HEADER MEMBRANE PROTEIN 11-DEC-19 6TOD TITLE CRYSTAL STRUCTURE OF THE OREXIN-1 RECEPTOR IN COMPLEX WITH EMPA 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: EMPA BOUND IN 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 6TOD 1 COMPND REMARK HETNAM SITE REVDAT 3 11-MAR-20 6TOD 1 JRNL REVDAT 2 29-JAN-20 6TOD 1 JRNL REVDAT 1 01-JAN-20 6TOD 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. 2.11 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) : 2.11 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.62 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 61.3 REMARK 3 NUMBER OF REFLECTIONS : 57581 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) : 0.189 REMARK 3 R VALUE (WORKING SET) : 0.188 REMARK 3 FREE R VALUE : 0.208 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 2826 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) : 2.11 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.28 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 5.98 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) : 0.2331 REMARK 3 BIN FREE R VALUE : 0.2591 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 48 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 : 4876 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 862 REMARK 3 SOLVENT ATOMS : 211 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.10 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.77150 REMARK 3 B22 (A**2) : -2.96840 REMARK 3 B33 (A**2) : 2.19690 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 1.97620 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.290 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.193 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.163 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.197 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.166 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 : 0.923 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.919 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 5963 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 7979 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 2254 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL REMARK 3 GENERAL PLANES : 821 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 5963 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 771 ; 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 : 6676 ; 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) : 2.78 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.97 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: {A|45 - 378} REMARK 3 ORIGIN FOR THE GROUP (A): 16.0291 3.4247 23.8437 REMARK 3 T TENSOR REMARK 3 T11: -0.081 T22: -0.186 REMARK 3 T33: -0.1452 T12: -0.0395 REMARK 3 T13: 0.0072 T23: -0.0121 REMARK 3 L TENSOR REMARK 3 L11: 1.4259 L22: 1.9266 REMARK 3 L33: 1.455 L12: 0.1973 REMARK 3 L13: -0.5058 L23: -0.2458 REMARK 3 S TENSOR REMARK 3 S11: -0.0882 S12: -0.3148 S13: 0.2134 REMARK 3 S21: -0.3148 S22: 0.0428 S23: -0.1168 REMARK 3 S31: 0.2134 S32: -0.1168 S33: 0.0455 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: {B|29 - 383} REMARK 3 ORIGIN FOR THE GROUP (A): 26.9653 30.1577 40.3921 REMARK 3 T TENSOR REMARK 3 T11: -0.1505 T22: -0.1231 REMARK 3 T33: -0.0739 T12: -0.0005 REMARK 3 T13: 0.0201 T23: -0.0766 REMARK 3 L TENSOR REMARK 3 L11: 1.7308 L22: 1.251 REMARK 3 L33: 0.6012 L12: -0.031 REMARK 3 L13: -0.0918 L23: 0.0851 REMARK 3 S TENSOR REMARK 3 S11: 0.027 S12: 0.0321 S13: -0.0593 REMARK 3 S21: 0.0321 S22: 0.0077 S23: 0.05 REMARK 3 S31: -0.0593 S32: 0.05 S33: -0.0348 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 6TOD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-DEC-19. REMARK 100 THE DEPOSITION ID IS D_1292105799. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 08-JAN-13 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) : 0.9686 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 : 57581 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.110 REMARK 200 RESOLUTION RANGE LOW (A) : 30.620 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 61.3 REMARK 200 DATA REDUNDANCY : 3.300 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.11 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28 REMARK 200 COMPLETENESS FOR SHELL (%) : 6.0 REMARK 200 DATA REDUNDANCY IN SHELL : 3.60 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 (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRISODIUM CITRATE 50MM SODIUM REMARK 280 CHLORIDE 50MM LITHIUM SULPHATE 15-34% PEG400, PH 6.3, VAPOR REMARK 280 DIFFUSION, TEMPERATURE 284K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z+1/2 REMARK 290 4555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 19.78699 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 79.44550 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 90.71505 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 19.78699 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 79.44550 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 90.71505 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 SER A 27 REMARK 465 GLU A 28 REMARK 465 ASP A 29 REMARK 465 GLU A 30 REMARK 465 PHE A 31 REMARK 465 LEU A 32 REMARK 465 ARG A 33 REMARK 465 TYR A 34 REMARK 465 LEU A 35 REMARK 465 TRP A 36 REMARK 465 ARG A 37 REMARK 465 ASP A 38 REMARK 465 TYR A 39 REMARK 465 LEU A 40 REMARK 465 TYR A 41 REMARK 465 PRO A 42 REMARK 465 LYS A 43 REMARK 465 GLN A 44 REMARK 465 ALA A 285 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 LEU B 189 REMARK 465 PRO B 190 REMARK 465 GLU B 191 REMARK 465 LEU B 192 REMARK 465 ALA B 193 REMARK 465 ALA B 194 REMARK 465 ARG B 195 REMARK 465 THR B 196 REMARK 465 ARG B 197 REMARK 465 ALA B 198 REMARK 465 GLN B 246 REMARK 465 ILE B 247 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 224 -68.69 -136.51 REMARK 500 LEU A 377 115.34 -171.57 REMARK 500 TYR B 39 -62.82 -137.44 REMARK 500 GLN B 44 -67.67 -135.22 REMARK 500 TYR B 224 -69.04 -137.26 REMARK 500 THR B 250 -25.81 -146.33 REMARK 500 ARG B 328 59.69 -95.55 REMARK 500 TRP B 375 -58.26 -131.26 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 A 408 REMARK 610 SOG A 415 REMARK 610 SOG A 419 REMARK 610 SOG A 420 REMARK 610 SOG A 421 REMARK 610 SOG A 422 REMARK 610 SOG A 423 REMARK 610 SOG A 424 REMARK 610 SOG A 425 REMARK 610 SOG A 426 REMARK 610 SOG A 427 REMARK 610 SOG A 428 REMARK 610 SOG B 413 REMARK 610 SOG B 415 REMARK 610 SOG B 416 REMARK 610 SOG B 417 REMARK 610 SOG B 418 REMARK 610 SOG B 419 REMARK 610 SOG B 420 REMARK 610 SOG B 421 REMARK 610 SOG B 422 REMARK 610 SOG B 423 REMARK 610 SOG B 424 REMARK 610 SOG B 425 REMARK 610 SOG B 426 REMARK 610 SOG B 427 REMARK 610 SOG B 428 REMARK 610 SOG B 429 REMARK 610 SOG B 430 REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A 430 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 92 OD1 REMARK 620 2 TYR A 311 OH 119.4 REMARK 620 3 ASN A 350 OD1 125.7 114.8 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA B 432 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 92 OD1 REMARK 620 2 TYR B 311 OH 122.5 REMARK 620 3 ASN B 350 OD1 124.4 104.8 REMARK 620 N 1 2 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6TO7 RELATED DB: PDB DBREF 6TOD A 28 380 UNP O43613 OX1R_HUMAN 28 380 DBREF 6TOD B 28 380 UNP O43613 OX1R_HUMAN 28 380 SEQADV 6TOD ALA A 25 UNP O43613 EXPRESSION TAG SEQADV 6TOD ALA A 26 UNP O43613 EXPRESSION TAG SEQADV 6TOD SER A 27 UNP O43613 EXPRESSION TAG SEQADV 6TOD ALA A 46 UNP O43613 GLU 46 ENGINEERED MUTATION SEQADV 6TOD LEU A 85 UNP O43613 ILE 85 ENGINEERED MUTATION SEQADV 6TOD ALA A 95 UNP O43613 VAL 95 ENGINEERED MUTATION SEQADV 6TOD THR A 127 UNP O43613 ALA 127 ENGINEERED MUTATION SEQADV 6TOD LEU A 162 UNP O43613 ARG 162 ENGINEERED MUTATION SEQADV 6TOD ALA A 194 UNP O43613 ASN 194 ENGINEERED MUTATION SEQADV 6TOD ALA A 198 UNP O43613 LEU 198 ENGINEERED MUTATION SEQADV 6TOD ALA A 211 UNP O43613 TYR 211 ENGINEERED MUTATION SEQADV 6TOD A UNP O43613 ALA 253 DELETION SEQADV 6TOD A UNP O43613 LEU 254 DELETION SEQADV 6TOD A UNP O43613 VAL 255 DELETION SEQADV 6TOD A UNP O43613 ARG 256 DELETION SEQADV 6TOD A UNP O43613 ASN 257 DELETION SEQADV 6TOD A UNP O43613 TRP 258 DELETION SEQADV 6TOD A UNP O43613 LYS 259 DELETION SEQADV 6TOD A UNP O43613 ARG 260 DELETION SEQADV 6TOD A UNP O43613 PRO 261 DELETION SEQADV 6TOD A UNP O43613 SER 262 DELETION SEQADV 6TOD A UNP O43613 ASP 263 DELETION SEQADV 6TOD A UNP O43613 GLN 264 DELETION SEQADV 6TOD A UNP O43613 LEU 265 DELETION SEQADV 6TOD A UNP O43613 GLY 266 DELETION SEQADV 6TOD A UNP O43613 ASP 267 DELETION SEQADV 6TOD A UNP O43613 LEU 268 DELETION SEQADV 6TOD A UNP O43613 GLU 269 DELETION SEQADV 6TOD A UNP O43613 GLN 270 DELETION SEQADV 6TOD A UNP O43613 GLY 271 DELETION SEQADV 6TOD A UNP O43613 LEU 272 DELETION SEQADV 6TOD A UNP O43613 SER 273 DELETION SEQADV 6TOD A UNP O43613 GLY 274 DELETION SEQADV 6TOD A UNP O43613 GLU 275 DELETION SEQADV 6TOD A UNP O43613 PRO 276 DELETION SEQADV 6TOD A UNP O43613 GLN 277 DELETION SEQADV 6TOD A UNP O43613 PRO 278 DELETION SEQADV 6TOD A UNP O43613 ARG 279 DELETION SEQADV 6TOD A UNP O43613 ALA 280 DELETION SEQADV 6TOD A UNP O43613 ARG 281 DELETION SEQADV 6TOD A UNP O43613 ALA 282 DELETION SEQADV 6TOD A UNP O43613 PHE 283 DELETION SEQADV 6TOD A UNP O43613 