 -3915 -2192 C ATOM 1613 O ILE A 238 44.181 -26.819 103.051 1.00 76.60 O ANISOU 1613 O ILE A 238 9623 10361 9119 4131 -4199 -2426 O ATOM 1614 CB ILE A 238 42.893 -24.737 100.756 1.00 72.14 C ANISOU 1614 CB ILE A 238 8503 9930 8979 3255 -3441 -2174 C ATOM 1615 CG1 ILE A 238 43.113 -24.630 99.226 1.00 71.84 C ANISOU 1615 CG1 ILE A 238 8165 9961 9168 3042 -3185 -2174 C ATOM 1616 CG2 ILE A 238 43.986 -23.972 101.524 1.00 72.60 C ANISOU 1616 CG2 ILE A 238 8285 10104 9196 3388 -3696 -2469 C ATOM 1617 CD1 ILE A 238 42.526 -23.404 98.593 1.00 76.14 C ANISOU 1617 CD1 ILE A 238 8549 10535 9846 2697 -2920 -2082 C ATOM 1618 N PHE A 239 42.017 -26.293 103.535 1.00 74.90 N ANISOU 1618 N PHE A 239 9888 9958 8611 3788 -3873 -2015 N ATOM 1619 CA PHE A 239 42.093 -26.519 104.984 1.00 75.91 C ANISOU 1619 CA PHE A 239 10372 9983 8487 4059 -4148 -2066 C ATOM 1620 C PHE A 239 42.451 -27.980 105.277 1.00 82.37 C ANISOU 1620 C PHE A 239 11542 10680 9074 4399 -4334 -2076 C ATOM 1621 O PHE A 239 43.336 -28.235 106.093 1.00 82.82 O ANISOU 1621 O PHE A 239 11669 10738 9061 4733 -4680 -2271 O ATOM 1622 CB PHE A 239 40.776 -26.128 105.682 1.00 77.69 C ANISOU 1622 CB PHE A 239 10946 10070 8502 3890 -3984 -1852 C ATOM 1623 CG PHE A 239 40.789 -26.376 107.169 1.00 79.23 C ANISOU 1623 CG PHE A 239 11575 10125 8404 4155 -4231 -1887 C ATOM 1624 CD1 PHE A 239 41.203 -25.387 108.050 1.00 82.30 C ANISOU 1624 CD1 PHE A 239 11865 10573 8833 4208 -4426 -2041 C ATOM 1625 CD2 PHE A 239 40.412 -27.610 107.690 1.00 81.44 C ANISOU 1625 CD2 PHE A 239 12393 10199 8353 4354 -4266 -1774 C ATOM 1626 CE1 PHE A 239 41.237 -25.624 109.428 1.00 83.24 C ANISOU 1626 CE1 PHE A 239 12423 10549 8658 4467 -4667 -2078 C ATOM 1627 CE2 PHE A 239 40.463 -27.852 109.065 1.00 84.03 C ANISOU 1627 CE2 PHE A 239 13176 10372 8381 4614 -4494 -1810 C ATOM 1628 CZ PHE A 239 40.867 -26.855 109.925 1.00 82.05 C ANISOU 1628 CZ PHE A 239 12828 10183 8166 4672 -4698 -1959 C ATOM 1629 N ARG A 240 41.759 -28.927 104.604 1.00 79.93 N ANISOU 1629 N ARG A 240 11463 10261 8646 4319 -4112 -1874 N ATOM 1630 CA ARG A 240 41.971 -30.371 104.722 1.00 79.72 C ANISOU 1630 CA ARG A 240 11803 10096 8392 4602 -4223 -1850 C ATOM 1631 C ARG A 240 43.378 -30.776 104.265 1.00 86.29 C ANISOU 1631 C ARG A 240 12317 11058 9411 4859 -4457 -2096 C ATOM 1632 O ARG A 240 44.007 -31.622 104.917 1.00 87.83 O ANISOU 1632 O ARG A 240 12769 11171 9430 5235 -4743 -2201 O ATOM 1633 CB ARG A 240 40.893 -31.149 103.945 1.00 77.24 C ANISOU 1633 CB ARG A 240 11730 9656 7961 4392 -3890 -1593 C ATOM 1634 CG ARG A 240 39.535 -31.204 104.643 1.00 86.07 C ANISOU 1634 CG ARG A 240 13305 10584 8815 4245 -3702 -1377 C ATOM 1635 CD ARG A 240 39.494 -32.261 105.730 1.00104.30 C ANISOU 1635 CD ARG A 240 16221 12662 10748 4548 -3855 -1350 C ATOM 1636 NE ARG A 240 38.332 -32.129 106.611 1.00121.37 N ANISOU 1636 NE ARG A 240 18808 14639 12669 4419 -3690 -1193 N ATOM 1637 CZ ARG A 240 37.252 -32.905 106.556 1.00141.73 C ANISOU 1637 CZ ARG A 240 21779 17023 15048 4279 -3416 -1001 C ATOM 1638 NH1 ARG A 240 37.162 -33.869 105.645 1.00128.55 N ANISOU 1638 NH1 ARG A 240 20141 15321 13382 4246 -3284 -931 N ATOM 1639 NH2 ARG A 240 36.246 -32.712 107.399 1.00131.92 N ANISOU 1639 NH2 ARG A 240 20893 15615 13614 4156 -3254 -890 N ATOM 1640 N LYS A 241 43.887 -30.157 103.176 1.00 82.57 N ANISOU 1640 N LYS A 241 11301 10778 9296 4668 -4337 -2201 N ATOM 1641 CA LYS A 241 45.228 -30.457 102.665 1.00 82.56 C ANISOU 1641 CA LYS A 241 10935 10911 9525 4872 -4512 -2460 C ATOM 1642 C LYS A 241 46.338 -29.864 103.534 1.00 88.53 C ANISOU 1642 C LYS A 241 11439 11786 10411 5117 -4878 -2776 C ATOM 1643 O LYS A 241 47.333 -30.547 103.774 1.00 88.66 O ANISOU 1643 O LYS A 241 11408 11829 10449 5467 -5167 -2989 O ATOM 1644 CB LYS A 241 45.392 -30.023 101.195 1.00 84.36 C ANISOU 1644 CB LYS A 241 10703 11275 10075 4571 -4220 -2471 C ATOM 1645 CG LYS A 241 46.375 -30.885 100.394 1.00 93.98 C ANISOU 1645 CG LYS A 241 11723 12546 11437 4751 -4270 -2626 C ATOM 1646 CD LYS A 241 45.758 -32.213 99.917 1.00102.50 C ANISOU 1646 CD LYS A 241 13203 13463 12280 4793 -4132 -2404 C ATOM 1647 CE LYS A 241 46.758 -33.162 99.286 1.00112.60 C ANISOU 1647 CE LYS A 241 14345 14773 13664 5027 -4215 -2563 C ATOM 1648 NZ LYS A 241 47.051 -32.825 97.866 1.00120.32 N ANISOU 1648 NZ LYS A 241 14904 15867 14946 4762 -3934 -2602 N ATOM 1649 N LEU A 242 46.165 -28.614 104.025 1.00 85.81 N ANISOU 1649 N LEU A 242 10939 11512 10155 4947 -4880 -2818 N ATOM 1650 CA LEU A 242 47.187 -27.914 104.817 1.00 85.76 C ANISOU 1650 CA LEU A 242 10655 11632 10300 5133 -5214 -3134 C ATOM 1651 C LEU A 242 47.204 -28.198 106.341 1.00 89.02 C ANISOU 1651 C LEU A 242 11507 11922 10395 5475 -5581 -3177 C ATOM 1652 O LEU A 242 48.229 -27.926 106.967 1.00 88.77 O ANISOU 1652 O LEU A 242 11268 11988 10471 5730 -5938 -3480 O ATOM 1653 CB LEU A 242 47.120 -26.391 104.585 1.00 85.84 C ANISOU 1653 CB LEU A 242 10255 11780 10580 4785 -5042 -3195 C ATOM 1654 CG LEU A 242 47.544 -25.864 103.206 1.00 90.42 C ANISOU 1654 CG LEU A 242 10306 12511 11538 4503 -4765 -3283 C ATOM 1655 CD1 LEU A 242 47.410 -24.363 103.150 1.00 90.47 C ANISOU 1655 CD1 LEU A 242 10012 12612 11749 4182 -4607 -3328 C ATOM 1656 CD2 LEU A 242 48.981 -26.246 102.864 1.00 92.39 C ANISOU 1656 CD2 LEU A 242 10156 12895 12052 4733 -4966 -3627 C ATOM 1657 N TRP A 243 46.103 -28.701 106.939 1.00 84.59 N ANISOU 1657 N TRP A 243 11542 11144 9455 5478 -5494 -2899 N ATOM 1658 CA TRP A 243 46.067 -28.964 108.382 1.00102.28 C ANISOU 1658 CA TRP A 243 14271 13233 11359 5790 -5808 -2924 C ATOM 1659 C TRP A 243 45.857 -30.435 108.736 1.00123.77 C ANISOU 1659 C TRP A 243 17587 15730 13710 6099 -5906 -2802 C ATOM 1660 O TRP A 243 44.983 -31.096 108.184 1.00 90.03 O ANISOU 1660 O TRP A 243 13584 11327 9296 5935 -5597 -2543 O ATOM 1661 CB TRP A 243 45.034 -28.071 109.079 1.00100.96 C ANISOU 1661 CB TRP A 243 14330 12982 11048 5546 -5648 -2752 C ATOM 1662 CG TRP A 243 45.519 -26.670 109.327 1.00101.78 C ANISOU 1662 CG TRP A 243 13992 13266 11416 5420 -5743 -2953 C ATOM 1663 CD1 TRP A 243 46.206 -26.222 110.416 1.00104.54 C ANISOU 1663 CD1 TRP A 243 14352 13643 11724 5665 -6121 -3187 C ATOM 1664 CD2 TRP A 243 45.341 -25.530 108.467 1.00101.55 C ANISOU 1664 CD2 TRP A 243 13468 13398 11720 5019 -5453 -2946 C ATOM 1665 NE1 TRP A 243 46.466 -24.876 110.292 1.00103.82 N ANISOU 1665 NE1 TRP A 243 13788 13726 11932 5424 -6071 -3328 N ATOM 1666 CE2 TRP A 243 45.948 -24.426 109.105 1.00105.19 C ANISOU 1666 CE2 TRP A 243 13657 13977 12334 5028 -5657 -3180 C ATOM 1667 CE3 TRP A 243 44.739 -25.338 107.208 1.00102.62 C ANISOU 1667 CE3 TRP A 243 13383 13579 12028 4661 -5049 -2770 C ATOM 1668 CZ2 TRP A 243 45.965 -23.147 108.534 1.00104.39 C ANISOU 1668 CZ2 TRP A 243 13090 14027 12547 4684 -5446 -3237 C ATOM 1669 CZ3 TRP A 243 44.768 -24.074 106.638 1.00103.86 C ANISOU 1669 CZ3 TRP A 243 13094 13883 12486 4341 -4859 -2824 C ATOM 1670 CH2 TRP A 243 45.382 -22.998 107.294 1.00104.46 C ANISOU 1670 CH2 TRP A 243 12918 14065 12706 4350 -5046 -3054 C ATOM 1671 N GLU A 286 59.809 -28.650 102.322 1.00122.45 N ANISOU 1671 N GLU A 286 10505 17795 18226 6891 -6961 -6937 N ATOM 1672 CA GLU A 286 58.362 -28.701 102.113 1.00121.31 C ANISOU 1672 CA GLU A 286 10941 17466 17684 6618 -6636 -6387 C ATOM 1673 C GLU A 286 57.573 -28.278 103.362 1.00125.61 C ANISOU 1673 C GLU A 286 11943 17918 17866 6671 -6867 -6193 C ATOM 1674 O GLU A 286 56.483 -27.723 103.226 1.00125.22 O ANISOU 1674 O GLU A 286 12160 17780 17638 6316 -6554 -5844 O ATOM 1675 CB GLU A 286 57.936 -30.093 101.632 1.00122.26 C ANISOU 1675 CB GLU A 286 11499 17430 17525 6805 -6566 -6110 C ATOM 1676 CG GLU A 286 58.347 -30.384 100.199 1.00130.80 C ANISOU 1676 CG GLU A 286 12231 18561 18906 6613 -6181 -6170 C ATOM 1677 CD GLU A 286 58.051 -31.787 99.709 1.00149.81 C ANISOU 1677 CD GLU A 286 15029 20823 21069 6816 -6129 -5944 C ATOM 1678 OE1 GLU A 286 56.856 -32.155 99.619 1.00147.62 O ANISOU 1678 OE1 GLU A 286 15302 20372 20415 6681 -5938 -5503 O ATOM 1679 OE2 GLU A 286 59.019 -32.515 99.395 1.00140.56 O ANISOU 1679 OE2 GLU A 286 13599 19711 20098 7102 -6268 -6223 O ATOM 1680 N VAL A 287 58.133 -28.528 104.565 1.00122.73 N ANISOU 1680 N VAL A 287 11670 17567 17394 7121 -7419 -6430 N ATOM 1681 CA VAL A 287 57.560 -28.172 105.874 1.00122.70 C ANISOU 1681 CA VAL A 287 12101 17470 17047 7241 -7705 -6313 C ATOM 1682 C VAL A 287 57.546 -26.639 106.003 1.00126.01 C ANISOU 1682 C VAL A 287 12151 18015 17713 6858 -7561 -6432 C ATOM 1683 O VAL A 287 56.552 -26.073 106.466 1.00125.64 O ANISOU 1683 O VAL A 287 12460 17866 17410 6644 -7433 -6141 O ATOM 1684 CB VAL A 287 58.343 -28.853 107.044 1.00126.84 C ANISOU 1684 CB VAL A 287 12779 17985 17429 7857 -8362 -6600 C ATOM 1685 CG1 VAL A 287 57.745 -28.509 108.406 1.00126.38 C ANISOU 1685 CG1 VAL A 287 13232 17804 16981 7986 -8648 -6471 C ATOM 1686 CG2 VAL A 287 58.402 -30.368 106.864 1.00126.76 C ANISOU 1686 CG2 VAL A 287 13133 17842 17187 8243 -8491 -6498 C ATOM 1687 N LYS A 288 58.647 -25.981 105.569 1.00122.10 N ANISOU 1687 N LYS A 288 10938 17731 17724 6761 -7557 -6870 N ATOM 1688 CA LYS A 288 58.839 -24.522 105.582 1.00121.43 C ANISOU 1688 CA LYS A 288 10418 17776 17942 6392 -7402 -7058 C ATOM 1689 C LYS A 288 57.793 -23.838 104.687 1.00123.68 C ANISOU 1689 C LYS A 288 10805 17991 18198 5840 -6798 -6675 C ATOM 1690 O LYS A 288 57.249 -22.795 105.066 1.00123.37 O ANISOU 1690 O LYS A 288 10835 17936 18103 5576 -6690 -6570 O ATOM 1691 CB LYS A 288 60.264 -24.174 105.115 1.00123.64 C ANISOU 1691 CB LYS A 288 9910 18277 18790 6396 -7454 -7611 C ATOM 1692 CG LYS A 288 60.804 -22.846 105.623 1.00136.18 C ANISOU 1692 CG LYS A 288 11055 20011 20675 6218 -7547 -7962 C ATOM 1693 CD LYS A 288 62.252 -22.669 105.182 1.00150.83 C ANISOU 1693 CD LYS A 288 12131 22078 23100 6261 -7618 -8546 C ATOM 1694 CE LYS A 288 63.000 -21.629 105.977 1.00161.20 C ANISOU 1694 CE LYS A 288 13253 23475 24520 5933 -7551 -8444 C ATOM 1695 NZ LYS A 288 64.458 -21.659 105.683 1.00169.93 N ANISOU 1695 NZ LYS A 288 14197 24628 25742 5412 -6979 -7807 N ATOM 1696 N GLN A 289 57.503 -24.446 103.514 1.00118.46 N ANISOU 1696 N GLN A 289 10177 17275 17556 5689 -6424 -6467 N ATOM 1697 CA GLN A 289 56.506 -23.948 102.572 1.00117.53 C ANISOU 1697 CA GLN A 289 10190 17078 17389 5211 -5877 -6101 C ATOM 1698 C GLN A 289 55.102 -24.188 103.129 1.00119.64 C ANISOU 1698 C GLN A 289 11137 17158 17163 5198 -5857 -5626 C ATOM 1699 O GLN A 289 54.248 -23.313 102.985 1.00119.88 O ANISOU 1699 O GLN A 289 11269 17144 17135 4840 -5568 -5398 O ATOM 1700 CB GLN A 289 56.670 -24.594 101.187 1.00118.78 C ANISOU 1700 CB GLN A 289 10206 17227 17699 5092 -5527 -6044 C ATOM 1701 CG GLN A 289 55.935 -23.833 100.084 1.00129.58 C ANISOU 1701 CG GLN A 289 11552 18550 19133 4571 -4962 -5790 C ATOM 1702 CD GLN A 289 56.139 -24.437 98.721 1.00149.36 C ANISOU 1702 CD GLN A 289 13930 21037 21782 4454 -4622 -5753 C ATOM 1703 OE1 GLN A 289 55.829 -25.611 98.470 1.00145.17 O ANISOU 1703 OE1 GLN A 289 13716 20413 21031 4649 -4653 -5554 O ATOM 1704 NE2 GLN A 289 56.651 -23.632 97.802 1.00141.12 N ANISOU 1704 NE2 GLN A 289 12449 20067 21101 4120 -4268 -5941 N ATOM 1705 N MET A 290 54.875 -25.350 103.790 1.00113.94 N ANISOU 1705 N MET A 290 10881 16318 16092 5590 -6160 -5494 N ATOM 1706 CA MET A 290 53.596 -25.720 104.414 1.00113.02 C ANISOU 1706 CA MET A 290 11437 16006 15500 5613 -6153 -5077 C ATOM 1707 C MET A 290 53.238 -24.770 105.572 1.00113.67 C ANISOU 1707 C MET A 290 11666 16074 15449 5587 -6335 -5083 C ATOM 1708 O MET A 290 52.057 -24.557 105.846 1.00112.28 O ANISOU 1708 O MET A 290 11913 15763 14987 5416 -6164 -4741 O ATOM 1709 CB MET A 290 53.629 -27.180 104.889 1.00115.75 C ANISOU 1709 CB MET A 290 12235 16220 15525 6061 -6444 -4998 C ATOM 1710 CG MET A 290 52.334 -27.645 105.547 1.00119.93 C ANISOU 1710 CG MET A 290 13404 16531 15633 5975 -6224 -4527 C ATOM 1711 SD MET A 290 52.264 -29.430 105.879 1.00124.64 S ANISOU 1711 SD MET A 290 14717 16926 15715 6288 -6571 -4368 S ATOM 1712 CE MET A 290 50.720 -29.549 106.794 1.00121.35 C ANISOU 1712 CE MET A 290 14480 16460 15168 6903 -7046 -4588 C ATOM 1713 N ARG A 291 54.268 -24.206 106.240 1.00108.53 N ANISOU 1713 N ARG A 291 10652 15563 15019 5754 -6677 -5490 N ATOM 1714 CA ARG A 291 54.143 -23.242 107.336 1.00107.13 C ANISOU 1714 CA ARG A 291 10545 15395 14766 5741 -6881 -5568 C ATOM 1715 C ARG A 291 53.773 -21.858 106.776 1.00106.15 C ANISOU 1715 C ARG A 291 10120 15339 14875 5227 -6472 -5517 C ATOM 1716 O ARG A 291 52.977 -21.137 107.386 1.00105.19 O ANISOU 1716 O ARG A 291 10257 15143 14569 5071 -6416 -5337 O ATOM 1717 CB ARG A 291 55.470 -23.185 108.117 1.00109.10 C ANISOU 1717 CB ARG A 291 10468 15781 15203 6106 -7401 -6058 C ATOM 1718 CG ARG A 291 55.373 -22.477 109.463 1.00126.53 C ANISOU 1718 CG ARG A 291 12870 17965 17241 6205 -7718 -6139 C ATOM 1719 CD ARG A 291 56.646 -22.640 110.279 1.00147.28 C ANISOU 1719 CD ARG A 291 15246 20710 20003 6640 -8300 -6619 C ATOM 1720 NE ARG A 291 56.630 -21.817 111.494 1.00160.77 N ANISOU 1720 NE ARG A 291 17072 22415 21598 6695 -8591 -6740 N ATOM 1721 CZ ARG A 291 57.552 -21.871 112.452 1.00176.00 C ANISOU 1721 CZ ARG A 291 19038 24379 23457 6457 -8493 -6371 C ATOM 1722 NH1 ARG A 291 58.573 -22.713 112.355 1.00162.01 N ANISOU 1722 NH1 ARG A 291 16930 22718 21907 7296 -9304 -7222 N ATOM 1723 NH2 ARG A 291 57.455 -21.087 113.518 1.00165.92 N ANISOU 1723 NH2 ARG A 291 17791 23115 22135 6960 -9233 -7039 N ATOM 1724 N ALA A 292 54.353 -21.506 105.605 1.00 99.04 N ANISOU 1724 N ALA A 292 8697 14563 14371 4972 -6175 -5678 N ATOM 1725 CA ALA A 292 54.128 -20.245 104.892 1.00 97.03 C ANISOU 1725 CA ALA A 292 8145 14360 14361 4488 -5755 -5656 C ATOM 1726 C ALA A 292 52.704 -20.214 104.324 1.00 96.83 C ANISOU 1726 C ALA A 292 8527 14183 14080 4197 -5350 -5163 C ATOM 1727 O ALA A 292 51.969 -19.243 104.542 1.00 96.61 O ANISOU 1727 O ALA A 292 8608 14112 13985 3933 -5177 -5006 O ATOM 1728 CB ALA A 292 55.149 -20.099 103.768 1.00 97.63 C ANISOU 1728 CB ALA A 292 7626 14575 14892 4335 -5544 -5961 C ATOM 1729 N ARG A 293 52.327 -21.307 103.618 1.00 88.69 N ANISOU 1729 N ARG A 293 7718 13070 12910 4265 -5217 -4937 N ATOM 1730 CA ARG A 293 51.032 -21.558 103.005 1.00 86.16 C ANISOU 1730 CA ARG A 293 7779 12607 12350 4046 -4873 -4496 C ATOM 1731 C ARG A 293 49.875 -21.468 103.993 1.00 87.57 C ANISOU 1731 C ARG A 293 8477 12646 12149 4073 -4949 -4205 C ATOM 1732 O ARG A 293 48.830 -20.924 103.635 1.00 88.42 O ANISOU 1732 O ARG A 293 8746 12681 12169 3771 -4637 -3924 O ATOM 1733 CB ARG A 293 51.031 -22.930 102.312 1.00 82.77 C ANISOU 1733 CB ARG A 293 7504 12120 11827 4208 -4829 -4378 C ATOM 1734 CG ARG A 293 51.407 -22.854 100.845 1.00 83.78 C ANISOU 1734 CG ARG A 293 7271 12311 12252 3963 -4475 -4436 C ATOM 1735 CD ARG A 293 51.679 -24.221 100.279 1.00 84.30 C ANISOU 1735 CD ARG A 293 7433 12338 12260 4180 -4499 -4403 C ATOM 1736 NE ARG A 293 51.918 -24.167 98.839 1.00 85.92 N ANISOU 1736 NE ARG A 293 7360 12576 12711 3924 -4123 -4420 N ATOM 1737 CZ ARG A 293 52.205 -25.224 98.088 1.00 99.79 C ANISOU 1737 CZ ARG A 293 9130 14307 14478 4043 -4060 -4409 C ATOM 1738 NH1 ARG A 293 52.306 -26.430 98.637 1.00 87.82 N ANISOU 1738 NH1 ARG A 293 7887 12734 12748 4421 -4353 -4384 N ATOM 1739 NH2 ARG A 293 52.389 -25.085 96.784 1.00 85.64 N ANISOU 1739 NH2 ARG A 293 7110 12532 12899 3787 -3695 -4421 N ATOM 1740 N ARG A 294 50.045 -22.010 105.214 1.00 81.22 N ANISOU 1740 N ARG A 294 7949 11795 11117 4437 -5356 -4277 N ATOM 1741 CA ARG A 294 49.023 -21.987 106.261 1.00 80.33 C ANISOU 1741 CA ARG A 294 8362 11530 10629 4493 -5440 -4032 C ATOM 1742 C ARG A 294 48.719 -20.555 106.703 1.00 84.04 C ANISOU 1742 C ARG A 294 8723 12034 11175 4235 -5353 -4051 C ATOM 1743 O ARG A 294 47.553 -20.246 106.967 1.00 84.69 O ANISOU 1743 O ARG A 294 9146 11995 11036 4069 -5171 -3758 O ATOM 1744 CB ARG A 294 49.457 -22.817 107.472 1.00 79.86 C ANISOU 1744 CB ARG A 294 8614 11406 10322 4961 -5913 -4158 C ATOM 1745 CG ARG A 294 49.229 -24.311 107.353 1.00 86.46 C ANISOU 1745 CG ARG A 294 9844 12108 10897 5222 -5971 -3994 C ATOM 1746 CD ARG A 294 49.486 -24.949 108.695 1.00 93.61 C ANISOU 1746 CD ARG A 294 11170 12905 11490 5664 -6421 -4078 C ATOM 1747 NE ARG A 294 49.897 -26.345 108.588 1.00104.96 N ANISOU 1747 NE ARG A 294 12818 14272 12790 6017 -6604 -4097 N ATOM 1748 CZ ARG A 294 50.108 -27.140 109.631 1.00117.42 C ANISOU 1748 CZ ARG A 294 14843 15719 14052 6446 -6987 -4144 C ATOM 1749 NH1 ARG A 294 49.934 -26.687 110.867 1.00105.98 N ANISOU 1749 NH1 ARG A 294 13691 14193 12385 6569 -7226 -4173 N ATOM 1750 NH2 ARG A 294 50.484 -28.399 109.447 1.00 98.85 N ANISOU 1750 NH2 ARG A 294 12680 13295 11582 6761 -7130 -4158 N ATOM 1751 N LYS A 295 49.762 -19.685 106.782 1.00 78.58 N ANISOU 1751 N LYS A 295 7548 11502 10805 4197 -5474 -4408 N ATOM 1752 CA LYS A 295 49.629 -18.276 107.168 1.00 77.01 C ANISOU 1752 CA LYS A 295 7200 11345 10714 3949 -5396 -4474 C ATOM 1753 C LYS A 295 48.783 -17.500 106.144 1.00 80.08 C ANISOU 1753 C LYS A 295 7520 11708 11198 3506 -4899 -4229 C ATOM 1754 O LYS A 295 47.855 -16.789 106.540 1.00 80.17 O ANISOU 1754 O LYS A 295 7759 11638 11062 3331 -4766 -4028 O ATOM 1755 CB LYS A 295 50.999 -17.612 107.359 1.00 78.23 C ANISOU 1755 CB LYS A 295 6823 11677 11223 3997 -5615 -4941 C ATOM 1756 CG LYS A 295 51.662 -17.943 108.684 1.00 95.91 C ANISOU 1756 CG LYS A 295 9169 13934 13339 4409 -6152 -5191 C ATOM 1757 CD LYS A 295 52.907 -17.084 108.898 1.00109.04 C ANISOU 1757 CD LYS A 295 10273 15778 15377 4401 -6348 -5669 C ATOM 1758 CE LYS A 295 53.873 -17.652 109.912 1.00117.34 C ANISOU 1758 CE LYS A 295 11314 16883 16386 4868 -6926 -6001 C ATOM 1759 NZ LYS A 295 54.949 -16.677 110.252 1.00123.41 N ANISOU 1759 NZ LYS A 295 11552 17825 17513 4827 -7120 -6470 N ATOM 1760 N THR A 296 49.085 -17.667 104.835 1.00 75.07 N ANISOU 1760 N THR A 296 6602 11130 10792 3344 -4633 -4246 N ATOM 1761 CA THR A 296 48.369 -17.025 103.732 1.00 74.31 C ANISOU 1761 CA THR A 296 6456 11000 10780 2956 -4179 -4030 C ATOM 1762 C THR A 296 46.938 -17.571 103.628 1.00 78.68 C ANISOU 1762 C THR A 296 7493 11397 11004 2913 -4018 -3603 C ATOM 1763 O THR A 296 46.000 -16.781 103.495 1.00 78.90 O ANISOU 1763 O THR A 296 7642 11364 10974 2660 -3780 -3396 O ATOM 1764 CB THR A 296 49.149 -17.152 102.414 1.00 77.53 C ANISOU 1764 CB THR A 296 6474 11491 11494 2827 -3958 -4181 C ATOM 1765 OG1 THR A 296 50.498 -16.741 102.613 1.00 74.36 O ANISOU 1765 OG1 THR A 296 5613 11233 11408 2892 -4126 -4614 O ATOM 1766 CG2 THR A 296 48.546 -16.318 101.293 1.00 76.65 C ANISOU 1766 CG2 THR A 296 6305 11338 11481 2427 -3506 -4007 C ATOM 1767 N ALA A 297 46.771 -18.910 103.710 1.00 74.51 N ANISOU 1767 N ALA A 297 7239 10802 10269 3163 -4149 -3489 N ATOM 1768 CA ALA A 297 45.462 -19.559 103.651 1.00 73.96 C ANISOU 1768 CA ALA A 297 7624 10582 9897 3133 -4004 -3119 C ATOM 1769 C ALA A 297 44.549 -19.067 104.775 1.00 77.49 C ANISOU 1769 C ALA A 297 8411 10928 10103 3121 -4058 -2967 C ATOM 1770 O ALA A 297 43.401 -18.737 104.496 1.00 77.48 O ANISOU 1770 O ALA A 297 8586 10845 10007 2898 -3797 -2706 O ATOM 1771 CB ALA A 297 45.606 -21.072 103.691 1.00 74.62 C ANISOU 1771 CB ALA A 297 7944 10605 9805 3427 -4164 -3075 C ATOM 1772 N LYS A 298 45.070 -18.943 106.018 1.00 73.92 N ANISOU 1772 N LYS A 298 8032 10485 9570 3354 -4393 -3149 N ATOM 1773 CA LYS A 298 44.309 -18.425 107.161 1.00 73.90 C ANISOU 1773 CA LYS A 298 8356 10382 9341 3353 -4454 -3039 C ATOM 1774 C LYS A 298 43.806 -17.003 106.846 1.00 78.16 C ANISOU 1774 C LYS A 298 8711 10953 10034 3000 -4183 -2981 C ATOM 1775 O LYS A 298 42.615 -16.727 107.008 1.00 79.55 O ANISOU 1775 O LYS A 298 9160 11018 10046 2852 -3990 -2725 O ATOM 1776 CB LYS A 298 45.167 -18.431 108.445 1.00 76.51 C ANISOU 1776 CB LYS A 298 8734 10736 9602 3663 -4883 -3303 C ATOM 1777 CG LYS A 298 44.405 -18.052 109.723 1.00 91.31 C ANISOU 1777 CG LYS A 298 11025 12477 11191 3707 -4970 -3191 C ATOM 1778 CD LYS A 298 45.327 -17.924 110.943 1.00102.01 C ANISOU 1778 CD LYS A 298 12405 13863 12493 4006 -5412 -3481 C ATOM 1779 CE LYS A 298 44.557 -17.590 112.205 1.00112.53 C ANISOU 1779 CE LYS A 298 14199 15041 13516 4051 -5481 -3361 C ATOM 1780 NZ LYS A 298 45.426 -17.564 113.416 1.00117.90 N ANISOU 1780 NZ LYS A 298 14968 15730 14100 4374 -5942 -3636 N ATOM 1781 N MET A 299 44.705 -16.131 106.343 1.00 72.24 N ANISOU 1781 N MET A 299 7499 10344 9606 2863 -4150 -3225 N ATOM 1782 CA MET A 299 44.433 -14.736 105.997 1.00 70.55 C ANISOU 1782 CA MET A 299 7085 10160 9563 2539 -3901 -3218 C ATOM 1783 C MET A 299 43.362 -14.591 104.896 1.00 73.17 C ANISOU 1783 C MET A 299 7495 10424 9883 2267 -3512 -2919 C ATOM 1784 O MET A 299 42.408 -13.819 105.066 1.00 73.84 O ANISOU 1784 O MET A 299 7732 10438 9888 2093 -3345 -2744 O ATOM 1785 CB MET A 299 45.739 -14.048 105.591 1.00 72.40 C ANISOU 1785 CB MET A 299 6814 10546 10150 2462 -3930 -3568 C ATOM 1786 CG MET A 299 45.601 -12.571 105.379 1.00 75.76 C ANISOU 1786 CG MET A 299 7054 10988 10743 2146 -3697 -3603 C ATOM 1787 SD MET A 299 47.010 -11.870 104.509 1.00 79.64 S ANISOU 1787 SD MET A 299 6960 11627 11673 1970 -3583 -3979 S ATOM 1788 CE MET A 299 46.787 -12.603 102.851 1.00 75.71 C ANISOU 1788 CE MET A 299 6423 11104 11241 1849 -3259 -3800 C ATOM 1789 N LEU A 300 43.517 -15.329 103.786 1.00 66.66 N ANISOU 1789 N LEU A 300 6572 9620 9136 2246 -3381 -2872 N ATOM 1790 CA LEU A 300 42.580 -15.292 102.664 1.00 64.84 C ANISOU 1790 CA LEU A 300 6414 9327 8894 2016 -3048 -2612 C ATOM 1791 C LEU A 300 41.198 -15.810 103.049 1.00 67.21 C ANISOU 1791 C LEU A 300 7136 9496 8906 2041 -2999 -2307 C ATOM 1792 O LEU A 300 40.207 -15.314 102.525 1.00 66.94 O ANISOU 1792 O LEU A 300 7179 9404 8852 1831 -2756 -2106 O ATOM 1793 CB LEU A 300 43.129 -16.033 101.441 1.00 64.44 C ANISOU 1793 CB LEU A 300 6188 9320 8976 2010 -2942 -2650 C ATOM 1794 CG LEU A 300 44.457 -15.530 100.857 1.00 68.57 C ANISOU 1794 CG LEU A 300 6270 9964 9820 1938 -2909 -2958 C ATOM 1795 CD1 LEU A 300 45.071 -16.568 99.965 1.00 68.86 C ANISOU 1795 CD1 LEU A 300 6193 10033 9939 2029 -2884 -3017 C ATOM 1796 CD2 LEU A 300 44.291 -14.212 100.123 1.00 70.21 C ANISOU 1796 CD2 LEU A 300 6316 10166 10195 1610 -2604 -2949 C ATOM 1797 N MET A 301 41.121 -16.759 103.997 1.00 63.24 N ANISOU 1797 N MET A 301 6913 8933 8181 2298 -3226 -2285 N ATOM 1798 CA MET A 301 39.837 -17.270 104.477 1.00 62.77 C ANISOU 1798 CA MET A 301 7270 8731 7847 2316 -3163 -2025 C ATOM 1799 C MET A 301 39.113 -16.165 105.251 1.00 64.68 C ANISOU 1799 C MET A 301 7617 8923 8034 2191 -3103 -1963 C ATOM 1800 O MET A 301 37.890 -16.042 105.133 1.00 64.54 O ANISOU 1800 O MET A 301 7791 8815 7917 2052 -2901 -1741 O ATOM 1801 CB MET A 301 40.003 -18.539 105.328 1.00 65.32 C ANISOU 1801 CB MET A 301 7910 8978 7932 2624 -3406 -2036 C ATOM 1802 CG MET A 301 40.343 -19.767 104.517 1.00 69.81 C ANISOU 1802 CG MET A 301 8479 9550 8496 2731 -3405 -2015 C ATOM 1803 SD MET A 301 41.122 -21.068 105.531 1.00 75.49 S ANISOU 1803 SD MET A 301 9459 10217 9006 3157 -3781 -2152 S ATOM 1804 CE MET A 301 41.892 -22.107 104.234 1.00 71.99 C ANISOU 1804 CE MET A 301 8809 9842 8703 3226 -3747 -2205 C ATOM 1805 N VAL A 302 39.882 -15.319 105.988 1.00 58.64 N ANISOU 1805 N VAL A 302 6700 8223 7356 2233 -3271 -2177 N ATOM 1806 CA VAL A 302 39.351 -14.179 106.747 1.00 56.77 C ANISOU 1806 CA VAL A 302 6538 7946 7086 2118 -3227 -2153 C ATOM 1807 C VAL A 302 38.858 -13.087 105.767 1.00 58.33 C ANISOU 1807 C VAL A 302 6526 8169 7466 1811 -2925 -2066 C ATOM 1808 O VAL A 302 37.739 -12.611 105.912 1.00 58.78 O ANISOU 1808 O VAL A 302 6754 8142 7437 1684 -2760 -1884 O ATOM 1809 CB VAL A 302 40.331 -13.666 107.845 1.00 60.15 C ANISOU 1809 CB VAL A 302 6891 8428 7536 2267 -3519 -2418 C ATOM 1810 CG1 VAL A 302 39.805 -12.393 108.525 1.00 59.88 C ANISOU 1810 CG1 VAL A 302 6916 8352 7484 2121 -3445 -2396 C ATOM 1811 CG2 VAL A 302 40.605 -14.756 108.888 1.00 59.60 C ANISOU 1811 CG2 VAL A 302 7133 8293 7220 2597 -3824 -2465 C ATOM 1812 N VAL A 303 39.665 -12.753 104.743 1.00 51.82 N ANISOU 1812 N VAL A 303 5356 7447 6886 1701 -2845 -2197 N ATOM 1813 CA VAL A 303 39.326 -11.804 103.676 1.00 50.28 C ANISOU 1813 CA VAL A 303 4992 7258 6853 1427 -2558 -2127 C ATOM 1814 C VAL A 303 37.976 -12.211 103.014 1.00 54.48 C ANISOU 1814 C VAL A 303 5740 7697 7261 1338 -2351 -1829 C ATOM 1815 O VAL A 303 37.087 -11.363 102.897 1.00 54.11 O ANISOU 1815 O VAL A 303 5756 7595 7207 1178 -2182 -1699 O ATOM 1816 CB VAL A 303 40.496 -11.684 102.652 1.00 53.03 C ANISOU 1816 CB VAL A 303 4984 7708 7456 1353 -2499 -2326 C ATOM 1817 CG1 VAL A 303 40.073 -10.985 101.365 1.00 52.64 C ANISOU 1817 CG1 VAL A 303 4850 7629 7521 1093 -2182 -2215 C ATOM 1818 CG2 VAL A 303 41.704 -10.986 103.267 1.00 52.44 C ANISOU 1818 CG2 VAL A 303 4647 7726 7550 1381 -2659 -2644 C ATOM 1819 N VAL A 304 37.820 -13.513 102.635 1.00 50.40 N ANISOU 1819 N VAL A 304 5340 7162 6648 1451 -2379 -1737 N ATOM 1820 CA VAL A 304 36.601 -14.081 102.033 1.00 49.72 C ANISOU 1820 CA VAL A 304 5448 6993 6448 1384 -2213 -1486 C ATOM 1821 C VAL A 304 35.429 -14.045 103.035 1.00 56.60 C ANISOU 1821 C VAL A 304 6614 7761 7131 1402 -2205 -1339 C ATOM 1822 O VAL A 304 34.342 -13.599 102.667 1.00 57.70 O ANISOU 1822 O VAL A 304 6811 7848 7266 1254 -2023 -1183 O ATOM 1823 CB VAL A 304 36.830 -15.492 101.417 1.00 52.47 C ANISOU 1823 CB VAL A 304 5844 7344 6746 1497 -2247 -1452 C ATOM 1824 CG1 VAL A 304 35.525 -16.125 100.932 1.00 51.77 C ANISOU 1824 CG1 VAL A 304 5974 7166 6531 1432 -2096 -1212 C ATOM 1825 CG2 VAL A 304 37.844 -15.439 100.283 1.00 52.08 C ANISOU 1825 CG2 VAL A 304 5504 7382 6901 1437 -2189 -1580 C ATOM 1826 N LEU A 305 35.650 -14.477 104.293 1.00 54.56 N ANISOU 1826 N LEU A 305 6545 7466 6719 1586 -2398 -1402 N ATOM 1827 CA LEU A 305 34.613 -14.459 105.329 1.00 55.45 C ANISOU 1827 CA LEU A 305 6965 7462 6643 1603 -2370 -1284 C ATOM 1828 C LEU A 305 34.101 -13.026 105.620 1.00 59.03 C ANISOU 1828 C LEU A 305 7356 7905 7169 1443 -2258 -1270 C ATOM 1829 O LEU A 305 32.888 -12.826 105.734 1.00 58.61 O ANISOU 1829 O LEU A 305 7450 7766 7052 1347 -2096 -1116 O ATOM 1830 CB LEU A 305 35.098 -15.152 106.615 1.00 56.29 C ANISOU 1830 CB LEU A 305 7321 7513 6553 1847 -2610 -1374 C ATOM 1831 CG LEU A 305 34.172 -15.029 107.844 1.00 61.96 C ANISOU 1831 CG LEU A 305 8389 8090 7061 1870 -2580 -1284 C ATOM 1832 CD1 LEU A 305 32.999 -16.034 107.780 1.00 62.24 C ANISOU 1832 CD1 LEU A 305 8718 7995 6934 1850 -2412 -1090 C ATOM 1833 CD2 LEU A 305 34.963 -15.124 109.144 1.00 64.10 C ANISOU 1833 CD2 LEU A 305 8836 8332 7186 2094 -2855 -1440 C ATOM 1834 N VAL A 306 35.024 -12.044 105.724 1.00 54.85 N ANISOU 1834 N VAL A 306 6600 7459 6784 1412 -2337 -1445 N ATOM 1835 CA VAL A 306 34.706 -10.633 105.965 1.00 54.46 C ANISOU 1835 CA VAL A 306 6482 7398 6811 1262 -2235 -1455 C ATOM 1836 C VAL A 306 33.944 -10.047 104.751 1.00 56.93 C ANISOU 1836 C VAL A 306 6683 7706 7244 1057 -1983 -1316 C ATOM 1837 O VAL A 306 32.947 -9.339 104.942 1.00 56.94 O ANISOU 1837 O VAL A 306 6773 7640 7223 959 -1850 -1207 O ATOM 1838 CB VAL A 306 35.957 -9.823 106.395 1.00 58.45 C ANISOU 1838 CB VAL A 306 6781 7988 7440 1279 -2387 -1701 C ATOM 1839 CG1 VAL A 306 35.700 -8.315 106.392 1.00 58.30 C ANISOU 1839 CG1 VAL A 306 6668 7958 7527 1091 -2242 -1713 C ATOM 1840 CG2 VAL A 306 36.425 -10.273 107.773 1.00 58.46 C ANISOU 1840 CG2 VAL A 306 6964 7968 7281 1496 -2654 -1819 C ATOM 1841 N PHE A 307 34.371 -10.406 103.516 1.00 50.79 N ANISOU 1841 N PHE A 307 5736 6985 6577 1011 -1925 -1319 N ATOM 1842 CA PHE A 307 33.701 -10.000 102.276 1.00 49.39 C ANISOU 1842 CA PHE A 307 5493 6789 6484 848 -1713 -1189 C ATOM 1843 C PHE A 307 32.263 -10.526 102.285 1.00 54.18 C ANISOU 1843 C PHE A 307 6308 7312 6966 844 -1624 -984 C ATOM 1844 O PHE A 307 31.342 -9.751 102.037 1.00 55.22 O ANISOU 1844 O PHE A 307 6461 7396 7124 736 -1489 -886 O ATOM 1845 CB PHE A 307 34.437 -10.547 101.038 1.00 50.09 C ANISOU 1845 CB PHE A 307 5420 6936 6675 827 -1681 -1231 C ATOM 1846 CG PHE A 307 33.945 -9.982 99.726 1.00 50.42 C ANISOU 1846 CG PHE A 307 5408 6949 6799 663 -1478 -1128 C ATOM 1847 CD1 PHE A 307 32.884 -10.578 99.044 1.00 52.33 C ANISOU 1847 CD1 PHE A 307 5773 7141 6968 646 -1396 -945 C ATOM 1848 CD2 PHE A 307 34.532 -8.845 99.174 1.00 51.67 C ANISOU 1848 CD2 PHE A 307 5414 7118 7100 527 -1368 -1225 C ATOM 1849 CE1 PHE A 307 32.432 -10.057 97.826 1.00 52.57 C ANISOU 1849 CE1 PHE A 307 5781 7136 7056 520 -1241 -858 C ATOM 1850 CE2 PHE A 307 34.080 -8.326 97.957 1.00 53.84 C ANISOU 1850 CE2 PHE A 307 5699 7341 7418 393 -1185 -1126 C ATOM 1851 CZ PHE A 307 33.032 -8.934 97.291 1.00 51.65 C ANISOU 1851 CZ PHE A 307 5553 7018 7056 403 -1138 -942 C ATOM 1852 N ALA A 308 32.078 -11.830 102.589 1.00 49.15 N ANISOU 1852 N ALA A 308 5825 6651 6200 966 -1698 -935 N ATOM 1853 CA ALA A 308 30.767 -12.465 102.662 1.00 48.59 C ANISOU 1853 CA ALA A 308 5948 6495 6020 955 -1603 -773 C ATOM 1854 C ALA A 308 29.861 -11.800 103.713 1.00 52.74 C ANISOU 1854 C ALA A 308 6619 6942 6479 927 -1546 -730 C ATOM 1855 O ALA A 308 28.668 -11.640 103.464 1.00 51.45 O ANISOU 1855 O ALA A 308 6499 6725 6325 840 -1402 -616 O ATOM 1856 CB ALA A 308 30.910 -13.960 102.928 1.00 49.00 C ANISOU 1856 CB ALA A 308 6166 6519 5932 1091 -1688 -757 C ATOM 1857 N LEU A 309 30.423 -11.363 104.852 1.00 51.58 N ANISOU 1857 N LEU A 309 6534 6787 6278 1000 -1657 -835 N ATOM 1858 CA LEU A 309 29.626 -10.682 105.886 1.00 52.36 C ANISOU 1858 CA LEU A 309 6785 6801 6309 973 -1592 -804 C ATOM 1859 C LEU A 309 29.247 -9.274 105.467 1.00 54.21 C ANISOU 1859 C LEU A 309 6865 7048 6683 831 -1472 -789 C ATOM 1860 O LEU A 309 28.072 -8.947 105.538 1.00 53.85 O ANISOU 1860 O LEU A 309 6888 6936 6638 763 -1330 -691 O ATOM 1861 CB LEU A 309 30.278 -10.698 107.286 1.00 53.15 C ANISOU 1861 CB LEU A 309 7055 6867 6273 1107 -1756 -916 C ATOM 1862 CG LEU A 309 30.543 -12.084 107.898 1.00 58.84 C ANISOU 1862 CG LEU A 309 8014 7536 6806 1281 -1884 -926 C ATOM 1863 CD1 LEU A 309 31.097 -11.961 109.303 1.00 58.62 C ANISOU 1863 CD1 LEU A 309 8186 7459 6627 1427 -2063 -1041 C ATOM 1864 CD2 LEU A 309 29.293 -12.969 107.859 1.00 62.71 C ANISOU 1864 CD2 LEU A 309 8721 7916 7191 1249 -1714 -774 C ATOM 1865 N CYS A 310 30.208 -8.489 104.940 1.00 49.47 N ANISOU 1865 N CYS A 310 6057 6526 6212 783 -1513 -891 N ATOM 1866 CA CYS A 310 30.000 -7.122 104.457 1.00 49.02 C ANISOU 1866 CA CYS A 310 5877 6467 6279 650 -1395 -887 C ATOM 1867 C CYS A 310 28.968 -6.993 103.348 1.00 47.83 C ANISOU 1867 C CYS A 310 5695 6290 6190 561 -1240 -744 C ATOM 1868 O CYS A 310 28.271 -5.978 103.292 1.00 46.80 O ANISOU 1868 O CYS A 310 5566 6111 6105 488 -1135 -698 O ATOM 1869 CB CYS A 310 31.322 -6.492 104.037 1.00 50.82 C ANISOU 1869 CB CYS A 310 5906 6773 6632 605 -1447 -1043 C ATOM 1870 SG CYS A 310 32.389 -6.029 105.423 1.00 55.82 S ANISOU 1870 SG CYS A 310 6537 7433 7237 678 -1626 -1248 S ATOM 1871 N TYR A 311 28.891 -7.999 102.455 1.00 41.82 N ANISOU 1871 N TYR A 311 4909 5554 5426 578 -1239 -684 N ATOM 1872 CA TYR A 311 28.028 -7.983 101.281 1.00 40.11 C ANISOU 1872 CA TYR A 311 4659 5319 5264 510 -1131 -568 C ATOM 1873 C TYR A 311 26.696 -8.685 101.476 1.00 44.87 C ANISOU 1873 C TYR A 311 5374 5867 5806 528 -1077 -459 C ATOM 1874 O TYR A 311 25.808 -8.515 100.642 1.00 45.28 O ANISOU 1874 O TYR A 311 5392 5899 5912 479 -1002 -380 O ATOM 1875 CB TYR A 311 28.780 -8.534 100.064 1.00 40.34 C ANISOU 1875 CB TYR A 311 4585 5402 5339 497 -1147 -582 C ATOM 1876 CG TYR A 311 29.744 -7.532 99.483 1.00 43.46 C ANISOU 1876 CG TYR A 311 4853 5821 5838 419 -1110 -674 C ATOM 1877 CD1 TYR A 311 31.010 -7.351 100.034 1.00 46.13 C ANISOU 1877 CD1 TYR A 311 5099 6213 6214 436 -1187 -834 C ATOM 1878 CD2 TYR A 311 29.372 -6.706 98.422 1.00 45.26 C ANISOU 1878 CD2 TYR A 311 5064 6006 6125 327 -993 -615 C ATOM 1879 CE1 TYR A 311 31.873 -6.361 99.562 1.00 47.81 C ANISOU 1879 CE1 TYR A 311 5188 6438 6541 336 -1119 -943 C ATOM 1880 CE2 TYR A 311 30.237 -5.721 97.927 1.00 46.34 C ANISOU 1880 CE2 TYR A 311 5124 6136 6347 236 -919 -705 C ATOM 1881 CZ TYR A 311 31.493 -5.569 98.489 1.00 55.97 C ANISOU 1881 CZ TYR A 311 6232 7412 7622 227 -968 -873 C ATOM 1882 OH TYR A 311 32.361 -4.621 98.005 1.00 61.63 O ANISOU 1882 OH TYR A 311 6861 8115 8440 114 -866 -986 O ATOM 1883 N LEU A 312 26.526 -9.436 102.567 1.00 41.52 N ANISOU 1883 N LEU A 312 5094 5409 5271 597 -1111 -468 N ATOM 1884 CA LEU A 312 25.285 -10.164 102.797 1.00 41.79 C ANISOU 1884 CA LEU A 312 5243 5379 5258 592 -1024 -388 C ATOM 1885 C LEU A 312 24.069 -9.225 102.931 1.00 44.78 C ANISOU 1885 C LEU A 312 5600 5706 5710 526 -901 -348 C ATOM 1886 O LEU A 312 23.116 -9.412 102.150 1.00 44.27 O ANISOU 1886 O LEU A 312 5475 5633 5713 484 -835 -289 O ATOM 1887 CB LEU A 312 25.410 -11.152 103.984 1.00 42.29 C ANISOU 1887 CB LEU A 312 5520 5386 5163 677 -1060 -413 C ATOM 1888 CG LEU A 312 24.219 -12.073 104.296 1.00 46.62 C ANISOU 1888 CG LEU A 312 6219 5846 5648 655 -935 -351 C ATOM 1889 CD1 LEU A 312 24.063 -13.169 103.252 1.00 45.59 C ANISOU 1889 CD1 LEU A 312 6050 5742 5531 641 -931 -303 C ATOM 1890 CD2 LEU A 312 24.396 -12.711 105.646 1.00 50.11 C ANISOU 1890 CD2 LEU A 312 6933 6196 5910 737 -949 -382 C ATOM 1891 N PRO A 313 24.077 -8.192 103.834 1.00 40.26 N ANISOU 1891 N PRO A 313 5064 5097 5135 521 -879 -388 N ATOM 1892 CA PRO A 313 22.895 -7.317 103.955 1.00 39.15 C ANISOU 1892 CA PRO A 313 4901 4903 5073 473 -757 -356 C ATOM 1893 C PRO A 313 22.439 -6.655 102.653 1.00 40.83 C ANISOU 1893 C PRO A 313 4959 5142 5413 433 -737 -312 C ATOM 1894 O PRO A 313 21.254 -6.702 102.359 1.00 38.43 O ANISOU 1894 O PRO A 313 4617 4809 5174 418 -665 -275 O ATOM 1895 CB PRO A 313 23.318 -6.299 105.028 1.00 40.09 C ANISOU 1895 CB PRO A 313 5086 4988 5157 480 -762 -417 C ATOM 1896 CG PRO A 313 24.302 -7.016 105.839 1.00 43.92 C ANISOU 1896 CG PRO A 313 5695 5481 5511 548 -870 -477 C ATOM 1897 CD PRO A 313 25.088 -7.812 104.849 1.00 40.64 C ANISOU 1897 CD PRO A 313 5184 5147 5109 569 -967 -476 C ATOM 1898 N ILE A 314 23.360 -6.069 101.871 1.00 38.77 N ANISOU 1898 N ILE A 314 4620 4926 5185 419 -796 -327 N ATOM 1899 CA ILE A 314 22.983 -5.412 100.615 1.00 39.44 C ANISOU 1899 CA ILE A 314 4620 5009 5356 393 -777 -282 C ATOM 1900 C ILE A 314 22.401 -6.414 99.595 1.00 44.40 C ANISOU 1900 C ILE A 314 5210 5659 5999 401 -798 -225 C ATOM 1901 O ILE A 314 21.381 -6.111 98.967 1.00 44.98 O ANISOU 1901 O ILE A 314 5244 5708 6140 408 -778 -187 O ATOM 1902 CB ILE A 314 24.113 -4.522 100.011 1.00 42.15 C ANISOU 1902 CB ILE A 314 4929 5366 5721 356 -794 -319 C ATOM 1903 CG1 ILE A 314 23.535 -3.547 98.950 1.00 41.67 C ANISOU 1903 CG1 ILE A 314 4860 5255 5719 342 -751 -268 C ATOM 1904 CG2 ILE A 314 25.321 -5.343 99.499 1.00 41.90 C ANISOU 1904 CG2 ILE A 314 4858 5400 5663 350 -858 -358 C ATOM 1905 CD1 ILE A 314 24.407 -2.394 98.579 1.00 51.88 C ANISOU 1905 CD1 ILE A 314 6171 6514 7029 289 -708 -308 C ATOM 1906 N SER A 315 23.003 -7.616 99.496 1.00 38.97 N ANISOU 1906 N SER A 315 4541 5014 5251 412 -846 -230 N ATOM 1907 CA SER A 315 22.592 -8.653 98.556 1.00 37.84 C ANISOU 1907 CA SER A 315 4377 4891 5110 413 -867 -185 C ATOM 1908 C SER A 315 21.179 -9.181 98.830 1.00 43.79 C ANISOU 1908 C SER A 315 5133 5612 5895 407 -811 -167 C ATOM 1909 O SER A 315 20.354 -9.300 97.904 1.00 41.57 O ANISOU 1909 O SER A 315 4787 5331 5679 400 -821 -141 O ATOM 1910 CB SER A 315 23.625 -9.771 98.540 1.00 39.36 C ANISOU 1910 CB SER A 315 4605 5127 5225 434 -924 -205 C ATOM 1911 OG SER A 315 24.898 -9.246 98.198 1.00 43.07 O ANISOU 1911 OG SER A 315 5031 5632 5703 430 -963 -250 O ATOM 1912 N VAL A 316 20.907 -9.468 100.120 1.00 42.75 N ANISOU 1912 N VAL A 316 5084 5441 5719 408 -747 -195 N ATOM 1913 CA VAL A 316 19.642 -9.982 100.614 1.00 43.56 C ANISOU 1913 CA VAL A 316 5203 5495 5855 380 -645 -206 C ATOM 1914 C VAL A 316 18.575 -8.913 100.420 1.00 48.91 C ANISOU 1914 C VAL A 316 5767 6151 6665 373 -601 -217 C ATOM 1915 O VAL A 316 17.571 -9.201 99.775 1.00 50.44 O ANISOU 1915 O VAL A 316 5862 6349 6953 358 -589 -225 O ATOM 1916 CB VAL A 316 19.780 -10.472 102.089 1.00 48.61 C ANISOU 1916 CB VAL A 316 6016 6071 6384 384 -569 -236 C ATOM 1917 CG1 VAL A 316 18.420 -10.678 102.752 1.00 48.53 C ANISOU 1917 CG1 VAL A 316 6028 5984 6429 332 -406 -267 C ATOM 1918 CG2 VAL A 316 20.613 -11.754 102.166 1.00 48.60 C ANISOU 1918 CG2 VAL A 316 6139 6075 6250 415 -623 -229 C ATOM 1919 N LEU A 317 18.802 -7.679 100.948 1.00 44.47 N ANISOU 1919 N LEU A 317 5215 5568 6115 391 -588 -227 N ATOM 1920 CA LEU A 317 17.887 -6.548 100.846 1.00 43.38 C ANISOU 1920 CA LEU A 317 4992 5399 6092 406 -552 -240 C ATOM 1921 C LEU A 317 17.495 -6.254 99.398 1.00 45.33 C ANISOU 1921 C LEU A 317 5132 5674 6418 440 -644 -214 C ATOM 1922 O LEU A 317 16.314 -6.008 99.137 1.00 45.08 O ANISOU 1922 O LEU A 317 5000 5626 6501 466 -632 -242 O ATOM 1923 CB LEU A 317 18.454 -5.296 101.528 1.00 43.77 C ANISOU 1923 CB LEU A 317 5100 5416 6114 419 -534 -250 C ATOM 1924 CG LEU A 317 18.467 -5.266 103.064 1.00 48.44 C ANISOU 1924 CG LEU A 317 5807 5953 6644 402 -436 -290 C ATOM 1925 CD1 LEU A 317 19.100 -3.988 103.575 1.00 47.08 C ANISOU 1925 CD1 LEU A 317 5687 5757 6446 410 -442 -306 C ATOM 1926 CD2 LEU A 317 17.064 -5.450 103.662 1.00 51.43 C ANISOU 1926 CD2 LEU A 317 6161 6272 7106 384 -295 -326 C ATOM 1927 N ASN A 318 18.462 -6.327 98.454 1.00 40.81 N ANISOU 1927 N ASN A 318 4585 5136 5783 446 -736 -172 N ATOM 1928 CA ASN A 318 18.200 -6.149 97.015 1.00 40.52 C ANISOU 1928 CA ASN A 318 4507 5107 5782 482 -827 -140 C ATOM 1929 C ASN A 318 17.305 -7.211 96.436 1.00 43.23 C ANISOU 1929 C ASN A 318 4773 5477 6175 482 -863 -153 C ATOM 1930 O ASN A 318 16.385 -6.874 95.694 1.00 42.06 O ANISOU 1930 O ASN A 318 4553 5318 6109 534 -928 -167 O ATOM 1931 CB ASN A 318 19.466 -6.018 96.196 1.00 43.38 C ANISOU 1931 CB ASN A 318 4939 5481 6061 470 -876 -103 C ATOM 1932 CG ASN A 318 19.731 -4.575 95.878 1.00 76.41 C ANISOU 1932 CG ASN A 318 9176 9610 10248 492 -869 -93 C ATOM 1933 OD1 ASN A 318 19.147 -4.005 94.941 1.00 79.19 O ANISOU 1933 OD1 ASN A 318 9548 9917 10623 548 -920 -69 O ATOM 1934 ND2 ASN A 318 20.575 -3.940 96.682 1.00 66.16 N ANISOU 1934 ND2 ASN A 318 7915 8300 8921 454 -809 -120 N ATOM 1935 N VAL A 319 17.531 -8.483 96.818 1.00 40.81 N ANISOU 1935 N VAL A 319 4489 5196 5820 430 -826 -160 N ATOM 1936 CA VAL A 319 16.719 -9.627 96.399 1.00 41.17 C ANISOU 1936 CA VAL A 319 4473 5260 5911 403 -832 -186 C ATOM 1937 C VAL A 319 15.307 -9.478 96.996 1.00 47.63 C ANISOU 1937 C VAL A 319 5179 6051 6868 392 -751 -265 C ATOM 1938 O VAL A 319 14.334 -9.532 96.244 1.00 47.60 O ANISOU 1938 O VAL A 319 5050 6061 6974 415 -813 -311 O ATOM 1939 CB VAL A 319 17.407 -10.988 96.731 1.00 45.04 C ANISOU 1939 CB VAL A 319 5056 5763 6295 354 -795 -173 C ATOM 1940 CG1 VAL A 319 16.403 -12.125 96.826 1.00 45.33 C ANISOU 1940 CG1 VAL A 319 5052 5787 6383 296 -729 -223 C ATOM 1941 CG2 VAL A 319 18.475 -11.322 95.702 1.00 44.61 C ANISOU 1941 CG2 VAL A 319 5051 5744 6155 370 -892 -119 C ATOM 1942 N LEU A 320 15.198 -9.231 98.330 1.00 44.84 N ANISOU 1942 N LEU A 320 4867 5656 6513 363 -617 -294 N ATOM 1943 CA LEU A 320 13.907 -9.054 98.991 1.00 44.74 C ANISOU 1943 CA LEU A 320 4751 5607 6642 340 -500 -384 C ATOM 1944 C LEU A 320 13.117 -7.934 98.336 1.00 48.49 C ANISOU 1944 C LEU A 320 5080 6089 7255 425 -587 -416 C ATOM 1945 O LEU A 320 11.925 -8.094 98.104 1.00 50.77 O ANISOU 1945 O LEU A 320 5204 6384 7701 428 -580 -509 O ATOM 1946 CB LEU A 320 14.053 -8.793 100.503 1.00 45.14 C ANISOU 1946 CB LEU A 320 4917 5593 6643 305 -339 -400 C ATOM 1947 CG LEU A 320 14.678 -9.886 101.373 1.00 49.83 C ANISOU 1947 CG LEU A 320 5699 6148 7085 244 -246 -384 C ATOM 1948 CD1 LEU A 320 14.859 -9.378 102.804 1.00 49.17 C ANISOU 1948 CD1 LEU A 320 5762 5990 6931 238 -123 -397 C ATOM 1949 CD2 LEU A 320 13.848 -11.199 101.342 1.00 50.71 C ANISOU 1949 CD2 LEU A 320 5791 6235 7241 159 -138 -443 C ATOM 1950 N LYS A 321 13.780 -6.835 97.995 1.00 42.84 N ANISOU 1950 N LYS A 321 4426 5367 6483 497 -674 -353 N ATOM 1951 CA LYS A 321 13.146 -5.692 97.350 1.00 42.63 C ANISOU 1951 CA LYS A 321 4320 5326 6551 602 -770 -371 C ATOM 1952 C LYS A 321 12.770 -5.937 95.872 1.00 48.19 C ANISOU 1952 C LYS A 321 4961 6061 7286 671 -948 -372 C ATOM 1953 O LYS A 321 11.654 -5.610 95.465 1.00 48.35 O ANISOU 1953 O LYS A 321 4842 6081 7446 751 -1022 -451 O ATOM 1954 CB LYS A 321 14.064 -4.459 97.470 1.00 43.45 C ANISOU 1954 CB LYS A 321 4559 5390 6560 643 -781 -301 C ATOM 1955 CG LYS A 321 13.466 -3.174 96.927 1.00 37.67 C ANISOU 1955 CG LYS A 321 3803 4612 5897 764 -862 -312 C ATOM 1956 CD LYS A 321 14.540 -2.155 96.750 1.00 43.49 C ANISOU 1956 CD LYS A 321 4710 5303 6514 779 -873 -237 C ATOM 1957 CE LYS A 321 14.022 -0.865 96.200 1.00 54.86 C ANISOU 1957 CE LYS A 321 6186 6671 7988 907 -944 -237 C ATOM 1958 NZ LYS A 321 15.121 -0.121 95.529 1.00 76.54 N ANISOU 1958 NZ LYS A 321 9127 9359 10595 907 -966 -160 N ATOM 1959 N ARG A 322 13.711 -6.449 95.068 1.00 45.61 N ANISOU 1959 N ARG A 322 4742 5756 6831 652 -1024 -295 N ATOM 1960 CA ARG A 322 13.530 -6.600 93.622 1.00 46.63 C ANISOU 1960 CA ARG A 322 4874 5895 6948 721 -1196 -282 C ATOM 1961 C ARG A 322 12.882 -7.898 93.142 1.00 53.86 C ANISOU 1961 C ARG A 322 5681 6861 7923 680 -1243 -342 C ATOM 1962 O ARG A 322 12.268 -7.909 92.073 1.00 54.19 O ANISOU 1962 O ARG A 322 5673 6909 8008 760 -1402 -377 O ATOM 1963 CB ARG A 322 14.871 -6.411 92.909 1.00 46.62 C ANISOU 1963 CB ARG A 322 5061 5875 6780 717 -1234 -178 C ATOM 1964 CG ARG A 322 15.526 -5.042 93.126 1.00 46.58 C ANISOU 1964 CG ARG A 322 5175 5807 6718 752 -1196 -132 C ATOM 1965 CD ARG A 322 14.822 -4.015 92.308 1.00 48.45 C ANISOU 1965 CD ARG A 322 5449 5979 6979 887 -1316 -137 C ATOM 1966 NE ARG A 322 15.355 -2.680 92.536 1.00 65.92 N ANISOU 1966 NE ARG A 322 7794 8114 9138 915 -1259 -100 N ATOM 1967 CZ ARG A 322 14.995 -1.623 91.825 1.00 76.59 C ANISOU 1967 CZ ARG A 322 9257 9377 10465 1039 -1346 -86 C ATOM 1968 NH1 ARG A 322 14.113 -1.748 90.842 1.00 69.02 N ANISOU 1968 NH1 ARG A 322 8291 8404 9528 1163 -1519 -109 N ATOM 1969 NH2 ARG A 322 15.524 -0.438 92.077 1.00 61.81 N ANISOU 1969 NH2 ARG A 322 7525 7421 8538 1047 -1268 -55 N ATOM 1970 N VAL A 323 13.036 -8.984 93.905 1.00 51.24 N ANISOU 1970 N VAL A 323 5336 6553 7582 562 -1111 -358 N ATOM 1971 CA VAL A 323 12.502 -10.292 93.546 1.00 51.05 C ANISOU 1971 CA VAL A 323 5232 6563 7603 497 -1119 -418 C ATOM 1972 C VAL A 323 11.263 -10.608 94.382 1.00 57.48 C ANISOU 1972 C VAL A 323 5871 7374 8594 437 -994 -553 C ATOM 1973 O VAL A 323 10.347 -11.230 93.860 1.00 58.65 O ANISOU 1973 O VAL A 323 5874 7548 8861 416 -1041 -656 O ATOM 1974 CB VAL A 323 13.594 -11.402 93.622 1.00 53.52 C ANISOU 1974 CB VAL A 323 5691 6885 7761 411 -1059 -343 C ATOM 1975 CG1 VAL A 323 13.103 -12.720 93.026 1.00 53.30 C ANISOU 1975 CG1 VAL A 323 5612 6880 7759 350 -1085 -394 C ATOM 1976 CG2 VAL A 323 14.887 -10.959 92.939 1.00 52.75 C ANISOU 1976 CG2 VAL A 323 5746 6785 7513 459 -1140 -231 C ATOM 1977 N PHE A 324 11.216 -10.173 95.651 1.00 54.39 N ANISOU 1977 N PHE A 324 5495 6946 8227 403 -828 -568 N ATOM 1978 CA PHE A 324 10.078 -10.460 96.520 1.00 55.23 C ANISOU 1978 CA PHE A 324 5457 7030 8500 328 -660 -705 C ATOM 1979 C PHE A 324 9.194 -9.236 96.812 1.00 62.70 C ANISOU 1979 C PHE A 324 6250 7961 9611 414 -661 -788 C ATOM 1980 O PHE A 324 8.314 -9.310 97.673 1.00 64.04 O ANISOU 1980 O PHE A 324 6304 8102 9928 350 -486 -908 O ATOM 1981 CB PHE A 324 10.543 -11.154 97.814 1.00 57.11 C ANISOU 1981 CB PHE A 324 5854 7211 8634 209 -432 -681 C ATOM 1982 CG PHE A 324 11.187 -12.494 97.545 1.00 58.61 C ANISOU 1982 CG PHE A 324 6173 7406 8688 134 -425 -631 C ATOM 1983 CD1 PHE A 324 12.570 -12.615 97.458 1.00 61.70 C ANISOU 1983 CD1 PHE A 324 6760 7805 8877 166 -491 -499 C ATOM 1984 CD2 PHE A 324 10.411 -13.628 97.326 1.00 60.71 C ANISOU 1984 CD2 PHE A 324 6355 7670 9041 36 -357 -730 C ATOM 1985 CE1 PHE A 324 13.162 -13.852 97.170 1.00 62.06 C ANISOU 1985 CE1 PHE A 324 6922 7854 8803 117 -494 -459 C ATOM 1986 CE2 PHE A 324 11.007 -14.858 97.031 1.00 62.65 C ANISOU 1986 CE2 PHE A 324 6739 7911 9154 -25 -352 -680 C ATOM 1987 CZ PHE A 324 12.374 -14.962 96.959 1.00 60.26 C ANISOU 1987 CZ PHE A 324 6637 7614 8644 25 -424 -541 C ATOM 1988 N GLY A 325 9.403 -8.148 96.063 1.00 59.47 N ANISOU 1988 N GLY A 325 5856 7561 9179 558 -845 -732 N ATOM 1989 CA GLY A 325 8.645 -6.909 96.162 1.00 59.45 C ANISOU 1989 CA GLY A 325 5739 7538 9312 677 -887 -798 C ATOM 1990 C GLY A 325 8.438 -6.392 97.571 1.00 65.27 C ANISOU 1990 C GLY A 325 6476 8222 10101 630 -668 -833 C ATOM 1991 O GLY A 325 7.350 -5.925 97.899 1.00 65.92 O ANISOU 1991 O GLY A 325 6376 8292 10378 673 -622 -964 O ATOM 1992 N MET A 326 9.460 -6.496 98.424 1.00 62.53 N ANISOU 1992 N MET A 326 6333 7839 9585 547 -535 -732 N ATOM 1993 CA MET A 326 9.359 -6.039 99.805 1.00 62.55 C ANISOU 1993 CA MET A 326 6390 7778 9599 500 -328 -756 C ATOM 1994 C MET A 326 9.726 -4.575 99.895 1.00 66.66 C ANISOU 1994 C MET A 326 6980 8266 10081 609 -387 -698 C ATOM 1995 O MET A 326 10.228 -4.000 98.916 1.00 66.92 O ANISOU 1995 O MET A 326 7060 8316 10049 707 -571 -624 O ATOM 1996 CB MET A 326 10.246 -6.874 100.735 1.00 65.16 C ANISOU 1996 CB MET A 326 6930 8075 9752 379 -180 -691 C ATOM 1997 CG MET A 326 9.769 -8.276 100.910 1.00 70.22 C ANISOU 1997 CG MET A 326 7543 8711 10427 258 -58 -761 C ATOM 1998 SD MET A 326 10.683 -9.094 102.228 1.00 76.44 S ANISOU 1998 SD MET A 326 8631 9419 10994 151 131 -699 S ATOM 1999 CE MET A 326 9.920 -10.724 102.176 1.00 73.33 C ANISOU 1999 CE MET A 326 8197 9001 10662 13 278 -796 C ATOM 2000 N PHE A 327 9.468 -3.972 101.081 1.00 62.34 N ANISOU 2000 N PHE A 327 6466 7655 9567 587 -212 -734 N ATOM 2001 CA PHE A 327 9.775 -2.580 101.462 1.00 61.41 C ANISOU 2001 CA PHE A 327 6437 7486 9410 666 -213 -691 C ATOM 2002 C PHE A 327 9.122 -1.505 100.583 1.00 71.06 C ANISOU 2002 C PHE A 327 7542 8706 10749 829 -369 -722 C ATOM 2003 O PHE A 327 9.621 -0.384 100.558 1.00 70.70 O ANISOU 2003 O PHE A 327 7620 8616 10626 903 -414 -656 O ATOM 2004 CB PHE A 327 11.296 -2.335 101.563 1.00 60.87 C ANISOU 2004 CB PHE A 327 6601 7411 9117 640 -259 -557 C ATOM 2005 CG PHE A 327 12.114 -3.523 101.999 1.00 59.25 C ANISOU 2005 CG PHE A 327 6516 7225 8772 528 -203 -517 C ATOM 2006 CD1 PHE A 327 12.011 -4.021 103.295 1.00 59.32 C ANISOU 2006 CD1 PHE A 327 6613 7180 8745 439 -13 -556 C ATOM 2007 CD2 PHE A 327 12.991 -4.144 101.115 1.00 59.45 C ANISOU 2007 CD2 PHE A 327 6591 7308 8691 520 -338 -444 C ATOM 2008 CE1 PHE A 327 12.759 -5.134 103.696 1.00 59.71 C ANISOU 2008 CE1 PHE A 327 6809 7231 8647 363 21 -520 C ATOM 2009 CE2 PHE A 327 13.739 -5.257 101.513 1.00 61.52 C ANISOU 2009 CE2 PHE A 327 6964 7583 8825 439 -299 -414 C ATOM 2010 CZ PHE A 327 13.611 -5.750 102.798 1.00 59.37 C ANISOU 2010 CZ PHE A 327 6791 7256 8512 370 -131 -452 C ATOM 2011 N ARG A 328 7.996 -1.824 99.903 1.00 73.10 N ANISOU 2011 N ARG A 328 7575 9006 11195 892 -453 -837 N ATOM 2012 CA ARG A 328 7.232 -0.869 99.083 1.00 75.18 C ANISOU 2012 CA ARG A 328 7723 9263 11581 1081 -628 -893 C ATOM 2013 C ARG A 328 6.233 -0.105 99.968 1.00 85.55 C ANISOU 2013 C ARG A 328 8901 10526 13078 1129 -487 -1017 C ATOM 2014 O ARG A 328 5.819 1.010 99.637 1.00 85.44 O ANISOU 2014 O ARG A 328 8862 10474 13125 1299 -594 -1042 O ATOM 2015 CB ARG A 328 6.515 -1.581 97.927 1.00 75.17 C ANISOU 2015 CB ARG A 328 7533 9332 11696 1143 -817 -980 C ATOM 2016 CG ARG A 328 7.193 -1.377 96.576 1.00 86.78 C ANISOU 2016 CG ARG A 328 9157 10810 13007 1244 -1064 -865 C ATOM 2017 CD ARG A 328 6.292 -1.760 95.412 1.00102.14 C ANISOU 2017 CD ARG A 328 10924 12805 15078 1362 -1293 -973 C ATOM 2018 NE ARG A 328 6.691 -3.032 94.802 1.00118.66 N ANISOU 2018 NE ARG A 328 13037 14958 17091 1258 -1347 -938 N ATOM 2019 CZ ARG A 328 6.058 -3.619 93.789 1.00132.61 C ANISOU 2019 CZ ARG A 328 14673 16775 18938 1322 -1542 -1025 C ATOM 2020 NH1 ARG A 328 6.497 -4.774 93.306 1.00114.22 N ANISOU 2020 NH1 ARG A 328 12389 14490 16520 1214 -1567 -984 N ATOM 2021 NH2 ARG A 328 4.978 -3.059 93.254 1.00122.26 N ANISOU 2021 NH2 ARG A 328 13186 15469 17797 1504 -1725 -1166 N ATOM 2022 N GLN A 329 5.908 -0.721 101.107 1.00 87.17 N ANISOU 2022 N GLN A 329 9052 10715 13354 978 -233 -1093 N ATOM 2023 CA GLN A 329 5.002 -0.156 102.139 1.00 89.24 C ANISOU 2023 CA GLN A 329 9201 10918 13787 973 -23 -1222 C ATOM 2024 C GLN A 329 5.696 1.038 102.803 1.00 95.86 C ANISOU 2024 C GLN A 329 10262 11672 14487 1012 42 -1120 C ATOM 2025 O GLN A 329 6.887 0.920 103.132 1.00 95.68 O ANISOU 2025 O GLN A 329 10483 11624 14249 913 107 -993 O ATOM 2026 CB GLN A 329 4.703 -1.235 103.180 1.00 91.24 C ANISOU 2026 CB GLN A 329 9421 11151 14094 768 263 -1309 C ATOM 2027 CG GLN A 329 3.881 -2.398 102.639 1.00107.88 C ANISOU 2027 CG GLN A 329 11488 13324 16179 651 234 -1317 C ATOM 2028 CD GLN A 329 3.657 -3.487 103.661 1.00123.48 C ANISOU 2028 CD GLN A 329 13752 15301 17866 563 211 -1135 C ATOM 2029 OE1 GLN A 329 4.432 -3.652 104.600 1.00119.82 O ANISOU 2029 OE1 GLN A 329 13520 14789 17218 561 245 -1016 O ATOM 2030 NE2 GLN A 329 2.584 -4.243 103.485 1.00109.12 N ANISOU 2030 NE2 GLN A 329 11915 13537 16010 493 146 -1125 N ATOM 2031 N ALA A 330 4.948 2.111 103.070 1.00 93.96 N ANISOU 2031 N ALA A 330 9937 11388 14375 1166 12 -1187 N ATOM 2032 CA ALA A 330 5.519 3.346 103.658 1.00 94.11 C ANISOU 2032 CA ALA A 330 10159 11319 14280 1219 63 -1105 C ATOM 2033 C ALA A 330 5.217 3.459 105.158 1.00 97.56 C ANISOU 2033 C ALA A 330 10650 11674 14746 1113 365 -1160 C ATOM 2034 O ALA A 330 5.442 4.549 105.708 1.00 97.89 O ANISOU 2034 O ALA A 330 10840 11635 14718 1165 412 -1115 O ATOM 2035 CB ALA A 330 4.999 4.545 102.906 1.00 94.93 C ANISOU 2035 CB ALA A 330 10201 11394 14475 1454 -122 -1137 C ATOM 2036 N SER A 331 4.777 2.381 105.810 1.00 92.38 N ANISOU 2036 N SER A 331 9909 11020 14172 957 579 -1255 N ATOM 2037 CA SER A 331 4.413 2.499 107.248 1.00 91.05 C ANISOU 2037 CA SER A 331 9826 10753 14016 840 895 -1318 C ATOM 2038 C SER A 331 5.613 2.971 108.077 1.00 90.21 C ANISOU 2038 C SER A 331 10056 10572 13647 801 940 -1173 C ATOM 2039 O SER A 331 5.448 3.933 108.838 1.00 90.27 O ANISOU 2039 O SER A 331 10125 10510 13664 881 979 -1174 O ATOM 2040 CB SER A 331 3.911 1.181 107.769 1.00 95.38 C ANISOU 2040 CB SER A 331 10337 11299 14604 657 1103 -1399 C ATOM 2041 OG SER A 331 4.995 0.292 108.000 1.00105.43 O ANISOU 2041 OG SER A 331 11798 12609 15650 562 1025 -1268 O ATOM 2042 N ASP A 332 6.787 2.371 107.877 1.00 82.57 N ANISOU 2042 N ASP A 332 9296 9624 12453 691 911 -1058 N ATOM 2043 CA ASP A 332 8.011 2.774 108.621 1.00 79.93 C ANISOU 2043 CA ASP A 332 9256 9241 11874 655 904 -940 C ATOM 2044 C ASP A 332 9.140 2.953 107.605 1.00 76.59 C ANISOU 2044 C ASP A 332 8887 8900 