LEU 284 DELETION SEQADV 6TOD VAL A 304 UNP O43613 LEU 304 ENGINEERED MUTATION SEQADV 6TOD ALA A 339 UNP O43613 CYS 339 ENGINEERED MUTATION SEQADV 6TOD TRP A 375 UNP O43613 CYS 375 ENGINEERED MUTATION SEQADV 6TOD TRP A 376 UNP O43613 CYS 376 ENGINEERED MUTATION SEQADV 6TOD ALA A 381 UNP O43613 EXPRESSION TAG SEQADV 6TOD ALA A 382 UNP O43613 EXPRESSION TAG SEQADV 6TOD ALA A 383 UNP O43613 EXPRESSION TAG SEQADV 6TOD HIS A 384 UNP O43613 EXPRESSION TAG SEQADV 6TOD HIS A 385 UNP O43613 EXPRESSION TAG SEQADV 6TOD HIS A 386 UNP O43613 EXPRESSION TAG SEQADV 6TOD HIS A 387 UNP O43613 EXPRESSION TAG SEQADV 6TOD HIS A 388 UNP O43613 EXPRESSION TAG SEQADV 6TOD HIS A 389 UNP O43613 EXPRESSION TAG SEQADV 6TOD HIS A 390 UNP O43613 EXPRESSION TAG SEQADV 6TOD HIS A 391 UNP O43613 EXPRESSION TAG SEQADV 6TOD HIS A 392 UNP O43613 EXPRESSION TAG SEQADV 6TOD ALA B 25 UNP O43613 EXPRESSION TAG SEQADV 6TOD ALA B 26 UNP O43613 EXPRESSION TAG SEQADV 6TOD SER B 27 UNP O43613 EXPRESSION TAG SEQADV 6TOD ALA B 46 UNP O43613 GLU 46 ENGINEERED MUTATION SEQADV 6TOD LEU B 85 UNP O43613 ILE 85 ENGINEERED MUTATION SEQADV 6TOD ALA B 95 UNP O43613 VAL 95 ENGINEERED MUTATION SEQADV 6TOD THR B 127 UNP O43613 ALA 127 ENGINEERED MUTATION SEQADV 6TOD LEU B 162 UNP O43613 ARG 162 ENGINEERED MUTATION SEQADV 6TOD ALA B 194 UNP O43613 ASN 194 ENGINEERED MUTATION SEQADV 6TOD ALA B 198 UNP O43613 LEU 198 ENGINEERED MUTATION SEQADV 6TOD ALA B 211 UNP O43613 TYR 211 ENGINEERED MUTATION SEQADV 6TOD B UNP O43613 ALA 253 DELETION SEQADV 6TOD B UNP O43613 LEU 254 DELETION SEQADV 6TOD B UNP O43613 VAL 255 DELETION SEQADV 6TOD B UNP O43613 ARG 256 DELETION SEQADV 6TOD B UNP O43613 ASN 257 DELETION SEQADV 6TOD B UNP O43613 TRP 258 DELETION SEQADV 6TOD B UNP O43613 LYS 259 DELETION SEQADV 6TOD B UNP O43613 ARG 260 DELETION SEQADV 6TOD B UNP O43613 PRO 261 DELETION SEQADV 6TOD B UNP O43613 SER 262 DELETION SEQADV 6TOD B UNP O43613 ASP 263 DELETION SEQADV 6TOD B UNP O43613 GLN 264 DELETION SEQADV 6TOD B UNP O43613 LEU 265 DELETION SEQADV 6TOD B UNP O43613 GLY 266 DELETION SEQADV 6TOD B UNP O43613 ASP 267 DELETION SEQADV 6TOD B UNP O43613 LEU 268 DELETION SEQADV 6TOD B UNP O43613 GLU 269 DELETION SEQADV 6TOD B UNP O43613 GLN 270 DELETION SEQADV 6TOD B UNP O43613 GLY 271 DELETION SEQADV 6TOD B UNP O43613 LEU 272 DELETION SEQADV 6TOD B UNP O43613 SER 273 DELETION SEQADV 6TOD B UNP O43613 GLY 274 DELETION SEQADV 6TOD B UNP O43613 GLU 275 DELETION SEQADV 6TOD B UNP O43613 PRO 276 DELETION SEQADV 6TOD B UNP O43613 GLN 277 DELETION SEQADV 6TOD B UNP O43613 PRO 278 DELETION SEQADV 6TOD B UNP O43613 ARG 279 DELETION SEQADV 6TOD B UNP O43613 ALA 280 DELETION SEQADV 6TOD B UNP O43613 ARG 281 DELETION SEQADV 6TOD B UNP O43613 ALA 282 DELETION SEQADV 6TOD B UNP O43613 PHE 283 DELETION SEQADV 6TOD B UNP O43613 LEU 284 DELETION SEQADV 6TOD VAL B 304 UNP O43613 LEU 304 ENGINEERED MUTATION SEQADV 6TOD ALA B 339 UNP O43613 CYS 339 ENGINEERED MUTATION SEQADV 6TOD TRP B 375 UNP O43613 CYS 375 ENGINEERED MUTATION SEQADV 6TOD TRP B 376 UNP O43613 CYS 376 ENGINEERED MUTATION SEQADV 6TOD ALA B 381 UNP O43613 EXPRESSION TAG SEQADV 6TOD ALA B 382 UNP O43613 EXPRESSION TAG SEQADV 6TOD ALA B 383 UNP O43613 EXPRESSION TAG SEQADV 6TOD HIS B 384 UNP O43613 EXPRESSION TAG SEQADV 6TOD HIS B 385 UNP O43613 EXPRESSION TAG SEQADV 6TOD HIS B 386 UNP O43613 EXPRESSION TAG SEQADV 6TOD HIS B 387 UNP O43613 EXPRESSION TAG SEQADV 6TOD HIS B 388 UNP O43613 EXPRESSION TAG SEQADV 6TOD HIS B 389 UNP O43613 EXPRESSION TAG SEQADV 6TOD HIS B 390 UNP O43613 EXPRESSION TAG SEQADV 6TOD HIS B 391 UNP O43613 EXPRESSION TAG SEQADV 6TOD 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 THR 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 THR 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 7MA A 401 58 HET SO4 A 402 5 HET PG4 A 403 13 HET PG4 A 404 13 HET PG4 A 405 13 HET CIT A 406 13 HET SOG A 407 17 HET SOG A 408 16 HET SOG A 409 20 HET SOG A 410 20 HET SOG A 411 20 HET SOG A 412 20 HET SOG A 413 20 HET SOG A 414 20 HET SOG A 415 14 HET SOG A 416 20 HET SOG A 417 20 HET SOG A 418 20 HET SOG A 419 7 HET SOG A 420 7 HET SOG A 421 7 HET SOG A 422 7 HET SOG A 423 7 HET SOG A 424 7 HET SOG A 425 7 HET SOG A 426 7 HET SOG A 427 7 HET SOG A 428 7 HET PGW A 429 51 HET NA A 430 1 HET 7MA B 401 58 HET SO4 B 402 5 HET SO4 B 403 5 HET PG4 B 404 13 HET PG4 B 405 13 HET SOG B 406 20 HET SOG B 407 20 HET SOG B 408 20 HET SOG B 409 20 HET SOG B 410 20 HET SOG B 411 20 HET SOG B 412 20 HET SOG B 413 16 HET SOG B 414 20 HET SOG B 415 6 HET SOG B 416 10 HET SOG B 417 9 HET SOG B 418 8 HET SOG B 419 9 HET SOG B 420 5 HET SOG B 421 16 HET SOG B 422 8 HET SOG B 423 9 HET SOG B 424 6 HET SOG B 425 7 HET SOG B 426 7 HET SOG B 427 7 HET SOG B 428 7 HET SOG B 429 7 HET SOG B 430 7 HET PGW B 431 51 HET NA B 432 1 HETNAM 7MA N-ETHYL-2-[(6-METHOXYPYRIDIN-3-YL)-(2-METHYLPHENYL) HETNAM 2 7MA SULFONYL-AMINO]-N-(PYRIDIN-3-YLMETHYL)ETHANAMIDE HETNAM SO4 SULFATE ION HETNAM PG4 TETRAETHYLENE GLYCOL HETNAM CIT CITRIC ACID 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 HETNAM NA SODIUM ION 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 7MA 2(C23 H26 N4 O4 S) FORMUL 4 SO4 3(O4 S 2-) FORMUL 5 PG4 5(C8 H18 O5) FORMUL 8 CIT C6 H8 O7 FORMUL 9 SOG 47(C14 H28 O5 S) FORMUL 31 PGW 2(C40 H77 O10 P) FORMUL 32 NA 2(NA 1+) FORMUL 65 HOH *211(H2 O) HELIX 1 AA1 TYR A 45 ASN A 74 1 30 HELIX 2 AA2 HIS A 75 ARG A 78 5 4 HELIX 3 AA3 THR A 79 GLU A 110 1 32 HELIX 4 AA4 PHE A 114 HIS A 150 1 37 HELIX 5 AA5 THR A 157 MET A 176 1 20 HELIX 6 AA6 MET A 176 VAL A 182 1 7 HELIX 7 AA7 LEU A 189 ALA A 193 5 5 HELIX 8 AA8 LEU A 210 TYR A 224 1 15 HELIX 9 AA9 TYR A 224 TRP A 243 1 20 HELIX 10 AB1 THR A 251 SER A 252 5 2 HELIX 11 AB2 GLU A 286 GLU A 286 5 1 HELIX 12 AB3 VAL A 287 VAL A 323 1 37 HELIX 13 AB4 GLN A 329 SER A 331 5 3 HELIX 14 AB5 ASP A 332 SER A 362 1 31 HELIX 15 AB6 SER A 362 TRP A 375 1 14 HELIX 16 AB7 GLU B 30 TYR B 39 1 10 HELIX 17 AB8 TYR B 39 GLN B 44 1 6 HELIX 18 AB9 GLN B 44 ARG B 73 1 30 HELIX 19 AC1 ASN B 74 ARG B 78 5 5 HELIX 20 AC2 THR B 79 GLU B 110 1 32 HELIX 21 AC3 PHE B 114 HIS B 150 1 37 HELIX 22 AC4 THR B 157 MET B 176 1 20 HELIX 23 AC5 MET B 176 VAL B 182 1 7 HELIX 24 AC6 LEU B 210 TYR B 224 1 15 HELIX 25 AC7 TYR B 224 TRP B 243 1 20 HELIX 26 AC8 SER B 252 VAL B 323 1 40 HELIX 27 AC9 ASP B 332 SER B 362 1 31 HELIX 28 AD1 SER B 362 TRP B 375 1 14 HELIX 29 AD2 TRP B 375 ALA B 383 1 9 SHEET 1 AA1 2 MET A 183 SER A 187 0 SHEET 2 AA1 2 SER A 200 GLU A 204 -1 O VAL A 201 N SER A 186 SHEET 1 AA2 2 MET B 183 SER B 186 0 SHEET 2 AA2 2 VAL B 201 GLU B 204 -1 O VAL B 201 N SER B 186 SSBOND 1 CYS A 119 CYS A 202 1555 1555 2.06 SSBOND 2 CYS B 119 CYS B 202 1555 1555 2.05 LINK OD1 ASP A 92 NA NA A 430 1555 1555 2.87 LINK OH TYR A 311 NA NA A 430 1555 1555 2.78 LINK OD1 ASN A 350 NA NA A 430 1555 1555 2.77 LINK OD1 ASP B 92 NA NA B 432 1555 1555 2.63 LINK OH TYR B 311 NA NA B 432 1555 1555 2.84 LINK OD1 ASN B 350 NA NA B 432 1555 1555 3.05 CRYST1 57.907 158.891 182.354 90.00 95.77 90.00 I 1 2 1 8 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 0.017269 0.000000 0.001745 0.00000 SCALE2 0.000000 0.006294 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005512 0.00000 ATOM 1 N TYR A 45 -3.185 -16.030 26.987 1.00 90.92 N ANISOU 1 N TYR A 45 11504 9892 13151 -2951 127 -414 N ATOM 2 CA TYR A 45 -2.518 -14.806 26.532 1.00 90.67 C ANISOU 2 CA TYR A 45 11482 10003 12967 -2783 28 -424 C ATOM 3 C TYR A 45 -0.975 -14.866 26.701 1.00 91.06 C ANISOU 3 C TYR A 45 11734 9951 12914 -2603 126 -408 C ATOM 4 O TYR A 45 -0.263 -14.062 26.093 1.00 89.97 O ANISOU 4 O TYR A 45 11651 9889 12645 -2492 51 -447 O ATOM 5 CB TYR A 45 -3.144 -13.562 27.205 1.00 93.03 C ANISOU 5 CB TYR A 45 11561 10509 13277 -2685 -9 -319 C ATOM 6 CG TYR A 45 -2.515 -12.237 26.821 1.00 96.61 C ANISOU 6 CG TYR A 45 12017 11105 13587 -2516 -104 -321 C ATOM 7 CD1 TYR A 45 -2.716 -11.685 25.557 1.00 98.94 C ANISOU 7 CD1 TYR A 45 12300 11493 13800 -2565 -284 -417 C ATOM 8 CD2 TYR A 45 -1.721 -11.533 27.723 1.00 98.13 C ANISOU 8 CD2 TYR A 45 12230 11334 13719 -2314 -16 -225 C ATOM 9 CE1 TYR A 45 -2.125 -10.473 25.193 1.00100.79 C ANISOU 9 CE1 TYR A 45 12548 11844 13903 -2412 -361 -411 C ATOM 10 CE2 TYR A 45 -1.133 -10.316 27.376 1.00 99.62 C ANISOU 10 CE2 TYR A 45 12426 11639 13785 -2169 -95 -228 C ATOM 11 CZ TYR A 45 -1.337 -9.788 26.109 1.00109.16 C ANISOU 11 CZ TYR A 45 13626 12929 14920 -2216 -261 -318 C ATOM 12 OH TYR A 45 -0.763 -8.582 25.776 1.00111.35 O ANISOU 12 OH TYR A 45 13916 13312 15079 -2075 -329 -311 O ATOM 13 N ALA A 46 -0.471 -15.849 27.485 1.00 85.51 N ANISOU 13 N ALA A 46 11139 9075 12277 -2578 294 -346 N ATOM 14 CA ALA A 46 0.956 -16.080 27.724 1.00 84.16 C ANISOU 14 CA ALA A 46 11144 8792 12039 -2413 397 -315 C ATOM 15 C ALA A 46 1.699 -16.487 26.442 1.00 86.51 C ANISOU 15 C ALA A 46 11625 8989 12256 -2433 356 -459 C ATOM 16 O ALA A 46 2.817 -16.013 26.241 1.00 85.83 O ANISOU 16 O ALA A 46 11622 8922 12067 -2273 365 -457 O ATOM 17 CB ALA A 46 1.155 -17.128 28.808 1.00 84.71 C ANISOU 17 CB ALA A 46 11281 8692 12212 -2404 573 -212 C ATOM 18 N TRP A 47 1.077 -17.335 25.567 1.00 82.00 N ANISOU 18 N TRP A 47 11113 8317 11727 -2636 312 -589 N ATOM 19 CA TRP A 47 1.674 -17.755 24.287 1.00 81.24 C ANISOU 19 CA TRP A 47 11202 8122 11543 -2678 277 -746 C ATOM 20 C TRP A 47 1.879 -16.538 23.385 1.00 77.11 C ANISOU 20 C TRP A 47 10650 7788 10862 -2610 125 -801 C ATOM 21 O TRP A 47 2.909 -16.443 22.719 1.00 75.89 O ANISOU 21 O TRP A 47 10643 7590 10600 -2516 144 -862 O ATOM 22 CB TRP A 47 0.832 -18.830 23.542 1.00 81.64 C ANISOU 22 CB TRP A 47 11315 8043 11661 -2932 243 -885 C ATOM 23 CG TRP A 47 1.379 -19.152 22.169 1.00 84.14 C ANISOU 23 CG TRP A 47 11827 8281 11861 -2983 196 -1061 C ATOM 24 CD1 TRP A 47 2.375 -20.039 21.877 1.00 87.43 C ANISOU 24 CD1 TRP A 47 12469 8481 12269 -2941 329 -1126 C ATOM 25 CD2 TRP A 47 1.076 -18.470 20.932 1.00 84.52 C ANISOU 25 CD2 TRP A 47 11867 8478 11767 -3054 11 -1181 C ATOM 26 NE1 TRP A 47 2.682 -19.986 20.532 1.00 87.33 N ANISOU 26 NE1 TRP A 47 12595 8468 12116 -2992 250 -1291 N ATOM 27 CE2 TRP A 47 1.910 -19.023 19.932 1.00 88.85 C ANISOU 27 CE2 TRP A 47 12654 8889 12216 -3062 49 -1323 C ATOM 28 CE3 TRP A 47 0.178 -17.446 20.571 1.00 85.96 C ANISOU 28 CE3 TRP A 47 11868 8897 11898 -3105 -182 -1174 C ATOM 29 CZ2 TRP A 47 1.864 -18.596 18.595 1.00 88.23 C ANISOU 29 CZ2 TRP A 47 12647 8906 11972 -3130 -98 -1462 C ATOM 30 CZ3 TRP A 47 0.147 -17.011 19.252 1.00 87.48 C ANISOU 30 CZ3 TRP A 47 12122 9184 11931 -3163 -338 -1299 C ATOM 31 CH2 TRP A 47 0.977 -17.586 18.280 1.00 88.16 C ANISOU 31 CH2 TRP A 47 12458 9135 11905 -3180 -297 -1442 C ATOM 32 N VAL A 48 0.872 -15.643 23.339 1.00 68.65 N ANISOU 32 N VAL A 48 9385 6915 9783 -2661 -17 -778 N ATOM 33 CA VAL A 48 0.857 -14.418 22.540 1.00 66.64 C ANISOU 33 CA VAL A 48 9076 6852 9393 -2604 -173 -809 C ATOM 34 C VAL A 48 2.006 -13.503 23.000 1.00 67.35 C ANISOU 34 C VAL A 48 9188 6998 9403 -2365 -109 -718 C ATOM 35 O VAL A 48 2.732 -12.976 22.155 1.00 66.73 O ANISOU 35 O VAL A 48 9206 6956 9193 -2291 -154 -775 O ATOM 36 CB VAL A 48 -0.536 -13.719 22.592 1.00 70.30 C ANISOU 36 CB VAL A 48 9303 7503 9906 -2695 -318 -773 C ATOM 37 CG1 VAL A 48 -0.581 -12.479 21.704 1.00 70.09 C ANISOU 37 CG1 VAL A 48 9225 7664 9741 -2634 -485 -795 C ATOM 38 CG2 VAL A 48 -1.657 -14.683 22.206 1.00 70.17 C ANISOU 38 CG2 VAL A 48 9247 7428 9985 -2945 -380 -859 C ATOM 39 N LEU A 49 2.202 -13.384 24.338 1.00 60.57 N ANISOU 39 N LEU A 49 8252 6139 8624 -2254 3 -580 N ATOM 40 CA LEU A 49 3.248 -12.598 24.993 1.00 57.99 C ANISOU 40 CA LEU A 49 7929 5862 8241 -2041 70 -483 C ATOM 41 C LEU A 49 4.648 -13.176 24.736 1.00 57.59 C ANISOU 41 C LEU A 49 8074 5663 8145 -1945 175 -515 C ATOM 42 O LEU A 49 5.557 -12.406 24.421 1.00 56.75 O ANISOU 42 O LEU A 49 8006 5617 7938 -1812 162 -514 O ATOM 43 CB LEU A 49 2.949 -12.475 26.505 1.00 57.83 C ANISOU 43 CB LEU A 49 7786 5872 8315 -1981 160 -338 C ATOM 44 CG LEU A 49 3.868 -11.589 27.369 1.00 62.01 C ANISOU 44 CG LEU A 49 8295 6477 8789 -1777 215 -231 C ATOM 45 CD1 LEU A 49 3.867 -10.128 26.906 1.00 61.24 C ANISOU 45 CD1 LEU A 49 8114 6560 8595 -1700 99 -241 C ATOM 46 CD2 LEU A 49 3.483 -11.692 28.829 1.00 63.75 C ANISOU 46 CD2 LEU A 49 8425 6705 9093 -1749 312 -102 C ATOM 47 N ILE A 50 4.817 -14.517 24.861 1.00 51.67 N ANISOU 47 N ILE A 50 7441 4712 7477 -2011 285 -540 N ATOM 48 CA ILE A 50 6.090 -15.214 24.599 1.00 50.23 C ANISOU 48 CA ILE A 50 7443 4365 7276 -1922 399 -571 C ATOM 49 C ILE A 50 6.470 -15.010 23.128 1.00 52.68 C ANISOU 49 C ILE A 50 7870 4685 7463 -1951 328 -719 C ATOM 50 O ILE A 50 7.595 -14.605 22.849 1.00 51.05 O ANISOU 50 O ILE A 50 7734 4482 7180 -1810 367 -720 O ATOM 51 CB ILE A 50 6.079 -16.723 25.017 1.00 52.79 C ANISOU 51 CB ILE A 50 7873 4456 7727 -1993 535 -568 C ATOM 52 CG1 ILE A 50 5.903 -16.882 26.547 1.00 53.01 C ANISOU 52 CG1 ILE A 50 7806 4478 7859 -1939 621 -400 C ATOM 53 CG2 ILE A 50 7.352 -17.453 24.543 1.00 52.82 C ANISOU 53 CG2 ILE A 50 8070 4281 7719 -1899 652 -616 C ATOM 54 CD1 ILE A 50 5.237 -18.213 27.031 1.00 51.90 C ANISOU 54 CD1 ILE A 50 7703 4156 7861 -2084 713 -387 C ATOM 55 N ALA A 51 5.509 -15.233 22.203 1.00 48.71 N ANISOU 55 N ALA A 51 7374 4198 6934 -2137 217 -839 N ATOM 56 CA ALA A 51 5.713 -15.064 20.764 1.00 47.74 C ANISOU 56 CA ALA A 51 7371 4096 6674 -2191 135 -985 C ATOM 57 C ALA A 51 6.132 -13.632 20.416 1.00 51.14 C ANISOU 57 C ALA A 51 7740 4716 6974 -2062 49 -950 C ATOM 58 O ALA A 51 7.068 -13.450 19.636 1.00 51.58 O ANISOU 58 O ALA A 51 7926 4750 6922 -1988 78 -1010 O ATOM 59 CB ALA A 51 4.451 -15.451 20.006 1.00 48.09 C ANISOU 59 CB ALA A 51 7397 4160 6715 -2423 2 -1098 C ATOM 60 N ALA A 52 5.461 -12.620 21.018 1.00 46.40 N ANISOU 60 N ALA A 52 6947 4294 6390 -2030 -43 -849 N ATOM 61 CA ALA A 52 5.735 -11.188 20.812 1.00 44.64 C ANISOU 61 CA ALA A 52 6649 4248 6063 -1910 -124 -801 C ATOM 62 C ALA A 52 7.137 -10.834 21.296 1.00 45.70 C ANISOU 62 C ALA A 52 6836 4351 6175 -1715 -3 -734 C ATOM 63 O ALA A 52 7.847 -10.090 20.626 1.00 44.14 O ANISOU 63 O ALA A 52 6694 4214 5866 -1634 -24 -758 O ATOM 64 CB ALA A 52 4.698 -10.348 21.543 1.00 45.34 C ANISOU 64 CB ALA A 52 6521 4493 6211 -1911 -210 -701 C ATOM 65 N TYR A 53 7.538 -11.397 22.450 1.00 42.02 N ANISOU 65 N TYR A 53 6354 3793 5818 -1646 123 -647 N ATOM 66 CA TYR A 53 8.856 -11.206 23.031 1.00 41.75 C ANISOU 66 CA TYR A 53 6355 3725 5784 -1468 235 -573 C ATOM 67 C TYR A 53 9.930 -11.911 22.194 1.00 45.65 C ANISOU 67 C TYR A 53 7031 4074 6238 -1436 327 -661 C ATOM 68 O TYR A 53 11.017 -11.366 22.048 1.00 45.08 O ANISOU 68 O TYR A 53 6988 4031 6111 -1304 367 -642 O ATOM 69 CB TYR A 53 8.915 -11.682 24.483 1.00 42.33 C ANISOU 69 CB TYR A 53 6366 3741 5974 -1414 330 -449 C ATOM 70 CG TYR A 53 8.768 -10.579 25.512 1.00 43.10 C ANISOU 70 CG TYR A 53 6310 3996 6071 -1321 298 -330 C ATOM 71 CD1 TYR A 53 7.652 -10.514 26.337 1.00 45.03 C ANISOU 71 CD1 TYR A 53 6429 4297 6383 -1386 275 -266 C ATOM 72 CD2 TYR A 53 9.776 -9.636 25.707 1.00 42.92 C ANISOU 72 CD2 TYR A 53 6270 4056 5983 -1171 304 -283 C ATOM 73 CE1 TYR A 53 7.547 -9.550 27.341 1.00 45.09 C ANISOU 73 CE1 TYR A 53 6312 4434 6386 -1297 266 -164 C ATOM 74 CE2 TYR A 53 9.670 -8.655 26.695 1.00 43.15 C ANISOU 74 CE2 TYR A 53 6173 4214 6007 -1093 282 -185 C ATOM 75 CZ TYR A 53 8.551 -8.613 27.510 1.00 48.45 C ANISOU 75 CZ TYR A 53 6735 4936 6738 -1153 266 -128 C ATOM 76 OH TYR A 53 8.447 -7.649 28.489 1.00 47.70 O ANISOU 76 OH TYR A 53 6531 4963 6632 -1076 258 -42 O ATOM 77 N VAL A 54 9.626 -13.109 21.637 1.00 42.93 N ANISOU 77 N VAL A 54 6810 3573 5929 -1560 367 -761 N ATOM 78 CA VAL A 54 10.533 -13.888 20.769 1.00 42.51 C ANISOU 78 CA VAL A 54 6947 3362 5844 -1544 469 -865 C ATOM 79 C VAL A 54 10.761 -13.129 19.452 1.00 46.85 C ANISOU 79 C VAL A 54 7565 4005 6230 -1556 394 -967 C ATOM 80 O VAL A 54 11.911 -12.935 19.062 1.00 46.95 O ANISOU 80 O VAL A 54 7656 3992 6191 -1437 477 -979 O ATOM 81 CB VAL A 54 10.053 -15.357 20.550 1.00 45.98 C ANISOU 81 CB VAL A 54 7508 3597 6365 -1688 535 -955 C ATOM 82 CG1 VAL A 54 10.809 -16.035 19.407 1.00 45.77 C ANISOU 82 CG1 VAL A 54 7692 3420 6278 -1694 626 -1097 C ATOM 83 CG2 VAL A 54 10.178 -16.179 21.831 1.00 45.48 C ANISOU 83 CG2 VAL A 54 7412 3406 6461 -1637 652 -838 C ATOM 84 N ALA A 55 9.667 -12.655 18.807 1.00 43.20 N ANISOU 84 N ALA A 55 7062 3663 5689 -1692 234 -1025 N ATOM 85 CA ALA A 55 9.702 -11.875 17.561 1.00 42.20 C ANISOU 85 CA ALA A 55 6997 3646 5393 -1716 137 -1107 C ATOM 86 C ALA A 55 10.569 -10.630 17.718 1.00 46.26 C ANISOU 86 C ALA A 55 7447 4281 5847 -1545 146 -1017 C ATOM 87 O ALA A 55 11.454 -10.402 16.898 1.00 46.89 O ANISOU 87 O ALA A 55 7642 4347 5825 -1487 198 -1071 O ATOM 88 CB ALA A 55 8.290 -11.485 17.139 1.00 42.82 C ANISOU 88 CB ALA A 55 6989 3856 5425 -1871 -54 -1138 C ATOM 89 N VAL A 56 10.357 -9.862 18.805 1.00 41.78 N ANISOU 89 N VAL A 56 6703 3821 5349 -1466 113 -884 N ATOM 90 CA VAL A 56 11.073 -8.627 19.152 1.00 39.65 C ANISOU 90 CA VAL A 56 6352 3668 5045 -1315 115 -790 C ATOM 91 C VAL A 56 12.560 -8.911 19.441 1.00 42.67 C ANISOU 91 C VAL A 56 6800 3953 5459 -1173 274 -763 C ATOM 92 O VAL A 56 13.412 -8.203 18.925 1.00 42.95 O ANISOU 92 O VAL A 56 6870 4035 5415 -1089 299 -767 O ATOM 93 CB VAL A 56 10.326 -7.884 20.296 1.00 42.30 C ANISOU 93 CB VAL A 56 6493 4124 5453 -1289 45 -671 C ATOM 94 CG1 VAL A 56 11.260 -7.087 21.186 1.00 42.17 C ANISOU 94 CG1 VAL A 56 6403 4161 5460 -1125 106 -565 C ATOM 95 CG2 VAL A 56 9.214 -7.005 19.741 1.00 41.80 C ANISOU 95 CG2 VAL A 56 6349 4209 5323 -1367 -120 -682 C ATOM 96 N PHE A 57 12.865 -9.965 20.214 1.00 38.32 N ANISOU 96 N PHE A 57 6266 3265 5029 -1147 384 -733 N ATOM 97 CA PHE A 57 14.231 -10.386 20.551 1.00 37.21 C ANISOU 97 CA PHE A 57 6173 3020 4944 -1010 533 -696 C ATOM 98 C PHE A 57 15.054 -10.689 19.279 1.00 42.29 C ANISOU 98 C PHE A 57 6981 3580 5507 -999 615 -811 C ATOM 99 O PHE A 57 16.182 -10.202 19.149 1.00 41.50 O ANISOU 99 O PHE A 57 6881 3500 5385 -876 686 -784 O ATOM 100 CB PHE A 57 14.178 -11.616 21.481 1.00 38.27 C ANISOU 100 CB PHE A 57 6316 3005 5220 -1009 623 -648 C ATOM 101 CG PHE A 57 15.498 -12.225 21.879 1.00 39.10 C ANISOU 101 CG PHE A 57 6463 2988 5404 -866 773 -598 C ATOM 102 CD1 PHE A 57 16.238 -11.694 22.933 1.00 41.57 C ANISOU 102 CD1 PHE A 57 6660 3372 5764 -724 791 -462 C ATOM 103 CD2 PHE A 57 15.982 -13.360 21.233 1.00 40.96 C ANISOU 103 CD2 PHE A 57 6854 3035 5673 -872 897 -684 C ATOM 104 CE1 PHE A 57 17.457 -12.272 23.318 1.00 42.40 C