11313 698 641 -814 C ATOM 2045 O ASP A 332 10.024 2.093 107.525 1.00 75.05 O ANISOU 2045 O ASP A 332 8779 8755 10981 623 576 -751 O ATOM 2046 CB ASP A 332 8.339 1.808 109.758 1.00 81.92 C ANISOU 2046 CB ASP A 332 9724 9427 11976 508 1100 -940 C ATOM 2047 CG ASP A 332 9.145 2.486 110.847 1.00 89.73 C ANISOU 2047 CG ASP A 332 10999 10337 12757 486 1137 -875 C ATOM 2048 OD1 ASP A 332 9.589 3.620 110.613 1.00 88.23 O ANISOU 2048 OD1 ASP A 332 10840 10154 12529 563 1006 -820 O ATOM 2049 OD2 ASP A 332 9.316 1.878 111.915 1.00 98.28 O ANISOU 2049 OD2 ASP A 332 12295 11340 13707 392 1294 -887 O ATOM 2050 N ARG A 333 9.081 4.072 106.892 1.00 68.22 N ANISOU 2050 N ARG A 333 7778 7842 10302 829 501 -790 N ATOM 2051 CA ARG A 333 9.966 4.469 105.805 1.00 66.06 C ANISOU 2051 CA ARG A 333 7569 7610 9923 888 284 -688 C ATOM 2052 C ARG A 333 11.408 4.571 106.318 1.00 65.11 C ANISOU 2052 C ARG A 333 7681 7475 9581 791 285 -602 C ATOM 2053 O ARG A 333 12.331 4.086 105.651 1.00 64.07 O ANISOU 2053 O ARG A 333 7591 7406 9345 757 156 -535 O ATOM 2054 CB ARG A 333 9.483 5.836 105.292 1.00 67.20 C ANISOU 2054 CB ARG A 333 7693 7695 10144 1046 215 -698 C ATOM 2055 CG ARG A 333 9.927 6.240 103.897 1.00 82.73 C ANISOU 2055 CG ARG A 333 9695 9683 12054 1146 -4 -623 C ATOM 2056 CD ARG A 333 9.464 7.660 103.559 1.00102.28 C ANISOU 2056 CD ARG A 333 12219 12067 14576 1313 -52 -632 C ATOM 2057 NE ARG A 333 10.083 8.681 104.420 1.00118.56 N ANISOU 2057 NE ARG A 333 14483 14033 16531 1268 71 -598 N ATOM 2058 CZ ARG A 333 9.944 9.999 104.265 1.00129.61 C ANISOU 2058 CZ ARG A 333 15997 15328 17919 1386 59 -588 C ATOM 2059 NH1 ARG A 333 9.211 10.486 103.269 1.00118.46 N ANISOU 2059 NH1 ARG A 333 14535 13888 16587 1579 -86 -605 N ATOM 2060 NH2 ARG A 333 10.540 10.837 105.102 1.00105.77 N ANISOU 2060 NH2 ARG A 333 13162 12224 14801 1321 184 -567 N ATOM 2061 N GLU A 334 11.585 5.173 107.522 1.00 57.95 N ANISOU 2061 N GLU A 334 6919 6487 8613 747 429 -621 N ATOM 2062 CA GLU A 334 12.882 5.383 108.176 1.00 55.67 C ANISOU 2062 CA GLU A 334 6842 6178 8131 664 426 -575 C ATOM 2063 C GLU A 334 13.588 4.091 108.558 1.00 56.36 C ANISOU 2063 C GLU A 334 6995 6319 8099 568 410 -560 C ATOM 2064 O GLU A 334 14.807 4.013 108.408 1.00 56.01 O ANISOU 2064 O GLU A 334 7044 6314 7924 529 302 -519 O ATOM 2065 CB GLU A 334 12.771 6.335 109.375 1.00 56.41 C ANISOU 2065 CB GLU A 334 7079 6162 8193 652 576 -612 C ATOM 2066 CG GLU A 334 12.538 7.789 108.989 1.00 61.29 C ANISOU 2066 CG GLU A 334 7707 6716 8866 745 561 -607 C ATOM 2067 CD GLU A 334 13.542 8.451 108.057 1.00 76.83 C ANISOU 2067 CD GLU A 334 9745 8697 10749 757 414 -541 C ATOM 2068 OE1 GLU A 334 13.162 9.440 107.387 1.00 60.88 O ANISOU 2068 OE1 GLU A 334 7721 6624 8786 859 380 -529 O ATOM 2069 OE2 GLU A 334 14.704 7.983 107.996 1.00 67.97 O ANISOU 2069 OE2 GLU A 334 8690 7630 9504 667 339 -512 O ATOM 2070 N ALA A 335 12.832 3.071 108.995 1.00 51.39 N ANISOU 2070 N ALA A 335 6317 5687 7521 532 521 -605 N ATOM 2071 CA ALA A 335 13.343 1.737 109.325 1.00 50.32 C ANISOU 2071 CA ALA A 335 6266 5583 7269 457 518 -593 C ATOM 2072 C ALA A 335 14.013 1.095 108.069 1.00 52.79 C ANISOU 2072 C ALA A 335 6487 6009 7562 469 322 -533 C ATOM 2073 O ALA A 335 15.104 0.525 108.160 1.00 50.91 O ANISOU 2073 O ALA A 335 6355 5809 7179 434 233 -499 O ATOM 2074 CB ALA A 335 12.202 0.861 109.825 1.00 50.78 C ANISOU 2074 CB ALA A 335 6278 5597 7418 412 705 -662 C ATOM 2075 N VAL A 336 13.364 1.245 106.902 1.00 49.48 N ANISOU 2075 N VAL A 336 5877 5638 7287 530 247 -529 N ATOM 2076 CA VAL A 336 13.849 0.759 105.610 1.00 49.14 C ANISOU 2076 CA VAL A 336 5753 5683 7233 550 74 -475 C ATOM 2077 C VAL A 336 15.100 1.554 105.193 1.00 51.16 C ANISOU 2077 C VAL A 336 6107 5949 7382 558 -41 -418 C ATOM 2078 O VAL A 336 16.091 0.935 104.783 1.00 49.69 O ANISOU 2078 O VAL A 336 5953 5823 7103 522 -136 -382 O ATOM 2079 CB VAL A 336 12.736 0.788 104.524 1.00 52.39 C ANISOU 2079 CB VAL A 336 5961 6124 7819 629 14 -503 C ATOM 2080 CG1 VAL A 336 13.229 0.179 103.212 1.00 52.25 C ANISOU 2080 CG1 VAL A 336 5897 6186 7768 645 -159 -447 C ATOM 2081 CG2 VAL A 336 11.476 0.070 105.012 1.00 51.31 C ANISOU 2081 CG2 VAL A 336 5698 5975 7825 600 156 -598 C ATOM 2082 N TYR A 337 15.062 2.911 105.357 1.00 47.49 N ANISOU 2082 N TYR A 337 5693 5417 6932 597 -10 -423 N ATOM 2083 CA TYR A 337 16.174 3.840 105.054 1.00 47.09 C ANISOU 2083 CA TYR A 337 5748 5350 6794 583 -72 -391 C ATOM 2084 C TYR A 337 17.405 3.465 105.864 1.00 49.60 C ANISOU 2084 C TYR A 337 6176 5692 6977 494 -79 -406 C ATOM 2085 O TYR A 337 18.484 3.365 105.294 1.00 48.79 O ANISOU 2085 O TYR A 337 6086 5637 6815 458 -169 -392 O ATOM 2086 CB TYR A 337 15.797 5.324 105.332 1.00 48.61 C ANISOU 2086 CB TYR A 337 6005 5443 7022 633 -4 -405 C ATOM 2087 CG TYR A 337 14.829 5.959 104.348 1.00 50.55 C ANISOU 2087 CG TYR A 337 6176 5654 7378 756 -47 -392 C ATOM 2088 CD1 TYR A 337 14.609 5.396 103.089 1.00 52.11 C ANISOU 2088 CD1 TYR A 337 6281 5906 7611 810 -173 -361 C ATOM 2089 CD2 TYR A 337 14.164 7.142 104.658 1.00 51.30 C ANISOU 2089 CD2 TYR A 337 6308 5652 7529 835 22 -417 C ATOM 2090 CE1 TYR A 337 13.712 5.968 102.186 1.00 51.77 C ANISOU 2090 CE1 TYR A 337 6190 5825 7656 950 -248 -360 C ATOM 2091 CE2 TYR A 337 13.270 7.728 103.760 1.00 52.40 C ANISOU 2091 CE2 TYR A 337 6392 5753 7764 981 -47 -416 C ATOM 2092 CZ TYR A 337 13.044 7.132 102.525 1.00 62.83 C ANISOU 2092 CZ TYR A 337 7626 7131 9114 1044 -193 -390 C ATOM 2093 OH TYR A 337 12.188 7.704 101.612 1.00 67.93 O ANISOU 2093 OH TYR A 337 8240 7734 9838 1213 -296 -398 O ATOM 2094 N ALA A 338 17.232 3.243 107.188 1.00 45.23 N ANISOU 2094 N ALA A 338 5709 5100 6378 465 16 -448 N ATOM 2095 CA ALA A 338 18.288 2.843 108.129 1.00 44.42 C ANISOU 2095 CA ALA A 338 5737 5006 6134 411 -12 -480 C ATOM 2096 C ALA A 338 18.903 1.480 107.776 1.00 46.58 C ANISOU 2096 C ALA A 338 5985 5367 6348 397 -114 -465 C ATOM 2097 O ALA A 338 20.124 1.312 107.880 1.00 45.43 O ANISOU 2097 O ALA A 338 5882 5265 6114 374 -217 -490 O ATOM 2098 CB ALA A 338 17.745 2.833 109.555 1.00 44.97 C ANISOU 2098 CB ALA A 338 5942 4990 6156 402 122 -522 C ATOM 2099 N ALA A 339 18.060 0.504 107.360 1.00 43.50 N ANISOU 2099 N ALA A 339 5515 4999 6014 412 -87 -439 N ATOM 2100 CA ALA A 339 18.514 -0.836 106.951 1.00 41.94 C ANISOU 2100 CA ALA A 339 5300 4873 5763 404 -170 -419 C ATOM 2101 C ALA A 339 19.355 -0.729 105.666 1.00 45.25 C ANISOU 2101 C ALA A 339 5621 5371 6201 406 -304 -388 C ATOM 2102 O ALA A 339 20.434 -1.301 105.613 1.00 45.66 O ANISOU 2102 O ALA A 339 5700 5477 6172 394 -397 -400 O ATOM 2103 CB ALA A 339 17.328 -1.764 106.737 1.00 41.95 C ANISOU 2103 CB ALA A 339 5231 4869 5841 403 -89 -412 C ATOM 2104 N PHE A 340 18.894 0.045 104.668 1.00 40.90 N ANISOU 2104 N PHE A 340 4976 4814 5748 429 -310 -358 N ATOM 2105 CA PHE A 340 19.621 0.209 103.407 1.00 41.05 C ANISOU 2105 CA PHE A 340 4947 4879 5772 426 -404 -327 C ATOM 2106 C PHE A 340 20.906 1.026 103.550 1.00 45.11 C ANISOU 2106 C PHE A 340 5522 5387 6232 378 -425 -364 C ATOM 2107 O PHE A 340 21.880 0.719 102.883 1.00 44.98 O ANISOU 2107 O PHE A 340 5479 5422 6190 346 -489 -372 O ATOM 2108 CB PHE A 340 18.712 0.756 102.291 1.00 42.30 C ANISOU 2108 CB PHE A 340 5038 5010 6025 484 -415 -286 C ATOM 2109 CG PHE A 340 17.914 -0.332 101.609 1.00 42.92 C ANISOU 2109 CG PHE A 340 5016 5134 6156 514 -458 -265 C ATOM 2110 CD1 PHE A 340 16.664 -0.709 102.092 1.00 45.78 C ANISOU 2110 CD1 PHE A 340 5307 5483 6606 538 -393 -295 C ATOM 2111 CD2 PHE A 340 18.422 -0.997 100.496 1.00 44.77 C ANISOU 2111 CD2 PHE A 340 5227 5422 6362 508 -551 -229 C ATOM 2112 CE1 PHE A 340 15.925 -1.722 101.462 1.00 46.91 C ANISOU 2112 CE1 PHE A 340 5342 5669 6814 551 -429 -298 C ATOM 2113 CE2 PHE A 340 17.688 -2.016 99.868 1.00 47.37 C ANISOU 2113 CE2 PHE A 340 5470 5792 6738 530 -596 -217 C ATOM 2114 CZ PHE A 340 16.439 -2.365 100.350 1.00 45.87 C ANISOU 2114 CZ PHE A 340 5196 5592 6641 549 -540 -256 C ATOM 2115 N THR A 341 20.922 2.010 104.454 1.00 42.37 N ANISOU 2115 N THR A 341 5249 4977 5872 364 -361 -404 N ATOM 2116 CA THR A 341 22.065 2.870 104.785 1.00 41.65 C ANISOU 2116 CA THR A 341 5212 4871 5741 304 -366 -468 C ATOM 2117 C THR A 341 23.199 2.067 105.393 1.00 46.28 C ANISOU 2117 C THR A 341 5802 5529 6254 276 -454 -538 C ATOM 2118 O THR A 341 24.319 2.125 104.883 1.00 46.63 O ANISOU 2118 O THR A 341 5796 5619 6302 228 -507 -590 O ATOM 2119 CB THR A 341 21.600 4.011 105.679 1.00 43.90 C ANISOU 2119 CB THR A 341 5587 5066 6030 305 -274 -493 C ATOM 2120 OG1 THR A 341 20.691 4.782 104.906 1.00 44.91 O ANISOU 2120 OG1 THR A 341 5704 5129 6229 352 -219 -437 O ATOM 2121 CG2 THR A 341 22.751 4.894 106.163 1.00 34.35 C ANISOU 2121 CG2 THR A 341 4436 3836 4780 230 -276 -581 C ATOM 2122 N PHE A 342 22.903 1.296 106.457 1.00 43.50 N ANISOU 2122 N PHE A 342 5517 5177 5834 312 -466 -550 N ATOM 2123 CA PHE A 342 23.868 0.404 107.097 1.00 43.74 C ANISOU 2123 CA PHE A 342 5587 5262 5772 326 -576 -615 C ATOM 2124 C PHE A 342 24.414 -0.604 106.074 1.00 46.68 C ANISOU 2124 C PHE A 342 5856 5722 6160 335 -662 -596 C ATOM 2125 O PHE A 342 25.614 -0.866 106.059 1.00 47.83 O ANISOU 2125 O PHE A 342 5961 5929 6283 329 -765 -676 O ATOM 2126 CB PHE A 342 23.239 -0.326 108.308 1.00 45.95 C ANISOU 2126 CB PHE A 342 6018 5490 5951 375 -548 -609 C ATOM 2127 CG PHE A 342 24.206 -1.282 108.968 1.00 48.08 C ANISOU 2127 CG PHE A 342 6373 5797 6097 424 -685 -673 C ATOM 2128 CD1 PHE A 342 25.188 -0.815 109.844 1.00 51.42 C ANISOU 2128 CD1 PHE A 342 6866 6220 6450 434 -785 -783 C ATOM 2129 CD2 PHE A 342 24.171 -2.646 108.677 1.00 50.63 C ANISOU 2129 CD2 PHE A 342 6710 6152 6373 468 -729 -635 C ATOM 2130 CE1 PHE A 342 26.110 -1.699 110.428 1.00 52.47 C ANISOU 2130 CE1 PHE A 342 7079 6389 6469 511 -949 -859 C ATOM 2131 CE2 PHE A 342 25.092 -3.530 109.260 1.00 53.67 C ANISOU 2131 CE2 PHE A 342 7194 6563 6634 540 -873 -698 C ATOM 2132 CZ PHE A 342 26.051 -3.050 110.135 1.00 51.94 C ANISOU 2132 CZ PHE A 342 7042 6346 6347 572 -993 -811 C ATOM 2133 N SER A 343 23.539 -1.153 105.221 1.00 42.07 N ANISOU 2133 N SER A 343 5219 5144 5622 350 -622 -506 N ATOM 2134 CA SER A 343 23.916 -2.112 104.182 1.00 41.72 C ANISOU 2134 CA SER A 343 5092 5169 5589 356 -688 -477 C ATOM 2135 C SER A 343 24.845 -1.474 103.119 1.00 47.20 C ANISOU 2135 C SER A 343 5698 5895 6341 303 -706 -505 C ATOM 2136 O SER A 343 25.789 -2.136 102.678 1.00 47.01 O ANISOU 2136 O SER A 343 5617 5937 6309 298 -777 -544 O ATOM 2137 CB SER A 343 22.680 -2.746 103.551 1.00 43.07 C ANISOU 2137 CB SER A 343 5233 5329 5801 378 -641 -389 C ATOM 2138 OG SER A 343 22.199 -1.969 102.467 1.00 51.43 O ANISOU 2138 OG SER A 343 6228 6368 6945 369 -609 -344 O ATOM 2139 N HIS A 344 24.604 -0.184 102.747 1.00 44.80 N ANISOU 2139 N HIS A 344 5401 5530 6090 264 -629 -495 N ATOM 2140 CA HIS A 344 25.457 0.560 101.795 1.00 44.70 C ANISOU 2140 CA HIS A 344 5355 5509 6120 194 -599 -529 C ATOM 2141 C HIS A 344 26.790 0.852 102.468 1.00 49.60 C ANISOU 2141 C HIS A 344 5942 6165 6739 137 -632 -668 C ATOM 2142 O HIS A 344 27.832 0.622 101.863 1.00 49.84 O ANISOU 2142 O HIS A 344 5891 6243 6802 89 -651 -736 O ATOM 2143 CB HIS A 344 24.816 1.887 101.301 1.00 44.74 C ANISOU 2143 CB HIS A 344 5428 5412 6159 179 -500 -484 C ATOM 2144 CG HIS A 344 23.536 1.727 100.537 1.00 47.80 C ANISOU 2144 CG HIS A 344 5832 5765 6564 254 -497 -374 C ATOM 2145 ND1 HIS A 344 22.478 2.598 100.719 1.00 49.73 N ANISOU 2145 ND1 HIS A 344 6132 5927 6835 305 -447 -336 N ATOM 2146 CD2 HIS A 344 23.157 0.764 99.666 1.00 49.58 C ANISOU 2146 CD2 HIS A 344 6016 6031 6793 293 -552 -314 C ATOM 2147 CE1 HIS A 344 21.509 2.160 99.933 1.00 48.94 C ANISOU 2147 CE1 HIS A 344 6006 5827 6762 379 -486 -267 C ATOM 2148 NE2 HIS A 344 21.873 1.063 99.273 1.00 49.30 N ANISOU 2148 NE2 HIS A 344 5999 5943 6791 368 -549 -250 N ATOM 2149 N TRP A 345 26.752 1.301 103.737 1.00 46.68 N ANISOU 2149 N TRP A 345 5628 5773 6336 146 -643 -723 N ATOM 2150 CA TRP A 345 27.939 1.606 104.522 1.00 47.00 C ANISOU 2150 CA TRP A 345 5638 5847 6374 106 -704 -876 C ATOM 2151 C TRP A 345 28.870 0.413 104.687 1.00 51.31 C ANISOU 2151 C TRP A 345 6104 6494 6897 153 -849 -956 C ATOM 2152 O TRP A 345 30.083 0.611 104.643 1.00 52.03 O ANISOU 2152 O TRP A 345 6090 6636 7042 104 -897 -1103 O ATOM 2153 CB TRP A 345 27.577 2.179 105.900 1.00 46.25 C ANISOU 2153 CB TRP A 345 5656 5697 6219 128 -705 -908 C ATOM 2154 CG TRP A 345 28.801 2.409 106.749 1.00 47.50 C ANISOU 2154 CG TRP A 345 5785 5896 6368 102 -807 -1083 C ATOM 2155 CD1 TRP A 345 29.718 3.411 106.605 1.00 50.25 C ANISOU 2155 CD1 TRP A 345 6061 6240 6792 -6 -772 -1214 C ATOM 2156 CD2 TRP A 345 29.341 1.510 107.731 1.00 47.31 C ANISOU 2156 CD2 TRP A 345 5790 5927 6260 191 -975 -1166 C ATOM 2157 NE1 TRP A 345 30.755 3.233 107.488 1.00 49.74 N ANISOU 2157 NE1 TRP A 345 5949 6236 6713 9 -921 -1388 N ATOM 2158 CE2 TRP A 345 30.547 2.077 108.199 1.00 51.06 C ANISOU 2158 CE2 TRP A 345 6190 6439 6772 144 -1062 -1357 C ATOM 2159 CE3 TRP A 345 28.887 0.312 108.312 1.00 48.71 C ANISOU 2159 CE3 TRP A 345 6075 6109 6322 309 -1058 -1105 C ATOM 2160 CZ2 TRP A 345 31.300 1.496 109.229 1.00 50.11 C ANISOU 2160 CZ2 TRP A 345 6096 6367 6576 237 -1262 -1490 C ATOM 2161 CZ3 TRP A 345 29.645 -0.274 109.316 1.00 50.28 C ANISOU 2161 CZ3 TRP A 345 6337 6341 6426 399 -1236 -1220 C ATOM 2162 CH2 TRP A 345 30.831 0.323 109.772 1.00 50.83 C ANISOU 2162 CH2 TRP A 345 6327 6453 6532 374 -1353 -1411 C ATOM 2163 N LEU A 346 28.315 -0.808 104.920 1.00 46.73 N ANISOU 2163 N LEU A 346 5577 5936 6242 250 -913 -877 N ATOM 2164 CA LEU A 346 29.081 -2.053 105.100 1.00 45.60 C ANISOU 2164 CA LEU A 346 5400 5873 6055 326 -1056 -936 C ATOM 2165 C LEU A 346 29.910 -2.436 103.891 1.00 49.93 C ANISOU 2165 C LEU A 346 5795 6490 6687 289 -1065 -973 C ATOM 2166 O LEU A 346 30.955 -3.064 104.044 1.00 50.53 O ANISOU 2166 O LEU A 346 5791 6640 6769 333 -1187 -1090 O ATOM 2167 CB LEU A 346 28.157 -3.222 105.437 1.00 45.59 C ANISOU 2167 CB LEU A 346 5522 5849 5951 418 -1073 -825 C ATOM 2168 CG LEU A 346 28.020 -3.657 106.890 1.00 50.07 C ANISOU 2168 CG LEU A 346 6268 6375 6382 506 -1146 -855 C ATOM 2169 CD1 LEU A 346 27.427 -5.050 106.939 1.00 50.68 C ANISOU 2169 CD1 LEU A 346 6456 6435 6365 581 -1153 -769 C ATOM 2170 CD2 LEU A 346 29.370 -3.651 107.631 1.00 49.60 C ANISOU 2170 CD2 LEU A 346 6194 6366 6287 561 -1322 -1025 C ATOM 2171 N VAL A 347 29.423 -2.125 102.685 1.00 47.74 N ANISOU 2171 N VAL A 347 5491 6182 6467 223 -944 -877 N ATOM 2172 CA VAL A 347 30.108 -2.429 101.418 1.00 48.18 C ANISOU 2172 CA VAL A 347 5439 6276 6591 175 -913 -897 C ATOM 2173 C VAL A 347 31.444 -1.659 101.374 1.00 52.86 C ANISOU 2173 C VAL A 347 5909 6894 7280 81 -892 -1079 C ATOM 2174 O VAL A 347 32.471 -2.206 100.959 1.00 53.80 O ANISOU 2174 O VAL A 347 5900 7083 7459 74 -934 -1188 O ATOM 2175 CB VAL A 347 29.173 -2.110 100.205 1.00 52.03 C ANISOU 2175 CB VAL A 347 5982 6695 7091 135 -791 -753 C ATOM 2176 CG1 VAL A 347 29.949 -1.972 98.898 1.00 51.74 C ANISOU 2176 CG1 VAL A 347 5885 6657 7118 52 -711 -789 C ATOM 2177 CG2 VAL A 347 28.076 -3.162 100.071 1.00 51.68 C ANISOU 2177 CG2 VAL A 347 5996 6654 6985 220 -830 -619 C ATOM 2178 N TYR A 348 31.411 -0.397 101.834 1.00 47.51 N ANISOU 2178 N TYR A 348 5266 6158 6628 7 -820 -1126 N ATOM 2179 CA TYR A 348 32.557 0.493 101.886 1.00 46.74 C ANISOU 2179 CA TYR A 348 5061 6067 6632 -108 -773 -1313 C ATOM 2180 C TYR A 348 33.474 0.130 103.043 1.00 54.32 C ANISOU 2180 C TYR A 348 5923 7115 7600 -48 -953 -1494 C ATOM 2181 O TYR A 348 34.705 0.176 102.901 1.00 55.18 O ANISOU 2181 O TYR A 348 5857 7287 7821 -104 -978 -1690 O ATOM 2182 CB TYR A 348 32.071 1.946 101.958 1.00 46.24 C ANISOU 2182 CB TYR A 348 5103 5892 6575 -203 -627 -1287 C ATOM 2183 CG TYR A 348 31.307 2.340 100.714 1.00 44.40 C ANISOU 2183 CG TYR A 348 4980 5562 6329 -242 -472 -1133 C ATOM 2184 CD1 TYR A 348 31.911 2.293 99.456 1.00 45.45 C ANISOU 2184 CD1 TYR A 348 5075 5677 6517 -327 -363 -1158 C ATOM 2185 CD2 TYR A 348 29.957 2.678 100.780 1.00 43.47 C ANISOU 2185 CD2 TYR A 348 5011 5366 6140 -178 -444 -969 C ATOM 2186 CE1 TYR A 348 31.191 2.569 98.298 1.00 44.22 C ANISOU 2186 CE1 TYR A 348 5061 5421 6319 -336 -249 -1012 C ATOM 2187 CE2 TYR A 348 29.228 2.961 99.625 1.00 43.68 C ANISOU 2187 CE2 TYR A 348 5143 5307 6147 -177 -347 -837 C ATOM 2188 CZ TYR A 348 29.856 2.917 98.389 1.00 48.44 C ANISOU 2188 CZ TYR A 348 5742 5885 6779 -252 -258 -855 C ATOM 2189 OH TYR A 348 29.180 3.228 97.243 1.00 49.08 O ANISOU 2189 OH TYR A 348 5969 5864 6816 -238 -177 -731 O ATOM 2190 N ALA A 349 32.873 -0.276 104.177 1.00 51.47 N ANISOU 2190 N ALA A 349 5682 6754 7122 74 -1079 -1439 N ATOM 2191 CA ALA A 349 33.572 -0.743 105.368 1.00 51.67 C ANISOU 2191 CA ALA A 349 5688 6843 7103 177 -1286 -1586 C ATOM 2192 C ALA A 349 34.516 -1.909 104.999 1.00 56.57 C ANISOU 2192 C ALA A 349 6165 7567 7763 258 -1422 -1684 C ATOM 2193 O ALA A 349 35.561 -2.076 105.625 1.00 56.37 O ANISOU 2193 O ALA A 349 6032 7613 7773 316 -1591 -1885 O ATOM 2194 CB ALA A 349 32.559 -1.192 106.412 1.00 52.28 C ANISOU 2194 CB ALA A 349 5984 6867 7013 298 -1354 -1462 C ATOM 2195 N ASN A 350 34.172 -2.664 103.937 1.00 53.97 N ANISOU 2195 N ASN A 350 5826 7244 7437 264 -1350 -1556 N ATOM 2196 CA ASN A 350 34.965 -3.783 103.436 1.00 53.52 C ANISOU 2196 CA ASN A 350 5645 7272 7418 337 -1446 -1627 C ATOM 2197 C ASN A 350 36.329 -3.346 102.891 1.00 57.90 C ANISOU 2197 C ASN A 350 5949 7892 8159 236 -1415 -1853 C ATOM 2198 O ASN A 350 37.318 -4.028 103.151 1.00 57.24 O ANISOU 2198 O ASN A 350 5724 7898 8126 330 -1577 -2023 O ATOM 2199 CB ASN A 350 34.188 -4.578 102.405 1.00 51.53 C ANISOU 2199 CB ASN A 350 5462 6996 7121 348 -1355 -1433 C ATOM 2200 CG ASN A 350 34.876 -5.861 102.038 1.00 67.74 C ANISOU 2200 CG ASN A 350 7431 9125 9182 448 -1464 -1487 C ATOM 2201 OD1 ASN A 350 34.896 -6.811 102.824 1.00 59.65 O ANISOU 2201 OD1 ASN A 350 6491 8122 8050 605 -1633 -1491 O ATOM 2202 ND2 ASN A 350 35.491 -5.897 100.855 1.00 56.87 N ANISOU 2202 ND2 ASN A 350 5906 7776 7927 362 -1361 -1540 N ATOM 2203 N SER A 351 36.382 -2.204 102.164 1.00 55.56 N ANISOU 2203 N SER A 351 5605 7539 7965 51 -1202 -1869 N ATOM 2204 CA SER A 351 37.598 -1.608 101.590 1.00 55.77 C ANISOU 2204 CA SER A 351 5412 7596 8181 -95 -1098 -2092 C ATOM 2205 C SER A 351 38.560 -1.181 102.687 1.00 61.75 C ANISOU 2205 C SER A 351 6017 8422 9023 -85 -1251 -2357 C ATOM 2206 O SER A 351 39.768 -1.229 102.474 1.00 61.61 O ANISOU 2206 O SER A 351 5754 8480 9175 -132 -1269 -2601 O ATOM 2207 CB SER A 351 37.250 -0.409 100.717 1.00 60.15 C ANISOU 2207 CB SER A 351 6042 8034 8779 -291 -822 -2024 C ATOM 2208 OG SER A 351 36.382 -0.788 99.660 1.00 74.79 O ANISOU 2208 OG SER A 351 8040 9823 10552 -286 -707 -1798 O ATOM 2209 N ALA A 352 38.026 -0.762 103.860 1.00 59.61 N ANISOU 2209 N ALA A 352 5888 8120 8639 -23 -1361 -2323 N ATOM 2210 CA ALA A 352 38.818 -0.383 105.037 1.00 59.53 C ANISOU 2210 CA ALA A 352 5782 8165 8671 13 -1547 -2562 C ATOM 2211 C ALA A 352 39.259 -1.644 105.796 1.00 64.78 C ANISOU 2211 C ALA A 352 6426 8925 9264 251 -1856 -2643 C ATOM 2212 O ALA A 352 40.343 -1.661 106.373 1.00 64.65 O ANISOU 2212 O ALA A 352 6224 8995 9345 303 -2044 -2914 O ATOM 2213 CB ALA A 352 38.016 0.538 105.954 1.00 59.84 C ANISOU 2213 CB ALA A 352 6029 8115 8595 -9 -1529 -2477 C ATOM 2214 N ALA A 353 38.439 -2.709 105.746 1.00 63.10 N ANISOU 2214 N ALA A 353 6401 8688 8884 395 -1907 -2422 N ATOM 2215 CA ALA A 353 38.687 -3.987 106.416 1.00 63.27 C ANISOU 2215 CA ALA A 353 6487 8763 8791 634 -2174 -2452 C ATOM 2216 C ALA A 353 39.902 -4.757 105.900 1.00 69.38 C ANISOU 2216 C ALA A 353 7001 9651 9710 704 -2289 -2652 C ATOM 2217 O ALA A 353 40.718 -5.194 106.724 1.00 70.32 O ANISOU 2217 O ALA A 353 7054 9839 9826 874 -2563 -2853 O ATOM 2218 CB ALA A 353 37.446 -4.865 106.366 1.00 63.62 C ANISOU 2218 CB ALA A 353 6803 8732 8637 726 -2134 -2165 C ATOM 2219 N ASN A 354 40.034 -4.928 104.563 1.00 65.26 N ANISOU 2219 N ASN A 354 6344 9143 9310 589 -2091 -2607 N ATOM 2220 CA ASN A 354 41.124 -5.717 103.967 1.00 64.93 C ANISOU 2220 CA ASN A 354 6058 9199 9413 650 -2161 -2784 C ATOM 2221 C ASN A 354 42.520 -5.297 104.427 1.00 67.94 C ANISOU 2221 C ASN A 354 6132 9684 9997 654 -2310 -3155 C ATOM 2222 O ASN A 354 43.220 -6.174 104.926 1.00 68.12 O ANISOU 2222 O ASN A 354 6074 9788 10019 868 -2581 -3309 O ATOM 2223 CB ASN A 354 41.062 -5.783 102.432 1.00 64.64 C ANISOU 2223 CB ASN A 354 5940 9140 9480 491 -1883 -2692 C ATOM 2224 CG ASN A 354 39.738 -6.214 101.866 1.00 72.41 C ANISOU 2224 CG ASN A 354 7189 10034 10290 490 -1755 -2360 C ATOM 2225 OD1 ASN A 354 39.096 -7.158 102.347 1.00 56.80 O ANISOU 2225 OD1 ASN A 354 5405 8041 8134 659 -1894 -2213 O ATOM 2226 ND2 ASN A 354 39.308 -5.519 100.819 1.00 64.82 N ANISOU 2226 ND2 ASN A 354 6249 9001 9377 297 -1485 -2249 N ATOM 2227 N PRO A 355 42.964 -4.014 104.330 1.00 63.51 N ANISOU 2227 N PRO A 355 5403 9119 9608 439 -2161 -3321 N ATOM 2228 CA PRO A 355 44.321 -3.676 104.806 1.00 62.60 C ANISOU 2228 CA PRO A 355 4965 9113 9708 442 -2319 -3712 C ATOM 2229 C PRO A 355 44.535 -3.921 106.299 1.00 66.10 C ANISOU 2229 C PRO A 355 5482 9601 10032 678 -2701 -3835 C ATOM 2230 O PRO A 355 45.654 -4.205 106.700 1.00 65.92 O ANISOU 2230 O PRO A 355 5206 9690 10151 797 -2942 -4148 O ATOM 2231 CB PRO A 355 44.483 -2.205 104.420 1.00 64.25 C ANISOU 2231 CB PRO A 355 5065 9269 10079 139 -2036 -3810 C ATOM 2232 CG PRO A 355 43.443 -1.947 103.395 1.00 69.07 C ANISOU 2232 CG PRO A 355 5889 9757 10598 -11 -1714 -3495 C ATOM 2233 CD PRO A 355 42.295 -2.819 103.777 1.00 65.05 C ANISOU 2233 CD PRO A 355 5692 9207 9818 187 -1846 -3186 C ATOM 2234 N ILE A 356 43.463 -3.850 107.110 1.00 63.58 N ANISOU 2234 N ILE A 356 5516 9188 9452 756 -2761 -3600 N ATOM 2235 CA ILE A 356 43.506 -4.145 108.545 1.00 64.04 C ANISOU 2235 CA ILE A 356 5745 9252 9337 991 -3106 -3671 C ATOM 2236 C ILE A 356 43.739 -5.673 108.732 1.00 70.97 C ANISOU 2236 C ILE A 356 6701 10170 10094 1290 -3369 -3658 C ATOM 2237 O ILE A 356 44.542 -6.077 109.580 1.00 70.76 O ANISOU 2237 O ILE A 356 6622 10209 10055 1511 -3712 -3891 O ATOM 2238 CB ILE A 356 42.253 -3.583 109.294 1.00 66.35 C ANISOU 2238 CB ILE A 356 6407 9411 9393 959 -3034 -3424 C ATOM 2239 CG1 ILE A 356 42.232 -2.037 109.231 1.00 65.77 C ANISOU 2239 CG1 ILE A 356 6236 9302 9450 694 -2824 -3498 C ATOM 2240 CG2 ILE A 356 42.196 -4.067 110.758 1.00 66.71 C ANISOU 2240 CG2 ILE A 356 6714 9428 9204 1222 -3373 -3458 C ATOM 2241 CD1 ILE A 356 40.887 -1.373 109.558 1.00 66.20 C ANISOU 2241 CD1 ILE A 356 6614 9217 9322 609 -2646 -3223 C ATOM 2242 N ILE A 357 43.079 -6.505 107.889 1.00 68.75 N ANISOU 2242 N ILE A 357 6542 9848 9732 1299 -3213 -3405 N ATOM 2243 CA ILE A 357 43.234 -7.966 107.877 1.00 68.33 C ANISOU 2243 CA ILE A 357 6580 9815 9567 1553 -3402 -3366 C ATOM 2244 C ILE A 357 44.689 -8.326 107.505 1.00 73.31 C ANISOU 2244 C ILE A 357 6820 10589 10446 1636 -3559 -3700 C ATOM 2245 O ILE A 357 45.297 -9.144 108.203 1.00 73.86 O ANISOU 2245 O ILE A 357 6912 10703 10448 1919 -3896 -3850 O ATOM 2246 CB ILE A 357 42.170 -8.672 106.964 1.00 71.07 C ANISOU 2246 CB ILE A 357 7125 10083 9794 1500 -3162 -3029 C ATOM 2247 CG1 ILE A 357 40.725 -8.399 107.451 1.00 70.99 C ANISOU 2247 CG1 ILE A 357 7484 9938 9553 1447 -3036 -2735 C ATOM 2248 CG2 ILE A 357 42.420 -10.188 106.836 1.00 70.94 C ANISOU 2248 CG2 ILE A 357 7187 10084 9682 1744 -3331 -3006 C ATOM 2249 CD1 ILE A 357 39.655 -8.396 106.335 1.00 74.29 C ANISOU 2249 CD1 ILE A 357 7975 10289 9962 1265 -2712 -2456 C ATOM 2250 N TYR A 358 45.262 -7.689 106.453 1.00 69.80 N ANISOU 2250 N TYR A 358 6028 10204 10288 1397 -3316 -3834 N ATOM 2251 CA TYR A 358 46.646 -7.972 106.039 1.00 69.81 C ANISOU 2251 CA TYR A 358 5617 10339 10568 1442 -3414 -4178 C ATOM 2252 C TYR A 358 47.649 -7.546 107.112 1.00 77.64 C ANISOU 2252 C TYR A 358 6403 11424 11673 1558 -3736 -4547 C ATOM 2253 O TYR A 358 48.718 -8.139 107.228 1.00 77.95 O ANISOU 2253 O TYR A 358 6181 11576 11862 1742 -3981 -4840 O ATOM 2254 CB TYR A 358 47.038 -7.334 104.687 1.00 69.83 C ANISOU 2254 CB TYR A 358 5320 10361 10850 1133 -3038 -4254 C ATOM 2255 CG TYR A 358 46.027 -7.332 103.554 1.00 70.23 C ANISOU 2255 CG TYR A 358 5567 10305 10812 950 -2678 -3911 C ATOM 2256 CD1 TYR A 358 45.110 -8.372 103.399 1.00 71.34 C ANISOU 2256 CD1 TYR A 358 6010 10383 10711 1094 -2703 -3605 C ATOM 2257 CD2 TYR A 358 46.059 -6.347 102.575 1.00 71.10 C ANISOU 2257 CD2 TYR A 358 5556 10371 11088 637 -2313 -3917 C ATOM 2258 CE1 TYR A 358 44.188 -8.376 102.348 1.00 70.26 C ANISOU 2258 CE1 TYR A 358 6037 10156 10504 935 -2401 -3315 C ATOM 2259 CE2 TYR A 358 45.151 -6.345 101.518 1.00 72.18 C ANISOU 2259 CE2 TYR A 358 5890 10403 11131 493 -2015 -3616 C ATOM 2260 CZ TYR A 358 44.217 -7.360 101.405 1.00 75.58 C ANISOU 2260 CZ TYR A 358 6598 10789 11330 647 -2073 -3321 C ATOM 2261 OH TYR A 358 43.328 -7.314 100.357 1.00 71.67 O ANISOU 2261 OH TYR A 358 6279 10195 10755 507 -1800 -3051 O ATOM 2262 N ASN A 359 47.301 -6.521 107.894 1.00 77.01 N ANISOU 2262 N ASN A 359 6438 11296 11525 1460 -3744 -4546 N ATOM 2263 CA ASN A 359 48.126 -6.004 108.979 1.00 77.51 C ANISOU 2263 CA ASN A 359 6349 11433 11670 1554 -4052 -4884 C ATOM 2264 C ASN A 359 48.267 -7.053 110.093 1.00 84.02 C ANISOU 2264 C ASN A 359 7399 12264 12259 1957 -4511 -4921 C ATOM 2265 O ASN A 359 49.391 -7.375 110.465 1.00 84.75 O ANISOU 2265 O ASN A 359 7230 12474 12499 2150 -4832 -5271 O ATOM 2266 CB ASN A 359 47.534 -4.696 109.516 1.00 76.98 C ANISOU 2266 CB ASN A 359 6422 11284 11542 1346 -3918 -4818 C ATOM 2267 CG ASN A 359 48.387 -3.993 110.544 1.00 95.43 C ANISOU 2267 CG ASN A 359 8581 13692 13985 1392 -4199 -5183 C ATOM 2268 OD1 ASN A 359 49.534 -3.605 110.286 1.00 88.47 O ANISOU 2268 OD1 ASN A 359 7260 12930 13423 1307 -4231 -5559 O ATOM 2269 ND2 ASN A 359 47.830 -3.794 111.732 1.00 83.64 N ANISOU 2269 ND2 ASN A 359 7428 12122 12230 1518 -4397 -5093 N ATOM 2270 N PHE A 360 47.147 -7.628 110.580 1.00 81.00 N ANISOU 2270 N PHE A 360 7504 11751 11523 2092 -4537 -4577 N ATOM 2271 CA PHE A 360 47.201 -8.609 111.666 1.00 81.03 C ANISOU 2271 CA PHE A 360 7812 11719 11257 2470 -4941 -4587 C ATOM 2272 C PHE A 360 47.547 -10.036 111.234 1.00 84.63 C ANISOU 2272 C PHE A 360 8273 12205 11677 2720 -5078 -4575 C ATOM 2273 O PHE A 360 48.256 -10.713 111.969 1.00 84.75 O ANISOU 2273 O PHE A 360 8328 12255 11618 3049 -5481 -4775 O ATOM 2274 CB PHE A 360 45.905 -8.602 112.496 1.00 83.07 C ANISOU 2274 CB PHE A 360 8616 11803 11144 2505 -4900 -4259 C ATOM 2275 CG PHE A 360 45.620 -7.290 113.192 1.00 85.08 C ANISOU 2275 CG PHE A 360 8925 12017 11387 2336 -4849 -4297 C ATOM 2276 CD1 PHE A 360 46.333 -6.913 114.324 1.00 88.41 C ANISOU 2276 CD1 PHE A 360 9334 12472 11787 2493 -5206 -4583 C ATOM 2277 CD2 PHE A 360 44.623 -6.440 112.728 1.00 87.68 C ANISOU 2277 CD2 PHE A 360 9332 12265 11715 2035 -4459 -4051 C ATOM 2278 CE1 PHE A 360 46.075 -5.694 114.961 1.00 89.50 C ANISOU 2278 CE1 PHE A 360 9530 12565 11910 2329 -5151 -4621 C ATOM 2279 CE2 PHE A 360 44.361 -5.226 113.370 1.00 90.65 C ANISOU 2279 CE2 PHE A 360 9770 12595 12079 1886 -4405 -4086 C ATOM 2280 CZ PHE A 360 45.091 -4.858 114.480 1.00 88.67 C ANISOU 2280 CZ PHE A 360 9503 12378 11810 2024 -4741 -4368 C ATOM 2281 N LEU A 361 47.061 -10.495 110.065 1.00 80.81 N ANISOU 2281 N LEU A 361 7771 11701 11234 2583 -4765 -4350 N ATOM 2282 CA LEU A 361 47.257 -11.871 109.587 1.00 79.79 C ANISOU 2282 CA LEU A 361 7688 11579 11048 2801 -4853 -4299 C ATOM 2283 C LEU A 361 48.392 -12.054 108.543 1.00 84.76 C ANISOU 2283 C LEU A 361 7813 12358 12036 2761 -4809 -4566 C ATOM 2284 O LEU A 361 48.524 -13.135 107.940 1.00 84.43 O ANISOU 2284 O LEU A 361 7780 12322 11977 2898 -4816 -4510 O ATOM 2285 CB LEU A 361 45.927 -12.437 109.071 1.00 79.26 C ANISOU 2285 CB LEU A 361 7989 11376 10751 2717 -4570 -3872 C ATOM 2286 CG LEU A 361 44.852 -12.657 110.133 1.00 83.12 C ANISOU 2286 CG LEU A 361 9012 11704 10864 2830 -4641 -3626 C ATOM 2287 CD1 LEU A 361 43.505 -12.566 109.540 1.00 82.98 C ANISOU 2287 CD1 LEU A 361 9211 11578 10739 2600 -4268 -3265 C ATOM 2288 CD2 LEU A 361 45.013 -13.992 110.840 1.00 84.94 C ANISOU 2288 CD2 LEU A 361 9567 11870 10837 3206 -4958 -3621 C ATOM 2289 N SER A 362 49.236 -11.022 108.374 1.00 82.10 N ANISOU 2289 N SER A 362 7041 12133 12019 2578 -4763 -4876 N ATOM 2290 CA SER A 362 50.412 -11.070 107.506 1.00 82.69 C ANISOU 2290 CA SER A 362 6604 12348 12468 2521 -4711 -5193 C ATOM 2291 C SER A 362 51.529 -10.255 108.152 1.00 90.50 C ANISOU 2291 C SER A 362 7207 13461 13718 2527 -4940 -5644 C ATOM 2292 O SER A 362 51.355 -9.060 108.408 1.00 91.36 O ANISOU 2292 O SER A 362 7271 13555 13889 2287 -4807 -5683 O ATOM 2293 CB SER A 362 50.098 -10.588 106.093 1.00 84.41 C ANISOU 2293 CB SER A 362 6673 12541 12857 2152 -4208 -5048 C ATOM 2294 OG SER A 362 51.256 -10.154 105.399 1.00 88.33 O ANISOU 2294 OG SER A 362 6654 13155 13751 2001 -4088 -5404 O ATOM 2295 N GLY A 363 52.635 -10.928 108.462 1.00 87.46 N ANISOU 2295 N GLY A 363 6565 13193 13472 2818 -5301 -5987 N ATOM 2296 CA GLY A 363 53.796 -10.304 109.080 1.00 87.73 C ANISOU 2296 CA GLY A 363 6187 13365 13782 2866 -5574 -6471 C ATOM 2297 C GLY A 363 54.571 -9.406 108.137 1.00 92.93 C ANISOU 2297 C GLY A 363 6297 14121 14889 2505 -5239 -6757 C ATOM 2298 O GLY A 363 55.138 -8.399 108.568 1.00 93.03 O ANISOU 2298 O GLY A 363 6041 14199 15107 2363 -5284 -7060 O ATOM 2299 N LYS A 364 54.598 -9.775 106.845 1.00 90.24 N ANISOU 2299 N LYS A 364 5810 13779 14696 2349 -4886 -6669 N ATOM 2300 CA LYS A 364 55.265 -9.047 105.765 1.00 90.36 C ANISOU 2300 CA LYS A 364 5366 13850 15116 1989 -4486 -6901 C ATOM 2301 C LYS A 364 54.560 -7.707 105.485 1.00 94.79 C ANISOU 2301 C LYS A 364 6046 14308 15661 1574 -4080 -6723 C ATOM 2302 O LYS A 364 55.246 -6.685 105.386 1.00 95.99 O ANISOU 2302 O LYS A 364 5841 14513 16119 1321 -3932 -7044 O ATOM 2303 CB LYS A 364 55.345 -9.920 104.496 1.00 92.87 C ANISOU 2303 CB LYS A 364 5612 14159 15517 1965 -4224 -6792 C ATOM 2304 CG LYS A 364 56.478 -10.933 104.520 1.00100.62 C ANISOU 2304 CG LYS A 364 6249 15277 16705 2279 -4530 -7143 C ATOM 2305 CD LYS A 364 56.419 -11.867 103.327 1.00108.15 C ANISOU 2305 CD LYS A 364 7211 16199 17684 2274 -4275 -6985 C ATOM 2306 CE LYS A 364 57.515 -12.912 103.347 1.00113.74 C ANISOU 2306 CE LYS A 364 7596 17034 18586 2611 -4582 -7323 C ATOM 2307 NZ LYS A 364 57.317 -13.932 104.415 1.00118.12 N ANISOU 2307 NZ LYS A 364 8480 17582 18819 3089 -5108 -7228 N ATOM 2308 N PHE A 365 53.201 -7.706 105.408 1.00 89.43 N ANISOU 2308 N PHE A 365 5868 13479 14632 1513 -3912 -6234 N ATOM 2309 CA PHE A 365 52.389 -6.499 105.199 1.00 88.66 C ANISOU 2309 CA PHE A 365 5953 13266 14469 1171 -3560 -6022 C ATOM 2310 C PHE A 365 52.485 -5.568 106.400 1.00 94.61 C ANISOU 2310 C PHE A 365 6713 14034 15200 1166 -3777 -6189 C ATOM 2311 O PHE A 365 52.589 -4.355 106.213 1.00 94.64 O ANISOU 2311 O PHE A 365 6586 14010 15363 853 -3517 -6295 O ATOM 2312 CB PHE A 365 50.911 -6.836 104.907 1.00 89.73 C ANISOU 2312 CB PHE A 365 6601 13251 14242 1163 -3389 -5487 C ATOM 2313 CG PHE A 365 50.576 -7.000 103.442 1.00 90.56 C ANISOU 2313 CG PHE A 365 6721 13288 14398 952 -2966 -5283 C ATOM 2314 CD1 PHE A 365 50.683 -5.928 102.560 1.00 92.69 C ANISOU 2314 CD1 PHE A 365 6852 13505 14860 583 -2547 -5330 C ATOM 2315 CD2 PHE A 365 50.142 -8.225 102.942 1.00 92.07 C ANISOU 2315 CD2 PHE A 365 7102 13453 14427 1123 -2985 -5042 C ATOM 2316 CE1 PHE A 365 50.401 -6.090 101.200 1.00 93.28 C ANISOU 2316 CE1 PHE A 365 6980 13501 14960 404 -2169 -5149 C ATOM 2317 CE2 PHE A 365 49.837 -8.379 101.586 1.00 94.26 C ANISOU 2317 CE2 PHE A 365 7410 13663 14741 934 -2610 -4862 C ATOM 2318 CZ PHE A 365 49.969 -7.311 100.724 1.00 92.11 C ANISOU 2318 CZ PHE A 365 7009 13338 14653 583 -2212 -4915 C ATOM 2319 N ARG A 366 52.473 -6.144 107.629 1.00 92.07 N ANISOU 2319 N ARG A 366 6569 13744 14671 1518 -4251 -6219 N ATOM 2320 CA ARG A 366 52.599 -5.448 108.916 1.00 92.16 C ANISOU 2320 CA ARG A 366 6631 13769 14617 1588 -4543 -6388 C ATOM 2321 C ARG A 366 53.910 -4.663 108.973 1.00 98.49 C ANISOU 2321 C ARG A 366 6884 14706 15831 1450 -4592 -6918 C ATOM 2322 O ARG A 366 53.895 -3.514 109.399 1.00 97.11 O ANISOU 2322 O ARG A 366 6678 14507 15712 1241 -4516 -7022 O ATOM 2323 CB ARG A 366 52.520 -6.463 110.069 1.00 90.68 C ANISOU 2323 CB ARG A 366 6731 13585 14138 2037 -5057 -6356 C ATOM 2324 CG ARG A 366 52.516 -5.870 111.478 1.00 95.91 C ANISOU 2324 CG ARG A 366 7558 14231 14651 2152 -5387 -6479 C ATOM 2325 CD ARG A 366 51.903 -6.804 112.518 1.00106.87 C ANISOU 2325 CD ARG A 366 9462 15529 15614 2535 -5750 -6259 C ATOM 2326 NE ARG A 366 52.295 -8.205 112.333 1.00123.54 N ANISOU 2326 NE ARG A 366 11579 17682 17677 2866 -5986 -6281 N ATOM 2327 CZ ARG A 366 51.587 -9.250 112.754 1.00141.53 C ANISOU 2327 CZ ARG A 366 14346 19848 19583 3143 -6140 -5989 C ATOM 2328 NH1 ARG A 366 50.445 -9.068 113.409 1.00133.53 N ANISOU 2328 NH1 ARG A 366 13842 18675 18219 3128 -6079 -5660 N ATOM 2329 NH2 ARG A 366 52.014 -10.484 112.524 1.00124.27 N ANISOU 2329 NH2 ARG A 366 12148 17697 17374 3432 -6337 -6030 N ATOM 2330 N GLU A 367 55.031 -5.278 108.514 1.00 98.63 N ANISOU 2330 N GLU A 367 6463 14862 16150 1553 -4696 -7262 N ATOM 2331 CA GLU A 367 56.357 -4.654 108.469 1.00 99.91 C ANISOU 2331 CA GLU A 367 6036 15166 16759 1420 -4726 -7816 C ATOM 2332 C GLU A 367 56.329 -3.387 107.616 1.00105.09 C ANISOU 2332 C GLU A 367 6528 15759 17643 920 -4174 -7846 C ATOM 2333 O GLU A 367 56.879 -2.363 108.025 1.00105.87 O ANISOU 2333 O GLU A 367 6374 15899 17955 734 -4170 -8171 O ATOM 2334 CB GLU A 367 57.427 -5.625 107.934 1.00101.87 C ANISOU 2334 CB GLU A 367 5861 15554 17292 1602 -4852 -8129 C ATOM 2335 CG GLU A 367 57.741 -6.836 108.803 1.00118.96 C ANISOU 2335 CG GLU A 367 8114 17792 19291 2124 -5437 -8206 C ATOM 2336 CD GLU A 367 58.197 -6.578 110.225 1.00157.11 C ANISOU 2336 CD GLU A 367 12929 22694 24070 2381 -5977 -8498 C ATOM 2337 OE1 GLU A 367 59.418 -6.398 110.437 1.00156.43 O ANISOU 2337 OE1 GLU A 367 12321 22767 24346 2444 -6214 -9033 O ATOM 2338 OE2 GLU A 367 57.331 -6.572 111.131 1.00160.59 O ANISOU 2338 OE2 GLU A 367 13882 23026 24110 2524 -6165 -8202 O ATOM 2339 N GLN A 368 55.656 -3.452 106.454 1.00101.37 N ANISOU 2339 N GLN A 368 6236 15174 17105 708 -3717 -7502 N ATOM 2340 CA GLN A 368 55.504 -2.330 105.525 1.00100.86 C ANISOU 2340 CA GLN A 368 6120 15009 17195 251 -3162 -7465 C ATOM 2341 C GLN A 368 54.610 -1.241 106.099 1.00104.04 C ANISOU 2341 C GLN A 368 6869 15286 17377 87 -3066 -7240 C ATOM 2342 O GLN A 368 54.898 -0.054 105.910 1.00104.18 O ANISOU 2342 O GLN A 368 6734 15262 17587 -246 -2781 -7420 O ATOM 2343 CB GLN A 368 54.955 -2.805 104.170 1.00101.96 C ANISOU 2343 CB GLN A 368 6425 15048 17268 130 -2758 -7134 C ATOM 2344 CG GLN A 368 55.751 -3.931 103.516 1.00109.17 C ANISOU 2344 CG GLN A 368 7039 16064 18377 287 -2809 -7314 C ATOM 2345 CD GLN A 368 57.210 -3.623 103.286 1.00119.81 C ANISOU 2345 CD GLN A 368 7776 17539 20208 153 -2750 -7888 C ATOM 2346 OE1 GLN A 368 57.613 -2.478 103.033 1.00110.50 O ANISOU 2346 OE1 GLN A 368 6392 16326 19267 -201 -2435 -8113 O ATOM 2347 NE2 GLN A 368 58.033 -4.659 103.358 1.00112.53 N ANISOU 2347 NE2 GLN A 368 6551 16759 19446 436 -3042 -8147 N ATOM 2348 N PHE A 369 53.529 -1.644 106.799 1.00 99.06 N ANISOU 2348 N PHE A 369 6710 14585 16343 313 -3283 -6854 N ATOM 2349 CA PHE A 369 52.593 -0.715 107.428 1.00 98.25 C ANISOU 2349 CA PHE A 369 6967 14360 16004 202 -3220 -6619 C ATOM 2350 C PHE A 369 53.266 0.009 108.596 1.00103.23 C ANISOU 2350 C PHE A 369 7416 15064 16741 224 -3513 -6988 C ATOM 2351 O PHE A 369 53.116 1.225 108.710 1.00102.07 O ANISOU 2351 O PHE A 369 7299 14843 16640 -49 -3297 -7025 O ATOM 2352 CB PHE A 369 51.286 -1.419 107.850 1.00 99.28 C ANISOU 2352 CB PHE A 369 7626 14395 15701 439 -3357 -6140 C ATOM 2353 CG PHE A 369 50.460 -2.047 106.743 1.00 99.79 C ANISOU 2353 CG PHE A 369 7911 14372 15632 402 -3067 -5750 C ATOM 2354 CD1 PHE A 369 50.460 -1.513 105.457 1.00102.04 C ANISOU 2354 CD1 PHE A 369 8095 14593 16082 83 -2601 -5704 C ATOM 2355 CD2 PHE A 369 49.639 -3.136 107.002 1.00101.12 C ANISOU 2355 CD2 PHE A 369 8424 14505 15493 676 -3250 -5428 C ATOM 2356 CE1 PHE A 369 49.687 -2.084 104.444 1.00102.50 C ANISOU 2356 CE1 PHE A 369 8374 14568 16005 60 -2361 -5353 C ATOM 2357 CE2 PHE A 369 48.854 -3.696 105.991 1.00103.68 C ANISOU 2357 CE2 PHE A 369 8945 14750 15700 632 -2992 -5085 C ATOM 2358 CZ PHE A 369 48.883 -3.165 104.720 1.00101.66 C ANISOU 2358 CZ PHE A 369 8571 14443 15611 332 -2565 -5050 C ATOM 2359 N LYS A 370 54.070 -0.728 109.410 1.00101.69 N ANISOU 2359 N LYS A 370 7023 15012 16601 549 -4006 -7287 N ATOM 2360 CA LYS A 370 54.850 -0.188 110.535 1.00102.27 C ANISOU 2360 CA LYS A 370 6885 15179 16795 621 -4364 -7697 C ATOM 2361 C LYS A 370 55.905 0.787 110.014 1.00107.39 C ANISOU 2361 C LYS A 370 7007 15896 17900 271 -4107 -8150 C ATOM 2362 O LYS A 370 56.123 1.832 110.629 1.00106.37 O ANISOU 2362 O LYS A 370 6808 15758 17849 106 -4122 -8359 O ATOM 2363 CB LYS A 370 55.522 -1.308 111.345 1.00105.08 C ANISOU 2363 CB LYS A 370 7138 15669 17117 1074 -4951 -7927 C ATOM 2364 CG LYS A 370 54.616 -1.974 112.376 1.00123.79 C ANISOU 2364 CG LYS A 370 10067 17953 19015 1424 -5298 -7591 C ATOM 2365 CD LYS A 370 55.375 -3.047 113.162 1.00135.17 C ANISOU 2365 CD LYS A 370 11428 19510 20421 1886 -5888 -7849 C ATOM 2366 CE LYS A 370 54.491 -3.819 114.112 1.00144.31 C ANISOU 2366 CE LYS A 370 13188 20553 21089 2234 -6195 -7509 C ATOM 2367 NZ LYS A 370 55.123 -5.100 114.527 1.00150.51 N ANISOU 2367 NZ LYS A 370 13957 21419 21810 2695 -6695 -7682 N ATOM 2368 N ALA A 371 56.528 0.454 108.858 1.00105.71 N ANISOU 2368 N ALA A 371 6446 15737 17982 141 -3839 -8297 N ATOM 2369 CA ALA A 371 57.516 1.289 108.178 1.00106.49 C ANISOU 2369 CA ALA A 371 6050 15879 18532 -224 -3504 -8719 C ATOM 2370 C ALA A 371 56.873 2.601 107.698 1.00113.95 C ANISOU 2370 C ALA A 371 7215 16645 19436 -653 -2982 -8522 C ATOM 2371 O ALA A 371 57.493 3.652 107.814 1.00114.13 O ANISOU 2371 O ALA A 371 6972 16672 19719 -935 -2829 -8869 O ATOM 2372 CB ALA A 371 58.125 0.536 107.003 1.00107.03 C ANISOU 2372 CB ALA A 371 5807 16005 18854 -254 -3287 -8829 C ATOM 2373 N ALA A 372 55.618 2.539 107.206 1.00112.97 N ANISOU 2373 N ALA A 372 7584 16359 18980 -689 -2730 -7978 N ATOM 2374 CA ALA A 372 54.860 3.695 106.724 1.00113.92 C ANISOU 2374 CA ALA A 372 7989 16290 19005 -1039 -2262 -7732 C ATOM 2375 C ALA A 372 54.474 4.642 107.860 1.00120.91 C ANISOU 2375 C ALA A 372 9070 17127 19743 -1067 -2420 -7736 C ATOM 2376 O ALA A 372 54.609 5.856 107.705 1.00120.47 O ANISOU 2376 O ALA A 372 8960 16988 19827 -1402 -2113 -7879 O ATOM 2377 CB ALA A 372 53.618 3.233 105.983 1.00114.63 C ANISOU 2377 CB ALA A 372 8538 16242 18775 -997 -2046 -7171 C ATOM 2378 N PHE A 373 53.995 4.093 108.998 1.00119.83 N ANISOU 2378 N PHE A 373 9183 17029 19318 -720 -2882 -7586 N ATOM 2379 CA PHE A 373 53.611 4.890 110.166 1.00120.52 C ANISOU 2379 CA PHE A 373 9490 17067 19234 -708 -3067 -7582 C ATOM 2380 C PHE A 373 54.831 5.533 110.819 1.00127.09 C ANISOU 2380 C PHE A 373 9889 18019 20381 -794 -3265 -8152 C ATOM 2381 O PHE A 373 54.741 6.679 111.255 1.00127.49 O ANISOU 2381 O PHE A 373 10008 17995 20437 -1006 -3159 -8235 O ATOM 2382 CB PHE A 373 52.794 4.066 111.180 1.00122.08 C ANISOU 2382 CB PHE A 373 10099 17255 19032 -316 -3482 -7279 C ATOM 2383 CG PHE A 373 51.522 3.445 110.644 1.00123.31 C ANISOU 2383 CG PHE A 373 10684 17292 18877 -233 -3304 -6734 C ATOM 2384 CD1 PHE A 373 50.632 4.189 109.876 1.00126.13 C ANISOU 2384 CD1 PHE A 373 11278 17489 19156 -507 -2838 -6420 C ATOM 2385 CD2 PHE A 373 51.188 2.131 110.953 1.00125.09 C ANISOU 2385 CD2 PHE A 373 11098 17555 18876 128 -3615 -6541 C ATOM 2386 CE1 PHE A 373 49.455 3.616 109.385 1.00126.61 C ANISOU 2386 CE1 PHE A 373 11708 17450 18948 -422 -2699 -5947 C ATOM 2387 CE2 PHE A 373 50.012 1.556 110.457 1.00127.51 C ANISOU 2387 CE2 PHE A 373 11781 17753 18914 187 -3442 -6063 C ATOM 2388 CZ PHE A 373 49.152 2.305 109.684 1.00125.39 C ANISOU 2388 CZ PHE A 373 11701 17344 18596 -88 -2996 -5778 C ATOM 2389 N SER A 374 55.976 4.818 110.850 1.00125.22 N ANISOU 2389 N SER A 374 9192 17965 20421 -638 -3541 -8559 N ATOM 2390 CA SER A 374 57.232 5.332 111.411 1.00125.78 C ANISOU 2390 CA SER A 374 8773 18173 20844 -707 -3754 -9161 C ATOM 2391 C SER A 374 57.820 6.448 110.534 1.00131.96 C ANISOU 2391 C SER A 374 9234 18906 21998 -1202 -3218 -9433 C ATOM 2392 O SER A 374 58.293 7.449 111.075 1.00132.03 O ANISOU 2392 O SER A 374 9076 18920 22169 -1402 -3220 -9759 O ATOM 2393 CB SER A 374 58.246 4.210 111.611 1.00128.73 C ANISOU 2393 CB SER A 374 8742 18753 21416 -379 -4196 -9516 C ATOM 2394 OG SER A 374 57.834 3.322 112.638 1.00138.06 O ANISOU 2394 OG SER A 374 10243 19965 22249 81 -4733 -9333 O ATOM 2395 N TRP A 375 57.758 6.284 109.189 1.00129.12 N ANISOU 2395 N TRP A 375 8829 18480 21751 -1406 -2747 -9292 N ATOM 2396 CA TRP A 375 58.236 7.265 108.207 1.00129.40 C ANISOU 2396 CA TRP A 375 8641 18425 22099 -1884 -2166 -9499 C ATOM 2397 C TRP A 375 57.313 8.493 108.176 1.00133.55 C ANISOU 2397 C TRP A 375 9605 18731 22408 -2168 -1803 -9202 C ATOM 2398 O TRP A 375 57.804 9.625 108.191 1.00133.60 O ANISOU 2398 O TRP A 375 9445 18683 22633 -2505 -1555 -9505 O ATOM 2399 CB TRP A 375 58.358 6.630 106.810 1.00128.78 C ANISOU 2399 CB TRP A 375 8473 18316 22140 -1974 -1793 -9391 C ATOM 2400 CG TRP A 375 58.957 7.537 105.779 1.00130.61 C ANISOU 2400 CG TRP A 375 8476 18445 22703 -2453 -1189 -9644 C ATOM 2401 CD1 TRP A 375 58.285 8.344 104.908 1.00133.75 C ANISOU 2401 CD1 TRP A 375 9230 18609 22978 -2780 -632 -9348 C ATOM 2402 CD2 TRP A 375 60.355 7.741 105.522 1.00130.94 C ANISOU 2402 CD2 TRP A 375 7898 18600 23254 -2662 -1073 -10262 C ATOM 2403 NE1 TRP A 375 59.176 9.039 104.123 1.00133.89 N ANISOU 2403 NE1 TRP A 375 8930 18568 23374 -3187 -155 -9729 N ATOM 2404 CE2 TRP A 375 60.455 8.691 104.481 1.00135.49 C ANISOU 2404 CE2 TRP A 375 8513 18985 23984 -3139 -399 -10302 C ATOM 2405 CE3 TRP A 375 61.539 7.215 106.075 1.00132.13 C ANISOU 2405 CE3 TRP A 375 7462 18989 23752 -2487 -1475 -10804 C ATOM 2406 CZ2 TRP A 375 61.692 9.126 103.978 1.00134.88 C ANISOU 2406 CZ2 TRP A 375 7907 18941 24401 -3471 -79 -10866 C ATOM 2407 CZ3 TRP A 375 62.761 7.653 105.583 1.00133.57 C ANISOU 2407 CZ3 TRP A 375 7080 19226 24447 -2804 -1185 -11377 C ATOM 2408 CH2 TRP A 375 62.830 8.589 104.543 1.00134.39 C ANISOU 2408 CH2 TRP A 375 7232 19130 24701 -3303 -476 -11405 C ATOM 2409 N TRP A 376 55.984 8.264 108.138 1.00130.09 N ANISOU 2409 N TRP A 376 9717 18163 21547 -2029 -1773 -8626 N ATOM 2410 CA TRP A 376 54.971 9.321 108.134 1.00159.29 C ANISOU 2410 CA TRP A 376 13872 21650 24999 -2230 -1471 -8293 C ATOM 2411 C TRP A 376 54.258 9.364 109.478 1.00176.15 C ANISOU 2411 C TRP A 376 16323 23791 26816 -1971 -1888 -8113 C ATOM 2412 O TRP A 376 53.750 10.409 109.869 1.00135.53 O ANISOU 2412 O TRP A 376 11436 18514 21545 -2133 -1747 -8016 O ATOM 2413 CB TRP A 376 53.956 9.112 106.999 1.00158.09 C ANISOU 2413 CB TRP A 376 14105 21335 24626 -2282 -1091 -7790 C ATOM 2414 CG TRP A 376 54.519 9.308 105.623 1.00159.06 C ANISOU 2414 CG TRP A 376 14039 21387 25010 -2593 -589 -7920 C ATOM 2415 CD1 TRP A 376 54.875 10.490 105.043 1.00161.98 C ANISOU 2415 CD1 TRP A 376 14378 21608 25559 -3007 -105 -8094 C ATOM 2416 CD2 TRP A 376 54.736 8.294 104.632 1.00158.88 C ANISOU 2416 CD2 TRP A 376 13888 21411 25069 -2519 -491 -7865 C ATOM 2417 NE1 TRP A 376 55.335 10.273 103.766 1.00161.40 N ANISOU 2417 NE1 TRP A 376 14165 21483 25678 -3199 292 -8166 N ATOM 2418 CE2 TRP A 376 55.253 8.934 103.484 1.00162.84 C ANISOU 2418 CE2 TRP A 376 14279 21787 25806 -2904 62 -8025 C ATOM 2419 CE3 TRP A 376 54.556 6.900 104.607 1.00160.05 C ANISOU 2419 CE3 TRP A 376 14019 21683 25108 -2168 -807 -7703 C ATOM 2420 CZ2 TRP A 376 55.599 8.228 102.325 1.00162.16 C ANISOU 2420 CZ2 TRP A 376 14063 21700 25850 -2946 303 -8030 C ATOM 2421 CZ3 TRP A 376 54.900 6.202 103.459 1.00161.44 C ANISOU 2421 CZ3 TRP A 376 14053 21868 25421 -2207 -578 -7707 C ATOM 2422 CH2 TRP A 376 55.411 6.863 102.334 1.00162.10 C ANISOU 2422 CH2 TRP A 376 14025 21827 25738 -2591 -30 -7868 C TER 2423 TRP A 376 ATOM 2424 N LYS B 43 9.740 -48.927 73.566 1.00116.02 N ANISOU 2424 N LYS B 43 15816 12118 16147 -2361 -1552 -911 N ATOM 2425 CA LYS B 43 10.556 -49.496 72.493 1.00115.73 C ANISOU 2425 CA LYS B 43 16095 12020 15858 -2300 -1702 -1028 C ATOM 2426 C LYS B 43 10.156 -48.943 71.111 1.00119.06 C ANISOU 2426 C LYS B 43 16485 12541 16209 -2317 -2065 -1166 C ATOM 2427 O LYS B 43 10.678 -49.392 70.082 1.00118.72 O ANISOU 2427 O LYS B 43 16712 12440 15956 -2288 -2214 -1287 O ATOM 2428 CB LYS B 43 10.488 -51.034 72.525 1.00118.17 C ANISOU 2428 CB LYS B 43 16587 12051 16262 -2449 -1629 -1105 C ATOM 2429 CG LYS B 43 11.842 -51.712 72.322 1.00131.06 C ANISOU 2429 CG LYS B 43 18592 13592 17610 -2292 -1531 -1114 C ATOM 2430 CD LYS B 43 11.734 -53.239 72.395 1.00138.93 C ANISOU 2430 CD LYS B 43 19778 14292 18719 -2436 -1450 -1185 C ATOM 2431 CE LYS B 43 13.057 -53.915 72.126 1.00143.86 C ANISOU 2431 CE LYS B 43 20763 14815 19084 -2266 -1364 -1206 C ATOM 2432 NZ LYS B 43 12.927 -55.393 72.091 1.00148.19 N ANISOU 2432 NZ LYS B 43 21513 15054 19739 -2404 -1308 -1290 N ATOM 2433 N GLN B 44 9.247 -47.948 71.099 1.00114.58 N ANISOU 2433 N GLN B 44 15607 12120 15808 -2350 -2204 -1146 N ATOM 2434 CA GLN B 44 8.750 -47.300 69.883 1.00113.61 C ANISOU 2434 CA GLN B 44 15433 12099 15636 -2353 -2572 -1255 C ATOM 2435 C GLN B 44 9.784 -46.334 69.293 1.00113.61 C ANISOU 2435 C GLN B 44 15631 12271 15266 -2121 -2617 -1211 C ATOM 2436 O GLN B 44 9.954 -46.298 68.071 1.00113.72 O ANISOU 2436 O GLN B 44 15843 12292 15071 -2093 -2867 -1323 O ATOM 2437 CB GLN B 44 7.432 -46.555 70.160 1.00115.26 C ANISOU 2437 CB GLN B 44 15220 12393 16181 -2448 -2692 -1236 C ATOM 2438 CG GLN B 44 6.258 -47.457 70.539 1.00134.99 C ANISOU 2438 CG GLN B 44 17478 14719 19092 -2707 -2683 -1306 C ATOM 2439 CD GLN B 44 5.048 -46.651 70.944 1.00159.71 C ANISOU 2439 CD GLN B 44 20159 17943 22579 -2772 -2732 -1269 C ATOM 2440 OE1 GLN B 44 5.100 -45.796 71.839 1.00156.02 O ANISOU 2440 OE1 GLN B 44 19537 17597 22146 -2663 -2507 -1123 O ATOM 2441 NE2 GLN B 44 3.923 -46.911 70.294 1.00154.15 N ANISOU 2441 NE2 GLN B 44 19230 17180 22161 -2949 -3031 -1411 N ATOM 2442 N TYR B 45 10.465 -45.552 70.156 1.00106.10 N ANISOU 2442 N TYR B 45 14636 11446 14230 -1961 -2370 -1054 N ATOM 2443 CA TYR B 45 11.458 -44.576 69.714 1.00104.04 C ANISOU 2443 CA TYR B 45 14530 11342 13658 -1753 -2372 -1002 C ATOM 2444 C TYR B 45 12.914 -45.041 69.905 1.00102.67 C ANISOU 2444 C TYR B 45 14644 11128 13237 -1618 -2139 -970 C ATOM 2445 O TYR B 45 13.821 -44.341 69.463 1.00102.04 O ANISOU 2445 O TYR B 45 14704 11158 12908 -1457 -2121 -944 O ATOM 2446 CB TYR B 45 11.203 -43.195 70.359 1.00105.33 C ANISOU 2446 CB TYR B 45 14435 11688 13899 -1660 -2315 -870 C ATOM 2447 CG TYR B 45 11.431 -43.113 71.855 1.00107.35 C ANISOU 2447 CG TYR B 45 14563 11955 14268 -1627 -1990 -732 C ATOM 2448 CD1 TYR B 45 10.409 -43.409 72.754 1.00109.46 C ANISOU 2448 CD1 TYR B 45 14576 12158 14858 -1768 -1891 -701 C ATOM 2449 CD2 TYR B 45 12.636 -42.643 72.372 1.00107.98 C ANISOU 2449 CD2 TYR B 45 14770 12117 14139 -1453 -1787 -635 C ATOM 2450 CE1 TYR B 45 10.600 -43.292 74.134 1.00110.13 C ANISOU 2450 CE1 TYR B 45 14585 12248 15012 -1732 -1587 -571 C ATOM 2451 CE2 TYR B 45 12.839 -42.524 73.748 1.00108.72 C ANISOU 2451 CE2 TYR B 45 14775 12223 14311 -1415 -1521 -513 C ATOM 2452 CZ TYR B 45 11.818 -42.848 74.626 1.00114.44 C ANISOU 2452 CZ TYR B 45 15290 12875 15316 -1551 -1418 -479 C ATOM 2453 OH TYR B 45 12.021 -42.731 75.982 1.00112.00 O ANISOU 2453 OH TYR B 45 14939 12568 15047 -1508 -1147 -357 O ATOM 2454 N ALA B 46 13.129 -46.228 70.515 1.00 95.67 N ANISOU 2454 N ALA B 46 13846 10074 12432 -1682 -1967 -977 N ATOM 2455 CA ALA B 46 14.441 -46.826 70.799 1.00 93.88 C ANISOU 2455 CA ALA B 46 13868 9778 12024 -1553 -1754 -950 C ATOM 2456 C ALA B 46 15.390 -46.898 69.596 1.00 95.26 C ANISOU 2456 C ALA B 46 14334 9956 11906 -1443 -1832 -1049 C ATOM 2457 O ALA B 46 16.553 -46.526 69.734 1.00 93.97 O ANISOU 2457 O ALA B 46 14271 9865 11567 -1267 -1680 -992 O ATOM 2458 CB ALA B 46 14.272 -48.200 71.427 1.00 94.44 C ANISOU 2458 CB ALA B 46 14006 9627 12249 -1667 -1622 -964 C ATOM 2459 N TRP B 47 14.900 -47.354 68.425 1.00 91.34 N ANISOU 2459 N TRP B 47 13972 9375 11359 -1546 -2064 -1204 N ATOM 2460 CA TRP B 47 15.699 -47.435 67.195 1.00 90.63 C ANISOU 2460 CA TRP B 47 14193 9271 10971 -1454 -2135 -1313 C ATOM 2461 C TRP B 47 16.059 -46.036 66.686 1.00 86.41 C ANISOU 2461 C TRP B 47 13649 8941 10243 -1320 -2189 -1258 C ATOM 2462 O TRP B 47 17.193 -45.822 66.256 1.00 85.24 O ANISOU 2462 O TRP B 47 13703 8825 9859 -1172 -2065 -1261 O ATOM 2463 CB TRP B 47 14.968 -48.231 66.099 1.00 91.01 C ANISOU 2463 CB TRP B 47 14402 9174 11004 -1611 -2397 -1499 C ATOM 2464 CG TRP B 47 15.757 -48.330 64.824 1.00 93.48 C ANISOU 2464 CG TRP B 47 15074 9458 10984 -1517 -2452 -1617 C ATOM 2465 CD1 TRP B 47 16.695 -49.272 64.513 1.00 96.85 C ANISOU 2465 CD1 TRP B 47 15796 9738 11266 -1453 -2296 -1700 C ATOM 2466 CD2 TRP B 47 15.729 -47.410 63.719 1.00 93.81 C ANISOU 2466 CD2 TRP B 47 15238 9619 10785 -1460 -2647 -1656 C ATOM 2467 NE1 TRP B 47 17.234 -49.014 63.272 1.00 97.00 N ANISOU 2467 NE1 TRP B 47 16110 9776 10970 -1369 -2364 -1797 N ATOM 2468 CE2 TRP B 47 16.664 -47.872 62.764 1.00 98.48 C ANISOU 2468 CE2 TRP B 47 16213 10124 11080 -1374 -2579 -1767 C ATOM 2469 CE3 TRP B 47 14.987 -46.250 63.431 1.00 95.24 C ANISOU 2469 CE3 TRP B 47 15257 9958 10972 -1468 -2870 -1606 C ATOM 2470 CZ2 TRP B 47 16.866 -47.222 61.537 1.00 97.80 C ANISOU 2470 CZ2 TRP B 47 16375 10101 10683 -1307 -2715 -1826 C ATOM 2471 CZ3 TRP B 47 15.204 -45.596 62.227 1.00 96.81 C ANISOU 2471 CZ3 TRP B 47 15700 10218 10865 -1391 -3026 -1656 C ATOM 2472 CH2 TRP B 47 16.128 -46.085 61.293 1.00 97.53 C ANISOU 2472 CH2 TRP B 47 16195 10219 10645 -1317 -2943 -1763 C ATOM 2473 N VAL B 48 15.073 -45.107 66.704 1.00 77.91 N ANISOU 2473 N VAL B 48 12336 7985 9280 -1374 -2370 -1212 N ATOM 2474 CA VAL B 48 15.203 -43.698 66.290 1.00 75.39 C ANISOU 2474 CA VAL B 48 11982 7847 8816 -1262 -2444 -1145 C ATOM 2475 C VAL B 48 16.278 -43.016 67.153 1.00 73.33 C ANISOU 2475 C VAL B 48 11662 7696 8506 -1102 -2154 -1005 C ATOM 2476 O VAL B 48 17.160 -42.340 66.625 1.00 71.89 O ANISOU 2476 O VAL B 48 11624 7592 8097 -972 -2090 -987 O ATOM 2477 CB VAL B 48 13.830 -42.960 66.357 1.00 78.74 C ANISOU 2477 CB VAL B 48 12117 8353 9446 -1352 -2684 -1117 C ATOM 2478 CG1 VAL B 48 13.964 -41.481 66.016 1.00 78.18 C ANISOU 2478 CG1 VAL B 48 12014 8452 9238 -1222 -2746 -1030 C ATOM 2479 CG2 VAL B 48 12.804 -43.624 65.445 