ANISOU 104 CE1 PHE A 57 6786 3373 5951 -587 917 -403 C ATOM 105 CE2 PHE A 57 17.202 -13.940 21.618 1.00 43.34 C ANISOU 105 CE2 PHE A 57 7181 3220 6067 -725 1040 -625 C ATOM 106 CZ PHE A 57 17.925 -13.396 22.667 1.00 41.14 C ANISOU 106 CZ PHE A 57 6767 3024 5838 -582 1042 -479 C ATOM 107 N VAL A 58 14.470 -11.474 18.337 1.00 39.64 N ANISOU 107 N VAL A 58 6783 3154 5123 -1136 607 -944 N ATOM 108 CA VAL A 58 15.113 -11.876 17.083 1.00 39.21 C ANISOU 108 CA VAL A 58 6911 3007 4977 -1148 692 -1074 C ATOM 109 C VAL A 58 15.290 -10.684 16.148 1.00 44.49 C ANISOU 109 C VAL A 58 7595 3826 5482 -1140 620 -1103 C ATOM 110 O VAL A 58 16.400 -10.469 15.673 1.00 46.10 O ANISOU 110 O VAL A 58 7863 4008 5644 -1041 728 -1118 O ATOM 111 CB VAL A 58 14.418 -13.091 16.399 1.00 42.40 C ANISOU 111 CB VAL A 58 7473 3264 5374 -1310 705 -1217 C ATOM 112 CG1 VAL A 58 15.043 -13.411 15.039 1.00 42.21 C ANISOU 112 CG1 VAL A 58 7655 3156 5228 -1328 795 -1365 C ATOM 113 CG2 VAL A 58 14.446 -14.323 17.302 1.00 41.39 C ANISOU 113 CG2 VAL A 58 7350 2955 5420 -1301 813 -1181 C ATOM 114 N VAL A 59 14.232 -9.903 15.899 1.00 39.76 N ANISOU 114 N VAL A 59 6932 3377 4799 -1234 446 -1101 N ATOM 115 CA VAL A 59 14.300 -8.726 15.023 1.00 38.82 C ANISOU 115 CA VAL A 59 6827 3401 4522 -1226 364 -1111 C ATOM 116 C VAL A 59 15.300 -7.688 15.571 1.00 42.94 C ANISOU 116 C VAL A 59 7245 4001 5069 -1062 418 -996 C ATOM 117 O VAL A 59 16.103 -7.181 14.794 1.00 43.19 O ANISOU 117 O VAL A 59 7352 4054 5003 -1010 474 -1022 O ATOM 118 CB VAL A 59 12.894 -8.141 14.721 1.00 42.46 C ANISOU 118 CB VAL A 59 7222 4002 4909 -1352 158 -1114 C ATOM 119 CG1 VAL A 59 12.971 -6.824 13.950 1.00 41.69 C ANISOU 119 CG1 VAL A 59 7124 4055 4661 -1321 72 -1091 C ATOM 120 CG2 VAL A 59 12.034 -9.154 13.967 1.00 42.30 C ANISOU 120 CG2 VAL A 59 7323 3908 4840 -1529 102 -1249 C ATOM 121 N ALA A 60 15.301 -7.424 16.900 1.00 38.47 N ANISOU 121 N ALA A 60 6515 3470 4632 -987 411 -875 N ATOM 122 CA ALA A 60 16.240 -6.474 17.506 1.00 37.28 C ANISOU 122 CA ALA A 60 6262 3391 4511 -845 454 -772 C ATOM 123 C ALA A 60 17.711 -6.918 17.402 1.00 42.74 C ANISOU 123 C ALA A 60 7016 3981 5244 -733 627 -779 C ATOM 124 O ALA A 60 18.542 -6.096 17.029 1.00 43.13 O ANISOU 124 O ALA A 60 7061 4086 5239 -662 666 -762 O ATOM 125 CB ALA A 60 15.873 -6.179 18.946 1.00 37.23 C ANISOU 125 CB ALA A 60 6086 3443 4618 -803 406 -655 C ATOM 126 N LEU A 61 18.043 -8.190 17.713 1.00 39.34 N ANISOU 126 N LEU A 61 6637 3395 4914 -716 737 -800 N ATOM 127 CA LEU A 61 19.438 -8.652 17.640 1.00 39.38 C ANISOU 127 CA LEU A 61 6686 3298 4980 -596 908 -798 C ATOM 128 C LEU A 61 19.968 -8.685 16.218 1.00 41.65 C ANISOU 128 C LEU A 61 7132 3542 5150 -612 994 -914 C ATOM 129 O LEU A 61 21.084 -8.232 15.991 1.00 40.98 O ANISOU 129 O LEU A 61 7034 3474 5064 -510 1090 -890 O ATOM 130 CB LEU A 61 19.668 -10.000 18.347 1.00 40.09 C ANISOU 130 CB LEU A 61 6793 3222 5217 -559 1009 -778 C ATOM 131 CG LEU A 61 19.493 -10.034 19.880 1.00 45.54 C ANISOU 131 CG LEU A 61 7331 3942 6031 -506 966 -639 C ATOM 132 CD1 LEU A 61 19.761 -11.420 20.408 1.00 46.07 C ANISOU 132 CD1 LEU A 61 7445 3828 6232 -470 1077 -620 C ATOM 133 CD2 LEU A 61 20.422 -9.055 20.588 1.00 47.69 C ANISOU 133 CD2 LEU A 61 7460 4328 6334 -374 965 -525 C ATOM 134 N VAL A 62 19.159 -9.166 15.254 1.00 37.57 N ANISOU 134 N VAL A 62 6764 2983 4528 -747 955 -1038 N ATOM 135 CA VAL A 62 19.553 -9.217 13.847 1.00 36.38 C ANISOU 135 CA VAL A 62 6792 2796 4234 -780 1031 -1161 C ATOM 136 C VAL A 62 19.686 -7.796 13.291 1.00 39.20 C ANISOU 136 C VAL A 62 7119 3320 4457 -766 960 -1127 C ATOM 137 O VAL A 62 20.757 -7.428 12.818 1.00 39.39 O ANISOU 137 O VAL A 62 7176 3341 4449 -682 1081 -1128 O ATOM 138 CB VAL A 62 18.631 -10.114 12.987 1.00 39.89 C ANISOU 138 CB VAL A 62 7412 3156 4588 -942 993 -1309 C ATOM 139 CG1 VAL A 62 19.055 -10.093 11.515 1.00 39.18 C ANISOU 139 CG1 VAL A 62 7522 3045 4319 -979 1068 -1438 C ATOM 140 CG2 VAL A 62 18.615 -11.550 13.516 1.00 39.50 C ANISOU 140 CG2 VAL A 62 7409 2914 4686 -950 1093 -1343 C ATOM 141 N GLY A 63 18.622 -7.009 13.403 1.00 34.60 N ANISOU 141 N GLY A 63 6462 2872 3812 -842 774 -1089 N ATOM 142 CA GLY A 63 18.566 -5.638 12.917 1.00 33.68 C ANISOU 142 CA GLY A 63 6316 2908 3573 -836 687 -1046 C ATOM 143 C GLY A 63 19.668 -4.734 13.424 1.00 37.26 C ANISOU 143 C GLY A 63 6656 3414 4088 -700 764 -943 C ATOM 144 O GLY A 63 20.264 -4.001 12.636 1.00 37.07 O ANISOU 144 O GLY A 63 6688 3435 3962 -673 811 -949 O ATOM 145 N ASN A 64 19.954 -4.788 14.735 1.00 33.20 N ANISOU 145 N ASN A 64 5984 2894 3736 -620 777 -849 N ATOM 146 CA ASN A 64 20.962 -3.946 15.373 1.00 32.63 C ANISOU 146 CA ASN A 64 5784 2878 3736 -502 829 -750 C ATOM 147 C ASN A 64 22.398 -4.399 15.081 1.00 37.21 C ANISOU 147 C ASN A 64 6405 3366 4366 -407 1023 -769 C ATOM 148 O ASN A 64 23.289 -3.548 15.047 1.00 36.83 O ANISOU 148 O ASN A 64 6297 3375 4322 -338 1076 -719 O ATOM 149 CB ASN A 64 20.687 -3.792 16.865 1.00 30.78 C ANISOU 149 CB ASN A 64 5376 2687 3633 -461 758 -645 C ATOM 150 CG ASN A 64 19.511 -2.884 17.134 1.00 41.64 C ANISOU 150 CG ASN A 64 6679 4183 4958 -525 588 -606 C ATOM 151 OD1 ASN A 64 19.568 -1.681 16.884 1.00 39.66 O ANISOU 151 OD1 ASN A 64 6396 4031 4642 -513 540 -572 O ATOM 152 ND2 ASN A 64 18.414 -3.428 17.645 1.00 30.40 N ANISOU 152 ND2 ASN A 64 5227 2750 3574 -592 503 -607 N ATOM 153 N THR A 65 22.625 -5.711 14.836 1.00 34.50 N ANISOU 153 N THR A 65 6165 2876 4067 -406 1135 -843 N ATOM 154 CA THR A 65 23.938 -6.243 14.446 1.00 34.46 C ANISOU 154 CA THR A 65 6210 2768 4116 -311 1336 -871 C ATOM 155 C THR A 65 24.228 -5.726 13.038 1.00 40.50 C ANISOU 155 C THR A 65 7116 3558 4714 -347 1400 -952 C ATOM 156 O THR A 65 25.348 -5.288 12.764 1.00 40.79 O ANISOU 156 O THR A 65 7125 3605 4768 -264 1526 -927 O ATOM 157 CB THR A 65 23.958 -7.784 14.516 1.00 40.43 C ANISOU 157 CB THR A 65 7056 3346 4961 -306 1439 -935 C ATOM 158 OG1 THR A 65 23.795 -8.163 15.881 1.00 40.88 O ANISOU 158 OG1 THR A 65 6973 3388 5170 -259 1387 -835 O ATOM 159 CG2 THR A 65 25.251 -8.404 13.958 1.00 33.99 C ANISOU 159 CG2 THR A 65 6311 2407 4198 -206 1664 -980 C ATOM 160 N LEU A 66 23.194 -5.728 12.165 1.00 37.44 N ANISOU 160 N LEU A 66 6871 3192 4160 -475 1305 -1040 N ATOM 161 CA LEU A 66 23.293 -5.241 10.786 1.00 36.75 C ANISOU 161 CA LEU A 66 6944 3141 3880 -526 1340 -1115 C ATOM 162 C LEU A 66 23.621 -3.749 10.714 1.00 39.10 C ANISOU 162 C LEU A 66 7152 3580 4123 -491 1296 -1022 C ATOM 163 O LEU A 66 24.355 -3.346 9.834 1.00 39.55 O ANISOU 163 O LEU A 66 7297 3644 4087 -471 1410 -1046 O ATOM 164 CB LEU A 66 22.029 -5.577 9.978 1.00 36.52 C ANISOU 164 CB LEU A 66 7071 3119 3685 -678 1212 -1218 C ATOM 165 CG LEU A 66 21.754 -7.049 9.691 1.00 40.57 C ANISOU 165 CG LEU A 66 7728 3475 4210 -741 1278 -1346 C ATOM 166 CD1 LEU A 66 20.508 -7.209 8.863 1.00 41.09 C ANISOU 166 CD1 LEU A 66 7934 3576 4102 -907 1124 -1445 C ATOM 167 CD2 LEU A 66 22.928 -7.730 9.001 1.00 42.27 C ANISOU 167 CD2 LEU A 66 8084 3556 4422 -676 1522 -1432 C ATOM 168 N VAL A 67 23.115 -2.950 11.653 1.00 35.84 N ANISOU 168 N VAL A 67 6573 3270 3775 -483 1147 -916 N ATOM 169 CA VAL A 67 23.389 -1.516 11.749 1.00 35.14 C ANISOU 169 CA VAL A 67 6390 3300 3661 -450 1103 -823 C ATOM 170 C VAL A 67 24.875 -1.337 12.092 1.00 41.84 C ANISOU 170 C VAL A 67 7145 4122 4630 -336 1270 -773 C ATOM 171 O VAL A 67 25.572 -0.576 11.416 1.00 41.65 O ANISOU 171 O VAL A 67 7153 4133 4540 -317 1353 -761 O ATOM 172 CB VAL A 67 22.441 -0.785 12.752 1.00 37.06 C ANISOU 172 CB VAL A 67 6482 3644 3953 -469 912 -735 C ATOM 173 CG1 VAL A 67 22.872 0.668 12.988 1.00 35.64 C ANISOU 173 CG1 VAL A 67 6199 3562 3779 -422 891 -639 C ATOM 174 CG2 VAL A 67 20.991 -0.846 12.274 1.00 37.05 C ANISOU 174 CG2 VAL A 67 6559 3685 3832 -581 748 -778 C ATOM 175 N CYS A 68 25.354 -2.053 13.130 1.00 39.59 N ANISOU 175 N CYS A 68 6744 3777 4523 -262 1318 -739 N ATOM 176 CA CYS A 68 26.751 -2.013 13.567 1.00 38.91 C ANISOU 176 CA CYS A 68 6542 3667 4575 -150 1461 -685 C ATOM 177 C CYS A 68 27.695 -2.448 12.457 1.00 42.90 C ANISOU 177 C CYS A 68 7170 4089 5039 -118 1668 -759 C ATOM 178 O CYS A 68 28.698 -1.780 12.241 1.00 42.14 O ANISOU 178 O CYS A 68 7016 4027 4968 -66 1772 -721 O ATOM 179 CB CYS A 68 26.943 -2.842 14.831 1.00 38.44 C ANISOU 179 CB CYS A 68 6356 3555 4695 -82 1456 -634 C ATOM 180 SG CYS A 68 26.072 -2.187 16.268 1.00 41.98 S ANISOU 180 SG CYS A 68 6641 4111 5197 -103 1246 -534 S ATOM 181 N LEU A 69 27.347 -3.526 11.723 1.00 41.05 N ANISOU 181 N LEU A 69 7112 3747 4737 -158 1732 -870 N ATOM 182 CA LEU A 69 28.137 -4.058 10.607 1.00 41.79 C ANISOU 182 CA LEU A 69 7356 3747 4775 -135 1943 -962 C ATOM 183 C LEU A 69 28.192 -3.128 9.396 1.00 45.79 C ANISOU 183 C LEU A 69 7988 4324 5084 -192 1973 -994 C ATOM 184 O LEU A 69 29.275 -2.960 8.833 1.00 45.68 O ANISOU 184 O LEU A 69 7991 4288 5077 -134 2160 -1000 O ATOM 185 CB LEU A 69 27.655 -5.456 10.192 1.00 42.30 C ANISOU 185 CB LEU A 69 7591 3669 4811 -177 1993 -1084 C ATOM 186 CG LEU A 69 28.156 -6.624 11.057 1.00 48.47 C ANISOU 186 CG LEU A 69 8293 4320 5804 -80 2085 -1067 C ATOM 187 CD1 LEU A 69 27.413 -7.914 10.730 1.00 48.49 C ANISOU 187 CD1 LEU A 69 8472 4181 5772 -150 2100 -1187 C ATOM 188 CD2 LEU A 69 29.661 -6.850 10.883 1.00 51.41 C ANISOU 188 CD2 LEU A 69 8616 4624 6295 54 2321 -1051 C ATOM 189 N ALA A 70 27.040 -2.519 9.000 1.00 41.23 N ANISOU 189 N ALA A 70 7492 3834 4337 -301 1794 -1004 N ATOM 190 CA ALA A 70 26.936 -1.584 7.867 1.00 40.33 C ANISOU 190 CA ALA A 70 7508 3798 4018 -360 1791 -1016 C ATOM 191 C ALA A 70 27.884 -0.391 8.037 1.00 44.86 C ANISOU 191 C ALA A 70 7952 4445 4648 -295 1858 -911 C ATOM 192 O ALA A 70 28.582 -0.025 7.088 1.00 44.34 O ANISOU 192 O ALA A 70 7985 4378 4485 -290 2005 -929 O ATOM 193 CB ALA A 70 25.500 -1.093 7.708 1.00 40.58 C ANISOU 193 CB ALA A 70 7591 3922 3906 -468 1553 -1011 C ATOM 194 N VAL A 71 27.923 0.193 9.257 1.00 41.69 N ANISOU 194 N VAL A 71 7335 4103 4403 -252 1756 -804 N ATOM 195 CA VAL A 71 28.764 1.345 9.586 1.00 41.31 C ANISOU 195 CA VAL A 71 7144 4123 4429 -205 1797 -705 C ATOM 196 C VAL A 71 30.242 0.922 9.696 1.00 49.11 C ANISOU 196 C VAL A 71 8046 5046 5567 -108 2016 -700 C ATOM 197 O VAL A 71 31.104 1.631 9.173 1.00 49.16 O ANISOU 197 O VAL A 71 8043 5075 5559 -91 2144 -672 O ATOM 198 CB VAL A 71 28.231 2.139 10.818 1.00 43.35 C ANISOU 198 CB VAL A 71 7221 4467 4782 -205 1607 -608 C ATOM 199 CG1 VAL A 71 29.167 3.288 11.220 1.00 43.06 C ANISOU 199 CG1 VAL A 71 7037 4489 4834 -165 1653 -517 C ATOM 200 CG2 VAL A 71 26.825 2.679 10.550 1.00 42.59 C ANISOU 200 CG2 VAL A 71 7206 4438 4538 -292 1412 -606 C ATOM 201 N TRP A 72 30.529 -0.239 10.315 1.00 49.67 N ANISOU 201 N TRP A 72 8058 5032 5782 -44 2068 -724 N ATOM 202 CA TRP A 72 31.900 -0.724 10.480 1.00 52.36 C ANISOU 202 CA TRP A 72 8297 5310 6288 63 2268 -711 C ATOM 203 C TRP A 72 32.605 -1.049 9.158 1.00 53.81 C ANISOU 203 C TRP A 72 8642 5421 6385 75 2503 -794 C ATOM 204 O TRP A 72 33.777 -0.718 9.004 1.00 52.85 O ANISOU 204 O TRP A 72 8428 5301 6351 138 2669 -757 O ATOM 205 CB TRP A 72 31.976 -1.927 11.448 1.00 53.94 C ANISOU 205 CB TRP A 72 8406 5429 6661 136 2261 -704 C ATOM 206 CG TRP A 72 33.382 -2.428 11.656 1.00 57.61 C ANISOU 206 CG TRP A 72 8745 5833 7313 261 2454 -674 C ATOM 207 CD1 TRP A 72 34.412 -1.750 12.243 1.00 61.11 C ANISOU 207 CD1 TRP A 72 8974 6345 7900 324 2485 -576 C ATOM 208 CD2 TRP A 72 33.938 -3.662 11.174 1.00 58.69 C ANISOU 208 CD2 TRP A 72 8964 5826 7511 335 2655 -745 C ATOM 209 NE1 TRP A 72 35.572 -2.492 12.167 1.00 61.45 N ANISOU 209 NE1 TRP A 72 8944 6307 8098 438 2685 -573 N ATOM 210 CE2 TRP A 72 35.305 -3.678 11.537 1.00 63.39 C ANISOU 210 CE2 TRP A 72 9370 6416 8300 454 2798 -674 C ATOM 211 CE3 TRP A 72 33.397 -4.792 10.537 1.00 61.32 C ANISOU 211 CE3 TRP A 72 9506 6028 7764 311 2723 -863 C ATOM 212 CZ2 TRP A 72 36.144 -4.768 11.265 1.00 64.03 C ANISOU 212 CZ2 TRP A 72 9461 6364 8505 565 3014 -709 C ATOM 213 CZ3 TRP A 72 34.231 -5.870 10.245 1.00 64.07 C ANISOU 213 CZ3 TRP A 72 9885 6234 8225 413 2946 -910 C ATOM 214 CH2 TRP A 72 35.589 -5.852 10.603 1.00 65.01 C ANISOU 214 CH2 TRP A 72 9809 6349 8544 546 3094 -830 C ATOM 215 N ARG A 73 31.894 -1.696 8.223 1.00 48.78 N ANISOU 215 N ARG A 73 8239 4720 5573 10 2520 -908 N ATOM 216 CA ARG A 73 32.433 -2.170 6.954 1.00 47.98 C ANISOU 216 CA ARG A 73 8329 4537 5362 13 2746 -1009 C ATOM 217 C ARG A 73 32.415 -1.157 5.806 1.00 52.31 C ANISOU 217 C ARG A 73 9019 5160 5696 -59 2785 -1015 C ATOM 218 O ARG A 73 33.035 -1.412 4.769 1.00 52.34 O ANISOU 218 O ARG A 73 9164 5108 5613 -47 3001 -1084 O ATOM 219 CB ARG A 73 31.705 -3.461 6.531 1.00 45.82 C ANISOU 219 CB ARG A 73 8257 4149 5005 -29 2753 -1142 C ATOM 220 CG ARG A 73 31.919 -4.609 7.503 1.00 53.98 C ANISOU 220 CG ARG A 73 9180 5074 6257 55 2775 -1139 C ATOM 221 CD ARG A 73 31.851 -5.972 6.858 1.00 76.24 C ANISOU 221 CD ARG A 73 12199 7728 9040 53 2917 -1281 C ATOM 222 NE ARG A 73 30.518 -6.276 6.340 1.00 95.25 N ANISOU 222 NE ARG A 73 14812 10132 11248 -89 2767 -1383 N ATOM 223 CZ ARG A 73 30.221 -7.368 5.644 1.00117.54 C ANISOU 223 CZ ARG A 73 17850 12821 13989 -134 2856 -1530 C ATOM 224 NH1 ARG A 73 31.158 -8.272 5.382 1.00104.37 N ANISOU 224 NH1 ARG A 73 16230 10999 12425 -38 3108 -1592 N ATOM 225 NH2 ARG A 73 28.985 -7.564 5.203 1.00110.44 N ANISOU 225 NH2 ARG A 73 17118 11937 12908 -278 2695 -1617 N ATOM 226 N ASN A 74 31.717 -0.027 5.971 1.00 49.31 N ANISOU 226 N ASN A 74 8608 4899 5228 -127 2589 -941 N ATOM 227 CA ASN A 74 31.599 0.945 4.887 1.00 49.05 C ANISOU 227 CA ASN A 74 8722 4933 4982 -196 2608 -933 C ATOM 228 C ASN A 74 31.965 2.367 5.299 1.00 53.08 C ANISOU 228 C ASN A 74 9071 5541 5554 -188 2561 -801 C ATOM 229 O ASN A 74 31.267 2.988 6.098 1.00 51.66 O ANISOU 229 O ASN A 74 8779 5432 5416 -211 2352 -729 O ATOM 230 CB ASN A 74 30.190 0.912 4.278 1.00 48.67 C ANISOU 230 CB ASN A 74 8871 4921 4699 -307 2419 -989 C ATOM 231 CG ASN A 74 29.754 -0.411 3.730 1.00 60.86 C ANISOU 231 CG ASN A 74 10606 6370 6148 -345 2458 -1134 C ATOM 232 OD1 ASN A 74 29.207 -1.256 4.436 1.00 51.99 O ANISOU 232 OD1 ASN A 74 9434 5196 5123 -345 2363 -1170 O ATOM 233 ND2 ASN A 74 29.998 -0.606 2.447 1.00 56.18 N ANISOU 233 ND2 ASN A 74 10245 5747 5354 -383 2605 -1222 N ATOM 234 N HIS A 75 33.037 2.888 4.706 1.00 51.84 N ANISOU 234 N HIS A 75 8916 5383 5397 -162 2766 -775 N ATOM 235 CA HIS A 75 33.536 4.231 4.940 1.00 52.91 C ANISOU 235 CA HIS A 75 8919 5594 5591 -165 2764 -659 C ATOM 236 C HIS A 75 32.481 5.318 4.686 1.00 52.41 C ANISOU 236 C HIS A 75 8941 5615 5356 -249 2564 -602 C ATOM 237 O HIS A 75 32.443 6.289 5.437 1.00 51.79 O ANISOU 237 O HIS A 75 8708 5594 5378 -251 2454 -506 O ATOM 238 CB HIS A 75 34.805 4.497 4.114 1.00 55.80 C ANISOU 238 CB HIS A 75 9312 5933 5955 -139 3045 -655 C ATOM 239 CG HIS A 75 35.283 5.901 4.269 1.00 61.36 C ANISOU 239 CG HIS A 75 9893 6704 6717 -158 3050 -539 C ATOM 240 ND1 HIS A 75 34.812 6.921 3.445 1.00 64.34 N ANISOU 240 ND1 HIS A 75 10421 7130 6895 -233 3011 -493 N ATOM 241 CD2 HIS A 75 36.089 6.438 5.215 1.00 64.68 C ANISOU 241 CD2 HIS A 75 10055 7149 7370 -119 3065 -460 C ATOM 242 CE1 HIS A 75 35.377 8.034 3.894 1.00 64.36 C ANISOU 242 CE1 HIS A 75 10259 7170 7023 -237 3023 -392 C ATOM 243 NE2 HIS A 75 36.155 7.794 4.957 1.00 64.84 N ANISOU 243 NE2 HIS A 75 10070 7223 7342 -176 3052 -374 N ATOM 244 N HIS A 76 31.638 5.164 3.633 1.00 46.60 N ANISOU 244 N HIS A 76 8452 4886 4368 -316 2516 -659 N ATOM 245 CA HIS A 76 30.575 6.117 3.282 1.00 45.69 C ANISOU 245 CA HIS A 76 8432 4851 4078 -387 2321 -601 C ATOM 246 C HIS A 76 29.462 6.208 4.351 1.00 49.15 C ANISOU 246 C HIS A 76 8744 5333 4597 -398 2052 -568 C ATOM 247 O HIS A 76 28.724 7.199 4.375 1.00 48.67 O ANISOU 247 O HIS A 76 8683 5341 4470 -432 1893 -488 O ATOM 248 CB HIS A 76 29.988 5.827 1.886 1.00 46.49 C ANISOU 248 CB HIS A 76 8825 4955 3883 -456 2331 -673 C ATOM 249 CG HIS A 76 29.077 4.636 1.817 1.00 50.42 C ANISOU 249 CG HIS A 76 9427 5425 4305 -493 2219 -789 C ATOM 250 ND1 HIS A 76 29.570 3.360 1.608 1.00 52.73 N ANISOU 250 ND1 HIS A 76 9788 5621 4627 -470 2381 -912 N ATOM 251 CD2 HIS A 76 27.727 4.569 1.899 1.00 52.51 C ANISOU 251 CD2 HIS A 76 9737 5741 4474 -556 1969 -798 C ATOM 252 CE1 HIS A 76 28.511 2.559 1.608 1.00 52.06 C ANISOU 252 CE1 HIS A 76 9790 5526 4465 -527 2223 -995 C ATOM 253 NE2 HIS A 76 27.381 3.240 1.766 1.00 52.22 N ANISOU 253 NE2 HIS A 76 9795 5640 4407 -583 1971 -930 N ATOM 254 N MET A 77 29.341 5.167 5.222 1.00 44.53 N ANISOU 254 N MET A 77 8058 4705 4157 -366 2013 -624 N ATOM 255 CA MET A 77 28.365 5.046 6.317 1.00 43.09 C ANISOU 255 CA MET A 77 7750 4554 4070 -372 1791 -602 C ATOM 256 C MET A 77 28.850 5.705 7.604 1.00 45.60 C ANISOU 256 C MET A 77 7820 4899 4606 -318 1759 -510 C ATOM 257 O MET A 77 28.051 5.922 8.500 1.00 45.04 O ANISOU 257 O MET A 77 7647 4869 4599 -325 1578 -472 O ATOM 258 CB MET A 77 28.080 3.563 6.638 1.00 45.24 C ANISOU 258 CB MET A 77 8040 4755 4396 -364 1786 -701 C ATOM 259 CG MET A 77 27.457 2.767 5.514 1.00 48.80 C ANISOU 259 CG MET A 77 8731 5172 4639 -434 1787 -813 C ATOM 260 SD MET A 77 25.837 3.345 4.971 1.00 53.05 S ANISOU 260 SD MET A 77 9387 5809 4959 -538 1524 -796 S ATOM 261 CE MET A 77 24.822 2.827 6.338 1.00 49.94 C ANISOU 261 CE MET A 77 8817 5425 4731 -542 1316 -783 C ATOM 262 N ARG A 78 30.158 5.978 7.720 1.00 42.52 N ANISOU 262 N ARG A 78 7332 4488 4335 -268 1935 -479 N ATOM 263 CA ARG A 78 30.787 6.543 8.919 1.00 41.31 C ANISOU 263 CA ARG A 78 6944 4361 4392 -225 1917 -402 C ATOM 264 C ARG A 78 30.569 8.063 9.072 1.00 44.09 C ANISOU 264 C ARG A 78 7250 4778 4726 -261 1827 -310 C ATOM 265 O ARG A 78 31.521 8.842 9.092 1.00 44.21 O ANISOU 265 O ARG A 78 7182 4799 4816 -254 1935 -258 O ATOM 266 CB ARG A 78 32.279 6.157 8.972 1.00 39.38 C ANISOU 266 CB ARG A 78 6596 4071 4294 -161 2136 -407 C ATOM 267 CG ARG A 78 32.483 4.656 9.182 1.00 46.49 C ANISOU 267 CG ARG A 78 7493 4898 5273 -103 2205 -481 C ATOM 268 CD ARG A 78 33.937 4.250 9.311 1.00 52.10 C ANISOU 268 CD ARG A 78 8075 5566 6155 -23 2413 -474 C ATOM 269 NE ARG A 78 34.145 2.877 8.849 1.00 61.22 N ANISOU 269 NE ARG A 78 9325 6624 7313 27 2549 -562 N ATOM 270 CZ ARG A 78 35.055 2.522 7.946 1.00 86.28 C ANISOU 270 CZ ARG A 78 12568 9737 10476 63 2790 -607 C ATOM 271 NH1 ARG A 78 35.879 3.429 7.429 1.00 75.48 N ANISOU 271 NH1 ARG A 78 11174 8404 9102 52 2924 -563 N ATOM 272 NH2 ARG A 78 35.164 1.257 7.569 1.00 80.38 N ANISOU 272 NH2 ARG A 78 11918 8888 9735 109 2912 -695 N ATOM 273 N THR A 79 29.298 8.468 9.185 1.00 39.49 