1.00 78.63 C ANISOU 2479 CG2 VAL B 48 12153 8232 9493 -1509 -3012 -1270 C ATOM 2480 N LEU B 49 16.214 -43.257 68.468 1.00 66.99 N ANISOU 2480 N LEU B 49 10662 6881 7911 -1121 -1977 -916 N ATOM 2481 CA LEU B 49 17.121 -42.753 69.486 1.00 65.85 C ANISOU 2481 CA LEU B 49 10442 6821 7757 -988 -1727 -792 C ATOM 2482 C LEU B 49 18.561 -43.195 69.250 1.00 68.61 C ANISOU 2482 C LEU B 49 11026 7127 7914 -857 -1557 -820 C ATOM 2483 O LEU B 49 19.469 -42.366 69.315 1.00 69.30 O ANISOU 2483 O LEU B 49 11121 7326 7886 -723 -1443 -763 O ATOM 2484 CB LEU B 49 16.634 -43.180 70.879 1.00 65.63 C ANISOU 2484 CB LEU B 49 10218 6746 7974 -1055 -1596 -709 C ATOM 2485 CG LEU B 49 17.361 -42.577 72.072 1.00 70.27 C ANISOU 2485 CG LEU B 49 10710 7425 8565 -930 -1378 -578 C ATOM 2486 CD1 LEU B 49 17.287 -41.053 72.059 1.00 69.81 C ANISOU 2486 CD1 LEU B 49 10507 7548 8470 -859 -1414 -509 C ATOM 2487 CD2 LEU B 49 16.825 -43.147 73.366 1.00 72.95 C ANISOU 2487 CD2 LEU B 49 10925 7685 9106 -1004 -1248 -505 C ATOM 2488 N ILE B 50 18.766 -44.481 68.980 1.00 64.10 N ANISOU 2488 N ILE B 50 10637 6388 7331 -897 -1534 -914 N ATOM 2489 CA ILE B 50 20.082 -45.048 68.701 1.00 63.59 C ANISOU 2489 CA ILE B 50 10793 6254 7115 -770 -1371 -960 C ATOM 2490 C ILE B 50 20.608 -44.452 67.394 1.00 66.55 C ANISOU 2490 C ILE B 50 11354 6689 7241 -700 -1418 -1031 C ATOM 2491 O ILE B 50 21.729 -43.949 67.381 1.00 66.00 O ANISOU 2491 O ILE B 50 11319 6693 7066 -558 -1253 -996 O ATOM 2492 CB ILE B 50 20.020 -46.600 68.690 1.00 66.68 C ANISOU 2492 CB ILE B 50 11344 6424 7567 -838 -1349 -1051 C ATOM 2493 CG1 ILE B 50 19.749 -47.148 70.116 1.00 66.26 C ANISOU 2493 CG1 ILE B 50 11141 6301 7734 -874 -1236 -949 C ATOM 2494 CG2 ILE B 50 21.292 -47.225 68.058 1.00 67.70 C ANISOU 2494 CG2 ILE B 50 11736 6462 7526 -704 -1212 -1137 C ATOM 2495 CD1 ILE B 50 19.250 -48.618 70.177 1.00 66.06 C ANISOU 2495 CD1 ILE B 50 11231 6039 7829 -1004 -1251 -1024 C ATOM 2496 N ALA B 51 19.775 -44.447 66.324 1.00 62.47 N ANISOU 2496 N ALA B 51 10954 6145 6638 -803 -1647 -1127 N ATOM 2497 CA ALA B 51 20.130 -43.889 65.012 1.00 61.72 C ANISOU 2497 CA ALA B 51 11090 6090 6272 -749 -1712 -1193 C ATOM 2498 C ALA B 51 20.531 -42.403 65.100 1.00 63.97 C ANISOU 2498 C ALA B 51 11264 6557 6484 -646 -1646 -1076 C ATOM 2499 O ALA B 51 21.564 -42.030 64.541 1.00 63.61 O ANISOU 2499 O ALA B 51 11382 6537 6250 -534 -1492 -1086 O ATOM 2500 CB ALA B 51 18.991 -44.088 64.023 1.00 62.39 C ANISOU 2500 CB ALA B 51 11289 6118 6297 -883 -2024 -1301 C ATOM 2501 N ALA B 52 19.753 -41.581 65.857 1.00 58.67 N ANISOU 2501 N ALA B 52 10312 5998 5982 -683 -1733 -967 N ATOM 2502 CA ALA B 52 20.012 -40.151 66.065 1.00 57.16 C ANISOU 2502 CA ALA B 52 9998 5965 5756 -597 -1678 -853 C ATOM 2503 C ALA B 52 21.306 -39.916 66.837 1.00 59.59 C ANISOU 2503 C ALA B 52 10242 6320 6078 -473 -1393 -785 C ATOM 2504 O ALA B 52 22.071 -39.032 66.462 1.00 59.03 O ANISOU 2504 O ALA B 52 10228 6325 5875 -383 -1288 -753 O ATOM 2505 CB ALA B 52 18.843 -39.502 66.778 1.00 57.77 C ANISOU 2505 CB ALA B 52 9786 6123 6040 -665 -1821 -768 C ATOM 2506 N TYR B 53 21.569 -40.725 67.891 1.00 55.78 N ANISOU 2506 N TYR B 53 9656 5781 5756 -469 -1273 -767 N ATOM 2507 CA TYR B 53 22.796 -40.663 68.697 1.00 54.69 C ANISOU 2507 CA TYR B 53 9454 5673 5652 -345 -1042 -714 C ATOM 2508 C TYR B 53 24.009 -41.072 67.864 1.00 59.37 C ANISOU 2508 C TYR B 53 10266 6205 6086 -249 -896 -800 C ATOM 2509 O TYR B 53 25.034 -40.398 67.935 1.00 58.94 O ANISOU 2509 O TYR B 53 10175 6226 5994 -144 -739 -768 O ATOM 2510 CB TYR B 53 22.697 -41.559 69.945 1.00 54.94 C ANISOU 2510 CB TYR B 53 9375 5631 5868 -360 -984 -677 C ATOM 2511 CG TYR B 53 22.322 -40.845 71.229 1.00 55.60 C ANISOU 2511 CG TYR B 53 9215 5813 6100 -362 -961 -553 C ATOM 2512 CD1 TYR B 53 23.267 -40.118 71.948 1.00 56.78 C ANISOU 2512 CD1 TYR B 53 9265 6058 6251 -245 -828 -483 C ATOM 2513 CD2 TYR B 53 21.053 -40.981 71.779 1.00 56.05 C ANISOU 2513 CD2 TYR B 53 9140 5851 6305 -484 -1060 -516 C ATOM 2514 CE1 TYR B 53 22.941 -39.497 73.156 1.00 54.71 C ANISOU 2514 CE1 TYR B 53 8813 5873 6101 -244 -805 -381 C ATOM 2515 CE2 TYR B 53 20.716 -40.366 72.985 1.00 56.47 C ANISOU 2515 CE2 TYR B 53 8994 5981 6482 -481 -1006 -408 C ATOM 2516 CZ TYR B 53 21.664 -39.628 73.670 1.00 58.31 C ANISOU 2516 CZ TYR B 53 9166 6309 6681 -358 -883 -342 C ATOM 2517 OH TYR B 53 21.326 -39.046 74.861 1.00 56.80 O ANISOU 2517 OH TYR B 53 8813 6181 6588 -356 -832 -247 O ATOM 2518 N VAL B 54 23.887 -42.158 67.060 1.00 57.47 N ANISOU 2518 N VAL B 54 10250 5823 5762 -289 -939 -919 N ATOM 2519 CA VAL B 54 24.970 -42.666 66.198 1.00 58.07 C ANISOU 2519 CA VAL B 54 10563 5816 5686 -199 -782 -1020 C ATOM 2520 C VAL B 54 25.307 -41.646 65.109 1.00 62.21 C ANISOU 2520 C VAL B 54 11227 6416 5994 -167 -750 -1034 C ATOM 2521 O VAL B 54 26.492 -41.374 64.891 1.00 63.52 O ANISOU 2521 O VAL B 54 11434 6598 6101 -57 -527 -1044 O ATOM 2522 CB VAL B 54 24.729 -44.102 65.642 1.00 62.26 C ANISOU 2522 CB VAL B 54 11321 6157 6179 -252 -831 -1153 C ATOM 2523 CG1 VAL B 54 25.876 -44.548 64.739 1.00 62.52 C ANISOU 2523 CG1 VAL B 54 11605 6101 6050 -146 -638 -1263 C ATOM 2524 CG2 VAL B 54 24.545 -45.107 66.771 1.00 61.87 C ANISOU 2524 CG2 VAL B 54 11153 6010 6344 -271 -817 -1123 C ATOM 2525 N ALA B 55 24.272 -41.046 64.472 1.00 56.94 N ANISOU 2525 N ALA B 55 10620 5792 5224 -258 -968 -1027 N ATOM 2526 CA ALA B 55 24.443 -40.009 63.442 1.00 55.70 C ANISOU 2526 CA ALA B 55 10626 5696 4841 -231 -966 -1019 C ATOM 2527 C ALA B 55 25.132 -38.792 64.037 1.00 61.10 C ANISOU 2527 C ALA B 55 11113 6513 5590 -152 -801 -901 C ATOM 2528 O ALA B 55 26.064 -38.289 63.407 1.00 63.45 O ANISOU 2528 O ALA B 55 11542 6820 5747 -81 -608 -911 O ATOM 2529 CB ALA B 55 23.101 -39.609 62.855 1.00 56.05 C ANISOU 2529 CB ALA B 55 10727 5762 4809 -332 -1279 -1016 C ATOM 2530 N VAL B 56 24.703 -38.333 65.261 1.00 54.46 N ANISOU 2530 N VAL B 56 9964 5764 4966 -170 -857 -796 N ATOM 2531 CA VAL B 56 25.304 -37.184 65.951 1.00 52.74 C ANISOU 2531 CA VAL B 56 9547 5665 4828 -105 -722 -693 C ATOM 2532 C VAL B 56 26.770 -37.463 66.259 1.00 56.50 C ANISOU 2532 C VAL B 56 9993 6124 5352 -1 -454 -720 C ATOM 2533 O VAL B 56 27.614 -36.665 65.883 1.00 56.66 O ANISOU 2533 O VAL B 56 10039 6185 5304 53 -289 -706 O ATOM 2534 CB VAL B 56 24.501 -36.686 67.192 1.00 55.45 C ANISOU 2534 CB VAL B 56 9599 6094 5375 -144 -833 -590 C ATOM 2535 CG1 VAL B 56 25.368 -35.848 68.126 1.00 54.48 C ANISOU 2535 CG1 VAL B 56 9279 6063 5357 -68 -665 -513 C ATOM 2536 CG2 VAL B 56 23.263 -35.898 66.768 1.00 55.24 C ANISOU 2536 CG2 VAL B 56 9566 6115 5310 -213 -1057 -547 C ATOM 2537 N PHE B 57 27.064 -38.617 66.881 1.00 53.11 N ANISOU 2537 N PHE B 57 9516 5618 5044 26 -413 -762 N ATOM 2538 CA PHE B 57 28.404 -39.081 67.247 1.00 52.84 C ANISOU 2538 CA PHE B 57 9432 5551 5094 141 -196 -796 C ATOM 2539 C PHE B 57 29.384 -39.004 66.049 1.00 57.72 C ANISOU 2539 C PHE B 57 10250 6123 5556 200 7 -880 C ATOM 2540 O PHE B 57 30.458 -38.402 66.194 1.00 57.90 O ANISOU 2540 O PHE B 57 10163 6198 5639 277 200 -866 O ATOM 2541 CB PHE B 57 28.314 -40.522 67.813 1.00 54.51 C ANISOU 2541 CB PHE B 57 9656 5643 5413 153 -229 -839 C ATOM 2542 CG PHE B 57 29.629 -41.168 68.189 1.00 55.39 C ANISOU 2542 CG PHE B 57 9723 5696 5627 291 -40 -880 C ATOM 2543 CD1 PHE B 57 30.232 -40.897 69.414 1.00 57.11 C ANISOU 2543 CD1 PHE B 57 9701 5981 6019 372 -1 -807 C ATOM 2544 CD2 PHE B 57 30.267 -42.046 67.316 1.00 56.36 C ANISOU 2544 CD2 PHE B 57 10048 5691 5674 349 89 -998 C ATOM 2545 CE1 PHE B 57 31.453 -41.481 69.753 1.00 57.87 C ANISOU 2545 CE1 PHE B 57 9737 6023 6229 513 140 -847 C ATOM 2546 CE2 PHE B 57 31.482 -42.641 67.664 1.00 58.81 C ANISOU 2546 CE2 PHE B 57 10292 5942 6111 494 261 -1038 C ATOM 2547 CZ PHE B 57 32.063 -42.359 68.883 1.00 56.63 C ANISOU 2547 CZ PHE B 57 9755 5739 6025 578 272 -960 C ATOM 2548 N VAL B 58 28.999 -39.578 64.872 1.00 53.00 N ANISOU 2548 N VAL B 58 9950 5427 4761 157 -35 -972 N ATOM 2549 CA VAL B 58 29.819 -39.550 63.657 1.00 53.61 C ANISOU 2549 CA VAL B 58 10277 5443 4651 206 172 -1058 C ATOM 2550 C VAL B 58 30.046 -38.107 63.182 1.00 60.53 C ANISOU 2550 C VAL B 58 11167 6416 5416 199 258 -988 C ATOM 2551 O VAL B 58 31.201 -37.667 63.155 1.00 61.88 O ANISOU 2551 O VAL B 58 11269 6604 5636 272 521 -992 O ATOM 2552 CB VAL B 58 29.299 -40.470 62.504 1.00 57.56 C ANISOU 2552 CB VAL B 58 11134 5805 4930 158 89 -1179 C ATOM 2553 CG1 VAL B 58 30.077 -40.228 61.204 1.00 57.30 C ANISOU 2553 CG1 VAL B 58 11400 5717 4655 203 317 -1255 C ATOM 2554 CG2 VAL B 58 29.354 -41.945 62.895 1.00 57.30 C ANISOU 2554 CG2 VAL B 58 11113 5643 5017 181 82 -1264 C ATOM 2555 N VAL B 59 28.949 -37.373 62.838 1.00 56.53 N ANISOU 2555 N VAL B 59 10732 5962 4784 114 38 -924 N ATOM 2556 CA VAL B 59 28.978 -35.987 62.339 1.00 55.96 C ANISOU 2556 CA VAL B 59 10715 5961 4586 104 82 -845 C ATOM 2557 C VAL B 59 29.788 -35.073 63.278 1.00 61.37 C ANISOU 2557 C VAL B 59 11095 6745 5479 148 250 -762 C ATOM 2558 O VAL B 59 30.676 -34.371 62.800 1.00 62.71 O ANISOU 2558 O VAL B 59 11319 6916 5591 179 488 -756 O ATOM 2559 CB VAL B 59 27.551 -35.443 62.013 1.00 58.66 C ANISOU 2559 CB VAL B 59 11140 6339 4810 22 -238 -784 C ATOM 2560 CG1 VAL B 59 27.557 -33.948 61.702 1.00 57.97 C ANISOU 2560 CG1 VAL B 59 11077 6318 4629 26 -204 -679 C ATOM 2561 CG2 VAL B 59 26.924 -36.221 60.855 1.00 58.06 C ANISOU 2561 CG2 VAL B 59 11415 6156 4490 -20 -395 -884 C ATOM 2562 N ALA B 60 29.541 -35.131 64.595 1.00 57.44 N ANISOU 2562 N ALA B 60 10291 6314 5218 148 145 -710 N ATOM 2563 CA ALA B 60 30.274 -34.329 65.582 1.00 57.08 C ANISOU 2563 CA ALA B 60 9958 6357 5371 187 264 -646 C ATOM 2564 C ALA B 60 31.788 -34.619 65.610 1.00 63.26 C ANISOU 2564 C ALA B 60 10668 7108 6259 274 548 -714 C ATOM 2565 O ALA B 60 32.565 -33.678 65.668 1.00 63.69 O ANISOU 2565 O ALA B 60 10609 7209 6381 289 714 -687 O ATOM 2566 CB ALA B 60 29.673 -34.502 66.968 1.00 57.36 C ANISOU 2566 CB ALA B 60 9739 6453 5602 174 87 -589 C ATOM 2567 N LEU B 61 32.210 -35.893 65.547 1.00 61.29 N ANISOU 2567 N LEU B 61 10474 6770 6043 331 607 -807 N ATOM 2568 CA LEU B 61 33.636 -36.249 65.570 1.00 62.14 C ANISOU 2568 CA LEU B 61 10490 6838 6284 431 870 -881 C ATOM 2569 C LEU B 61 34.357 -35.831 64.295 1.00 67.03 C ANISOU 2569 C LEU B 61 11310 7405 6751 437 1145 -934 C ATOM 2570 O LEU B 61 35.431 -35.229 64.381 1.00 67.21 O ANISOU 2570 O LEU B 61 11175 7454 6907 474 1374 -941 O ATOM 2571 CB LEU B 61 33.872 -37.751 65.853 1.00 62.49 C ANISOU 2571 CB LEU B 61 10547 6782 6414 508 857 -963 C ATOM 2572 CG LEU B 61 33.582 -38.270 67.277 1.00 67.43 C ANISOU 2572 CG LEU B 61 10951 7436 7236 537 669 -912 C ATOM 2573 CD1 LEU B 61 33.891 -39.745 67.370 1.00 68.03 C ANISOU 2573 CD1 LEU B 61 11093 7381 7373 621 690 -993 C ATOM 2574 CD2 LEU B 61 34.378 -37.518 68.360 1.00 69.19 C ANISOU 2574 CD2 LEU B 61 10853 7759 7678 593 709 -860 C ATOM 2575 N VAL B 62 33.761 -36.126 63.118 1.00 62.41 N ANISOU 2575 N VAL B 62 11081 6743 5888 394 1123 -975 N ATOM 2576 CA VAL B 62 34.333 -35.746 61.821 1.00 61.78 C ANISOU 2576 CA VAL B 62 11272 6599 5605 394 1390 -1020 C ATOM 2577 C VAL B 62 34.383 -34.212 61.711 1.00 66.36 C ANISOU 2577 C VAL B 62 11807 7256 6150 340 1456 -915 C ATOM 2578 O VAL B 62 35.449 -33.639 61.470 1.00 66.55 O ANISOU 2578 O VAL B 62 11771 7271 6246 361 1761 -926 O ATOM 2579 CB VAL B 62 33.592 -36.411 60.620 1.00 64.21 C ANISOU 2579 CB VAL B 62 12011 6801 5585 359 1302 -1087 C ATOM 2580 CG1 VAL B 62 33.969 -35.759 59.289 1.00 63.79 C ANISOU 2580 CG1 VAL B 62 12293 6689 5257 346 1544 -1101 C ATOM 2581 CG2 VAL B 62 33.848 -37.910 60.579 1.00 63.25 C ANISOU 2581 CG2 VAL B 62 11960 6567 5504 420 1329 -1214 C ATOM 2582 N GLY B 63 33.235 -33.582 61.930 1.00 62.60 N ANISOU 2582 N GLY B 63 11345 6848 5594 270 1174 -816 N ATOM 2583 CA GLY B 63 33.062 -32.141 61.839 1.00 61.95 C ANISOU 2583 CA GLY B 63 11250 6824 5463 220 1182 -706 C ATOM 2584 C GLY B 63 33.990 -31.324 62.703 1.00 64.38 C ANISOU 2584 C GLY B 63 11222 7200 6040 232 1351 -669 C ATOM 2585 O GLY B 63 34.575 -30.358 62.220 1.00 65.20 O ANISOU 2585 O GLY B 63 11379 7288 6107 209 1576 -636 O ATOM 2586 N ASN B 64 34.106 -31.679 63.982 1.00 59.65 N ANISOU 2586 N ASN B 64 10292 6666 5704 263 1239 -672 N ATOM 2587 CA ASN B 64 34.932 -30.932 64.920 1.00 59.43 C ANISOU 2587 CA ASN B 64 9933 6707 5940 273 1341 -648 C ATOM 2588 C ASN B 64 36.429 -31.154 64.728 1.00 64.11 C ANISOU 2588 C ASN B 64 10412 7254 6693 329 1668 -740 C ATOM 2589 O ASN B 64 37.205 -30.248 65.015 1.00 64.25 O ANISOU 2589 O ASN B 64 10233 7301 6876 309 1824 -727 O ATOM 2590 CB ASN B 64 34.498 -31.171 66.357 1.00 57.63 C ANISOU 2590 CB ASN B 64 9431 6561 5906 290 1092 -616 C ATOM 2591 CG ASN B 64 33.201 -30.493 66.657 1.00 68.97 C ANISOU 2591 CG ASN B 64 10895 8054 7255 226 842 -515 C ATOM 2592 OD1 ASN B 64 33.110 -29.272 66.720 1.00 73.79 O ANISOU 2592 OD1 ASN B 64 11468 8703 7867 182 860 -445 O ATOM 2593 ND2 ASN B 64 32.165 -31.258 66.834 1.00 58.49 N ANISOU 2593 ND2 ASN B 64 9630 6724 5869 217 613 -507 N ATOM 2594 N THR B 65 36.841 -32.316 64.221 1.00 62.09 N ANISOU 2594 N THR B 65 10272 6915 6403 395 1782 -839 N ATOM 2595 CA THR B 65 38.256 -32.549 63.918 1.00 62.56 C ANISOU 2595 CA THR B 65 10226 6918 6625 459 2123 -937 C ATOM 2596 C THR B 65 38.621 -31.745 62.653 1.00 67.38 C ANISOU 2596 C THR B 65 11084 7463 7053 400 2434 -932 C ATOM 2597 O THR B 65 39.756 -31.284 62.539 1.00 68.36 O ANISOU 2597 O THR B 65 11054 7565 7356 406 2743 -973 O ATOM 2598 CB THR B 65 38.608 -34.046 63.860 1.00 70.47 C ANISOU 2598 CB THR B 65 11259 7840 7675 565 2154 -1046 C ATOM 2599 OG1 THR B 65 37.690 -34.716 63.007 1.00 71.99 O ANISOU 2599 OG1 THR B 65 11829 7961 7561 542 2056 -1062 O ATOM 2600 CG2 THR B 65 38.603 -34.701 65.236 1.00 67.11 C ANISOU 2600 CG2 THR B 65 10540 7467 7493 638 1917 -1045 C ATOM 2601 N LEU B 66 37.628 -31.501 61.755 1.00 62.39 N ANISOU 2601 N LEU B 66 10831 6799 6076 340 2339 -875 N ATOM 2602 CA LEU B 66 37.808 -30.695 60.546 1.00 61.45 C ANISOU 2602 CA LEU B 66 11023 6608 5719 285 2595 -846 C ATOM 2603 C LEU B 66 37.973 -29.225 60.873 1.00 65.66 C ANISOU 2603 C LEU B 66 11407 7191 6350 210 2654 -744 C ATOM 2604 O LEU B 66 38.706 -28.535 60.162 1.00 64.41 O ANISOU 2604 O LEU B 66 11357 6964 6153 172 2992 -738 O ATOM 2605 CB LEU B 66 36.666 -30.895 59.537 1.00 61.25 C ANISOU 2605 CB LEU B 66 11458 6529 5286 257 2417 -816 C ATOM 2606 CG LEU B 66 36.631 -32.234 58.745 1.00 65.14 C ANISOU 2606 CG LEU B 66 12241 6919 5589 312 2462 -937 C ATOM 2607 CD1 LEU B 66 35.574 -32.181 57.657 1.00 64.91 C ANISOU 2607 CD1 LEU B 66 12691 6832 5140 271 2292 -907 C ATOM 2608 CD2 LEU B 66 37.998 -32.594 58.148 1.00 64.04 C ANISOU 2608 CD2 LEU B 66 12134 6683 5517 366 2926 -1046 C ATOM 2609 N VAL B 67 37.300 -28.746 61.956 1.00 62.65 N ANISOU 2609 N VAL B 67 10789 6916 6100 186 2346 -666 N ATOM 2610 CA VAL B 67 37.376 -27.365 62.444 1.00 61.88 C ANISOU 2610 CA VAL B 67 10525 6865 6121 118 2358 -576 C ATOM 2611 C VAL B 67 38.829 -27.119 62.871 1.00 68.59 C ANISOU 2611 C VAL B 67 11046 7712 7304 118 2654 -647 C ATOM 2612 O VAL B 67 39.439 -26.155 62.405 1.00 67.86 O ANISOU 2612 O VAL B 67 10979 7568 7237 52 2927 -621 O ATOM 2613 CB VAL B 67 36.341 -27.084 63.577 1.00 64.51 C ANISOU 2613 CB VAL B 67 10675 7305 6530 107 1968 -500 C ATOM 2614 CG1 VAL B 67 36.501 -25.679 64.168 1.00 63.82 C ANISOU 2614 CG1 VAL B 67 10404 7256 6591 43 1991 -425 C ATOM 2615 CG2 VAL B 67 34.917 -27.281 63.076 1.00 64.16 C ANISOU 2615 CG2 VAL B 67 10925 7256 6195 101 1688 -437 C ATOM 2616 N CYS B 68 39.397 -28.045 63.683 1.00 68.08 N ANISOU 2616 N CYS B 68 10688 7687 7492 196 2607 -740 N ATOM 2617 CA CYS B 68 40.780 -28.014 64.181 1.00 69.06 C ANISOU 2617 CA CYS B 68 10449 7813 7976 222 2827 -829 C ATOM 2618 C CYS B 68 41.797 -28.091 63.038 1.00 75.51 C ANISOU 2618 C CYS B 68 11382 8518 8789 220 3277 -904 C ATOM 2619 O CYS B 68 42.816 -27.404 63.091 1.00 75.47 O ANISOU 2619 O CYS B 68 11153 8493 9030 176 3542 -938 O ATOM 2620 CB CYS B 68 41.015 -29.118 65.210 1.00 69.25 C ANISOU 2620 CB CYS B 68 10199 7892 8222 331 2625 -901 C ATOM 2621 SG CYS B 68 39.894 -29.059 66.636 1.00 73.08 S ANISOU 2621 SG CYS B 68 10560 8495 8711 331 2144 -814 S ATOM 2622 N LEU B 69 41.520 -28.916 62.010 1.00 73.12 N ANISOU 2622 N LEU B 69 11436 8134 8212 262 3375 -937 N ATOM 2623 CA LEU B 69 42.405 -29.062 60.859 1.00 73.93 C ANISOU 2623 CA LEU B 69 11713 8115 8262 268 3827 -1011 C ATOM 2624 C LEU B 69 42.364 -27.819 59.956 1.00 79.16 C ANISOU 2624 C LEU B 69 12648 8710 8719 152 4071 -922 C ATOM 2625 O LEU B 69 43.390 -27.474 59.363 1.00 78.68 O ANISOU 2625 O LEU B 69 12569 8563 8761 119 4505 -968 O ATOM 2626 CB LEU B 69 42.042 -30.313 60.029 1.00 74.29 C ANISOU 2626 CB LEU B 69 12107 8082 8039 348 3839 -1080 C ATOM 2627 CG LEU B 69 42.403 -31.696 60.577 1.00 78.93 C ANISOU 2627 CG LEU B 69 12487 8671 8831 478 3755 -1195 C ATOM 2628 CD1 LEU B 69 41.563 -32.751 59.912 1.00 78.66 C ANISOU 2628 CD1 LEU B 69 12842 8574 8471 522 3611 -1227 C ATOM 2629 CD2 LEU B 69 43.873 -32.021 60.355 1.00 82.01 C ANISOU 2629 CD2 LEU B 69 12664 8987 9507 546 4175 -1321 C ATOM 2630 N ALA B 70 41.173 -27.180 59.823 1.00 76.35 N ANISOU 2630 N ALA B 70 12552 8380 8076 95 3803 -794 N ATOM 2631 CA ALA B 70 40.952 -25.992 58.989 1.00 76.81 C ANISOU 2631 CA ALA B 70 12921 8366 7897 0 3969 -684 C ATOM 2632 C ALA B 70 41.785 -24.805 59.467 1.00 82.25 C ANISOU 2632 C ALA B 70 13304 9055 8893 -90 4185 -657 C ATOM 2633 O ALA B 70 42.462 -24.168 58.652 1.00 81.36 O ANISOU 2633 O ALA B 70 13343 8830 8740 -158 4591 -644 O ATOM 2634 CB ALA B 70 39.476 -25.623 58.975 1.00 77.53 C ANISOU 2634 CB ALA B 70 13264 8500 7694 -16 3564 -559 C ATOM 2635 N VAL B 71 41.757 -24.540 60.794 1.00 80.25 N ANISOU 2635 N VAL B 71 12629 8916 8944 -96 3922 -655 N ATOM 2636 CA VAL B 71 42.492 -23.455 61.459 1.00 80.71 C ANISOU 2636 CA VAL B 71 12348 8987 9331 -185 4045 -648 C ATOM 2637 C VAL B 71 44.001 -23.763 61.450 1.00 87.44 C ANISOU 2637 C VAL B 71 12888 9796 10539 -182 4423 -785 C ATOM 2638 O VAL B 71 44.807 -22.852 61.249 1.00 87.22 O ANISOU 2638 O VAL B 71 12753 9698 10689 -285 4745 -787 O ATOM 2639 CB VAL B 71 41.928 -23.140 62.877 1.00 83.51 C ANISOU 2639 CB VAL B 71 12394 9472 9863 -183 3623 -615 C ATOM 2640 CG1 VAL B 71 42.600 -21.917 63.491 1.00 82.96 C ANISOU 2640 CG1 VAL B 71 12027 9398 10095 -288 3733 -611 C ATOM 2641 CG2 VAL B 71 40.421 -22.930 62.829 1.00 83.27 C ANISOU 2641 CG2 VAL B 71 12656 9477 9507 -175 3277 -490 C ATOM 2642 N TRP B 72 44.373 -25.041 61.623 1.00 86.31 N ANISOU 2642 N TRP B 72 12607 9681 10507 -65 4399 -899 N ATOM 2643 CA TRP B 72 45.771 -25.464 61.572 1.00 88.00 C ANISOU 2643 CA TRP B 72 12516 9849 11070 -32 4745 -1039 C ATOM 2644 C TRP B 72 46.356 -25.315 60.152 1.00 90.52 C ANISOU 2644 C TRP B 72 13140 10014 11239 -79 5279 -1057 C ATOM 2645 O TRP B 72 47.474 -24.823 60.014 1.00 89.59 O ANISOU 2645 O TRP B 72 12787 9834 11422 -144 5660 -1118 O ATOM 2646 CB TRP B 72 45.938 -26.909 62.085 1.00 88.15 C ANISOU 2646 CB TRP B 72 12356 9919 11219 127 4565 -1145 C ATOM 2647 CG TRP B 72 47.299 -27.486 61.829 1.00 90.37 C ANISOU 2647 CG TRP B 72 12380 10134 11823 191 4935 -1293 C ATOM 2648 CD1 TRP B 72 48.424 -27.304 62.580 1.00 93.52 C ANISOU 2648 CD1 TRP B 72 12260 10563 12712 200 5008 -1387 C ATOM 2649 CD2 TRP B 72 47.687 -28.300 60.712 1.00 90.97 C ANISOU 2649 CD2 TRP B 72 12705 10093 11765 259 5292 -1370 C ATOM 2650 NE1 TRP B 72 49.487 -27.973 62.012 1.00 93.62 N ANISOU 2650 NE1 TRP B 72 12151 10487 12932 276 5390 -1517 N ATOM 2651 CE2 TRP B 72 49.067 -28.576 60.853 1.00 95.35 C ANISOU 2651 CE2 TRP B 72 12849 10612 12769 312 5593 -1509 C ATOM 2652 CE3 TRP B 72 47.005 -28.808 59.590 1.00 92.69 C ANISOU 2652 CE3 TRP B 72 13463 10227 11526 280 5386 -1344 C ATOM 2653 CZ2 TRP B 72 49.776 -29.342 59.917 1.00 95.06 C ANISOU 2653 CZ2 TRP B 72 12920 10455 12744 391 6013 -1620 C ATOM 2654 CZ3 TRP B 72 47.709 -29.563 58.660 1.00 94.51 C ANISOU 2654 CZ3 TRP B 72 13833 10337 11738 352 5793 -1456 C ATOM 2655 CH2 TRP B 72 49.076 -29.827 58.828 1.00 95.26 C ANISOU 2655 CH2 TRP B 72 13509 10394 12290 409 6117 -1591 C ATOM 2656 N ARG B 73 45.610 -25.753 59.116 1.00 86.65 N ANISOU 2656 N ARG B 73 13171 9459 10294 -47 5305 -1011 N ATOM 2657 CA ARG B 73 46.051 -25.715 57.719 1.00 86.41 C ANISOU 2657 CA ARG B 73 13523 9272 10036 -77 5797 -1025 C ATOM 2658 C ARG B 73 46.113 -24.300 57.135 1.00 91.14 C ANISOU 2658 C ARG B 73 14325 9781 10522 -227 6062 -909 C ATOM 2659 O ARG B 73 47.075 -23.989 56.426 1.00 90.82 O ANISOU 2659 O ARG B 73 14309 9618 10581 -287 6582 -950 O ATOM 2660 CB ARG B 73 45.197 -26.643 56.837 1.00 84.94 C ANISOU 2660 CB ARG B 73 13857 9041 9374 6 5691 -1020 C ATOM 2661 CG ARG B 73 45.890 -27.094 55.571 1.00 92.02 C ANISOU 2661 CG ARG B 73 15072 9782 10110 29 6205 -1102 C ATOM 2662 CD ARG B 73 44.894 -27.589 54.550 1.00 98.99 C ANISOU 2662 CD ARG B 73 16580 10600 10431 68 6089 -1066 C ATOM 2663 NE ARG B 73 45.455 -27.561 53.199 1.00104.07 N ANISOU 2663 NE ARG B 73 17651 11071 10821 50 6622 -1098 N ATOM 2664 CZ ARG B 73 44.732 -27.610 52.085 1.00117.02 C ANISOU 2664 CZ ARG B 73 19928 12617 11919 49 6624 -1045 C ATOM 2665 NH1 ARG B 73 43.408 -27.685 52.146 1.00 93.05 N ANISOU 2665 NH1 ARG B 73 17142 9646 8566 64 6106 -962 N ATOM 2666 NH2 ARG B 73 45.328 -27.585 50.897 1.00112.66 N ANISOU 2666 NH2 ARG B 73 19771 11898 11138 35 7145 -1079 N ATOM 2667 N ASN B 74 45.095 -23.460 57.419 1.00 87.93 N ANISOU 2667 N ASN B 74 14069 9421 9918 -283 5727 -764 N ATOM 2668 CA ASN B 74 45.008 -22.081 56.925 1.00 87.99 C ANISOU 2668 CA ASN B 74 14302 9334 9795 -415 5919 -634 C ATOM 2669 C ASN B 74 45.477 -21.082 57.997 1.00 93.67 C ANISOU 2669 C ASN B 74 14541 10105 10944 -514 5872 -626 C ATOM 2670 O ASN B 74 44.764 -20.815 58.971 1.00 92.29 O ANISOU 2670 O ASN B 74 14189 10047 10831 -505 5431 -579 O ATOM 2671 CB ASN B 74 43.580 -21.770 56.426 1.00 86.37 C ANISOU 2671 CB ASN B 74 14604 9122 9090 -400 5594 -481 C ATOM 2672 CG ASN B 74 43.395 -20.525 55.566 1.00 88.83 C ANISOU 2672 CG ASN B 74 15328 9290 9131 -500 5822 -332 C ATOM 2673 OD1 ASN B 74 44.141 -19.536 55.647 1.00 78.70 O ANISOU 2673 OD1 ASN B 74 13894 7932 8078 -616 6136 -306 O ATOM 2674 ND2 ASN B 74 42.354 -20.540 54.733 1.00 72.10 N ANISOU 2674 ND2 ASN B 74 13753 7125 6516 -455 5643 -228 N ATOM 2675 N HIS B 75 46.691 -20.532 57.795 1.00 92.67 N ANISOU 2675 N HIS B 75 14211 9881 11120 -617 6346 -681 N ATOM 2676 CA HIS B 75 47.331 -19.552 58.681 1.00 93.19 C ANISOU 2676 CA HIS B 75 13821 9962 11624 -736 6379 -700 C ATOM 2677 C HIS B 75 46.564 -18.231 58.799 1.00 94.69 C ANISOU 2677 C HIS B 75 14209 10118 11651 -839 6219 -539 C ATOM 2678 O HIS B 75 46.639 -17.593 59.850 1.00 93.55 O ANISOU 2678 O HIS B 75 13701 10039 11804 -899 6008 -550 O ATOM 2679 CB HIS B 75 48.787 -19.308 58.263 1.00 94.66 C ANISOU 2679 CB HIS B 75 13779 10027 12162 -833 6967 -802 C ATOM 2680 CG HIS B 75 49.725 -20.406 58.661 1.00 98.85 C ANISOU 2680 CG HIS B 75 13868 10620 13071 -735 7042 -987 C ATOM 2681 ND1 HIS B 75 50.695 -20.209 59.630 1.00101.01 N ANISOU 2681 ND1 HIS B 75 13522 10944 13912 -780 7042 -1108 N ATOM 2682 CD2 HIS B 75 49.821 -21.675 58.198 1.00101.26 C ANISOU 2682 CD2 HIS B 75 14282 10931 13262 -591 7109 -1070 C ATOM 2683 CE1 HIS B 75 51.348 -21.360 59.723 1.00100.75 C ANISOU 2683 CE1 HIS B 75 13233 10950 14099 -651 7105 -1253 C ATOM 2684 NE2 HIS B 75 50.856 -22.273 58.886 1.00101.11 N ANISOU 2684 NE2 HIS B 75 13702 10966 13750 -534 7156 -1235 N ATOM 2685 N HIS B 76 45.820 -17.834 57.737 1.00 90.22 N ANISOU 2685 N HIS B 76 14228 9442 10608 -850 6302 -393 N ATOM 2686 CA HIS B 76 44.992 -16.613 57.717 1.00 89.97 C ANISOU 2686 CA HIS B 76 14453 9358 10375 -919 6144 -224 C ATOM 2687 C HIS B 76 43.759 -16.744 58.626 1.00 91.03 C ANISOU 2687 C HIS B 76 14522 9650 10416 -829 5522 -174 C ATOM 2688 O HIS B 76 43.236 -15.739 59.122 1.00 91.22 O ANISOU 2688 O HIS B 76 14529 9670 10460 -881 5329 -79 O ATOM 2689 CB HIS B 76 44.569 -16.259 56.284 1.00 91.40 C ANISOU 2689 CB HIS B 76 15299 9370 10058 -930 6392 -85 C ATOM 2690 CG HIS B 76 45.725 -16.072 55.360 1.00 95.24 C ANISOU 2690 CG HIS B 76 15901 9683 10604 -1026 7044 -121 C ATOM 2691 ND1 HIS B 76 46.377 -14.857 55.261 1.00 97.36 N ANISOU 2691 ND1 HIS B 76 16119 9805 11068 -1191 7408 -68 N ATOM 2692 CD2 HIS B 76 46.336 -16.966 54.548 1.00 97.54 C ANISOU 2692 CD2 HIS B 76 16338 9918 10804 -981 7399 -212 C ATOM 2693 CE1 HIS B 76 47.344 -15.040 54.373 1.00 97.14 C ANISOU 2693 CE1 HIS B 76 16211 9639 11061 -1246 7986 -121 C ATOM 2694 NE2 HIS B 76 47.362 -16.295 53.918 1.00 97.48 N ANISOU 2694 NE2 HIS B 76 16376 9731 10931 -1118 8007 -211 N ATOM 2695 N MET B 77 43.324 -17.996 58.860 1.00 84.72 N ANISOU 2695 N MET B 77 13677 8978 9535 -695 5235 -244 N ATOM 2696 CA MET B 77 42.205 -18.370 59.721 1.00 82.60 C ANISOU 2696 CA MET B 77 13323 8861 9202 -604 4682 -218 C ATOM 2697 C MET B 77 42.595 -18.349 61.202 1.00 82.77 C ANISOU 2697 C MET B 77 12776 9008 9663 -615 4473 -310 C ATOM 2698 O MET B 77 41.741 -18.590 62.045 1.00 83.05 O ANISOU 2698 O MET B 77 12709 9164 9684 -551 4047 -291 O ATOM 2699 CB MET B 77 41.691 -19.771 59.340 1.00 84.79 C ANISOU 2699 CB MET B 77 13779 9197 9239 -474 4510 -268 C ATOM 2700 CG MET B 77 40.901 -19.804 58.047 1.00 88.36 C ANISOU 2700 CG MET B 77 14831 9554 9189 -443 4531 -168 C ATOM 2701 SD MET B 77 39.896 -21.300 57.859 1.00 92.46 S ANISOU 2701 SD MET B 77 15541 10159 9429 -304 4155 -217 S ATOM 2702 CE MET B 77 38.617 -20.936 58.965 1.00 89.19 C ANISOU 2702 CE MET B 77 14954 9879 9056 -281 3594 -132 C ATOM 2703 N ARG B 78 43.864 -18.076 61.534 1.00 76.40 N ANISOU 2703 N ARG B 78 11607 8171 9249 -695 4764 -412 N ATOM 2704 CA ARG B 78 44.316 -18.063 62.925 1.00 74.99 C ANISOU 2704 CA ARG B 78 10902 8106 9487 -702 4552 -512 C ATOM 2705 C ARG B 78 44.039 -16.715 63.601 1.00 76.97 C ANISOU 2705 C ARG B 78 11062 8342 9843 -808 4422 -444 C ATOM 2706 O ARG B 78 44.953 -15.952 63.927 1.00 77.20 O ANISOU 2706 O ARG B 78 10816 8315 10202 -927 4623 -502 O ATOM 2707 CB ARG B 78 45.781 -18.506 63.053 1.00 74.28 C ANISOU 2707 CB ARG B 78 10419 8001 9802 -722 4856 -674 C ATOM 2708 CG ARG B 78 46.026 -19.959 62.681 1.00 78.08 C ANISOU 2708 CG ARG B 78 10914 8515 10236 -586 4907 -763 C ATOM 2709 CD ARG B 78 47.504 -20.180 62.482 1.00 87.43 C ANISOU 2709 CD ARG B 78 11776 9639 11804 -616 5317 -906 C ATOM 2710 NE ARG B 78 47.801 -21.527 62.003 1.00 97.46 N ANISOU 2710 NE ARG B 78 13092 10910 13026 -482 5430 -993 N ATOM 2711 CZ ARG B 78 48.989 -22.109 62.117 1.00111.50 C ANISOU 2711 CZ ARG B 78 14507 12677 15182 -441 5661 -1143 C ATOM 2712 NH1 ARG B 78 49.994 -21.472 62.703 1.00 96.64 N ANISOU 2712 NH1 ARG B 78 12167 10789 13764 -531 5784 -1227 N ATOM 2713 NH2 ARG B 78 49.178 -23.337 61.656 1.00102.53 N ANISOU 2713 NH2 ARG B 78 13452 11528 13977 -306 5760 -1218 N ATOM 2714 N THR B 79 42.744 -16.439 63.796 1.00 70.46 N ANISOU 2714 N THR B 79 10470 7558 8745 -762 4083 -325 N ATOM 2715 CA THR B 79 42.199 -15.245 64.428 1.00 68.20 C ANISOU 2715 CA THR B 79 10163 7258 8493 -827 3904 -247 C ATOM 2716 C THR B 79 41.684 -15.644 65.813 1.00 69.35 C ANISOU 2716 C THR B 79 10021 7564 8764 -752 3463 -298 C ATOM 2717 O THR B 79 41.359 -16.813 66.019 1.00 69.40 O ANISOU 2717 O THR B 79 9996 7677 8697 -637 3265 -337 O ATOM 2718 CB THR B 79 41.086 -14.643 63.543 1.00 69.80 C ANISOU 2718 CB THR B 79 10860 7371 8289 -814 3867 -71 C ATOM 2719 OG1 THR B 79 39.929 -15.485 63.542 1.00 65.48 O ANISOU 2719 OG1 THR B 79 10483 6924 7470 -681 3517 -28 O ATOM 2720 CG2 THR B 79 41.543 -14.398 62.113 1.00 68.44 C ANISOU 2720 CG2 THR B 79 11047 7033 7923 -870 4299 -12 C ATOM 2721 N VAL B 80 41.613 -14.679 66.752 1.00 63.53 N ANISOU 2721 N VAL B 80 9098 6834 8208 -818 3324 -299 N ATOM 2722 CA VAL B 80 41.131 -14.847 68.134 1.00 62.10 C ANISOU 2722 CA VAL B 80 8675 6783 8136 -762 2932 -342 C ATOM 2723 C VAL B 80 39.840 -15.694 68.167 1.00 64.22 C ANISOU 2723 C VAL B 80 9140 7147 8112 -626 2621 -270 C ATOM 2724 O VAL B 80 39.781 -16.679 68.903 1.00 62.70 O ANISOU 2724 O VAL B 80 8769 7072 7982 -541 2407 -339 O ATOM 2725 CB VAL B 80 40.975 -13.468 68.874 1.00 64.87 C ANISOU 2725 CB VAL B 80 8950 7084 8615 -857 2858 -320 C ATOM 2726 CG1 VAL B 80 40.292 -13.623 70.231 1.00 64.55 C ANISOU 2726 CG1 VAL B 80 8746 7168 8613 -787 2461 -348 C ATOM 2727 CG2 VAL B 80 42.320 -12.781 69.052 1.00 64.27 C ANISOU 2727 CG2 VAL B 80 8602 6926 8893 -1001 3118 -426 C ATOM 2728 N THR B 81 38.843 -15.327 67.326 1.00 60.82 N ANISOU 2728 N THR B 81 9082 6655 7371 -607 2605 -132 N ATOM 2729 CA THR B 81 37.538 -15.991 67.180 1.00 60.31 C ANISOU 2729 CA THR B 81 9226 6657 7033 -497 2324 -57 C ATOM 2730 C THR B 81 37.680 -17.468 66.832 1.00 63.95 C ANISOU 2730 C THR B 81 9699 7181 7419 -417 2311 -122 C ATOM 2731 O THR B 81 37.090 -18.307 67.518 1.00 64.19 O ANISOU 2731 O THR B 81 9624 7319 7448 -339 2039 -149 O ATOM 2732 CB THR B 81 36.692 -15.263 66.130 1.00 64.33 C ANISOU 2732 CB THR B 81 10137 7060 7247 -498 2356 91 C ATOM 2733 OG1 THR B 81 36.843 -13.857 66.296 1.00 65.90 O ANISOU 2733 OG1 THR B 81 10338 7160 7542 -583 2460 144 O ATOM 2734 CG2 THR B 81 35.224 -15.647 66.180 1.00 59.64 C ANISOU 2734 CG2 THR B 81 9697 6531 6433 -397 2011 169 C ATOM 2735 N ASN B 82 38.458 -17.784 65.773 1.00 59.84 N ANISOU 2735 N ASN B 82 9316 6581 6838 -439 2623 -148 N ATOM 2736 CA ASN B 82 38.675 -19.162 65.322 1.00 59.73 C ANISOU 2736 CA ASN B 82 9345 6599 6749 -362 2658 -219 C ATOM 2737 C ASN B 82 39.450 -20.005 66.336 1.00 64.08 C ANISOU 2737 C ASN B 82 9503 7243 7602 -321 2596 -353 C ATOM 2738 O ASN B 82 39.199 -21.207 66.431 1.00 63.67 O ANISOU 2738 O ASN B 82 9451 7249 7492 -230 2457 -396 O ATOM 2739 CB ASN B 82 39.314 -19.212 63.933 1.00 56.63 C ANISOU 2739 CB ASN B 82 9222 6084 6210 -394 3040 -218 C ATOM 2740 CG ASN B 82 38.406 -18.722 62.828 1.00 78.01 C ANISOU 2740 CG ASN B 82 12402 8703 8537 -395 3037 -83 C ATOM 2741 OD1 ASN B 82 37.177 -18.665 62.966 1.00 68.56 O ANISOU 2741 OD1 ASN B 82 11341 7549 7160 -347 2711 -1 O ATOM 2742 ND2 ASN B 82 38.986 -18.358 61.691 1.00 74.00 N ANISOU 2742 ND2 ASN B 82 12161 8061 7895 -447 3403 -56 N ATOM 2743 N TYR B 83 40.367 -19.374 67.101 1.00 60.21 N ANISOU 2743 N TYR B 83 8685 6759 7434 -385 2678 -420 N ATOM 2744 CA TYR B 83 41.131 -20.044 68.146 1.00 60.47 C ANISOU 2744 CA TYR B 83 8334 6876 7766 -338 2576 -544 C ATOM 2745 C TYR B 83 40.164 -20.494 69.250 1.00 62.58 C ANISOU 2745 C TYR B 83 8542 7255 7980 -259 2167 -521 C ATOM 2746 O TYR B 83 40.241 -21.637 69.709 1.00 63.19 O ANISOU 2746 O TYR B 83 8507 7396 8106 -164 2027 -580 O ATOM 2747 CB TYR B 83 42.232 -19.117 68.682 1.00 63.40 C ANISOU 2747 CB TYR B 83 8388 7218 8483 -438 2721 -621 C ATOM 2748 CG TYR B 83 43.556 -19.227 67.950 1.00 68.10 C ANISOU 2748 CG TYR B 83 8862 7732 9280 -483 3115 -710 C ATOM 2749 CD1 TYR B 83 43.721 -20.115 66.886 1.00 70.70 C ANISOU 2749 CD1 TYR B 83 9390 8016 9457 -424 3334 -719 C ATOM 2750 CD2 TYR B 83 44.653 -18.463 68.336 1.00 69.80 C ANISOU 2750 CD2 TYR B 83 8757 7910 9855 -586 3275 -798 C ATOM 2751 CE1 TYR B 83 44.945 -20.242 66.232 1.00 71.45 C ANISOU 2751 CE1 TYR B 83 9366 8030 9753 -459 3730 -808 C ATOM 2752 CE2 TYR B 83 45.881 -18.579 67.683 1.00 71.27 C ANISOU 2752 CE2 TYR B 83 8794 8018 10269 -631 3660 -889 C ATOM 2753 CZ TYR B 83 46.020 -19.466 66.629 1.00 80.12 C ANISOU 2753 CZ TYR B 83 10117 9094 11232 -563 3901 -891 C ATOM 2754 OH TYR B 83 47.225 -19.567 65.980 1.00 85.80 O ANISOU 2754 OH TYR B 83 10688 9726 12185 -605 4317 -984 O ATOM 2755 N PHE B 84 39.196 -19.620 69.604 1.00 55.18 N ANISOU 2755 N PHE B 84 7711 6328 6928 -295 1996 -428 N ATOM 2756 CA PHE B 84 38.142 -19.931 70.555 1.00 52.96 C ANISOU 2756 CA PHE B 84 7415 6136 6573 -231 1654 -391 C ATOM 2757 C PHE B 84 37.182 -20.963 69.961 1.00 56.50 C ANISOU 2757 C PHE B 84 8101 6602 6766 -154 1541 -341 C ATOM 2758 O PHE B 84 36.658 -21.777 70.708 1.00 56.39 O ANISOU 2758 O PHE B 84 8019 6660 6748 -86 1314 -354 O ATOM 2759 CB PHE B 84 37.389 -18.670 71.000 1.00 53.40 C ANISOU 2759 CB PHE B 84 7521 6178 6589 -286 1545 -312 C ATOM 2760 CG PHE B 84 38.053 -17.804 72.052 1.00 53.50 C ANISOU 2760 CG PHE B 84 7274 6198 6856 -348 1525 -377 C ATOM 2761 CD1 PHE B 84 38.427 -18.334 73.279 1.00 56.02 C ANISOU 2761 CD1 PHE B 84 7340 6603 7344 -301 1340 -467 C ATOM 2762 CD2 PHE B 84 38.211 -16.438 71.851 1.00 54.57 C ANISOU 2762 CD2 PHE B 84 7445 6245 7043 -450 1664 -346 C ATOM 2763 CE1 PHE B 84 39.018 -17.527 74.255 1.00 57.29 C ANISOU 2763 CE1 PHE B 84 7280 6766 7721 -359 1289 -539 C ATOM 2764 CE2 PHE B 84 38.791 -15.632 72.832 1.00 56.80 C ANISOU 2764 CE2 PHE B 84 7497 6524 7561 -517 1629 -420 C ATOM 2765 CZ PHE B 84 39.205 -16.183 74.020 1.00 55.28 C ANISOU 2765 CZ PHE B 84 7049 6424 7532 -473 1435 -523 C ATOM 2766 N LEU B 85 36.979 -20.959 68.627 1.00 53.05 N ANISOU 2766 N LEU B 85 7953 6088 6114 -169 1701 -290 N ATOM 2767 CA LEU B 85 36.128 -21.955 67.948 1.00 52.47 C ANISOU 2767 CA LEU B 85 8123 6018 5795 -107 1592 -261 C ATOM 2768 C LEU B 85 36.734 -23.350 68.030 1.00 56.71 C ANISOU 2768 C LEU B 85 8562 6577 6407 -37 1619 -363 C ATOM 2769 O LEU B 85 35.982 -24.311 68.233 1.00 57.10 O ANISOU 2769 O LEU B 85 8667 6665 6364 22 1412 -361 O ATOM 2770 CB LEU B 85 35.767 -21.558 66.494 1.00 51.98 C ANISOU 2770 CB LEU B 85 8432 5860 5457 -134 1733 -186 C ATOM 2771 CG LEU B 85 34.797 -20.359 66.374 1.00 55.49 C ANISOU 2771 CG LEU B 85 9032 6276 5774 -168 1617 -62 C ATOM 2772 CD1 LEU B 85 34.438 -20.067 64.930 1.00 54.92 C ANISOU 2772 CD1 LEU B 85 9361 6103 5405 -176 1724 16 C ATOM 2773 CD2 LEU B 85 33.538 -20.545 67.253 1.00 54.63 C ANISOU 2773 CD2 LEU B 85 8846 6254 5658 -123 1262 -22 C ATOM 2774 N VAL B 86 38.101 -23.457 67.922 1.00 52.33 N ANISOU 2774 N VAL B 86 7840 5992 6050 -42 1874 -455 N ATOM 2775 CA VAL B 86 38.876 -24.706 68.077 1.00 51.26 C ANISOU 2775 CA VAL B 86 7562 5866 6048 41 1921 -563 C ATOM 2776 C VAL B 86 38.662 -25.200 69.528 1.00 54.09 C ANISOU 2776 C VAL B 86 7675 6317 6558 103 1622 -584 C ATOM 2777 O VAL B 86 38.496 -26.394 69.736 1.00 55.86 O ANISOU 2777 O VAL B 86 7910 6556 6761 187 1506 -616 O ATOM 2778 CB VAL B 86 40.395 -24.538 67.764 1.00 54.84 C ANISOU 2778 CB VAL B 86 7829 6267 6742 23 2256 -659 C ATOM 2779 CG1 VAL B 86 41.180 -25.812 68.076 1.00 54.28 C ANISOU 2779 CG1 VAL B 86 7567 6206 6849 134 2269 -772 C ATOM 2780 CG2 VAL B 86 40.640 -24.098 66.326 1.00 54.54 C ANISOU 2780 CG2 VAL B 86 8068 6121 6534 -38 2595 -635 C ATOM 2781 N ASN B 87 38.655 -24.285 70.514 1.00 48.22 N ANISOU 2781 N ASN B 87 6746 5624 5953 60 1505 -565 N ATOM 2782 CA ASN B 87 38.401 -24.628 71.919 1.00 47.71 C ANISOU 2782 CA ASN B 87 6498 5638 5991 114 1226 -576 C ATOM 2783 C ASN B 87 36.976 -25.173 72.152 1.00 50.29 C ANISOU 2783 C ASN B 87 7007 5996 6105 144 989 -496 C ATOM 2784 O ASN B 87 36.776 -26.034 73.011 1.00 50.31 O ANISOU 2784 O ASN B 87 6936 6036 6143 215 810 -511 O ATOM 2785 CB ASN B 87 38.688 -23.453 72.863 1.00 46.04 C ANISOU 2785 CB ASN B 87 6088 5460 5945 54 1163 -583 C ATOM 2786 CG ASN B 87 38.898 -23.931 74.270 1.00 57.77 C ANISOU 2786 CG ASN B 87 7368 7013 7571 124 927 -630 C ATOM 2787 OD1 ASN B 87 39.646 -24.879 74.509 1.00 53.53 O ANISOU 2787 OD1 ASN B 87 6699 6481 7159 211 910 -702 O ATOM 2788 ND2 ASN B 87 38.222 -23.323 75.221 1.00 48.05 N ANISOU 2788 ND2 ASN B 87 6126 5824 6308 101 740 -588 N ATOM 2789 N LEU B 88 36.000 -24.672 71.386 1.00 45.69 N ANISOU 2789 N LEU B 88 6659 5389 5314 92 990 -411 N ATOM 2790 CA LEU B 88 34.616 -25.127 71.427 1.00 45.27 C ANISOU 2790 CA LEU B 88 6764 5355 5083 108 783 -342 C ATOM 2791 C LEU B 88 34.593 -26.563 70.887 1.00 52.42 C ANISOU 2791 C LEU B 88 7785 6229 5904 165 782 -385 C ATOM 2792 O LEU B 88 34.021 -27.430 71.548 1.00 55.04 O ANISOU 2792 O LEU B 88 8097 6585 6231 205 604 -381 O ATOM 2793 CB LEU B 88 33.724 -24.140 70.624 1.00 44.92 C ANISOU 2793 CB LEU B 88 6925 5280 4863 48 785 -250 C ATOM 2794 CG LEU B 88 32.199 -24.356 70.537 1.00 49.12 C ANISOU 2794 CG LEU B 88 7603 5825 5234 52 564 -176 C ATOM 2795 CD1 LEU B 88 31.531 -24.468 71.935 1.00 49.66 C ANISOU 2795 CD1 LEU B 88 7501 5961 5406 71 363 -159 C ATOM 2796 CD2 LEU B 88 31.563 -23.226 69.773 1.00 47.90 C ANISOU 2796 CD2 LEU B 88 7621 5633 4947 12 572 -90 C ATOM 2797 N SER B 89 35.337 -26.837 69.778 1.00 47.71 N ANISOU 2797 N SER B 89 7298 5568 5262 170 1006 -436 N ATOM 2798 CA SER B 89 35.492 -28.154 69.163 1.00 48.10 C ANISOU 2798 CA SER B 89 7472 5566 5237 228 1053 -497 C ATOM 2799 C SER B 89 36.154 -29.206 70.088 1.00 55.13 C ANISOU 2799 C SER B 89 8155 6471 6321 318 999 -569 C ATOM 2800 O SER B 89 35.696 -30.360 70.129 1.00 54.02 O ANISOU 2800 O SER B 89 8105 6303 6116 366 892 -585 O ATOM 2801 CB SER B 89 36.260 -28.048 67.849 1.00 51.46 C ANISOU 2801 CB SER B 89 8056 5913 5584 214 1349 -540 C ATOM 2802 OG SER B 89 35.448 -27.438 66.862 1.00 60.46 O ANISOU 2802 OG SER B 89 9488 7016 6467 155 1349 -469 O ATOM 2803 N LEU B 90 37.225 -28.804 70.828 1.00 53.38 N ANISOU 2803 N LEU B 90 7661 6281 6339 342 1060 -613 N ATOM 2804 CA LEU B 90 37.914 -29.646 71.815 1.00 53.70 C ANISOU 2804 CA LEU B 90 7487 6338 6579 442 972 -673 C ATOM 2805 C LEU B 90 36.936 -30.094 72.909 1.00 58.16 C ANISOU 2805 C LEU B 90 8058 6944 7094 466 689 -613 C ATOM 2806 O LEU B 90 36.946 -31.255 73.288 1.00 58.14 O ANISOU 2806 O LEU B 90 8059 6914 7118 551 601 -635 O ATOM 2807 CB LEU B 90 39.106 -28.910 72.451 1.00 53.86 C ANISOU 2807 CB LEU B 90 7209 6392 6864 447 1040 -730 C ATOM 2808 CG LEU B 90 40.307 -28.547 71.572 1.00 58.07 C ANISOU 2808 CG LEU B 90 7653 6875 7536 431 1351 -809 C ATOM 2809 CD1 LEU B 90 41.423 -28.007 72.424 1.00 57.75 C ANISOU 2809 CD1 LEU B 90 7267 6870 7806 441 1347 -878 C ATOM 2810 CD2 LEU B 90 40.829 -29.752 70.773 1.00 61.17 C ANISOU 2810 CD2 LEU B 90 8119 7191 7930 524 1509 -882 C ATOM 2811 N ALA B 91 36.068 -29.186 73.376 1.00 55.93 N ANISOU 2811 N ALA B 91 7794 6715 6740 393 567 -535 N ATOM 2812 CA ALA B 91 35.022 -29.490 74.359 1.00 55.99 C ANISOU 2812 CA ALA B 91 7825 6755 6692 399 341 -472 C ATOM 2813 C ALA B 91 33.919 -30.355 73.723 1.00 61.14 C ANISOU 2813 C ALA B 91 8699 7362 7169 382 283 -437 C ATOM 2814 O ALA B 91 33.324 -31.183 74.414 1.00 62.05 O ANISOU 2814 O ALA B 91 8837 7468 7273 410 143 -413 O ATOM 2815 CB ALA B 91 34.415 -28.201 74.899 1.00 56.31 C ANISOU 2815 CB ALA B 91 7824 6853 6719 327 268 -410 C ATOM 2816 N ASP B 92 33.616 -30.132 72.426 1.00 57.28 N ANISOU 2816 N ASP B 92 8385 6839 6541 329 383 -435 N ATOM 2817 CA ASP B 92 32.601 -30.893 71.702 1.00 57.18 C ANISOU 2817 CA ASP B 92 8588 6778 6362 304 309 -420 C ATOM 2818 C ASP B 92 33.079 -32.334 71.525 1.00 61.79 C ANISOU 2818 C ASP B 92 9225 7289 6965 375 344 -493 C ATOM 2819 O ASP B 92 32.297 -33.263 71.734 1.00 60.97 O ANISOU 2819 O ASP B 92 9200 7147 6816 373 214 -482 O ATOM 2820 CB ASP B 92 32.266 -30.229 70.348 1.00 59.60 C ANISOU 2820 CB ASP B 92 9093 7057 6494 243 393 -404 C ATOM 2821 CG ASP B 92 31.481 -28.901 70.399 1.00 73.39 C ANISOU 2821 CG ASP B 92 10843 8852 8190 178 318 -317 C ATOM 2822 OD1 ASP B 92 30.936 -28.559 71.492 1.00 70.40 O ANISOU 2822 OD1 ASP B 92 10322 8528 7899 169 184 -269 O ATOM 2823 OD2 ASP B 92 31.417 -28.198 69.342 1.00 82.12 O ANISOU 2823 OD2 ASP B 92 12112 9928 9162 142 402 -295 O ATOM 2824 N VAL B 93 34.389 -32.517 71.207 1.00 58.79 N ANISOU 2824 N VAL B 93 8780 6879 6680 441 530 -569 N ATOM 2825 CA VAL B 93 35.039 -33.817 71.041 1.00 57.98 C ANISOU 2825 CA VAL B 93 8705 6695 6629 533 596 -649 C ATOM 2826 C VAL B 93 35.109 -34.535 72.393 1.00 60.16 C ANISOU 2826 C VAL B 93 8838 6976 7043 611 437 -634 C ATOM 2827 O VAL B 93 34.868 -35.737 72.438 1.00 61.37 O ANISOU 2827 O VAL B 93 9093 7052 7174 656 382 -653 O ATOM 2828 CB VAL B 93 36.400 -33.714 70.283 1.00 62.12 C ANISOU 2828 CB VAL B 93 9179 7183 7242 585 864 -737 C ATOM 2829 CG1 VAL B 93 37.281 -34.945 70.498 1.00 62.01 C ANISOU 2829 CG1 VAL B 93 9088 7098 7375 716 919 -821 C ATOM 2830 CG2 VAL B 93 36.169 -33.495 68.793 1.00 61.77 C ANISOU 2830 CG2 VAL B 93 9399 7086 6987 523 1026 -757 C ATOM 2831 N LEU B 94 35.364 -33.808 73.491 1.00 54.90 N ANISOU 2831 N LEU B 94 7972 6391 6499 621 354 -596 N ATOM 2832 CA LEU B 94 35.371 -34.401 74.831 1.00 54.18 C ANISOU 2832 CA LEU B 94 7786 6302 6497 695 188 -569 C ATOM 2833 C LEU B 94 33.985 -34.955 75.160 1.00 56.27 C ANISOU 2833 C LEU B 94 8205 6541 6633 639 43 -496 C ATOM 2834 O LEU B 94 33.879 -36.103 75.581 1.00 56.09 O ANISOU 2834 O LEU B 94 8244 6443 6622 699 -23 -493 O ATOM 2835 CB LEU B 94 35.818 -33.398 75.921 1.00 54.31 C ANISOU 2835 CB LEU B 94 7594 6408 6632 702 113 -548 C ATOM 2836 CG LEU B 94 35.813 -33.941 77.376 1.00 59.34 C ANISOU 2836 CG LEU B 94 8175 7047 7325 786 -74 -513 C ATOM 2837 CD1 LEU B 94 36.784 -35.140 77.551 1.00 59.28 C ANISOU 2837 CD1 LEU B 94 8126 6962 7437 936 -82 -570 C ATOM 2838 CD2 LEU B 94 36.025 -32.826 78.409 1.00 60.69 C ANISOU 2838 CD2 LEU B 94 8192 7305 7560 769 -167 -497 C ATOM 2839 N ALA B 95 32.932 -34.144 74.965 1.00 51.14 N ANISOU 2839 N ALA B 95 7611 5942 5880 526 1 -438 N ATOM 2840 CA ALA B 95 31.554 -34.557 75.210 1.00 50.28 C ANISOU 2840 CA ALA B 95 7611 5811 5683 457 -122 -376 C ATOM 2841 C ALA B 95 31.146 -35.738 74.288 1.00 54.77 C ANISOU 2841 C ALA B 95 8365 6275 6170 441 -111 -418 C ATOM 2842 O ALA B 95 30.608 -36.723 74.779 1.00 53.96 O ANISOU 2842 O ALA B 95 8324 6104 6075 442 -190 -399 O ATOM 2843 CB ALA B 95 30.610 -33.376 75.014 1.00 50.46 C ANISOU 2843 CB ALA B 95 7630 5903 5639 355 -160 -320 C ATOM 2844 N THR B 96 31.422 -35.643 72.975 1.00 52.56 N ANISOU 2844 N THR B 96 8193 5970 5807 424 -6 -477 N ATOM 2845 CA THR B 96 31.058 -36.664 71.987 1.00 53.89 C ANISOU 2845 CA THR B 96 8569 6035 5873 402 3 -535 C ATOM 2846 C THR B 96 31.757 -38.024 72.227 1.00 60.92 C ANISOU 2846 C THR B 96 9491 6818 6839 504 47 -594 C ATOM 2847 O THR B 96 31.063 -39.041 72.329 1.00 60.27 O ANISOU 2847 O THR B 96 9523 6644 6732 477 -37 -597 O ATOM 2848 CB THR B 96 31.267 -36.130 70.568 1.00 60.52 C ANISOU 2848 CB THR B 96 9546 6871 6576 370 118 -583 C ATOM 2849 OG1 THR B 96 30.497 -34.932 70.440 1.00 60.63 O ANISOU 2849 OG1 THR B 96 9544 6968 6523 287 44 -513 O ATOM 2850 CG2 THR B 96 30.852 -37.130 69.500 1.00 59.87 C ANISOU 2850 CG2 THR B 96 9714 6678 6354 343 111 -655 C ATOM 2851 N ALA B 97 33.108 -38.031 72.330 1.00 59.08 N ANISOU 2851 N ALA B 97 9146 6585 6717 620 175 -641 N ATOM 2852 CA ALA B 97 33.899 -39.243 72.525 1.00 59.34 C ANISOU 2852 CA ALA B 97 9190 6511 6846 745 223 -700 C ATOM 2853 C ALA B 97 33.580 -40.021 73.805 1.00 64.94 C ANISOU 2853 C ALA B 97 9869 7175 7629 792 73 -637 C ATOM 2854 O ALA B 97 33.227 -41.198 73.718 1.00 64.35 O ANISOU 2854 O ALA B 97 9945 6975 7531 803 45 -655 O ATOM 2855 CB ALA B 97 35.383 -38.924 72.457 1.00 59.90 C ANISOU 2855 CB ALA B 97 9092 6605 7061 861 379 -762 C ATOM 2856 N ILE B 98 33.676 -39.367 74.978 1.00 62.25 N ANISOU 2856 N ILE B 98 9362 6925 7366 814 -18 -565 N ATOM 2857 CA ILE B 98 33.516 -40.014 76.282 1.00 62.68 C ANISOU 2857 CA ILE B 98 9407 6935 7472 875 -146 -498 C ATOM 2858 C ILE B 98 32.078 -40.027 76.837 1.00 65.50 C ANISOU 2858 C ILE B 98 9853 7293 7742 750 -252 -407 C ATOM 2859 O ILE B 98 31.657 -41.041 77.399 1.00 67.10 O ANISOU 2859 O ILE B 98 10163 7387 7944 764 -305 -368 O ATOM 2860 CB ILE B 98 34.521 -39.377 77.296 1.00 66.28 C ANISOU 2860 CB ILE B 98 9658 7476 8052 983 -195 -483 C ATOM 2861 CG1 ILE B 98 35.980 -39.791 76.942 1.00 67.71 C ANISOU 2861 CG1 ILE B 98 9733 7613 8381 1138 -106 -577 C ATOM 2862 CG2 ILE B 98 34.198 -39.742 78.755 1.00 66.19 C ANISOU 2862 CG2 ILE B 98 9669 7442 8039 1029 -348 -392 C ATOM 2863 CD1 ILE B 98 37.097 -38.954 77.627 1.00 79.97 C ANISOU 2863 CD1 ILE B 98 11032 9262 10090 1223 -143 -598 C ATOM 2864 N CYS B 99 31.341 -38.936 76.696 1.00 59.16 N ANISOU 2864 N CYS B 99 9001 6595 6882 634 -269 -372 N ATOM 2865 CA CYS B 99 30.036 -38.790 77.334 1.00 57.24 C ANISOU 2865 CA CYS B 99 8787 6365 6598 526 -352 -289 C ATOM 2866 C CYS B 99 28.834 -39.271 76.521 1.00 58.25 C ANISOU 2866 C CYS B 99 9041 6428 6662 396 -373 -300 C ATOM 2867 O CYS B 99 27.973 -39.924 77.102 1.00 58.02 O ANISOU 2867 O CYS B 99 9070 6328 6648 339 -420 -252 O ATOM 2868 CB CYS B 99 29.855 -37.355 77.805 1.00 57.02 C ANISOU 2868 CB CYS B 99 8622 6475 6569 487 -373 -244 C ATOM 2869 SG CYS B 99 31.301 -36.700 78.681 1.00 60.79 S ANISOU 2869 SG CYS B 99 8937 7027 7132 621 -374 -258 S ATOM 2870 N LEU B 100 28.756 -38.966 75.220 1.00 53.10 N ANISOU 2870 N LEU B 100 8440 5792 5942 346 -343 -364 N ATOM 2871 CA LEU B 100 27.637 -39.393 74.354 1.00 52.07 C ANISOU 2871 CA LEU B 100 8437 5601 5747 224 -403 -391 C ATOM 2872 C LEU B 100 27.282 -40.914 74.485 1.00 55.03 C ANISOU 2872 C LEU B 100 8945 5814 6151 206 -427 -414 C ATOM 2873 O LEU B 100 26.092 -41.202 74.677 1.00 52.87 O ANISOU 2873 O LEU B 100 8686 5500 5901 88 -505 -384 O ATOM 2874 CB LEU B 100 27.885 -38.990 72.875 1.00 51.47 C ANISOU 2874 CB LEU B 100 8458 5542 5558 207 -362 -469 C ATOM 2875 CG LEU B 100 26.770 -39.254 71.861 1.00 55.53 C ANISOU 2875 CG LEU B 100 9114 6007 5978 86 -465 -509 C ATOM 2876 CD1 LEU B 100 26.842 -38.270 70.700 1.00 55.15 C ANISOU 2876 CD1 LEU B 100 9135 6025 5795 69 -452 -536 C ATOM 2877 CD2 LEU B 100 26.808 -40.707 71.323 1.00 55.86 C ANISOU 2877 CD2 LEU B 100 9342 5889 5994 82 -461 -598 C ATOM 2878 N PRO B 101 28.248 -41.884 74.376 1.00 52.09 N ANISOU 2878 N PRO B 101 8662 5336 5795 315 -355 -470 N ATOM 2879 CA PRO B 101 27.871 -43.307 74.486 1.00 51.94 C ANISOU 2879 CA PRO B 101 8788 5141 5804 293 -374 -489 C ATOM 2880 C PRO B 101 27.341 -43.697 75.867 1.00 53.81 C ANISOU 2880 C PRO B 101 8992 5332 6120 277 -411 -384 C ATOM 2881 O PRO B 101 26.449 -44.542 75.963 1.00 52.09 O ANISOU 2881 O PRO B 101 8871 4990 5930 177 -442 -377 O ATOM 2882 CB PRO B 101 29.161 -44.057 74.111 1.00 53.94 C ANISOU 2882 CB PRO B 101 9123 5303 6069 445 -275 -568 C ATOM 2883 CG PRO B 101 30.041 -43.026 73.445 1.00 58.48 C ANISOU 2883 CG PRO B 101 9610 6004 6606 506 -192 -613 C ATOM 2884 CD PRO B 101 29.705 -41.756 74.153 1.00 53.93 C ANISOU 2884 CD PRO B 101 8856 5588 6045 464 -247 -521 C ATOM 2885 N ALA B 102 27.853 -43.038 76.923 1.00 49.95 N ANISOU 2885 N ALA B 102 8378 4938 5662 364 -405 -306 N ATOM 2886 CA ALA B 102 27.392 -43.218 78.300 1.00 49.02 C ANISOU 2886 CA ALA B 102 8253 4790 5581 357 -426 -197 C ATOM 2887 C ALA B 102 25.928 -42.752 78.399 1.00 53.58 C ANISOU 2887 C ALA B 102 8781 5408 6169 179 -455 -153 C ATOM 2888 O ALA B 102 25.094 -43.511 78.895 1.00 55.02 O ANISOU 2888 O ALA B 102 9035 5475 6394 95 -445 -108 O ATOM 2889 CB ALA B 102 28.276 -42.443 79.265 1.00 48.95 C ANISOU 2889 CB ALA B 102 8132 4889 5577 486 -435 -145 C ATOM 2890 N SER B 103 25.601 -41.572 77.819 1.00 48.80 N ANISOU 2890 N SER B 103 8056 4945 5539 120 -483 -172 N ATOM 2891 CA SER B 103 24.243 -41.025 77.810 1.00 47.96 C ANISOU 2891 CA SER B 103 7869 4886 5468 -28 -523 -140 C ATOM 2892 C SER B 103 23.258 -41.860 77.016 1.00 50.19 C ANISOU 2892 C SER B 103 8226 5057 5787 -166 -576 -195 C ATOM 2893 O SER B 103 22.156 -42.108 77.516 1.00 49.87 O ANISOU 2893 O SER B 103 8145 4967 5836 -283 -581 -153 O ATOM 2894 CB SER B 103 24.223 -39.572 77.360 1.00 51.49 C ANISOU 2894 CB SER B 103 8186 5496 5881 -32 -552 -144 C ATOM 2895 OG SER B 103 24.740 -38.739 78.380 1.00 58.14 O ANISOU 2895 OG SER B 103 8937 6430 6722 51 -512 -83 O ATOM 2896 N LEU B 104 23.652 -42.330 75.816 1.00 46.64 N ANISOU 2896 N LEU B 104 7890 4556 5274 -157 -607 -296 N ATOM 2897 CA LEU B 104 22.822 -43.209 74.984 1.00 47.03 C ANISOU 2897 CA LEU B 104 8043 4484 5344 -286 -681 -372 C ATOM 2898 C LEU B 104 22.544 -44.541 75.724 1.00 51.94 C ANISOU 2898 C LEU B 104 8758 4923 6056 -326 -632 -348 C ATOM 2899 O LEU B 104 21.415 -45.031 75.710 1.00 50.79 O ANISOU 2899 O LEU B 104 8602 4691 6006 -480 -677 -357 O ATOM 2900 CB LEU B 104 23.503 -43.466 73.617 1.00 47.59 C ANISOU 2900 CB LEU B 104 8266 4524 5293 -242 -699 -491 C ATOM 2901 CG LEU B 104 23.156 -44.779 72.851 1.00 53.36 C ANISOU 2901 CG LEU B 104 9186 5070 6017 -321 -744 -596 C ATOM 2902 CD1 LEU B 104 21.709 -44.774 72.321 1.00 53.86 C ANISOU 2902 CD1 LEU B 104 9220 5115 6128 -508 -903 -636 C ATOM 2903 CD2 LEU B 104 24.125 -45.018 71.712 1.00 55.41 C ANISOU 2903 CD2 LEU B 104 9620 5296 6138 -229 -700 -706 C ATOM 2904 N LEU B 105 23.568 -45.110 76.371 1.00 50.01 N ANISOU 2904 N LEU B 105 8598 4610 5794 -186 -543 -316 N ATOM 2905 CA LEU B 105 23.413 -46.358 77.116 1.00 50.61 C ANISOU 2905 CA LEU B 105 8798 4496 5938 -199 -488 -276 C ATOM 2906 C LEU B 105 22.496 -46.184 78.335 1.00 54.37 C ANISOU 2906 C LEU B 105 9192 4970 6496 -288 -443 -157 C ATOM 2907 O LEU B 105 21.706 -47.078 78.615 1.00 55.27 O ANISOU 2907 O LEU B 105 9377 4925 6698 -407 -409 -140 O ATOM 2908 CB LEU B 105 24.780 -46.945 77.499 1.00 50.98 C ANISOU 2908 CB LEU B 105 8955 4471 5944 0 -427 -266 C ATOM 2909 CG LEU B 105 24.846 -48.427 77.752 1.00 57.15 C ANISOU 2909 CG LEU B 105 9932 5012 6769 12 -384 -266 C ATOM 2910 CD1 LEU B 105 24.698 -49.232 76.462 1.00 57.25 C ANISOU 2910 CD1 LEU B 105 10077 4898 6776 -59 -410 -406 C ATOM 2911 CD2 LEU B 105 26.149 -48.783 78.396 1.00 62.16 C ANISOU 2911 CD2 LEU B 105 10633 5602 7383 236 -345 -223 C ATOM 2912 N VAL B 106 22.569 -45.036 79.027 1.00 50.14 N ANISOU 2912 N VAL B 106 8516 4598 5938 -240 -428 -83 N ATOM 2913 CA VAL B 106 21.695 -44.735 80.171 1.00 50.71 C ANISOU 2913 CA VAL B 106 8515 4679 6072 -316 -360 23 C ATOM 2914 C VAL B 106 20.249 -44.536 79.682 1.00 57.47 C ANISOU 2914 C VAL B 106 9241 5542 7053 -518 -393 -8 C ATOM 2915 O VAL B 106 19.316 -45.054 80.288 1.00 56.99 O ANISOU 2915 O VAL B 106 9177 5372 7104 -641 -315 40 O ATOM 2916 CB VAL B 106 22.185 -43.501 80.998 1.00 54.01 C ANISOU 2916 CB VAL B 106 8833 5268 6422 -204 -340 93 C ATOM 2917 CG1 VAL B 106 21.184 -43.110 82.079 1.00 53.29 C ANISOU 2917 CG1 VAL B 106 8672 5190 6386 -292 -250 186 C ATOM 2918 CG2 VAL B 106 23.538 -43.764 81.626 1.00 53.94 C ANISOU 2918 CG2 VAL B 106 8936 5236 6323 -13 -330 126 C ATOM 2919 N ASP B 107 20.071 -43.772 78.598 1.00 56.74 N ANISOU 2919 N ASP B 107 9042 5569 6949 -549 -509 -87 N ATOM 2920 CA ASP B 107 18.750 -43.441 78.085 1.00 57.74 C ANISOU 2920 CA ASP B 107 9019 5720 7199 -715 -587 -122 C ATOM 2921 C ASP B 107 17.973 -44.660 77.569 1.00 63.89 C ANISOU 2921 C ASP B 107 9866 6320 8091 -873 -632 -195 C ATOM 2922 O ASP B 107 16.755 -44.710 77.724 1.00 64.59 O ANISOU 2922 O ASP B 107 9817 6372 8352 -1030 -642 -193 O ATOM 2923 CB ASP B 107 18.840 -42.314 77.034 1.00 59.64 C ANISOU 2923 CB ASP B 107 9168 6123 7368 -683 -720 -179 C ATOM 2924 CG ASP B 107 19.060 -40.888 77.593 1.00 70.86 C ANISOU 2924 CG ASP B 107 10453 7718 8753 -594 -682 -106 C ATOM 2925 OD1 ASP B 107 18.950 -40.700 78.837 1.00 69.67 O ANISOU 2925 OD1 ASP B 107 10252 7573 8645 -577 -562 -16 O ATOM 2926 OD2 ASP B 107 19.316 -39.959 76.780 1.00 76.78 O ANISOU 2926 OD2 ASP B 107 11165 8584 9422 -545 -766 -140 O ATOM 2927 N ILE B 108 18.678 -45.653 77.023 1.00 61.19 N ANISOU 2927 N ILE B 108 9724 5853 7671 -831 -647 -262 N ATOM 2928 CA ILE B 108 18.115 -46.872 76.438 1.00 61.59 C ANISOU 2928 CA ILE B 108 9883 5713 7808 -971 -696 -351 C ATOM 2929 C ILE B 108 17.868 -47.985 77.480 1.00 65.23 C ANISOU 2929 C ILE B 108 10437 5973 8373 -1030 -543 -279 C ATOM 2930 O ILE B 108 16.917 -48.759 77.320 1.00 64.68 O ANISOU 2930 O ILE B 108 10363 5753 8459 -1212 -556 -324 O ATOM 2931 CB ILE B 108 19.061 -47.304 75.266 1.00 65.17 C ANISOU 2931 CB ILE B 108 10528 6128 8104 -880 -773 -469 C ATOM 2932 CG1 ILE B 108 18.797 -46.448 73.992 1.00 66.58 C ANISOU 2932 CG1 ILE B 108 10649 6443 8204 -907 -947 -562 C ATOM 2933 CG2 ILE B 108 19.086 -48.803 74.965 1.00 65.49 C ANISOU 2933 CG2 ILE B 108 10777 5928 8180 -943 -760 -546 C ATOM 2934 CD1 ILE B 108 17.460 -46.689 73.225 1.00 81.60 C ANISOU 2934 CD1 ILE B 108 12489 8290 10225 -1112 -1128 -657 C ATOM 2935 N THR B 109 18.714 -48.069 78.532 1.00 60.75 N ANISOU 2935 N THR B 109 9964 5392 7724 -880 -408 -169 N ATOM 2936 CA THR B 109 18.604 -49.119 79.548 1.00 59.79 C ANISOU 2936 CA THR B 109 9988 5068 7661 -906 -258 -82 C ATOM 2937 C THR B 109 17.969 -48.640 80.853 1.00 66.39 C ANISOU 2937 C THR B 109 10729 5936 8558 -949 -113 54 C ATOM 2938 O THR B 109 17.549 -49.474 81.662 1.00 68.18 O ANISOU 2938 O THR B 109 11068 5980 8858 -1025 31 129 O ATOM 2939 CB THR B 109 19.969 -49.806 79.810 1.00 55.86 C ANISOU 2939 CB THR B 109 9719 4479 7027 -701 -220 -56 C ATOM 2940 OG1 THR B 109 20.820 -48.960 80.585 1.00 54.53 O ANISOU 2940 OG1 THR B 109 9514 4464 6740 -517 -196 33 O ATOM 2941 CG2 THR B 109 20.664 -50.292 78.540 1.00 48.59 C ANISOU 2941 CG2 THR B 109 8905 3512 6045 -643 -322 -196 C ATOM 2942 N GLU B 110 17.936 -47.313 81.078 1.00 63.43 N ANISOU 2942 N GLU B 110 10177 5779 8145 -895 -133 88 N ATOM 2943 CA GLU B 110 17.449 -46.648 82.299 1.00 63.64 C ANISOU 2943 CA GLU B 110 10119 5865 8197 -906 10 206 C ATOM 2944 C GLU B 110 18.327 -47.014 83.521 1.00 65.88 C ANISOU 2944 C GLU B 110 10622 6075 8333 -751 127 326 C ATOM 2945 O GLU B 110 17.938 -46.785 84.678 1.00 65.48 O ANISOU 2945 O GLU B 110 10596 6009 8277 -765 279 433 O ATOM 2946 CB GLU B 110 15.951 -46.913 82.543 1.00 65.43 C ANISOU 2946 CB GLU B 110 10213 5996 8650 -1134 115 216 C ATOM 2947 CG GLU B 110 15.045 -46.025 81.712 1.00 79.87 C ANISOU 2947 CG GLU B 110 11758 7967 10620 -1242 -11 130 C ATOM 2948 CD GLU B 110 13.554 -46.241 81.890 1.00112.25 C ANISOU 2948 CD GLU B 110 15671 11984 14996 -1466 74 122 C ATOM 2949 OE1 GLU B 110 13.150 -46.889 82.884 1.00117.18 O ANISOU 2949 OE1 GLU B 110 16372 12452 15697 -1545 294 207 O ATOM 2950 OE2 GLU B 110 12.785 -45.750 81.031 1.00110.07 O ANISOU 2950 OE2 GLU B 110 15168 11790 14864 -1561 -79 31 O ATOM 2951 N SER B 111 19.535 -47.564 83.238 1.00 59.88 N ANISOU 2951 N SER B 111 10030 5270 7451 -592 49 302 N ATOM 2952 CA SER B 111 20.506 -48.010 84.231 1.00 57.51 C ANISOU 2952 CA SER B 111 9947 4890 7015 -415 98 399 C ATOM 2953 C SER B 111 21.958 -47.542 83.957 1.00 57.11 C ANISOU 2953 C SER B 111 9896 4969 6832 -190 -32 361 C ATOM 2954 O SER B 111 22.317 -47.210 82.822 1.00 56.37 O ANISOU 2954 O SER B 111 9694 4974 6750 -175 -136 249 O ATOM 2955 CB SER B 111 20.436 -49.531 84.399 1.00 59.40 C ANISOU 2955 CB SER B 111 10422 4853 7292 -452 172 428 C ATOM 2956 OG SER B 111 20.951 -50.219 83.273 1.00 65.96 O ANISOU 2956 OG SER B 111 11303 5614 8144 -423 67 312 O ATOM 2957 N TRP B 112 22.785 -47.526 85.017 1.00 50.52 N ANISOU 2957 N TRP B 112 9192 4126 5878 -18 -24 454 N ATOM 2958 CA TRP B 112 24.200 -47.188 84.941 1.00 48.48 C ANISOU 2958 CA TRP B 112 8925 3966 5529 201 -145 423 C ATOM 2959 C TRP B 112 24.959 -48.488 85.062 1.00 53.36 C ANISOU 2959 C TRP B 112 9763 4382 6130 332 -163 442 C ATOM 2960 O TRP B 112 24.917 -49.170 86.107 1.00 52.72 O ANISOU 2960 O TRP B 112 9893 4147 5992 380 -108 558 O ATOM 2961 CB TRP B 112 24.610 -46.190 86.031 1.00 45.53 C ANISOU 2961 CB TRP B 112 8524 3730 5046 309 -166 498 C ATOM 2962 CG TRP B 112 26.030 -45.741 85.887 1.00 44.59 C ANISOU 2962 CG TRP B 112 8342 3724 4878 511 -303 447 C ATOM 2963 CD1 TRP B 112 27.111 -46.208 86.575 1.00 47.05 C ANISOU 2963 CD1 TRP B 112 8785 3968 5123 713 -385 490 C ATOM 2964 CD2 TRP B 112 26.525 -44.747 84.979 1.00 43.65 C ANISOU 2964 CD2 TRP B 112 8001 3792 4793 528 -373 342 C ATOM 2965 NE1 TRP B 112 28.245 -45.545 86.178 1.00 46.63 N ANISOU 2965 NE1 TRP B 112 8573 4058 5087 848 -500 408 N ATOM 2966 CE2 TRP B 112 27.912 -44.626 85.211 1.00 47.60 C ANISOU 2966 CE2 TRP B 112 8486 4335 5265 732 -477 320 C ATOM 2967 CE3 TRP B 112 25.912 -43.862 84.070 1.00 44.00 C ANISOU 2967 CE3 TRP B 112 7860 3971 4888 394 -359 272 C ATOM 2968 CZ2 TRP B 112 28.709 -43.711 84.508 1.00 46.52 C ANISOU 2968 CZ2 TRP B 112 8150 4361 5164 786 -535 225 C ATOM 2969 CZ3 TRP B 112 26.697 -42.943 83.394 1.00 44.73 C ANISOU 2969 CZ3 TRP B 112 7792 4220 4984 459 -423 191 C ATOM 2970 CH2 TRP B 112 28.079 -42.885 83.598 1.00 45.44 C ANISOU 2970 CH2 TRP B 112 7865 4341 5058 643 -494 166 C ATOM 2971 N LEU B 113 25.650 -48.834 83.973 1.00 49.94 N ANISOU 2971 N LEU B 113 9297 3937 5740 395 -229 329 N ATOM 2972 CA LEU B 113 26.337 -50.109 83.840 1.00 49.64 C ANISOU 2972 CA LEU B 113 9449 3693 5718 516 -239 319 C ATOM 2973 C LEU B 113 27.856 -50.054 83.982 1.00 55.46 C ANISOU 2973 C LEU B 113 10174 4474 6423 781 -340 301 C ATOM 2974 O LEU B 113 28.505 -51.093 83.843 1.00 56.22 O ANISOU 2974 O LEU B 113 10410 4399 6550 909 -353 284 O ATOM 2975 CB LEU B 113 25.936 -50.731 82.488 1.00 49.29 C ANISOU 2975 CB LEU B 113 9409 3558 5760 390 -219 190 C ATOM 2976 CG LEU B 113 24.430 -50.984 82.261 1.00 53.64 C ANISOU 2976 CG LEU B 113 9964 4030 6388 122 -145 187 C ATOM 2977 CD1 LEU B 113 24.169 -51.422 80.819 1.00 53.43 C ANISOU 2977 CD1 LEU B 113 9927 3951 6424 13 -179 33 C ATOM 2978 CD2 LEU B 113 23.878 -52.035 83.249 1.00 55.79 C ANISOU 2978 CD2 LEU B 113 10457 4059 6682 68 -37 308 C ATOM 2979 N PHE B 114 28.410 -48.888 84.340 1.00 52.45 N ANISOU 2979 N PHE B 114 9628 4303 5996 864 -412 306 N ATOM 2980 CA PHE B 114 29.846 -48.633 84.407 1.00 53.82 C ANISOU 2980 CA PHE B 114 9716 4552 6179 1095 -520 268 C ATOM 2981 C PHE B 114 30.480 -48.579 85.816 1.00 58.62 C ANISOU 2981 C PHE B 114 10414 5149 6708 1272 -623 380 C ATOM 2982 O PHE B 114 31.696 -48.353 85.935 1.00 58.05 O ANISOU 2982 O PHE B 114 10245 5141 6670 1467 -742 343 O ATOM 2983 CB PHE B 114 30.148 -47.320 83.663 1.00 57.15 C ANISOU 2983 CB PHE B 114 9873 5215 6628 1060 -539 169 C ATOM 2984 CG PHE B 114 29.528 -47.126 82.299 1.00 59.54 C ANISOU 2984 CG PHE B 114 10095 5558 6968 893 -466 66 C ATOM 2985 CD1 PHE B 114 30.035 -47.788 81.186 1.00 64.18 C ANISOU 2985 CD1 PHE B 114 10710 6065 7610 937 -435 -44 C ATOM 2986 CD2 PHE B 114 28.466 -46.248 82.120 1.00 61.60 C ANISOU 2986 CD2 PHE B 114 10261 5939 7205 704 -436 73 C ATOM 2987 CE1 PHE B 114 29.491 -47.567 79.917 1.00 65.84 C ANISOU 2987 CE1 PHE B 114 10882 6314 7820 791 -387 -144 C ATOM 2988 CE2 PHE B 114 27.913 -46.036 80.855 1.00 64.99 C ANISOU 2988 CE2 PHE B 114 10630 6407 7656 566 -407 -22 C ATOM 2989 CZ PHE B 114 28.449 -46.675 79.758 1.00 63.88 C ANISOU 2989 CZ PHE B 114 10542 6188 7539 609 -389 -129 C ATOM 2990 N GLY B 115 29.678 -48.766 86.863 1.00 55.60 N ANISOU 2990 N GLY B 115 10216 4685 6226 1203 -580 509 N ATOM 2991 CA GLY B 115 30.197 -48.718 88.223 1.00 55.66 C ANISOU 2991 CA GLY B 115 10365 4669 6115 1365 -684 620 C ATOM 2992 C GLY B 115 30.445 -47.323 88.764 1.00 62.83 C ANISOU 2992 C GLY B 115 11113 5804 6955 1382 -767 611 C ATOM 2993 O GLY B 115 30.188 -46.325 88.087 1.00 62.41 O ANISOU 2993 O GLY B 115 10829 5928 6956 1264 -731 526 O ATOM 2994 N HIS B 116 30.922 -47.265 90.014 1.00 62.39 N ANISOU 2994 N HIS B 116 11209 5726 6770 1530 -887 701 N ATOM 2995 CA HIS B 116 31.141 -46.074 90.822 1.00 63.54 C ANISOU 2995 CA HIS B 116 11286 6043 6813 1560 -984 708 C ATOM 2996 C HIS B 116 32.226 -45.111 90.319 1.00 65.74 C ANISOU 2996 C HIS B 116 11257 6520 7202 1648 -1129 577 C ATOM 2997 O HIS B 116 32.012 -43.900 90.377 1.00 65.73 O ANISOU 2997 O HIS B 116 11104 6691 7180 1556 -1120 536 O ATOM 2998 CB HIS B 116 31.412 -46.454 92.291 1.00 66.08 C ANISOU 2998 CB HIS B 116 11910 6253 6943 1713 -1098 838 C ATOM 2999 CG HIS B 116 31.574 -45.248 93.177 1.00 71.35 C ANISOU 2999 CG HIS B 116 12550 7081 7480 1734 -1200 837 C ATOM 3000 ND1 HIS B 116 32.820 -44.877 93.684 1.00 73.91 N ANISOU 3000 ND1 HIS B 116 12819 7478 7786 1939 -1465 796 N ATOM 3001 CD2 HIS B 116 30.663 -44.311 93.536 1.00 73.93 C ANISOU 3001 CD2 HIS B 116 12866 7508 7717 1571 -1072 851 C ATOM 3002 CE1 HIS B 116 32.612 -43.771 94.378 1.00 73.69 C ANISOU 3002 CE1 HIS B 116 12785 7580 7634 1888 -1494 790 C ATOM 3003 NE2 HIS B 116 31.331 -43.389 94.313 1.00 74.27 N ANISOU 3003 NE2 HIS B 116 12888 7673 7658 1673 -1252 823 N ATOM 3004 N ALA B 117 33.390 -45.617 89.884 1.00 61.60 N ANISOU 3004 N ALA B 117 10642 5961 6803 1826 -1251 512 N ATOM 3005 CA ALA B 117 34.484 -44.757 89.399 1.00 60.65 C ANISOU 3005 CA ALA B 117 10212 6010 6821 1908 -1365 383 C ATOM 3006 C ALA B 117 34.049 -43.812 88.254 1.00 62.09 C ANISOU 3006 C ALA B 117 10151 6349 7092 1718 -1216 283 C ATOM 3007 O ALA B 117 34.270 -42.603 88.351 1.00 60.97 O ANISOU 3007 O ALA B 117 9830 6375 6961 1682 -1260 230 O ATOM 3008 CB ALA B 117 35.678 -45.603 88.969 1.00 61.22 C ANISOU 3008 CB ALA B 117 10217 5991 7052 2117 -1463 326 C ATOM 3009 N LEU B 118 33.376 -44.376 87.215 1.00 57.47 N ANISOU 3009 N LEU B 118 9588 5693 6554 1595 -1049 261 N ATOM 3010 CA LEU B 118 32.896 -43.683 86.018 1.00 56.28 C ANISOU 3010 CA LEU B 118 9263 5656 6466 1424 -918 174 C ATOM 3011 C LEU B 118 31.609 -42.881 86.247 1.00 61.87 C ANISOU 3011 C LEU B 118 9985 6443 7079 1224 -831 224 C ATOM 3012 O LEU B 118 31.325 -41.962 85.471 1.00 62.17 O ANISOU 3012 O LEU B 118 9858 6609 7155 1108 -770 160 O ATOM 3013 CB LEU B 118 32.755 -44.648 84.820 1.00 55.33 C ANISOU 3013 CB LEU B 118 9183 5418 6424 1391 -809 117 C ATOM 3014 CG LEU B 118 34.038 -45.363 84.353 1.00 58.68 C ANISOU 3014 CG LEU B 118 9554 5767 6975 1587 -851 40 C ATOM 3015 CD1 LEU B 118 33.732 -46.381 83.280 1.00 59.14 C ANISOU 3015 CD1 LEU B 118 9715 5681 7075 1541 -729 -12 C ATOM 3016 CD2 LEU B 118 35.078 -44.400 83.831 1.00 58.47 C ANISOU 3016 CD2 LEU B 118 9252 5901 7061 1645 -870 -69 C ATOM 3017 N CYS B 119 30.849 -43.201 87.316 1.00 59.29 N ANISOU 3017 N CYS B 119 9859 6035 6632 1194 -818 339 N ATOM 3018 CA CYS B 119 29.635 -42.469 87.705 1.00 59.74 C ANISOU 3018 CA CYS B 119 9930 6153 6614 1024 -720 391 C ATOM 3019 C CYS B 119 30.048 -41.061 88.169 1.00 62.07 C ANISOU 3019 C CYS B 119 10081 6628 6876 1048 -796 359 C ATOM 3020 O CYS B 119 29.286 -40.112 88.035 1.00 61.49 O ANISOU 3020 O CYS B 119 9912 6655 6796 916 -719 350 O ATOM 3021 CB CYS B 119 28.868 -43.228 88.788 1.00 60.87 C ANISOU 3021 CB CYS B 119 10344 6143 6643 1003 -658 521 C ATOM 3022 SG CYS B 119 27.413 -42.361 89.452 1.00 65.52 S ANISOU 3022 SG CYS B 119 10952 6789 7153 816 -504 587 S ATOM 3023 N LYS B 120 31.280 -40.928 88.666 1.00 57.36 N ANISOU 3023 N LYS B 120 9456 6063 6277 1221 -958 332 N ATOM 3024 CA LYS B 120 31.819 -39.647 89.082 1.00 56.18 C ANISOU 3024 CA LYS B 120 9164 6066 6114 1248 -1053 282 C ATOM 3025 C LYS B 120 32.500 -38.930 87.940 1.00 59.31 C ANISOU 3025 C LYS B 120 9284 6582 6668 1231 -1051 161 C ATOM 3026 O LYS B 120 32.182 -37.769 87.697 1.00 61.15 O ANISOU 3026 O LYS B 120 9387 6936 6910 1126 -1003 124 O ATOM 3027 CB LYS B 120 32.713 -39.798 90.316 1.00 57.96 C ANISOU 3027 CB LYS B 120 9508 6261 6253 1428 -1251 313 C ATOM 3028 CG LYS B 120 31.843 -39.971 91.541 1.00 57.53 C ANISOU 3028 CG LYS B 120 9742 6124 5992 1402 -1212 435 C ATOM 3029 CD LYS B 120 32.596 -40.256 92.775 1.00 55.61 C ANISOU 3029 CD LYS B 120 9688 5826 5615 1583 -1416 481 C ATOM 3030 CE LYS B 120 32.217 -39.272 93.849 1.00 61.84 C ANISOU 3030 CE LYS B 120 10581 6685 6230 1544 -1436 500 C ATOM 3031 NZ LYS B 120 30.784 -39.297 94.209 1.00 57.65 N ANISOU 3031 NZ LYS B 120 10242 6093 5569 1395 -1202 597 N ATOM 3032 N VAL B 121 33.333 -39.650 87.170 1.00 53.53 N ANISOU 3032 N VAL B 121 8481 5800 6058 1323 -1069 103 N ATOM 3033 CA VAL B 121 34.123 -39.149 86.046 1.00 51.91 C ANISOU 3033 CA VAL B 121 8036 5680 6006 1326 -1036 -13 C ATOM 3034 C VAL B 121 33.288 -38.649 84.857 1.00 53.22 C ANISOU 3034 C VAL B 121 8138 5900 6182 1149 -870 -44 C ATOM 3035 O VAL B 121 33.487 -37.510 84.453 1.00 52.95 O ANISOU 3035 O VAL B 121 7942 5986 6191 1090 -843 -99 O ATOM 3036 CB VAL B 121 35.181 -40.203 85.601 1.00 55.94 C ANISOU 3036 CB VAL B 121 8517 6095 6642 1488 -1072 -64 C ATOM 3037 CG1 VAL B 121 35.962 -39.751 84.361 1.00 55.32 C ANISOU 3037 CG1 VAL B 121 8208 6088 6724 1481 -982 -186 C ATOM 3038 CG2 VAL B 121 36.140 -40.528 86.743 1.00 55.75 C ANISOU 3038 CG2 VAL B 121 8515 6034 6634 1685 -1280 -45 C ATOM 3039 N ILE B 122 32.415 -39.484 84.263 1.00 50.15 N ANISOU 3039 N ILE B 122 7879 5417 5761 1068 -774 -14 N ATOM 3040 CA ILE B 122 31.686 -39.137 83.018 1.00 49.40 C ANISOU 3040 CA ILE B 122 7739 5359 5674 918 -655 -54 C ATOM 3041 C ILE B 122 30.680 -37.958 83.225 1.00 51.38 C ANISOU 3041 C ILE B 122 7941 5714 5866 778 -627 -16 C ATOM 3042 O ILE B 122 30.836 -36.964 82.522 1.00 49.92 O ANISOU 3042 O ILE B 122 7625 5629 5711 728 -593 -68 O ATOM 3043 CB ILE B 122 31.075 -40.381 82.308 1.00 51.63 C ANISOU 3043 CB ILE B 122 8168 5501 5949 870 -591 -52 C ATOM 3044 CG1 ILE B 122 32.217 -41.301 81.826 1.00 51.03 C ANISOU 3044 CG1 ILE B 122 8102 5335 5951 1016 -591 -119 C ATOM 3045 CG2 ILE B 122 30.195 -39.955 81.131 1.00 52.00 C ANISOU 3045 CG2 ILE B 122 8187 5589 5980 710 -514 -90 C ATOM 3046 CD1 ILE B 122 31.841 -42.777 81.492 1.00 57.91 C ANISOU 3046 CD1 ILE B 122 9167 6020 6816 1020 -556 -110 C ATOM 3047 N PRO B 123 29.732 -37.959 84.193 1.00 48.07 N ANISOU 3047 N PRO B 123 7622 5270 5372 723 -628 71 N ATOM 3048 CA PRO B 123 28.895 -36.769 84.390 1.00 46.86 C ANISOU 3048 CA PRO B 123 7399 5216 5191 615 -592 93 C ATOM 3049 C PRO B 123 29.733 -35.503 84.615 1.00 50.68 C ANISOU 3049 C PRO B 123 7744 5823 5692 662 -642 46 C ATOM 3050 O PRO B 123 29.361 -34.415 84.151 1.00 50.80 O ANISOU 3050 O PRO B 123 7656 5924 5723 580 -601 25 O ATOM 3051 CB PRO B 123 28.084 -37.142 85.637 1.00 48.65 C ANISOU 3051 CB PRO B 123 7774 5373 5338 595 -571 189 C ATOM 3052 CG PRO B 123 27.926 -38.591 85.519 1.00 53.42 C ANISOU 3052 CG PRO B 123 8522 5828 5947 609 -552 219 C ATOM 3053 CD PRO B 123 29.314 -39.031 85.120 1.00 49.48 C ANISOU 3053 CD PRO B 123 7992 5317 5492 752 -634 155 C ATOM 3054 N TYR B 124 30.884 -35.653 85.305 1.00 46.43 N ANISOU 3054 N TYR B 124 7197 5282 5162 797 -743 24 N ATOM 3055 CA TYR B 124 31.820 -34.565 85.594 1.00 45.55 C ANISOU 3055 CA TYR B 124 6942 5271 5094 843 -814 -37 C ATOM 3056 C TYR B 124 32.438 -34.007 84.306 1.00 49.18 C ANISOU 3056 C TYR B 124 7227 5790 5668 813 -750 -123 C ATOM 3057 O TYR B 124 32.470 -32.796 84.108 1.00 47.54 O ANISOU 3057 O TYR B 124 6910 5666 5486 751 -722 -155 O ATOM 3058 CB TYR B 124 32.901 -35.035 86.590 1.00 46.66 C ANISOU 3058 CB TYR B 124 7113 5381 5236 1002 -970 -46 C ATOM 3059 CG TYR B 124 34.088 -34.102 86.677 1.00 48.51 C ANISOU 3059 CG TYR B 124 7154 5705 5575 1054 -1062 -139 C ATOM 3060 CD1 TYR B 124 34.031 -32.936 87.440 1.00 50.10 C ANISOU 3060 CD1 TYR B 124 7326 5980 5731 1016 -1118 -154 C ATOM 3061 CD2 TYR B 124 35.250 -34.352 85.950 1.00 48.83 C ANISOU 3061 CD2 TYR B 124 7031 5746 5777 1131 -1074 -223 C ATOM 3062 CE1 TYR B 124 35.104 -32.047 87.478 1.00 49.76 C ANISOU 3062 CE1 TYR B 124 7092 6009 5807 1041 -1201 -251 C ATOM 3063 CE2 TYR B 124 36.324 -33.468 85.979 1.00 48.98 C ANISOU 3063 CE2 TYR B 124 6839 5840 5930 1157 -1139 -317 C ATOM 3064 CZ TYR B 124 36.247 -32.319 86.743 1.00 52.73 C ANISOU 3064 CZ TYR B 124 7284 6386 6364 1107 -1211 -332 C ATOM 3065 OH TYR B 124 37.331 -31.480 86.778 1.00 54.01 O ANISOU 3065 OH TYR B 124 7231 6609 6682 1121 -1282 -435 O ATOM 3066 N LEU B 125 32.930 -34.888 83.434 1.00 47.87 N ANISOU 3066 N LEU B 125 7056 5567 5566 859 -711 -161 N ATOM 3067 CA LEU B 125 33.525 -34.478 82.171 1.00 47.49 C ANISOU 3067 CA LEU B 125 6882 5555 5607 834 -614 -240 C ATOM 3068 C LEU B 125 32.506 -33.813 81.268 1.00 52.11 C ANISOU 3068 C LEU B 125 7494 6176 6131 691 -515 -223 C ATOM 3069 O LEU B 125 32.855 -32.893 80.527 1.00 53.41 O ANISOU 3069 O LEU B 125 7561 6397 6334 647 -442 -267 O ATOM 3070 CB LEU B 125 34.163 -35.677 81.478 1.00 47.56 C ANISOU 3070 CB LEU B 125 6918 5474 5677 922 -575 -285 C ATOM 3071 CG LEU B 125 35.470 -36.191 82.090 1.00 52.16 C ANISOU 3071 CG LEU B 125 7410 6028 6379 1090 -668 -329 C ATOM 3072 CD1 LEU B 125 36.088 -37.222 81.205 1.00 51.49 C ANISOU 3072 CD1 LEU B 125 7333 5855 6377 1171 -587 -388 C ATOM 3073 CD2 LEU B 125 36.461 -35.047 82.363 1.00 55.04 C ANISOU 3073 CD2 LEU B 125 7555 6494 6866 1108 -705 -396 C ATOM 3074 N GLN B 126 31.237 -34.242 81.352 1.00 47.77 N ANISOU 3074 N GLN B 126 7071 5585 5495 618 -514 -156 N ATOM 3075 CA GLN B 126 30.185 -33.662 80.530 1.00 47.07 C ANISOU 3075 CA GLN B 126 6999 5524 5361 494 -459 -138 C ATOM 3076 C GLN B 126 29.866 -32.244 80.981 1.00 50.80 C ANISOU 3076 C GLN B 126 7388 6086 5829 445 -464 -115 C ATOM 3077 O GLN B 126 29.843 -31.350 80.131 1.00 50.98 O ANISOU 3077 O GLN B 126 7360 6154 5858 393 -413 -137 O ATOM 3078 CB GLN B 126 28.957 -34.571 80.483 1.00 48.06 C ANISOU 3078 CB GLN B 126 7247 5572 5439 428 -467 -88 C ATOM 3079 CG GLN B 126 28.116 -34.432 79.215 1.00 51.47 C ANISOU 3079 CG GLN B 126 7710 6002 5845 325 -441 -102 C ATOM 3080 CD GLN B 126 27.121 -33.307 79.279 1.00 69.97 C ANISOU 3080 CD GLN B 126 9993 8412 8179 240 -452 -58 C ATOM 3081 OE1 GLN B 126 26.996 -32.512 78.347 1.00 75.41 O ANISOU 3081 OE1 GLN B 126 10659 9145 8849 200 -440 -76 O ATOM 3082 NE2 GLN B 126 26.400 -33.199 80.377 1.00 50.96 N ANISOU 3082 NE2 GLN B 126 7573 6005 5785 217 -464 1 N ATOM 3083 N ALA B 127 29.693 -32.023 82.319 1.00 45.23 N ANISOU 3083 N ALA B 127 6690 5393 5103 469 -518 -75 N ATOM 3084 CA ALA B 127 29.468 -30.708 82.907 1.00 43.32 C ANISOU 3084 CA ALA B 127 6385 5220 4854 436 -520 -65 C ATOM 3085 C ALA B 127 30.650 -29.765 82.600 1.00 47.76 C ANISOU 3085 C ALA B 127 6820 5840 5488 459 -517 -137 C ATOM 3086 O ALA B 127 30.430 -28.608 82.249 1.00 48.16 O ANISOU 3086 O ALA B 127 6816 5933 5551 398 -472 -143 O ATOM 3087 CB ALA B 127 29.255 -30.828 84.404 1.00 43.70 C ANISOU 3087 CB ALA B 127 6505 5253 4845 476 -574 -24 C ATOM 3088 N VAL B 128 31.892 -30.268 82.672 1.00 44.53 N ANISOU 3088 N VAL B 128 6355 5419 5144 546 -555 -194 N ATOM 3089 CA VAL B 128 33.108 -29.506 82.328 1.00 44.02 C ANISOU 3089 CA VAL B 128 6138 5396 5192 562 -534 -276 C ATOM 3090 C VAL B 128 33.007 -29.023 80.863 1.00 47.60 C ANISOU 3090 C VAL B 128 6573 5855 5660 484 -393 -290 C ATOM 3091 O VAL B 128 33.260 -27.845 80.601 1.00 48.60 O ANISOU 3091 O VAL B 128 6622 6016 5829 429 -338 -313 O ATOM 3092 CB VAL B 128 34.416 -30.327 82.601 1.00 47.41 C ANISOU 3092 CB VAL B 128 6488 5800 5724 683 -601 -338 C ATOM 3093 CG1 VAL B 128 35.637 -29.713 81.914 1.00 46.85 C ANISOU 3093 CG1 VAL B 128 6232 5756 5813 683 -528 -431 C ATOM 3094 CG2 VAL B 128 34.670 -30.470 84.098 1.00 47.22 C ANISOU 3094 CG2 VAL B 128 6488 5778 5675 765 -772 -329 C ATOM 3095 N SER B 129 32.579 -29.908 79.936 1.00 42.01 N ANISOU 3095 N SER B 129 5962 5098 4900 476 -339 -274 N ATOM 3096 CA SER B 129 32.478 -29.567 78.517 1.00 42.00 C ANISOU 3096 CA SER B 129 5997 5089 4871 414 -218 -287 C ATOM 3097 C SER B 129 31.406 -28.517 78.224 1.00 47.50 C ANISOU 3097 C SER B 129 6739 5814 5496 322 -210 -229 C ATOM 3098 O SER B 129 31.588 -27.733 77.292 1.00 49.17 O ANISOU 3098 O SER B 129 6957 6030 5697 277 -118 -239 O ATOM 3099 CB SER B 129 32.323 -30.816 77.638 1.00 44.92 C ANISOU 3099 CB SER B 129 6487 5393 5190 433 -183 -299 C ATOM 3100 OG SER B 129 31.000 -31.321 77.643 1.00 53.05 O ANISOU 3100 OG SER B 129 7636 6394 6126 384 -251 -240 O ATOM 3101 N VAL B 130 30.336 -28.446 79.046 1.00 43.20 N ANISOU 3101 N VAL B 130 6223 5281 4910 300 -295 -169 N ATOM 3102 CA VAL B 130 29.264 -27.449 78.928 1.00 42.18 C ANISOU 3102 CA VAL B 130 6109 5173 4743 233 -299 -116 C ATOM 3103 C VAL B 130 29.832 -26.076 79.374 1.00 45.83 C ANISOU 3103 C VAL B 130 6479 5673 5262 224 -268 -136 C ATOM 3104 O VAL B 130 29.596 -25.045 78.724 1.00 45.98 O ANISOU 3104 O VAL B 130 6504 5694 5272 177 -217 -118 O ATOM 3105 CB VAL B 130 28.035 -27.862 79.785 1.00 46.26 C ANISOU 3105 CB VAL B 130 6660 5682 5237 219 -367 -58 C ATOM 3106 CG1 VAL B 130 26.946 -26.795 79.768 1.00 45.92 C ANISOU 3106 CG1 VAL B 130 6598 5657 5191 167 -368 -9 C ATOM 3107 CG2 VAL B 130 27.470 -29.200 79.330 1.00 46.26 C ANISOU 3107 CG2 VAL B 130 6745 5628 5204 208 -395 -46 C ATOM 3108 N SER B 131 30.562 -26.077 80.499 1.00 39.96 N ANISOU 3108 N SER B 131 5663 4947 4571 270 -313 -174 N ATOM 3109 CA SER B 131 31.186 -24.893 81.104 1.00 37.45 C ANISOU 3109 CA SER B 131 5254 4656 4318 258 -312 -214 C ATOM 3110 C SER B 131 32.237 -24.299 80.143 1.00 38.94 C ANISOU 3110 C SER B 131 5366 4838 4589 229 -207 -268 C ATOM 3111 O SER B 131 32.193 -23.121 79.859 1.00 37.24 O ANISOU 3111 O SER B 131 5137 4618 4395 171 -145 -263 O ATOM 3112 CB SER B 131 31.774 -25.267 82.463 1.00 37.96 C ANISOU 3112 CB SER B 131 5282 4733 4406 324 -420 -253 C ATOM 3113 OG SER B 131 32.657 -24.292 82.973 1.00 49.33 O ANISOU 3113 OG SER B 131 6622 6194 5928 314 -444 -320 O ATOM 3114 N VAL B 132 33.116 -25.134 79.585 1.00 38.84 N ANISOU 3114 N VAL B 132 5320 4812 4627 267 -165 -314 N ATOM 3115 CA VAL B 132 34.139 -24.748 78.602 1.00 38.93 C ANISOU 3115 CA VAL B 132 5263 4805 4725 240 -20 -368 C ATOM 3116 C VAL B 132 33.444 -24.067 77.410 1.00 42.78 C ANISOU 3116 C VAL B 132 5877 5265 5114 168 92 -309 C ATOM 3117 O VAL B 132 33.861 -22.980 77.017 1.00 43.01 O ANISOU 3117 O VAL B 132 5874 5275 5191 110 197 -320 O ATOM 3118 CB VAL B 132 35.017 -25.962 78.155 1.00 42.78 C ANISOU 3118 CB VAL B 132 5714 5270 5271 310 24 -423 C ATOM 3119 CG1 VAL B 132 35.880 -25.614 76.944 1.00 43.72 C ANISOU 3119 CG1 VAL B 132 5798 5356 5459 273 229 -470 C ATOM 3120 CG2 VAL B 132 35.894 -26.468 79.283 1.00 41.79 C ANISOU 3120 CG2 VAL B 132 5446 5162 5270 395 -99 -485 C ATOM 3121 N ALA B 133 32.358 -24.695 76.890 1.00 39.85 N ANISOU 3121 N ALA B 133 5653 4881 4608 170 52 -248 N ATOM 3122 CA ALA B 133 31.546 -24.264 75.746 1.00 39.26 C ANISOU 3122 CA ALA B 133 5727 4777 4414 123 98 -188 C ATOM 3123 C ALA B 133 30.922 -22.883 75.932 1.00 44.45 C ANISOU 3123 C ALA B 133 6387 5436 5066 79 85 -134 C ATOM 3124 O ALA B 133 31.082 -22.023 75.061 1.00 44.98 O ANISOU 3124 O ALA B 133 6521 5465 5103 39 187 -112 O ATOM 3125 CB ALA B 133 30.484 -25.313 75.417 1.00 39.20 C ANISOU 3125 CB ALA B 133 5839 4759 4297 137 0 -150 C ATOM 3126 N VAL B 134 30.243 -22.672 77.075 1.00 41.33 N ANISOU 3126 N VAL B 134 5933 5072 4698 91 -25 -114 N ATOM 3127 CA VAL B 134 29.606 -21.432 77.514 1.00 41.05 C ANISOU 3127 CA VAL B 134 5886 5033 4678 66 -43 -74 C ATOM 3128 C VAL B 134 30.649 -20.311 77.756 1.00 44.98 C ANISOU 3128 C VAL B 134 6305 5513 5273 31 47 -124 C ATOM 3129 O VAL B 134 30.422 -19.175 77.341 1.00 45.95 O ANISOU 3129 O VAL B 134 6475 5594 5391 -6 107 -88 O ATOM 3130 CB VAL B 134 28.747 -21.758 78.771 1.00 46.28 C ANISOU 3130 CB VAL B 134 6512 5726 5345 96 -152 -59 C ATOM 3131 CG1 VAL B 134 28.117 -20.533 79.418 1.00 46.58 C ANISOU 3131 CG1 VAL B 134 6500 5765 5435 87 -154 -68 C ATOM 3132 CG2 VAL B 134 27.682 -22.746 78.416 1.00 46.71 C ANISOU 3132 CG2 VAL B 134 6635 5774 5338 97 -215 9 C ATOM 3133 N LEU B 135 31.763 -20.619 78.438 1.00 40.77 N ANISOU 3133 N LEU B 135 5650 5002 4838 42 46 -207 N ATOM 3134 CA LEU B 135 32.810 -19.647 78.702 1.00 41.42 C ANISOU 3134 CA LEU B 135 5626 5065 5047 -4 115 -274 C ATOM 3135 C LEU B 135 33.546 -19.318 77.408 1.00 44.96 C ANISOU 3135 C LEU B 135 6094 5462 5526 -55 296 -280 C ATOM 3136 O LEU B 135 34.002 -18.199 77.262 1.00 45.10 O ANISOU 3136 O LEU B 135 6082 5433 5622 -121 395 -297 O ATOM 3137 CB LEU B 135 33.804 -20.129 79.779 1.00 42.43 C ANISOU 3137 CB LEU B 135 5604 5231 5287 30 27 -370 C ATOM 3138 CG LEU B 135 33.350 -20.110 81.249 1.00 47.11 C ANISOU 3138 CG LEU B 135 6194 5855 5850 68 -132 -381 C ATOM 3139 CD1 LEU B 135 34.461 -20.637 82.159 1.00 47.21 C ANISOU 3139 CD1 LEU B 135 6081 5898 5960 115 -244 -476 C ATOM 3140 CD2 LEU B 135 32.943 -18.714 81.694 1.00 46.79 C ANISOU 3140 CD2 LEU B 135 6175 5785 5817 15 -120 -380 C ATOM 3141 N THR B 136 33.648 -20.268 76.461 1.00 42.48 N ANISOU 3141 N THR B 136 5852 5145 5146 -30 356 -267 N ATOM 3142 CA THR B 136 34.283 -19.991 75.168 1.00 42.27 C ANISOU 3142 CA THR B 136 5890 5058 5113 -75 559 -268 C ATOM 3143 C THR B 136 33.417 -18.992 74.407 1.00 46.30 C ANISOU 3143 C THR B 136 6583 5512 5497 -116 604 -171 C ATOM 3144 O THR B 136 33.952 -18.006 73.900 1.00 44.77 O ANISOU 3144 O THR B 136 6413 5250 5346 -180 764 -166 O ATOM 3145 CB THR B 136 34.572 -21.296 74.362 1.00 42.36 C ANISOU 3145 CB THR B 136 5963 5070 5063 -28 615 -288 C ATOM 3146 OG1 THR B 136 35.585 -22.037 75.048 1.00 42.16 O ANISOU 3146 OG1 THR B 136 5745 5077 5195 17 594 -383 O ATOM 3147 CG2 THR B 136 35.050 -21.018 72.928 1.00 32.18 C ANISOU 3147 CG2 THR B 136 4806 3706 3713 -72 847 -278 C ATOM 3148 N LEU B 137 32.080 -19.244 74.349 1.00 44.45 N ANISOU 3148 N LEU B 137 6469 5296 5124 -76 459 -93 N ATOM 3149 CA LEU B 137 31.117 -18.387 73.651 1.00 44.93 C ANISOU 3149 CA LEU B 137 6699 5303 5068 -87 450 5 C ATOM 3150 C LEU B 137 31.048 -17.001 74.263 1.00 53.40 C ANISOU 3150 C LEU B 137 7723 6339 6229 -121 466 21 C ATOM 3151 O LEU B 137 30.992 -16.009 73.523 1.00 56.02 O ANISOU 3151 O LEU B 137 8181 6588 6517 -152 562 80 O ATOM 3152 CB LEU B 137 29.727 -19.038 73.526 1.00 44.55 C ANISOU 3152 CB LEU B 137 6740 5286 4901 -35 271 66 C ATOM 3153 CG LEU B 137 29.635 -20.283 72.607 1.00 48.12 C ANISOU 3153 CG LEU B 137 7310 5742 5230 -14 253 58 C ATOM 3154 CD1 LEU B 137 28.250 -20.870 72.620 1.00 47.03 C ANISOU 3154 CD1 LEU B 137 7218 5630 5021 18 58 103 C ATOM 3155 CD2 LEU B 137 30.066 -19.962 71.163 1.00 50.42 C ANISOU 3155 CD2 LEU B 137 7806 5958 5391 -38 401 85 C ATOM 3156 N SER B 138 31.130 -16.930 75.605 1.00 48.51 N ANISOU 3156 N SER B 138 6940 5767 5724 -114 382 -36 N ATOM 3157 CA SER B 138 31.164 -15.686 76.371 1.00 46.85 C ANISOU 3157 CA SER B 138 6672 5519 5608 -147 390 -51 C ATOM 3158 C SER B 138 32.392 -14.862 76.013 1.00 53.32 C ANISOU 3158 C SER B 138 7453 6268 6538 -232 567 -99 C ATOM 3159 O SER B 138 32.260 -13.663 75.830 1.00 53.44 O ANISOU 3159 O SER B 138 7532 6197 6574 -274 637 -65 O ATOM 3160 CB SER B 138 31.172 -15.989 77.866 1.00 44.57 C ANISOU 3160 CB SER B 138 6245 5297 5393 -121 266 -121 C ATOM 3161 OG SER B 138 29.933 -16.561 78.234 1.00 42.35 O ANISOU 3161 OG SER B 138 6005 5058 5027 -57 141 -67 O ATOM 3162 N PHE B 139 33.581 -15.500 75.911 1.00 52.87 N ANISOU 3162 N PHE B 139 7282 6235 6570 -256 647 -181 N ATOM 3163 CA PHE B 139 34.853 -14.836 75.583 1.00 53.84 C ANISOU 3163 CA PHE B 139 7320 6291 6844 -348 836 -245 C ATOM 3164 C PHE B 139 34.930 -14.361 74.146 1.00 55.98 C ANISOU 3164 C PHE B 139 7778 6464 7028 -394 1048 -167 C ATOM 3165 O PHE B 139 35.585 -13.350 73.896 1.00 55.12 O ANISOU 3165 O PHE B 139 7660 6260 7022 -486 1217 -180 O ATOM 3166 CB PHE B 139 36.054 -15.710 75.943 1.00 57.10 C ANISOU 3166 CB PHE B 139 7523 6761 7409 -344 846 -362 C ATOM 3167 CG PHE B 139 36.437 -15.674 77.404 1.00 61.37 C ANISOU 3167 CG PHE B 139 7870 7357 8092 -336 676 -462 C ATOM 3168 CD1 PHE B 139 35.465 -15.533 78.398 1.00 65.55 C ANISOU 3168 CD1 PHE B 139 8447 7923 8534 -288 488 -436 C ATOM 3169 CD2 PHE B 139 37.763 -15.827 77.795 1.00 66.53 C ANISOU 3169 CD2 PHE B 139 8294 8021 8963 -368 697 -586 C ATOM 3170 CE1 PHE B 139 35.815 -15.515 79.749 1.00 67.27 C ANISOU 3170 CE1 PHE B 139 8534 8184 8843 -275 329 -529 C ATOM 3171 CE2 PHE B 139 38.113 -15.826 79.156 1.00 70.46 C ANISOU 3171 CE2 PHE B 139 8637 8567 9568 -349 498 -682 C ATOM 3172 CZ PHE B 139 37.134 -15.669 80.121 1.00 68.23 C ANISOU 3172 CZ PHE B 139 8451 8317 9157 -303 316 -650 C ATOM 3173 N ILE B 140 34.237 -15.055 73.210 1.00 52.42 N ANISOU 3173 N ILE B 140 7515 6023 6379 -335 1036 -87 N ATOM 3174 CA ILE B 140 34.166 -14.639 71.810 1.00 52.71 C ANISOU 3174 CA ILE B 140 7796 5961 6272 -362 1209 1 C ATOM 3175 C ILE B 140 33.348 -13.347 71.747 1.00 56.22 C ANISOU 3175 C ILE B 140 8383 6320 6659 -372 1178 99 C ATOM 3176 O ILE B 140 33.793 -12.377 71.126 1.00 56.97 O ANISOU 3176 O ILE B 140 8589 6294 6765 -442 1372 137 O ATOM 3177 CB ILE B 140 33.586 -15.731 70.858 1.00 56.10 C ANISOU 3177 CB ILE B 140 8413 6418 6484 -292 1162 49 C ATOM 3178 CG1 ILE B 140 34.461 -16.993 70.832 1.00 56.53 C ANISOU 3178 CG1 ILE B 140 8345 6531 6602 -276 1225 -50 C ATOM 3179 CG2 ILE B 140 33.442 -15.177 69.435 1.00 56.46 C ANISOU 3179 CG2 ILE B 140 8763 6349 6341 -313 1319 147 C ATOM 3180 CD1 ILE B 140 33.730 -18.327 70.410 1.00 56.99 C ANISOU 3180 CD1 ILE B 140 8522 6645 6487 -195 1085 -36 C ATOM 3181 N ALA B 141 32.171 -13.335 72.429 1.00 51.33 N ANISOU 3181 N ALA B 141 7754 5751 5997 -300 948 137 N ATOM 3182 CA ALA B 141 31.223 -12.212 72.497 1.00 50.04 C ANISOU 3182 CA ALA B 141 7701 5514 5797 -277 881 226 C ATOM 3183 C ALA B 141 31.908 -10.967 73.054 1.00 52.30 C ANISOU 3183 C ALA B 141 7910 5712 6251 -362 1005 184 C ATOM 3184 O ALA B 141 31.782 -9.884 72.480 1.00 50.95 O ANISOU 3184 O ALA B 141 7901 5409 6048 -387 1106 263 O ATOM 3185 CB ALA B 141 30.017 -12.593 73.358 1.00 50.33 C ANISOU 3185 CB ALA B 141 7664 5637 5822 -190 642 238 C ATOM 3186 N LEU B 142 32.674 -11.156 74.143 1.00 48.88 N ANISOU 3186 N LEU B 142 7239 5339 5994 -406 991 57 N ATOM 3187 CA LEU B 142 33.453 -10.145 74.850 1.00 48.96 C ANISOU 3187 CA LEU B 142 7129 5281 6194 -500 1073 -24 C ATOM 3188 C LEU B 142 34.561 -9.545 73.951 1.00 55.17 C ANISOU 3188 C LEU B 142 7955 5946 7060 -617 1346 -30 C ATOM 3189 O LEU B 142 34.796 -8.342 73.992 1.00 55.19 O ANISOU 3189 O LEU B 142 7999 5821 7151 -696 1456 -24 O ATOM 3190 CB LEU B 142 34.044 -10.804 76.112 1.00 48.68 C ANISOU 3190 CB LEU B 142 6843 5358 6296 -502 949 -164 C ATOM 3191 CG LEU B 142 34.802 -9.920 77.096 1.00 52.83 C ANISOU 3191 CG LEU B 142 7216 5836 7022 -591 955 -281 C ATOM 3192 CD1 LEU B 142 33.878 -8.922 77.773 1.00 52.11 C ANISOU 3192 CD1 LEU B 142 7210 5686 6901 -567 869 -254 C ATOM 3193 CD2 LEU B 142 35.529 -10.768 78.121 1.00 53.14 C ANISOU 3193 CD2 LEU B 142 7030 5990 7172 -581 821 -415 C ATOM 3194 N ASP B 143 35.217 -10.383 73.129 1.00 54.03 N ANISOU 3194 N ASP B 143 7811 5830 6886 -629 1473 -41 N ATOM 3195 CA ASP B 143 36.270 -9.995 72.182 1.00 53.80 C ANISOU 3195 CA ASP B 143 7828 5690 6924 -737 1775 -44 C ATOM 3196 C ASP B 143 35.655 -9.120 71.085 1.00 58.08 C ANISOU 3196 C ASP B 143 8704 6086 7279 -738 1898 111 C ATOM 3197 O ASP B 143 36.220 -8.075 70.732 1.00 57.76 O ANISOU 3197 O ASP B 143 8728 5894 7323 -845 2117 129 O ATOM 3198 CB ASP B 143 36.900 -11.268 71.587 1.00 55.85 C ANISOU 3198 CB ASP B 143 8036 6024 7159 -713 1864 -88 C ATOM 3199 CG ASP B 143 37.706 -11.103 70.309 1.00 69.50 C ANISOU 3199 CG ASP B 143 9901 7637 8867 -791 2203 -59 C ATOM 3200 OD1 ASP B 143 38.798 -10.499 70.371 1.00 70.50 O ANISOU 3200 OD1 ASP B 143 9881 7684 9224 -915 2421 -133 O ATOM 3201 OD2 ASP B 143 37.260 -11.614 69.254 1.00 75.46 O ANISOU 3201 OD2 ASP B 143 10912 8380 9379 -732 2254 28 O ATOM 3202 N ARG B 144 34.482 -9.558 70.564 1.00 53.53 N ANISOU 3202 N ARG B 144 8339 5546 6453 -619 1741 222 N ATOM 3203 CA ARG B 144 33.728 -8.877 69.513 1.00 52.50 C ANISOU 3203 CA ARG B 144 8550 5291 6108 -581 1781 380 C ATOM 3204 C ARG B 144 33.153 -7.542 69.980 1.00 56.26 C ANISOU 3204 C ARG B 144 9078 5659 6640 -582 1727 437 C ATOM 3205 O ARG B 144 33.178 -6.553 69.236 1.00 55.53 O ANISOU 3205 O ARG B 144 9219 5396 6482 -616 1884 537 O ATOM 3206 CB ARG B 144 32.624 -9.793 68.955 1.00 50.38 C ANISOU 3206 CB ARG B 144 8442 5105 5594 -450 1571 456 C ATOM 3207 CG ARG B 144 33.118 -11.056 68.238 1.00 55.54 C ANISOU 3207 CG ARG B 144 9136 5825 6141 -444 1651 417 C ATOM 3208 CD ARG B 144 33.861 -10.790 66.936 1.00 58.70 C ANISOU 3208 CD ARG B 144 9792 6091 6420 -508 1959 469 C ATOM 3209 NE ARG B 144 35.235 -10.352 67.193 1.00 58.13 N ANISOU 3209 NE ARG B 144 9536 5960 6590 -642 2248 378 N ATOM 3210 CZ ARG B 144 35.958 -9.614 66.362 1.00 71.73 C ANISOU 3210 CZ ARG B 144 11430 7524 8300 -737 2571 422 C ATOM 3211 NH1 ARG B 144 35.459 -9.241 65.187 1.00 60.50 N ANISOU 3211 NH1 ARG B 144 10410 5981 6595 -703 2646 566 N ATOM 3212 NH2 ARG B 144 37.192 -9.257 66.688 1.00 53.98 N ANISOU 3212 NH2 ARG B 144 8958 5229 6324 -868 2821 322 N ATOM 3213 N TRP B 145 32.640 -7.524 71.215 1.00 52.17 N ANISOU 3213 N TRP B 145 8361 5226 6236 -540 1517 373 N ATOM 3214 CA TRP B 145 32.054 -6.357 71.853 1.00 51.15 C ANISOU 3214 CA TRP B 145 8250 5005 6180 -526 1452 401 C ATOM 3215 C TRP B 145 33.114 -5.271 71.990 1.00 55.75 C ANISOU 3215 C TRP B 145 8797 5440 6946 -675 1683 347 C ATOM 3216 O TRP B 145 32.916 -4.149 71.514 1.00 56.30 O ANISOU 3216 O TRP B 145 9069 5334 6990 -693 1789 440 O ATOM 3217 CB TRP B 145 31.477 -6.764 73.210 1.00 49.56 C ANISOU 3217 CB TRP B 145 7829 4938 6062 -462 1220 315 C ATOM 3218 CG TRP B 145 30.534 -5.763 73.771 1.00 50.22 C ANISOU 3218 CG TRP B 145 7966 4943 6172 -401 1124 358 C ATOM 3219 CD1 TRP B 145 29.292 -5.448 73.302 1.00 52.85 C ANISOU 3219 CD1 TRP B 145 8470 5228 6381 -279 1011 488 C ATOM 3220 CD2 TRP B 145 30.795 -4.872 74.859 1.00 50.06 C ANISOU 3220 CD2 TRP B 145 7836 4862 6324 -457 1140 266 C ATOM 3221 NE1 TRP B 145 28.732 -4.465 74.080 1.00 52.20 N ANISOU 3221 NE1 TRP B 145 8373 5065 6395 -244 967 483 N ATOM 3222 CE2 TRP B 145 29.643 -4.072 75.030 1.00 53.65 C ANISOU 3222 CE2 TRP B 145 8404 5232 6747 -356 1053 346 C ATOM 3223 CE3 TRP B 145 31.882 -4.698 75.736 1.00 51.09 C ANISOU 3223 CE3 TRP B 145 7776 4999 6637 -578 1201 112 C ATOM 3224 CZ2 TRP B 145 29.528 -3.139 76.070 1.00 52.72 C ANISOU 3224 CZ2 TRP B 145 8233 5039 6761 -371 1045 273 C ATOM 3225 CZ3 TRP B 145 31.782 -3.748 76.740 1.00 52.61 C ANISOU 3225 CZ3 TRP B 145 7927 5114 6948 -603 1172 39 C ATOM 3226 CH2 TRP B 145 30.625 -2.966 76.888 1.00 53.29 C ANISOU 3226 CH2 TRP B 145 8150 5112 6986 -502 1110 119 C ATOM 3227 N TYR B 146 34.276 -5.620 72.554 1.00 52.11 N ANISOU 3227 N TYR B 146 8086 5036 6676 -783 1767 199 N ATOM 3228 CA TYR B 146 35.373 -4.663 72.656 1.00 51.50 C ANISOU 3228 CA TYR B 146 7938 4818 6811 -946 1990 128 C ATOM 3229 C TYR B 146 35.957 -4.305 71.275 1.00 59.29 C ANISOU 3229 C TYR B 146 9139 5652 7736 -1029 2303 222 C ATOM 3230 O TYR B 146 36.328 -3.164 71.073 1.00 59.84 O ANISOU 3230 O TYR B 146 9304 5536 7896 -1133 2490 248 O ATOM 3231 CB TYR B 146 36.458 -5.145 73.638 1.00 51.07 C ANISOU 3231 CB TYR B 146 7535 4866 7004 -1034 1962 -65 C ATOM 3232 CG TYR B 146 36.106 -4.900 75.092 1.00 51.72 C ANISOU 3232 CG TYR B 146 7463 5007 7180 -1006 1724 -166 C ATOM 3233 CD1 TYR B 146 36.106 -3.611 75.624 1.00 52.81 C ANISOU 3233 CD1 TYR B 146 7627 5001 7437 -1081 1752 -200 C ATOM 3234 CD2 TYR B 146 35.798 -5.959 75.947 1.00 51.97 C ANISOU 3234 CD2 TYR B 146 7345 5225 7175 -907 1485 -231 C ATOM 3235 CE1 TYR B 146 35.775 -3.379 76.958 1.00 52.32 C ANISOU 3235 CE1 TYR B 146 7459 4984 7437 -1052 1546 -301 C ATOM 3236 CE2 TYR B 146 35.472 -5.737 77.287 1.00 52.19 C ANISOU 3236 CE2 TYR B 146 7273 5298 7259 -879 1287 -322 C ATOM 3237 CZ TYR B 146 35.459 -4.444 77.785 1.00 56.49 C ANISOU 3237 CZ TYR B 146 7857 5702 7905 -950 1318 -360 C ATOM 3238 OH TYR B 146 35.146 -4.208 79.100 1.00 52.76 O ANISOU 3238 OH TYR B 146 7317 5263 7466 -921 1136 -458 O ATOM 3239 N ALA B 147 36.008 -5.248 70.318 1.00 57.94 N ANISOU 3239 N ALA B 147 9075 5543 7398 -983 2372 275 N ATOM 3240 CA ALA B 147 36.573 -4.967 68.992 1.00 57.99 C ANISOU 3240 CA ALA B 147 9321 5399 7313 -1057 2695 363 C ATOM 3241 C ALA B 147 35.771 -3.973 68.150 1.00 63.83 C ANISOU 3241 C ALA B 147 10457 5956 7839 -1013 2744 550 C ATOM 3242 O ALA B 147 36.369 -3.198 67.401 1.00 63.64 O ANISOU 3242 O ALA B 147 10616 5742 7824 -1121 3046 611 O ATOM 3243 CB ALA B 147 36.765 -6.260 68.214 1.00 58.23 C ANISOU 3243 CB ALA B 147 9398 5537 7188 -1003 2743 365 C ATOM 3244 N ILE B 148 34.428 -4.008 68.280 1.00 61.63 N ANISOU 3244 N ILE B 148 10305 5728 7384 -852 2449 641 N ATOM 3245 CA ILE B 148 33.452 -3.257 67.488 1.00 61.55 C ANISOU 3245 CA ILE B 148 10667 5573 7148 -756 2403 827 C ATOM 3246 C ILE B 148 32.803 -2.094 68.248 1.00 65.71 C ANISOU 3246 C ILE B 148 11182 5998 7785 -724 2282 853 C ATOM 3247 O ILE B 148 32.743 -0.980 67.724 1.00 67.07 O ANISOU 3247 O ILE B 148 11608 5955 7920 -746 2422 965 O ATOM 3248 CB ILE B 148 32.389 -4.276 66.917 1.00 64.97 C ANISOU 3248 CB ILE B 148 11246 6136 7305 -585 2147 906 C ATOM 3249 CG1 ILE B 148 33.053 -5.291 65.935 1.00 64.70 C ANISOU 3249 CG1 ILE B 148 11317 6148 7118 -618 2314 895 C ATOM 3250 CG2 ILE B 148 31.164 -3.572 66.265 1.00 66.53 C ANISOU 3250 CG2 ILE B 148 11780 6211 7287 -446 1989 1089 C ATOM 3251 CD1 ILE B 148 32.341 -6.684 65.775 1.00 61.24 C ANISOU 3251 CD1 ILE B 148 10860 5900 6511 -495 2054 878 C ATOM 3252 N CYS B 149 32.290 -2.348 69.450 1.00 60.71 N ANISOU 3252 N CYS B 149 10287 5506 7275 -663 2036 756 N ATOM 3253 CA CYS B 149 31.583 -1.322 70.215 1.00 59.20 C ANISOU 3253 CA CYS B 149 10090 5224 7178 -613 1920 770 C ATOM 3254 C CYS B 149 32.487 -0.422 71.053 1.00 63.22 C ANISOU 3254 C CYS B 149 10443 5627 7953 -771 2078 648 C ATOM 3255 O CYS B 149 32.162 0.749 71.248 1.00 63.09 O ANISOU 3255 O CYS B 149 10545 5433 7993 -769 2107 693 O ATOM 3256 CB CYS B 149 30.492 -1.967 71.063 1.00 58.42 C ANISOU 3256 CB CYS B 149 9827 5304 7068 -466 1604 735 C ATOM 3257 SG CYS B 149 29.285 -2.908 70.095 1.00 61.39 S ANISOU 3257 SG CYS B 149 10382 5779 7166 -284 1381 874 S ATOM 3258 N HIS B 150 33.590 -0.960 71.585 1.00 60.06 N ANISOU 3258 N HIS B 150 9770 5326 7726 -903 2159 486 N ATOM 3259 CA HIS B 150 34.508 -0.200 72.441 1.00 59.48 C ANISOU 3259 CA HIS B 150 9509 5165 7926 -1065 2269 340 C ATOM 3260 C HIS B 150 35.967 -0.471 72.054 1.00 64.40 C ANISOU 3260 C HIS B 150 9994 5773 8702 -1245 2529 252 C ATOM 3261 O HIS B 150 36.719 -1.078 72.829 1.00 64.19 O ANISOU 3261 O HIS B 150 9655 5879 8854 -1311 2472 84 O ATOM 3262 CB HIS B 150 34.215 -0.501 73.929 1.00 59.89 C ANISOU 3262 CB HIS B 150 9302 5367 8089 -1019 2013 192 C ATOM 3263 CG HIS B 150 32.819 -0.122 74.319 1.00 62.85 C ANISOU 3263 CG HIS B 150 9800 5728 8353 -854 1816 271 C ATOM 3264 ND1 HIS B 150 31.783 -1.029 74.246 1.00 64.21 N ANISOU 3264 ND1 HIS B 150 9987 6056 8351 -686 1612 341 N ATOM 3265 CD2 HIS B 150 32.315 1.086 74.658 1.00 64.08 C ANISOU 3265 CD2 HIS B 150 10075 5711 8561 -835 1820 297 C ATOM 3266 CE1 HIS B 150 30.697 -0.363 74.587 1.00 63.12 C ANISOU 3266 CE1 HIS B 150 9948 5849 8186 -569 1498 401 C ATOM 3267 NE2 HIS B 150 30.971 0.908 74.861 1.00 63.62 N ANISOU 3267 NE2 HIS B 150 10081 5716 8376 -645 1617 376 N ATOM 3268 N PRO B 151 36.391 -0.079 70.828 1.00 62.10 N ANISOU 3268 N PRO B 151 9936 5318 8341 -1318 2819 365 N ATOM 3269 CA PRO B 151 37.774 -0.366 70.427 1.00 62.34 C ANISOU 3269 CA PRO B 151 9818 5329 8539 -1488 3104 277 C ATOM 3270 C PRO B 151 38.835 0.399 71.212 1.00 70.05 C ANISOU 3270 C PRO B 151 10536 6208 9874 -1690 3227 111 C ATOM 3271 O PRO B 151 38.549 1.406 71.870 1.00 71.21 O ANISOU 3271 O PRO B 151 10706 6235 10114 -1722 3159 87 O ATOM 3272 CB PRO B 151 37.785 -0.015 68.943 1.00 63.48 C ANISOU 3272 CB PRO B 151 10340 5297 8482 -1504 3392 459 C ATOM 3273 CG PRO B 151 36.718 0.990 68.785 1.00 67.15 C ANISOU 3273 CG PRO B 151 11117 5605 8791 -1410 3300 613 C ATOM 3274 CD PRO B 151 35.662 0.646 69.762 1.00 63.10 C ANISOU 3274 CD PRO B 151 10478 5260 8238 -1247 2911 577 C ATOM 3275 N LEU B 152 40.070 -0.119 71.158 1.00 67.28 N ANISOU 3275 N LEU B 152 9921 5907 9737 -1822 3398 -18 N ATOM 3276 CA LEU B 152 41.295 0.459 71.721 1.00 67.31 C ANISOU 3276 CA LEU B 152 9631 5821 10123 -2038 3546 -193 C ATOM 3277 C LEU B 152 41.325 0.572 73.271 1.00 72.07 C ANISOU 3277 C LEU B 152 9939 6521 10922 -2047 3227 -380 C ATOM 3278 O LEU B 152 42.204 1.244 73.809 1.00 72.21 O ANISOU 3278 O LEU B 152 9747 6438 11251 -2228 3301 -529 O ATOM 3279 CB LEU B 152 41.633 1.817 71.050 1.00 67.26 C ANISOU 3279 CB LEU B 152 9845 5509 10201 -2206 3891 -113 C ATOM 3280 CG LEU B 152 41.328 1.972 69.533 1.00 71.84 C ANISOU 3280 CG LEU B 152 10851 5941 10503 -2172 4183 114 C ATOM 3281 CD1 LEU B 152 41.536 3.405 69.075 1.00 72.19 C ANISOU 3281 CD1 LEU B 152 11141 5666 10620 -2322 4475 201 C ATOM 3282 CD2 LEU B 152 42.116 0.972 68.662 1.00 72.93 C ANISOU 3282 CD2 LEU B 152 10923 6157 10630 -2204 4432 106 C ATOM 3283 N LEU B 153 40.438 -0.148 73.986 1.00 69.30 N ANISOU 3283 N LEU B 153 9566 6367 10400 -1863 2881 -385 N ATOM 3284 CA LEU B 153 40.480 -0.214 75.452 1.00 68.75 C ANISOU 3284 CA LEU B 153 9248 6406 10468 -1853 2579 -560 C ATOM 3285 C LEU B 153 41.318 -1.446 75.848 1.00 72.14 C ANISOU 3285 C LEU B 153 9340 7040 11031 -1848 2473 -702 C ATOM 3286 O LEU B 153 42.215 -1.336 76.684 1.00 71.91 O ANISOU 3286 O LEU B 153 9019 7028 11276 -1957 2390 -891 O ATOM 3287 CB LEU B 153 39.075 -0.318 76.091 1.00 68.61 C ANISOU 3287 CB LEU B 153 9389 6477 10203 -1659 2287 -492 C ATOM 3288 CG LEU B 153 38.065 0.804 75.861 1.00 73.01 C ANISOU 3288 CG LEU B 153 10261 6856 10625 -1609 2322 -356 C ATOM 3289 CD1 LEU B 153 36.774 0.490 76.590 1.00 73.21 C ANISOU 3289 CD1 LEU B 153 10354 7002 10459 -1414 2032 -323 C ATOM 3290 CD2 LEU B 153 38.603 2.173 76.323 1.00 74.05 C ANISOU 3290 CD2 LEU B 153 10381 6766 10989 -1783 2433 -452 C ATOM 3291 N PHE B 154 41.028 -2.610 75.228 1.00 68.67 N ANISOU 3291 N PHE B 154 8947 6743 10401 -1716 2465 -613 N ATOM 3292 CA PHE B 154 41.716 -3.883 75.478 1.00 68.96 C ANISOU 3292 CA PHE B 154 8704 6965 10534 -1677 2374 -722 C ATOM 3293 C PHE B 154 42.219 -4.496 74.191 1.00 77.16 C ANISOU 3293 C PHE B 154 9786 7993 11539 -1689 2662 -649 C ATOM 3294 O PHE B 154 41.431 -4.648 73.245 1.00 77.17 O ANISOU 3294 O PHE B 154 10096 7968 11256 -1601 2752 -477 O ATOM 3295 CB PHE B 154 40.794 -4.894 76.219 1.00 69.33 C ANISOU 3295 CB PHE B 154 8757 7214 10370 -1481 2029 -710 C ATOM 3296 CG PHE B 154 40.374 -4.428 77.591 1.00 69.84 C ANISOU 3296 CG PHE B 154 8775 7303 10459 -1460 1753 -801 C ATOM 3297 CD1 PHE B 154 41.237 -4.537 78.676 1.00 72.12 C ANISOU 3297 CD1 PHE B 154 8775 7649 10978 -1520 1584 -995 C ATOM 3298 CD2 PHE B 154 39.143 -3.819 77.788 1.00 71.99 C ANISOU 3298 CD2 PHE B 154 9297 7525 10530 -1378 1666 -698 C ATOM 3299 CE1 PHE B 154 40.871 -4.056 79.935 1.00 73.07 C ANISOU 3299 CE1 PHE B 154 8895 7775 11092 -1505 1339 -1086 C ATOM 3300 CE2 PHE B 154 38.779 -3.328 79.047 1.00 75.17 C ANISOU 3300 CE2 PHE B 154 9677 7931 10953 -1362 1450 -790 C ATOM 3301 CZ PHE B 154 39.645 -3.452 80.113 1.00 73.12 C ANISOU 3301 CZ PHE B 154 9167 7728 10890 -1429 1292 -984 C ATOM 3302 N LYS B 155 43.529 -4.867 74.165 1.00 76.54 N ANISOU 3302 N LYS B 155 9395 7932 11754 -1790 2798 -787 N ATOM 3303 CA LYS B 155 44.194 -5.552 73.040 1.00 77.40 C ANISOU 3303 CA LYS B 155 9491 8037 11881 -1804 3098 -756 C ATOM 3304 C LYS B 155 43.974 -7.060 73.162 1.00 84.28 C ANISOU 3304 C LYS B 155 10287 9115 12620 -1625 2901 -768 C ATOM 3305 O LYS B 155 44.422 -7.667 74.142 1.00 83.46 O ANISOU 3305 O LYS B 155 9878 9140 12693 -1587 2666 -911 O ATOM 3306 CB LYS B 155 45.705 -5.237 72.989 1.00 79.20 C ANISOU 3306 CB LYS B 155 9386 8175 12532 -1996 3357 -909 C ATOM 3307 CG LYS B 155 46.083 -4.267 71.879 1.00 93.68 C ANISOU 3307 CG LYS B 155 11411 9773 14409 -2164 3801 -822 C ATOM 3308 CD LYS B 155 47.381 -3.531 72.195 1.00104.39 C ANISOU 3308 CD LYS B 155 12414 11010 16238 -2393 3997 -993 C ATOM 3309 CE LYS B 155 47.616 -2.345 71.288 1.00110.74 C ANISOU 3309 CE LYS B 155 13438 11549 17090 -2580 4420 -902 C ATOM 3310 NZ LYS B 155 49.054 -1.965 71.236 1.00116.79 N ANISOU 3310 NZ LYS B 155 13837 12202 18338 -2807 4719 -1062 N ATOM 3311 N SER B 156 43.254 -7.651 72.185 1.00 83.67 N ANISOU 3311 N SER B 156 10509 9060 12223 -1512 2978 -618 N ATOM 3312 CA SER B 156 42.961 -9.090 72.135 1.00 84.69 C ANISOU 3312 CA SER B 156 10622 9357 12198 -1348 2823 -614 C ATOM 3313 C SER B 156 43.717 -9.706 70.966 1.00 89.74 C ANISOU 3313 C SER B 156 11277 9961 12860 -1367 3160 -610 C ATOM 3314 O SER B 156 43.317 -9.562 69.807 1.00 89.42 O ANISOU 3314 O SER B 156 11572 9830 12575 -1362 3380 -476 O ATOM 3315 CB SER B 156 41.458 -9.351 72.027 1.00 89.50 C ANISOU 3315 CB SER B 156 11550 10024 12432 -1201 2607 -465 C ATOM 3316 OG SER B 156 40.735 -8.693 73.057 1.00102.16 O ANISOU 3316 OG SER B 156 13158 11639 14020 -1186 2350 -464 O ATOM 3317 N THR B 157 44.853 -10.346 71.290 1.00 87.19 N ANISOU 3317 N THR B 157 10591 9698 12840 -1386 3203 -766 N ATOM 3318 CA THR B 157 45.779 -11.006 70.362 1.00 87.06 C ANISOU 3318 CA THR B 157 10500 9651 12927 -1402 3536 -805 C ATOM 3319 C THR B 157 45.651 -12.535 70.450 1.00 91.67 C ANISOU 3319 C THR B 157 11027 10390 13412 -1223 3364 -836 C ATOM 3320 O THR B 157 45.113 -13.047 71.432 1.00 91.30 O ANISOU 3320 O THR B 157 10902 10476 13313 -1113 2984 -860 O ATOM 3321 CB THR B 157 47.222 -10.563 70.671 1.00 92.25 C ANISOU 3321 CB THR B 157 10744 10244 14062 -1557 3732 -972 C ATOM 3322 OG1 THR B 157 47.573 -10.973 71.996 1.00 90.99 O ANISOU 3322 OG1 THR B 157 10213 10217 14144 -1506 3372 -1121 O ATOM 3323 CG2 THR B 157 47.430 -9.059 70.504 1.00 87.95 C ANISOU 3323 CG2 THR B 157 10261 9515 13639 -1758 3953 -947 C ATOM 3324 N ALA B 158 46.162 -13.257 69.431 1.00 89.05 N ANISOU 3324 N ALA B 158 10750 10028 13057 -1196 3662 -839 N ATOM 3325 CA ALA B 158 46.150 -14.723 69.339 1.00 89.00 C ANISOU 3325 CA ALA B 158 10711 10133 12970 -1034 3568 -874 C ATOM 3326 C ALA B 158 46.915 -15.393 70.490 1.00 93.24 C ANISOU 3326 C ALA B 158 10796 10786 13846 -971 3328 -1037 C ATOM 3327 O ALA B 158 46.515 -16.469 70.945 1.00 92.92 O ANISOU 3327 O ALA B 158 10744 10862 13699 -816 3059 -1045 O ATOM 3328 CB ALA B 158 46.725 -15.160 68.002 1.00 89.74 C ANISOU 3328 CB ALA B 158 10938 10136 13022 -1044 4002 -867 C ATOM 3329 N ARG B 159 48.004 -14.746 70.959 1.00 89.86 N ANISOU 3329 N ARG B 159 10002 10314 13826 -1094 3415 -1165 N ATOM 3330 CA ARG B 159 48.854 -15.204 72.061 1.00 89.68 C ANISOU 3330 CA ARG B 159 9526 10382 14165 -1048 3174 -1331 C ATOM 3331 C ARG B 159 48.076 -15.157 73.380 1.00 92.83 C ANISOU 3331 C ARG B 159 9932 10891 14450 -979 2686 -1323 C ATOM 3332 O ARG B 159 48.100 -16.130 74.142 1.00 93.07 O ANISOU 3332 O ARG B 159 9824 11036 14503 -833 2390 -1377 O ATOM 3333 CB ARG B 159 50.138 -14.351 72.151 1.00 91.35 C ANISOU 3333 CB ARG B 159 9364 10500 14846 -1225 3395 -1470 C ATOM 3334 CG ARG B 159 51.015 -14.375 70.894 1.00107.58 C ANISOU 3334 CG ARG B 159 11376 12435 17064 -1305 3927 -1492 C ATOM 3335 CD ARG B 159 51.822 -15.662 70.783 1.00128.52 C ANISOU 3335 CD ARG B 159 13756 15151 19924 -1164 3974 -1602 C ATOM 3336 NE ARG B 159 52.673 -15.691 69.590 1.00142.05 N ANISOU 3336 NE ARG B 159 15430 16742 21802 -1238 4519 -1632 N ATOM 3337 CZ ARG B 159 52.337 -16.262 68.437 1.00155.10 C ANISOU 3337 CZ ARG B 159 17432 18348 23150 -1172 4812 -1538 C ATOM 3338 NH1 ARG B 159 51.155 -16.853 68.299 1.00142.16 N ANISOU 3338 NH1 ARG B 159 16192 16779 21045 -1039 4591 -1410 N ATOM 3339 NH2 ARG B 159 53.179 -16.246 67.412 1.00139.18 N ANISOU 3339 NH2 ARG B 159 15375 16209 21297 -1245 5332 -1577 N ATOM 3340 N ARG B 160 47.357 -14.031 73.623 1.00 87.33 N ANISOU 3340 N ARG B 160 9427 10144 13611 -1077 2621 -1248 N ATOM 3341 CA ARG B 160 46.512 -13.796 74.800 1.00 85.90 C ANISOU 3341 CA ARG B 160 9308 10041 13289 -1027 2218 -1230 C ATOM 3342 C ARG B 160 45.271 -14.697 74.780 1.00 86.64 C ANISOU 3342 C ARG B 160 9694 10228 12997 -861 2024 -1106 C ATOM 3343 O ARG B 160 44.710 -14.973 75.840 1.00 85.93 O ANISOU 3343 O ARG B 160 9599 10230 12819 -775 1682 -1112 O ATOM 3344 CB ARG B 160 46.087 -12.318 74.883 1.00 86.46 C ANISOU 3344 CB ARG B 160 9524 10004 13321 -1175 2268 -1182 C ATOM 3345 CG ARG B 160 47.150 -11.402 75.461 1.00100.08 C ANISOU 3345 CG ARG B 160 10925 11659 15443 -1337 2297 -1335 C ATOM 3346 CD ARG B 160 46.668 -9.962 75.584 1.00117.72 C ANISOU 3346 CD ARG B 160 13329 13771 17628 -1477 2338 -1288 C ATOM 3347 NE ARG B 160 47.165 -9.106 74.500 1.00131.17 N ANISOU 3347 NE ARG B 160 15092 15300 19448 -1647 2772 -1252 N ATOM 3348 CZ ARG B 160 48.329 -8.460 74.516 1.00146.83 C ANISOU 3348 CZ ARG B 160 16780 17181 21827 -1823 2960 -1385 C ATOM 3349 NH1 ARG B 160 49.147 -8.574 75.557 1.00132.44 N ANISOU 3349 NH1 ARG B 160 14563 15422 20335 -1847 2720 -1573 N ATOM 3350 NH2 ARG B 160 48.690 -7.706 73.487 1.00136.68 N ANISOU 3350 NH2 ARG B 160 15595 15721 20614 -1978 3388 -1331 N ATOM 3351 N ALA B 161 44.835 -15.135 73.573 1.00 81.34 N ANISOU 3351 N ALA B 161 9289 9524 12094 -824 2248 -996 N ATOM 3352 CA ALA B 161 43.676 -16.013 73.387 1.00 80.09 C ANISOU 3352 CA ALA B 161 9406 9437 11588 -685 2091 -885 C ATOM 3353 C ALA B 161 43.951 -17.400 73.985 1.00 82.47 C ANISOU 3353 C ALA B 161 9535 9848 11950 -537 1886 -959 C ATOM 3354 O ALA B 161 43.085 -17.934 74.678 1.00 82.25 O ANISOU 3354 O ALA B 161 9604 9903 11745 -437 1600 -914 O ATOM 3355 CB ALA B 161 43.310 -16.115 71.912 1.00 80.49 C ANISOU 3355 CB ALA B 161 9772 9410 11401 -693 2380 -776 C ATOM 3356 N LEU B 162 45.175 -17.946 73.778 1.00 77.78 N ANISOU 3356 N LEU B 162 8676 9245 11630 -524 2035 -1074 N ATOM 3357 CA LEU B 162 45.602 -19.245 74.314 1.00 77.00 C ANISOU 3357 CA LEU B 162 8391 9228 11636 -373 1858 -1152 C ATOM 3358 C LEU B 162 45.662 -19.245 75.852 1.00 77.77 C ANISOU 3358 C LEU B 162 8288 9410 11851 -324 1467 -1220 C ATOM 3359 O LEU B 162 45.391 -20.272 76.482 1.00 77.09 O ANISOU 3359 O LEU B 162 8205 9397 11687 -179 1220 -1219 O ATOM 3360 CB LEU B 162 46.933 -19.699 73.695 1.00 77.38 C ANISOU 3360 CB LEU B 162 8183 9230 11986 -370 2135 -1264 C ATOM 3361 CG LEU B 162 46.870 -20.118 72.208 1.00 83.48 C ANISOU 3361 CG LEU B 162 9196 9927 12594 -367 2507 -1206 C ATOM 3362 CD1 LEU B 162 48.228 -19.935 71.508 1.00 83.97 C ANISOU 3362 CD1 LEU B 162 9010 9903 12994 -441 2898 -1314 C ATOM 3363 CD2 LEU B 162 46.373 -21.562 72.041 1.00 86.31 C ANISOU 3363 CD2 LEU B 162 9712 10334 12746 -195 2394 -1176 C ATOM 3364 N GLY B 163 45.963 -18.082 76.426 1.00 71.89 N ANISOU 3364 N GLY B 163 7410 8640 11266 -447 1418 -1274 N ATOM 3365 CA GLY B 163 46.021 -17.868 77.866 1.00 70.76 C ANISOU 3365 CA GLY B 163 7118 8559 11210 -423 1057 -1346 C ATOM 3366 C GLY B 163 44.631 -17.836 78.460 1.00 72.63 C ANISOU 3366 C GLY B 163 7651 8843 11103 -371 831 -1233 C ATOM 3367 O GLY B 163 44.411 -18.362 79.557 1.00 73.36 O ANISOU 3367 O GLY B 163 7724 9008 11141 -268 520 -1254 O ATOM 3368 N SER B 164 43.675 -17.232 77.716 1.00 65.96 N