N ANISOU 273 N THR A 79 6716 4237 4052 -300 1633 -290 N ATOM 274 CA THR A 79 28.885 9.858 9.417 1.00 38.09 C ANISOU 274 CA THR A 79 6500 4108 3865 -325 1529 -203 C ATOM 275 C THR A 79 28.694 10.018 10.931 1.00 37.98 C ANISOU 275 C THR A 79 6286 4118 4025 -301 1407 -175 C ATOM 276 O THR A 79 28.559 9.006 11.623 1.00 36.79 O ANISOU 276 O THR A 79 6069 3956 3952 -274 1369 -217 O ATOM 277 CB THR A 79 27.602 10.212 8.617 1.00 43.12 C ANISOU 277 CB THR A 79 7303 4777 4304 -370 1393 -190 C ATOM 278 OG1 THR A 79 26.453 9.599 9.215 1.00 39.89 O ANISOU 278 OG1 THR A 79 6864 4389 3902 -376 1216 -220 O ATOM 279 CG2 THR A 79 27.697 9.818 7.150 1.00 39.97 C ANISOU 279 CG2 THR A 79 7122 4361 3705 -400 1496 -235 C ATOM 280 N VAL A 80 28.694 11.274 11.444 1.00 33.01 N ANISOU 280 N VAL A 80 5575 3516 3451 -313 1353 -104 N ATOM 281 CA VAL A 80 28.495 11.593 12.873 1.00 32.00 C ANISOU 281 CA VAL A 80 5277 3415 3468 -299 1239 -79 C ATOM 282 C VAL A 80 27.189 10.952 13.396 1.00 34.50 C ANISOU 282 C VAL A 80 5599 3753 3757 -295 1074 -104 C ATOM 283 O VAL A 80 27.219 10.268 14.423 1.00 34.52 O ANISOU 283 O VAL A 80 5490 3760 3867 -269 1034 -124 O ATOM 284 CB VAL A 80 28.591 13.122 13.169 1.00 34.85 C ANISOU 284 CB VAL A 80 5588 3787 3867 -322 1215 -10 C ATOM 285 CG1 VAL A 80 28.175 13.456 14.602 1.00 33.87 C ANISOU 285 CG1 VAL A 80 5320 3690 3858 -314 1087 2 C ATOM 286 CG2 VAL A 80 29.992 13.650 12.886 1.00 34.72 C ANISOU 286 CG2 VAL A 80 5527 3748 3918 -335 1384 11 C ATOM 287 N THR A 81 26.074 11.130 12.650 1.00 29.57 N ANISOU 287 N THR A 81 5104 3143 2987 -322 981 -98 N ATOM 288 CA THR A 81 24.760 10.569 12.985 1.00 28.98 C ANISOU 288 CA THR A 81 5036 3093 2881 -330 825 -119 C ATOM 289 C THR A 81 24.825 9.043 13.091 1.00 31.46 C ANISOU 289 C THR A 81 5360 3379 3217 -324 854 -195 C ATOM 290 O THR A 81 24.327 8.490 14.072 1.00 29.01 O ANISOU 290 O THR A 81 4957 3075 2989 -313 773 -206 O ATOM 291 CB THR A 81 23.691 11.029 11.981 1.00 34.15 C ANISOU 291 CB THR A 81 5828 3775 3372 -362 730 -95 C ATOM 292 OG1 THR A 81 23.633 12.449 12.009 1.00 33.92 O ANISOU 292 OG1 THR A 81 5782 3758 3348 -355 707 -14 O ATOM 293 CG2 THR A 81 22.290 10.437 12.270 1.00 29.79 C ANISOU 293 CG2 THR A 81 5268 3256 2795 -380 564 -117 C ATOM 294 N ASN A 82 25.466 8.375 12.106 1.00 28.35 N ANISOU 294 N ASN A 82 5079 2944 2750 -329 983 -246 N ATOM 295 CA ASN A 82 25.570 6.909 12.079 1.00 28.62 C ANISOU 295 CA ASN A 82 5146 2927 2801 -321 1034 -325 C ATOM 296 C ASN A 82 26.438 6.345 13.190 1.00 33.61 C ANISOU 296 C ASN A 82 5622 3531 3617 -264 1099 -321 C ATOM 297 O ASN A 82 26.145 5.246 13.635 1.00 35.14 O ANISOU 297 O ASN A 82 5803 3691 3859 -253 1076 -361 O ATOM 298 CB ASN A 82 25.987 6.389 10.724 1.00 28.54 C ANISOU 298 CB ASN A 82 5312 2875 2659 -341 1163 -387 C ATOM 299 CG ASN A 82 24.924 6.551 9.673 1.00 44.70 C ANISOU 299 CG ASN A 82 7528 4951 4504 -406 1064 -407 C ATOM 300 OD1 ASN A 82 23.773 6.904 9.958 1.00 37.36 O ANISOU 300 OD1 ASN A 82 6576 4073 3548 -434 888 -377 O ATOM 301 ND2 ASN A 82 25.277 6.283 8.432 1.00 37.72 N ANISOU 301 ND2 ASN A 82 6819 4041 3474 -430 1173 -458 N ATOM 302 N TYR A 83 27.431 7.107 13.694 1.00 30.23 N ANISOU 302 N TYR A 83 5072 3120 3293 -232 1164 -268 N ATOM 303 CA TYR A 83 28.241 6.713 14.851 1.00 30.82 C ANISOU 303 CA TYR A 83 4979 3189 3542 -178 1195 -249 C ATOM 304 C TYR A 83 27.332 6.692 16.094 1.00 30.92 C ANISOU 304 C TYR A 83 4900 3239 3610 -180 1032 -224 C ATOM 305 O TYR A 83 27.365 5.730 16.867 1.00 30.77 O ANISOU 305 O TYR A 83 4817 3199 3675 -147 1019 -233 O ATOM 306 CB TYR A 83 29.415 7.689 15.052 1.00 34.78 C ANISOU 306 CB TYR A 83 5370 3714 4129 -165 1279 -199 C ATOM 307 CG TYR A 83 30.681 7.319 14.307 1.00 40.75 C ANISOU 307 CG TYR A 83 6138 4428 4918 -134 1476 -218 C ATOM 308 CD1 TYR A 83 30.656 6.410 13.254 1.00 43.57 C ANISOU 308 CD1 TYR A 83 6647 4726 5183 -128 1579 -282 C ATOM 309 CD2 TYR A 83 31.906 7.882 14.652 1.00 42.82 C ANISOU 309 CD2 TYR A 83 6257 4707 5304 -115 1564 -177 C ATOM 310 CE1 TYR A 83 31.820 6.055 12.575 1.00 45.47 C ANISOU 310 CE1 TYR A 83 6899 4922 5457 -93 1780 -303 C ATOM 311 CE2 TYR A 83 33.076 7.537 13.977 1.00 44.59 C ANISOU 311 CE2 TYR A 83 6474 4894 5574 -82 1757 -190 C ATOM 312 CZ TYR A 83 33.027 6.635 12.926 1.00 52.59 C ANISOU 312 CZ TYR A 83 7643 5844 6493 -67 1873 -253 C ATOM 313 OH TYR A 83 34.171 6.301 12.237 1.00 52.66 O ANISOU 313 OH TYR A 83 7650 5811 6547 -29 2083 -269 O ATOM 314 N PHE A 84 26.475 7.728 16.241 1.00 25.30 N ANISOU 314 N PHE A 84 4191 2576 2845 -217 915 -192 N ATOM 315 CA PHE A 84 25.499 7.817 17.326 1.00 24.22 C ANISOU 315 CA PHE A 84 3980 2476 2746 -222 772 -171 C ATOM 316 C PHE A 84 24.415 6.754 17.163 1.00 28.73 C ANISOU 316 C PHE A 84 4624 3028 3266 -242 704 -212 C ATOM 317 O PHE A 84 24.051 6.145 18.150 1.00 29.12 O ANISOU 317 O PHE A 84 4600 3079 3387 -229 651 -208 O ATOM 318 CB PHE A 84 24.883 9.211 17.428 1.00 25.34 C ANISOU 318 CB PHE A 84 4113 2662 2852 -247 687 -127 C ATOM 319 CG PHE A 84 25.744 10.304 18.018 1.00 26.04 C ANISOU 319 CG PHE A 84 4104 2769 3020 -239 721 -88 C ATOM 320 CD1 PHE A 84 26.235 10.203 19.312 1.00 28.27 C ANISOU 320 CD1 PHE A 84 4249 3073 3417 -218 704 -76 C ATOM 321 CD2 PHE A 84 25.987 11.479 17.312 1.00 27.10 C ANISOU 321 CD2 PHE A 84 4289 2901 3109 -261 760 -59 C ATOM 322 CE1 PHE A 84 27.023 11.221 19.861 1.00 28.23 C ANISOU 322 CE1 PHE A 84 4156 3088 3481 -227 724 -50 C ATOM 323 CE2 PHE A 84 26.742 12.510 17.879 1.00 28.63 C ANISOU 323 CE2 PHE A 84 4393 3101 3382 -269 789 -29 C ATOM 324 CZ PHE A 84 27.261 12.368 19.145 1.00 26.41 C ANISOU 324 CZ PHE A 84 3974 2845 3216 -256 769 -31 C ATOM 325 N LEU A 85 23.935 6.482 15.926 1.00 25.68 N ANISOU 325 N LEU A 85 4383 2621 2752 -280 711 -254 N ATOM 326 CA LEU A 85 22.955 5.409 15.674 1.00 24.57 C ANISOU 326 CA LEU A 85 4317 2456 2561 -317 649 -308 C ATOM 327 C LEU A 85 23.563 4.037 16.021 1.00 30.51 C ANISOU 327 C LEU A 85 5059 3136 3398 -287 739 -349 C ATOM 328 O LEU A 85 22.828 3.163 16.477 1.00 30.49 O ANISOU 328 O LEU A 85 5051 3111 3425 -306 679 -371 O ATOM 329 CB LEU A 85 22.415 5.408 14.233 1.00 23.66 C ANISOU 329 CB LEU A 85 4371 2340 2279 -373 632 -350 C ATOM 330 CG LEU A 85 21.591 6.617 13.785 1.00 27.14 C ANISOU 330 CG LEU A 85 4838 2850 2625 -401 521 -301 C ATOM 331 CD1 LEU A 85 21.145 6.436 12.366 1.00 26.75 C ANISOU 331 CD1 LEU A 85 4962 2802 2399 -456 502 -342 C ATOM 332 CD2 LEU A 85 20.370 6.878 14.697 1.00 25.31 C ANISOU 332 CD2 LEU A 85 4503 2667 2448 -411 366 -263 C ATOM 333 N VAL A 86 24.905 3.857 15.844 1.00 28.02 N ANISOU 333 N VAL A 86 4730 2781 3136 -236 887 -353 N ATOM 334 CA VAL A 86 25.583 2.619 16.273 1.00 28.22 C ANISOU 334 CA VAL A 86 4724 2732 3267 -185 980 -374 C ATOM 335 C VAL A 86 25.493 2.513 17.826 1.00 31.55 C ANISOU 335 C VAL A 86 4988 3182 3818 -149 902 -312 C ATOM 336 O VAL A 86 25.140 1.455 18.340 1.00 31.84 O ANISOU 336 O VAL A 86 5021 3170 3907 -139 888 -322 O ATOM 337 CB VAL A 86 27.024 2.459 15.713 1.00 31.27 C ANISOU 337 CB VAL A 86 5115 3072 3693 -129 1161 -386 C ATOM 338 CG1 VAL A 86 27.802 1.362 16.446 1.00 31.43 C ANISOU 338 CG1 VAL A 86 5051 3028 3863 -52 1243 -376 C ATOM 339 CG2 VAL A 86 26.985 2.151 14.227 1.00 30.63 C ANISOU 339 CG2 VAL A 86 5221 2943 3473 -167 1253 -465 C ATOM 340 N ASN A 87 25.748 3.623 18.545 1.00 26.92 N ANISOU 340 N ASN A 87 4286 2671 3270 -136 851 -250 N ATOM 341 CA ASN A 87 25.652 3.680 20.002 1.00 26.72 C ANISOU 341 CA ASN A 87 4126 2686 3340 -111 773 -194 C ATOM 342 C ASN A 87 24.233 3.314 20.509 1.00 31.76 C ANISOU 342 C ASN A 87 4782 3333 3951 -151 655 -197 C ATOM 343 O ASN A 87 24.099 2.568 21.485 1.00 30.94 O ANISOU 343 O ASN A 87 4621 3214 3918 -128 632 -172 O ATOM 344 CB ASN A 87 26.088 5.035 20.538 1.00 25.29 C ANISOU 344 CB ASN A 87 3846 2581 3184 -109 739 -146 C ATOM 345 CG ASN A 87 26.476 4.960 21.977 1.00 36.66 C ANISOU 345 CG ASN A 87 5148 4058 4723 -72 697 -95 C ATOM 346 OD1 ASN A 87 27.248 4.076 22.379 1.00 29.53 O ANISOU 346 OD1 ASN A 87 4192 3125 3904 -18 750 -77 O ATOM 347 ND2 ASN A 87 25.944 5.877 22.784 1.00 18.87 N ANISOU 347 ND2 ASN A 87 2840 1868 2461 -97 600 -69 N ATOM 348 N LEU A 88 23.191 3.800 19.802 1.00 27.69 N ANISOU 348 N LEU A 88 4346 2841 3334 -211 585 -224 N ATOM 349 CA LEU A 88 21.793 3.479 20.068 1.00 27.29 C ANISOU 349 CA LEU A 88 4309 2801 3257 -260 479 -232 C ATOM 350 C LEU A 88 21.586 1.954 19.901 1.00 30.66 C ANISOU 350 C LEU A 88 4802 3145 3704 -275 515 -278 C ATOM 351 O LEU A 88 20.972 1.334 20.764 1.00 30.02 O ANISOU 351 O LEU A 88 4676 3054 3679 -283 470 -260 O ATOM 352 CB LEU A 88 20.883 4.307 19.139 1.00 26.97 C ANISOU 352 CB LEU A 88 4339 2803 3105 -313 403 -247 C ATOM 353 CG LEU A 88 19.362 4.192 19.286 1.00 31.76 C ANISOU 353 CG LEU A 88 4941 3440 3687 -367 280 -249 C ATOM 354 CD1 LEU A 88 18.896 4.459 20.713 1.00 32.18 C ANISOU 354 CD1 LEU A 88 4867 3533 3826 -347 226 -197 C ATOM 355 CD2 LEU A 88 18.662 5.133 18.332 1.00 33.16 C ANISOU 355 CD2 LEU A 88 5173 3667 3760 -401 205 -245 C ATOM 356 N SER A 89 22.165 1.349 18.843 1.00 27.33 N ANISOU 356 N SER A 89 4488 2654 3241 -275 613 -337 N ATOM 357 CA SER A 89 22.137 -0.102 18.598 1.00 26.83 C ANISOU 357 CA SER A 89 4504 2487 3202 -286 675 -392 C ATOM 358 C SER A 89 22.870 -0.872 19.704 1.00 31.83 C ANISOU 358 C SER A 89 5047 