ANISOU 3368 N SER B 164 7089 7948 10024 -437 994 -1108 N ATOM 3369 CA SER B 164 42.260 -17.167 78.081 1.00 64.68 C ANISOU 3369 CA SER B 164 7205 7819 9550 -392 831 -991 C ATOM 3370 C SER B 164 41.659 -18.585 78.002 1.00 66.65 C ANISOU 3370 C SER B 164 7579 8137 9609 -244 727 -928 C ATOM 3371 O SER B 164 40.920 -18.978 78.906 1.00 66.57 O ANISOU 3371 O SER B 164 7649 8186 9459 -165 484 -896 O ATOM 3372 CB SER B 164 41.506 -16.234 77.138 1.00 68.23 C ANISOU 3372 CB SER B 164 7900 8186 9837 -484 1041 -877 C ATOM 3373 OG SER B 164 42.143 -14.972 77.028 1.00 78.74 O ANISOU 3373 OG SER B 164 9135 9426 11356 -631 1192 -929 O ATOM 3374 N ILE B 165 42.027 -19.357 76.941 1.00 60.74 N ANISOU 3374 N ILE B 165 6847 7367 8864 -210 927 -918 N ATOM 3375 CA ILE B 165 41.597 -20.738 76.682 1.00 59.64 C ANISOU 3375 CA ILE B 165 6824 7266 8570 -82 871 -874 C ATOM 3376 C ILE B 165 42.016 -21.698 77.832 1.00 64.90 C ANISOU 3376 C ILE B 165 7322 7998 9340 43 607 -945 C ATOM 3377 O ILE B 165 41.186 -22.468 78.306 1.00 65.39 O ANISOU 3377 O ILE B 165 7528 8099 9218 132 429 -883 O ATOM 3378 CB ILE B 165 42.070 -21.198 75.272 1.00 61.19 C ANISOU 3378 CB ILE B 165 7073 7404 8773 -86 1175 -875 C ATOM 3379 CG1 ILE B 165 41.152 -20.602 74.166 1.00 60.09 C ANISOU 3379 CG1 ILE B 165 7246 7209 8379 -159 1345 -756 C ATOM 3380 CG2 ILE B 165 42.183 -22.727 75.166 1.00 60.08 C ANISOU 3380 CG2 ILE B 165 6935 7288 8603 55 1122 -895 C ATOM 3381 CD1 ILE B 165 41.699 -20.682 72.698 1.00 57.77 C ANISOU 3381 CD1 ILE B 165 7047 6830 8073 -199 1698 -757 C ATOM 3382 N LEU B 166 43.277 -21.623 78.291 1.00 61.20 N ANISOU 3382 N LEU B 166 6552 7532 9170 48 577 -1071 N ATOM 3383 CA LEU B 166 43.788 -22.430 79.406 1.00 60.16 C ANISOU 3383 CA LEU B 166 6255 7451 9153 176 299 -1142 C ATOM 3384 C LEU B 166 43.078 -22.081 80.722 1.00 61.11 C ANISOU 3384 C LEU B 166 6471 7618 9132 188 2 -1115 C ATOM 3385 O LEU B 166 42.885 -22.963 81.560 1.00 60.98 O ANISOU 3385 O LEU B 166 6499 7638 9033 314 -230 -1102 O ATOM 3386 CB LEU B 166 45.302 -22.221 79.573 1.00 60.51 C ANISOU 3386 CB LEU B 166 5929 7483 9580 164 319 -1294 C ATOM 3387 CG LEU B 166 46.211 -22.901 78.560 1.00 65.25 C ANISOU 3387 CG LEU B 166 6375 8041 10376 208 573 -1349 C ATOM 3388 CD1 LEU B 166 47.585 -22.280 78.590 1.00 65.60 C ANISOU 3388 CD1 LEU B 166 6039 8057 10827 135 663 -1496 C ATOM 3389 CD2 LEU B 166 46.303 -24.392 78.814 1.00 67.21 C ANISOU 3389 CD2 LEU B 166 6624 8312 10601 401 423 -1349 C ATOM 3390 N GLY B 167 42.718 -20.802 80.880 1.00 54.96 N ANISOU 3390 N GLY B 167 5739 6823 8323 61 29 -1107 N ATOM 3391 CA GLY B 167 41.988 -20.262 82.026 1.00 53.67 C ANISOU 3391 CA GLY B 167 5692 6685 8014 53 -195 -1087 C ATOM 3392 C GLY B 167 40.544 -20.718 82.064 1.00 55.99 C ANISOU 3392 C GLY B 167 6278 6998 7996 104 -230 -949 C ATOM 3393 O GLY B 167 40.006 -20.951 83.146 1.00 55.27 O ANISOU 3393 O GLY B 167 6285 6939 7775 165 -441 -930 O ATOM 3394 N ILE B 168 39.912 -20.875 80.868 1.00 52.32 N ANISOU 3394 N ILE B 168 5960 6508 7411 78 -21 -857 N ATOM 3395 CA ILE B 168 38.556 -21.418 80.679 1.00 51.65 C ANISOU 3395 CA ILE B 168 6122 6435 7067 119 -38 -733 C ATOM 3396 C ILE B 168 38.557 -22.883 81.172 1.00 54.84 C ANISOU 3396 C ILE B 168 6545 6869 7422 252 -185 -727 C ATOM 3397 O ILE B 168 37.644 -23.288 81.895 1.00 55.50 O ANISOU 3397 O ILE B 168 6772 6973 7342 298 -319 -663 O ATOM 3398 CB ILE B 168 38.101 -21.322 79.187 1.00 54.12 C ANISOU 3398 CB ILE B 168 6570 6706 7289 65 196 -659 C ATOM 3399 CG1 ILE B 168 37.738 -19.862 78.799 1.00 53.41 C ANISOU 3399 CG1 ILE B 168 6545 6571 7179 -51 312 -623 C ATOM 3400 CG2 ILE B 168 36.949 -22.322 78.860 1.00 53.15 C ANISOU 3400 CG2 ILE B 168 6650 6595 6951 128 156 -561 C ATOM 3401 CD1 ILE B 168 37.772 -19.567 77.279 1.00 52.84 C ANISOU 3401 CD1 ILE B 168 6575 6435 7068 -112 567 -576 C ATOM 3402 N TRP B 169 39.593 -23.655 80.797 1.00 49.37 N ANISOU 3402 N TRP B 169 5708 6168 6883 314 -144 -792 N ATOM 3403 CA TRP B 169 39.749 -25.051 81.206 1.00 47.96 C ANISOU 3403 CA TRP B 169 5539 5997 6688 452 -275 -792 C ATOM 3404 C TRP B 169 39.973 -25.196 82.698 1.00 51.47 C ANISOU 3404 C TRP B 169 5940 6471 7147 530 -548 -825 C ATOM 3405 O TRP B 169 39.262 -25.964 83.326 1.00 53.53 O ANISOU 3405 O TRP B 169 6363 6733 7243 605 -676 -757 O ATOM 3406 CB TRP B 169 40.834 -25.724 80.397 1.00 46.24 C ANISOU 3406 CB TRP B 169 5168 5749 6653 506 -143 -862 C ATOM 3407 CG TRP B 169 40.321 -26.154 79.065 1.00 47.04 C ANISOU 3407 CG TRP B 169 5430 5812 6632 481 76 -805 C ATOM 3408 CD1 TRP B 169 40.440 -25.486 77.884 1.00 49.68 C ANISOU 3408 CD1 TRP B 169 5785 6114 6979 382 328 -807 C ATOM 3409 CD2 TRP B 169 39.510 -27.310 78.795 1.00 47.00 C ANISOU 3409 CD2 TRP B 169 5626 5784 6445 547 51 -735 C ATOM 3410 NE1 TRP B 169 39.810 -26.186 76.880 1.00 49.14 N ANISOU 3410 NE1 TRP B 169 5923 6011 6739 394 446 -750 N ATOM 3411 CE2 TRP B 169 39.223 -27.306 77.411 1.00 50.66 C ANISOU 3411 CE2 TRP B 169 6217 6208 6821 488 276 -711 C ATOM 3412 CE3 TRP B 169 39.035 -28.374 79.583 1.00 47.97 C ANISOU 3412 CE3 TRP B 169 5846 5904 6474 647 -135 -694 C ATOM 3413 CZ2 TRP B 169 38.481 -28.321 76.796 1.00 49.66 C ANISOU 3413 CZ2 TRP B 169 6296 6045 6526 522 297 -661 C ATOM 3414 CZ3 TRP B 169 38.320 -29.390 78.969 1.00 49.45 C ANISOU 3414 CZ3 TRP B 169 6224 6049 6517 674 -88 -640 C ATOM 3415 CH2 TRP B 169 38.048 -29.356 77.591 1.00 50.03 C ANISOU 3415 CH2 TRP B 169 6405 6089 6515 610 115 -631 C ATOM 3416 N ALA B 170 40.873 -24.389 83.275 1.00 45.46 N ANISOU 3416 N ALA B 170 4984 5724 6564 500 -637 -926 N ATOM 3417 CA ALA B 170 41.153 -24.323 84.702 1.00 43.91 C ANISOU 3417 CA ALA B 170 4761 5553 6371 562 -920 -974 C ATOM 3418 C ALA B 170 39.866 -23.993 85.522 1.00 48.79 C ANISOU 3418 C ALA B 170 5638 6181 6719 539 -1005 -887 C ATOM 3419 O ALA B 170 39.599 -24.670 86.508 1.00 46.63 O ANISOU 3419 O ALA B 170 5491 5912 6315 639 -1193 -856 O ATOM 3420 CB ALA B 170 42.238 -23.286 84.966 1.00 43.81 C ANISOU 3420 CB ALA B 170 4494 5545 6606 492 -972 -1109 C ATOM 3421 N VAL B 171 39.060 -22.981 85.104 1.00 46.88 N ANISOU 3421 N VAL B 171 5485 5933 6395 416 -855 -843 N ATOM 3422 CA VAL B 171 37.830 -22.612 85.837 1.00 46.03 C ANISOU 3422 CA VAL B 171 5596 5828 6065 396 -901 -769 C ATOM 3423 C VAL B 171 36.795 -23.752 85.753 1.00 47.73 C ANISOU 3423 C VAL B 171 6003 6038 6095 462 -878 -651 C ATOM 3424 O VAL B 171 36.258 -24.173 86.780 1.00 46.66 O ANISOU 3424 O VAL B 171 6016 5902 5811 522 -1002 -611 O ATOM 3425 CB VAL B 171 37.244 -21.225 85.419 1.00 49.54 C ANISOU 3425 CB VAL B 171 6072 6255 6497 265 -752 -755 C ATOM 3426 CG1 VAL B 171 35.890 -20.975 86.076 1.00 49.27 C ANISOU 3426 CG1 VAL B 171 6250 6216 6252 263 -768 -674 C ATOM 3427 CG2 VAL B 171 38.205 -20.087 85.756 1.00 49.25 C ANISOU 3427 CG2 VAL B 171 5873 6205 6636 191 -798 -879 C ATOM 3428 N SER B 172 36.551 -24.248 84.528 1.00 44.00 N ANISOU 3428 N SER B 172 5534 5552 5631 446 -716 -602 N ATOM 3429 CA SER B 172 35.615 -25.326 84.208 1.00 43.97 C ANISOU 3429 CA SER B 172 5689 5531 5488 485 -680 -505 C ATOM 3430 C SER B 172 35.880 -26.610 84.978 1.00 48.47 C ANISOU 3430 C SER B 172 6311 6084 6020 609 -827 -496 C ATOM 3431 O SER B 172 34.926 -27.223 85.468 1.00 48.37 O ANISOU 3431 O SER B 172 6472 6052 5856 632 -859 -415 O ATOM 3432 CB SER B 172 35.637 -25.617 82.715 1.00 46.24 C ANISOU 3432 CB SER B 172 5959 5799 5813 450 -505 -490 C ATOM 3433 OG SER B 172 35.197 -24.471 82.002 1.00 53.29 O ANISOU 3433 OG SER B 172 6861 6692 6696 344 -374 -471 O ATOM 3434 N LEU B 173 37.168 -27.012 85.080 1.00 44.34 N ANISOU 3434 N LEU B 173 5636 5560 5652 690 -912 -577 N ATOM 3435 CA LEU B 173 37.586 -28.220 85.781 1.00 44.68 C ANISOU 3435 CA LEU B 173 5720 5574 5682 832 -1073 -572 C ATOM 3436 C LEU B 173 37.333 -28.105 87.293 1.00 48.18 C ANISOU 3436 C LEU B 173 6295 6021 5990 881 -1273 -553 C ATOM 3437 O LEU B 173 36.908 -29.077 87.941 1.00 47.03 O ANISOU 3437 O LEU B 173 6329 5832 5707 965 -1354 -481 O ATOM 3438 CB LEU B 173 39.067 -28.541 85.469 1.00 44.87 C ANISOU 3438 CB LEU B 173 5510 5595 5944 915 -1116 -675 C ATOM 3439 CG LEU B 173 39.376 -29.098 84.053 1.00 49.11 C ANISOU 3439 CG LEU B 173 5972 6102 6587 913 -910 -689 C ATOM 3440 CD1 LEU B 173 40.859 -29.082 83.772 1.00 48.36 C ANISOU 3440 CD1 LEU B 173 5599 6008 6768 969 -909 -808 C ATOM 3441 CD2 LEU B 173 38.844 -30.518 83.873 1.00 52.62 C ANISOU 3441 CD2 LEU B 173 6591 6484 6918 999 -904 -615 C ATOM 3442 N ALA B 174 37.561 -26.899 87.830 1.00 43.64 N ANISOU 3442 N ALA B 174 5656 5484 5442 821 -1336 -618 N ATOM 3443 CA ALA B 174 37.409 -26.549 89.236 1.00 43.33 C ANISOU 3443 CA ALA B 174 5752 5447 5266 853 -1519 -625 C ATOM 3444 C ALA B 174 35.956 -26.379 89.677 1.00 49.36 C ANISOU 3444 C ALA B 174 6760 6195 5801 799 -1423 -524 C ATOM 3445 O ALA B 174 35.580 -26.974 90.681 1.00 49.76 O ANISOU 3445 O ALA B 174 7014 6212 5679 873 -1521 -469 O ATOM 3446 CB ALA B 174 38.196 -25.290 89.545 1.00 43.62 C ANISOU 3446 CB ALA B 174 5627 5517 5430 794 -1607 -748 C ATOM 3447 N ILE B 175 35.146 -25.570 88.954 1.00 46.48 N ANISOU 3447 N ILE B 175 6378 5844 5438 678 -1231 -498 N ATOM 3448 CA ILE B 175 33.751 -25.280 89.324 1.00 46.06 C ANISOU 3448 CA ILE B 175 6507 5776 5217 625 -1127 -415 C ATOM 3449 C ILE B 175 32.812 -26.487 89.182 1.00 50.72 C ANISOU 3449 C ILE B 175 7243 6327 5702 653 -1052 -302 C ATOM 3450 O ILE B 175 31.699 -26.441 89.737 1.00 51.49 O ANISOU 3450 O ILE B 175 7497 6401 5666 628 -983 -235 O ATOM 3451 CB ILE B 175 33.147 -24.022 88.611 1.00 48.79 C ANISOU 3451 CB ILE B 175 6786 6138 5613 505 -967 -418 C ATOM 3452 CG1 ILE B 175 32.934 -24.269 87.079 1.00 48.00 C ANISOU 3452 CG1 ILE B 175 6594 6041 5604 456 -817 -379 C ATOM 3453 CG2 ILE B 175 33.960 -22.727 88.913 1.00 48.52 C ANISOU 3453 CG2 ILE B 175 6643 6120 5674 459 -1029 -530 C ATOM 3454 CD1 ILE B 175 31.930 -23.334 86.409 1.00 43.22 C ANISOU 3454 CD1 ILE B 175 6003 5432 4986 364 -669 -333 C ATOM 3455 N MET B 176 33.224 -27.543 88.431 1.00 45.37 N ANISOU 3455 N MET B 176 6511 5631 5097 698 -1046 -287 N ATOM 3456 CA MET B 176 32.373 -28.723 88.244 1.00 44.03 C ANISOU 3456 CA MET B 176 6477 5407 4846 711 -977 -191 C ATOM 3457 C MET B 176 32.641 -29.835 89.264 1.00 47.45 C ANISOU 3457 C MET B 176 7069 5779 5180 829 -1106 -153 C ATOM 3458 O MET B 176 31.940 -30.846 89.251 1.00 47.02 O ANISOU 3458 O MET B 176 7148 5659 5057 837 -1045 -71 O ATOM 3459 CB MET B 176 32.421 -29.245 86.796 1.00 45.93 C ANISOU 3459 CB MET B 176 6623 5640 5189 681 -875 -190 C ATOM 3460 CG MET B 176 31.718 -28.310 85.784 1.00 48.79 C ANISOU 3460 CG MET B 176 6916 6036 5585 562 -734 -186 C ATOM 3461 SD MET B 176 30.057 -27.742 86.272 1.00 51.74 S ANISOU 3461 SD MET B 176 7401 6405 5853 481 -652 -106 S ATOM 3462 CE MET B 176 29.628 -26.692 84.888 1.00 47.81 C ANISOU 3462 CE MET B 176 6794 5940 5430 382 -542 -115 C ATOM 3463 N VAL B 177 33.608 -29.627 90.185 1.00 44.07 N ANISOU 3463 N VAL B 177 6642 5363 4739 919 -1291 -210 N ATOM 3464 CA VAL B 177 33.954 -30.592 91.240 1.00 44.12 C ANISOU 3464 CA VAL B 177 6827 5306 4630 1052 -1452 -171 C ATOM 3465 C VAL B 177 32.718 -30.834 92.178 1.00 49.83 C ANISOU 3465 C VAL B 177 7835 5970 5129 1028 -1369 -65 C ATOM 3466 O VAL B 177 32.462 -32.007 92.478 1.00 51.83 O ANISOU 3466 O VAL B 177 8260 6136 5298 1090 -1368 20 O ATOM 3467 CB VAL B 177 35.286 -30.239 91.997 1.00 47.28 C ANISOU 3467 CB VAL B 177 7156 5734 5074 1158 -1709 -268 C ATOM 3468 CG1 VAL B 177 35.527 -31.155 93.194 1.00 45.79 C ANISOU 3468 CG1 VAL B 177 7207 5471 4721 1307 -1900 -214 C ATOM 3469 CG2 VAL B 177 36.484 -30.304 91.051 1.00 47.38 C ANISOU 3469 CG2 VAL B 177 6879 5782 5343 1192 -1756 -363 C ATOM 3470 N PRO B 178 31.889 -29.818 92.583 1.00 44.03 N ANISOU 3470 N PRO B 178 7156 5264 4310 935 -1267 -62 N ATOM 3471 CA PRO B 178 30.719 -30.133 93.418 1.00 43.76 C ANISOU 3471 CA PRO B 178 7376 5162 4088 912 -1146 37 C ATOM 3472 C PRO B 178 29.727 -31.091 92.737 1.00 48.73 C ANISOU 3472 C PRO B 178 8029 5732 4755 850 -963 131 C ATOM 3473 O PRO B 178 29.128 -31.928 93.426 1.00 49.43 O ANISOU 3473 O PRO B 178 8340 5729 4714 867 -898 223 O ATOM 3474 CB PRO B 178 30.129 -28.752 93.744 1.00 45.15 C ANISOU 3474 CB PRO B 178 7543 5385 4226 827 -1056 -4 C ATOM 3475 CG PRO B 178 31.246 -27.814 93.558 1.00 48.40 C ANISOU 3475 CG PRO B 178 7773 5872 4746 839 -1210 -126 C ATOM 3476 CD PRO B 178 31.998 -28.357 92.390 1.00 43.93 C ANISOU 3476 CD PRO B 178 6994 5329 4369 855 -1248 -150 C ATOM 3477 N GLN B 179 29.644 -31.045 91.384 1.00 44.71 N ANISOU 3477 N GLN B 179 7306 5262 4418 782 -895 104 N ATOM 3478 CA GLN B 179 28.812 -31.935 90.562 1.00 45.11 C ANISOU 3478 CA GLN B 179 7355 5260 4527 716 -761 167 C ATOM 3479 C GLN B 179 29.335 -33.389 90.655 1.00 51.88 C ANISOU 3479 C GLN B 179 8327 6021 5362 812 -836 208 C ATOM 3480 O GLN B 179 28.532 -34.305 90.793 1.00 52.33 O ANISOU 3480 O GLN B 179 8523 5984 5377 778 -736 289 O ATOM 3481 CB GLN B 179 28.751 -31.444 89.096 1.00 46.08 C ANISOU 3481 CB GLN B 179 7254 5447 4807 635 -705 116 C ATOM 3482 CG GLN B 179 27.821 -32.249 88.177 1.00 56.93 C ANISOU 3482 CG GLN B 179 8623 6770 6239 555 -594 162 C ATOM 3483 CD GLN B 179 26.353 -32.031 88.478 1.00 73.16 C ANISOU 3483 CD GLN B 179 10724 8801 8273 454 -454 224 C ATOM 3484 OE1 GLN B 179 25.846 -30.894 88.538 1.00 66.87 O ANISOU 3484 OE1 GLN B 179 9850 8063 7494 403 -400 210 O ATOM 3485 NE2 GLN B 179 25.634 -33.125 88.666 1.00 58.54 N ANISOU 3485 NE2 GLN B 179 8989 6851 6403 424 -383 292 N ATOM 3486 N ALA B 180 30.676 -33.585 90.630 1.00 48.72 N ANISOU 3486 N ALA B 180 7867 5637 5007 932 -1008 149 N ATOM 3487 CA ALA B 180 31.310 -34.895 90.752 1.00 48.93 C ANISOU 3487 CA ALA B 180 7992 5568 5029 1053 -1101 180 C ATOM 3488 C ALA B 180 31.100 -35.470 92.179 1.00 55.17 C ANISOU 3488 C ALA B 180 9080 6261 5621 1133 -1158 272 C ATOM 3489 O ALA B 180 30.788 -36.646 92.333 1.00 54.87 O ANISOU 3489 O ALA B 180 9217 6100 5533 1165 -1117 355 O ATOM 3490 CB ALA B 180 32.795 -34.786 90.427 1.00 49.38 C ANISOU 3490 CB ALA B 180 7872 5674 5217 1168 -1270 83 C ATOM 3491 N ALA B 181 31.219 -34.615 93.202 1.00 52.81 N ANISOU 3491 N ALA B 181 8861 6008 5197 1157 -1236 257 N ATOM 3492 CA ALA B 181 31.039 -34.936 94.619 1.00 52.21 C ANISOU 3492 CA ALA B 181 9101 5848 4888 1231 -1289 335 C ATOM 3493 C ALA B 181 29.646 -35.491 94.988 1.00 56.37 C ANISOU 3493 C ALA B 181 9851 6269 5297 1138 -1049 456 C ATOM 3494 O ALA B 181 29.539 -36.238 95.965 1.00 58.09 O ANISOU 3494 O ALA B 181 10369 6367 5335 1212 -1063 550 O ATOM 3495 CB ALA B 181 31.339 -33.701 95.456 1.00 52.67 C ANISOU 3495 CB ALA B 181 9178 5989 4846 1241 -1393 267 C ATOM 3496 N VAL B 182 28.581 -35.098 94.258 1.00 51.33 N ANISOU 3496 N VAL B 182 9074 5666 4762 977 -833 456 N ATOM 3497 CA VAL B 182 27.210 -35.550 94.557 1.00 49.53 C ANISOU 3497 CA VAL B 182 8998 5342 4479 868 -589 555 C ATOM 3498 C VAL B 182 26.796 -36.793 93.761 1.00 53.70 C ANISOU 3498 C VAL B 182 9514 5768 5121 818 -501 607 C ATOM 3499 O VAL B 182 25.800 -37.417 94.115 1.00 53.35 O ANISOU 3499 O VAL B 182 9624 5610 5037 740 -317 696 O ATOM 3500 CB VAL B 182 26.133 -34.442 94.436 1.00 51.49 C ANISOU 3500 CB VAL B 182 9122 5664 4777 729 -403 531 C ATOM 3501 CG1 VAL B 182 26.323 -33.357 95.488 1.00 50.88 C ANISOU 3501 CG1 VAL B 182 9146 5640 4544 773 -444 494 C ATOM 3502 CG2 VAL B 182 26.073 -33.867 93.027 1.00 50.87 C ANISOU 3502 CG2 VAL B 182 8720 5691 4917 647 -403 452 C ATOM 3503 N MET B 183 27.530 -37.145 92.693 1.00 50.66 N ANISOU 3503 N MET B 183 8951 5414 4883 853 -613 545 N ATOM 3504 CA MET B 183 27.187 -38.294 91.860 1.00 50.84 C ANISOU 3504 CA MET B 183 8967 5337 5014 805 -542 572 C ATOM 3505 C MET B 183 27.423 -39.604 92.586 1.00 59.59 C ANISOU 3505 C MET B 183 10357 6271 6014 904 -568 666 C ATOM 3506 O MET B 183 28.543 -39.892 93.010 1.00 59.32 O ANISOU 3506 O MET B 183 10404 6218 5916 1073 -756 662 O ATOM 3507 CB MET B 183 27.936 -38.280 90.520 1.00 52.54 C ANISOU 3507 CB MET B 183 8947 5623 5393 826 -635 472 C ATOM 3508 CG MET B 183 27.644 -37.063 89.670 1.00 55.91 C ANISOU 3508 CG MET B 183 9126 6195 5921 722 -594 393 C ATOM 3509 SD MET B 183 25.885 -36.695 89.401 1.00 59.28 S ANISOU 3509 SD MET B 183 9506 6623 6396 523 -387 431 S ATOM 3510 CE MET B 183 25.431 -38.031 88.321 1.00 55.47 C ANISOU 3510 CE MET B 183 9027 6023 6025 448 -337 436 C ATOM 3511 N GLU B 184 26.355 -40.394 92.746 1.00 58.22 N ANISOU 3511 N GLU B 184 10329 5960 5831 797 -381 753 N ATOM 3512 CA GLU B 184 26.450 -41.694 93.379 1.00 58.34 C ANISOU 3512 CA GLU B 184 10639 5780 5748 870 -369 858 C ATOM 3513 C GLU B 184 25.700 -42.669 92.492 1.00 64.44 C ANISOU 3513 C GLU B 184 11408 6416 6660 756 -239 878 C ATOM 3514 O GLU B 184 24.770 -42.312 91.774 1.00 62.47 O ANISOU 3514 O GLU B 184 10977 6206 6552 586 -113 836 O ATOM 3515 CB GLU B 184 25.949 -41.681 94.837 1.00 59.32 C ANISOU 3515 CB GLU B 184 11070 5817 5653 879 -262 972 C ATOM 3516 CG GLU B 184 26.672 -40.714 95.768 1.00 70.21 C ANISOU 3516 CG GLU B 184 12522 7301 6854 1008 -421 950 C ATOM 3517 CD GLU B 184 28.163 -40.848 96.031 1.00 90.89 C ANISOU 3517 CD GLU B 184 15178 9942 9412 1226 -730 916 C ATOM 3518 OE1 GLU B 184 28.734 -41.934 95.776 1.00 73.73 O ANISOU 3518 OE1 GLU B 184 13073 7657 7284 1328 -823 945 O ATOM 3519 OE2 GLU B 184 28.759 -39.857 96.516 1.00 89.85 O ANISOU 3519 OE2 GLU B 184 15003 9934 9202 1297 -882 853 O ATOM 3520 N CYS B 185 26.172 -43.910 92.581 1.00 64.86 N ANISOU 3520 N CYS B 185 11674 6297 6672 860 -289 939 N ATOM 3521 CA CYS B 185 25.632 -45.082 91.862 1.00 65.35 C ANISOU 3521 CA CYS B 185 11797 6186 6845 773 -182 962 C ATOM 3522 C CYS B 185 24.863 -45.895 92.900 1.00 70.71 C ANISOU 3522 C CYS B 185 12777 6670 7418 702 11 1103 C ATOM 3523 O CYS B 185 25.470 -46.265 93.912 1.00 71.69 O ANISOU 3523 O CYS B 185 13184 6709 7348 841 -37 1201 O ATOM 3524 CB CYS B 185 26.796 -45.921 91.358 1.00 65.66 C ANISOU 3524 CB CYS B 185 11881 6146 6921 949 -354 933 C ATOM 3525 SG CYS B 185 26.432 -46.804 89.825 1.00 69.52 S ANISOU 3525 SG CYS B 185 12148 6628 7637 852 -335 806 S ATOM 3526 N SER B 186 23.573 -46.125 92.676 1.00 68.36 N ANISOU 3526 N SER B 186 12425 6302 7248 485 228 1112 N ATOM 3527 CA SER B 186 22.786 -46.895 93.668 1.00 69.46 C ANISOU 3527 CA SER B 186 12828 6241 7322 383 466 1244 C ATOM 3528 C SER B 186 21.832 -47.865 92.970 1.00 76.41 C ANISOU 3528 C SER B 186 13667 6960 8405 185 627 1236 C ATOM 3529 O SER B 186 21.441 -47.604 91.822 1.00 74.95 O ANISOU 3529 O SER B 186 13189 6868 8419 54 613 1123 O ATOM 3530 CB SER B 186 22.066 -45.989 94.630 1.00 73.15 C ANISOU 3530 CB SER B 186 13302 6793 7699 305 634 1285 C ATOM 3531 OG SER B 186 21.348 -44.981 93.937 1.00 85.80 O ANISOU 3531 OG SER B 186 14561 8623 9418 233 602 1172 O ATOM 3532 N SER B 187 21.518 -48.961 93.656 1.00 75.96 N ANISOU 3532 N SER B 187 13926 6646 8290 167 769 1358 N ATOM 3533 CA SER B 187 20.614 -49.982 93.161 1.00 76.96 C ANISOU 3533 CA SER B 187 14074 6567 8601 -27 941 1366 C ATOM 3534 C SER B 187 19.259 -49.843 93.847 1.00 84.41 C ANISOU 3534 C SER B 187 15045 7434 9594 -238 1257 1441 C ATOM 3535 O SER B 187 19.198 -49.314 94.967 1.00 82.82 O ANISOU 3535 O SER B 187 15007 7256 9203 -181 1362 1533 O ATOM 3536 CB SER B 187 21.212 -51.351 93.457 1.00 79.15 C ANISOU 3536 CB SER B 187 14695 6580 8798 87 915 1456 C ATOM 3537 OG SER B 187 20.523 -52.329 92.701 1.00 89.17 O ANISOU 3537 OG SER B 187 15935 7666 10279 -98 1029 1421 O ATOM 3538 N VAL B 188 18.174 -50.339 93.180 1.00 83.93 N ANISOU 3538 N VAL B 188 14824 7273 9793 -482 1412 1394 N ATOM 3539 CA VAL B 188 16.787 -50.291 93.676 1.00 84.87 C ANISOU 3539 CA VAL B 188 14898 7303 10044 -715 1736 1444 C ATOM 3540 C VAL B 188 16.731 -50.793 95.138 1.00 90.29 C ANISOU 3540 C VAL B 188 16015 7783 10510 -670 1974 1630 C ATOM 3541 O VAL B 188 16.106 -50.150 95.983 1.00 89.74 O ANISOU 3541 O VAL B 188 15973 7747 10378 -724 2194 1689 O ATOM 3542 CB VAL B 188 15.771 -50.980 92.713 1.00 89.23 C ANISOU 3542 CB VAL B 188 15235 7738 10930 -975 1822 1358 C ATOM 3543 CG1 VAL B 188 16.066 -52.470 92.516 1.00 89.14 C ANISOU 3543 CG1 VAL B 188 15483 7448 10939 -986 1820 1394 C ATOM 3544 CG2 VAL B 188 14.328 -50.756 93.163 1.00 89.17 C ANISOU 3544 CG2 VAL B 188 15091 7675 11115 -1216 2147 1387 C ATOM 3545 N LEU B 189 17.466 -51.892 95.419 1.00 88.07 N ANISOU 3545 N LEU B 189 16084 7291 10088 -545 1913 1720 N ATOM 3546 CA LEU B 189 17.717 -52.489 96.725 1.00 88.22 C ANISOU 3546 CA LEU B 189 16587 7093 9838 -439 2055 1906 C ATOM 3547 C LEU B 189 19.258 -52.552 96.780 1.00 95.54 C ANISOU 3547 C LEU B 189 17682 8082 10539 -124 1702 1914 C ATOM 3548 O LEU B 189 19.828 -53.377 96.076 1.00 94.18 O ANISOU 3548 O LEU B 189 17522 7814 10449 -60 1541 1874 O ATOM 3549 CB LEU B 189 17.092 -53.889 96.838 1.00 87.99 C ANISOU 3549 CB LEU B 189 16793 6716 9922 -600 2298 1998 C ATOM 3550 CG LEU B 189 15.574 -53.983 96.678 1.00 92.06 C ANISOU 3550 CG LEU B 189 17104 7146 10730 -932 2642 1975 C ATOM 3551 CD1 LEU B 189 15.174 -55.319 96.106 1.00 91.71 C ANISOU 3551 CD1 LEU B 189 17114 6820 10910 -1103 2733 1969 C ATOM 3552 CD2 LEU B 189 14.862 -53.732 97.990 1.00 94.12 C ANISOU 3552 CD2 LEU B 189 17599 7313 10850 -999 3007 2120 C ATOM 3553 N PRO B 190 19.949 -51.601 97.484 1.00 96.69 N ANISOU 3553 N PRO B 190 17899 8406 10435 70 1559 1935 N ATOM 3554 CA PRO B 190 21.435 -51.564 97.484 1.00 97.13 C ANISOU 3554 CA PRO B 190 18039 8542 10324 365 1195 1918 C ATOM 3555 C PRO B 190 22.160 -52.919 97.451 1.00 99.91 C ANISOU 3555 C PRO B 190 18670 8654 10636 517 1070 1988 C ATOM 3556 O PRO B 190 23.155 -53.044 96.731 1.00100.36 O ANISOU 3556 O PRO B 190 18580 8794 10757 675 791 1894 O ATOM 3557 CB PRO B 190 21.749 -50.817 98.779 1.00 99.18 C ANISOU 3557 CB PRO B 190 18548 8871 10266 508 1177 2006 C ATOM 3558 CG PRO B 190 20.643 -49.819 98.873 1.00103.64 C ANISOU 3558 CG PRO B 190 18894 9572 10911 302 1423 1962 C ATOM 3559 CD PRO B 190 19.407 -50.478 98.284 1.00 99.06 C ANISOU 3559 CD PRO B 190 18182 8843 10614 24 1717 1957 C ATOM 3560 N GLU B 191 21.641 -53.926 98.193 1.00 93.57 N ANISOU 3560 N GLU B 191 18264 7544 9743 467 1296 2151 N ATOM 3561 CA GLU B 191 22.146 -55.304 98.307 1.00 91.74 C ANISOU 3561 CA GLU B 191 18369 7023 9465 596 1235 2250 C ATOM 3562 C GLU B 191 22.331 -56.002 96.927 1.00 91.23 C ANISOU 3562 C GLU B 191 18063 6905 9697 531 1153 2119 C ATOM 3563 O GLU B 191 23.187 -56.875 96.774 1.00 90.30 O ANISOU 3563 O GLU B 191 18125 6620 9563 707 999 2147 O ATOM 3564 CB GLU B 191 21.248 -56.133 99.258 1.00 93.36 C ANISOU 3564 CB GLU B 191 19019 6902 9552 478 1580 2446 C ATOM 3565 CG GLU B 191 21.223 -55.683 100.720 1.00107.83 C ANISOU 3565 CG GLU B 191 21064 8773 11134 446 1785 2557 C ATOM 3566 CD GLU B 191 20.236 -54.574 101.050 1.00137.84 C ANISOU 3566 CD GLU B 191 24517 12739 15115 170 2051 2468 C ATOM 3567 OE1 GLU B 191 19.570 -54.079 100.113 1.00144.79 O ANISOU 3567 OE1 GLU B 191 25342 13457 16216 -97 2370 2481 O ATOM 3568 OE2 GLU B 191 20.139 -54.184 102.237 1.00128.57 O ANISOU 3568 OE2 GLU B 191 23112 11853 13886 220 1935 2379 O ATOM 3569 N LEU B 192 21.522 -55.595 95.940 1.00 85.13 N ANISOU 3569 N LEU B 192 16896 6266 9185 287 1251 1974 N ATOM 3570 CA LEU B 192 21.506 -56.086 94.564 1.00 84.10 C ANISOU 3570 CA LEU B 192 16516 6113 9327 182 1189 1825 C ATOM 3571 C LEU B 192 22.763 -55.785 93.731 1.00 82.93 C ANISOU 3571 C LEU B 192 16166 6148 9195 405 854 1692 C ATOM 3572 O LEU B 192 23.077 -56.568 92.831 1.00 81.81 O ANISOU 3572 O LEU B 192 15993 5895 9194 420 778 1610 O ATOM 3573 CB LEU B 192 20.262 -55.480 93.879 1.00 84.56 C ANISOU 3573 CB LEU B 192 16204 6303 9622 -125 1352 1710 C ATOM 3574 CG LEU B 192 19.614 -56.214 92.695 1.00 89.23 C ANISOU 3574 CG LEU B 192 16624 6775 10506 -346 1405 1589 C ATOM 3575 CD1 LEU B 192 19.447 -57.719 92.965 1.00 88.62 C ANISOU 3575 CD1 LEU B 192 16906 6309 10458 -397 1559 1692 C ATOM 3576 CD2 LEU B 192 18.267 -55.592 92.385 1.00 91.93 C ANISOU 3576 CD2 LEU B 192 16648 7225 11056 -639 1581 1517 C ATOM 3577 N ALA B 193 23.466 -54.651 94.023 1.00 75.15 N ANISOU 3577 N ALA B 193 15045 5432 8076 569 670 1663 N ATOM 3578 CA ALA B 193 24.704 -54.206 93.353 1.00 72.75 C ANISOU 3578 CA ALA B 193 14529 5322 7792 781 373 1540 C ATOM 3579 C ALA B 193 25.858 -55.241 93.437 1.00 74.37 C ANISOU 3579 C ALA B 193 14969 5339 7951 1044 201 1583 C ATOM 3580 O ALA B 193 26.753 -55.234 92.584 1.00 75.82 O ANISOU 3580 O ALA B 193 14960 5608 8240 1175 18 1459 O ATOM 3581 CB ALA B 193 25.151 -52.868 93.912 1.00 72.97 C ANISOU 3581 CB ALA B 193 14431 5620 7673 891 242 1530 C ATOM 3582 N ALA B 194 25.811 -56.146 94.427 1.00 66.09 N ANISOU 3582 N ALA B 194 14339 4019 6754 1120 276 1759 N ATOM 3583 CA ALA B 194 26.786 -57.210 94.573 1.00 65.62 C ANISOU 3583 CA ALA B 194 14537 3739 6656 1372 126 1820 C ATOM 3584 C ALA B 194 26.557 -58.308 93.523 1.00 70.21 C ANISOU 3584 C ALA B 194 15105 4113 7460 1273 214 1743 C ATOM 3585 O ALA B 194 27.337 -59.267 93.493 1.00 71.19 O ANISOU 3585 O ALA B 194 15422 4035 7592 1480 105 1774 O ATOM 3586 CB ALA B 194 26.680 -57.825 95.969 1.00 66.36 C ANISOU 3586 CB ALA B 194 15123 3585 6504 1466 199 2045 C ATOM 3587 N ARG B 195 25.484 -58.210 92.693 1.00 64.90 N ANISOU 3587 N ARG B 195 14222 3470 6967 966 402 1643 N ATOM 3588 CA ARG B 195 25.163 -59.248 91.698 1.00 64.71 C ANISOU 3588 CA ARG B 195 14203 3237 7146 841 485 1555 C ATOM 3589 C ARG B 195 25.176 -58.729 90.257 1.00 67.95 C ANISOU 3589 C ARG B 195 14215 3862 7740 744 405 1331 C ATOM 3590 O ARG B 195 25.725 -59.383 89.372 1.00 67.27 O ANISOU 3590 O ARG B 195 14112 3684 7762 823 326 1224 O ATOM 3591 CB ARG B 195 23.822 -59.960 92.018 1.00 64.22 C ANISOU 3591 CB ARG B 195 14333 2919 7147 551 784 1643 C ATOM 3592 CG ARG B 195 23.740 -60.600 93.407 1.00 68.27 C ANISOU 3592 CG ARG B 195 15303 3169 7467 628 912 1878 C ATOM 3593 CD ARG B 195 22.374 -61.191 93.703 1.00 69.96 C ANISOU 3593 CD ARG B 195 15667 3145 7771 312 1250 1957 C ATOM 3594 NE ARG B 195 22.173 -62.472 93.025 1.00 72.51 N ANISOU 3594 NE ARG B 195 16120 3157 8274 216 1326 1917 N ATOM 3595 CZ ARG B 195 21.046 -63.176 93.050 1.00 85.00 C ANISOU 3595 CZ ARG B 195 17810 4487 9999 -75 1605 1953 C ATOM 3596 NH1 ARG B 195 19.996 -62.737 93.727 1.00 77.66 N ANISOU 3596 NH1 ARG B 195 16863 3579 9064 -296 1857 2035 N ATOM 3597 NH2 ARG B 195 20.964 -64.330 92.406 1.00 75.76 N ANISOU 3597 NH2 ARG B 195 16765 3030 8992 -150 1647 1901 N ATOM 3598 N THR B 196 24.546 -57.576 90.026 1.00 64.15 N ANISOU 3598 N THR B 196 13438 3649 7287 576 435 1263 N ATOM 3599 CA THR B 196 24.436 -56.915 88.722 1.00 63.62 C ANISOU 3599 CA THR B 196 13008 3803 7362 468 363 1067 C ATOM 3600 C THR B 196 24.468 -55.415 88.923 1.00 64.19 C ANISOU 3600 C THR B 196 12818 4209 7364 477 295 1046 C ATOM 3601 O THR B 196 24.250 -54.946 90.048 1.00 64.32 O ANISOU 3601 O THR B 196 12928 4264 7246 493 353 1173 O ATOM 3602 CB THR B 196 23.080 -57.236 88.062 1.00 73.34 C ANISOU 3602 CB THR B 196 14153 4942 8770 137 527 997 C ATOM 3603 OG1 THR B 196 22.003 -56.956 88.960 1.00 73.74 O ANISOU 3603 OG1 THR B 196 14239 4973 8806 -46 718 1113 O ATOM 3604 CG2 THR B 196 22.976 -58.615 87.674 1.00 74.48 C ANISOU 3604 CG2 THR B 196 14514 4772 9013 87 591 980 C ATOM 3605 N ARG B 197 24.687 -54.668 87.819 1.00 56.26 N ANISOU 3605 N ARG B 197 11506 3428 6443 455 188 883 N ATOM 3606 CA ARG B 197 24.617 -53.209 87.755 1.00 54.51 C ANISOU 3606 CA ARG B 197 11004 3515 6190 429 132 836 C ATOM 3607 C ARG B 197 23.355 -52.867 86.939 1.00 57.08 C ANISOU 3607 C ARG B 197 11121 3905 6660 143 225 746 C ATOM 3608 O ARG B 197 23.056 -51.701 86.708 1.00 55.48 O ANISOU 3608 O ARG B 197 10675 3937 6467 79 195 696 O ATOM 3609 CB ARG B 197 25.865 -52.622 87.096 1.00 52.97 C ANISOU 3609 CB ARG B 197 10633 3507 5987 627 -55 726 C ATOM 3610 CG ARG B 197 27.158 -52.894 87.850 1.00 60.03 C ANISOU 3610 CG ARG B 197 11671 4361 6777 920 -185 797 C ATOM 3611 CD ARG B 197 28.302 -52.451 86.978 1.00 66.54 C ANISOU 3611 CD ARG B 197 12282 5339 7661 1077 -329 661 C ATOM 3612 NE ARG B 197 29.598 -52.455 87.652 1.00 66.72 N ANISOU 3612 NE ARG B 197 12350 5376 7626 1361 -489 702 N ATOM 3613 CZ ARG B 197 30.748 -52.266 87.011 1.00 78.51 C ANISOU 3613 CZ ARG B 197 13671 6958 9199 1532 -603 593 C ATOM 3614 NH1 ARG B 197 30.761 -52.095 85.692 1.00 52.74 N ANISOU 3614 NH1 ARG B 197 10226 3768 6046 1450 -554 445 N ATOM 3615 NH2 ARG B 197 31.892 -52.256 87.679 1.00 73.16 N ANISOU 3615 NH2 ARG B 197 13007 6294 8499 1787 -766 628 N ATOM 3616 N ALA B 198 22.593 -53.917 86.547 1.00 54.70 N ANISOU 3616 N ALA B 198 10925 3377 6482 -29 329 727 N ATOM 3617 CA ALA B 198 21.347 -53.873 85.776 1.00 55.12 C ANISOU 3617 CA ALA B 198 10806 3433 6706 -310 396 636 C ATOM 3618 C ALA B 198 20.251 -53.025 86.417 1.00 61.44 C ANISOU 3618 C ALA B 198 11457 4344 7543 -476 521 699 C ATOM 3619 O ALA B 198 19.402 -52.490 85.713 1.00 61.84 O ANISOU 3619 O ALA B 198 11261 4509 7728 -653 508 606 O ATOM 3620 CB ALA B 198 20.836 -55.285 85.549 1.00 55.78 C ANISOU 3620 CB ALA B 198 11082 3204 6907 -446 493 626 C ATOM 3621 N PHE B 199 20.254 -52.929 87.752 1.00 59.26 N ANISOU 3621 N PHE B 199 11345 4024 7147 -411 642 857 N ATOM 3622 CA PHE B 199 19.259 -52.180 88.518 1.00 57.79 C ANISOU 3622 CA PHE B 199 11060 3917 6982 -548 805 928 C ATOM 3623 C PHE B 199 19.898 -50.996 89.239 1.00 62.29 C ANISOU 3623 C PHE B 199 11592 4710 7365 -370 739 978 C ATOM 3624 O PHE B 199 19.337 -50.495 90.219 1.00 63.33 O ANISOU 3624 O PHE B 199 11755 4866 7441 -417 894 1071 O ATOM 3625 CB PHE B 199 18.487 -53.120 89.460 1.00 58.29 C ANISOU 3625 CB PHE B 199 11372 3703 7072 -677 1061 1063 C ATOM 3626 CG PHE B 199 17.991 -54.363 88.757 1.00 59.26 C ANISOU 3626 CG PHE B 199 11555 3578 7383 -846 1112 1006 C ATOM 3627 CD1 PHE B 199 16.879 -54.315 87.926 1.00 61.83 C ANISOU 3627 CD1 PHE B 199 11618 3915 7960 -1107 1147 890 C ATOM 3628 CD2 PHE B 199 18.655 -55.580 88.906 1.00 60.72 C ANISOU 3628 CD2 PHE B 199 12057 3511 7501 -739 1105 1060 C ATOM 3629 CE1 PHE B 199 16.439 -55.461 87.261 1.00 62.32 C ANISOU 3629 CE1 PHE B 199 11738 3742 8198 -1273 1171 820 C ATOM 3630 CE2 PHE B 199 18.221 -56.722 88.229 1.00 63.19 C ANISOU 3630 CE2 PHE B 199 12437 3581 7990 -898 1149 993 C ATOM 3631 CZ PHE B 199 17.125 -56.651 87.405 1.00 61.37 C ANISOU 3631 CZ PHE B 199 11947 3369 8003 -1170 1178 869 C ATOM 3632 N SER B 200 21.068 -50.537 88.718 1.00 57.24 N ANISOU 3632 N SER B 200 10878 4227 6642 -174 518 905 N ATOM 3633 CA SER B 200 21.858 -49.418 89.227 1.00 56.24 C ANISOU 3633 CA SER B 200 10692 4316 6361 2 409 921 C ATOM 3634 C SER B 200 21.570 -48.152 88.435 1.00 63.09 C ANISOU 3634 C SER B 200 11222 5438 7310 -71 341 808 C ATOM 3635 O SER B 200 21.251 -48.208 87.258 1.00 62.22 O ANISOU 3635 O SER B 200 10944 5360 7339 -175 289 696 O ATOM 3636 CB SER B 200 23.349 -49.740 89.219 1.00 57.38 C ANISOU 3636 CB SER B 200 10954 4453 6394 262 222 915 C ATOM 3637 OG SER B 200 23.722 -50.549 90.328 1.00 62.63 O ANISOU 3637 OG SER B 200 11952 4924 6921 387 255 1054 O ATOM 3638 N VAL B 201 21.611 -47.010 89.112 1.00 62.34 N ANISOU 3638 N VAL B 201 11055 5512 7121 -22 344 840 N ATOM 3639 CA VAL B 201 21.316 -45.699 88.542 1.00 62.10 C ANISOU 3639 CA VAL B 201 10731 5713 7153 -78 295 754 C ATOM 3640 C VAL B 201 22.385 -44.739 89.051 1.00 64.28 C ANISOU 3640 C VAL B 201 10998 6152 7272 112 170 757 C ATOM 3641 O VAL B 201 22.773 -44.827 90.211 1.00 63.39 O ANISOU 3641 O VAL B 201 11092 5988 7005 220 191 850 O ATOM 3642 CB VAL B 201 19.864 -45.280 88.945 1.00 66.20 C ANISOU 3642 CB VAL B 201 11147 6232 7772 -273 490 790 C ATOM 3643 CG1 VAL B 201 19.630 -43.784 88.824 1.00 65.78 C ANISOU 3643 CG1 VAL B 201 10848 6407 7739 -282 455 738 C ATOM 3644 CG2 VAL B 201 18.816 -46.053 88.142 1.00 66.08 C ANISOU 3644 CG2 VAL B 201 11047 6089 7971 -482 563 745 C ATOM 3645 N CYS B 202 22.890 -43.862 88.174 1.00 60.98 N ANISOU 3645 N CYS B 202 10361 5918 6893 153 36 652 N ATOM 3646 CA CYS B 202 23.879 -42.861 88.552 1.00 60.64 C ANISOU 3646 CA CYS B 202 10265 6034 6743 305 -83 634 C ATOM 3647 C CYS B 202 23.172 -41.520 88.706 1.00 62.19 C ANISOU 3647 C CYS B 202 10288 6384 6955 218 -24 619 C ATOM 3648 O CYS B 202 22.852 -40.877 87.722 1.00 62.96 O ANISOU 3648 O CYS B 202 10172 6593 7158 142 -54 541 O ATOM 3649 CB CYS B 202 25.015 -42.794 87.535 1.00 61.20 C ANISOU 3649 CB CYS B 202 10221 6181 6851 414 -241 532 C ATOM 3650 SG CYS B 202 26.295 -41.568 87.914 1.00 65.27 S ANISOU 3650 SG CYS B 202 10629 6882 7287 583 -389 490 S ATOM 3651 N ASP B 203 22.855 -41.140 89.927 1.00 56.44 N ANISOU 3651 N ASP B 203 9675 5648 6121 228 69 697 N ATOM 3652 CA ASP B 203 22.194 -39.866 90.172 1.00 55.19 C ANISOU 3652 CA ASP B 203 9372 5619 5978 161 142 683 C ATOM 3653 C ASP B 203 22.884 -39.071 91.271 1.00 53.75 C ANISOU 3653 C ASP B 203 9298 5507 5616 291 92 705 C ATOM 3654 O ASP B 203 23.852 -39.533 91.858 1.00 51.68 O ANISOU 3654 O ASP B 203 9218 5197 5222 433 -18 735 O ATOM 3655 CB ASP B 203 20.673 -40.033 90.431 1.00 57.75 C ANISOU 3655 CB ASP B 203 9678 5860 6404 -14 367 733 C ATOM 3656 CG ASP B 203 19.851 -38.754 90.181 1.00 74.25 C ANISOU 3656 CG ASP B 203 11529 8086 8596 -99 428 689 C ATOM 3657 OD1 ASP B 203 20.332 -37.862 89.413 1.00 71.59 O ANISOU 3657 OD1 ASP B 203 11016 7898 8288 -57 286 610 O ATOM 3658 OD2 ASP B 203 18.736 -38.640 90.748 1.00 87.54 O ANISOU 3658 OD2 ASP B 203 13203 9717 10340 -202 630 735 O ATOM 3659 N GLU B 204 22.422 -37.854 91.501 1.00 49.67 N ANISOU 3659 N GLU B 204 8665 5105 5103 250 150 681 N ATOM 3660 CA GLU B 204 22.943 -36.986 92.537 1.00 48.90 C ANISOU 3660 CA GLU B 204 8670 5072 4838 350 111 685 C ATOM 3661 C GLU B 204 22.378 -37.417 93.881 1.00 53.68 C ANISOU 3661 C GLU B 204 9561 5547 5289 346 282 789 C ATOM 3662 O GLU B 204 21.174 -37.683 93.999 1.00 51.99 O ANISOU 3662 O GLU B 204 9346 5253 5154 214 507 838 O ATOM 3663 CB GLU B 204 22.529 -35.541 92.281 1.00 49.42 C ANISOU 3663 CB GLU B 204 8525 5280 4973 298 142 619 C ATOM 3664 CG GLU B 204 23.026 -34.957 90.981 1.00 56.00 C ANISOU 3664 CG GLU B 204 9103 6236 5939 295 2 525 C ATOM 3665 CD GLU B 204 22.366 -33.629 90.670 1.00 74.10 C ANISOU 3665 CD GLU B 204 11203 8635 8319 228 61 481 C ATOM 3666 OE1 GLU B 204 21.724 -33.063 91.587 1.00 54.21 O ANISOU 3666 OE1 GLU B 204 8746 6105 5745 209 195 510 O ATOM 3667 OE2 GLU B 204 22.479 -33.161 89.511 1.00 65.62 O ANISOU 3667 OE2 GLU B 204 9933 7642 7360 201 -17 420 O ATOM 3668 N ARG B 205 23.244 -37.446 94.894 1.00 52.90 N ANISOU 3668 N ARG B 205 9705 5425 4972 489 176 820 N ATOM 3669 CA ARG B 205 22.882 -37.763 96.268 1.00 54.39 C ANISOU 3669 CA ARG B 205 10231 5489 4948 513 318 922 C ATOM 3670 C ARG B 205 22.916 -36.477 97.079 1.00 58.25 C ANISOU 3670 C ARG B 205 10762 6072 5296 549 328 882 C ATOM 3671 O ARG B 205 23.944 -35.800 97.120 1.00 56.97 O ANISOU 3671 O ARG B 205 10557 6018 5071 658 98 807 O ATOM 3672 CB ARG B 205 23.825 -38.820 96.867 1.00 57.09 C ANISOU 3672 CB ARG B 205 10870 5709 5113 665 165 993 C ATOM 3673 CG ARG B 205 23.296 -39.479 98.147 1.00 73.97 C ANISOU 3673 CG ARG B 205 13409 7665 7030 671 352 1129 C ATOM 3674 CD ARG B 205 22.534 -40.768 97.876 1.00 93.55 C ANISOU 3674 CD ARG B 205 15969 9963 9615 563 547 1220 C ATOM 3675 NE ARG B 205 23.425 -41.914 97.673 1.00107.72 N ANISOU 3675 NE ARG B 205 17894 11649 11385 685 360 1258 N ATOM 3676 CZ ARG B 205 23.016 -43.137 97.347 1.00123.13 C ANISOU 3676 CZ ARG B 205 19928 13426 13429 616 474 1326 C ATOM 3677 NH1 ARG B 205 21.722 -43.389 97.174 1.00104.44 N ANISOU 3677 NH1 ARG B 205 17506 10976 11200 414 766 1359 N ATOM 3678 NH2 ARG B 205 23.896 -44.117 97.185 1.00113.85 N ANISOU 3678 NH2 ARG B 205 18879 12150 12230 750 294 1355 N ATOM 3679 N TRP B 206 21.774 -36.135 97.697 1.00 55.99 N ANISOU 3679 N TRP B 206 10550 5741 4984 452 607 923 N ATOM 3680 CA TRP B 206 21.622 -34.945 98.532 1.00 55.95 C ANISOU 3680 CA TRP B 206 10620 5799 4841 475 673 885 C ATOM 3681 C TRP B 206 21.099 -35.344 99.892 1.00 65.47 C ANISOU 3681 C TRP B 206 12218 6854 5805 483 899 988 C ATOM 3682 O TRP B 206 20.120 -36.087 99.981 1.00 66.13 O ANISOU 3682 O TRP B 206 12359 6810 5958 374 1169 1073 O ATOM 3683 CB TRP B 206 20.678 -33.911 97.881 1.00 53.06 C ANISOU 3683 CB TRP B 206 9927 5532 4702 355 823 815 C ATOM 3684 CG TRP B 206 21.166 -33.388 96.568 1.00 53.06 C ANISOU 3684 CG TRP B 206 9582 5674 4904 349 615 719 C ATOM 3685 CD1 TRP B 206 20.759 -33.782 95.326 1.00 55.89 C ANISOU 3685 CD1 TRP B 206 9681 6050 5504 259 610 707 C ATOM 3686 CD2 TRP B 206 22.119 -32.334 96.364 1.00 52.44 C ANISOU 3686 CD2 TRP B 206 9395 5729 4800 428 399 620 C ATOM 3687 NE1 TRP B 206 21.412 -33.049 94.359 1.00 55.06 N ANISOU 3687 NE1 TRP B 206 9339 6080 5502 285 416 615 N ATOM 3688 CE2 TRP B 206 22.254 -32.153 94.969 1.00 56.02 C ANISOU 3688 CE2 TRP B 206 9536 6272 5477 383 294 562 C ATOM 3689 CE3 TRP B 206 22.876 -31.523 97.226 1.00 53.04 C ANISOU 3689 CE3 TRP B 206 9618 5848 4685 525 282 569 C ATOM 3690 CZ2 TRP B 206 23.127 -31.206 94.418 1.00 54.79 C ANISOU 3690 CZ2 TRP B 206 9213 6239 5365 429 107 466 C ATOM 3691 CZ3 TRP B 206 23.747 -30.595 96.677 1.00 53.81 C ANISOU 3691 CZ3 TRP B 206 9525 6071 4850 564 76 463 C ATOM 3692 CH2 TRP B 206 23.874 -30.451 95.290 1.00 54.18 C ANISOU 3692 CH2 TRP B 206 9262 6198 5127 515 5 418 C ATOM 3693 N ALA B 207 21.744 -34.837 100.956 1.00 65.58 N ANISOU 3693 N ALA B 207 12512 6873 5531 606 792 976 N ATOM 3694 CA ALA B 207 21.372 -35.090 102.351 1.00 66.18 C ANISOU 3694 CA ALA B 207 13033 6807 5307 638 987 1068 C ATOM 3695 C ALA B 207 20.080 -34.355 102.710 1.00 73.09 C ANISOU 3695 C ALA B 207 13873 7667 6230 517 1364 1060 C ATOM 3696 O ALA B 207 19.291 -34.869 103.496 1.00 73.92 O ANISOU 3696 O ALA B 207 14247 7619 6219 467 1674 1159 O ATOM 3697 CB ALA B 207 22.495 -34.650 103.277 1.00 66.71 C ANISOU 3697 CB ALA B 207 13388 6901 5057 808 709 1031 C ATOM 3698 N ASP B 208 19.863 -33.158 102.136 1.00 70.30 N ANISOU 3698 N ASP B 208 13193 7460 6057 475 1352 943 N ATOM 3699 CA ASP B 208 18.672 -32.357 102.411 1.00 69.99 C ANISOU 3699 CA ASP B 208 13076 7414 6102 382 1692 919 C ATOM 3700 C ASP B 208 17.990 -31.820 101.136 1.00 71.98 C ANISOU 3700 C ASP B 208 12828 7773 6749 271 1736 852 C ATOM 3701 O ASP B 208 18.539 -31.929 100.044 1.00 69.22 O ANISOU 3701 O ASP B 208 12218 7515 6568 272 1486 813 O ATOM 3702 CB ASP B 208 18.990 -31.236 103.415 1.00 72.13 C ANISOU 3702 CB ASP B 208 13579 7718 6111 472 1676 846 C ATOM 3703 CG ASP B 208 19.897 -30.152 102.878 1.00 83.97 C ANISOU 3703 CG ASP B 208 14855 9383 7669 534 1354 710 C ATOM 3704 OD1 ASP B 208 21.133 -30.297 103.001 1.00 85.77 O ANISOU 3704 OD1 ASP B 208 15191 9650 7749 641 1014 683 O ATOM 3705 OD2 ASP B 208 19.373 -29.155 102.348 1.00 88.76 O ANISOU 3705 OD2 ASP B 208 15177 10070 8479 477 1446 632 O ATOM 3706 N ASP B 209 16.772 -31.275 101.304 1.00 70.16 N ANISOU 3706 N ASP B 209 12483 7517 6658 183 2064 843 N ATOM 3707 CA ASP B 209 15.891 -30.731 100.273 1.00 70.52 C ANISOU 3707 CA ASP B 209 12082 7637 7073 85 2144 789 C ATOM 3708 C ASP B 209 16.318 -29.347 99.776 1.00 72.51 C ANISOU 3708 C ASP B 209 12123 8041 7388 143 1950 672 C ATOM 3709 O ASP B 209 15.991 -28.989 98.638 1.00 73.90 O ANISOU 3709 O ASP B 209 11932 8300 7846 93 1872 629 O ATOM 3710 CB ASP B 209 14.442 -30.639 100.813 1.00 73.54 C ANISOU 3710 CB ASP B 209 12436 7919 7587 -13 2584 822 C ATOM 3711 CG ASP B 209 13.778 -31.948 101.222 1.00 92.62 C ANISOU 3711 CG ASP B 209 15009 10166 10014 -110 2849 939 C ATOM 3712 OD1 ASP B 209 13.927 -32.952 100.482 1.00 95.70 O ANISOU 3712 OD1 ASP B 209 15296 10535 10531 -167 2716 980 O ATOM 3713 OD2 ASP B 209 13.083 -31.962 102.271 1.00100.01 O ANISOU 3713 OD2 ASP B 209 16178 10981 10841 -135 3210 986 O ATOM 3714 N LEU B 210 17.023 -28.564 100.625 1.00 64.73 N ANISOU 3714 N LEU B 210 11381 7077 6136 246 1870 618 N ATOM 3715 CA LEU B 210 17.438 -27.192 100.316 1.00 62.05 C ANISOU 3715 CA LEU B 210 10887 6853 5837 296 1716 503 C ATOM 3716 C LEU B 210 18.675 -27.087 99.402 1.00 62.65 C ANISOU 3716 C LEU B 210 10811 7045 5949 341 1326 450 C ATOM 3717 O LEU B 210 18.633 -26.317 98.440 1.00 63.48 O ANISOU 3717 O LEU B 210 10614 7240 6265 318 1239 389 O ATOM 3718 CB LEU B 210 17.634 -26.399 101.622 1.00 61.55 C ANISOU 3718 CB LEU B 210 11153 6748 5484 372 1803 452 C ATOM 3719 CG LEU B 210 17.739 -24.870 101.558 1.00 65.61 C ANISOU 3719 CG LEU B 210 11549 7336 6044 406 1755 329 C ATOM 3720 CD1 LEU B 210 16.516 -24.233 100.907 1.00 65.39 C ANISOU 3720 CD1 LEU B 210 11186 7318 6341 341 1989 315 C ATOM 3721 CD2 LEU B 210 17.931 -24.297 102.936 1.00 66.81 C ANISOU 3721 CD2 LEU B 210 12090 7423 5871 477 1838 278 C ATOM 3722 N ALA B 211 19.760 -27.833 99.690 1.00 55.67 N ANISOU 3722 N ALA B 211 10132 6151 4870 409 1102 473 N ATOM 3723 CA ALA B 211 20.994 -27.801 98.887 1.00 54.20 C ANISOU 3723 CA ALA B 211 9799 6063 4730 457 757 418 C ATOM 3724 C ALA B 211 20.786 -28.069 97.352 1.00 55.40 C ANISOU 3724 C ALA B 211 9587 6279 5184 384 699 422 C ATOM 3725 O ALA B 211 21.313 -27.270 96.573 1.00 55.53 O ANISOU 3725 O ALA B 211 9395 6393 5311 392 540 344 O ATOM 3726 CB ALA B 211 22.034 -28.738 99.467 1.00 54.86 C ANISOU 3726 CB ALA B 211 10149 6103 4592 550 555 456 C ATOM 3727 N PRO B 212 20.005 -29.100 96.879 1.00 48.18 N ANISOU 3727 N PRO B 212 8595 5304 4406 306 831 502 N ATOM 3728 CA PRO B 212 19.803 -29.252 95.423 1.00 46.37 C ANISOU 3728 CA PRO B 212 8045 5134 4437 239 752 487 C ATOM 3729 C PRO B 212 19.060 -28.066 94.808 1.00 49.69 C ANISOU 3729 C PRO B 212 8205 5623 5054 192 826 434 C ATOM 3730 O PRO B 212 19.324 -27.718 93.663 1.00 49.87 O ANISOU 3730 O PRO B 212 8005 5723 5218 179 678 394 O ATOM 3731 CB PRO B 212 19.006 -30.562 95.306 1.00 47.72 C ANISOU 3731 CB PRO B 212 8239 5201 4690 157 898 575 C ATOM 3732 CG PRO B 212 18.368 -30.751 96.630 1.00 51.59 C ANISOU 3732 CG PRO B 212 8983 5581 5036 150 1154 636 C ATOM 3733 CD PRO B 212 19.294 -30.168 97.626 1.00 47.91 C ANISOU 3733 CD PRO B 212 8776 5134 4294 267 1052 604 C ATOM 3734 N LYS B 213 18.162 -27.427 95.573 1.00 45.92 N ANISOU 3734 N LYS B 213 7767 5105 4574 177 1057 435 N ATOM 3735 CA LYS B 213 17.429 -26.240 95.124 1.00 46.29 C ANISOU 3735 CA LYS B 213 7582 5198 4806 156 1136 386 C ATOM 3736 C LYS B 213 18.372 -25.035 94.949 1.00 49.33 C ANISOU 3736 C LYS B 213 7949 5667 5127 225 953 300 C ATOM 3737 O LYS B 213 18.245 -24.304 93.962 1.00 48.51 O ANISOU 3737 O LYS B 213 7613 5622 5195 212 879 266 O ATOM 3738 CB LYS B 213 16.284 -25.875 96.097 1.00 49.01 C ANISOU 3738 CB LYS B 213 7991 5464 5166 137 1457 402 C ATOM 3739 CG LYS B 213 15.118 -26.849 96.072 1.00 59.81 C ANISOU 3739 CG LYS B 213 9281 6748 6697 40 1679 476 C ATOM 3740 CD LYS B 213 14.128 -26.548 97.189 1.00 65.31 C ANISOU 3740 CD LYS B 213 10088 7351 7377 29 2035 491 C ATOM 3741 CE LYS B 213 12.963 -27.505 97.183 1.00 74.52 C ANISOU 3741 CE LYS B 213 11153 8421 8740 -84 2282 559 C ATOM 3742 NZ LYS B 213 12.081 -27.311 98.364 1.00 90.24 N ANISOU 3742 NZ LYS B 213 13280 10306 10700 -96 2672 576 N ATOM 3743 N ILE B 214 19.309 -24.822 95.907 1.00 44.88 N ANISOU 3743 N ILE B 214 7637 5097 4319 295 874 264 N ATOM 3744 CA ILE B 214 20.278 -23.721 95.819 1.00 44.14 C ANISOU 3744 CA ILE B 214 7530 5069 4174 346 694 171 C ATOM 3745 C ILE B 214 21.284 -23.986 94.680 1.00 45.80 C ANISOU 3745 C ILE B 214 7581 5356 4467 345 441 153 C ATOM 3746 O ILE B 214 21.541 -23.095 93.877 1.00 45.44 O ANISOU 3746 O ILE B 214 7362 5365 4538 336 360 101 O ATOM 3747 CB ILE B 214 20.951 -23.392 97.186 1.00 47.26 C ANISOU 3747 CB ILE B 214 8233 5429 4293 415 661 121 C ATOM 3748 CG1 ILE B 214 19.917 -22.846 98.202 1.00 47.90 C ANISOU 3748 CG1 ILE B 214 8467 5433 4300 416 946 119 C ATOM 3749 CG2 ILE B 214 22.074 -22.382 97.018 1.00 47.14 C ANISOU 3749 CG2 ILE B 214 8176 5476 4257 449 439 13 C ATOM 3750 CD1 ILE B 214 20.298 -23.070 99.633 1.00 47.81 C ANISOU 3750 CD1 ILE B 214 8844 5355 3969 476 965 109 C ATOM 3751 N TYR B 215 21.812 -25.214 94.612 1.00 40.63 N ANISOU 3751 N TYR B 215 6998 4688 3751 357 343 198 N ATOM 3752 CA TYR B 215 22.790 -25.650 93.630 1.00 40.79 C ANISOU 3752 CA TYR B 215 6898 4764 3837 367 135 181 C ATOM 3753 C TYR B 215 22.260 -25.577 92.188 1.00 46.99 C ANISOU 3753 C TYR B 215 7427 5588 4841 301 147 193 C ATOM 3754 O TYR B 215 22.963 -25.061 91.310 1.00 46.97 O ANISOU 3754 O TYR B 215 7291 5645 4910 304 22 143 O ATOM 3755 CB TYR B 215 23.357 -27.080 93.963 1.00 40.92 C ANISOU 3755 CB TYR B 215 7071 4733 3745 409 52 234 C ATOM 3756 CG TYR B 215 24.373 -27.544 92.934 1.00 40.67 C ANISOU 3756 CG TYR B 215 6905 4751 3799 430 -139 207 C ATOM 3757 CD1 TYR B 215 25.661 -27.010 92.908 1.00 41.96 C ANISOU 3757 CD1 TYR B 215 7032 4970 3940 489 -327 125 C ATOM 3758 CD2 TYR B 215 24.009 -28.418 91.907 1.00 40.43 C ANISOU 3758 CD2 TYR B 215 6761 4706 3894 381 -117 249 C ATOM 3759 CE1 TYR B 215 26.570 -27.361 91.911 1.00 42.53 C ANISOU 3759 CE1 TYR B 215 6958 5082 4118 505 -459 92 C ATOM 3760 CE2 TYR B 215 24.909 -28.767 90.896 1.00 40.26 C ANISOU 3760 CE2 TYR B 215 6623 4724 3950 401 -260 214 C ATOM 3761 CZ TYR B 215 26.191 -28.244 90.908 1.00 47.40 C ANISOU 3761 CZ TYR B 215 7492 5683 4836 466 -415 138 C ATOM 3762 OH TYR B 215 27.104 -28.602 89.942 1.00 48.11 O ANISOU 3762 OH TYR B 215 7461 5802 5015 489 -521 100 O ATOM 3763 N HIS B 216 21.048 -26.127 91.943 1.00 44.02 N ANISOU 3763 N HIS B 216 6990 5168 4566 239 293 256 N ATOM 3764 CA HIS B 216 20.464 -26.160 90.614 1.00 44.65 C ANISOU 3764 CA HIS B 216 6851 5275 4839 179 276 267 C ATOM 3765 C HIS B 216 19.990 -24.804 90.128 1.00 48.84 C ANISOU 3765 C HIS B 216 7226 5845 5486 172 302 233 C ATOM 3766 O HIS B 216 19.918 -24.599 88.914 1.00 48.93 O ANISOU 3766 O HIS B 216 7085 5893 5614 148 217 228 O ATOM 3767 CB HIS B 216 19.396 -27.235 90.502 1.00 45.88 C ANISOU 3767 CB HIS B 216 6981 5366 5087 108 390 331 C ATOM 3768 CG HIS B 216 20.040 -28.566 90.310 1.00 49.83 C ANISOU 3768 CG HIS B 216 7579 5832 5524 110 300 357 C ATOM 3769 ND1 HIS B 216 20.194 -29.454 91.369 1.00 52.24 N ANISOU 3769 ND1 HIS B 216 8103 6058 5688 134 366 404 N ATOM 3770 CD2 HIS B 216 20.677 -29.062 89.225 1.00 50.99 C ANISOU 3770 CD2 HIS B 216 7660 6006 5710 109 150 337 C ATOM 3771 CE1 HIS B 216 20.882 -30.465 90.880 1.00 51.06 C ANISOU 3771 CE1 HIS B 216 7995 5888 5519 150 246 413 C ATOM 3772 NE2 HIS B 216 21.206 -30.264 89.598 1.00 51.25 N ANISOU 3772 NE2 HIS B 216 7847 5975 5649 135 121 367 N ATOM 3773 N SER B 217 19.742 -23.865 91.061 1.00 45.11 N ANISOU 3773 N SER B 217 6819 5356 4964 202 410 208 N ATOM 3774 CA SER B 217 19.424 -22.460 90.785 1.00 43.87 C ANISOU 3774 CA SER B 217 6552 5218 4899 216 437 170 C ATOM 3775 C SER B 217 20.710 -21.758 90.304 1.00 47.93 C ANISOU 3775 C SER B 217 7063 5783 5365 243 268 110 C ATOM 3776 O SER B 217 20.677 -21.061 89.290 1.00 49.28 O ANISOU 3776 O SER B 217 7101 5978 5645 233 215 102 O ATOM 3777 CB SER B 217 18.891 -21.780 92.044 1.00 45.01 C ANISOU 3777 CB SER B 217 6809 5312 4982 246 618 150 C ATOM 3778 OG SER B 217 17.589 -22.261 92.334 1.00 47.00 O ANISOU 3778 OG SER B 217 7011 5512 5338 212 813 202 O ATOM 3779 N CYS B 218 21.850 -21.967 91.011 1.00 43.62 N ANISOU 3779 N CYS B 218 6666 5246 4663 276 180 68 N ATOM 3780 CA CYS B 218 23.158 -21.410 90.641 1.00 42.99 C ANISOU 3780 CA CYS B 218 6563 5208 4565 290 25 -1 C ATOM 3781 C CYS B 218 23.618 -21.981 89.329 1.00 45.13 C ANISOU 3781 C CYS B 218 6710 5517 4921 266 -73 19 C ATOM 3782 O CYS B 218 24.014 -21.227 88.465 1.00 45.71 O ANISOU 3782 O CYS B 218 6684 5612 5071 250 -114 -8 O ATOM 3783 CB CYS B 218 24.199 -21.639 91.728 1.00 43.67 C ANISOU 3783 CB CYS B 218 6814 5290 4488 336 -72 -53 C ATOM 3784 SG CYS B 218 23.848 -20.779 93.273 1.00 48.27 S ANISOU 3784 SG CYS B 218 7593 5821 4925 368 24 -103 S ATOM 3785 N PHE B 219 23.545 -23.313 89.173 1.00 40.56 N ANISOU 3785 N PHE B 219 6157 4931 4322 263 -94 66 N ATOM 3786 CA PHE B 219 23.931 -24.045 87.974 1.00 38.49 C ANISOU 3786 CA PHE B 219 5812 4690 4120 245 -171 79 C ATOM 3787 C PHE B 219 23.239 -23.490 86.735 1.00 40.16 C ANISOU 3787 C PHE B 219 5892 4914 4451 201 -150 100 C ATOM 3788 O PHE B 219 23.894 -23.233 85.728 1.00 38.87 O ANISOU 3788 O PHE B 219 5673 4777 4320 193 -213 78 O ATOM 3789 CB PHE B 219 23.629 -25.560 88.139 1.00 39.94 C ANISOU 3789 CB PHE B 219 6068 4835 4270 242 -162 132 C ATOM 3790 CG PHE B 219 24.279 -26.394 87.054 1.00 40.67 C ANISOU 3790 CG PHE B 219 6116 4939 4397 239 -252 126 C ATOM 3791 CD1 PHE B 219 23.631 -26.618 85.841 1.00 43.17 C ANISOU 3791 CD1 PHE B 219 6344 5254 4802 185 -246 147 C ATOM 3792 CD2 PHE B 219 25.550 -26.928 87.234 1.00 42.42 C ANISOU 3792 CD2 PHE B 219 6387 5166 4567 298 -349 90 C ATOM 3793 CE1 PHE B 219 24.236 -27.379 84.836 1.00 44.39 C ANISOU 3793 CE1 PHE B 219 6489 5408 4967 185 -313 130 C ATOM 3794 CE2 PHE B 219 26.152 -27.696 86.230 1.00 45.47 C ANISOU 3794 CE2 PHE B 219 6732 5551 4992 304 -403 76 C ATOM 3795 CZ PHE B 219 25.497 -27.902 85.032 1.00 43.36 C ANISOU 3795 CZ PHE B 219 6405 5279 4791 245 -374 94 C ATOM 3796 N PHE B 220 21.918 -23.301 86.816 1.00 37.38 N ANISOU 3796 N PHE B 220 5497 4538 4169 177 -58 142 N ATOM 3797 CA PHE B 220 21.117 -22.784 85.711 1.00 37.39 C ANISOU 3797 CA PHE B 220 5376 4543 4289 151 -68 167 C ATOM 3798 C PHE B 220 21.526 -21.372 85.320 1.00 41.12 C ANISOU 3798 C PHE B 220 5817 5027 4780 171 -84 138 C ATOM 3799 O PHE B 220 21.705 -21.110 84.134 1.00 41.11 O ANISOU 3799 O PHE B 220 5774 5036 4811 160 -149 147 O ATOM 3800 CB PHE B 220 19.612 -22.856 86.046 1.00 39.19 C ANISOU 3800 CB PHE B 220 5533 4735 4622 130 32 209 C ATOM 3801 CG PHE B 220 18.699 -22.205 85.035 1.00 40.79 C ANISOU 3801 CG PHE B 220 5597 4937 4964 124 -5 232 C ATOM 3802 CD1 PHE B 220 18.590 -22.715 83.737 1.00 44.56 C ANISOU 3802 CD1 PHE B 220 6027 5426 5476 93 -129 248 C ATOM 3803 CD2 PHE B 220 17.972 -21.068 85.363 1.00 41.67 C ANISOU 3803 CD2 PHE B 220 5641 5027 5164 158 71 235 C ATOM 3804 CE1 PHE B 220 17.790 -22.076 82.778 1.00 44.88 C ANISOU 3804 CE1 PHE B 220 5966 5462 5625 101 -202 271 C ATOM 3805 CE2 PHE B 220 17.155 -20.441 84.412 1.00 44.54 C ANISOU 3805 CE2 PHE B 220 5879 5382 5661 173 8 261 C ATOM 3806 CZ PHE B 220 17.067 -20.951 83.125 1.00 42.90 C ANISOU 3806 CZ PHE B 220 5635 5190 5474 145 -141 282 C ATOM 3807 N ILE B 221 21.681 -20.465 86.307 1.00 37.76 N ANISOU 3807 N ILE B 221 5436 4587 4325 198 -22 102 N ATOM 3808 CA ILE B 221 22.016 -19.056 86.060 1.00 36.74 C ANISOU 3808 CA ILE B 221 5290 4445 4226 210 -20 70 C ATOM 3809 C ILE B 221 23.455 -18.903 85.542 1.00 41.17 C ANISOU 3809 C ILE B 221 5867 5029 4747 195 -99 24 C ATOM 3810 O ILE B 221 23.676 -18.160 84.601 1.00 41.04 O ANISOU 3810 O ILE B 221 5817 5000 4776 181 -111 30 O ATOM 3811 CB ILE B 221 21.692 -18.203 87.320 1.00 39.45 C ANISOU 3811 CB ILE B 221 5691 4750 4549 240 80 33 C ATOM 3812 CG1 ILE B 221 20.159 -18.097 87.539 1.00 39.17 C ANISOU 3812 CG1 ILE B 221 5592 4679 4612 258 194 81 C ATOM 3813 CG2 ILE B 221 22.349 -16.822 87.279 1.00 39.57 C ANISOU 3813 