3071 3974 -209 736 -343 C ATOM 359 O SER A 89 22.385 -1.917 20.096 1.00 31.50 O ANISOU 359 O SER A 89 5025 2963 3979 -224 731 -353 O ATOM 360 CB SER A 89 22.723 -0.440 17.230 1.00 29.71 C ANISOU 360 CB SER A 89 5011 2790 3488 -294 785 -470 C ATOM 361 OG SER A 89 21.818 -0.059 16.207 1.00 40.90 O ANISOU 361 OG SER A 89 6537 4243 4761 -379 709 -520 O ATOM 362 N LEU A 90 24.006 -0.347 20.237 1.00 30.33 N ANISOU 362 N LEU A 90 4754 2916 3853 -132 785 -285 N ATOM 363 CA LEU A 90 24.735 -0.987 21.350 1.00 30.45 C ANISOU 363 CA LEU A 90 4669 2905 3997 -53 822 -220 C ATOM 364 C LEU A 90 23.903 -0.983 22.654 1.00 33.47 C ANISOU 364 C LEU A 90 4973 3335 4410 -67 710 -160 C ATOM 365 O LEU A 90 23.842 -2.003 23.345 1.00 34.64 O ANISOU 365 O LEU A 90 5107 3424 4630 -39 724 -128 O ATOM 366 CB LEU A 90 26.131 -0.369 21.582 1.00 30.53 C ANISOU 366 CB LEU A 90 4574 2956 4070 22 884 -172 C ATOM 367 CG LEU A 90 27.150 -0.513 20.443 1.00 35.71 C ANISOU 367 CG LEU A 90 5286 3556 4726 56 1030 -218 C ATOM 368 CD1 LEU A 90 28.384 0.312 20.732 1.00 36.26 C ANISOU 368 CD1 LEU A 90 5226 3689 4860 109 1070 -164 C ATOM 369 CD2 LEU A 90 27.499 -1.985 20.148 1.00 35.92 C ANISOU 369 CD2 LEU A 90 5380 3452 4816 105 1145 -249 C ATOM 370 N ALA A 91 23.229 0.133 22.927 1.00 28.53 N ANISOU 370 N ALA A 91 4304 2806 3729 -110 609 -145 N ATOM 371 CA ALA A 91 22.347 0.247 24.107 1.00 28.66 C ANISOU 371 CA ALA A 91 4256 2874 3759 -131 513 -98 C ATOM 372 C ALA A 91 21.154 -0.694 23.915 1.00 35.28 C ANISOU 372 C ALA A 91 5166 3651 4586 -193 488 -132 C ATOM 373 O ALA A 91 20.783 -1.363 24.864 1.00 36.76 O ANISOU 373 O ALA A 91 5321 3816 4828 -189 476 -90 O ATOM 374 CB ALA A 91 21.898 1.675 24.269 1.00 28.94 C ANISOU 374 CB ALA A 91 4251 3008 3736 -164 431 -91 C ATOM 375 N ASP A 92 20.603 -0.743 22.704 1.00 31.09 N ANISOU 375 N ASP A 92 4736 3094 3983 -256 484 -207 N ATOM 376 CA ASP A 92 19.479 -1.603 22.377 1.00 30.38 C ANISOU 376 CA ASP A 92 4716 2950 3877 -335 451 -254 C ATOM 377 C ASP A 92 19.852 -3.093 22.399 1.00 36.75 C ANISOU 377 C ASP A 92 5585 3627 4752 -320 542 -273 C ATOM 378 O ASP A 92 19.031 -3.892 22.836 1.00 37.58 O ANISOU 378 O ASP A 92 5697 3687 4896 -367 519 -269 O ATOM 379 CB ASP A 92 18.818 -1.158 21.070 1.00 31.50 C ANISOU 379 CB ASP A 92 4945 3115 3907 -410 401 -326 C ATOM 380 CG ASP A 92 17.969 0.108 21.245 1.00 41.81 C ANISOU 380 CG ASP A 92 6182 4536 5168 -436 289 -292 C ATOM 381 OD1 ASP A 92 17.809 0.579 22.411 1.00 43.25 O ANISOU 381 OD1 ASP A 92 6256 4773 5406 -403 257 -227 O ATOM 382 OD2 ASP A 92 17.450 0.616 20.238 1.00 44.58 O ANISOU 382 OD2 ASP A 92 6592 4921 5427 -485 234 -330 O ATOM 383 N VAL A 93 21.094 -3.454 22.048 1.00 33.34 N ANISOU 383 N VAL A 93 5183 3132 4351 -248 653 -282 N ATOM 384 CA VAL A 93 21.568 -4.844 22.117 1.00 33.56 C ANISOU 384 CA VAL A 93 5266 3022 4463 -211 757 -291 C ATOM 385 C VAL A 93 21.801 -5.254 23.584 1.00 38.01 C ANISOU 385 C VAL A 93 5727 3583 5132 -143 752 -182 C ATOM 386 O VAL A 93 21.493 -6.383 23.946 1.00 37.13 O ANISOU 386 O VAL A 93 5653 3370 5084 -150 785 -171 O ATOM 387 CB VAL A 93 22.785 -5.128 21.179 1.00 36.77 C ANISOU 387 CB VAL A 93 5741 3356 4875 -149 893 -339 C ATOM 388 CG1 VAL A 93 23.493 -6.432 21.534 1.00 36.06 C ANISOU 388 CG1 VAL A 93 5667 3128 4905 -70 1009 -316 C ATOM 389 CG2 VAL A 93 22.335 -5.179 19.728 1.00 36.66 C ANISOU 389 CG2 VAL A 93 5878 3308 4745 -234 909 -458 C ATOM 390 N LEU A 94 22.312 -4.331 24.424 1.00 37.01 N ANISOU 390 N LEU A 94 5478 3568 5018 -86 707 -103 N ATOM 391 CA LEU A 94 22.513 -4.569 25.860 1.00 37.46 C ANISOU 391 CA LEU A 94 5439 3648 5145 -29 683 4 C ATOM 392 C LEU A 94 21.158 -4.926 26.535 1.00 41.95 C ANISOU 392 C LEU A 94 6018 4216 5707 -104 617 22 C ATOM 393 O LEU A 94 21.086 -5.919 27.260 1.00 42.96 O ANISOU 393 O LEU A 94 6151 4269 5901 -82 648 78 O ATOM 394 CB LEU A 94 23.165 -3.329 26.533 1.00 37.12 C ANISOU 394 CB LEU A 94 5277 3740 5088 17 627 61 C ATOM 395 CG LEU A 94 23.242 -3.312 28.082 1.00 40.82 C ANISOU 395 CG LEU A 94 5651 4270 5590 58 572 167 C ATOM 396 CD1 LEU A 94 24.140 -4.446 28.629 1.00 41.20 C ANISOU 396 CD1 LEU A 94 5679 4240 5736 153 636 245 C ATOM 397 CD2 LEU A 94 23.659 -1.947 28.603 1.00 39.01 C ANISOU 397 CD2 LEU A 94 5326 4175 5319 67 505 191 C ATOM 398 N ALA A 95 20.105 -4.179 26.206 1.00 36.75 N ANISOU 398 N ALA A 95 5359 3633 4973 -190 536 -22 N ATOM 399 CA ALA A 95 18.755 -4.398 26.772 1.00 35.94 C ANISOU 399 CA ALA A 95 5248 3541 4868 -268 478 -11 C ATOM 400 C ALA A 95 18.144 -5.697 26.233 1.00 39.07 C ANISOU 400 C ALA A 95 5742 3804 5299 -337 520 -64 C ATOM 401 O ALA A 95 17.619 -6.461 27.026 1.00 37.51 O ANISOU 401 O ALA A 95 5538 3555 5157 -357 533 -15 O ATOM 402 CB ALA A 95 17.883 -3.213 26.457 1.00 36.22 C ANISOU 402 CB ALA A 95 5248 3685 4828 -330 387 -45 C ATOM 403 N THR A 96 18.205 -5.908 24.920 1.00 36.27 N ANISOU 403 N THR A 96 5486 3389 4906 -377 549 -162 N ATOM 404 CA THR A 96 17.665 -7.106 24.255 1.00 36.50 C ANISOU 404 CA THR A 96 5627 3285 4955 -457 589 -237 C ATOM 405 C THR A 96 18.334 -8.409 24.691 1.00 40.46 C ANISOU 405 C THR A 96 6175 3637 5560 -396 701 -201 C ATOM 406 O THR A 96 17.632 -9.382 24.969 1.00 41.15 O ANISOU 406 O THR A 96 6303 3629 5702 -459 718 -202 O ATOM 407 CB THR A 96 17.699 -6.949 22.723 1.00 40.36 C ANISOU 407 CB THR A 96 6224 3758 5355 -511 592 -357 C ATOM 408 OG1 THR A 96 17.061 -5.718 22.385 1.00 37.27 O ANISOU 408 OG1 THR A 96 5784 3506 4873 -555 481 -368 O ATOM 409 CG2 THR A 96 17.001 -8.111 21.991 1.00 38.07 C ANISOU 409 CG2 THR A 96 6059 3341 5066 -621 614 -455 C ATOM 410 N ALA A 97 19.667 -8.441 24.729 1.00 36.80 N ANISOU 410 N ALA A 97 5702 3147 5133 -276 781 -167 N ATOM 411 CA ALA A 97 20.403 -9.650 25.079 1.00 37.23 C ANISOU 411 CA ALA A 97 5796 3054 5296 -197 894 -123 C ATOM 412 C ALA A 97 20.334 -10.052 26.562 1.00 42.32 C ANISOU 412 C ALA A 97 6363 3699 6017 -147 880 14 C ATOM 413 O ALA A 97 20.097 -11.219 26.852 1.00 41.85 O ANISOU 413 O ALA A 97 6364 3502 6035 -156 941 38 O ATOM 414 CB ALA A 97 21.857 -9.536 24.628 1.00 38.09 C ANISOU 414 CB ALA A 97 5899 3141 5430 -77 984 -122 C ATOM 415 N ILE A 98 20.539 -9.100 27.491 1.00 39.39 N ANISOU 415 N ILE A 98 5871 3477 5620 -98 805 102 N ATOM 416 CA ILE A 98 20.625 -9.388 28.925 1.00 38.61 C ANISOU 416 CA ILE A 98 5704 3396 5569 -40 791 238 C ATOM 417 C ILE A 98 19.332 -9.128 29.697 1.00 39.61 C ANISOU 417 C ILE A 98 5800 3592 5658 -133 716 267 C ATOM 418 O ILE A 98 18.999 -9.912 30.581 1.00 39.62 O ANISOU 418 O ILE A 98 5811 3535 5709 -132 741 350 O ATOM 419 CB ILE A 98 21.849 -8.613 29.535 1.00 42.26 C ANISOU 419 CB ILE A 98 6057 3971 6028 78 764 320 C ATOM 420 CG1 ILE A 98 23.183 -9.197 29.013 1.00 42.86 C ANISOU 420 CG1 ILE A 98 6146 3955 6185 189 862 326 C ATOM 421 CG2 ILE A 98 21.859 -8.622 31.070 1.00 42.80 C ANISOU 421 CG2 ILE A 98 6052 4107 6104 123 715 458 C ATOM 422 CD1 ILE A 98 23.873 -8.312 28.127 1.00 57.38 C ANISOU 422 CD1 ILE A 98 7959 5858 7983 203 868 253 C ATOM 423 N CYS A 99 18.616 -8.045 29.395 1.00 33.67 N ANISOU 423 N CYS A 99 5008 2961 4823 -205 635 208 N ATOM 424 CA CYS A 99 17.430 -7.639 30.151 1.00 31.95 C ANISOU 424 CA CYS A 99 4738 2825 4574 -278 571 238 C ATOM 425 C CYS A 99 16.095 -8.199 29.630 1.00 34.25 C ANISOU 425 C CYS A 99 5080 3054 4881 -410 566 170 C ATOM 426 O CYS A 99 15.254 -8.540 30.458 1.00 32.67 O ANISOU 426 O CYS A 99 4853 2854 4707 -458 565 225 O ATOM 427 CB CYS A 99 17.389 -6.121 30.279 1.00 31.52 C ANISOU 427 CB CYS A 99 4602 2935 4440 -271 490 228 C ATOM 428 SG CYS A 99 18.949 -5.390 30.850 1.00 34.90 S ANISOU 428 SG CYS A 99 4963 3446 4852 -141 484 294 S ATOM 429 N LEU A 100 15.893 -8.297 28.292 1.00 31.06 N ANISOU 429 N LEU A 100 4744 2603 4456 -475 561 54 N ATOM 430 CA LEU A 100 14.644 -8.802 27.692 1.00 31.04 C ANISOU 430 CA LEU A 100 4783 2549 4462 -615 537 -22 C ATOM 431 C LEU A 100 14.250 -10.206 28.227 1.00 37.26 C ANISOU 431 C LEU A 100 5621 3189 5345 -660 611 15 C ATOM 432 O LEU A 100 13.100 -10.330 28.659 1.00 37.32 O ANISOU 432 O LEU A 100 5587 3217 5377 -754 581 30 O ATOM 433 CB LEU A 100 14.681 -8.746 26.142 1.00 30.72 C ANISOU 433 CB LEU A 100 4829 2478 4365 -671 520 -155 C ATOM 434 CG LEU A 100 13.423 -9.156 25.346 1.00 34.19 C ANISOU 434 CG LEU A 100 5312 2885 4794 -829 468 -250 C ATOM 435 CD1 LEU A 100 13.457 -8.556 23.983 1.00 33.88 C ANISOU 435 CD1 LEU A 100 5326 2894 4652 -867 410 -356 C ATOM 436 CD2 LEU A 100 13.304 -10.689 25.186 1.00 34.39 C ANISOU 436 CD2 LEU A 100 5448 2721 4898 -892 554 -290 C ATOM 437 N PRO A 101 15.140 -11.253 28.244 1.00 34.64 N ANISOU 437 N PRO A 101 5375 2707 5080 -593 712 37 N ATOM 438 CA PRO A 101 14.732 -12.559 28.808 1.00 34.79 C ANISOU 438 CA PRO A 101 5448 2575 5196 -635 788 84 C ATOM 439 C PRO A 101 14.301 -12.527 30.287 1.00 39.61 C ANISOU 439 C PRO A 101 5977 3241 5831 -618 783 224 C ATOM 440 O PRO A 101 13.334 -13.191 30.624 1.00 40.52 O ANISOU 440 O PRO A 101 6103 3293 5999 -718 805 238 O ATOM 441 CB PRO A 101 15.968 -13.444 28.585 1.00 36.52 C ANISOU 441 CB PRO A 101 5758 2639 5478 -527 897 98 C ATOM 442 CG PRO A 101 16.725 -12.775 27.470 1.00 40.34 C ANISOU 442 CG PRO A 101 6264 3171 5894 -485 884 2 C ATOM 443 CD PRO A 101 16.537 -11.316 27.761 1.00 35.95 C ANISOU 443 CD PRO A 101 5587 2825 5248 -475 774 26 C ATOM 444 N ALA A 