CG2 ILE B 221 5723 4737 4574 244 73 -23 C ATOM 3814 CD1 ILE B 221 19.738 -17.815 88.967 1.00 52.69 C ANISOU 3814 CD1 ILE B 221 7396 6351 6274 286 336 50 C ATOM 3815 N VAL B 222 24.399 -19.660 86.096 1.00 39.16 N ANISOU 3815 N VAL B 222 5660 4799 4418 199 -150 -17 N ATOM 3816 CA VAL B 222 25.833 -19.618 85.768 1.00 39.55 C ANISOU 3816 CA VAL B 222 5693 4870 4464 189 -219 -76 C ATOM 3817 C VAL B 222 26.176 -20.311 84.424 1.00 44.73 C ANISOU 3817 C VAL B 222 6304 5545 5147 170 -246 -49 C ATOM 3818 O VAL B 222 26.979 -19.789 83.652 1.00 44.93 O ANISOU 3818 O VAL B 222 6292 5567 5212 147 -240 -76 O ATOM 3819 CB VAL B 222 26.631 -20.178 86.975 1.00 43.40 C ANISOU 3819 CB VAL B 222 6246 5372 4873 222 -286 -131 C ATOM 3820 CG1 VAL B 222 28.052 -20.595 86.605 1.00 43.57 C ANISOU 3820 CG1 VAL B 222 6212 5421 4924 225 -374 -187 C ATOM 3821 CG2 VAL B 222 26.627 -19.176 88.133 1.00 42.96 C ANISOU 3821 CG2 VAL B 222 6258 5290 4776 231 -271 -188 C ATOM 3822 N THR B 223 25.581 -21.471 84.143 1.00 41.88 N ANISOU 3822 N THR B 223 5958 5190 4765 175 -261 0 N ATOM 3823 CA THR B 223 25.860 -22.189 82.897 1.00 40.69 C ANISOU 3823 CA THR B 223 5795 5046 4619 160 -286 14 C ATOM 3824 C THR B 223 24.923 -21.825 81.758 1.00 43.66 C ANISOU 3824 C THR B 223 6163 5407 5021 134 -278 68 C ATOM 3825 O THR B 223 25.248 -22.112 80.613 1.00 42.89 O ANISOU 3825 O THR B 223 6087 5306 4904 120 -293 71 O ATOM 3826 CB THR B 223 25.867 -23.702 83.129 1.00 43.58 C ANISOU 3826 CB THR B 223 6200 5411 4948 177 -322 24 C ATOM 3827 OG1 THR B 223 24.513 -24.136 83.293 1.00 41.61 O ANISOU 3827 OG1 THR B 223 5962 5141 4709 158 -305 81 O ATOM 3828 CG2 THR B 223 26.778 -24.126 84.313 1.00 38.57 C ANISOU 3828 CG2 THR B 223 5598 4783 4275 225 -361 -19 C ATOM 3829 N TYR B 224 23.746 -21.245 82.054 1.00 40.90 N ANISOU 3829 N TYR B 224 5788 5041 4712 136 -260 108 N ATOM 3830 CA TYR B 224 22.783 -20.931 81.008 1.00 40.30 C ANISOU 3830 CA TYR B 224 5692 4946 4672 128 -294 160 C ATOM 3831 C TYR B 224 22.270 -19.454 80.970 1.00 44.42 C ANISOU 3831 C TYR B 224 6190 5436 5250 150 -265 184 C ATOM 3832 O TYR B 224 22.561 -18.731 80.018 1.00 43.21 O ANISOU 3832 O TYR B 224 6076 5259 5081 150 -276 201 O ATOM 3833 CB TYR B 224 21.591 -21.923 81.084 1.00 40.84 C ANISOU 3833 CB TYR B 224 5723 5011 4785 113 -329 194 C ATOM 3834 CG TYR B 224 20.684 -21.849 79.878 1.00 42.95 C ANISOU 3834 CG TYR B 224 5966 5263 5091 104 -418 234 C ATOM 3835 CD1 TYR B 224 20.977 -22.563 78.716 1.00 44.36 C ANISOU 3835 CD1 TYR B 224 6212 5440 5202 81 -498 229 C ATOM 3836 CD2 TYR B 224 19.581 -20.990 79.859 1.00 43.77 C ANISOU 3836 CD2 TYR B 224 5990 5345 5295 129 -432 271 C ATOM 3837 CE1 TYR B 224 20.189 -22.439 77.571 1.00 44.90 C ANISOU 3837 CE1 TYR B 224 6292 5490 5279 78 -611 261 C ATOM 3838 CE2 TYR B 224 18.799 -20.842 78.716 1.00 44.71 C ANISOU 3838 CE2 TYR B 224 6092 5447 5448 136 -555 308 C ATOM 3839 CZ TYR B 224 19.104 -21.574 77.575 1.00 54.41 C ANISOU 3839 CZ TYR B 224 7410 6678 6585 108 -655 302 C ATOM 3840 OH TYR B 224 18.319 -21.455 76.458 1.00 55.72 O ANISOU 3840 OH TYR B 224 7586 6822 6761 119 -805 333 O ATOM 3841 N LEU B 225 21.433 -19.052 81.935 1.00 42.05 N ANISOU 3841 N LEU B 225 5841 5122 5014 173 -216 190 N ATOM 3842 CA LEU B 225 20.726 -17.786 81.868 1.00 42.66 C ANISOU 3842 CA LEU B 225 5885 5155 5167 209 -191 217 C ATOM 3843 C LEU B 225 21.624 -16.529 81.817 1.00 49.05 C ANISOU 3843 C LEU B 225 6753 5929 5955 214 -148 189 C ATOM 3844 O LEU B 225 21.454 -15.736 80.876 1.00 49.48 O ANISOU 3844 O LEU B 225 6830 5940 6031 231 -172 232 O ATOM 3845 CB LEU B 225 19.676 -17.697 82.980 1.00 42.78 C ANISOU 3845 CB LEU B 225 5834 5155 5266 236 -113 218 C ATOM 3846 CG LEU B 225 18.627 -16.586 82.858 1.00 47.35 C ANISOU 3846 CG LEU B 225 6343 5681 5967 292 -90 251 C ATOM 3847 CD1 LEU B 225 17.748 -16.748 81.614 1.00 47.16 C ANISOU 3847 CD1 LEU B 225 6247 5650 6020 308 -216 313 C ATOM 3848 CD2 LEU B 225 17.758 -16.569 84.059 1.00 50.10 C ANISOU 3848 CD2 LEU B 225 6630 6009 6396 316 33 237 C ATOM 3849 N ALA B 226 22.569 -16.338 82.783 1.00 45.18 N ANISOU 3849 N ALA B 226 6295 5446 5425 197 -96 119 N ATOM 3850 CA ALA B 226 23.442 -15.147 82.764 1.00 43.54 C ANISOU 3850 CA ALA B 226 6128 5193 5224 181 -56 79 C ATOM 3851 C ALA B 226 24.389 -15.091 81.533 1.00 46.36 C ANISOU 3851 C ALA B 226 6515 5542 5556 140 -70 88 C ATOM 3852 O ALA B 226 24.326 -14.084 80.843 1.00 46.74 O ANISOU 3852 O ALA B 226 6604 5525 5629 141 -40 123 O ATOM 3853 CB ALA B 226 24.208 -14.981 84.070 1.00 43.59 C ANISOU 3853 CB ALA B 226 6155 5204 5202 168 -29 -12 C ATOM 3854 N PRO B 227 25.204 -16.117 81.171 1.00 43.30 N ANISOU 3854 N PRO B 227 6124 5206 5121 111 -98 66 N ATOM 3855 CA PRO B 227 26.045 -15.988 79.955 1.00 42.63 C ANISOU 3855 CA PRO B 227 6080 5101 5016 75 -67 74 C ATOM 3856 C PRO B 227 25.284 -15.643 78.679 1.00 46.82 C ANISOU 3856 C PRO B 227 6688 5588 5514 91 -83 163 C ATOM 3857 O PRO B 227 25.721 -14.778 77.934 1.00 47.09 O ANISOU 3857 O PRO B 227 6793 5558 5539 70 -21 185 O ATOM 3858 CB PRO B 227 26.687 -17.373 79.807 1.00 44.04 C ANISOU 3858 CB PRO B 227 6239 5341 5156 66 -98 42 C ATOM 3859 CG PRO B 227 26.553 -18.022 81.091 1.00 48.01 C ANISOU 3859 CG PRO B 227 6695 5885 5661 90 -143 5 C ATOM 3860 CD PRO B 227 25.415 -17.430 81.825 1.00 44.49 C ANISOU 3860 CD PRO B 227 6248 5419 5236 117 -141 35 C ATOM 3861 N LEU B 228 24.146 -16.312 78.433 1.00 44.28 N ANISOU 3861 N LEU B 228 6359 5290 5174 128 -172 215 N ATOM 3862 CA LEU B 228 23.338 -16.126 77.219 1.00 43.40 C ANISOU 3862 CA LEU B 228 6324 5143 5024 155 -243 295 C ATOM 3863 C LEU B 228 22.580 -14.814 77.173 1.00 44.77 C ANISOU 3863 C LEU B 228 6511 5244 5254 203 -248 350 C ATOM 3864 O LEU B 228 22.486 -14.240 76.100 1.00 43.61 O ANISOU 3864 O LEU B 228 6479 5036 5054 221 -271 413 O ATOM 3865 CB LEU B 228 22.404 -17.321 76.972 1.00 43.23 C ANISOU 3865 CB LEU B 228 6268 5167 4991 168 -361 314 C ATOM 3866 CG LEU B 228 23.116 -18.641 76.700 1.00 47.28 C ANISOU 3866 CG LEU B 228 6810 5724 5430 129 -365 270 C ATOM 3867 CD1 LEU B 228 22.167 -19.755 76.776 1.00 47.07 C ANISOU 3867 CD1 LEU B 228 6731 5727 5426 129 -465 276 C ATOM 3868 CD2 LEU B 228 23.828 -18.635 75.331 1.00 49.23 C ANISOU 3868 CD2 LEU B 228 7205 5940 5561 112 -345 283 C ATOM 3869 N GLY B 229 22.061 -14.346 78.311 1.00 41.56 N ANISOU 3869 N GLY B 229 6013 4833 4946 232 -218 328 N ATOM 3870 CA GLY B 229 21.411 -13.038 78.407 1.00 40.59 C ANISOU 3870 CA GLY B 229 5897 4627 4900 289 -201 368 C ATOM 3871 C GLY B 229 22.396 -11.927 78.091 1.00 43.55 C ANISOU 3871 C GLY B 229 6380 4919 5249 258 -106 364 C ATOM 3872 O GLY B 229 22.104 -11.032 77.289 1.00 44.10 O ANISOU 3872 O GLY B 229 6544 4898 5313 297 -118 437 O ATOM 3873 N LEU B 230 23.609 -12.023 78.658 1.00 39.13 N ANISOU 3873 N LEU B 230 5809 4381 4678 184 -19 281 N ATOM 3874 CA LEU B 230 24.703 -11.088 78.397 1.00 38.39 C ANISOU 3874 CA LEU B 230 5787 4209 4590 125 88 257 C ATOM 3875 C LEU B 230 25.149 -11.174 76.946 1.00 44.98 C ANISOU 3875 C LEU B 230 6744 5010 5336 99 111 320 C ATOM 3876 O LEU B 230 25.263 -10.147 76.291 1.00 46.36 O ANISOU 3876 O LEU B 230 7037 5075 5504 94 176 374 O ATOM 3877 CB LEU B 230 25.878 -11.329 79.353 1.00 38.24 C ANISOU 3877 CB LEU B 230 5691 4235 4605 53 140 139 C ATOM 3878 CG LEU B 230 25.608 -10.928 80.825 1.00 42.44 C ANISOU 3878 CG LEU B 230 6165 4766 5194 71 139 66 C ATOM 3879 CD1 LEU B 230 26.653 -11.498 81.746 1.00 42.52 C ANISOU 3879 CD1 LEU B 230 6108 4842 5206 20 126 -45 C ATOM 3880 CD2 LEU B 230 25.443 -9.411 80.991 1.00 40.21 C ANISOU 3880 CD2 LEU B 230 5943 4357 4979 75 210 65 C ATOM 3881 N MET B 231 25.320 -12.384 76.421 1.00 43.13 N ANISOU 3881 N MET B 231 6509 4856 5024 88 64 320 N ATOM 3882 CA MET B 231 25.689 -12.590 75.024 1.00 43.92 C ANISOU 3882 CA MET B 231 6754 4924 5009 69 93 373 C ATOM 3883 C MET B 231 24.666 -11.971 74.060 1.00 48.52 C ANISOU 3883 C MET B 231 7486 5428 5521 139 10 490 C ATOM 3884 O MET B 231 25.061 -11.232 73.161 1.00 48.47 O ANISOU 3884 O MET B 231 7649 5323 5444 124 93 547 O ATOM 3885 CB MET B 231 25.897 -14.085 74.734 1.00 46.29 C ANISOU 3885 CB MET B 231 7028 5319 5240 59 42 339 C ATOM 3886 CG MET B 231 27.266 -14.567 75.110 1.00 49.37 C ANISOU 3886 CG MET B 231 7341 5748 5671 -7 154 244 C ATOM 3887 SD MET B 231 27.459 -16.243 74.521 1.00 53.32 S ANISOU 3887 SD MET B 231 7860 6322 6077 -1 109 220 S ATOM 3888 CE MET B 231 27.345 -17.170 76.060 1.00 49.67 C ANISOU 3888 CE MET B 231 7211 5957 5706 18 17 147 C ATOM 3889 N ALA B 232 23.359 -12.223 74.286 1.00 45.21 N ANISOU 3889 N ALA B 232 7002 5043 5134 218 -150 524 N ATOM 3890 CA ALA B 232 22.257 -11.681 73.490 1.00 44.86 C ANISOU 3890 CA ALA B 232 7056 4931 5057 307 -281 628 C ATOM 3891 C ALA B 232 22.363 -10.142 73.442 1.00 50.52 C ANISOU 3891 C ALA B 232 7869 5512 5812 334 -195 682 C ATOM 3892 O ALA B 232 22.349 -9.547 72.353 1.00 49.58 O ANISOU 3892 O ALA B 232 7954 5294 5589 366 -210 774 O ATOM 3893 CB ALA B 232 20.915 -12.115 74.081 1.00 44.96 C ANISOU 3893 CB ALA B 232 6900 5002 5180 375 -436 627 C ATOM 3894 N MET B 233 22.561 -9.512 74.625 1.00 47.96 N ANISOU 3894 N MET B 233 7427 5172 5623 316 -96 619 N ATOM 3895 CA MET B 233 22.717 -8.059 74.750 1.00 47.03 C ANISOU 3895 CA MET B 233 7390 4913 5566 330 2 648 C ATOM 3896 C MET B 233 23.984 -7.534 74.048 1.00 51.13 C ANISOU 3896 C MET B 233 8074 5343 6012 235 167 659 C ATOM 3897 O MET B 233 23.934 -6.481 73.408 1.00 51.85 O ANISOU 3897 O MET B 233 8336 5287 6077 261 216 744 O ATOM 3898 CB MET B 233 22.652 -7.629 76.222 1.00 49.08 C ANISOU 3898 CB MET B 233 7497 5180 5973 325 64 557 C ATOM 3899 CG MET B 233 21.301 -7.879 76.845 1.00 53.03 C ANISOU 3899 CG MET B 233 7860 5725 6563 428 -48 563 C ATOM 3900 SD MET B 233 21.135 -7.228 78.532 1.00 57.62 S ANISOU 3900 SD MET B 233 8325 6282 7285 438 57 460 S ATOM 3901 CE MET B 233 22.099 -8.392 79.462 1.00 52.99 C ANISOU 3901 CE MET B 233 7642 5840 6653 330 94 339 C ATOM 3902 N ALA B 234 25.118 -8.253 74.184 1.00 46.74 N ANISOU 3902 N ALA B 234 7461 4861 5438 129 265 574 N ATOM 3903 CA ALA B 234 26.382 -7.917 73.514 1.00 45.73 C ANISOU 3903 CA ALA B 234 7447 4658 5270 25 451 568 C ATOM 3904 C ALA B 234 26.173 -7.893 71.995 1.00 50.24 C ANISOU 3904 C ALA B 234 8270 5157 5661 59 448 692 C ATOM 3905 O ALA B 234 26.515 -6.898 71.357 1.00 48.91 O ANISOU 3905 O ALA B 234 8288 4839 5456 34 576 761 O ATOM 3906 CB ALA B 234 27.457 -8.943 73.862 1.00 45.73 C ANISOU 3906 CB ALA B 234 7305 4772 5297 -64 515 454 C ATOM 3907 N TYR B 235 25.576 -8.983 71.438 1.00 47.61 N ANISOU 3907 N TYR B 235 7963 4919 5208 115 296 718 N ATOM 3908 CA TYR B 235 25.304 -9.183 70.012 1.00 47.67 C ANISOU 3908 CA TYR B 235 8228 4877 5008 155 247 819 C ATOM 3909 C TYR B 235 24.242 -8.258 69.459 1.00 55.59 C ANISOU 3909 C TYR B 235 9402 5764 5954 269 113 950 C ATOM 3910 O TYR B 235 24.332 -7.899 68.273 1.00 55.52 O ANISOU 3910 O TYR B 235 9682 5648 5767 287 142 1050 O ATOM 3911 CB TYR B 235 25.000 -10.649 69.702 1.00 48.20 C ANISOU 3911 CB TYR B 235 8259 5075 4981 171 109 783 C ATOM 3912 CG TYR B 235 26.268 -11.473 69.682 1.00 49.09 C ANISOU 3912 CG TYR B 235 8326 5246 5081 70 283 689 C ATOM 3913 CD1 TYR B 235 27.286 -11.199 68.766 1.00 51.23 C ANISOU 3913 CD1 TYR B 235 8791 5428 5245 5 500 709 C ATOM 3914 CD2 TYR B 235 26.460 -12.522 70.582 1.00 49.26 C ANISOU 3914 CD2 TYR B 235 8111 5399 5205 46 246 581 C ATOM 3915 CE1 TYR B 235 28.482 -11.914 68.779 1.00 52.10 C ANISOU 3915 CE1 TYR B 235 8826 5586 5386 -80 679 613 C ATOM 3916 CE2 TYR B 235 27.645 -13.264 70.585 1.00 49.83 C ANISOU 3916 CE2 TYR B 235 8127 5517 5290 -28 396 493 C ATOM 3917 CZ TYR B 235 28.652 -12.954 69.680 1.00 57.48 C ANISOU 3917 CZ TYR B 235 9256 6402 6182 -88 612 504 C ATOM 3918 OH TYR B 235 29.829 -13.654 69.665 1.00 59.46 O ANISOU 3918 OH TYR B 235 9425 6689 6478 -152 775 412 O ATOM 3919 N PHE B 236 23.289 -7.796 70.315 1.00 54.18 N ANISOU 3919 N PHE B 236 9065 5591 5930 350 -15 952 N ATOM 3920 CA PHE B 236 22.286 -6.795 69.916 1.00 54.95 C ANISOU 3920 CA PHE B 236 9288 5564 6025 478 -142 1071 C ATOM 3921 C PHE B 236 22.997 -5.447 69.661 1.00 58.83 C ANISOU 3921 C PHE B 236 9974 5870 6508 440 63 1130 C ATOM 3922 O PHE B 236 22.647 -4.757 68.705 1.00 60.91 O ANISOU 3922 O PHE B 236 10501 5995 6647 516 18 1261 O ATOM 3923 CB PHE B 236 21.172 -6.645 70.968 1.00 58.01 C ANISOU 3923 CB PHE B 236 9429 5998 6614 570 -279 1040 C ATOM 3924 CG PHE B 236 20.140 -5.603 70.612 1.00 61.27 C ANISOU 3924 CG PHE B 236 9938 6279 7065 720 -412 1155 C ATOM 3925 CD1 PHE B 236 19.129 -5.884 69.698 1.00 65.38 C ANISOU 3925 CD1 PHE B 236 10542 6799 7501 839 -670 1243 C ATOM 3926 CD2 PHE B 236 20.213 -4.317 71.144 1.00 65.74 C ANISOU 3926 CD2 PHE B 236 10523 6705 7750 747 -292 1171 C ATOM 3927 CE1 PHE B 236 18.205 -4.899 69.321 1.00 67.17 C ANISOU 3927 CE1 PHE B 236 10859 6893 7770 996 -816 1355 C ATOM 3928 CE2 PHE B 236 19.293 -3.326 70.762 1.00 69.13 C ANISOU 3928 CE2 PHE B 236 11057 6991 8218 902 -414 1284 C ATOM 3929 CZ PHE B 236 18.287 -3.628 69.860 1.00 67.11 C ANISOU 3929 CZ PHE B 236 10869 6742 7886 1034 -681 1379 C ATOM 3930 N GLN B 237 24.007 -5.092 70.494 1.00 53.44 N ANISOU 3930 N GLN B 237 9175 5175 5955 321 280 1033 N ATOM 3931 CA GLN B 237 24.838 -3.887 70.346 1.00 52.31 C ANISOU 3931 CA GLN B 237 9183 4853 5841 244 507 1061 C ATOM 3932 C GLN B 237 25.785 -4.016 69.136 1.00 57.33 C ANISOU 3932 C GLN B 237 10064 5421 6296 157 679 1115 C ATOM 3933 O GLN B 237 25.966 -3.052 68.397 1.00 56.81 O ANISOU 3933 O GLN B 237 10264 5170 6152 157 794 1224 O ATOM 3934 CB GLN B 237 25.617 -3.563 71.628 1.00 52.73 C ANISOU 3934 CB GLN B 237 9014 4922 6097 132 654 918 C ATOM 3935 CG GLN B 237 24.725 -3.080 72.764 1.00 57.95 C ANISOU 3935 CG GLN B 237 9514 5589 6917 219 544 877 C ATOM 3936 CD GLN B 237 25.461 -2.292 73.823 1.00 73.01 C ANISOU 3936 CD GLN B 237 11325 7425 8990 119 699 765 C ATOM 3937 OE1 GLN B 237 26.492 -2.707 74.353 1.00 70.27 O ANISOU 3937 OE1 GLN B 237 10843 7154 8703 -10 794 642 O ATOM 3938 NE2 GLN B 237 24.922 -1.138 74.182 1.00 63.76 N ANISOU 3938 NE2 GLN B 237 10216 6102 7906 185 709 797 N ATOM 3939 N ILE B 238 26.353 -5.214 68.911 1.00 55.23 N ANISOU 3939 N ILE B 238 9731 5294 5959 91 708 1045 N ATOM 3940 CA ILE B 238 27.214 -5.488 67.750 1.00 55.14 C ANISOU 3940 CA ILE B 238 9953 5229 5770 17 890 1084 C ATOM 3941 C ILE B 238 26.370 -5.331 66.463 1.00 62.76 C ANISOU 3941 C ILE B 238 11265 6102 6477 137 750 1246 C ATOM 3942 O ILE B 238 26.831 -4.684 65.517 1.00 63.13 O ANISOU 3942 O ILE B 238 11622 5987 6377 107 926 1344 O ATOM 3943 CB ILE B 238 27.926 -6.872 67.865 1.00 57.02 C ANISOU 3943 CB ILE B 238 10025 5635 6005 -58 936 962 C ATOM 3944 CG1 ILE B 238 28.932 -6.884 69.037 1.00 56.08 C ANISOU 3944 CG1 ILE B 238 9602 5574 6133 -177 1081 812 C ATOM 3945 CG2 ILE B 238 28.620 -7.269 66.549 1.00 57.80 C ANISOU 3945 CG2 ILE B 238 10393 5677 5890 -105 1113 1007 C ATOM 3946 CD1 ILE B 238 29.335 -8.258 69.520 1.00 56.15 C ANISOU 3946 CD1 ILE B 238 9384 5764 6187 -202 1036 689 C ATOM 3947 N PHE B 239 25.120 -5.876 66.462 1.00 61.06 N ANISOU 3947 N PHE B 239 11001 5981 6218 273 431 1273 N ATOM 3948 CA PHE B 239 24.173 -5.792 65.342 1.00 61.33 C ANISOU 3948 CA PHE B 239 11328 5947 6029 407 214 1411 C ATOM 3949 C PHE B 239 23.862 -4.326 64.976 1.00 68.03 C ANISOU 3949 C PHE B 239 12416 6579 6854 482 238 1555 C ATOM 3950 O PHE B 239 23.889 -3.959 63.792 1.00 67.19 O ANISOU 3950 O PHE B 239 12692 6333 6505 521 260 1684 O ATOM 3951 CB PHE B 239 22.869 -6.563 65.656 1.00 62.85 C ANISOU 3951 CB PHE B 239 11328 6280 6271 526 -139 1387 C ATOM 3952 CG PHE B 239 21.795 -6.369 64.610 1.00 64.52 C ANISOU 3952 CG PHE B 239 11799 6416 6300 678 -420 1520 C ATOM 3953 CD1 PHE B 239 21.853 -7.047 63.394 1.00 67.52 C ANISOU 3953 CD1 PHE B 239 12470 6795 6392 686 -497 1560 C ATOM 3954 CD2 PHE B 239 20.761 -5.461 64.810 1.00 66.67 C ANISOU 3954 CD2 PHE B 239 12045 6603 6681 822 -607 1605 C ATOM 3955 CE1 PHE B 239 20.905 -6.807 62.391 1.00 67.90 C ANISOU 3955 CE1 PHE B 239 12793 6759 6247 832 -782 1684 C ATOM 3956 CE2 PHE B 239 19.819 -5.217 63.802 1.00 69.14 C ANISOU 3956 CE2 PHE B 239 12608 6833 6830 976 -889 1733 C ATOM 3957 CZ PHE B 239 19.885 -5.909 62.610 1.00 66.61 C ANISOU 3957 CZ PHE B 239 12581 6517 6209 979 -992 1771 C ATOM 3958 N ARG B 240 23.524 -3.506 66.007 1.00 65.17 N ANISOU 3958 N ARG B 240 11848 6179 6733 513 230 1532 N ATOM 3959 CA ARG B 240 23.203 -2.091 65.868 1.00 64.04 C ANISOU 3959 CA ARG B 240 11890 5823 6619 591 255 1652 C ATOM 3960 C ARG B 240 24.383 -1.316 65.261 1.00 69.24 C ANISOU 3960 C ARG B 240 12834 6293 7181 465 591 1711 C ATOM 3961 O ARG B 240 24.169 -0.458 64.412 1.00 71.25 O ANISOU 3961 O ARG B 240 13437 6350 7284 539 598 1868 O ATOM 3962 CB ARG B 240 22.799 -1.514 67.228 1.00 63.06 C ANISOU 3962 CB ARG B 240 11464 5708 6788 618 235 1575 C ATOM 3963 CG ARG B 240 21.357 -1.806 67.631 1.00 79.84 C ANISOU 3963 CG ARG B 240 13399 7926 9012 791 -87 1580 C ATOM 3964 CD ARG B 240 20.459 -0.625 67.307 1.00104.89 C ANISOU 3964 CD ARG B 240 16745 10906 12202 967 -216 1723 C ATOM 3965 NE ARG B 240 19.039 -0.895 67.547 1.00122.26 N ANISOU 3965 NE ARG B 240 18753 13185 14515 1144 -532 1733 N ATOM 3966 CZ ARG B 240 18.306 -0.292 68.479 1.00139.85 C ANISOU 3966 CZ ARG B 240 20767 15382 16989 1242 -575 1702 C ATOM 3967 NH1 ARG B 240 18.853 0.614 69.283 1.00124.17 N ANISOU 3967 NH1 ARG B 240 18752 13286 15141 1181 -341 1655 N ATOM 3968 NH2 ARG B 240 17.021 -0.593 68.618 1.00129.82 N ANISOU 3968 NH2 ARG B 240 19304 14183 15839 1399 -847 1709 N ATOM 3969 N LYS B 241 25.621 -1.646 65.664 1.00 65.04 N ANISOU 3969 N LYS B 241 12159 5815 6737 279 865 1588 N ATOM 3970 CA LYS B 241 26.850 -1.023 65.179 1.00 64.62 C ANISOU 3970 CA LYS B 241 12307 5599 6648 127 1224 1614 C ATOM 3971 C LYS B 241 27.187 -1.446 63.738 1.00 71.63 C ANISOU 3971 C LYS B 241 13567 6431 7220 119 1319 1715 C ATOM 3972 O LYS B 241 27.605 -0.599 62.955 1.00 72.12 O ANISOU 3972 O LYS B 241 13968 6276 7159 84 1530 1835 O ATOM 3973 CB LYS B 241 28.024 -1.321 66.140 1.00 65.95 C ANISOU 3973 CB LYS B 241 12145 5861 7052 -60 1449 1430 C ATOM 3974 CG LYS B 241 29.166 -0.306 66.074 1.00 72.79 C ANISOU 3974 CG LYS B 241 13103 6528 8027 -226 1807 1428 C ATOM 3975 CD LYS B 241 28.998 0.829 67.089 1.00 83.41 C ANISOU 3975 CD LYS B 241 14315 7764 9612 -237 1805 1391 C ATOM 3976 CE LYS B 241 29.959 1.982 66.880 1.00 94.66 C ANISOU 3976 CE LYS B 241 15888 8945 11135 -392 2139 1414 C ATOM 3977 NZ LYS B 241 31.300 1.729 67.471 1.00101.82 N ANISOU 3977 NZ LYS B 241 16518 9909 12258 -607 2373 1237 N ATOM 3978 N LEU B 242 27.022 -2.745 63.386 1.00 70.56 N ANISOU 3978 N LEU B 242 13392 6474 6943 147 1179 1665 N ATOM 3979 CA LEU B 242 27.363 -3.260 62.045 1.00 71.05 C ANISOU 3979 CA LEU B 242 13818 6493 6686 137 1274 1736 C ATOM 3980 C LEU B 242 26.259 -3.103 60.985 1.00 76.67 C ANISOU 3980 C LEU B 242 14915 7119 7096 318 993 1904 C ATOM 3981 O LEU B 242 26.562 -3.118 59.800 1.00 75.81 O ANISOU 3981 O LEU B 242 15219 6898 6686 315 1108 1999 O ATOM 3982 CB LEU B 242 27.837 -4.726 62.093 1.00 71.00 C ANISOU 3982 CB LEU B 242 13623 6692 6662 72 1290 1593 C ATOM 3983 CG LEU B 242 29.101 -5.060 62.893 1.00 75.29 C ANISOU 3983 CG LEU B 242 13832 7316 7457 -101 1574 1429 C ATOM 3984 CD1 LEU B 242 29.367 -6.559 62.868 1.00 74.86 C ANISOU 3984 CD1 LEU B 242 13626 7454 7364 -119 1530 1307 C ATOM 3985 CD2 LEU B 242 30.323 -4.302 62.380 1.00 77.35 C ANISOU 3985 CD2 LEU B 242 14274 7393 7724 -248 2004 1459 C ATOM 3986 N TRP B 243 24.993 -2.991 61.391 1.00 75.39 N ANISOU 3986 N TRP B 243 14624 7009 7010 476 622 1933 N ATOM 3987 CA TRP B 243 23.902 -2.825 60.435 1.00 75.96 C ANISOU 3987 CA TRP B 243 15024 7004 6834 662 303 2083 C ATOM 3988 C TRP B 243 23.169 -1.525 60.643 1.00 86.78 C ANISOU 3988 C TRP B 243 16456 8208 8309 793 182 2207 C ATOM 3989 O TRP B 243 22.058 -1.351 60.137 1.00 87.41 O ANISOU 3989 O TRP B 243 16664 8255 8293 981 -170 2308 O ATOM 3990 CB TRP B 243 22.964 -4.031 60.423 1.00 73.68 C ANISOU 3990 CB TRP B 243 14567 6920 6508 752 -73 2013 C ATOM 3991 CG TRP B 243 23.554 -5.218 59.738 1.00 73.97 C ANISOU 3991 CG TRP B 243 14732 7052 6323 667 9 1943 C ATOM 3992 CD1 TRP B 243 23.504 -5.503 58.408 1.00 76.63 C ANISOU 3992 CD1 TRP B 243 15521 7311 6284 713 -49 2028 C ATOM 3993 CD2 TRP B 243 24.283 -6.294 60.355 1.00 73.73 C ANISOU 3993 CD2 TRP B 243 14390 7199 6424 531 161 1768 C ATOM 3994 NE1 TRP B 243 24.157 -6.686 58.153 1.00 76.31 N ANISOU 3994 NE1 TRP B 243 15467 7387 6139 610 77 1910 N ATOM 3995 CE2 TRP B 243 24.643 -7.195 59.332 1.00 77.56 C ANISOU 3995 CE2 TRP B 243 15150 7702 6615 502 203 1753 C ATOM 3996 CE3 TRP B 243 24.692 -6.569 61.674 1.00 74.74 C ANISOU 3996 CE3 TRP B 243 14056 7462 6880 437 268 1624 C ATOM 3997 CZ2 TRP B 243 25.350 -8.376 59.590 1.00 77.01 C ANISOU 3997 CZ2 TRP B 243 14885 7780 6594 393 341 1599 C ATOM 3998 CZ3 TRP B 243 25.399 -7.734 61.929 1.00 76.05 C ANISOU 3998 CZ3 TRP B 243 14037 7776 7083 332 385 1481 C ATOM 3999 CH2 TRP B 243 25.726 -8.622 60.896 1.00 76.78 C ANISOU 3999 CH2 TRP B 243 14388 7881 6904 313 426 1469 C ATOM 4000 N GLY B 244 23.818 -0.610 61.362 1.00 87.78 N ANISOU 4000 N GLY B 244 16492 8221 8641 694 471 2192 N ATOM 4001 CA GLY B 244 23.327 0.739 61.594 1.00 89.69 C ANISOU 4001 CA GLY B 244 16816 8265 8998 794 439 2301 C ATOM 4002 C GLY B 244 23.907 1.699 60.575 1.00 98.35 C ANISOU 4002 C GLY B 244 18413 9083 9874 768 686 2470 C ATOM 4003 O GLY B 244 24.633 1.277 59.665 1.00 96.98 O ANISOU 4003 O GLY B 244 18519 8879 9450 673 886 2499 O ATOM 4004 N ARG B 245 23.588 2.995 60.719 1.00100.22 N ANISOU 4004 N ARG B 245 18779 9098 10200 853 693 2583 N ATOM 4005 CA ARG B 245 24.091 4.037 59.824 1.00102.76 C ANISOU 4005 CA ARG B 245 19594 9117 10332 831 941 2759 C ATOM 4006 C ARG B 245 25.569 4.278 60.108 1.00110.59 C ANISOU 4006 C ARG B 245 20530 10042 11447 560 1439 2670 C ATOM 4007 O ARG B 245 25.942 4.569 61.249 1.00109.94 O ANISOU 4007 O ARG B 245 20079 10000 11696 452 1560 2532 O ATOM 4008 CB ARG B 245 23.281 5.344 59.962 1.00105.48 C ANISOU 4008 CB ARG B 245 20072 9234 10772 1007 799 2898 C ATOM 4009 CG ARG B 245 21.922 5.330 59.264 1.00123.21 C ANISOU 4009 CG ARG B 245 22530 11457 12829 1292 336 3047 C ATOM 4010 CD ARG B 245 22.013 5.694 57.789 1.00143.66 C ANISOU 4010 CD ARG B 245 25765 13818 15002 1364 359 3269 C ATOM 4011 NE ARG B 245 20.709 5.646 57.120 1.00161.88 N ANISOU 4011 NE ARG B 245 28268 16112 17126 1645 -136 3401 N ATOM 4012 CZ ARG B 245 20.171 4.550 56.586 1.00181.00 C ANISOU 4012 CZ ARG B 245 30690 18727 19353 1719 -454 3368 C ATOM 4013 NH1 ARG B 245 18.984 4.606 55.996 1.00169.69 N ANISOU 4013 NH1 ARG B 245 29427 17263 17784 1975 -925 3485 N ATOM 4014 NH2 ARG B 245 20.813 3.388 56.646 1.00168.70 N ANISOU 4014 NH2 ARG B 245 28957 17389 17752 1541 -316 3212 N ATOM 4015 N GLN B 246 26.409 4.108 59.079 1.00110.38 N ANISOU 4015 N GLN B 246 20859 9922 11159 449 1720 2737 N ATOM 4016 CA GLN B 246 27.853 4.315 59.178 1.00111.62 C ANISOU 4016 CA GLN B 246 20982 9999 11432 186 2218 2661 C ATOM 4017 C GLN B 246 28.165 5.808 59.309 1.00116.22 C ANISOU 4017 C GLN B 246 21740 10271 12146 127 2466 2757 C ATOM 4018 O GLN B 246 27.528 6.623 58.636 1.00114.96 O ANISOU 4018 O GLN B 246 21997 9887 11797 280 2366 2960 O ATOM 4019 CB GLN B 246 28.563 3.756 57.935 1.00113.52 C ANISOU 4019 CB GLN B 246 21598 10198 11337 106 2468 2722 C ATOM 4020 CG GLN B 246 29.039 2.320 58.080 1.00139.35 C ANISOU 4020 CG GLN B 246 24576 13753 14619 20 2478 2542 C ATOM 4021 CD GLN B 246 29.779 1.877 56.840 1.00164.55 C ANISOU 4021 CD GLN B 246 28167 16872 17484 -59 2775 2600 C ATOM 4022 OE1 GLN B 246 29.180 1.426 55.856 1.00160.69 O ANISOU 4022 OE1 GLN B 246 28045 16388 16623 80 2576 2701 O ATOM 4023 NE2 GLN B 246 31.099 1.987 56.860 1.00157.67 N ANISOU 4023 NE2 GLN B 246 27228 15926 16751 -285 3259 2526 N ATOM 4024 N ILE B 247 29.150 6.152 60.174 1.00114.08 N ANISOU 4024 N ILE B 247 21159 9982 12206 -94 2777 2609 N ATOM 4025 CA ILE B 247 29.638 7.516 60.411 1.00114.37 C ANISOU 4025 CA ILE B 247 21307 9724 12424 -207 3063 2656 C ATOM 4026 C ILE B 247 30.057 8.123 59.055 1.00119.27 C ANISOU 4026 C ILE B 247 22529 10046 12742 -243 3366 2872 C ATOM 4027 O ILE B 247 30.715 7.423 58.280 1.00119.32 O ANISOU 4027 O ILE B 247 22684 10100 12550 -337 3580 2875 O ATOM 4028 CB ILE B 247 30.791 7.515 61.472 1.00117.48 C ANISOU 4028 CB ILE B 247 21243 10187 13206 -472 3343 2425 C ATOM 4029 CG1 ILE B 247 30.214 7.466 62.902 1.00117.98 C ANISOU 4029 CG1 ILE B 247 20832 10429 13564 -410 3048 2258 C ATOM 4030 CG2 ILE B 247 31.757 8.709 61.311 1.00118.42 C ANISOU 4030 CG2 ILE B 247 21549 9981 13466 -680 3786 2468 C ATOM 4031 CD1 ILE B 247 31.219 7.071 64.012 1.00127.78 C ANISOU 4031 CD1 ILE B 247 21576 11832 15141 -630 3195 2002 C ATOM 4032 N PRO B 248 29.647 9.374 58.717 1.00115.69 N ANISOU 4032 N PRO B 248 22454 9279 12223 -153 3387 3061 N ATOM 4033 CA PRO B 248 30.050 9.945 57.416 1.00115.27 C ANISOU 4033 CA PRO B 248 23020 8923 11855 -185 3691 3282 C ATOM 4034 C PRO B 248 31.569 10.089 57.277 1.00119.39 C ANISOU 4034 C PRO B 248 23528 9327 12508 -508 4274 3208 C ATOM 4035 O PRO B 248 32.263 10.273 58.283 1.00119.29 O ANISOU 4035 O PRO B 248 23078 9353 12894 -703 4445 3020 O ATOM 4036 CB PRO B 248 29.331 11.297 57.375 1.00116.81 C ANISOU 4036 CB PRO B 248 23524 8807 12050 -32 3586 3467 C ATOM 4037 CG PRO B 248 29.063 11.638 58.791 1.00121.20 C ANISOU 4037 CG PRO B 248 23570 9452 13028 -38 3432 3294 C ATOM 4038 CD PRO B 248 28.846 10.335 59.505 1.00116.98 C ANISOU 4038 CD PRO B 248 22517 9329 12600 -20 3165 3082 C ATOM 4039 N GLY B 249 32.061 9.960 56.042 1.00115.32 N ANISOU 4039 N GLY B 249 23484 8675 11656 -558 4564 3347 N ATOM 4040 CA GLY B 249 33.479 10.043 55.696 1.00113.92 C ANISOU 4040 CA GLY B 249 23351 8367 11565 -854 5157 3301 C ATOM 4041 C GLY B 249 34.319 8.836 56.087 1.00113.54 C ANISOU 4041 C GLY B 249 22822 8623 11695 -1016 5286 3058 C ATOM 4042 O GLY B 249 35.429 9.007 56.596 1.00112.70 O ANISOU 4042 O GLY B 249 22400 8484 11936 -1276 5657 2908 O ATOM 4043 N THR B 250 33.823 7.608 55.833 1.00107.35 N ANISOU 4043 N THR B 250 21979 8122 10687 -867 4981 3014 N ATOM 4044 CA THR B 250 34.586 6.392 56.158 1.00106.21 C ANISOU 4044 CA THR B 250 21403 8260 10693 -996 5088 2791 C ATOM 4045 C THR B 250 35.439 5.918 54.982 1.00107.07 C ANISOU 4045 C THR B 250 21856 8285 10541 -1106 5526 2841 C ATOM 4046 O THR B 250 35.012 6.001 53.825 1.00106.29 O ANISOU 4046 O THR B 250 22358 8035 9993 -985 5538 3045 O ATOM 4047 CB THR B 250 33.719 5.254 56.737 1.00111.89 C ANISOU 4047 CB THR B 250 21779 9339 11396 -815 4566 2671 C ATOM 4048 OG1 THR B 250 32.584 5.013 55.907 1.00111.10 O ANISOU 4048 OG1 THR B 250 22102 9239 10871 -564 4213 2843 O ATOM 4049 CG2 THR B 250 33.294 5.513 58.170 1.00109.78 C ANISOU 4049 CG2 THR B 250 20995 9203 11512 -793 4273 2531 C ATOM 4050 N THR B 251 36.654 5.415 55.302 1.00101.00 N ANISOU 4050 N THR B 251 20702 7612 10060 -1331 5884 2648 N ATOM 4051 CA THR B 251 37.644 4.888 54.353 1.00 98.95 C ANISOU 4051 CA THR B 251 20652 7296 9651 -1465 6366 2644 C ATOM 4052 C THR B 251 37.154 3.569 53.786 1.00 98.98 C ANISOU 4052 C THR B 251 20777 7531 9300 -1294 6115 2626 C ATOM 4053 O THR B 251 36.296 2.932 54.397 1.00 97.49 O ANISOU 4053 O THR B 251 20323 7595 9124 -1131 5606 2551 O ATOM 4054 CB THR B 251 39.018 4.701 55.042 1.00105.43 C ANISOU 4054 CB THR B 251 20917 8174 10967 -1737 6759 2414 C ATOM 4055 OG1 THR B 251 38.898 3.789 56.145 1.00102.53 O ANISOU 4055 OG1 THR B 251 19936 8147 10872 -1696 6402 2191 O ATOM 4056 CG2 THR B 251 39.638 6.024 55.505 1.00104.33 C ANISOU 4056 CG2 THR B 251 20682 7772 11187 -1946 7065 2419 C ATOM 4057 N SER B 252 37.704 3.142 52.634 1.00 94.49 N ANISOU 4057 N SER B 252 20609 6870 8423 -1338 6486 2685 N ATOM 4058 CA SER B 252 37.323 1.857 52.037 1.00 93.50 C ANISOU 4058 CA SER B 252 20630 6944 7951 -1193 6286 2651 C ATOM 4059 C SER B 252 37.802 0.641 52.851 1.00 95.72 C ANISOU 4059 C SER B 252 20268 7547 8555 -1246 6210 2383 C ATOM 4060 O SER B 252 37.115 -0.384 52.894 1.00 95.20 O ANISOU 4060 O SER B 252 20132 7713 8327 -1087 5811 2323 O ATOM 4061 CB SER B 252 37.769 1.782 50.591 1.00 96.33 C ANISOU 4061 CB SER B 252 21629 7096 7875 -1224 6722 2783 C ATOM 4062 OG SER B 252 36.765 2.430 49.833 1.00107.58 O ANISOU 4062 OG SER B 252 23693 8334 8847 -1045 6485 3032 O ATOM 4063 N ALA B 253 38.943 0.803 53.553 1.00 90.55 N ANISOU 4063 N ALA B 253 19132 6894 8378 -1466 6566 2223 N ATOM 4064 CA ALA B 253 39.564 -0.174 54.437 1.00 89.37 C ANISOU 4064 CA ALA B 253 18337 7012 8606 -1535 6532 1969 C ATOM 4065 C ALA B 253 38.642 -0.469 55.615 1.00 93.48 C ANISOU 4065 C ALA B 253 18449 7779 9291 -1400 5928 1884 C ATOM 4066 O ALA B 253 38.707 -1.567 56.174 1.00 94.83 O ANISOU 4066 O ALA B 253 18230 8210 9591 -1360 5732 1715 O ATOM 4067 CB ALA B 253 40.899 0.356 54.937 1.00 89.70 C ANISOU 4067 CB ALA B 253 17990 6953 9138 -1797 7002 1843 C ATOM 4068 N GLU B 286 37.787 0.513 55.987 1.00 88.91 N ANISOU 4068 N GLU B 286 17971 7105 8706 -1325 5654 2002 N ATOM 4069 CA GLU B 286 36.801 0.422 57.073 1.00 87.97 C ANISOU 4069 CA GLU B 286 17522 7178 8726 -1189 5109 1946 C ATOM 4070 C GLU B 286 35.551 -0.266 56.570 1.00 91.47 C ANISOU 4070 C GLU B 286 18238 7745 8773 -948 4665 2037 C ATOM 4071 O GLU B 286 34.979 -1.072 57.293 1.00 90.44 O ANISOU 4071 O GLU B 286 17768 7863 8732 -850 4283 1925 O ATOM 4072 CB GLU B 286 36.439 1.816 57.610 1.00 88.99 C ANISOU 4072 CB GLU B 286 17672 7123 9018 -1206 5045 2034 C ATOM 4073 CG GLU B 286 37.341 2.294 58.731 1.00 96.34 C ANISOU 4073 CG GLU B 286 18101 8046 10456 -1412 5234 1863 C ATOM 4074 CD GLU B 286 37.258 3.769 59.069 1.00115.02 C ANISOU 4074 CD GLU B 286 20560 10163 12980 -1475 5299 1947 C ATOM 4075 OE1 GLU B 286 37.681 4.135 60.189 1.00103.26 O ANISOU 4075 OE1 GLU B 286 18633 8708 11892 -1594 5283 1792 O ATOM 4076 OE2 GLU B 286 36.786 4.562 58.221 1.00112.58 O ANISOU 4076 OE2 GLU B 286 20774 9613 12389 -1404 5361 2165 O ATOM 4077 N VAL B 287 35.124 0.054 55.327 1.00 89.09 N ANISOU 4077 N VAL B 287 18560 7257 8032 -855 4711 2240 N ATOM 4078 CA VAL B 287 33.954 -0.548 54.669 1.00 88.94 C ANISOU 4078 CA VAL B 287 18871 7321 7600 -629 4290 2336 C ATOM 4079 C VAL B 287 34.238 -2.045 54.485 1.00 92.16 C ANISOU 4079 C VAL B 287 19135 7955 7928 -626 4275 2183 C ATOM 4080 O VAL B 287 33.383 -2.872 54.801 1.00 91.62 O ANISOU 4080 O VAL B 287 18903 8099 7810 -488 3833 2122 O ATOM 4081 CB VAL B 287 33.592 0.167 53.331 1.00 92.39 C ANISOU 4081 CB VAL B 287 20050 7482 7573 -542 4376 2586 C ATOM 4082 CG1 VAL B 287 32.410 -0.512 52.639 1.00 92.38 C ANISOU 4082 CG1 VAL B 287 20377 7573 7149 -312 3906 2665 C ATOM 4083 CG2 VAL B 287 33.285 1.642 53.561 1.00 91.76 C ANISOU 4083 CG2 VAL B 287 20104 7167 7593 -531 4374 2738 C ATOM 4084 N LYS B 288 35.477 -2.374 54.037 1.00 87.98 N ANISOU 4084 N LYS B 288 18630 7370 7428 -788 4781 2111 N ATOM 4085 CA LYS B 288 35.995 -3.735 53.868 1.00 86.78 C ANISOU 4085 CA LYS B 288 18323 7397 7253 -808 4873 1950 C ATOM 4086 C LYS B 288 36.055 -4.439 55.240 1.00 87.91 C ANISOU 4086 C LYS B 288 17771 7811 7821 -826 4631 1742 C ATOM 4087 O LYS B 288 35.745 -5.626 55.318 1.00 87.27 O ANISOU 4087 O LYS B 288 17558 7929 7670 -741 4396 1640 O ATOM 4088 CB LYS B 288 37.390 -3.704 53.204 1.00 89.16 C ANISOU 4088 CB LYS B 288 18750 7546 7580 -990 5526 1918 C ATOM 4089 CG LYS B 288 37.915 -5.080 52.787 1.00108.96 C ANISOU 4089 CG LYS B 288 21212 10192 9995 -987 5667 1774 C ATOM 4090 CD LYS B 288 39.337 -5.024 52.235 1.00118.84 C ANISOU 4090 CD LYS B 288 22512 11294 11346 -1170 6347 1724 C ATOM 4091 CE LYS B 288 39.853 -6.395 51.864 1.00124.95 C ANISOU 4091 CE LYS B 288 23221 12201 12056 -1152 6491 1570 C ATOM 4092 NZ LYS B 288 41.205 -6.328 51.247 1.00132.92 N ANISOU 4092 NZ LYS B 288 24286 13051 13168 -1320 7183 1523 N ATOM 4093 N GLN B 289 36.432 -3.702 56.312 1.00 82.83 N ANISOU 4093 N GLN B 289 16714 7159 7597 -932 4680 1681 N ATOM 4094 CA GLN B 289 36.515 -4.238 57.674 1.00 82.42 C ANISOU 4094 CA GLN B 289 16037 7340 7937 -950 4454 1493 C ATOM 4095 C GLN B 289 35.173 -4.639 58.271 1.00 86.19 C ANISOU 4095 C GLN B 289 16424 7986 8338 -768 3881 1508 C ATOM 4096 O GLN B 289 35.105 -5.658 58.958 1.00 85.84 O ANISOU 4096 O GLN B 289 16022 8166 8426 -728 3657 1367 O ATOM 4097 CB GLN B 289 37.263 -3.274 58.617 1.00 83.62 C ANISOU 4097 CB GLN B 289 15832 7415 8526 -1116 4651 1424 C ATOM 4098 CG GLN B 289 37.357 -3.741 60.087 1.00 86.97 C ANISOU 4098 CG GLN B 289 15641 8064 9338 -1132 4403 1231 C ATOM 4099 CD GLN B 289 37.764 -2.628 61.033 1.00109.34 C ANISOU 4099 CD GLN B 289 18202 10804 12536 -1261 4477 1185 C ATOM 4100 OE1 GLN B 289 37.185 -1.526 61.051 1.00103.46 O ANISOU 4100 OE1 GLN B 289 17664 9902 11742 -1240 4411 1310 O ATOM 4101 NE2 GLN B 289 38.760 -2.903 61.864 1.00103.58 N ANISOU 4101 NE2 GLN B 289 17000 10167 12188 -1391 4594 995 N ATOM 4102 N MET B 290 34.111 -3.855 58.016 1.00 82.97 N ANISOU 4102 N MET B 290 16334 7462 7729 -653 3651 1680 N ATOM 4103 CA MET B 290 32.801 -4.154 58.581 1.00 83.23 C ANISOU 4103 CA MET B 290 16257 7638 7728 -480 3124 1696 C ATOM 4104 C MET B 290 32.040 -5.236 57.803 1.00 83.78 C ANISOU 4104 C MET B 290 16535 7828 7469 -343 2852 1706 C ATOM 4105 O MET B 290 31.298 -6.000 58.422 1.00 83.33 O ANISOU 4105 O MET B 290 16191 7971 7498 -259 2495 1621 O ATOM 4106 CB MET B 290 31.937 -2.897 58.755 1.00 86.59 C ANISOU 4106 CB MET B 290 16871 7900 8128 -396 2958 1855 C ATOM 4107 CG MET B 290 31.514 -2.218 57.462 1.00 91.95 C ANISOU 4107 CG MET B 290 18159 8400 8377 -270 2885 2066 C ATOM 4108 SD MET B 290 30.359 -0.849 57.735 1.00 97.51 S ANISOU 4108 SD MET B 290 18955 9060 9035 -49 2379 2210 S ATOM 4109 CE MET B 290 28.919 -1.737 57.990 1.00 93.71 C ANISOU 4109 CE MET B 290 17952 8897 8757 25 1972 2038 C ATOM 4110 N ARG B 291 32.273 -5.336 56.474 1.00 77.84 N ANISOU 4110 N ARG B 291 16281 6950 6346 -330 3035 1800 N ATOM 4111 CA ARG B 291 31.653 -6.342 55.601 1.00 76.69 C ANISOU 4111 CA ARG B 291 16398 6890 5850 -213 2797 1802 C ATOM 4112 C ARG B 291 32.148 -7.733 56.018 1.00 76.80 C ANISOU 4112 C ARG B 291 16060 7117 6004 -260 2820 1601 C ATOM 4113 O ARG B 291 31.357 -8.683 56.055 1.00 75.52 O ANISOU 4113 O ARG B 291 15844 7106 5742 -158 2459 1548 O ATOM 4114 CB ARG B 291 31.860 -6.083 54.099 1.00 78.30 C ANISOU 4114 CB ARG B 291 17262 6885 5604 -196 3023 1945 C ATOM 4115 CG ARG B 291 30.999 -4.937 53.552 1.00 86.81 C ANISOU 4115 CG ARG B 291 18765 7769 6449 -79 2837 2165 C ATOM 4116 CD ARG B 291 30.531 -5.208 52.130 1.00106.51 C ANISOU 4116 CD ARG B 291 21905 10160 8405 35 2733 2285 C ATOM 4117 NE ARG B 291 29.865 -4.047 51.529 1.00123.93 N ANISOU 4117 NE ARG B 291 24574 12145 10370 148 2603 2511 N ATOM 4118 CZ ARG B 291 28.563 -3.787 51.622 1.00137.80 C ANISOU 4118 CZ ARG B 291 26367 13927 12065 332 2076 2598 C ATOM 4119 NH1 ARG B 291 27.759 -4.608 52.293 1.00120.75 N ANISOU 4119 NH1 ARG B 291 23803 12006 10072 411 1643 2476 N ATOM 4120 NH2 ARG B 291 28.054 -2.705 51.048 1.00122.93 N ANISOU 4120 NH2 ARG B 291 24919 11821 9967 442 1983 2809 N ATOM 4121 N ALA B 292 33.444 -7.823 56.394 1.00 70.88 N ANISOU 4121 N ALA B 292 15042 6369 5519 -416 3233 1485 N ATOM 4122 CA ALA B 292 34.097 -9.030 56.905 1.00 69.25 C ANISOU 4122 CA ALA B 292 14457 6343 5512 -465 3301 1292 C ATOM 4123 C ALA B 292 33.539 -9.353 58.306 1.00 74.55 C ANISOU 4123 C ALA B 292 14611 7216 6499 -426 2934 1192 C ATOM 4124 O ALA B 292 33.285 -10.517 58.625 1.00 77.06 O ANISOU 4124 O ALA B 292 14734 7705 6841 -376 2730 1083 O ATOM 4125 CB ALA B 292 35.600 -8.801 56.988 1.00 69.30 C ANISOU 4125 CB ALA B 292 14296 6273 5764 -635 3826 1210 C ATOM 4126 N ARG B 293 33.354 -8.311 59.137 1.00 68.30 N ANISOU 4126 N ARG B 293 13624 6388 5940 -451 2868 1231 N ATOM 4127 CA ARG B 293 32.846 -8.396 60.500 1.00 66.27 C ANISOU 4127 CA ARG B 293 12921 6286 5972 -420 2565 1151 C ATOM 4128 C ARG B 293 31.371 -8.781 60.549 1.00 70.56 C ANISOU 4128 C ARG B 293 13528 6925 6357 -260 2093 1205 C ATOM 4129 O ARG B 293 30.928 -9.399 61.520 1.00 70.83 O ANISOU 4129 O ARG B 293 13216 7129 6568 -222 1841 1112 O ATOM 4130 CB ARG B 293 33.084 -7.067 61.224 1.00 61.67 C ANISOU 4130 CB ARG B 293 12194 5596 5641 -495 2668 1182 C ATOM 4131 CG ARG B 293 34.458 -6.974 61.855 1.00 56.93 C ANISOU 4131 CG ARG B 293 11259 4998 5374 -661 2996 1045 C ATOM 4132 CD ARG B 293 34.699 -5.565 62.292 1.00 61.71 C ANISOU 4132 CD ARG B 293 11830 5446 6170 -749 3129 1090 C ATOM 4133 NE ARG B 293 35.798 -5.462 63.244 1.00 69.38 N ANISOU 4133 NE ARG B 293 12381 6453 7526 -897 3314 931 N ATOM 4134 CZ ARG B 293 36.231 -4.316 63.759 1.00 81.53 C ANISOU 4134 CZ ARG B 293 13818 7861 9297 -1010 3456 922 C ATOM 4135 NH1 ARG B 293 35.678 -3.163 63.392 1.00 67.92 N ANISOU 4135 NH1 ARG B 293 12395 5951 7460 -988 3462 1073 N ATOM 4136 NH2 ARG B 293 37.226 -4.311 64.634 1.00 66.32 N ANISOU 4136 NH2 ARG B 293 11495 5980 7724 -1143 3581 758 N ATOM 4137 N ARG B 294 30.612 -8.402 59.513 1.00 67.49 N ANISOU 4137 N ARG B 294 13582 6418 5642 -165 1974 1357 N ATOM 4138 CA ARG B 294 29.190 -8.714 59.358 1.00 67.19 C ANISOU 4138 CA ARG B 294 13640 6447 5443 -9 1519 1416 C ATOM 4139 C ARG B 294 29.044 -10.217 59.145 1.00 70.91 C ANISOU 4139 C ARG B 294 14059 7074 5810 16 1373 1305 C ATOM 4140 O ARG B 294 28.153 -10.832 59.745 1.00 72.17 O ANISOU 4140 O ARG B 294 13987 7376 6058 88 1027 1255 O ATOM 4141 CB ARG B 294 28.605 -7.959 58.150 1.00 65.95 C ANISOU 4141 CB ARG B 294 14017 6104 4937 84 1449 1602 C ATOM 4142 CG ARG B 294 28.159 -6.547 58.447 1.00 69.59 C ANISOU 4142 CG ARG B 294 14522 6425 5493 129 1397 1732 C ATOM 4143 CD ARG B 294 27.528 -5.943 57.209 1.00 79.80 C ANISOU 4143 CD ARG B 294 16366 7540 6414 249 1274 1920 C ATOM 4144 NE ARG B 294 26.787 -4.729 57.536 1.00 84.69 N ANISOU 4144 NE ARG B 294 17005 8042 7130 344 1107 2046 N ATOM 4145 CZ ARG B 294 26.168 -3.962 56.649 1.00 96.51 C ANISOU 4145 CZ ARG B 294 18949 9359 8362 469 974 2229 C ATOM 4146 NH1 ARG B 294 26.165 -4.292 55.365 1.00 85.82 N ANISOU 4146 NH1 ARG B 294 18084 7925 6599 512 969 2309 N ATOM 4147 NH2 ARG B 294 25.536 -2.863 57.040 1.00 79.74 N ANISOU 4147 NH2 ARG B 294 16804 7124 6369 561 836 2332 N ATOM 4148 N LYS B 295 29.952 -10.804 58.322 1.00 65.15 N ANISOU 4148 N LYS B 295 13538 6306 4910 -49 1665 1260 N ATOM 4149 CA LYS B 295 30.006 -12.233 58.011 1.00 64.82 C ANISOU 4149 CA LYS B 295 13495 6379 4756 -36 1599 1145 C ATOM 4150 C LYS B 295 30.268 -13.072 59.262 1.00 67.42 C ANISOU 4150 C LYS B 295 13299 6891 5425 -75 1545 986 C ATOM 4151 O LYS B 295 29.535 -14.027 59.497 1.00 67.96 O ANISOU 4151 O LYS B 295 13256 7083 5481 -16 1248 925 O ATOM 4152 CB LYS B 295 31.037 -12.531 56.909 1.00 67.24 C ANISOU 4152 CB LYS B 295 14141 6578 4830 -98 1993 1131 C ATOM 4153 CG LYS B 295 30.610 -12.032 55.530 1.00 84.57 C ANISOU 4153 CG LYS B 295 16945 8601 6587 -34 1980 1282 C ATOM 4154 CD LYS B 295 31.675 -12.280 54.460 1.00 90.19 C ANISOU 4154 CD LYS B 295 18017 9190 7062 -102 2428 1267 C ATOM 4155 CE LYS B 295 31.069 -12.417 53.090 1.00 99.20 C ANISOU 4155 CE LYS B 295 19778 10218 7695 -10 2300 1365 C ATOM 4156 NZ LYS B 295 32.013 -13.057 52.137 1.00114.39 N ANISOU 4156 NZ LYS B 295 22020 12062 9382 -65 2702 1303 N ATOM 4157 N THR B 296 31.278 -12.697 60.074 1.00 62.60 N ANISOU 4157 N THR B 296 12377 6290 5119 -175 1815 922 N ATOM 4158 CA THR B 296 31.627 -13.383 61.322 1.00 62.29 C ANISOU 4158 CA THR B 296 11857 6408 5402 -208 1771 779 C ATOM 4159 C THR B 296 30.496 -13.285 62.368 1.00 66.67 C ANISOU 4159 C THR B 296 12158 7069 6105 -140 1395 788 C ATOM 4160 O THR B 296 30.131 -14.306 62.948 1.00 66.98 O ANISOU 4160 O THR B 296 11981 7245 6224 -108 1198 702 O ATOM 4161 CB THR B 296 32.950 -12.854 61.889 1.00 68.64 C ANISOU 4161 CB THR B 296 12417 7175 6486 -328 2124 712 C ATOM 4162 OG1 THR B 296 33.953 -12.922 60.883 1.00 65.07 O ANISOU 4162 OG1 THR B 296 12198 6615 5911 -391 2502 706 O ATOM 4163 CG2 THR B 296 33.404 -13.617 63.156 1.00 66.71 C ANISOU 4163 CG2 THR B 296 11700 7089 6557 -351 2065 560 C ATOM 4164 N ALA B 297 29.967 -12.062 62.611 1.00 62.96 N ANISOU 4164 N ALA B 297 11721 6522 5680 -119 1320 891 N ATOM 4165 CA ALA B 297 28.898 -11.786 63.578 1.00 62.52 C ANISOU 4165 CA ALA B 297 11440 6540 5774 -51 1010 906 C ATOM 4166 C ALA B 297 27.617 -12.530 63.253 1.00 65.91 C ANISOU 4166 C ALA B 297 11947 7044 6053 57 652 930 C ATOM 4167 O ALA B 297 26.959 -12.996 64.180 1.00 65.90 O ANISOU 4167 O ALA B 297 11659 7163 6216 87 440 872 O ATOM 4168 CB ALA B 297 28.634 -10.287 63.685 1.00 63.16 C ANISOU 4168 CB ALA B 297 11612 6486 5898 -37 1034 1020 C ATOM 4169 N LYS B 298 27.278 -12.684 61.945 1.00 61.39 N ANISOU 4169 N LYS B 298 11765 6394 5168 108 585 1006 N ATOM 4170 CA LYS B 298 26.092 -13.435 61.529 1.00 60.41 C ANISOU 4170 CA LYS B 298 11729 6328 4894 200 223 1015 C ATOM 4171 C LYS B 298 26.279 -14.874 62.022 1.00 63.41 C ANISOU 4171 C LYS B 298 11870 6853 5368 162 186 869 C ATOM 4172 O LYS B 298 25.451 -15.373 62.797 1.00 63.21 O ANISOU 4172 O LYS B 298 11585 6934 5496 195 -65 827 O ATOM 4173 CB LYS B 298 25.913 -13.378 60.009 1.00 62.88 C ANISOU 4173 CB LYS B 298 12541 6522 4827 248 189 1104 C ATOM 4174 CG LYS B 298 24.640 -14.060 59.492 1.00 80.43 C ANISOU 4174 CG LYS B 298 14876 8791 6892 344 -231 1110 C ATOM 4175 CD LYS B 298 24.599 -14.043 57.962 1.00 96.05 C ANISOU 4175 CD LYS B 298 17393 10644 8456 389 -261 1185 C ATOM 4176 CE LYS B 298 23.226 -14.316 57.397 1.00105.53 C ANISOU 4176 CE LYS B 298 18738 11854 9504 502 -735 1222 C ATOM 4177 NZ LYS B 298 23.196 -14.148 55.920 1.00107.37 N ANISOU 4177 NZ LYS B 298 19545 11947 9304 557 -779 1309 N ATOM 4178 N MET B 299 27.430 -15.482 61.668 1.00 57.87 N ANISOU 4178 N MET B 299 11236 6144 4608 91 469 793 N ATOM 4179 CA MET B 299 27.807 -16.829 62.084 1.00 56.67 C ANISOU 4179 CA MET B 299 10886 6103 4545 59 485 655 C ATOM 4180 C MET B 299 27.799 -17.028 63.619 1.00 58.04 C ANISOU 4180 C MET B 299 10605 6395 5051 39 428 584 C ATOM 4181 O MET B 299 27.235 -18.015 64.073 1.00 58.72 O ANISOU 4181 O MET B 299 10536 6576 5198 60 230 521 O ATOM 4182 CB MET B 299 29.163 -17.200 61.496 1.00 58.86 C ANISOU 4182 CB MET B 299 11291 6327 4746 -4 852 593 C ATOM 4183 CG MET B 299 29.504 -18.636 61.679 1.00 62.71 C ANISOU 4183 CG MET B 299 11649 6899 5277 -13 860 460 C ATOM 4184 SD MET B 299 31.091 -18.995 60.932 1.00 67.56 S ANISOU 4184 SD MET B 299 12402 7438 5832 -71 1318 384 S ATOM 4185 CE MET B 299 32.205 -18.379 62.236 1.00 63.70 C ANISOU 4185 CE MET B 299 11462 6990 5750 -142 1548 334 C ATOM 4186 N LEU B 300 28.414 -16.115 64.395 1.00 51.70 N ANISOU 4186 N LEU B 300 9617 5577 4449 -4 598 591 N ATOM 4187 CA LEU B 300 28.480 -16.209 65.856 1.00 51.01 C ANISOU 4187 CA LEU B 300 9146 5590 4646 -21 552 523 C ATOM 4188 C LEU B 300 27.129 -16.132 66.546 1.00 55.07 C ANISOU 4188 C LEU B 300 9526 6163 5234 42 248 558 C ATOM 4189 O LEU B 300 26.935 -16.836 67.529 1.00 54.49 O ANISOU 4189 O LEU B 300 9203 6190 5310 43 153 488 O ATOM 4190 CB LEU B 300 29.415 -15.171 66.464 1.00 51.04 C ANISOU 4190 CB LEU B 300 9013 5548 4833 -87 782 514 C ATOM 4191 CG LEU B 300 30.866 -15.150 66.009 1.00 55.47 C ANISOU 4191 CG LEU B 300 9608 6053 5416 -167 1120 461 C ATOM 4192 CD1 LEU B 300 31.582 -13.933 66.596 1.00 54.87 C ANISOU 4192 CD1 LEU B 300 9403 5911 5536 -242 1304 461 C ATOM 4193 CD2 LEU B 300 31.582 -16.473 66.314 1.00 56.46 C ANISOU 4193 CD2 LEU B 300 9553 6272 5628 -177 1170 333 C ATOM 4194 N MET B 301 26.212 -15.272 66.048 1.00 52.74 N ANISOU 4194 N MET B 301 9397 5798 4846 101 106 669 N ATOM 4195 CA MET B 301 24.849 -15.078 66.558 1.00 52.84 C ANISOU 4195 CA MET B 301 9289 5847 4942 174 -175 710 C ATOM 4196 C MET B 301 24.042 -16.369 66.349 1.00 56.43 C ANISOU 4196 C MET B 301 9720 6380 5341 199 -410 665 C ATOM 4197 O MET B 301 23.217 -16.749 67.195 1.00 56.34 O ANISOU 4197 O MET B 301 9473 6445 5490 220 -575 637 O ATOM 4198 CB MET B 301 24.157 -13.886 65.849 1.00 55.61 C ANISOU 4198 CB MET B 301 9860 6082 5189 246 -270 842 C ATOM 4199 CG MET B 301 24.637 -12.494 66.313 1.00 60.09 C ANISOU 4199 CG MET B 301 10401 6560 5872 228 -85 890 C ATOM 4200 SD MET B 301 24.157 -11.184 65.123 1.00 66.33 S ANISOU 4200 SD MET B 301 11570 7167 6467 311 -130 1060 S ATOM 4201 CE MET B 301 25.219 -9.817 65.656 1.00 62.99 C ANISOU 4201 CE MET B 301 11119 6627 6187 229 202 1075 C ATOM 4202 N VAL B 302 24.314 -17.061 65.229 1.00 51.91 N ANISOU 4202 N VAL B 302 9400 5779 4544 190 -402 651 N ATOM 4203 CA VAL B 302 23.661 -18.322 64.880 1.00 50.86 C ANISOU 4203 CA VAL B 302 9289 5699 4337 198 -612 595 C ATOM 4204 C VAL B 302 24.158 -19.444 65.811 1.00 54.64 C ANISOU 4204 C VAL B 302 9514 6271 4976 144 -530 480 C ATOM 4205 O VAL B 302 23.334 -20.221 66.302 1.00 56.33 O ANISOU 4205 O VAL B 302 9565 6548 5292 148 -720 442 O ATOM 4206 CB VAL B 302 23.778 -18.635 63.360 1.00 53.36 C ANISOU 4206 CB VAL B 302 10000 5937 4335 210 -634 610 C ATOM 4207 CG1 VAL B 302 23.303 -20.053 63.028 1.00 53.02 C ANISOU 4207 CG1 VAL B 302 9982 5940 4222 198 -820 520 C ATOM 4208 CG2 VAL B 302 22.996 -17.609 62.545 1.00 52.40 C ANISOU 4208 CG2 VAL B 302 10126 5725 4058 286 -807 734 C ATOM 4209 N VAL B 303 25.483 -19.479 66.100 1.00 48.08 N ANISOU 4209 N VAL B 303 8639 5441 4189 97 -249 429 N ATOM 4210 CA VAL B 303 26.109 -20.435 67.013 1.00 46.37 C ANISOU 4210 CA VAL B 303 8194 5300 4127 63 -162 329 C ATOM 4211 C VAL B 303 25.516 -20.264 68.415 1.00 51.83 C ANISOU 4211 C VAL B 303 8589 6062 5043 71 -268 329 C ATOM 4212 O VAL B 303 25.224 -21.261 69.071 1.00 52.74 O ANISOU 4212 O VAL B 303 8558 6236 5244 66 -355 274 O ATOM 4213 CB VAL B 303 27.662 -20.329 67.027 1.00 48.61 C ANISOU 4213 CB VAL B 303 8462 5561 4447 23 147 277 C ATOM 4214 CG1 VAL B 303 28.272 -21.197 68.135 1.00 47.87 C ANISOU 4214 CG1 VAL B 303 8103 5544 4542 10 193 182 C ATOM 4215 CG2 VAL B 303 28.256 -20.710 65.674 1.00 47.97 C ANISOU 4215 CG2 VAL B 303 8673 5407 4145 14 291 262 C ATOM 4216 N VAL B 304 25.309 -19.003 68.850 1.00 48.38 N ANISOU 4216 N VAL B 304 8089 5604 4691 85 -249 391 N ATOM 4217 CA VAL B 304 24.790 -18.669 70.169 1.00 48.31 C ANISOU 4217 CA VAL B 304 7833 5645 4877 97 -312 389 C ATOM 4218 C VAL B 304 23.290 -19.006 70.268 1.00 53.79 C ANISOU 4218 C VAL B 304 8467 6365 5606 137 -559 419 C ATOM 4219 O VAL B 304 22.864 -19.499 71.308 1.00 53.87 O ANISOU 4219 O VAL B 304 8278 6433 5756 132 -605 384 O ATOM 4220 CB VAL B 304 25.148 -17.211 70.585 1.00 51.60 C ANISOU 4220 CB VAL B 304 8218 6013 5375 95 -192 429 C ATOM 4221 CG1 VAL B 304 24.516 -16.822 71.921 1.00 50.90 C ANISOU 4221 CG1 VAL B 304 7911 5964 5465 117 -256 423 C ATOM 4222 CG2 VAL B 304 26.660 -17.026 70.657 1.00 51.28 C ANISOU 4222 CG2 VAL B 304 8169 5954 5361 36 49 374 C ATOM 4223 N LEU B 305 22.510 -18.794 69.193 1.00 51.39 N ANISOU 4223 N LEU B 305 8336 6013 5177 174 -716 480 N ATOM 4224 CA LEU B 305 21.074 -19.105 69.182 1.00 51.38 C ANISOU 4224 CA LEU B 305 8255 6031 5238 210 -972 499 C ATOM 4225 C LEU B 305 20.827 -20.620 69.210 1.00 53.83 C ANISOU 4225 C LEU B 305 8512 6390 5553 165 -1061 421 C ATOM 4226 O LEU B 305 19.917 -21.089 69.905 1.00 53.55 O ANISOU 4226 O LEU B 305 8278 6393 5676 159 -1175 403 O ATOM 4227 CB LEU B 305 20.370 -18.444 67.969 1.00 51.90 C ANISOU 4227 CB LEU B 305 8533 6023 5161 273 -1150 582 C ATOM 4228 CG LEU B 305 18.832 -18.655 67.830 1.00 57.24 C ANISOU 4228 CG LEU B 305 9108 6710 5929 321 -1456 601 C ATOM 4229 CD1 LEU B 305 18.039 -18.088 69.043 1.00 56.88 C ANISOU 4229 CD1 LEU B 305 8760 6695 6157 354 -1465 615 C ATOM 4230 CD2 LEU B 305 18.310 -18.087 66.510 1.00 59.17 C ANISOU 4230 CD2 LEU B 305 9607 6876 5998 396 -1658 680 C ATOM 4231 N VAL B 306 21.646 -21.381 68.452 1.00 49.34 N ANISOU 4231 N VAL B 306 8125 5805 4818 132 -990 373 N ATOM 4232 CA VAL B 306 21.564 -22.848 68.359 1.00 47.33 C ANISOU 4232 CA VAL B 306 7867 5571 4545 89 -1053 292 C ATOM 4233 C VAL B 306 21.933 -23.476 69.683 1.00 48.13 C ANISOU 4233 C VAL B 306 7741 5728 4820 59 -940 242 C ATOM 4234 O VAL B 306 21.248 -24.391 70.105 1.00 47.86 O ANISOU 4234 O VAL B 306 7593 5712 4879 31 -1046 208 O ATOM 4235 CB VAL B 306 22.354 -23.409 67.148 1.00 50.15 C ANISOU 4235 CB VAL B 306 8507 5879 4667 76 -985 252 C ATOM 4236 CG1 VAL B 306 22.540 -24.928 67.231 1.00 49.26 C ANISOU 4236 CG1 VAL B 306 8382 5777 4559 34 -986 154 C ATOM 4237 CG2 VAL B 306 21.656 -23.026 65.848 1.00 49.81 C ANISOU 4237 CG2 VAL B 306 8718 5778 4430 108 -1178 298 C ATOM 4238 N PHE B 307 22.968 -22.944 70.355 1.00 44.17 N ANISOU 4238 N PHE B 307 7173 5242 4366 63 -737 238 N ATOM 4239 CA PHE B 307 23.424 -23.371 71.670 1.00 44.12 C ANISOU 4239 CA PHE B 307 6977 5283 4504 50 -640 197 C ATOM 4240 C PHE B 307 22.295 -23.144 72.709 1.00 51.14 C ANISOU 4240 C PHE B 307 7676 6201 5553 56 -734 228 C ATOM 4241 O PHE B 307 21.998 -24.037 73.505 1.00 52.43 O ANISOU 4241 O PHE B 307 7731 6386 5802 35 -751 198 O ATOM 4242 CB PHE B 307 24.696 -22.598 72.065 1.00 45.66 C ANISOU 4242 CB PHE B 307 7144 5481 4722 56 -443 187 C ATOM 4243 CG PHE B 307 25.237 -23.006 73.418 1.00 47.78 C ANISOU 4243 CG PHE B 307 7241 5796 5120 54 -375 140 C ATOM 4244 CD1 PHE B 307 24.736 -22.436 74.591 1.00 49.69 C ANISOU 4244 CD1 PHE B 307 7338 6064 5478 64 -396 162 C ATOM 4245 CD2 PHE B 307 26.206 -24.003 73.528 1.00 50.25 C ANISOU 4245 CD2 PHE B 307 7550 6114 5428 55 -299 74 C ATOM 4246 CE1 PHE B 307 25.186 -22.862 75.841 1.00 49.64 C ANISOU 4246 CE1 PHE B 307 7216 6092 5553 69 -354 121 C ATOM 4247 CE2 PHE B 307 26.684 -24.398 74.781 1.00 52.50 C ANISOU 4247 CE2 PHE B 307 7696 6433 5817 69 -271 37 C ATOM 4248 CZ PHE B 307 26.166 -23.823 75.929 1.00 49.73 C ANISOU 4248 CZ PHE B 307 7232 6110 5553 74 -305 63 C ATOM 4249 N ALA B 308 21.673 -21.955 72.681 1.00 47.29 N ANISOU 4249 N ALA B 308 7161 5702 5106 88 -777 290 N ATOM 4250 CA ALA B 308 20.571 -21.570 73.550 1.00 46.82 C ANISOU 4250 CA ALA B 308 6926 5657 5206 106 -840 319 C ATOM 4251 C ALA B 308 19.359 -22.488 73.329 1.00 51.93 C ANISOU 4251 C ALA B 308 7509 6306 5917 84 -1013 311 C ATOM 4252 O ALA B 308 18.709 -22.853 74.295 1.00 52.17 O ANISOU 4252 O ALA B 308 7372 6354 6095 67 -1005 302 O ATOM 4253 CB ALA B 308 20.200 -20.101 73.311 1.00 47.11 C ANISOU 4253 CB ALA B 308 6978 5658 5263 160 -856 385 C ATOM 4254 N LEU B 309 19.077 -22.893 72.075 1.00 49.51 N ANISOU 4254 N LEU B 309 7343 5972 5498 76 -1162 307 N ATOM 4255 CA LEU B 309 17.965 -23.805 71.749 1.00 49.32 C ANISOU 4255 CA LEU B 309 7261 5939 5540 40 -1355 282 C ATOM 4256 C LEU B 309 18.224 -25.232 72.197 1.00 51.58 C ANISOU 4256 C LEU B 309 7521 6230 5848 -29 -1301 214 C ATOM 4257 O LEU B 309 17.355 -25.856 72.811 1.00 51.05 O ANISOU 4257 O LEU B 309 7294 6163 5942 -73 -1348 199 O ATOM 4258 CB LEU B 309 17.609 -23.758 70.245 1.00 49.86 C ANISOU 4258 CB LEU B 309 7522 5967 5456 57 -1560 290 C ATOM 4259 CG LEU B 309 16.903 -22.477 69.750 1.00 54.67 C ANISOU 4259 CG LEU B 309 8141 6552 6078 136 -1699 367 C ATOM 4260 CD1 LEU B 309 16.748 -22.495 68.239 1.00 54.61 C ANISOU 4260 CD1 LEU B 309 8395 6496 5858 160 -1897 377 C ATOM 4261 CD2 LEU B 309 15.525 -22.291 70.418 1.00 56.45 C ANISOU 4261 CD2 LEU B 309 8088 6792 6570 150 -1827 380 C ATOM 4262 N CYS B 310 19.435 -25.733 71.916 1.00 47.46 N ANISOU 4262 N CYS B 310 7151 5702 5180 -36 -1186 176 N ATOM 4263 CA CYS B 310 19.893 -27.068 72.271 1.00 47.10 C ANISOU 4263 CA CYS B 310 7117 5644 5134 -81 -1123 115 C ATOM 4264 C CYS B 310 19.957 -27.290 73.771 1.00 48.79 C ANISOU 4264 C CYS B 310 7164 5882 5490 -88 -1000 122 C ATOM 4265 O CYS B 310 19.727 -28.412 74.231 1.00 47.43 O ANISOU 4265 O CYS B 310 6959 5685 5378 -133 -998 91 O ATOM 4266 CB CYS B 310 21.248 -27.333 71.631 1.00 48.30 C ANISOU 4266 CB CYS B 310 7455 5780 5117 -62 -1008 75 C ATOM 4267 SG CYS B 310 21.165 -27.692 69.862 1.00 53.22 S ANISOU 4267 SG CYS B 310 8346 6346 5529 -73 -1139 38 S ATOM 4268 N TYR B 311 20.361 -26.252 74.532 1.00 43.53 N ANISOU 4268 N TYR B 311 6426 5252 4860 -44 -889 158 N ATOM 4269 CA TYR B 311 20.553 -26.385 75.970 1.00 41.86 C ANISOU 4269 CA TYR B 311 6105 5061 4740 -39 -772 162 C ATOM 4270 C TYR B 311 19.348 -25.947 76.775 1.00 45.72 C ANISOU 4270 C TYR B 311 6436 5555 5380 -47 -782 200 C ATOM 4271 O TYR B 311 19.330 -26.170 77.972 1.00 44.19 O ANISOU 4271 O TYR B 311 6178 5365 5247 -50 -682 203 O ATOM 4272 CB TYR B 311 21.843 -25.680 76.426 1.00 41.72 C ANISOU 4272 CB TYR B 311 6111 5071 4668 7 -643 154 C ATOM 4273 CG TYR B 311 23.102 -26.467 76.108 1.00 43.21 C ANISOU 4273 CG TYR B 311 6397 5250 4770 16 -586 103 C ATOM 4274 CD1 TYR B 311 23.637 -26.480 74.818 1.00 45.40 C ANISOU 4274 CD1 TYR B 311 6804 5509 4939 17 -589 81 C ATOM 4275 CD2 TYR B 311 23.743 -27.221 77.088 1.00 43.66 C ANISOU 4275 CD2 TYR B 311 6427 5308 4852 33 -526 77 C ATOM 4276 CE1 TYR B 311 24.764 -27.234 74.508 1.00 44.32 C ANISOU 4276 CE1 TYR B 311 6741 5354 4744 33 -513 25 C ATOM 4277 CE2 TYR B 311 24.902 -27.942 76.801 1.00 44.63 C ANISOU 4277 CE2 TYR B 311 6616 5416 4925 59 -479 26 C ATOM 4278 CZ TYR B 311 25.414 -27.935 75.510 1.00 54.24 C ANISOU 4278 CZ TYR B 311 7935 6616 6059 59 -461 -3 C ATOM 4279 OH TYR B 311 26.564 -28.627 75.217 1.00 59.34 O ANISOU 4279 OH TYR B 311 8630 7240 6677 92 -386 -61 O ATOM 4280 N LEU B 312 18.322 -25.389 76.130 1.00 44.88 N ANISOU 4280 N LEU B 312 6273 5441 5337 -45 -902 226 N ATOM 4281 CA LEU B 312 17.129 -24.919 76.836 1.00 45.87 C ANISOU 4281 CA LEU B 312 6220 5566 5643 -43 -901 256 C ATOM 4282 C LEU B 312 16.322 -26.056 77.481 1.00 50.15 C ANISOU 4282 C LEU B 312 6656 6082 6318 -115 -882 239 C ATOM 4283 O LEU B 312 16.067 -25.940 78.687 1.00 49.70 O ANISOU 4283 O LEU B 312 6510 6023 6350 -114 -739 255 O ATOM 4284 CB LEU B 312 16.241 -24.020 75.950 1.00 46.16 C ANISOU 4284 CB LEU B 312 6208 5594 5736 -4 -1057 289 C ATOM 4285 CG LEU B 312 14.947 -23.481 76.559 1.00 50.95 C ANISOU 4285 CG LEU B 312 6600 6191 6566 16 -1061 315 C ATOM 4286 CD1 LEU B 312 15.230 -22.362 77.541 1.00 50.84 C ANISOU 4286 CD1 LEU B 312 6554 6187 6576 78 -893 341 C ATOM 4287 CD2 LEU B 312 14.060 -22.946 75.474 1.00 54.69 C ANISOU 4287 CD2 LEU B 312 7032 6648 7100 55 -1281 337 C ATOM 4288 N PRO B 313 15.927 -27.155 76.758 1.00 46.12 N ANISOU 4288 N PRO B 313 6167 5537 5820 -184 -1004 204 N ATOM 4289 CA PRO B 313 15.135 -28.204 77.416 1.00 45.09 C ANISOU 4289 CA PRO B 313 5929 5362 5841 -268 -962 190 C ATOM 4290 C PRO B 313 15.826 -28.849 78.617 1.00 49.91 C ANISOU 4290 C PRO B 313 6603 5956 6404 -277 -768 197 C ATOM 4291 O PRO B 313 15.231 -28.898 79.695 1.00 51.05 O ANISOU 4291 O PRO B 313 6647 6081 6670 -299 -636 222 O ATOM 4292 CB PRO B 313 14.843 -29.192 76.284 1.00 46.38 C ANISOU 4292 CB PRO B 313 6153 5484 5987 -338 -1142 138 C ATOM 4293 CG PRO B 313 14.998 -28.406 75.046 1.00 50.42 C ANISOU 4293 CG PRO B 313 6750 6023 6384 -281 -1310 138 C ATOM 4294 CD PRO B 313 16.113 -27.476 75.325 1.00 46.54 C ANISOU 4294 CD PRO B 313 6354 5576 5752 -194 -1179 173 C ATOM 4295 N ILE B 314 17.082 -29.294 78.465 1.00 45.60 N ANISOU 4295 N ILE B 314 6227 5412 5686 -248 -743 178 N ATOM 4296 CA ILE B 314 17.801 -29.926 79.573 1.00 45.20 C ANISOU 4296 CA ILE B 314 6252 5340 5581 -236 -599 187 C ATOM 4297 C ILE B 314 17.853 -29.018 80.804 1.00 49.18 C ANISOU 4297 C ILE B 314 6710 5879 6099 -184 -464 224 C ATOM 4298 O ILE B 314 17.511 -29.473 81.888 1.00 50.07 O ANISOU 4298 O ILE B 314 6820 5953 6253 -206 -343 249 O ATOM 4299 CB ILE B 314 19.198 -30.472 79.160 1.00 48.01 C ANISOU 4299 CB ILE B 314 6771 5694 5776 -192 -610 153 C ATOM 4300 CG1 ILE B 314 19.687 -31.532 80.183 1.00 47.97 C ANISOU 4300 CG1 ILE B 314 6847 5635 5745 -187 -512 162 C ATOM 4301 CG2 ILE B 314 20.234 -29.337 78.895 1.00 47.12 C ANISOU 4301 CG2 ILE B 314 6691 5650 5561 -112 -600 148 C ATOM 4302 CD1 ILE B 314 20.833 -32.363 79.754 1.00 56.29 C ANISOU 4302 CD1 ILE B 314 8034 6659 6694 -148 -533 122 C ATOM 4303 N SER B 315 18.196 -27.733 80.608 1.00 44.96 N ANISOU 4303 N SER B 315 6154 5401 5527 -122 -478 228 N ATOM 4304 CA SER B 315 18.328 -26.685 81.630 1.00 44.51 C ANISOU 4304 CA SER B 315 6071 5372 5469 -69 -368 247 C ATOM 4305 C SER B 315 17.036 -26.378 82.371 1.00 51.45 C ANISOU 4305 C SER B 315 6821 6227 6501 -91 -278 274 C ATOM 4306 O SER B 315 17.043 -26.276 83.602 1.00 50.75 O ANISOU 4306 O SER B 315 6762 6125 6397 -74 -134 286 O ATOM 4307 CB SER B 315 18.851 -25.403 81.000 1.00 42.46 C ANISOU 4307 CB SER B 315 5817 5154 5161 -15 -417 241 C ATOM 4308 OG SER B 315 20.146 -25.638 80.488 1.00 41.11 O ANISOU 4308 OG SER B 315 5757 5001 4863 4 -448 211 O ATOM 4309 N VAL B 316 15.945 -26.190 81.608 1.00 49.78 N ANISOU 4309 N VAL B 316 6470 6007 6436 -120 -364 280 N ATOM 4310 CA VAL B 316 14.632 -25.877 82.134 1.00 50.32 C ANISOU 4310 CA VAL B 316 6366 6050 6704 -138 -285 298 C ATOM 4311 C VAL B 316 14.070 -27.101 82.869 1.00 55.78 C ANISOU 4311 C VAL B 316 7036 6681 7478 -224 -167 304 C ATOM 4312 O VAL B 316 13.612 -26.941 84.001 1.00 56.31 O ANISOU 4312 O VAL B 316 7070 6720 7606 -225 23 323 O ATOM 4313 CB VAL B 316 13.716 -25.274 81.034 1.00 54.06 C ANISOU 4313 CB VAL B 316 6685 6532 7323 -128 -452 299 C ATOM 4314 CG1 VAL B 316 12.231 -25.332 81.410 1.00 54.29 C ANISOU 4314 CG1 VAL B 316 6482 6522 7621 -165 -395 303 C ATOM 4315 CG2 VAL B 316 14.138 -23.844 80.729 1.00 53.04 C ANISOU 4315 CG2 VAL B 316 6590 6436 7128 -31 -490 313 C ATOM 4316 N LEU B 317 14.198 -28.315 82.282 1.00 52.21 N ANISOU 4316 N LEU B 317 6637 6196 7005 -295 -257 286 N ATOM 4317 CA LEU B 317 13.752 -29.571 82.902 1.00 51.89 C ANISOU 4317 CA LEU B 317 6605 6075 7035 -388 -145 295 C ATOM 4318 C LEU B 317 14.447 -29.826 84.245 1.00 57.27 C ANISOU 4318 C LEU B 317 7459 6732 7571 -354 45 328 C ATOM 4319 O LEU B 317 13.787 -30.199 85.222 1.00 57.61 O ANISOU 4319 O LEU B 317 7487 6710 7694 -402 231 358 O ATOM 4320 CB LEU B 317 13.991 -30.768 81.969 1.00 51.75 C ANISOU 4320 CB LEU B 317 6659 6017 6987 -456 -289 261 C ATOM 4321 CG LEU B 317 13.027 -31.002 80.805 1.00 55.84 C ANISOU 4321 CG LEU B 317 7025 6520 7673 -532 -474 220 C ATOM 4322 CD1 LEU B 317 13.555 -32.104 79.891 1.00 54.79 C ANISOU 4322 CD1 LEU B 317 7033 6346 7440 -580 -615 173 C ATOM 4323 CD2 LEU B 317 11.653 -31.388 81.295 1.00 58.41 C ANISOU 4323 CD2 LEU B 317 7145 6779 8271 -635 -380 222 C ATOM 4324 N ASN B 318 15.774 -29.627 84.294 1.00 54.32 N ANISOU 4324 N ASN B 318 7249 6401 6988 -272 -4 321 N ATOM 4325 CA ASN B 318 16.566 -29.779 85.512 1.00 54.36 C ANISOU 4325 CA ASN B 318 7430 6390 6835 -220 116 345 C ATOM 4326 C ASN B 318 16.096 -28.832 86.598 1.00 59.20 C ANISOU 4326 C ASN B 318 8020 7008 7464 -186 281 364 C ATOM 4327 O ASN B 318 15.960 -29.259 87.740 1.00 60.99 O ANISOU 4327 O ASN B 318 8361 7175 7636 -194 443 397 O ATOM 4328 CB ASN B 318 18.038 -29.575 85.237 1.00 55.88 C ANISOU 4328 CB ASN B 318 7743 6637 6852 -136 3 317 C ATOM 4329 CG ASN B 318 18.781 -30.856 85.039 1.00 79.48 C ANISOU 4329 CG ASN B 318 10862 9579 9759 -138 -55 313 C ATOM 4330 OD1 ASN B 318 18.314 -31.770 84.355 1.00 68.37 O ANISOU 4330 OD1 ASN B 318 9431 8120 8426 -209 -99 306 O ATOM 4331 ND2 ASN B 318 19.963 -30.940 85.636 1.00 78.56 N ANISOU 4331 ND2 ASN B 318 10881 9472 9495 -56 -67 309 N ATOM 4332 N VAL B 319 15.794 -27.570 86.247 1.00 54.24 N ANISOU 4332 N VAL B 319 7263 6437 6908 -149 251 345 N ATOM 4333 CA VAL B 319 15.276 -26.596 87.208 1.00 53.43 C ANISOU 4333 CA VAL B 319 7132 6330 6838 -111 415 351 C ATOM 4334 C VAL B 319 13.857 -26.965 87.654 1.00 57.78 C ANISOU 4334 C VAL B 319 7551 6813 7590 -183 593 376 C ATOM 4335 O VAL B 319 13.567 -26.917 88.844 1.00 57.57 O ANISOU 4335 O VAL B 319 7607 6737 7528 -178 808 395 O ATOM 4336 CB VAL B 319 15.407 -25.142 86.683 1.00 56.33 C ANISOU 4336 CB VAL B 319 7412 6758 7231 -43 333 324 C ATOM 4337 CG1 VAL B 319 14.379 -24.197 87.329 1.00 55.95 C ANISOU 4337 CG1 VAL B 319 7253 6686 7321 -16 497 326 C ATOM 4338 CG2 VAL B 319 16.815 -24.641 86.935 1.00 55.86 C ANISOU 4338 CG2 VAL B 319 7515 6740 6968 23 272 297 C ATOM 4339 N LEU B 320 12.988 -27.352 86.715 1.00 56.26 N ANISOU 4339 N LEU B 320 7161 6609 7605 -253 506 371 N ATOM 4340 CA LEU B 320 11.617 -27.740 87.047 1.00 57.37 C ANISOU 4340 CA LEU B 320 7127 6681 7992 -336 667 383 C ATOM 4341 C LEU B 320 11.568 -28.979 87.965 1.00 60.62 C ANISOU 4341 C LEU B 320 7686 6998 8351 -416 857 419 C ATOM 4342 O LEU B 320 10.753 -29.013 88.878 1.00 60.81 O ANISOU 4342 O LEU B 320 7673 6954 8476 -452 1111 441 O ATOM 4343 CB LEU B 320 10.722 -27.891 85.795 1.00 57.70 C ANISOU 4343 CB LEU B 320 6913 6728 8281 -397 486 356 C ATOM 4344 CG LEU B 320 10.530 -26.624 84.913 1.00 62.39 C ANISOU 4344 CG LEU B 320 7361 7393 8952 -310 309 336 C ATOM 4345 CD1 LEU B 320 9.640 -26.916 83.727 1.00 62.91 C ANISOU 4345 CD1 LEU B 320 7209 7456 9239 -368 97 310 C ATOM 4346 CD2 LEU B 320 9.971 -25.442 85.701 1.00 63.42 C ANISOU 4346 CD2 LEU B 320 7391 7520 9184 -234 489 341 C ATOM 4347 N LYS B 321 12.529 -29.896 87.818 1.00 56.77 N ANISOU 4347 N LYS B 321 7393 6496 7679 -424 757 429 N ATOM 4348 CA LYS B 321 12.648 -31.102 88.647 1.00 56.62 C ANISOU 4348 CA LYS B 321 7565 6373 7574 -480 908 475 C ATOM 4349 C LYS B 321 13.303 -30.827 90.013 1.00 61.62 C ANISOU 4349 C LYS B 321 8457 6990 7965 -396 1068 512 C ATOM 4350 O LYS B 321 12.718 -31.154 91.042 1.00 62.15 O ANISOU 4350 O LYS B 321 8607 6966 8039 -436 1322 555 O ATOM 4351 CB LYS B 321 13.451 -32.180 87.886 1.00 57.87 C ANISOU 4351 CB LYS B 321 7835 6514 7638 -502 718 467 C ATOM 4352 CG LYS B 321 13.585 -33.515 88.595 1.00 60.28 C ANISOU 4352 CG LYS B 321 8342 6690 7869 -557 846 518 C ATOM 4353 CD LYS B 321 14.769 -34.304 88.056 1.00 63.66 C ANISOU 4353 CD LYS B 321 8942 7114 8131 -510 660 509 C ATOM 4354 CE LYS B 321 14.930 -35.631 88.762 1.00 75.67 C ANISOU 4354 CE LYS B 321 10690 8491 9571 -545 778 569 C ATOM 4355 NZ LYS B 321 15.856 -36.546 88.034 1.00 86.73 N ANISOU 4355 NZ LYS B 321 12207 9862 10885 -515 599 549 N ATOM 4356 N ARG B 322 14.526 -30.259 90.010 1.00 57.59 N ANISOU 4356 N ARG B 322 8082 6558 7240 -285 918 491 N ATOM 4357 CA ARG B 322 15.360 -30.050 91.196 1.00 56.95 C ANISOU 4357 CA ARG B 322 8265 6468 6904 -196 986 510 C ATOM 4358 C ARG B 322 14.981 -28.911 92.102 1.00 63.39 C ANISOU 4358 C ARG B 322 9099 7295 7690 -149 1155 497 C ATOM 4359 O ARG B 322 15.156 -29.033 93.314 1.00 64.37 O ANISOU 4359 O ARG B 322 9462 7360 7638 -118 1308 528 O ATOM 4360 CB ARG B 322 16.823 -29.875 90.797 1.00 54.10 C ANISOU 4360 CB ARG B 322 8001 6184 6371 -104 746 475 C ATOM 4361 CG ARG B 322 17.395 -31.009 89.967 1.00 52.68 C ANISOU 4361 CG ARG B 322 7843 5986 6189 -125 588 478 C ATOM 4362 CD ARG B 322 17.760 -32.179 90.803 1.00 51.31 C ANISOU 4362 CD ARG B 322 7912 5709 5875 -115 650 535 C ATOM 4363 NE ARG B 322 18.400 -33.200 89.984 1.00 64.18 N ANISOU 4363 NE ARG B 322 9565 7315 7507 -117 496 528 N ATOM 4364 CZ ARG B 322 18.656 -34.435 90.396 1.00 72.72 C ANISOU 4364 CZ ARG B 322 10835 8285 8512 -116 522 579 C ATOM 4365 NH1 ARG B 322 18.312 -34.820 91.621 1.00 56.88 N ANISOU 4365 NH1 ARG B 322 9028 6178 6405 -118 700 651 N ATOM 4366 NH2 ARG B 322 19.245 -35.301 89.583 1.00 59.76 N ANISOU 4366 NH2 ARG B 322 9204 6616 6885 -109 384 560 N ATOM 4367 N VAL B 323 14.543 -27.783 91.524 1.00 59.96 N ANISOU 4367 N VAL B 323 8449 6930 7404 -132 1117 452 N ATOM 4368 CA VAL B 323 14.195 -26.574 92.249 1.00 59.57 C ANISOU 4368 CA VAL B 323 8399 6888 7348 -77 1264 426 C ATOM 4369 C VAL B 323 12.698 -26.533 92.575 1.00 67.52 C ANISOU 4369 C VAL B 323 9241 7826 8588 -139 1528 444 C ATOM 4370 O VAL B 323 12.342 -26.088 93.668 1.00 67.01 O ANISOU 4370 O VAL B 323 9289 7710 8462 -111 1768 444 O ATOM 4371 CB VAL B 323 14.666 -25.304 91.484 1.00 62.07 C ANISOU 4371 CB VAL B 323 8595 7297 7689 -8 1082 369 C ATOM 4372 CG1 VAL B 323 14.513 -24.043 92.335 1.00 61.39 C ANISOU 4372 CG1 VAL B 323 8570 7205 7552 61 1222 332 C ATOM 4373 CG2 VAL B 323 16.105 -25.447 90.991 1.00 61.45 C ANISOU 4373 CG2 VAL B 323 8622 7282 7443 31 834 348 C ATOM 4374 N PHE B 324 11.825 -26.990 91.641 1.00 66.59 N ANISOU 4374 N PHE B 324 8857 7700 8742 -223 1486 449 N ATOM 4375 CA PHE B 324 10.373 -26.901 91.842 1.00 67.32 C ANISOU 4375 CA PHE B 324 8726 7732 9122 -284 1717 453 C ATOM 4376 C PHE B 324 9.650 -28.244 92.108 1.00 74.81 C ANISOU 4376 C PHE B 324 9657 8573 10192 -417 1891 497 C ATOM 4377 O PHE B 324 8.419 -28.267 92.206 1.00 75.91 O ANISOU 4377 O PHE B 324 9568 8656 10619 -488 2084 494 O ATOM 4378 CB PHE B 324 9.726 -26.142 90.674 1.00 68.78 C ANISOU 4378 CB PHE B 324 8575 7978 9579 -270 1550 413 C ATOM 4379 CG PHE B 324 10.217 -24.715 90.590 1.00 70.13 C ANISOU 4379 CG PHE B 324 8764 8217 9663 -144 1461 378 C ATOM 4380 CD1 PHE B 324 9.770 -23.752 91.492 1.00 72.95 C ANISOU 4380 CD1 PHE B 324 9129 8542 10045 -78 1692 359 C ATOM 4381 CD2 PHE B 324 11.158 -24.341 89.637 1.00 72.59 C ANISOU 4381 CD2 PHE B 324 9105 8611 9863 -96 1169 361 C ATOM 4382 CE1 PHE B 324 10.239 -22.435 91.427 1.00 73.79 C ANISOU 4382 CE1 PHE B 324 9269 8693 10076 32 1612 321 C ATOM 4383 CE2 PHE B 324 11.630 -23.023 89.572 1.00 75.04 C ANISOU 4383 CE2 PHE B 324 9444 8967 10103 6 1104 331 C ATOM 4384 CZ PHE B 324 11.162 -22.078 90.463 1.00 73.21 C ANISOU 4384 CZ PHE B 324 9215 8696 9905 68 1316 310 C ATOM 4385 N GLY B 325 10.414 -29.314 92.296 1.00 72.22 N ANISOU 4385 N GLY B 325 9573 8206 9660 -448 1841 538 N ATOM 4386 CA GLY B 325 9.895 -30.640 92.609 1.00 72.47 C ANISOU 4386 CA GLY B 325 9655 8114 9767 -574 2008 588 C ATOM 4387 C GLY B 325 8.899 -31.226 91.629 1.00 77.51 C ANISOU 4387 C GLY B 325 9972 8723 10756 -706 1952 565 C ATOM 4388 O GLY B 325 7.980 -31.939 92.042 1.00 77.79 O ANISOU 4388 O GLY B 325 9939 8642 10975 -828 2194 591 O ATOM 4389 N MET B 326 9.069 -30.951 90.328 1.00 74.08 N ANISOU 4389 N MET B 326 9348 8385 10415 -689 1634 513 N ATOM 4390 CA MET B 326 8.153 -31.489 89.323 1.00 74.06 C ANISOU 4390 CA MET B 326 9051 8358 10730 -810 1521 477 C ATOM 4391 C MET B 326 8.559 -32.878 88.871 1.00 77.43 C ANISOU 4391 C MET B 326 9605 8717 11099 -905 1406 487 C ATOM 4392 O MET B 326 9.618 -33.378 89.273 1.00 77.14 O ANISOU 4392 O MET B 326 9875 8661 10774 -857 1393 526 O ATOM 4393 CB MET B 326 8.022 -30.551 88.118 1.00 76.75 C ANISOU 4393 CB MET B 326 9154 8816 11193 -747 1230 419 C ATOM 4394 CG MET B 326 7.400 -29.229 88.458 1.00 81.44 C ANISOU 4394 CG MET B 326 9568 9451 11925 -663 1342 404 C ATOM 4395 SD MET B 326 6.823 -28.416 86.970 1.00 86.75 S ANISOU 4395 SD MET B 326 9913 10210 12836 -621 1004 348 S ATOM 4396 CE MET B 326 6.902 -26.718 87.486 1.00 83.44 C ANISOU 4396 CE MET B 326 9477 9848 12379 -454 1105 348 C ATOM 4397 N PHE B 327 7.692 -33.504 88.041 1.00 73.64 N ANISOU 4397 N PHE B 327 8881 8190 10907 -1039 1313 445 N ATOM 4398 CA PHE B 327 7.867 -34.804 87.382 1.00 73.42 C ANISOU 4398 CA PHE B 327 8918 8086 10892 -1149 1174 428 C ATOM 4399 C PHE B 327 8.052 -35.988 88.346 1.00 84.81 C ANISOU 4399 C PHE B 327 10618 9373 12233 -1228 1424 497 C ATOM 4400 O PHE B 327 8.677 -36.987 87.977 1.00 84.64 O ANISOU 4400 O PHE B 327 10773 9290 12096 -1261 1306 498 O ATOM 4401 CB PHE B 327 9.019 -34.742 86.351 1.00 73.30 C ANISOU 4401 CB PHE B 327 9038 8167 10647 -1055 838 395 C ATOM 4402 CG PHE B 327 9.198 -33.426 85.628 1.00 72.43 C ANISOU 4402 CG PHE B 327 8799 8205 10515 -935 632 357 C ATOM 4403 CD1 PHE B 327 8.213 -32.940 84.777 1.00 73.92 C ANISOU 4403 CD1 PHE B 327 8680 8431 10974 -972 483 303 C ATOM 4404 CD2 PHE B 327 10.358 -32.684 85.784 1.00 73.40 C ANISOU 4404 CD2 PHE B 327 9111 8421 10357 -787 576 376 C ATOM 4405 CE1 PHE B 327 8.378 -31.722 84.111 1.00 74.62 C ANISOU 4405 CE1 PHE B 327 8684 8638 11031 -852 295 283 C ATOM 4406 CE2 PHE B 327 10.531 -31.473 85.105 1.00 75.96 C ANISOU 4406 CE2 PHE B 327 9337 8861 10665 -686 404 347 C ATOM 4407 CZ PHE B 327 9.538 -30.997 84.277 1.00 73.81 C ANISOU 4407 CZ PHE B 327 8788 8614 10640 -715 270 308 C ATOM 4408 N ARG B 328 7.470 -35.900 89.554 1.00 86.70 N ANISOU 4408 N ARG B 328 10889 9534 12521 -1258 1778 553 N ATOM 4409 CA ARG B 328 7.562 -36.960 90.561 1.00 89.11 C ANISOU 4409 CA ARG B 328 11467 9671 12718 -1330 2053 635 C ATOM 4410 C ARG B 328 6.466 -38.014 90.400 1.00 98.43 C ANISOU 4410 C ARG B 328 12474 10692 14233 -1548 2197 623 C ATOM 4411 O ARG B 328 6.689 -39.182 90.733 1.00 98.45 O ANISOU 4411 O ARG B 328 12708 10543 14157 -1628 2301 676 O ATOM 4412 CB ARG B 328 7.541 -36.359 91.975 1.00 90.79 C ANISOU 4412 CB ARG B 328 11861 9863 12773 -1253 2382 705 C ATOM 4413 CG ARG B 328 8.887 -35.795 92.395 1.00104.25 C ANISOU 4413 CG ARG B 328 13872 11664 14075 -1060 2255 732 C ATOM 4414 CD ARG B 328 8.786 -34.886 93.600 1.00116.43 C ANISOU 4414 CD ARG B 328 15543 13215 15478 -974 2519 766 C ATOM 4415 NE ARG B 328 10.050 -34.183 93.830 1.00126.42 N ANISOU 4415 NE ARG B 328 17035 14594 16406 -795 2332 762 N ATOM 4416 CZ ARG B 328 10.305 -33.412 94.882 1.00139.09 C ANISOU 4416 CZ ARG B 328 18840 16213 17797 -693 2486 782 C ATOM 4417 NH1 ARG B 328 11.482 -32.813 95.001 1.00125.89 N ANISOU 4417 NH1 ARG B 328 17343 14640 15848 -547 2277 763 N ATOM 4418 NH2 ARG B 328 9.383 -33.229 95.821 1.00124.05 N ANISOU 4418 NH2 ARG B 328 16959 14214 15959 -742 2857 812 N ATOM 4419 N GLN B 329 5.286 -37.597 89.886 1.00 98.76 N ANISOU 4419 N GLN B 329 12103 10760 14663 -1642 2195 552 N ATOM 4420 CA GLN B 329 4.084 -38.422 89.669 1.00100.04 C ANISOU 4420 CA GLN B 329 12000 10783 15229 -1864 2316 515 C ATOM 4421 C GLN B 329 4.343 -39.576 88.692 1.00106.61 C ANISOU 4421 C GLN B 329 12876 11544 16088 -1973 2052 467 C ATOM 4422 O GLN B 329 4.849 -39.345 87.588 1.00106.80 O ANISOU 4422 O GLN B 329 12863 11685 16032 -1901 1673 400 O ATOM 4423 CB GLN B 329 2.902 -37.559 89.170 1.00101.55 C ANISOU 4423 CB GLN B 329 11704 11052 15830 -1898 2268 430 C ATOM 4424 CG GLN B 329 2.648 -36.276 89.971 1.00122.67 C ANISOU 4424 CG GLN B 329 14305 13806 18497 -1767 2491 456 C ATOM 4425 CD GLN B 329 3.286 -35.054 89.338 1.00147.93 C ANISOU 4425 CD GLN B 329 17483 17201 21523 -1567 2175 423 C ATOM 4426 OE1 GLN B 329 4.516 -34.935 89.222 1.00143.19 O ANISOU 4426 OE1 GLN B 329 17189 16674 20544 -1443 1999 451 O ATOM 4427 NE2 GLN B 329 2.456 -34.108 88.924 1.00142.58 N ANISOU 4427 NE2 GLN B 329 16437 16600 21137 -1530 2103 364 N ATOM 4428 N ALA B 330 3.986 -40.813 89.100 1.00104.39 N ANISOU 4428 N ALA B 330 12691 11058 15914 -2149 2269 500 N ATOM 4429 CA ALA B 330 4.160 -42.037 88.303 1.00104.80 C ANISOU 4429 CA ALA B 330 12814 10998 16007 -2273 2073 453 C ATOM 4430 C ALA B 330 3.257 -42.092 87.050 1.00109.40 C ANISOU 4430 C ALA B 330 12987 11607 16974 -2412 1794 312 C ATOM 4431 O ALA B 330 3.485 -42.918 86.158 1.00108.79 O ANISOU 4431 O ALA B 330 12962 11472 16900 -2488 1543 244 O ATOM 4432 CB ALA B 330 3.936 -43.264 89.177 1.00105.62 C ANISOU 4432 CB ALA B 330 13135 10853 16142 -2428 2420 534 C ATOM 4433 N SER B 331 2.244 -41.203 86.989 1.00106.59 N ANISOU 4433 N SER B 331 12231 11331 16936 -2433 1827 264 N ATOM 4434 CA SER B 331 1.290 -41.069 85.884 1.00106.60 C ANISOU 4434 CA SER B 331 11805 11370 17326 -2540 1544 132 C ATOM 4435 C SER B 331 1.916 -40.352 84.673 1.00111.02 C ANISOU 4435 C SER B 331 12363 12121 17701 -2380 1071 65 C ATOM 4436 O SER B 331 1.359 -40.402 83.575 1.00111.11 O ANISOU 4436 O SER B 331 12123 12156 17937 -2454 747 -48 O ATOM 4437 CB SER B 331 0.044 -40.317 86.351 1.00109.87 C ANISOU 4437 CB SER B 331 11800 11799 18144 -2587 1765 115 C ATOM 4438 OG SER B 331 0.352 -39.010 86.814 1.00116.81 O ANISOU 4438 OG SER B 331 12702 12831 18849 -2373 1838 169 O ATOM 4439 N ASP B 332 3.072 -39.693 84.883 1.00107.22 N ANISOU 4439 N ASP B 332 12169 11762 16806 -2165 1034 134 N ATOM 4440 CA ASP B 332 3.801 -38.927 83.872 1.00106.76 C ANISOU 4440 CA ASP B 332 12160 11876 16527 -1999 655 93 C ATOM 4441 C ASP B 332 5.091 -39.607 83.352 1.00107.91 C ANISOU 4441 C ASP B 332 12681 12014 16305 -1941 474 94 C ATOM 4442 O ASP B 332 5.614 -39.170 82.326 1.00107.51 O ANISOU 4442 O ASP B 332 12665 12077 16106 -1843 154 42 O ATOM 4443 CB ASP B 332 4.118 -37.517 84.421 1.00109.18 C ANISOU 4443 CB ASP B 332 12464 12331 16686 -1800 742 154 C ATOM 4444 CG ASP B 332 2.939 -36.556 84.526 1.00122.39 C ANISOU 4444 CG ASP B 332 13738 14053 18713 -1800 807 127 C ATOM 4445 OD1 ASP B 332 1.840 -36.998 84.951 1.00123.46 O ANISOU 4445 OD1 ASP B 332 13624 14074 19210 -1961 1016 108 O ATOM 4446 OD2 ASP B 332 3.120 -35.358 84.211 1.00128.42 O ANISOU 4446 OD2 ASP B 332 14434 14957 19403 -1637 667 127 O ATOM 4447 N ARG B 333 5.582 -40.675 84.041 1.00102.26 N ANISOU 4447 N ARG B 333 12247 11152 15453 -1997 685 154 N ATOM 4448 CA ARG B 333 6.815 -41.441 83.749 1.00100.95 C ANISOU 4448 CA ARG B 333 12445 10948 14963 -1933 574 165 C ATOM 4449 C ARG B 333 7.132 -41.629 82.247 1.00101.30 C ANISOU 4449 C ARG B 333 12490 11042 14956 -1928 182 51 C ATOM 4450 O ARG B 333 8.280 -41.436 81.844 1.00100.04 O ANISOU 4450 O ARG B 333 12555 10964 14490 -1777 42 56 O ATOM 4451 CB ARG B 333 6.805 -42.805 84.470 1.00101.23 C ANISOU 4451 CB ARG B 333 12686 10761 15015 -2063 819 216 C ATOM 4452 CG ARG B 333 8.178 -43.483 84.546 1.00114.49 C ANISOU 4452 CG ARG B 333 14769 12393 16338 -1947 781 261 C ATOM 4453 CD ARG B 333 8.138 -44.788 85.323 1.00130.05 C ANISOU 4453 CD ARG B 333 16966 14126 18321 -2058 1034 330 C ATOM 4454 NE ARG B 333 9.283 -45.653 85.019 1.00143.03 N ANISOU 4454 NE ARG B 333 18938 15693 19713 -1976 916 333 N ATOM 4455 CZ ARG B 333 10.411 -45.695 85.723 1.00159.34 C ANISOU 4455 CZ ARG B 333 21312 17762 21469 -1799 987 429 C ATOM 4456 NH1 ARG B 333 10.569 -44.917 86.788 1.00148.80 N ANISOU 4456 NH1 ARG B 333 20027 16504 20006 -1691 1165 527 N ATOM 4457 NH2 ARG B 333 11.391 -46.516 85.369 1.00145.17 N ANISOU 4457 NH2 ARG B 333 19777 15887 19496 -1724 871 419 N ATOM 4458 N GLU B 334 6.122 -42.006 81.442 1.00 96.05 N ANISOU 4458 N GLU B 334 11582 10322 14590 -2094 14 -54 N ATOM 4459 CA GLU B 334 6.223 -42.233 79.995 1.00 94.83 C ANISOU 4459 CA GLU B 334 11430 10193 14406 -2114 -366 -177 C ATOM 4460 C GLU B 334 6.699 -40.955 79.268 1.00 93.99 C ANISOU 4460 C GLU B 334 11301 10293 14116 -1927 -607 -188 C ATOM 4461 O GLU B 334 7.692 -41.001 78.532 1.00 93.13 O ANISOU 4461 O GLU B 334 11430 10231 13723 -1825 -782 -215 O ATOM 4462 CB GLU B 334 4.855 -42.706 79.456 1.00 96.52 C ANISOU 4462 CB GLU B 334 11331 10313 15029 -2334 -493 -288 C ATOM 4463 CG GLU B 334 4.875 -43.344 78.074 1.00110.26 C ANISOU 4463 CG GLU B 334 13134 12011 16747 -2408 -860 -429 C ATOM 4464 CD GLU B 334 3.508 -43.674 77.494 1.00141.33 C ANISOU 4464 CD GLU B 334 16730 15873 21097 -2616 -1050 -555 C ATOM 4465 OE1 GLU B 334 2.611 -44.102 78.259 1.00138.90 O ANISOU 4465 OE1 GLU B 334 16195 15449 21132 -2782 -814 -543 O ATOM 4466 OE2 GLU B 334 3.338 -43.516 76.263 1.00139.58 O ANISOU 4466 OE2 GLU B 334 16476 15702 20858 -2616 -1436 -671 O ATOM 4467 N ALA B 335 6.005 -39.820 79.519 1.00 86.93 N ANISOU 4467 N ALA B 335 10132 9508 13390 -1880 -587 -163 N ATOM 4468 CA ALA B 335 6.267 -38.502 78.937 1.00 84.95 C ANISOU 4468 CA ALA B 335 9833 9433 13012 -1710 -786 -160 C ATOM 4469 C ALA B 335 7.540 -37.843 79.494 1.00 85.15 C ANISOU 4469 C ALA B 335 10112 9553 12690 -1520 -647 -66 C ATOM 4470 O ALA B 335 8.307 -37.255 78.730 1.00 83.99 O ANISOU 4470 O ALA B 335 10094 9507 12310 -1394 -837 -78 O ATOM 4471 CB ALA B 335 5.065 -37.599 79.158 1.00 85.62 C ANISOU 4471 CB ALA B 335 9538 9571 13422 -1721 -776 -161 C ATOM 4472 N VAL B 336 7.751 -37.942 80.824 1.00 79.67 N ANISOU 4472 N VAL B 336 9493 8815 11962 -1507 -316 24 N ATOM 4473 CA VAL B 336 8.903 -37.398 81.547 1.00 78.63 C ANISOU 4473 CA VAL B 336 9592 8754 11530 -1344 -174 108 C ATOM 4474 C VAL B 336 10.220 -37.967 81.009 1.00 81.67 C ANISOU 4474 C VAL B 336 10279 9136 11615 -1272 -296 93 C ATOM 4475 O VAL B 336 11.105 -37.191 80.637 1.00 81.05 O ANISOU 4475 O VAL B 336 10297 9174 11324 -1129 -401 98 O ATOM 4476 CB VAL B 336 8.755 -37.564 83.086 1.00 82.07 C ANISOU 4476 CB VAL B 336 10080 9114 11989 -1363 189 199 C ATOM 4477 CG1 VAL B 336 10.022 -37.141 83.822 1.00 81.66 C ANISOU 4477 CG1 VAL B 336 10299 9121 11607 -1198 289 272 C ATOM 4478 CG2 VAL B 336 7.564 -36.774 83.601 1.00 81.97 C ANISOU 4478 CG2 VAL B 336 9768 9124 12252 -1397 339 211 C ATOM 4479 N TYR B 337 10.338 -39.304 80.951 1.00 78.55 N ANISOU 4479 N TYR B 337 10026 8598 11220 -1372 -271 71 N ATOM 4480 CA TYR B 337 11.540 -39.972 80.458 1.00 79.25 C ANISOU 4480 CA TYR B 337 10393 8659 11058 -1303 -364 48 C ATOM 4481 C TYR B 337 11.841 -39.644 79.005 1.00 77.13 C ANISOU 4481 C TYR B 337 10136 8472 10698 -1262 -656 -42 C ATOM 4482 O TYR B 337 12.998 -39.404 78.682 1.00 76.64 O ANISOU 4482 O TYR B 337 10254 8472 10392 -1130 -705 -41 O ATOM 4483 CB TYR B 337 11.496 -41.485 80.703 1.00 83.92 C ANISOU 4483 CB TYR B 337 11133 9055 11696 -1421 -269 41 C ATOM 4484 CG TYR B 337 12.074 -41.886 82.044 1.00 91.15 C ANISOU 4484 CG TYR B 337 12243 9896 12494 -1363 -6 151 C ATOM 4485 CD1 TYR B 337 13.419 -42.225 82.173 1.00 93.88 C ANISOU 4485 CD1 TYR B 337 12856 10235 12579 -1220 -13 179 C ATOM 4486 CD2 TYR B 337 11.280 -41.913 83.190 1.00 93.99 C ANISOU 4486 CD2 TYR B 337 12525 10185 13002 -1444 249 227 C ATOM 4487 CE1 TYR B 337 13.959 -42.594 83.409 1.00 96.58 C ANISOU 4487 CE1 TYR B 337 13393 10504 12800 -1151 189 283 C ATOM 4488 CE2 TYR B 337 11.807 -42.285 84.430 1.00 96.05 C ANISOU 4488 CE2 TYR B 337 13012 10365 13117 -1384 481 334 C ATOM 4489 CZ TYR B 337 13.147 -42.630 84.534 1.00106.43 C ANISOU 4489 CZ TYR B 337 14601 11675 14161 -1234 430 363 C ATOM 4490 OH TYR B 337 13.667 -43.008 85.752 1.00109.52 O ANISOU 4490 OH TYR B 337 15231 11983 14400 -1161 620 470 O ATOM 4491 N ALA B 338 10.808 -39.578 78.152 1.00 69.17 N ANISOU 4491 N ALA B 338 8936 7463 9884 -1368 -846 -120 N ATOM 4492 CA ALA B 338 10.931 -39.226 76.740 1.00 67.40 C ANISOU 4492 CA ALA B 338 8739 7306 9565 -1335 -1142 -205 C ATOM 4493 C ALA B 338 11.488 -37.800 76.586 1.00 67.64 C ANISOU 4493 C ALA B 338 8767 7502 9433 -1166 -1182 -157 C ATOM 4494 O ALA B 338 12.412 -37.577 75.792 1.00 66.71 O ANISOU 4494 O ALA B 338 8835 7434 9078 -1070 -1290 -182 O ATOM 4495 CB ALA B 338 9.570 -39.329 76.069 1.00 68.20 C ANISOU 4495 CB ALA B 338 8601 7373 9939 -1477 -1345 -287 C ATOM 4496 N ALA B 339 10.943 -36.847 77.386 1.00 61.42 N ANISOU 4496 N ALA B 339 7778 6783 8776 -1132 -1068 -89 N ATOM 4497 CA ALA B 339 11.344 -35.444 77.406 1.00 59.26 C ANISOU 4497 CA ALA B 339 7482 6645 8389 -984 -1076 -39 C ATOM 4498 C ALA B 339 12.806 -35.315 77.854 1.00 61.13 C ANISOU 4498 C ALA B 339 7953 6920 8355 -862 -940 8 C ATOM 4499 O ALA B 339 13.577 -34.581 77.229 1.00 61.10 O ANISOU 4499 O ALA B 339 8047 6998 8170 -757 -1030 5 O ATOM 4500 CB ALA B 339 10.433 -34.661 78.338 1.00 59.66 C ANISOU 4500 CB ALA B 339 7283 6726 8659 -985 -934 16 C ATOM 4501 N PHE B 340 13.197 -36.060 78.911 1.00 55.19 N ANISOU 4501 N PHE B 340 7295 6096 7578 -876 -732 50 N ATOM 4502 CA PHE B 340 14.557 -36.009 79.428 1.00 53.54 C ANISOU 4502 CA PHE B 340 7285 5915 7141 -757 -626 89 C ATOM 4503 C PHE B 340 15.546 -36.618 78.467 1.00 56.42 C ANISOU 4503 C PHE B 340 7845 6260 7334 -720 -740 31 C ATOM 4504 O PHE B 340 16.627 -36.083 78.288 1.00 56.35 O ANISOU 4504 O PHE B 340 7935 6322 7153 -605 -744 36 O ATOM 4505 CB PHE B 340 14.646 -36.615 80.829 1.00 54.69 C ANISOU 4505 CB PHE B 340 7498 5982 7298 -769 -398 156 C ATOM 4506 CG PHE B 340 14.336 -35.622 81.927 1.00 55.76 C ANISOU 4506 CG PHE B 340 7537 6178 7471 -723 -240 222 C ATOM 4507 CD1 PHE B 340 15.317 -34.767 82.413 1.00 58.71 C ANISOU 4507 CD1 PHE B 340 7998 6640 7669 -588 -200 253 C ATOM 4508 CD2 PHE B 340 13.064 -35.548 82.482 1.00 58.62 C ANISOU 4508 CD2 PHE B 340 7717 6500 8056 -818 -122 243 C ATOM 4509 CE1 PHE B 340 15.031 -33.855 83.439 1.00 59.84 C ANISOU 4509 CE1 PHE B 340 8079 6825 7832 -547 -55 302 C ATOM 4510 CE2 PHE B 340 12.776 -34.632 83.511 1.00 61.24 C ANISOU 4510 CE2 PHE B 340 7980 6875 8413 -769 50 296 C ATOM 4511 CZ PHE B 340 13.764 -33.803 83.990 1.00 58.92 C ANISOU 4511 CZ PHE B 340 7807 6664 7917 -633 79 324 C ATOM 4512 N THR B 341 15.139 -37.689 77.796 1.00 53.19 N ANISOU 4512 N THR B 341 7479 5747 6984 -824 -832 -33 N ATOM 4513 CA THR B 341 15.890 -38.427 76.784 1.00 52.22 C ANISOU 4513 CA THR B 341 7549 5574 6716 -808 -937 -108 C ATOM 4514 C THR B 341 16.164 -37.505 75.604 1.00 54.43 C ANISOU 4514 C THR B 341 7849 5958 6873 -744 -1099 -149 C ATOM 4515 O THR B 341 17.306 -37.408 75.162 1.00 52.58 O ANISOU 4515 O THR B 341 7771 5752 6453 -646 -1085 -166 O ATOM 4516 CB THR B 341 15.102 -39.704 76.438 1.00 59.63 C ANISOU 4516 CB THR B 341 8505 6364 7786 -961 -999 -174 C ATOM 4517 OG1 THR B 341 15.164 -40.575 77.563 1.00 57.45 O ANISOU 4517 OG1 THR B 341 8281 5977 7572 -994 -809 -120 O ATOM 4518 CG2 THR B 341 15.615 -40.418 75.213 1.00 59.18 C ANISOU 4518 CG2 THR B 341 8643 6248 7596 -962 -1137 -275 C ATOM 4519 N PHE B 342 15.123 -36.794 75.133 1.00 52.74 N ANISOU 4519 N PHE B 342 7473 5794 6771 -792 -1242 -158 N ATOM 4520 CA PHE B 342 15.248 -35.836 74.038 1.00 53.16 C ANISOU 4520 CA PHE B 342 7561 5933 6705 -729 -1406 -179 C ATOM 4521 C PHE B 342 16.175 -34.685 74.396 1.00 54.28 C ANISOU 4521 C PHE B 342 7726 6180 6719 -595 -1292 -112 C ATOM 4522 O PHE B 342 16.981 -34.274 73.558 1.00 54.54 O ANISOU 4522 O PHE B 342 7906 6249 6567 -523 -1333 -132 O ATOM 4523 CB PHE B 342 13.882 -35.304 73.592 1.00 55.86 C ANISOU 4523 CB PHE B 342 7707 6296 7220 -792 -1598 -192 C ATOM 4524 CG PHE B 342 13.981 -34.415 72.373 1.00 58.35 C ANISOU 4524 CG PHE B 342 8108 6676 7386 -721 -1795 -209 C ATOM 4525 CD1 PHE B 342 14.158 -34.960 71.104 1.00 61.98 C ANISOU 4525 CD1 PHE B 342 8771 7087 7690 -746 -1976 -294 C ATOM 4526 CD2 PHE B 342 13.899 -33.034 72.492 1.00 61.31 C ANISOU 4526 CD2 PHE B 342 8390 7145 7760 -628 -1793 -138 C ATOM 4527 CE1 PHE B 342 14.267 -34.135 69.976 1.00 63.01 C ANISOU 4527 CE1 PHE B 342 9029 7264 7647 -676 -2147 -299 C ATOM 4528 CE2 PHE B 342 13.993 -32.213 71.364 1.00 64.77 C ANISOU 4528 CE2 PHE B 342 8941 7623 8046 -559 -1967 -139 C ATOM 4529 CZ PHE B 342 14.175 -32.771 70.113 1.00 62.89 C ANISOU 4529 CZ PHE B 342 8921 7337 7636 -583 -2142 -215 C ATOM 4530 N SER B 343 16.067 -34.174 75.634 1.00 48.48 N ANISOU 4530 N SER B 343 6857 5483 6080 -568 -1138 -40 N ATOM 4531 CA SER B 343 16.888 -33.067 76.121 1.00 47.43 C ANISOU 4531 CA SER B 343 6729 5439 5852 -455 -1031 15 C ATOM 4532 C SER B 343 18.385 -33.434 76.225 1.00 53.39 C ANISOU 4532 C SER B 343 7658 6191 6436 -379 -930 3 C ATOM 4533 O SER B 343 19.233 -32.567 75.983 1.00 54.67 O ANISOU 4533 O SER B 343 7865 6420 6487 -296 -904 12 O ATOM 4534 CB SER B 343 16.335 -32.524 77.431 1.00 48.22 C ANISOU 4534 CB SER B 343 6667 5564 6090 -452 -897 79 C ATOM 4535 OG SER B 343 16.679 -33.327 78.547 1.00 53.02 O ANISOU 4535 OG SER B 343 7324 6118 6703 -463 -737 103 O ATOM 4536 N HIS B 344 18.698 -34.716 76.553 1.00 48.80 N ANISOU 4536 N HIS B 344 7166 5522 5852 -407 -874 -20 N ATOM 4537 CA HIS B 344 20.059 -35.257 76.641 1.00 48.53 C ANISOU 4537 CA HIS B 344 7280 5466 5693 -326 -794 -39 C ATOM 4538 C HIS B 344 20.662 -35.404 75.238 1.00 53.21 C ANISOU 4538 C HIS B 344 8012 6051 6155 -304 -870 -112 C ATOM 4539 O HIS B 344 21.843 -35.145 75.072 1.00 53.01 O ANISOU 4539 O HIS B 344 8055 6057 6029 -215 -800 -125 O ATOM 4540 CB HIS B 344 20.086 -36.641 77.327 1.00 48.94 C ANISOU 4540 CB HIS B 344 7405 5401 5790 -357 -727 -38 C ATOM 4541 CG HIS B 344 19.591 -36.672 78.744 1.00 52.54 C ANISOU 4541 CG HIS B 344 7786 5838 6338 -376 -617 38 C ATOM 4542 ND1 HIS B 344 19.114 -37.846 79.311 1.00 54.70 N ANISOU 4542 ND1 HIS B 344 8108 5986 6689 -448 -559 54 N ATOM 4543 CD2 HIS B 344 19.515 -35.687 79.668 1.00 54.38 C ANISOU 4543 CD2 HIS B 344 7928 6149 6586 -334 -543 98 C ATOM 4544 CE1 HIS B 344 18.770 -37.537 80.551 1.00 54.03 C ANISOU 4544 CE1 HIS B 344 7970 5909 6651 -445 -441 129 C ATOM 4545 NE2 HIS B 344 19.005 -36.256 80.819 1.00 54.34 N ANISOU 4545 NE2 HIS B 344 7928 6071 6649 -374 -430 152 N ATOM 4546 N TRP B 345 19.879 -35.878 74.252 1.00 50.29 N ANISOU 4546 N TRP B 345 7690 5628 5790 -388 -1006 -167 N ATOM 4547 CA TRP B 345 20.352 -36.050 72.882 1.00 50.52 C ANISOU 4547 CA TRP B 345 7894 5635 5665 -372 -1078 -242 C ATOM 4548 C TRP B 345 20.681 -34.668 72.264 1.00 55.65 C ANISOU 4548 C TRP B 345 8551 6385 6210 -310 -1094 -216 C ATOM 4549 O TRP B 345 21.714 -34.531 71.600 1.00 55.94 O ANISOU 4549 O TRP B 345 8727 6425 6102 -246 -1025 -248 O ATOM 4550 CB TRP B 345 19.341 -36.850 72.036 1.00 49.50 C ANISOU 4550 CB TRP B 345 7827 5421 5561 -484 -1252 -314 C ATOM 4551 CG TRP B 345 19.658 -36.824 70.566 1.00 50.91 C ANISOU 4551 CG TRP B 345 8214 5583 5548 -468 -1350 -390 C ATOM 4552 CD1 TRP B 345 20.523 -37.641 69.900 1.00 53.79 C ANISOU 4552 CD1 TRP B 345 8794 5870 5773 -437 -1290 -469 C ATOM 4553 CD2 TRP B 345 19.173 -35.876 69.596 1.00 50.71 C ANISOU 4553 CD2 TRP B 345 8225 5612 5429 -467 -1507 -388 C ATOM 4554 NE1 TRP B 345 20.621 -37.253 68.582 1.00 53.01 N ANISOU 4554 NE1 TRP B 345 8880 5777 5485 -424 -1381 -520 N ATOM 4555 CE2 TRP B 345 19.785 -36.190 68.361 1.00 54.11 C ANISOU 4555 CE2 TRP B 345 8925 5993 5641 -442 -1529 -467 C ATOM 4556 CE3 TRP B 345 18.284 -34.786 69.655 1.00 51.75 C ANISOU 4556 CE3 TRP B 345 8203 5820 5639 -474 -1627 -326 C ATOM 4557 CZ2 TRP B 345 19.533 -35.460 67.189 1.00 53.24 C ANISOU 4557 CZ2 TRP B 345 8960 5906 5362 -428 -1674 -478 C ATOM 4558 CZ3 TRP B 345 18.038 -34.061 68.496 1.00 53.16 C ANISOU 4558 CZ3 TRP B 345 8506 6020 5672 -451 -1788 -334 C ATOM 4559 CH2 TRP B 345 18.663 -34.396 67.280 1.00 53.70 C ANISOU 4559 CH2 TRP B 345 8869 6037 5496 -430 -1813 -405 C ATOM 4560 N LEU B 346 19.817 -33.651 72.530 1.00 50.98 N ANISOU 4560 N LEU B 346 7807 5860 5705 -326 -1163 -156 N ATOM 4561 CA LEU B 346 19.949 -32.265 72.065 1.00 49.60 C ANISOU 4561 CA LEU B 346 7630 5760 5455 -270 -1183 -114 C ATOM 4562 C LEU B 346 21.273 -31.599 72.420 1.00 50.54 C ANISOU 4562 C LEU B 346 7772 5928 5503 -183 -1006 -90 C ATOM 4563 O LEU B 346 21.832 -30.880 71.593 1.00 49.33 O ANISOU 4563 O LEU B 346 7728 5795 5222 -143 -985 -91 O ATOM 4564 CB LEU B 346 18.783 -31.406 72.558 1.00 49.64 C ANISOU 4564 CB LEU B 346 7439 5812 5612 -290 -1263 -53 C ATOM 4565 CG LEU B 346 17.693 -31.066 71.550 1.00 53.90 C ANISOU 4565 CG LEU B 346 7978 6343 6160 -322 -1492 -63 C ATOM 4566 CD1 LEU B 346 16.780 -30.025 72.116 1.00 53.59 C ANISOU 4566 CD1 LEU B 346 7728 6352 6281 -305 -1528 4 C ATOM 4567 CD2 LEU B 346 18.280 -30.571 70.204 1.00 55.63 C ANISOU 4567 CD2 LEU B 346 8429 6560 6147 -273 -1559 -78 C ATOM 4568 N VAL B 347 21.772 -31.846 73.639 1.00 46.72 N ANISOU 4568 N VAL B 347 7194 5456 5101 -157 -881 -71 N ATOM 4569 CA VAL B 347 23.065 -31.363 74.152 1.00 47.21 C ANISOU 4569 CA VAL B 347 7245 5559 5134 -79 -735 -63 C ATOM 4570 C VAL B 347 24.213 -31.828 73.214 1.00 51.63 C ANISOU 4570 C VAL B 347 7960 6084 5574 -40 -665 -128 C ATOM 4571 O VAL B 347 25.090 -31.038 72.852 1.00 51.58 O ANISOU 4571 O VAL B 347 7978 6111 5511 2 -575 -131 O ATOM 4572 CB VAL B 347 23.250 -31.882 75.599 1.00 51.41 C ANISOU 4572 CB VAL B 347 7685 6086 5762 -61 -665 -41 C ATOM 4573 CG1 VAL B 347 24.719 -31.980 75.996 1.00 50.82 C ANISOU 4573 CG1 VAL B 347 7628 6022 5661 23 -558 -66 C ATOM 4574 CG2 VAL B 347 22.457 -31.029 76.585 1.00 51.51 C ANISOU 4574 CG2 VAL B 347 7558 6148 5868 -74 -663 22 C ATOM 4575 N TYR B 348 24.169 -33.110 72.813 1.00 47.23 N ANISOU 4575 N TYR B 348 7508 5447 4988 -62 -693 -185 N ATOM 4576 CA TYR B 348 25.137 -33.719 71.913 1.00 45.29 C ANISOU 4576 CA TYR B 348 7423 5149 4637 -23 -615 -259 C ATOM 4577 C TYR B 348 24.915 -33.268 70.494 1.00 48.17 C ANISOU 4577 C TYR B 348 7953 5505 4846 -48 -664 -284 C ATOM 4578 O TYR B 348 25.884 -32.918 69.838 1.00 47.93 O ANISOU 4578 O TYR B 348 8020 5473 4720 -1 -536 -311 O ATOM 4579 CB TYR B 348 25.137 -35.242 72.064 1.00 44.82 C ANISOU 4579 CB TYR B 348 7433 4990 4606 -31 -624 -312 C ATOM 4580 CG TYR B 348 25.474 -35.677 73.476 1.00 43.83 C ANISOU 4580 CG TYR B 348 7187 4861 4605 13 -570 -275 C ATOM 4581 CD1 TYR B 348 26.727 -35.413 74.031 1.00 44.48 C ANISOU 4581 CD1 TYR B 348 7204 4979 4718 113 -457 -275 C ATOM 4582 CD2 TYR B 348 24.524 -36.305 74.277 1.00 43.83 C ANISOU 4582 CD2 TYR B 348 7139 4818 4695 -47 -636 -238 C ATOM 4583 CE1 TYR B 348 27.029 -35.781 75.339 1.00 43.36 C ANISOU 4583 CE1 TYR B 348 6978 4830 4667 164 -442 -238 C ATOM 4584 CE2 TYR B 348 24.806 -36.652 75.597 1.00 44.01 C ANISOU 4584 CE2 TYR B 348 7093 4829 4798 -2 -584 -192 C ATOM 4585 CZ TYR B 348 26.069 -36.417 76.112 1.00 47.48 C ANISOU 4585 CZ TYR B 348 7498 5304 5239 111 -503 -192 C ATOM 4586 OH TYR B 348 26.355 -36.781 77.397 1.00 45.36 O ANISOU 4586 OH TYR B 348 7194 5015 5025 166 -484 -146 O ATOM 4587 N ALA B 349 23.645 -33.194 70.038 1.00 44.60 N ANISOU 4587 N ALA B 349 7529 5044 4374 -117 -847 -271 N ATOM 4588 CA ALA B 349 23.262 -32.683 68.715 1.00 44.20 C ANISOU 4588 CA ALA B 349 7655 4982 4158 -134 -948 -282 C ATOM 4589 C ALA B 349 23.959 -31.338 68.422 1.00 51.78 C ANISOU 4589 C ALA B 349 8641 5996 5038 -80 -832 -229 C ATOM 4590 O ALA B 349 24.385 -31.119 67.281 1.00 53.11 O ANISOU 4590 O ALA B 349 9029 6130 5021 -64 -792 -253 O ATOM 4591 CB ALA B 349 21.758 -32.514 68.640 1.00 44.38 C ANISOU 4591 CB ALA B 349 7609 5012 4243 -201 -1186 -256 C ATOM 4592 N ASN B 350 24.140 -30.474 69.476 1.00 47.77 N ANISOU 4592 N ASN B 350 7928 5558 4664 -55 -758 -163 N ATOM 4593 CA ASN B 350 24.807 -29.170 69.393 1.00 46.83 C ANISOU 4593 CA ASN B 350 7801 5479 4514 -17 -637 -114 C ATOM 4594 C ASN B 350 26.245 -29.234 68.894 1.00 51.02 C ANISOU 4594 C ASN B 350 8435 5985 4967 20 -419 -161 C ATOM 4595 O ASN B 350 26.664 -28.336 68.164 1.00 51.45 O ANISOU 4595 O ASN B 350 8601 6029 4917 30 -326 -136 O ATOM 4596 CB ASN B 350 24.741 -28.403 70.707 1.00 44.05 C ANISOU 4596 CB ASN B 350 7215 5191 4329 -5 -608 -56 C ATOM 4597 CG ASN B 350 25.183 -26.973 70.530 1.00 58.31 C ANISOU 4597 CG ASN B 350 9025 7022 6111 17 -517 -6 C ATOM 4598 OD1 ASN B 350 24.482 -26.163 69.928 1.00 53.30 O ANISOU 4598 OD1 ASN B 350 8466 6377 5407 14 -606 47 O ATOM 4599 ND2 ASN B 350 26.385 -26.647 70.984 1.00 44.54 N ANISOU 4599 ND2 ASN B 350 7206 5294 4422 41 -343 -26 N ATOM 4600 N SER B 351 27.000 -30.264 69.293 1.00 48.32 N ANISOU 4600 N SER B 351 8052 5621 4688 45 -326 -227 N ATOM 4601 CA SER B 351 28.383 -30.480 68.854 1.00 49.78 C ANISOU 4601 CA SER B 351 8297 5773 4843 90 -109 -288 C ATOM 4602 C SER B 351 28.434 -30.861 67.365 1.00 55.94 C ANISOU 4602 C SER B 351 9368 6477 5411 82 -68 -340 C ATOM 4603 O SER B 351 29.460 -30.661 66.721 1.00 55.20 O ANISOU 4603 O SER B 351 9367 6351 5254 110 144 -375 O ATOM 4604 CB SER B 351 29.021 -31.598 69.664 1.00 54.82 C ANISOU 4604 CB SER B 351 8820 6395 5613 137 -63 -344 C ATOM 4605 OG SER B 351 29.054 -31.233 71.029 1.00 66.26 O ANISOU 4605 OG SER B 351 10042 7908 7225 152 -95 -299 O ATOM 4606 N ALA B 352 27.347 -31.454 66.837 1.00 53.88 N ANISOU 4606 N ALA B 352 9251 6178 5044 42 -264 -353 N ATOM 4607 CA ALA B 352 27.275 -31.800 65.424 1.00 54.44 C ANISOU 4607 CA ALA B 352 9636 6171 4880 31 -268 -408 C ATOM 4608 C ALA B 352 26.819 -30.555 64.625 1.00 57.91 C ANISOU 4608 C ALA B 352 10224 6622 5157 17 -326 -333 C ATOM 4609 O ALA B 352 27.167 -30.418 63.456 1.00 55.98 O ANISOU 4609 O ALA B 352 10262 6317 4692 26 -234 -355 O ATOM 4610 CB ALA B 352 26.319 -32.974 65.212 1.00 55.18 C ANISOU 4610 CB ALA B 352 9817 6209 4940 -13 -481 -467 C ATOM 4611 N ALA B 353 26.082 -29.638 65.289 1.00 55.30 N ANISOU 4611 N ALA B 353 9717 6359 4935 3 -461 -241 N ATOM 4612 CA ALA B 353 25.547 -28.398 64.715 1.00 55.54 C ANISOU 4612 CA ALA B 353 9856 6396 4851 5 -545 -154 C ATOM 4613 C ALA B 353 26.634 -27.369 64.369 1.00 61.88 C ANISOU 4613 C ALA B 353 10737 7185 5590 29 -282 -113 C ATOM 4614 O ALA B 353 26.622 -26.814 63.258 1.00 62.27 O ANISOU 4614 O ALA B 353 11066 7177 5416 36 -260 -80 O ATOM 4615 CB ALA B 353 24.525 -27.778 65.663 1.00 55.90 C ANISOU 4615 CB ALA B 353 9655 6508 5076 -6 -730 -78 C ATOM 4616 N ASN B 354 27.567 -27.113 65.319 1.00 57.82 N ANISOU 4616 N ASN B 354 9986 6713 5270 38 -87 -117 N ATOM 4617 CA ASN B 354 28.635 -26.128 65.167 1.00 57.05 C ANISOU 4617 CA ASN B 354 9895 6601 5181 43 172 -89 C ATOM 4618 C ASN B 354 29.427 -26.256 63.865 1.00 62.18 C ANISOU 4618 C ASN B 354 10843 7162 5619 46 393 -127 C ATOM 4619 O ASN B 354 29.456 -25.253 63.148 1.00 62.39 O ANISOU 4619 O ASN B 354 11056 7144 5506 38 471 -57 O ATOM 4620 CB ASN B 354 29.537 -26.102 66.378 1.00 54.27 C ANISOU 4620 CB ASN B 354 9234 6304 5084 49 308 -120 C ATOM 4621 CG ASN B 354 28.792 -25.567 67.569 1.00 66.06 C ANISOU 4621 CG ASN B 354 10494 7868 6739 44 137 -63 C ATOM 4622 OD1 ASN B 354 27.867 -24.763 67.424 1.00 50.21 O ANISOU 4622 OD1 ASN B 354 8533 5863 4681 36 0 15 O ATOM 4623 ND2 ASN B 354 29.159 -26.012 68.768 1.00 58.84 N ANISOU 4623 ND2 ASN B 354 9337 7005 6016 57 140 -102 N ATOM 4624 N PRO B 355 29.991 -27.431 63.459 1.00 58.76 N ANISOU 4624 N PRO B 355 10501 6689 5136 63 499 -230 N ATOM 4625 CA PRO B 355 30.719 -27.477 62.180 1.00 58.37 C ANISOU 4625 CA PRO B 355 10764 6545 4868 69 742 -266 C ATOM 4626 C PRO B 355 29.834 -27.241 60.970 1.00 62.47 C ANISOU 4626 C PRO B 355 11672 7002 5063 61 588 -222 C ATOM 4627 O PRO B 355 30.312 -26.641 60.012 1.00 62.72 O ANISOU 4627 O PRO B 355 11976 6957 4896 59 789 -192 O ATOM 4628 CB PRO B 355 31.345 -28.866 62.179 1.00 60.30 C ANISOU 4628 CB PRO B 355 10989 6760 5162 100 848 -393 C ATOM 4629 CG PRO B 355 31.321 -29.300 63.624 1.00 64.35 C ANISOU 4629 CG PRO B 355 11125 7356 5968 115 729 -406 C ATOM 4630 CD PRO B 355 30.062 -28.739 64.139 1.00 59.99 C ANISOU 4630 CD PRO B 355 10499 6865 5429 83 435 -316 C ATOM 4631 N ILE B 356 28.546 -27.663 61.023 1.00 59.24 N ANISOU 4631 N ILE B 356 11286 6617 4604 56 233 -214 N ATOM 4632 CA ILE B 356 27.587 -27.461 59.924 1.00 59.45 C ANISOU 4632 CA ILE B 356 11660 6589 4338 57 8 -177 C ATOM 4633 C ILE B 356 27.330 -25.947 59.720 1.00 63.51 C ANISOU 4633 C ILE B 356 12246 7098 4787 67 -5 -39 C ATOM 4634 O ILE B 356 27.354 -25.465 58.584 1.00 63.20 O ANISOU 4634 O ILE B 356 12581 6973 4459 82 41 3 O ATOM 4635 CB ILE B 356 26.288 -28.315 60.062 1.00 62.49 C ANISOU 4635 CB ILE B 356 12006 6998 4740 40 -378 -218 C ATOM 4636 CG1 ILE B 356 26.630 -29.810 60.258 1.00 62.53 C ANISOU 4636 CG1 ILE B 356 11973 6980 4805 27 -331 -353 C ATOM 4637 CG2 ILE B 356 25.385 -28.141 58.822 1.00 63.63 C ANISOU 4637 CG2 ILE B 356 12524 7080 4575 47 -637 -195 C ATOM 4638 CD1 ILE B 356 25.434 -30.753 60.680 1.00 67.69 C ANISOU 4638 CD1 ILE B 356 12499 7653 5566 -13 -669 -401 C ATOM 4639 N ILE B 357 27.169 -25.203 60.832 1.00 59.91 N ANISOU 4639 N ILE B 357 11453 6718 4591 63 -40 29 N ATOM 4640 CA ILE B 357 26.996 -23.746 60.854 1.00 58.42 C ANISOU 4640 CA ILE B 357 11279 6518 4401 74 -30 155 C ATOM 4641 C ILE B 357 28.208 -23.092 60.171 1.00 62.49 C ANISOU 4641 C ILE B 357 12002 6949 4794 62 346 179 C ATOM 4642 O ILE B 357 28.010 -22.353 59.209 1.00 63.57 O ANISOU 4642 O ILE B 357 12471 7000 4684 79 350 263 O ATOM 4643 CB ILE B 357 26.767 -23.201 62.304 1.00 60.72 C ANISOU 4643 CB ILE B 357 11153 6900 5017 68 -89 193 C ATOM 4644 CG1 ILE B 357 25.486 -23.793 62.958 1.00 60.30 C ANISOU 4644 CG1 ILE B 357 10904 6917 5089 74 -430 178 C ATOM 4645 CG2 ILE B 357 26.759 -21.661 62.324 1.00 60.36 C ANISOU 4645 CG2 ILE B 357 11132 6821 4982 79 -29 313 C ATOM 4646 CD1 ILE B 357 25.330 -23.529 64.537 1.00 61.56 C ANISOU 4646 CD1 ILE B 357 10651 7168 5572 65 -446 188 C ATOM 4647 N TYR B 358 29.455 -23.413 60.613 1.00 58.60 N ANISOU 4647 N TYR B 358 11329 6468 4468 35 660 104 N ATOM 4648 CA TYR B 358 30.688 -22.851 60.030 1.00 58.38 C ANISOU 4648 CA TYR B 358 11442 6357 4384 9 1061 110 C ATOM 4649 C TYR B 358 30.804 -23.124 58.540 1.00 64.85 C ANISOU 4649 C TYR B 358 12743 7062 4836 21 1174 102 C ATOM 4650 O TYR B 358 31.390 -22.324 57.826 1.00 65.57 O ANISOU 4650 O TYR B 358 13073 7056 4784 3 1436 163 O ATOM 4651 CB TYR B 358 31.979 -23.336 60.732 1.00 59.00 C ANISOU 4651 CB TYR B 358 11215 6470 4734 -13 1345 5 C ATOM 4652 CG TYR B 358 31.996 -23.365 62.248 1.00 60.29 C ANISOU 4652 CG TYR B 358 10922 6744 5239 -16 1229 -18 C ATOM 4653 CD1 TYR B 358 31.234 -22.465 62.999 1.00 62.34 C ANISOU 4653 CD1 TYR B 358 11031 7053 5602 -24 1029 70 C ATOM 4654 CD2 TYR B 358 32.861 -24.208 62.933 1.00 60.59 C ANISOU 4654 CD2 TYR B 358 10696 6827 5499 -5 1344 -126 C ATOM 4655 CE1 TYR B 358 31.252 -22.489 64.396 1.00 61.87 C ANISOU 4655 CE1 TYR B 358 10595 7087 5825 -25 934 45 C ATOM 4656 CE2 TYR B 358 32.904 -24.227 64.326 1.00 61.42 C ANISOU 4656 CE2 TYR B 358 10425 7026 5887 -2 1229 -143 C ATOM 4657 CZ TYR B 358 32.084 -23.381 65.055 1.00 66.69 C ANISOU 4657 CZ TYR B 358 10975 7743 6622 -16 1026 -60 C ATOM 4658 OH TYR B 358 32.117 -23.440 66.427 1.00 64.89 O ANISOU 4658 OH TYR B 358 10417 7599 6639 -9 921 -83 O ATOM 4659 N ASN B 359 30.262 -24.248 58.070 1.00 64.34 N ANISOU 4659 N ASN B 359 12840 6996 4609 48 986 25 N ATOM 4660 CA ASN B 359 30.293 -24.607 56.655 1.00 65.65 C ANISOU 4660 CA ASN B 359 13501 7051 4392 65 1056 1 C ATOM 4661 C ASN B 359 29.400 -23.664 55.805 1.00 72.01 C ANISOU 4661 C ASN B 359 14675 7789 4896 89 850 133 C ATOM 4662 O ASN B 359 29.817 -23.230 54.728 1.00 70.39 O ANISOU 4662 O ASN B 359 14883 7466 4396 93 1068 176 O ATOM 4663 CB ASN B 359 29.885 -26.074 56.478 1.00 66.08 C ANISOU 4663 CB ASN B 359 13615 7118 4376 82 868 -129 C ATOM 4664 CG ASN B 359 29.993 -26.570 55.063 1.00 78.13 C ANISOU 4664 CG ASN B 359 15662 8522 5501 98 953 -183 C ATOM 4665 OD1 ASN B 359 31.048 -27.038 54.625 1.00 70.49 O ANISOU 4665 OD1 ASN B 359 14816 7486 4480 99 1321 -266 O ATOM 4666 ND2 ASN B 359 28.899 -26.480 54.323 1.00 68.21 N ANISOU 4666 ND2 ASN B 359 14726 7231 3959 117 610 -142 N ATOM 4667 N PHE B 360 28.190 -23.332 56.310 1.00 70.41 N ANISOU 4667 N PHE B 360 14323 7654 4774 111 443 200 N ATOM 4668 CA PHE B 360 27.226 -22.497 55.591 1.00 70.65 C ANISOU 4668 CA PHE B 360 14662 7627 4556 157 178 323 C ATOM 4669 C PHE B 360 27.396 -20.979 55.798 1.00 74.04 C ANISOU 4669 C PHE B 360 15063 8017 5050 163 305 474 C ATOM 4670 O PHE B 360 26.868 -20.189 55.014 1.00 73.98 O ANISOU 4670 O PHE B 360 15398 7922 4791 211 178 590 O ATOM 4671 CB PHE B 360 25.791 -22.934 55.948 1.00 72.63 C ANISOU 4671 CB PHE B 360 14761 7955 4880 186 -330 310 C ATOM 4672 CG PHE B 360 25.389 -24.264 55.354 1.00 74.72 C ANISOU 4672 CG PHE B 360 15208 8209 4974 180 -524 181 C ATOM 4673 CD1 PHE B 360 24.991 -24.360 54.026 1.00 77.79 C ANISOU 4673 CD1 PHE B 360 16106 8497 4954 215 -677 184 C ATOM 4674 CD2 PHE B 360 25.399 -25.421 56.126 1.00 76.98 C ANISOU 4674 CD2 PHE B 360 15180 8572 5496 140 -561 56 C ATOM 4675 CE1 PHE B 360 24.621 -25.596 53.478 1.00 78.91 C ANISOU 4675 CE1 PHE B 360 16428 8618 4936 201 -866 48 C ATOM 4676 CE2 PHE B 360 25.027 -26.655 55.575 1.00 79.30 C ANISOU 4676 CE2 PHE B 360 15651 8837 5641 126 -733 -70 C ATOM 4677 CZ PHE B 360 24.639 -26.734 54.261 1.00 77.31 C ANISOU 4677 CZ PHE B 360 15892 8488 4995 152 -888 -80 C ATOM 4678 N LEU B 361 28.116 -20.577 56.844 1.00 69.53 N ANISOU 4678 N LEU B 361 14106 7501 4813 118 537 470 N ATOM 4679 CA LEU B 361 28.256 -19.169 57.198 1.00 68.65 C ANISOU 4679 CA LEU B 361 13919 7351 4813 111 646 594 C ATOM 4680 C LEU B 361 29.718 -18.635 57.200 1.00 71.45 C ANISOU 4680 C LEU B 361 14254 7637 5256 39 1149 591 C ATOM 4681 O LEU B 361 29.940 -17.449 57.505 1.00 69.81 O ANISOU 4681 O LEU B 361 13979 7382 5163 15 1273 684 O ATOM 4682 CB LEU B 361 27.548 -18.930 58.556 1.00 68.07 C ANISOU 4682 CB LEU B 361 13384 7398 5084 121 396 603 C ATOM 4683 CG LEU B 361 26.016 -19.097 58.558 1.00 71.13 C ANISOU 4683 CG LEU B 361 13769 7828 5428 190 -81 638 C ATOM 4684 CD1 LEU B 361 25.461 -18.984 59.951 1.00 70.42 C ANISOU 4684 CD1 LEU B 361 13210 7852 5694 190 -242 627 C ATOM 4685 CD2 LEU B 361 25.329 -18.073 57.629 1.00 71.70 C ANISOU 4685 CD2 LEU B 361 14209 7788 5244 262 -238 784 C ATOM 4686 N SER B 362 30.698 -19.498 56.836 1.00 67.98 N ANISOU 4686 N SER B 362 13871 7181 4775 4 1441 479 N ATOM 4687 CA SER B 362 32.105 -19.108 56.735 1.00 67.99 C ANISOU 4687 CA SER B 362 13845 7111 4878 -66 1934 457 C ATOM 4688 C SER B 362 32.731 -19.692 55.500 1.00 73.71 C ANISOU 4688 C SER B 362 14974 7729 5303 -68 2218 408 C ATOM 4689 O SER B 362 32.879 -20.911 55.418 1.00 74.00 O ANISOU 4689 O SER B 362 14980 7810 5326 -48 2205 280 O ATOM 4690 CB SER B 362 32.904 -19.487 57.977 1.00 70.30 C ANISOU 4690 CB SER B 362 13607 7512 5593 -110 2057 346 C ATOM 4691 OG SER B 362 34.270 -19.135 57.824 1.00 74.93 O ANISOU 4691 OG SER B 362 14143 8024 6303 -181 2524 313 O ATOM 4692 N GLY B 363 33.065 -18.816 54.547 1.00 71.48 N ANISOU 4692 N GLY B 363 15089 7294 4776 -89 2478 511 N ATOM 4693 CA GLY B 363 33.709 -19.175 53.287 1.00 72.03 C ANISOU 4693 CA GLY B 363 15615 7232 4522 -95 2818 483 C ATOM 4694 C GLY B 363 35.065 -19.816 53.507 1.00 78.43 C ANISOU 4694 C GLY B 363 16176 8050 5576 -150 3257 339 C ATOM 4695 O GLY B 363 35.387 -20.823 52.862 1.00 79.42 O ANISOU 4695 O GLY B 363 16500 8144 5531 -123 3389 233 O ATOM 4696 N LYS B 364 35.858 -19.254 54.455 1.00 75.14 N ANISOU 4696 N LYS B 364 15304 7670 5574 -221 3467 325 N ATOM 4697 CA LYS B 364 37.171 -19.782 54.848 1.00 75.09 C ANISOU 4697 CA LYS B 364 14958 7684 5890 -267 3846 184 C ATOM 4698 C LYS B 364 37.042 -21.231 55.382 1.00 80.43 C ANISOU 4698 C LYS B 364 15381 8489 6690 -200 3628 35 C ATOM 4699 O LYS B 364 37.828 -22.096 54.972 1.00 82.52 O ANISOU 4699 O LYS B 364 15678 8718 6959 -185 3907 -84 O ATOM 4700 CB LYS B 364 37.873 -18.861 55.859 1.00 76.66 C ANISOU 4700 CB LYS B 364 14697 7909 6520 -353 3998 196 C ATOM 4701 CG LYS B 364 38.460 -17.617 55.223 1.00 86.18 C ANISOU 4701 CG LYS B 364 16131 8947 7665 -446 4394 301 C ATOM 4702 CD LYS B 364 39.032 -16.664 56.249 1.00 93.12 C ANISOU 4702 CD LYS B 364 16562 9846 8971 -541 4485 306 C ATOM 4703 CE LYS B 364 39.225 -15.291 55.659 1.00105.36 C ANISOU 4703 CE LYS B 364 18392 11219 10421 -631 4763 447 C ATOM 4704 NZ LYS B 364 39.509 -14.279 56.706 1.00116.99 N ANISOU 4704 NZ LYS B 364 19463 12709 12280 -720 4750 461 N ATOM 4705 N PHE B 365 36.007 -21.510 56.208 1.00 74.21 N ANISOU 4705 N PHE B 365 14385 7831 5981 -155 3146 46 N ATOM 4706 CA PHE B 365 35.742 -22.860 56.713 1.00 73.51 C ANISOU 4706 CA PHE B 365 14098 7847 5987 -96 2914 -75 C ATOM 4707 C PHE B 365 35.243 -23.810 55.613 1.00 78.88 C ANISOU 4707 C PHE B 365 15227 8465 6278 -42 2830 -121 C ATOM 4708 O PHE B 365 35.752 -24.926 55.506 1.00 78.45 O ANISOU 4708 O PHE B 365 15142 8406 6260 -11 2957 -254 O ATOM 4709 CB PHE B 365 34.777 -22.851 57.911 1.00 74.44 C ANISOU 4709 CB PHE B 365 13883 8103 6296 -76 2462 -45 C ATOM 4710 CG PHE B 365 35.436 -22.650 59.256 1.00 75.41 C ANISOU 4710 CG PHE B 365 13479 8319 6856 -104 2510 -88 C ATOM 4711 CD1 PHE B 365 36.252 -23.637 59.805 1.00 78.25 C ANISOU 4711 CD1 PHE B 365 13548 8727 7458 -79 2621 -221 C ATOM 4712 CD2 PHE B 365 35.199 -21.497 60.001 1.00 77.03 C ANISOU 4712 CD2 PHE B 365 13486 8557 7223 -144 2415 2 C ATOM 4713 CE1 PHE B 365 36.851 -23.453 61.059 1.00 79.33 C ANISOU 4713 CE1 PHE B 365 13214 8946 7980 -94 2623 -262 C ATOM 4714 CE2 PHE B 365 35.794 -21.316 61.256 1.00 79.57 C ANISOU 4714 CE2 PHE B 365 13347 8961 7926 -170 2432 -48 C ATOM 4715 CZ PHE B 365 36.618 -22.292 61.775 1.00 77.82 C ANISOU 4715 CZ PHE B 365 12849 8790 7928 -144 2525 -179 C ATOM 4716 N ARG B 366 34.267 -23.360 54.795 1.00 76.92 N ANISOU 4716 N ARG B 366 15404 8159 5662 -27 2612 -17 N ATOM 4717 CA ARG B 366 33.680 -24.112 53.677 1.00 77.44 C ANISOU 4717 CA ARG B 366 15954 8154 5313 19 2478 -54 C ATOM 4718 C ARG B 366 34.769 -24.640 52.731 1.00 85.07 C ANISOU 4718 C ARG B 366 17207 8999 6115 18 2949 -150 C ATOM 4719 O ARG B 366 34.711 -25.806 52.338 1.00 84.61 O ANISOU 4719 O ARG B 366 17294 8926 5929 57 2907 -274 O ATOM 4720 CB ARG B 366 32.672 -23.231 52.907 1.00 74.53 C ANISOU 4720 CB ARG B 366 16010 7721 4588 38 2227 95 C ATOM 4721 CG ARG B 366 31.838 -23.974 51.864 1.00 74.32 C ANISOU 4721 CG ARG B 366 16463 7639 4138 88 1956 56 C ATOM 4722 CD ARG B 366 30.452 -23.386 51.659 1.00 78.17 C ANISOU 4722 CD ARG B 366 17128 8138 4436 128 1462 175 C ATOM 4723 NE ARG B 366 30.485 -22.043 51.069 1.00 92.42 N ANISOU 4723 NE ARG B 366 19245 9835 6033 135 1579 343 N ATOM 4724 CZ ARG B 366 30.106 -20.922 51.686 1.00104.27 C ANISOU 4724 CZ ARG B 366 20534 11367 7716 135 1456 478 C ATOM 4725 NH1 ARG B 366 30.173 -19.759 51.055 1.00 93.92 N ANISOU 4725 NH1 ARG B 366 19562 9932 6193 144 1583 632 N ATOM 4726 NH2 ARG B 366 29.645 -20.961 52.933 1.00 82.03 N ANISOU 4726 NH2 ARG B 366 17188 8695 5286 128 1214 462 N ATOM 4727 N GLU B 367 35.770 -23.782 52.407 1.00 84.20 N ANISOU 4727 N GLU B 367 17161 8797 6035 -32 3414 -99 N ATOM 4728 CA GLU B 367 36.917 -24.074 51.537 1.00 85.10 C ANISOU 4728 CA GLU B 367 17516 8780 6037 -44 3953 -178 C ATOM 4729 C GLU B 367 37.774 -25.212 52.071 1.00 88.26 C ANISOU 4729 C GLU B 367 17542 9233 6759 -19 4133 -355 C ATOM 4730 O GLU B 367 38.130 -26.123 51.318 1.00 87.54 O ANISOU 4730 O GLU B 367 17717 9063 6481 23 4323 -470 O ATOM 4731 CB GLU B 367 37.786 -22.818 51.372 1.00 87.28 C ANISOU 4731 CB GLU B 367 17795 8961 6404 -124 4400 -81 C ATOM 4732 CG GLU B 367 37.313 -21.894 50.268 1.00105.71 C ANISOU 4732 CG GLU B 367 20724 11154 8285 -135 4430 78 C ATOM 4733 CD GLU B 367 38.165 -20.655 50.081 1.00140.91 C ANISOU 4733 CD GLU B 367 25207 15496 12838 -227 4894 181 C ATOM 4734 OE1 GLU B 367 38.827 -20.547 49.022 1.00140.57 O ANISOU 4734 OE1 GLU B 367 25575 15288 12546 -252 5360 184 O ATOM 4735 OE2 GLU B 367 38.168 -19.789 50.989 1.00138.69 O ANISOU 4735 OE2 GLU B 367 24546 15274 12876 -278 4805 254 O ATOM 4736 N GLN B 368 38.103 -25.154 53.379 1.00 84.57 N ANISOU 4736 N GLN B 368 16475 8890 6769 -34 4062 -380 N ATOM 4737 CA GLN B 368 38.917 -26.160 54.066 1.00 83.95 C ANISOU 4737 CA GLN B 368 15983 8867 7047 5 4185 -534 C ATOM 4738 C GLN B 368 38.191 -27.517 54.185 1.00 85.83 C ANISOU 4738 C GLN B 368 16264 9154 7192 82 3836 -630 C ATOM 4739 O GLN B 368 38.836 -28.567 54.116 1.00 84.79 O ANISOU 4739 O GLN B 368 16070 8991 7156 137 4019 -770 O ATOM 4740 CB GLN B 368 39.387 -25.643 55.442 1.00 85.07 C ANISOU 4740 CB GLN B 368 15515 9125 7685 -29 4145 -523 C ATOM 4741 CG GLN B 368 40.336 -24.433 55.407 1.00 97.25 C ANISOU 4741 CG GLN B 368 16935 10605 9409 -119 4545 -468 C ATOM 4742 CD GLN B 368 41.599 -24.662 54.601 1.00113.51 C ANISOU 4742 CD GLN B 368 19084 12538 11506 -130 5121 -562 C ATOM 4743 OE1 GLN B 368 42.487 -25.432 54.981 1.00107.66 O ANISOU 4743 OE1 GLN B 368 18014 11818 11073 -86 5295 -699 O ATOM 4744 NE2 GLN B 368 41.703 -23.993 53.465 1.00104.80 N ANISOU 4744 NE2 GLN B 368 18439 11291 10091 -182 5437 -486 N ATOM 4745 N PHE B 369 36.851 -27.478 54.350 1.00 80.69 N ANISOU 4745 N PHE B 369 15718 8567 6372 85 3344 -557 N ATOM 4746 CA PHE B 369 35.989 -28.656 54.461 1.00 79.16 C ANISOU 4746 CA PHE B 369 15575 8411 6090 133 2974 -635 C ATOM 4747 C PHE B 369 35.840 -29.339 53.099 1.00 85.42 C ANISOU 4747 C PHE B 369 16933 9072 6450 161 3058 -709 C ATOM 4748 O PHE B 369 35.941 -30.562 53.028 1.00 85.09 O ANISOU 4748 O PHE B 369 16916 9003 6411 207 3048 -845 O ATOM 4749 CB PHE B 369 34.611 -28.286 55.049 1.00 79.40 C ANISOU 4749 CB PHE B 369 15515 8544 6109 116 2451 -533 C ATOM 4750 CG PHE B 369 34.555 -27.783 56.479 1.00 78.97 C ANISOU 4750 CG PHE B 369 14933 8621 6451 96 2301 -475 C ATOM 4751 CD1 PHE B 369 35.665 -27.871 57.314 1.00 80.45 C ANISOU 4751 CD1 PHE B 369 14708 8849 7010 101 2549 -531 C ATOM 4752 CD2 PHE B 369 33.376 -27.269 57.005 1.00 79.54 C ANISOU 4752 CD2 PHE B 369 14921 8774 6528 80 1897 -374 C ATOM 4753 CE1 PHE B 369 35.595 -27.451 58.645 1.00 80.26 C ANISOU 4753 CE1 PHE B 369 14235 8941 7320 86 2386 -487 C ATOM 4754 CE2 PHE B 369 33.308 -26.849 58.336 1.00 81.37 C ANISOU 4754 CE2 PHE B 369 14697 9118 7102 65 1771 -330 C ATOM 4755 CZ PHE B 369 34.418 -26.941 59.144 1.00 79.07 C ANISOU 4755 CZ PHE B 369 14038 8863 7141 67 2011 -387 C ATOM 4756 N LYS B 370 35.640 -28.553 52.015 1.00 83.80 N ANISOU 4756 N LYS B 370 17206 8772 5864 138 3152 -622 N ATOM 4757 CA LYS B 370 35.531 -29.069 50.638 1.00 84.10 C ANISOU 4757 CA LYS B 370 17854 8668 5432 164 3250 -685 C ATOM 4758 C LYS B 370 36.854 -29.735 50.229 1.00 89.84 C ANISOU 4758 C LYS B 370 18618 9296 6221 192 3794 -825 C ATOM 4759 O LYS B 370 36.830 -30.788 49.590 1.00 89.64 O ANISOU 4759 O LYS B 370 18889 9189 5981 236 3821 -957 O ATOM 4760 CB LYS B 370 35.148 -27.946 49.659 1.00 86.26 C ANISOU 4760 CB LYS B 370 18620 8853 5301 140 3268 -540 C ATOM 4761 CG LYS B 370 34.540 -28.437 48.349 1.00101.32 C ANISOU 4761 CG LYS B 370 21197 10639 6660 172 3143 -585 C ATOM 4762 CD LYS B 370 34.201 -27.274 47.419 1.00111.82 C ANISOU 4762 CD LYS B 370 23032 11872 7584 163 3155 -424 C ATOM 4763 CE LYS B 370 33.759 -27.741 46.049 1.00121.58 C ANISOU 4763 CE LYS B 370 24986 12970 8240 201 3075 -475 C ATOM 4764 NZ LYS B 370 33.301 -26.612 45.192 1.00124.88 N ANISOU 4764 NZ LYS B 370 25915 13290 8243 208 3016 -301 N ATOM 4765 N ALA B 371 37.997 -29.140 50.655 1.00 87.63 N ANISOU 4765 N ALA B 371 18003 9022 6270 167 4214 -806 N ATOM 4766 CA ALA B 371 39.362 -29.633 50.448 1.00 88.16 C ANISOU 4766 CA ALA B 371 17971 9008 6517 195 4760 -933 C ATOM 4767 C ALA B 371 39.566 -30.998 51.107 1.00 95.98 C ANISOU 4767 C ALA B 371 18643 10046 7780 271 4657 -1092 C ATOM 4768 O ALA B 371 40.186 -31.888 50.508 1.00 96.04 O ANISOU 4768 O ALA B 371 18828 9946 7717 329 4958 -1234 O ATOM 4769 CB ALA B 371 40.361 -28.639 51.015 1.00 88.70 C ANISOU 4769 CB ALA B 371 17634 9102 6967 138 5107 -873 C ATOM 4770 N ALA B 372 39.026 -31.155 52.334 1.00 95.55 N ANISOU 4770 N ALA B 372 18142 10139 8025 275 4241 -1065 N ATOM 4771 CA ALA B 372 39.087 -32.362 53.153 1.00 97.01 C ANISOU 4771 CA ALA B 372 17996 10376 8489 345 4072 -1182 C ATOM 4772 C ALA B 372 38.267 -33.507 52.564 1.00105.53 C ANISOU 4772 C ALA B 372 19455 11388 9255 382 3826 -1277 C ATOM 4773 O ALA B 372 38.698 -34.656 52.664 1.00106.08 O ANISOU 4773 O ALA B 372 19457 11404 9444 455 3927 -1417 O ATOM 4774 CB ALA B 372 38.631 -32.056 54.568 1.00 97.71 C ANISOU 4774 CB ALA B 372 17589 10626 8910 325 3692 -1100 C ATOM 4775 N PHE B 373 37.100 -33.216 51.948 1.00104.88 N ANISOU 4775 N PHE B 373 19768 11296 8785 335 3496 -1207 N ATOM 4776 CA PHE B 373 36.297 -34.270 51.324 1.00106.40 C ANISOU 4776 CA PHE B 373 20341 11415 8671 353 3235 -1309 C ATOM 4777 C PHE B 373 36.873 -34.665 49.964 1.00116.35 C ANISOU 4777 C PHE B 373 22141 12500 9567 387 3617 -1418 C ATOM 4778 O PHE B 373 36.839 -35.848 49.613 1.00116.15 O ANISOU 4778 O PHE B 373 22309 12386 9435 431 3599 -1570 O ATOM 4779 CB PHE B 373 34.800 -33.920 51.272 1.00107.95 C ANISOU 4779 CB PHE B 373 20703 11672 8642 297 2691 -1213 C ATOM 4780 CG PHE B 373 34.148 -33.942 52.635 1.00109.49 C ANISOU 4780 CG PHE B 373 20387 12017 9197 275 2307 -1153 C ATOM 4781 CD1 PHE B 373 33.843 -35.148 53.262 1.00112.67 C ANISOU 4781 CD1 PHE B 373 20594 12433 9784 294 2095 -1254 C ATOM 4782 CD2 PHE B 373 33.865 -32.761 53.307 1.00111.51 C ANISOU 4782 CD2 PHE B 373 20372 12387 9608 235 2183 -995 C ATOM 4783 CE1 PHE B 373 33.272 -35.168 54.540 1.00113.22 C ANISOU 4783 CE1 PHE B 373 20216 12629 10175 272 1781 -1193 C ATOM 4784 CE2 PHE B 373 33.294 -32.781 54.584 1.00114.32 C ANISOU 4784 CE2 PHE B 373 20276 12873 10286 218 1865 -945 C ATOM 4785 CZ PHE B 373 32.996 -33.985 55.189 1.00112.25 C ANISOU 4785 CZ PHE B 373 19836 12624 10189 236 1671 -1041 C ATOM 4786 N SER B 374 37.476 -33.686 49.237 1.00117.31 N ANISOU 4786 N SER B 374 22500 12559 9513 365 4001 -1346 N ATOM 4787 CA SER B 374 38.147 -33.888 47.944 1.00119.00 C ANISOU 4787 CA SER B 374 23239 12597 9378 393 4457 -1434 C ATOM 4788 C SER B 374 39.355 -34.827 48.110 1.00128.48 C ANISOU 4788 C SER B 374 24209 13731 10874 470 4897 -1600 C ATOM 4789 O SER B 374 39.645 -35.618 47.208 1.00128.25 O ANISOU 4789 O SER B 374 24586 13555 10588 520 5136 -1741 O ATOM 4790 CB SER B 374 38.615 -32.554 47.365 1.00121.49 C ANISOU 4790 CB SER B 374 23762 12864 9533 343 4806 -1298 C ATOM 4791 OG SER B 374 37.534 -31.672 47.110 1.00127.14 O ANISOU 4791 OG SER B 374 24738 13617 9955 293 4416 -1141 O ATOM 4792 N TRP B 375 40.047 -34.730 49.270 1.00129.25 N ANISOU 4792 N TRP B 375 23662 13934 11515 487 4990 -1586 N ATOM 4793 CA TRP B 375 41.213 -35.537 49.630 1.00131.23 C ANISOU 4793 CA TRP B 375 23578 14143 12140 576 5355 -1728 C ATOM 4794 C TRP B 375 40.836 -37.005 49.855 1.00138.23 C ANISOU 4794 C TRP B 375 24471 14996 13054 655 5102 -1872 C ATOM 4795 O TRP B 375 41.546 -37.891 49.367 1.00138.21 O ANISOU 4795 O TRP B 375 24597 14863 13056 741 5438 -2029 O ATOM 4796 CB TRP B 375 41.923 -34.949 50.866 1.00130.63 C ANISOU 4796 CB TRP B 375 22813 14198 12622 570 5416 -1662 C ATOM 4797 CG TRP B 375 43.124 -35.730 51.319 1.00132.08 C ANISOU 4797 CG TRP B 375 22600 14348 13235 676 5740 -1802 C ATOM 4798 CD1 TRP B 375 43.202 -36.559 52.399 1.00135.10 C ANISOU 4798 CD1 TRP B 375 22546 14799 13987 757 5498 -1859 C ATOM 4799 CD2 TRP B 375 44.410 -35.781 50.679 1.00132.08 C ANISOU 4799 CD2 TRP B 375 22624 14223 13339 723 6366 -1904 C ATOM 4800 NE1 TRP B 375 44.458 -37.118 52.480 1.00134.73 N ANISOU 4800 NE1 TRP B 375 22237 14681 14275 864 5906 -1989 N ATOM 4801 CE2 TRP B 375 45.221 -36.656 51.437 1.00136.20 C ANISOU 4801 CE2 TRP B 375 22676 14751 14324 844 6451 -2025 C ATOM 4802 CE3 TRP B 375 44.962 -35.160 49.543 1.00133.43 C ANISOU 4802 CE3 TRP B 375 23166 14268 13263 678 6879 -1902 C ATOM 4803 CZ2 TRP B 375 46.552 -36.932 51.093 1.00135.62 C ANISOU 4803 CZ2 TRP B 375 22460 14568 14502 924 7021 -2152 C ATOM 4804 CZ3 TRP B 375 46.281 -35.433 49.204 1.00135.05 C ANISOU 4804 CZ3 TRP B 375 23241 14362 13709 743 7477 -2028 C ATOM 4805 CH2 TRP B 375 47.060 -36.310 49.972 1.00135.74 C ANISOU 4805 CH2 TRP B 375 22824 14464 14286 868 7540 -2156 C ATOM 4806 N TRP B 376 39.727 -37.266 50.578 1.00136.53 N ANISOU 4806 N TRP B 376 24124 14884 12867 624 4534 -1822 N ATOM 4807 CA TRP B 376 39.284 -38.635 50.843 1.00137.40 C ANISOU 4807 CA TRP B 376 24238 14953 13015 679 4270 -1946 C ATOM 4808 C TRP B 376 38.589 -39.276 49.632 1.00142.69 C ANISOU 4808 C TRP B 376 25558 15482 13176 663 4166 -2048 C ATOM 4809 O TRP B 376 38.916 -40.416 49.285 1.00142.44 O ANISOU 4809 O TRP B 376 25685 15319 13117 737 4301 -2214 O ATOM 4810 CB TRP B 376 38.436 -38.718 52.119 1.00136.45 C ANISOU 4810 CB TRP B 376 23705 14982 13158 645 3756 -1859 C ATOM 4811 CG TRP B 376 39.174 -38.288 53.358 1.00137.80 C ANISOU 4811 CG TRP B 376 23257 15275 13825 677 3838 -1790 C ATOM 4812 CD1 TRP B 376 40.508 -38.434 53.613 1.00140.76 C ANISOU 4812 CD1 TRP B 376 23336 15619 14527 766 4248 -1856 C ATOM 4813 CD2 TRP B 376 38.610 -37.657 54.519 1.00137.86 C ANISOU 4813 CD2 TRP B 376 22870 15448 14062 624 3485 -1651 C ATOM 4814 NE1 TRP B 376 40.814 -37.915 54.849 1.00140.45 N ANISOU 4814 NE1 TRP B 376 22751 15720 14894 767 4146 -1769 N ATOM 4815 CE2 TRP B 376 39.667 -37.438 55.432 1.00141.99 C ANISOU 4815 CE2 TRP B 376 22892 16034 15024 681 3690 -1642 C ATOM 4816 CE3 TRP B 376 37.311 -37.245 54.876 1.00139.13 C ANISOU 4816 CE3 TRP B 376 23049 15706 14107 537 3019 -1539 C ATOM 4817 CZ2 TRP B 376 39.466 -36.830 56.681 1.00141.34 C ANISOU 4817 CZ2 TRP B 376 22367 16104 15231 651 3440 -1528 C ATOM 4818 CZ3 TRP B 376 37.113 -36.645 56.112 1.00140.58 C ANISOU 4818 CZ3 TRP B 376 22783 16038 14592 511 2806 -1424 C ATOM 4819 CH2 TRP B 376 38.181 -36.444 57.000 1.00141.26 C ANISOU 4819 CH2 TRP B 376 22414 16180 15077 566 3013 -1420 C ATOM 4820 N LEU B 377 37.673 -38.536 48.965 1.00139.51 N ANISOU 4820 N LEU B 377 25544 15093 12370 577 3932 -1955 N ATOM 4821 CA LEU B 377 36.958 -39.026 47.780 1.00160.54 C ANISOU 4821 CA LEU B 377 28856 17626 14516 557 3783 -2048 C ATOM 4822 C LEU B 377 37.868 -39.014 46.557 1.00175.12 C ANISOU 4822 C LEU B 377 31179 19305 16054 604 4338 -2138 C ATOM 4823 O LEU B 377 37.693 -39.833 45.661 1.00136.34 O ANISOU 4823 O LEU B 377 26764 14244 10797 628 4360 -2286 O ATOM 4824 CB LEU B 377 35.693 -38.192 47.513 1.00160.51 C ANISOU 4824 CB LEU B 377 29082 17696 14208 465 3314 -1912 C ATOM 4825 CG LEU B 377 34.901 -38.563 46.260 1.00165.02 C ANISOU 4825 CG LEU B 377 30106 18189 14404 429 2873 -2009 C ATOM 4826 CD1 LEU B 377 34.364 -39.975 46.357 1.00165.10 C ANISOU 4826 CD1 LEU B 377 29891 18339 14501 352 2262 -1898 C ATOM 4827 CD2 LEU B 377 33.772 -37.578 46.001 1.00167.09 C ANISOU 4827 CD2 LEU B 377 31096 18311 14079 429 3010 -2042 C TER 4828 LEU B 377 HETATM 4829 C01 NRK A 401 24.354 -1.398 92.748 1.00 45.24 C HETATM 4830 C02 NRK A 401 22.917 -1.904 92.637 1.00 45.24 C HETATM 4831 C03 NRK A 401 23.604 -1.904 94.009 1.00 47.32 C HETATM 4832 C04 NRK A 401 22.888 -1.015 95.085 1.00 45.19 C HETATM 4833 C05 NRK A 401 24.899 0.037 92.919 1.00 53.96 C HETATM 4834 C06 NRK A 401 24.244 -3.111 94.675 1.00 47.08 C HETATM 4835 C07 NRK A 401 25.534 -2.965 95.186 1.00 45.23 C HETATM 4836 C08 NRK A 401 26.145 -4.039 95.808 1.00 48.46 C HETATM 4837 C09 NRK A 401 25.478 -5.244 95.956 1.00 45.24 C HETATM 4838 C10 NRK A 401 24.165 -5.386 95.493 1.00 45.20 C HETATM 4839 C11 NRK A 401 23.554 -4.316 94.840 1.00 45.22 C HETATM 4840 O12 NRK A 401 23.841 -0.294 95.889 1.00 45.95 O HETATM 4841 C13 NRK A 401 23.630 1.020 96.297 1.00 46.64 C HETATM 4842 C14 NRK A 401 24.692 1.710 96.924 1.00 47.06 C HETATM 4843 N15 NRK A 401 24.554 2.994 97.357 1.00 49.23 N HETATM 4844 C16 NRK A 401 23.380 3.647 97.125 1.00 47.60 C HETATM 4845 N17 NRK A 401 22.304 3.097 96.518 1.00 44.56 N HETATM 4846 C18 NRK A 401 22.447 1.798 96.115 1.00 45.14 C HETATM 4847 O19 NRK A 401 26.124 0.052 92.837 1.00 66.87 O HETATM 4848 N20 NRK A 401 24.194 1.157 93.189 1.00 45.21 N HETATM 4849 C21 NRK A 401 24.714 2.450 93.493 1.00 48.36 C HETATM 4850 C22 NRK A 401 26.032 2.722 93.979 1.00 45.20 C HETATM 4851 C23 NRK A 401 26.380 4.015 94.413 1.00 45.15 C HETATM 4852 C24 NRK A 401 25.418 5.040 94.361 1.00 48.95 C HETATM 4853 C25 NRK A 401 24.128 4.716 93.917 1.00 45.22 C HETATM 4854 N26 NRK A 401 23.771 3.454 93.531 1.00 48.49 N HETATM 4855 C27 NRK A 401 23.277 5.089 97.607 1.00 45.16 C HETATM 4856 C28 NRK A 401 26.044 1.090 97.250 1.00 45.16 C HETATM 4857 F29 NRK A 401 25.708 6.316 94.729 1.00 51.40 F HETATM 4858 F30 NRK A 401 27.383 -3.891 96.307 1.00 56.48 F HETATM 4859 H011 NRK A 401 25.031 -1.984 92.373 1.00 45.15 H HETATM 4860 H021 NRK A 401 22.773 -2.747 92.181 1.00 45.15 H HETATM 4861 H022 NRK A 401 22.184 -1.294 92.458 1.00 45.15 H HETATM 4862 H041 NRK A 401 22.348 -1.572 95.668 1.00 45.15 H HETATM 4863 H042 NRK A 401 22.256 -0.436 94.638 1.00 45.15 H HETATM 4864 H071 NRK A 401 25.990 -2.164 95.101 1.00 45.15 H HETATM 4865 H091 NRK A 401 25.895 -5.948 96.399 1.00 45.15 H HETATM 4866 H101 NRK A 401 23.722 -6.200 95.577 1.00 45.15 H HETATM 4867 H111 NRK A 401 22.690 -4.414 94.509 1.00 45.15 H HETATM 4868 H181 NRK A 401 21.695 1.443 95.701 1.00 45.15 H HETATM 4869 H201 NRK A 401 23.344 1.076 93.287 1.00 45.15 H HETATM 4870 H221 NRK A 401 26.668 2.061 94.065 1.00 45.15 H HETATM 4871 H231 NRK A 401 27.248 4.204 94.690 1.00 45.15 H HETATM 4872 H251 NRK A 401 23.474 5.376 93.875 1.00 45.15 H HETATM 4873 H271 NRK A 401 22.369 5.424 97.552 1.00 45.15 H HETATM 4874 H273 NRK A 401 23.843 5.666 97.070 1.00 45.15 H HETATM 4875 H272 NRK A 401 23.568 5.151 98.531 1.00 45.15 H HETATM 4876 H282 NRK A 401 25.994 0.126 97.353 1.00 45.15 H HETATM 4877 H281 NRK A 401 26.398 1.451 98.077 1.00 45.15 H HETATM 4878 H283 NRK A 401 26.676 1.281 96.539 1.00 45.15 H HETATM 4879 O1 PG4 A 402 24.087 4.541 78.366 1.00102.98 O ANISOU 4879 O1 PG4 A 402 16964 10543 11620 734 -152 447 O HETATM 4880 C1 PG4 A 402 24.442 5.915 78.504 1.00102.81 C ANISOU 4880 C1 PG4 A 402 17214 10319 11529 678 67 435 C HETATM 4881 C2 PG4 A 402 25.918 6.107 78.719 1.00102.00 C ANISOU 4881 C2 PG4 A 402 17073 10182 11500 371 464 342 C HETATM 4882 O2 PG4 A 402 26.365 5.345 79.834 1.00100.33 O ANISOU 4882 O2 PG4 A 402 16305 10264 11552 239 459 263 O HETATM 4883 C3 PG4 A 402 27.508 5.897 80.475 1.00 98.17 C ANISOU 4883 C3 PG4 A 402 15910 9988 11402 0 760 149 C HETATM 4884 C4 PG4 A 402 28.067 4.933 81.478 1.00 97.19 C ANISOU 4884 C4 PG4 A 402 15245 10160 11524 -116 731 59 C HETATM 4885 O3 PG4 A 402 28.978 4.030 80.864 1.00 96.43 O ANISOU 4885 O3 PG4 A 402 15104 10090 11443 -247 866 8 O HETATM 4886 C5 PG4 A 402 28.651 2.658 81.053 1.00 94.85 C ANISOU 4886 C5 PG4 A 402 14587 10121 11330 -168 635 33 C HETATM 4887 C6 PG4 A 402 29.001 1.865 79.829 1.00 94.13 C ANISOU 4887 C6 PG4 A 402 14679 9957 11130 -194 699 54 C HETATM 4888 O4 PG4 A 402 30.411 1.771 79.659 1.00 92.95 O ANISOU 4888 O4 PG4 A 402 14483 9773 11060 -427 1020 -76 O HETATM 4889 C7 PG4 A 402 30.786 1.206 78.409 1.00 91.08 C ANISOU 4889 C7 PG4 A 402 14498 9412 10696 -466 1140 -59 C HETATM 4890 C8 PG4 A 402 32.279 1.065 78.315 1.00 89.16 C ANISOU 4890 C8 PG4 A 402 14134 9159 10583 -715 1484 -225 C HETATM 4891 O5 PG4 A 402 32.748 -0.121 78.935 1.00 87.56 O ANISOU 4891 O5 PG4 A 402 13472 9220 10578 -740 1390 -301 O HETATM 4892 S SO4 A 403 53.123 -21.465 96.573 1.00113.08 S HETATM 4893 O1 SO4 A 403 53.296 -22.666 95.763 1.00112.57 O HETATM 4894 O2 SO4 A 403 52.780 -20.338 95.698 1.00112.24 O HETATM 4895 O3 SO4 A 403 52.068 -21.703 97.546 1.00112.73 O HETATM 4896 O4 SO4 A 403 54.362 -21.150 97.290 1.00114.46 O HETATM 4897 S SO4 A 404 53.453 -13.578 105.807 1.00139.78 S HETATM 4898 O1 SO4 A 404 52.372 -12.936 105.055 1.00140.42 O HETATM 4899 O2 SO4 A 404 54.282 -14.350 104.879 1.00139.95 O HETATM 4900 O3 SO4 A 404 52.884 -14.458 106.829 1.00138.59 O HETATM 4901 O4 SO4 A 404 54.274 -12.562 106.462 1.00139.99 O HETATM 4902 C1 SOG A 405 12.007 11.653 113.518 1.00 66.32 C HETATM 4903 C2 SOG A 405 12.050 13.135 113.099 1.00 64.25 C HETATM 4904 C3 SOG A 405 10.686 13.801 113.245 1.00 67.94 C HETATM 4905 C4 SOG A 405 9.545 12.983 112.635 1.00 70.94 C HETATM 4906 C5 SOG A 405 9.641 11.484 112.980 1.00 69.33 C HETATM 4907 C6 SOG A 405 8.665 10.676 112.138 1.00 70.76 C HETATM 4908 C1' SOG A 405 14.069 10.800 111.730 1.00 59.42 C HETATM 4909 C2' SOG A 405 15.590 10.682 111.701 1.00 58.50 C HETATM 4910 C3' SOG A 405 16.157 10.286 110.344 1.00 57.65 C HETATM 4911 C4' SOG A 405 16.833 11.459 109.631 1.00 56.80 C HETATM 4912 C5' SOG A 405 18.327 11.492 109.915 1.00 55.59 C HETATM 4913 C6' SOG A 405 19.042 12.616 109.187 1.00 55.25 C HETATM 4914 C7' SOG A 405 19.827 12.089 107.991 1.00 59.28 C HETATM 4915 C8' SOG A 405 21.323 12.206 108.201 1.00 60.76 C HETATM 4916 S1 SOG A 405 13.610 10.879 113.436 1.00 63.23 S HETATM 4917 O2 SOG A 405 12.997 13.847 113.894 1.00 60.92 O HETATM 4918 O3 SOG A 405 10.707 15.101 112.647 1.00 70.19 O HETATM 4919 O4 SOG A 405 8.304 13.532 113.115 1.00 73.98 O HETATM 4920 O5 SOG A 405 10.970 10.952 112.801 1.00 68.32 O HETATM 4921 O6 SOG A 405 7.372 10.746 112.756 1.00 73.55 O HETATM 4922 C1 SOG A 406 7.795 -14.391 93.785 1.00102.71 C HETATM 4923 C2 SOG A 406 7.643 -14.701 95.282 1.00105.34 C HETATM 4924 C3 SOG A 406 6.366 -14.065 95.823 1.00106.67 C HETATM 4925 C4 SOG A 406 6.365 -12.561 95.570 1.00106.50 C HETATM 4926 C5 SOG A 406 6.675 -12.199 94.104 1.00106.16 C HETATM 4927 C6 SOG A 406 7.045 -10.717 93.996 1.00108.22 C HETATM 4928 C1' SOG A 406 9.548 -14.321 91.655 1.00 93.33 C HETATM 4929 C2' SOG A 406 10.024 -15.354 90.641 1.00 86.58 C HETATM 4930 C3' SOG A 406 11.148 -14.802 89.774 1.00 80.08 C HETATM 4931 C4' SOG A 406 12.496 -15.334 90.245 1.00 73.58 C HETATM 4932 C5' SOG A 406 13.082 -16.275 89.209 1.00 67.47 C HETATM 4933 C6' SOG A 406 14.261 -15.627 88.512 1.00 63.60 C HETATM 4934 C7' SOG A 406 15.327 -16.667 88.204 1.00 60.59 C HETATM 4935 C8' SOG A 406 15.626 -16.654 86.729 1.00 57.81 C HETATM 4936 S1 SOG A 406 9.312 -15.105 93.220 1.00 99.21 S HETATM 4937 O2 SOG A 406 7.660 -16.109 95.559 1.00106.16 O HETATM 4938 O3 SOG A 406 6.267 -14.294 97.232 1.00108.57 O HETATM 4939 O4 SOG A 406 5.087 -12.056 95.967 1.00107.51 O HETATM 4940 O5 SOG A 406 7.772 -12.965 93.554 1.00103.55 O HETATM 4941 O6 SOG A 406 5.889 -9.909 93.718 1.00109.75 O HETATM 4942 C1 SOG A 407 3.683 -13.972 87.194 1.00130.34 C HETATM 4943 C2 SOG A 407 4.170 -12.573 86.787 1.00129.91 C HETATM 4944 C3 SOG A 407 5.659 -12.382 87.126 1.00128.26 C HETATM 4945 C4 SOG A 407 6.155 -13.078 88.408 1.00128.06 C HETATM 4946 C5 SOG A 407 5.329 -14.291 88.867 1.00128.28 C HETATM 4947 C6 SOG A 407 5.550 -14.597 90.340 1.00127.58 C HETATM 4948 C1' SOG A 407 1.985 -15.997 86.503 1.00132.38 C HETATM 4949 S1 SOG A 407 1.982 -14.260 86.812 1.00132.15 S HETATM 4950 O2 SOG A 407 3.982 -12.365 85.380 1.00130.72 O HETATM 4951 O3 SOG A 407 5.966 -10.983 87.194 1.00127.04 O HETATM 4952 O4 SOG A 407 7.514 -13.495 88.221 1.00127.79 O HETATM 4953 O5 SOG A 407 3.928 -14.150 88.593 1.00128.93 O HETATM 4954 O6 SOG A 407 6.688 -15.457 90.432 1.00126.93 O HETATM 4955 C1 SOG A 408 14.269 -3.074 79.589 1.00117.75 C HETATM 4956 C2 SOG A 408 13.815 -2.439 80.909 1.00116.76 C HETATM 4957 C3 SOG A 408 13.638 -0.944 80.631 1.00118.71 C HETATM 4958 C4 SOG A 408 14.972 -0.319 80.219 1.00120.57 C HETATM 4959 C5 SOG A 408 15.417 -1.019 78.919 1.00120.28 C HETATM 4960 C6 SOG A 408 16.727 -0.481 78.339 1.00120.50 C HETATM 4961 C1' SOG A 408 14.729 -5.329 78.073 1.00113.11 C HETATM 4962 C2' SOG A 408 14.881 -6.846 78.025 1.00108.93 C HETATM 4963 C3' SOG A 408 16.173 -7.241 77.321 1.00105.77 C HETATM 4964 C4' SOG A 408 16.687 -8.574 77.843 1.00102.53 C HETATM 4965 C5' SOG A 408 17.701 -9.179 76.885 1.00 99.96 C HETATM 4966 C6' SOG A 408 18.191 -10.517 77.417 1.00 98.53 C HETATM 4967 C7' SOG A 408 17.923 -11.618 76.405 1.00 98.20 C HETATM 4968 C8' SOG A 408 17.806 -12.956 77.101 1.00 98.93 C HETATM 4969 S1 SOG A 408 14.371 -4.837 79.731 1.00117.53 S HETATM 4970 O2 SOG A 408 12.600 -3.039 81.373 1.00115.04 O HETATM 4971 O3 SOG A 408 13.014 -0.226 81.690 1.00118.79 O HETATM 4972 O4 SOG A 408 14.832 1.106 80.080 1.00121.84 O HETATM 4973 O5 SOG A 408 15.492 -2.453 79.125 1.00118.67 O HETATM 4974 O6 SOG A 408 16.528 0.740 77.609 1.00120.27 O HETATM 4975 CAD PGW A 409 19.818 2.600 78.018 1.00120.54 C HETATM 4976 OAE PGW A 409 18.463 2.556 78.493 1.00120.91 O HETATM 4977 OAF PGW A 409 19.195 0.667 76.671 1.00118.84 O HETATM 4978 P PGW A 409 21.258 -0.067 74.246 1.00118.80 P HETATM 4979 C01 PGW A 409 19.323 -3.578 77.127 1.00 92.92 C HETATM 4980 C1 PGW A 409 23.131 -3.275 77.048 1.00 84.51 C HETATM 4981 O01 PGW A 409 21.749 -3.719 77.276 1.00 89.65 O HETATM 4982 C02 PGW A 409 20.655 -2.848 76.942 1.00 95.19 C HETATM 4983 C2 PGW A 409 24.148 -4.225 76.466 1.00 77.81 C HETATM 4984 O02 PGW A 409 23.478 -2.140 77.322 1.00 85.99 O HETATM 4985 C03 PGW A 409 20.706 -2.376 75.494 1.00104.40 C HETATM 4986 C3 PGW A 409 24.933 -4.926 77.567 1.00 72.03 C HETATM 4987 O03 PGW A 409 19.237 -4.231 78.401 1.00 89.63 O HETATM 4988 C04 PGW A 409 21.423 1.572 76.388 1.00119.57 C HETATM 4989 C4 PGW A 409 26.373 -5.102 77.108 1.00 66.92 C HETATM 4990 O04 PGW A 409 18.800 -2.356 79.687 1.00 86.19 O HETATM 4991 C05 PGW A 409 19.954 1.883 76.676 1.00119.75 C HETATM 4992 C5 PGW A 409 26.794 -6.561 77.042 1.00 61.61 C HETATM 4993 C06 PGW A 409 30.345 -11.753 78.680 1.00 60.04 C HETATM 4994 C6 PGW A 409 28.216 -6.701 77.565 1.00 60.06 C HETATM 4995 C07 PGW A 409 29.601 -12.882 79.372 1.00 62.01 C HETATM 4996 C7 PGW A 409 29.003 -7.793 76.857 1.00 61.08 C HETATM 4997 C08 PGW A 409 30.383 -13.410 80.568 1.00 66.62 C HETATM 4998 C8 PGW A 409 29.276 -8.986 77.763 1.00 62.01 C HETATM 4999 C09 PGW A 409 29.462 -14.285 81.419 1.00 73.22 C HETATM 5000 C9 PGW A 409 29.213 -10.269 76.955 1.00 62.44 C HETATM 5001 C10 PGW A 409 29.666 -11.469 77.359 1.00 61.04 C HETATM 5002 C11 PGW A 409 30.226 -14.963 82.552 1.00 77.21 C HETATM 5003 O11 PGW A 409 21.397 -1.127 75.461 1.00112.47 O HETATM 5004 C12 PGW A 409 29.533 -14.766 83.898 1.00 79.57 C HETATM 5005 O12 PGW A 409 21.637 1.330 74.987 1.00119.73 O HETATM 5006 C13 PGW A 409 30.334 -15.456 85.000 1.00 82.17 C HETATM 5007 O13 PGW A 409 22.314 -0.393 73.206 1.00118.69 O HETATM 5008 C14 PGW A 409 31.124 -14.464 85.834 1.00 82.77 C HETATM 5009 O14 PGW A 409 19.808 0.007 73.806 1.00119.70 O HETATM 5010 C15 PGW A 409 20.899 -11.580 81.922 1.00 56.97 C HETATM 5011 C16 PGW A 409 21.455 -11.626 83.337 1.00 51.90 C HETATM 5012 C17 PGW A 409 22.874 -11.094 83.421 1.00 49.16 C HETATM 5013 C18 PGW A 409 23.107 -10.410 84.763 1.00 48.89 C HETATM 5014 C19 PGW A 409 18.702 -3.568 79.588 1.00 84.37 C HETATM 5015 C20 PGW A 409 18.025 -4.343 80.698 1.00 76.96 C HETATM 5016 C21 PGW A 409 18.797 -5.590 81.099 1.00 71.32 C HETATM 5017 C22 PGW A 409 17.874 -6.794 80.984 1.00 68.81 C HETATM 5018 C23 PGW A 409 18.268 -7.905 81.942 1.00 67.83 C HETATM 5019 C24 PGW A 409 17.223 -9.019 81.958 1.00 69.07 C HETATM 5020 C25 PGW A 409 17.819 -10.342 82.451 1.00 70.48 C HETATM 5021 C26 PGW A 409 18.488 -11.174 81.341 1.00 68.46 C HETATM 5022 C27 PGW A 409 19.495 -12.190 81.889 1.00 62.55 C HETATM 5023 C28 PGW A 409 24.580 -10.051 84.968 1.00 47.52 C HETATM 5024 C29 PGW A 409 26.311 -9.346 86.655 1.00 47.45 C HETATM 5025 C30 PGW A 409 24.858 -9.697 86.422 1.00 47.09 C HETATM 5026 CAD PGW A 410 24.206 -32.831 100.240 1.00106.38 C HETATM 5027 OAE PGW A 410 23.612 -31.767 100.995 1.00104.88 O HETATM 5028 OAF PGW A 410 26.363 -31.838 100.621 1.00108.02 O HETATM 5029 P PGW A 410 28.920 -33.773 99.663 1.00117.20 P HETATM 5030 C01 PGW A 410 30.219 -30.085 98.392 1.00 95.54 C HETATM 5031 C1 PGW A 410 33.645 -30.531 97.460 1.00 84.37 C HETATM 5032 O01 PGW A 410 32.618 -30.472 98.507 1.00 91.33 O HETATM 5033 C02 PGW A 410 31.355 -31.079 98.180 1.00 97.49 C HETATM 5034 C2 PGW A 410 34.513 -29.326 97.155 1.00 76.06 C HETATM 5035 O02 PGW A 410 33.855 -31.588 96.890 1.00 86.33 O HETATM 5036 C03 PGW A 410 31.094 -32.333 99.020 1.00104.51 C HETATM 5037 C3 PGW A 410 34.389 -28.775 95.739 1.00 68.69 C HETATM 5038 O03 PGW A 410 29.300 -30.202 97.306 1.00 92.65 O HETATM 5039 C04 PGW A 410 26.277 -34.132 99.769 1.00111.70 C HETATM 5040 C4 PGW A 410 35.643 -27.962 95.417 1.00 65.24 C HETATM 5041 O04 PGW A 410 27.189 -30.072 98.241 1.00 92.33 O HETATM 5042 C05 PGW A 410 25.642 -33.076 100.674 1.00108.51 C HETATM 5043 C5 PGW A 410 35.361 -26.637 94.706 1.00 61.91 C HETATM 5044 C06 PGW A 410 36.793 -21.004 91.579 1.00 65.19 C HETATM 5045 C6 PGW A 410 36.591 -26.015 94.034 1.00 59.43 C HETATM 5046 C07 PGW A 410 35.596 -20.065 91.484 1.00 67.84 C HETATM 5047 C7 PGW A 410 36.210 -24.713 93.329 1.00 59.91 C HETATM 5048 C08 PGW A 410 35.482 -19.415 90.103 1.00 69.38 C HETATM 5049 C8 PGW A 410 37.383 -23.860 92.838 1.00 60.80 C HETATM 5050 C09 PGW A 410 34.306 -18.441 90.094 1.00 72.05 C HETATM 5051 C9 PGW A 410 37.378 -22.503 93.536 1.00 63.08 C HETATM 5052 C10 PGW A 410 37.126 -21.285 93.026 1.00 63.26 C HETATM 5053 C11 PGW A 410 33.771 -18.158 88.690 1.00 74.75 C HETATM 5054 O11 PGW A 410 29.853 -32.944 98.630 1.00110.88 O HETATM 5055 C12 PGW A 410 32.256 -18.382 88.588 1.00 74.94 C HETATM 5056 O12 PGW A 410 27.417 -33.605 99.080 1.00115.48 O HETATM 5057 C13 PGW A 410 31.474 -17.082 88.752 1.00 74.02 C HETATM 5058 O13 PGW A 410 29.276 -35.244 99.541 1.00118.01 O HETATM 5059 C14 PGW A 410 30.031 -17.256 88.343 1.00 73.32 C HETATM 5060 O14 PGW A 410 28.972 -33.082 101.016 1.00118.85 O HETATM 5061 C15 PGW A 410 27.312 -23.218 95.154 1.00 54.98 C HETATM 5062 C16 PGW A 410 27.593 -22.638 93.785 1.00 51.25 C HETATM 5063 C17 PGW A 410 27.244 -23.629 92.690 1.00 49.57 C HETATM 5064 C18 PGW A 410 27.938 -23.205 91.402 1.00 48.23 C HETATM 5065 C19 PGW A 410 27.960 -29.644 97.397 1.00 89.46 C HETATM 5066 C20 PGW A 410 27.526 -28.572 96.435 1.00 83.35 C HETATM 5067 C21 PGW A 410 27.112 -27.334 97.213 1.00 80.26 C HETATM 5068 C22 PGW A 410 25.617 -27.108 97.040 1.00 78.41 C HETATM 5069 C23 PGW A 410 25.059 -26.187 98.114 1.00 75.63 C HETATM 5070 C24 PGW A 410 24.781 -24.810 97.536 1.00 74.01 C HETATM 5071 C25 PGW A 410 25.842 -23.795 97.975 1.00 71.93 C HETATM 5072 C26 PGW A 410 25.889 -22.513 97.131 1.00 66.71 C HETATM 5073 C27 PGW A 410 25.936 -22.763 95.624 1.00 60.03 C HETATM 5074 C28 PGW A 410 27.658 -24.198 90.281 1.00 44.74 C HETATM 5075 C29 PGW A 410 28.466 -24.820 88.020 1.00 42.16 C HETATM 5076 C30 PGW A 410 28.236 -23.677 88.973 1.00 42.46 C HETATM 5077 C01 NRK B 401 25.115 -32.996 83.881 1.00 45.27 C HETATM 5078 C02 NRK B 401 24.130 -32.631 84.983 1.00 45.20 C HETATM 5079 C03 NRK B 401 23.639 -32.629 83.537 1.00 47.01 C HETATM 5080 C04 NRK B 401 22.477 -33.653 83.310 1.00 45.16 C HETATM 5081 C05 NRK B 401 25.660 -34.375 83.397 1.00 51.62 C HETATM 5082 C06 NRK B 401 23.452 -31.346 82.712 1.00 46.29 C HETATM 5083 C07 NRK B 401 24.027 -31.295 81.439 1.00 45.17 C HETATM 5084 C08 NRK B 401 23.892 -30.168 80.630 1.00 47.80 C HETATM 5085 C09 NRK B 401 23.159 -29.069 81.091 1.00 45.16 C HETATM 5086 C10 NRK B 401 22.559 -29.100 82.362 1.00 45.18 C HETATM 5087 C11 NRK B 401 22.677 -30.255 83.157 1.00 45.19 C HETATM 5088 O12 NRK B 401 22.543 -34.164 81.972 1.00 47.41 O HETATM 5089 C13 NRK B 401 22.461 -35.520 81.664 1.00 46.88 C HETATM 5090 C14 NRK B 401 22.961 -35.966 80.415 1.00 45.19 C HETATM 5091 N15 NRK B 401 22.927 -37.289 80.051 1.00 47.17 N HETATM 5092 C16 NRK B 401 22.410 -38.193 80.941 1.00 45.57 C HETATM 5093 N17 NRK B 401 21.955 -37.893 82.187 1.00 44.59 N HETATM 5094 C18 NRK B 401 21.987 -36.561 82.530 1.00 45.17 C HETATM 5095 O19 NRK B 401 26.734 -34.294 82.816 1.00 60.30 O HETATM 5096 N20 NRK B 401 25.091 -35.579 83.483 1.00 45.26 N HETATM 5097 C21 NRK B 401 25.540 -36.771 82.847 1.00 47.88 C HETATM 5098 C22 NRK B 401 26.273 -36.844 81.627 1.00 45.13 C HETATM 5099 C23 NRK B 401 26.510 -38.088 81.012 1.00 45.13 C HETATM 5100 C24 NRK B 401 25.964 -39.251 81.591 1.00 47.67 C HETATM 5101 C25 NRK B 401 25.210 -39.108 82.758 1.00 45.19 C HETATM 5102 N26 NRK B 401 24.959 -37.904 83.348 1.00 48.51 N HETATM 5103 C27 NRK B 401 22.389 -39.642 80.521 1.00 45.14 C HETATM 5104 C28 NRK B 401 23.523 -35.051 79.345 1.00 45.13 C HETATM 5105 F29 NRK B 401 26.132 -40.499 81.071 1.00 49.84 F HETATM 5106 F30 NRK B 401 24.452 -30.177 79.387 1.00 51.31 F HETATM 5107 H011 NRK B 401 25.779 -32.312 83.696 1.00 45.15 H HETATM 5108 H021 NRK B 401 24.265 -31.784 85.435 1.00 45.15 H HETATM 5109 H022 NRK B 401 23.808 -33.299 85.608 1.00 45.15 H HETATM 5110 H041 NRK B 401 21.619 -33.217 83.435 1.00 45.15 H HETATM 5111 H042 NRK B 401 22.508 -34.342 83.987 1.00 45.15 H HETATM 5112 H071 NRK B 401 24.487 -32.024 81.110 1.00 45.15 H HETATM 5113 H091 NRK B 401 23.061 -28.322 80.546 1.00 45.15 H HETATM 5114 H101 NRK B 401 22.071 -28.368 82.667 1.00 45.15 H HETATM 5115 H111 NRK B 401 22.307 -30.261 84.010 1.00 45.15 H HETATM 5116 H181 NRK B 401 21.644 -36.369 83.372 1.00 45.15 H HETATM 5117 H201 NRK B 401 24.313 -35.630 83.836 1.00 45.15 H HETATM 5118 H221 NRK B 401 26.607 -36.094 81.208 1.00 45.15 H HETATM 5119 H231 NRK B 401 27.019 -38.145 80.236 1.00 45.15 H HETATM 5120 H251 NRK B 401 24.839 -39.860 83.159 1.00 45.15 H HETATM 5121 H271 NRK B 401 21.806 -40.173 81.086 1.00 45.15 H HETATM 5122 H273 NRK B 401 23.280 -40.019 80.576 1.00 45.15 H HETATM 5123 H272 NRK B 401 22.075 -39.718 79.607 1.00 45.15 H HETATM 5124 H282 NRK B 401 23.393 -34.112 79.543 1.00 45.15 H HETATM 5125 H281 NRK B 401 23.103 -35.230 78.490 1.00 45.15 H HETATM 5126 H283 NRK B 401 24.477 -35.203 79.251 1.00 45.15 H HETATM 5127 S SO4 B 402 38.822 -7.569 64.096 1.00 91.16 S HETATM 5128 O1 SO4 B 402 37.382 -7.677 63.871 1.00 89.95 O HETATM 5129 O2 SO4 B 402 39.496 -7.731 62.808 1.00 93.67 O HETATM 5130 O3 SO4 B 402 39.313 -8.605 65.004 1.00 91.69 O HETATM 5131 O4 SO4 B 402 39.138 -6.268 64.687 1.00 90.80 O HETATM 5132 S SO4 B 403 34.440 -15.695 55.948 1.00121.19 S HETATM 5133 O1 SO4 B 403 35.393 -15.479 54.854 1.00122.01 O HETATM 5134 O2 SO4 B 403 33.152 -16.131 55.391 1.00119.70 O HETATM 5135 O3 SO4 B 403 34.985 -16.688 56.877 1.00120.17 O HETATM 5136 O4 SO4 B 403 34.242 -14.438 56.672 1.00122.94 O HETATM 5137 C1 SOG B 404 34.859 -50.057 84.171 1.00 99.29 C HETATM 5138 C2 SOG B 404 34.772 -51.205 85.180 1.00 96.81 C HETATM 5139 C3 SOG B 404 35.159 -50.716 86.584 1.00 98.29 C HETATM 5140 C4 SOG B 404 36.514 -49.983 86.573 1.00101.35 C HETATM 5141 C5 SOG B 404 36.540 -48.916 85.458 1.00101.41 C HETATM 5142 C6 SOG B 404 37.870 -48.180 85.347 1.00102.29 C HETATM 5143 C1' SOG B 404 35.103 -49.461 81.465 1.00102.16 C HETATM 5144 C2' SOG B 404 34.707 -49.768 80.023 1.00101.84 C HETATM 5145 C3' SOG B 404 33.448 -49.009 79.613 1.00101.38 C HETATM 5146 C4' SOG B 404 33.775 -47.905 78.612 1.00100.98 C HETATM 5147 C5' SOG B 404 33.637 -46.523 79.246 1.00100.43 C HETATM 5148 C6' SOG B 404 32.443 -45.766 78.667 1.00 99.50 C HETATM 5149 C7' SOG B 404 32.889 -44.580 77.818 1.00 98.11 C HETATM 5150 C8' SOG B 404 32.054 -44.464 76.563 1.00 97.24 C HETATM 5151 S1 SOG B 404 34.341 -50.611 82.573 1.00101.68 S HETATM 5152 O2 SOG B 404 33.459 -51.767 85.166 1.00 94.52 O HETATM 5153 O3 SOG B 404 35.197 -51.812 87.504 1.00 97.01 O HETATM 5154 O4 SOG B 404 36.822 -49.426 87.866 1.00101.97 O HETATM 5155 O5 SOG B 404 36.189 -49.502 84.189 1.00100.08 O HETATM 5156 O6 SOG B 404 37.949 -47.221 86.409 1.00103.12 O HETATM 5157 C1 SOG B 405 28.448 3.855 76.029 1.00115.88 C HETATM 5158 C2 SOG B 405 27.294 4.482 75.239 1.00116.73 C HETATM 5159 C3 SOG B 405 25.955 3.809 75.570 1.00118.75 C HETATM 5160 C4 SOG B 405 26.007 2.271 75.504 1.00118.31 C HETATM 5161 C5 SOG B 405 27.246 1.708 76.227 1.00117.13 C HETATM 5162 C6 SOG B 405 27.469 0.217 75.964 1.00116.77 C HETATM 5163 C1' SOG B 405 30.823 4.874 76.905 1.00113.34 C HETATM 5164 S1 SOG B 405 29.980 4.475 75.403 1.00114.65 S HETATM 5165 O2 SOG B 405 27.208 5.876 75.551 1.00116.29 O HETATM 5166 O3 SOG B 405 24.935 4.317 74.699 1.00119.81 O HETATM 5167 O4 SOG B 405 24.812 1.704 76.068 1.00118.03 O HETATM 5168 O5 SOG B 405 28.452 2.421 75.896 1.00116.57 O HETATM 5169 O6 SOG B 405 27.667 -0.090 74.574 1.00116.28 O HETATM 5170 C1 SOG B 406 36.019 -37.895 92.083 1.00 90.76 C HETATM 5171 C2 SOG B 406 36.539 -38.895 93.116 1.00 92.30 C HETATM 5172 C3 SOG B 406 35.704 -38.775 94.401 1.00 93.49 C HETATM 5173 C4 SOG B 406 35.357 -37.334 94.839 1.00 92.03 C HETATM 5174 C5 SOG B 406 35.244 -36.292 93.708 1.00 90.59 C HETATM 5175 C6 SOG B 406 35.631 -34.907 94.211 1.00 89.92 C HETATM 5176 C1' SOG B 406 37.671 -36.595 90.246 1.00 81.90 C HETATM 5177 C2' SOG B 406 36.800 -35.627 89.456 1.00 75.23 C HETATM 5178 C3' SOG B 406 37.279 -34.199 89.693 1.00 70.33 C HETATM 5179 C4' SOG B 406 38.571 -33.919 88.931 1.00 66.74 C HETATM 5180 C5' SOG B 406 39.436 -32.908 89.670 1.00 65.52 C HETATM 5181 C6' SOG B 406 40.505 -32.394 88.715 1.00 62.95 C HETATM 5182 C7' SOG B 406 41.011 -31.018 89.102 1.00 59.46 C HETATM 5183 C8' SOG B 406 41.437 -30.290 87.852 1.00 58.79 C HETATM 5184 S1 SOG B 406 36.797 -38.093 90.503 1.00 89.35 S HETATM 5185 O2 SOG B 406 36.468 -40.231 92.592 1.00 93.14 O HETATM 5186 O3 SOG B 406 36.345 -39.486 95.471 1.00 95.28 O HETATM 5187 O4 SOG B 406 34.129 -37.338 95.582 1.00 90.88 O HETATM 5188 O5 SOG B 406 36.138 -36.575 92.623 1.00 90.66 O HETATM 5189 O6 SOG B 406 34.511 -34.310 94.860 1.00 89.92 O HETATM 5190 C1 SOG B 407 43.560 -14.184 80.278 1.00124.75 C HETATM 5191 C2 SOG B 407 43.627 -12.852 79.513 1.00126.08 C HETATM 5192 C3 SOG B 407 44.865 -12.706 78.616 1.00127.60 C HETATM 5193 C4 SOG B 407 46.156 -13.321 79.186 1.00128.16 C HETATM 5194 C5 SOG B 407 45.921 -14.650 79.924 1.00126.92 C HETATM 5195 C6 SOG B 407 47.166 -15.136 80.669 1.00126.32 C HETATM 5196 C1' SOG B 407 42.100 -15.768 81.956 1.00117.54 C HETATM 5197 C2' SOG B 407 40.605 -16.075 82.003 1.00113.16 C HETATM 5198 C3' SOG B 407 40.274 -17.067 83.113 1.00108.77 C HETATM 5199 C4' SOG B 407 38.791 -17.415 83.113 1.00105.72 C HETATM 5200 S1 SOG B 407 42.352 -14.063 81.567 1.00122.09 S HETATM 5201 O2 SOG B 407 42.446 -12.685 78.721 1.00126.30 O HETATM 5202 O3 SOG B 407 45.075 -11.313 78.340 1.00128.10 O HETATM 5203 O4 SOG B 407 47.110 -13.515 78.131 1.00129.07 O HETATM 5204 O5 SOG B 407 44.832 -14.532 80.856 1.00125.97 O HETATM 5205 O6 SOG B 407 48.169 -15.558 79.734 1.00125.58 O HETATM 5206 C1 SOG B 408 9.766 -23.583 96.935 1.00101.96 C HETATM 5207 C2 SOG B 408 8.653 -24.643 96.995 1.00104.38 C HETATM 5208 C3 SOG B 408 7.960 -24.542 98.366 1.00106.12 C HETATM 5209 C4 SOG B 408 8.968 -24.629 99.531 1.00105.27 C HETATM 5210 C5 SOG B 408 10.220 -23.738 99.349 1.00103.39 C HETATM 5211 C6 SOG B 408 11.360 -24.153 100.280 1.00101.98 C HETATM 5212 C1' SOG B 408 11.287 -21.953 95.471 1.00 91.83 C HETATM 5213 C2' SOG B 408 12.662 -21.960 94.818 1.00 86.99 C HETATM 5214 C3' SOG B 408 13.800 -21.980 95.836 1.00 81.98 C HETATM 5215 C4' SOG B 408 15.129 -21.790 95.114 1.00 77.09 C HETATM 5216 C5' SOG B 408 16.188 -21.119 95.970 1.00 72.48 C HETATM 5217 C6' SOG B 408 17.090 -20.284 95.075 1.00 69.60 C HETATM 5218 C7' SOG B 408 18.497 -20.200 95.645 1.00 67.83 C HETATM 5219 C8' SOG B 408 19.223 -18.990 95.104 1.00 65.03 C HETATM 5220 S1 SOG B 408 10.566 -23.557 95.364 1.00 97.36 S HETATM 5221 O2 SOG B 408 7.708 -24.474 95.924 1.00103.94 O HETATM 5222 O3 SOG B 408 6.943 -25.549 98.497 1.00107.16 O HETATM 5223 O4 SOG B 408 8.328 -24.347 100.786 1.00104.50 O HETATM 5224 O5 SOG B 408 10.732 -23.757 97.998 1.00102.82 O HETATM 5225 O6 SOG B 408 10.939 -24.099 101.651 1.00101.97 O HETATM 5226 O HOH A 501 13.841 23.067 103.244 1.00 66.55 O HETATM 5227 O HOH A 502 36.974 -8.712 103.069 1.00 59.99 O HETATM 5228 O HOH A 503 24.652 -5.493 84.850 1.00 46.26 O HETATM 5229 O HOH A 504 11.851 17.208 113.833 1.00 54.67 O HETATM 5230 O HOH A 505 19.218 4.867 102.662 1.00 52.19 O HETATM 5231 O HOH A 506 49.216 -24.729 90.028 1.00 67.34 O HETATM 5232 O HOH A 507 13.205 0.768 90.494 1.00 54.09 O HETATM 5233 O HOH A 508 48.099 -27.001 89.052 1.00 60.89 O HETATM 5234 O HOH A 509 25.713 -5.067 103.011 1.00 37.59 O HETATM 5235 O HOH A 510 22.611 12.603 96.257 1.00 65.16 O HETATM 5236 O HOH A 511 20.376 -0.499 97.482 1.00 52.15 O HETATM 5237 O HOH A 512 18.578 8.896 94.472 1.00 60.74 O HETATM 5238 O HOH A 513 10.740 -5.887 90.814 1.00 52.41 O HETATM 5239 O HOH A 514 25.046 -9.004 95.246 1.00 40.97 O HETATM 5240 O HOH A 515 22.027 -8.626 95.294 1.00 40.34 O HETATM 5241 O HOH A 516 52.019 -25.679 89.041 1.00 74.56 O HETATM 5242 O HOH A 517 21.870 17.089 84.535 1.00 68.09 O HETATM 5243 O HOH A 518 9.777 20.082 120.873 1.00 68.72 O HETATM 5244 O HOH B 501 27.839 -31.380 73.341 1.00 45.97 O HETATM 5245 O HOH B 502 25.755 -23.857 68.768 1.00 46.11 O HETATM 5246 O HOH B 503 18.240 -29.920 75.901 1.00 32.51 O HETATM 5247 O HOH B 504 15.620 -31.240 94.810 1.00 62.51 O HETATM 5248 O HOH B 505 16.530 -40.501 80.102 1.00 71.17 O HETATM 5249 O HOH B 506 20.136 -26.796 87.217 1.00 46.21 O HETATM 5250 O HOH B 507 28.097 -15.345 57.507 1.00 61.75 O HETATM 5251 O HOH B 508 38.764 -7.141 71.785 1.00 57.33 O HETATM 5252 O HOH B 509 24.690 -47.562 81.240 1.00 48.15 O HETATM 5253 O HOH B 510 40.104 -9.471 68.008 1.00 55.80 O HETATM 5254 O HOH B 511 35.977 -11.124 61.893 1.00 77.54 O HETATM 5255 O HOH B 512 21.944 -25.463 82.756 1.00 42.44 O HETATM 5256 O HOH B 513 19.251 -34.806 83.353 1.00 47.06 O HETATM 5257 O HOH B 514 33.238 -2.595 61.727 1.00 51.72 O HETATM 5258 O HOH B 515 23.256 -30.063 87.208 1.00 48.88 O HETATM 5259 O HOH B 516 32.193 -16.201 59.110 1.00 51.82 O HETATM 5260 O HOH B 517 19.994 -26.364 84.527 1.00 37.13 O HETATM 5261 O HOH B 518 47.894 -16.358 64.815 1.00 69.38 O HETATM 5262 O HOH B 519 37.304 -17.786 59.059 1.00 74.97 O HETATM 5263 O HOH B 520 21.190 -43.790 85.438 1.00 54.68 O HETATM 5264 O HOH B 521 16.489 -35.487 101.172 1.00 70.07 O HETATM 5265 O HOH B 522 16.350 -43.010 81.145 1.00 64.45 O HETATM 5266 O HOH B 523 22.161 -36.693 86.405 1.00 73.07 O HETATM 5267 O HOH B 524 19.812 -13.371 57.273 1.00 73.89 O HETATM 5268 O HOH B 525 12.533 -39.378 72.374 1.00 52.69 O CONECT 753 1321 CONECT 1321 753 CONECT 3022 3650 CONECT 3650 3022 CONECT 4829 4830 4831 4833 4859 CONECT 4830 4829 4831 4860 4861 CONECT 4831 4829 4830 4832 4834 CONECT 4832 4831 4840 4862 4863 CONECT 4833 4829 4847 4848 CONECT 4834 4831 4835 4839 CONECT 4835 4834 4836 4864 CONECT 4836 4835 4837 4858 CONECT 4837 4836 4838 4865 CONECT 4838 4837 4839 4866 CONECT 4839 4834 4838 4867 CONECT 4840 4832 4841 CONECT 4841 4840 4842 4846 CONECT 4842 4841 4843 4856 CONECT 4843 4842 4844 CONECT 4844 4843 4845 4855 CONECT 4845 4844 4846 CONECT 4846 4841 4845 4868 CONECT 4847 4833 CONECT 4848 4833 4849 4869 CONECT 4849 4848 4850 4854 CONECT 4850 4849 4851 4870 CONECT 4851 4850 4852 4871 CONECT 4852 4851 4853 4857 CONECT 4853 4852 4854 4872 CONECT 4854 4849 4853 CONECT 4855 4844 4873 4874 4875 CONECT 4856 4842 4876 4877 4878 CONECT 4857 4852 CONECT 4858 4836 CONECT 4859 4829 CONECT 4860 4830 CONECT 4861 4830 CONECT 4862 4832 CONECT 4863 4832 CONECT 4864 4835 CONECT 4865 4837 CONECT 4866 4838 CONECT 4867 4839 CONECT 4868 4846 CONECT 4869 4848 CONECT 4870 4850 CONECT 4871 4851 CONECT 4872 4853 CONECT 4873 4855 CONECT 4874 4855 CONECT 4875 4855 CONECT 4876 4856 CONECT 4877 4856 CONECT 4878 4856 CONECT 4879 4880 CONECT 4880 4879 4881 CONECT 4881 4880 4882 CONECT 4882 4881 4883 CONECT 4883 4882 4884 CONECT 4884 4883 4885 CONECT 4885 4884 4886 CONECT 4886 4885 4887 CONECT 4887 4886 4888 CONECT 4888 4887 4889 CONECT 4889 4888 4890 CONECT 4890 4889 4891 CONECT 4891 4890 CONECT 4892 4893 4894 4895 4896 CONECT 4893 4892 CONECT 4894 4892 CONECT 4895 4892 CONECT 4896 4892 CONECT 4897 4898 4899 4900 4901 CONECT 4898 4897 CONECT 4899 4897 CONECT 4900 4897 CONECT 4901 4897 CONECT 4902 4903 4916 4920 CONECT 4903 4902 4904 4917 CONECT 4904 4903 4905 4918 CONECT 4905 4904 4906 4919 CONECT 4906 4905 4907 4920 CONECT 4907 4906 4921 CONECT 4908 4909 4916 CONECT 4909 4908 4910 CONECT 4910 4909 4911 CONECT 4911 4910 4912 CONECT 4912 4911 4913 CONECT 4913 4912 4914 CONECT 4914 4913 4915 CONECT 4915 4914 CONECT 4916 4902 4908 CONECT 4917 4903 CONECT 4918 4904 CONECT 4919 4905 CONECT 4920 4902 4906 CONECT 4921 4907 CONECT 4922 4923 4936 4940 CONECT 4923 4922 4924 4937 CONECT 4924 4923 4925 4938 CONECT 4925 4924 4926 4939 CONECT 4926 4925 4927 4940 CONECT 4927 4926 4941 CONECT 4928 4929 4936 CONECT 4929 4928 4930 CONECT 4930 4929 4931 CONECT 4931 4930 4932 CONECT 4932 4931 4933 CONECT 4933 4932 4934 CONECT 4934 4933 4935 CONECT 4935 4934 CONECT 4936 4922 4928 CONECT 4937 4923 CONECT 4938 4924 CONECT 4939 4925 CONECT 4940 4922 4926 CONECT 4941 4927 CONECT 4942 4943 4949 4953 CONECT 4943 4942 4944 4950 CONECT 4944 4943 4945 4951 CONECT 4945 4944 4946 4952 CONECT 4946 4945 4947 4953 CONECT 4947 4946 4954 CONECT 4948 4949 CONECT 4949 4942 4948 CONECT 4950 4943 CONECT 4951 4944 CONECT 4952 4945 CONECT 4953 4942 4946 CONECT 4954 4947 CONECT 4955 4956 4969 4973 CONECT 4956 4955 4957 4970 CONECT 4957 4956 4958 4971 CONECT 4958 4957 4959 4972 CONECT 4959 4958 4960 4973 CONECT 4960 4959 4974 CONECT 4961 4962 4969 CONECT 4962 4961 4963 CONECT 4963 4962 4964 CONECT 4964 4963 4965 CONECT 4965 4964 4966 CONECT 4966 4965 4967 CONECT 4967 4966 4968 CONECT 4968 4967 CONECT 4969 4955 4961 CONECT 4970 4956 CONECT 4971 4957 CONECT 4972 4958 CONECT 4973 4955 4959 CONECT 4974 4960 CONECT 4975 4976 4991 CONECT 4976 4975 CONECT 4977 4991 CONECT 4978 5003 5005 5007 5009 CONECT 4979 4982 4987 CONECT 4980 4981 4983 4984 CONECT 4981 4980 4982 CONECT 4982 4979 4981 4985 CONECT 4983 4980 4986 CONECT 4984 4980 CONECT 4985 4982 5003 CONECT 4986 4983 4989 CONECT 4987 4979 5014 CONECT 4988 4991 5005 CONECT 4989 4986 4992 CONECT 4990 5014 CONECT 4991 4975 4977 4988 CONECT 4992 4989 4994 CONECT 4993 4995 5001 CONECT 4994 4992 4996 CONECT 4995 4993 4997 CONECT 4996 4994 4998 CONECT 4997 4995 4999 CONECT 4998 4996 5000 CONECT 4999 4997 5002 CONECT 5000 4998 5001 CONECT 5001 4993 5000 CONECT 5002 4999 5004 CONECT 5003 4978 4985 CONECT 5004 5002 5006 CONECT 5005 4978 4988 CONECT 5006 5004 5008 CONECT 5007 4978 CONECT 5008 5006 CONECT 5009 4978 CONECT 5010 5011 5022 CONECT 5011 5010 5012 CONECT 5012 5011 5013 CONECT 5013 5012 5023 CONECT 5014 4987 4990 5015 CONECT 5015 5014 5016 CONECT 5016 5015 5017 CONECT 5017 5016 5018 CONECT 5018 5017 5019 CONECT 5019 5018 5020 CONECT 5020 5019 5021 CONECT 5021 5020 5022 CONECT 5022 5010 5021 CONECT 5023 5013 5025 CONECT 5024 5025 CONECT 5025 5023 5024 CONECT 5026 5027 5042 CONECT 5027 5026 CONECT 5028 5042 CONECT 5029 5054 5056 5058 5060 CONECT 5030 5033 5038 CONECT 5031 5032 5034 5035 CONECT 5032 5031 5033 CONECT 5033 5030 5032 5036 CONECT 5034 5031 5037 CONECT 5035 5031 CONECT 5036 5033 5054 CONECT 5037 5034 5040 CONECT 5038 5030 5065 CONECT 5039 5042 5056 CONECT 5040 5037 5043 CONECT 5041 5065 CONECT 5042 5026 5028 5039 CONECT 5043 5040 5045 CONECT 5044 5046 5052 CONECT 5045 5043 5047 CONECT 5046 5044 5048 CONECT 5047 5045 5049 CONECT 5048 5046 5050 CONECT 5049 5047 5051 CONECT 5050 5048 5053 CONECT 5051 5049 5052 CONECT 5052 5044 5051 CONECT 5053 5050 5055 CONECT 5054 5029 5036 CONECT 5055 5053 5057 CONECT 5056 5029 5039 CONECT 5057 5055 5059 CONECT 5058 5029 CONECT 5059 5057 CONECT 5060 5029 CONECT 5061 5062 5073 CONECT 5062 5061 5063 CONECT 5063 5062 5064 CONECT 5064 5063 5074 CONECT 5065 5038 5041 5066 CONECT 5066 5065 5067 CONECT 5067 5066 5068 CONECT 5068 5067 5069 CONECT 5069 5068 5070 CONECT 5070 5069 5071 CONECT 5071 5070 5072 CONECT 5072 5071 5073 CONECT 5073 5061 5072 CONECT 5074 5064 5076 CONECT 5075 5076 CONECT 5076 5074 5075 CONECT 5077 5078 5079 5081 5107 CONECT 5078 5077 5079 5108 5109 CONECT 5079 5077 5078 5080 5082 CONECT 5080 5079 5088 5110 5111 CONECT 5081 5077 5095 5096 CONECT 5082 5079 5083 5087 CONECT 5083 5082 5084 5112 CONECT 5084 5083 5085 5106 CONECT 5085 5084 5086 5113 CONECT 5086 5085 5087 5114 CONECT 5087 5082 5086 5115 CONECT 5088 5080 5089 CONECT 5089 5088 5090 5094 CONECT 5090 5089 5091 5104 CONECT 5091 5090 5092 CONECT 5092 5091 5093 5103 CONECT 5093 5092 5094 CONECT 5094 5089 5093 5116 CONECT 5095 5081 CONECT 5096 5081 5097 5117 CONECT 5097 5096 5098 5102 CONECT 5098 5097 5099 5118 CONECT 5099 5098 5100 5119 CONECT 5100 5099 5101 5105 CONECT 5101 5100 5102 5120 CONECT 5102 5097 5101 CONECT 5103 5092 5121 5122 5123 CONECT 5104 5090 5124 5125 5126 CONECT 5105 5100 CONECT 5106 5084 CONECT 5107 5077 CONECT 5108 5078 CONECT 5109 5078 CONECT 5110 5080 CONECT 5111 5080 CONECT 5112 5083 CONECT 5113 5085 CONECT 5114 5086 CONECT 5115 5087 CONECT 5116 5094 CONECT 5117 5096 CONECT 5118 5098 CONECT 5119 5099 CONECT 5120 5101 CONECT 5121 5103 CONECT 5122 5103 CONECT 5123 5103 CONECT 5124 5104 CONECT 5125 5104 CONECT 5126 5104 CONECT 5127 5128 5129 5130 5131 CONECT 5128 5127 CONECT 5129 5127 CONECT 5130 5127 CONECT 5131 5127 CONECT 5132 5133 5134 5135 5136 CONECT 5133 5132 CONECT 5134 5132 CONECT 5135 5132 CONECT 5136 5132 CONECT 5137 5138 5151 5155 CONECT 5138 5137 5139 5152 CONECT 5139 5138 5140 5153 CONECT 5140 5139 5141 5154 CONECT 5141 5140 5142 5155 CONECT 5142 5141 5156 CONECT 5143 5144 5151 CONECT 5144 5143 5145 CONECT 5145 5144 5146 CONECT 5146 5145 5147 CONECT 5147 5146 5148 CONECT 5148 5147 5149 CONECT 5149 5148 5150 CONECT 5150 5149 CONECT 5151 5137 5143 CONECT 5152 5138 CONECT 5153 5139 CONECT 5154 5140 CONECT 5155 5137 5141 CONECT 5156 5142 CONECT 5157 5158 5164 5168 CONECT 5158 5157 5159 5165 CONECT 5159 5158 5160 5166 CONECT 5160 5159 5161 5167 CONECT 5161 5160 5162 5168 CONECT 5162 5161 5169 CONECT 5163 5164 CONECT 5164 5157 5163 CONECT 5165 5158 CONECT 5166 5159 CONECT 5167 5160 CONECT 5168 5157 5161 CONECT 5169 5162 CONECT 5170 5171 5184 5188 CONECT 5171 5170 5172 5185 CONECT 5172 5171 5173 5186 CONECT 5173 5172 5174 5187 CONECT 5174 5173 5175 5188 CONECT 5175 5174 5189 CONECT 5176 5177 5184 CONECT 5177 5176 5178 CONECT 5178 5177 5179 CONECT 5179 5178 5180 CONECT 5180 5179 5181 CONECT 5181 5180 5182 CONECT 5182 5181 5183 CONECT 5183 5182 CONECT 5184 5170 5176 CONECT 5185 5171 CONECT 5186 5172 CONECT 5187 5173 CONECT 5188 5170 5174 CONECT 5189 5175 CONECT 5190 5191 5200 5204 CONECT 5191 5190 5192 5201 CONECT 5192 5191 5193 5202 CONECT 5193 5192 5194 5203 CONECT 5194 5193 5195 5204 CONECT 5195 5194 5205 CONECT 5196 5197 5200 CONECT 5197 5196 5198 CONECT 5198 5197 5199 CONECT 5199 5198 CONECT 5200 5190 5196 CONECT 5201 5191 CONECT 5202 5192 CONECT 5203 5193 CONECT 5204 5190 5194 CONECT 5205 5195 CONECT 5206 5207 5220 5224 CONECT 5207 5206 5208 5221 CONECT 5208 5207 5209 5222 CONECT 5209 5208 5210 5223 CONECT 5210 5209 5211 5224 CONECT 5211 5210 5225 CONECT 5212 5213 5220 CONECT 5213 5212 5214 CONECT 5214 5213 5215 CONECT 5215 5214 5216 CONECT 5216 5215 5217 CONECT 5217 5216 5218 CONECT 5218 5217 5219 CONECT 5219 5218 CONECT 5220 5206 5212 CONECT 5221 5207 CONECT 5222 5208 CONECT 5223 5209 CONECT 5224 5206 5210 CONECT 5225 5211 MASTER 356 0 18 24 4 0 0 6 5226 2 401 52 END