102 14.981 -11.735 31.153 1.00 36.62 N ANISOU 444 N ALA A 102 5519 2984 5409 -502 756 320 N ATOM 445 CA ALA A 102 14.641 -11.575 32.577 1.00 35.59 C ANISOU 445 CA ALA A 102 5323 2928 5272 -480 750 449 C ATOM 446 C ALA A 102 13.288 -10.895 32.749 1.00 39.72 C ANISOU 446 C ALA A 102 5771 3561 5759 -592 691 419 C ATOM 447 O ALA A 102 12.500 -11.323 33.598 1.00 39.47 O ANISOU 447 O ALA A 102 5724 3514 5760 -644 725 489 O ATOM 448 CB ALA A 102 15.711 -10.796 33.314 1.00 36.17 C ANISOU 448 CB ALA A 102 5336 3117 5290 -344 719 532 C ATOM 449 N SER A 103 12.999 -9.873 31.921 1.00 35.30 N ANISOU 449 N SER A 103 5167 3106 5140 -627 612 321 N ATOM 450 CA SER A 103 11.739 -9.131 31.937 1.00 34.63 C ANISOU 450 CA SER A 103 4998 3131 5030 -720 549 288 C ATOM 451 C SER A 103 10.579 -10.023 31.452 1.00 39.19 C ANISOU 451 C SER A 103 5597 3614 5678 -868 562 234 C ATOM 452 O SER A 103 9.500 -9.972 32.025 1.00 37.45 O ANISOU 452 O SER A 103 5305 3438 5486 -942 560 266 O ATOM 453 CB SER A 103 11.861 -7.848 31.117 1.00 38.26 C ANISOU 453 CB SER A 103 5415 3710 5413 -704 463 210 C ATOM 454 OG SER A 103 10.600 -7.240 30.894 1.00 50.10 O ANISOU 454 OG SER A 103 6834 5297 6905 -792 400 172 O ATOM 455 N LEU A 104 10.801 -10.855 30.417 1.00 38.06 N ANISOU 455 N LEU A 104 5554 3340 5567 -916 583 149 N ATOM 456 CA LEU A 104 9.785 -11.801 29.931 1.00 38.22 C ANISOU 456 CA LEU A 104 5610 3253 5657 -1070 594 86 C ATOM 457 C LEU A 104 9.438 -12.841 31.035 1.00 44.94 C ANISOU 457 C LEU A 104 6476 3999 6601 -1097 692 190 C ATOM 458 O LEU A 104 8.258 -13.145 31.216 1.00 44.97 O ANISOU 458 O LEU A 104 6430 3998 6661 -1225 689 186 O ATOM 459 CB LEU A 104 10.248 -12.483 28.620 1.00 37.76 C ANISOU 459 CB LEU A 104 5682 3066 5599 -1107 608 -35 C ATOM 460 CG LEU A 104 9.522 -13.751 28.134 1.00 41.77 C ANISOU 460 CG LEU A 104 6273 3410 6187 -1259 646 -108 C ATOM 461 CD1 LEU A 104 8.046 -13.486 27.801 1.00 41.36 C ANISOU 461 CD1 LEU A 104 6133 3439 6143 -1426 551 -167 C ATOM 462 CD2 LEU A 104 10.241 -14.369 26.948 1.00 43.38 C ANISOU 462 CD2 LEU A 104 6628 3482 6374 -1264 681 -225 C ATOM 463 N LEU A 105 10.444 -13.341 31.789 1.00 42.57 N ANISOU 463 N LEU A 105 6233 3623 6320 -977 774 291 N ATOM 464 CA LEU A 105 10.199 -14.286 32.877 1.00 43.09 C ANISOU 464 CA LEU A 105 6322 3589 6460 -987 868 410 C ATOM 465 C LEU A 105 9.450 -13.672 34.054 1.00 46.03 C ANISOU 465 C LEU A 105 6586 4097 6806 -998 860 506 C ATOM 466 O LEU A 105 8.637 -14.361 34.651 1.00 46.91 O ANISOU 466 O LEU A 105 6692 4146 6984 -1086 922 560 O ATOM 467 CB LEU A 105 11.476 -14.974 33.346 1.00 43.95 C ANISOU 467 CB LEU A 105 6519 3586 6595 -847 948 505 C ATOM 468 CG LEU A 105 11.830 -16.217 32.557 1.00 51.01 C ANISOU 468 CG LEU A 105 7546 4259 7577 -874 1025 444 C ATOM 469 CD1 LEU A 105 13.309 -16.431 32.532 1.00 52.51 C ANISOU 469 CD1 LEU A 105 7794 4386 7771 -706 1069 490 C ATOM 470 CD2 LEU A 105 11.133 -17.451 33.119 1.00 54.34 C ANISOU 470 CD2 LEU A 105 8025 4515 8106 -966 1121 508 C ATOM 471 N VAL A 106 9.695 -12.397 34.382 1.00 40.94 N ANISOU 471 N VAL A 106 5858 3629 6066 -915 794 523 N ATOM 472 CA VAL A 106 8.979 -11.705 35.463 1.00 39.65 C ANISOU 472 CA VAL A 106 5598 3600 5866 -921 793 598 C ATOM 473 C VAL A 106 7.522 -11.489 35.021 1.00 46.05 C ANISOU 473 C VAL A 106 6320 4455 6722 -1068 762 525 C ATOM 474 O VAL A 106 6.612 -11.750 35.794 1.00 46.52 O ANISOU 474 O VAL A 106 6329 4521 6824 -1135 818 587 O ATOM 475 CB VAL A 106 9.669 -10.376 35.892 1.00 41.31 C ANISOU 475 CB VAL A 106 5756 3976 5965 -799 734 619 C ATOM 476 CG1 VAL A 106 8.815 -9.608 36.884 1.00 41.21 C ANISOU 476 CG1 VAL A 106 5651 4096 5912 -816 741 670 C ATOM 477 CG2 VAL A 106 11.041 -10.634 36.488 1.00 40.58 C ANISOU 477 CG2 VAL A 106 5727 3853 5836 -663 759 709 C ATOM 478 N ASP A 107 7.304 -11.052 33.771 1.00 44.01 N ANISOU 478 N ASP A 107 6040 4226 6457 -1119 673 399 N ATOM 479 CA ASP A 107 5.963 -10.798 33.249 1.00 43.93 C ANISOU 479 CA ASP A 107 5930 4271 6489 -1254 618 330 C ATOM 480 C ASP A 107 5.131 -12.087 33.110 1.00 49.64 C ANISOU 480 C ASP A 107 6679 4856 7327 -1407 671 315 C ATOM 481 O ASP A 107 3.913 -12.034 33.261 1.00 50.08 O ANISOU 481 O ASP A 107 6627 4959 7443 -1519 663 312 O ATOM 482 CB ASP A 107 6.021 -9.972 31.946 1.00 45.53 C ANISOU 482 CB ASP A 107 6113 4551 6636 -1259 497 212 C ATOM 483 CG ASP A 107 6.526 -8.535 32.137 1.00 53.42 C ANISOU 483 CG ASP A 107 7056 5702 7540 -1135 445 229 C ATOM 484 OD1 ASP A 107 6.642 -8.091 33.300 1.00 52.71 O ANISOU 484 OD1 ASP A 107 6925 5676 7426 -1060 493 319 O ATOM 485 OD2 ASP A 107 6.806 -7.861 31.125 1.00 56.03 O ANISOU 485 OD2 ASP A 107 7391 6083 7815 -1117 359 150 O ATOM 486 N ILE A 108 5.784 -13.246 32.899 1.00 47.14 N ANISOU 486 N ILE A 108 6498 4362 7050 -1412 737 313 N ATOM 487 CA ILE A 108 5.107 -14.545 32.793 1.00 47.52 C ANISOU 487 CA ILE A 108 6594 4248 7213 -1559 802 298 C ATOM 488 C ILE A 108 4.840 -15.172 34.161 1.00 50.65 C ANISOU 488 C ILE A 108 6989 4586 7668 -1557 926 444 C ATOM 489 O ILE A 108 3.712 -15.583 34.424 1.00 51.30 O ANISOU 489 O ILE A 108 7006 4649 7837 -1694 962 457 O ATOM 490 CB ILE A 108 5.880 -15.523 31.857 1.00 51.36 C ANISOU 490 CB ILE A 108 7242 4551 7723 -1572 825 214 C ATOM 491 CG1 ILE A 108 5.870 -15.036 30.389 1.00 52.84 C ANISOU 491 CG1 ILE A 108 7438 4788 7852 -1623 706 55 C ATOM 492 CG2 ILE A 108 5.425 -16.985 31.979 1.00 51.81 C ANISOU 492 CG2 ILE A 108 7381 4399 7904 -1697 927 223 C ATOM 493 CD1 ILE A 108 4.519 -15.209 29.526 1.00 66.36 C ANISOU 493 CD1 ILE A 108 9092 6510 9612 -1834 622 -62 C ATOM 494 N THR A 109 5.882 -15.285 35.000 1.00 44.92 N ANISOU 494 N THR A 109 6337 3833 6898 -1407 991 557 N ATOM 495 CA THR A 109 5.843 -15.975 36.288 1.00 43.68 C ANISOU 495 CA THR A 109 6214 3606 6776 -1386 1111 711 C ATOM 496 C THR A 109 5.445 -15.121 37.495 1.00 46.21 C ANISOU 496 C THR A 109 6435 4094 7030 -1338 1128 814 C ATOM 497 O THR A 109 5.102 -15.685 38.530 1.00 46.14 O ANISOU 497 O THR A 109 6443 4038 7049 -1358 1233 934 O ATOM 498 CB THR A 109 7.196 -16.665 36.555 1.00 43.91 C ANISOU 498 CB THR A 109 6380 3509 6794 -1247 1167 790 C ATOM 499 OG1 THR A 109 8.153 -15.692 36.987 1.00 41.75 O ANISOU 499 OG1 THR A 109 6081 3379 6402 -1083 1112 837 O ATOM 500 CG2 THR A 109 7.723 -17.449 35.339 1.00 35.83 C ANISOU 500 CG2 THR A 109 5468 2313 5832 -1271 1168 681 C ATOM 501 N GLU A 110 5.531 -13.792 37.388 1.00 42.45 N ANISOU 501 N GLU A 110 5869 3800 6460 -1273 1038 770 N ATOM 502 CA GLU A 110 5.254 -12.857 38.493 1.00 42.29 C ANISOU 502 CA GLU A 110 5767 3940 6361 -1215 1056 848 C ATOM 503 C GLU A 110 6.245 -13.091 39.650 1.00 47.24 C ANISOU 503 C GLU A 110 6485 4555 6908 -1083 1115 989 C ATOM 504 O GLU A 110 5.908 -12.900 40.818 1.00 47.90 O ANISOU 504 O GLU A 110 6549 4709 6942 -1065 1181 1090 O ATOM 505 CB GLU A 110 3.777 -12.876 38.958 1.00 43.39 C ANISOU 505 CB GLU A 110 5798 4116 6571 -1344 1119 870 C ATOM 506 CG GLU A 110 2.759 -12.670 37.849 1.00 54.13 C ANISOU 506 CG GLU A 110 7046 5506 8013 -1475 1043 742 C ATOM 507 CD GLU A 110 1.318 -12.493 38.289 1.00 83.14 C ANISOU 507 CD GLU A 110 10578 9245 11767 -1590 1097 763 C ATOM 508 OE1 GLU A 110 0.886 -13.175 39.248 1.00 84.44 O ANISOU 508 OE1 GLU A 110 10759 9347 11978 -1636 1226 866 O ATOM 509 OE2 GLU A 110 0.611 -11.676 37.655 1.00 81.52 O ANISOU 509 OE2 GLU A 110 10240 9151 11584 -1632 1012 681 O ATOM 510 N SER A 111 7.482 -13.512 39.309 1.00 43.29 N ANISOU 510 N SER A 111 6084 3970 6395 -988 1092 998 N ATOM 511 CA SER A 111 8.550 -13.755 40.283 1.00 42.44 C ANISOU 511 CA SER A 111 6055 3852 6217 -853 1124 1133 C ATOM 512 C SER A 111 9.946 -13.518 39.710 1.00 44.29 C ANISOU 512 C SER A 111 6330 4086 6413 -726 1049 1100 C ATOM 513 O SER A 111 10.136 -13.609 38.492 1.00 44.01 O ANISOU 513 O SER A 111 6303 3991 6428 -752 1008 982 O ATOM 514 CB SER A 111 8.453 -15.170 40.842 1.00 45.33 C ANISOU 514 CB SER A 111 6518 4041 6663 -883 1239 1252 C ATOM 515 OG SER A 111 8.595 -16.137 39.819 1.00 51.64 O ANISOU 515 OG SER A 111 7383 4656 7581 -936 1257 1182 O ATOM 516 N TRP A 112 10.917 -13.216 40.598 1.00 39.30 N ANISOU 516 N TRP A 112 5719 3525 5688 -593 1032 1206 N ATOM 517 CA TRP A 112 12.321 -13.002 40.251 1.00 38.71 C ANISOU 517 CA TRP A 112 5666 3460 5583 -464 968 1201 C ATOM 518 C TRP A 112 13.082 -14.320 40.404 1.00 43.03 C ANISOU 518 C TRP A 112 6312 3832 6206 -395 1033 1307 C ATOM 519 O TRP A 112 13.243 -14.819 41.523 1.00 43.57 O ANISOU 519 O TRP A 112 6423 3883 6247 -347 1079 1462 O ATOM 520 CB TRP A 112 12.959 -11.897 41.109 1.00 36.79 C ANISOU 520 CB TRP A 112 5376 3401 5202 -367 898 1249 C ATOM 521 CG TRP A 112 14.348 -11.572 40.655 1.00 37.08 C ANISOU 521 CG TRP A 112 5407 3461 5220 -251 826 1229 C ATOM 522 CD1 TRP A 112 15.516 -11.996 41.213 1.00 39.69 C ANISOU 522 CD1 TRP A 112 5770 3772 5537 -128 815 1346 C ATOM 523 CD2 TRP A 112 14.704 -10.853 39.469 1.00 37.12 C ANISOU 523 CD2 TRP A 112 5369 3500 5236 -250 763 1089 C ATOM 524 NE1 TRP A 112 16.584 -11.531 40.483 1.00 39.47 N ANISOU 524 NE1 TRP A 112 5707 3773 5516 -52 752 1283 N ATOM 525 CE2 TRP A 112 16.116 -10.824 39.405 1.00 40.93 C ANISOU 525 CE2 TRP A 112 5853 3988 5711 -126 725 1125 C ATOM 526 CE3 TRP A 112 13.965 -10.161 38.487 1.00 38.37 C ANISOU 526 CE3 TRP A 112 5481 3695 5402 -338 731 945 C ATOM 527 CZ2 TRP A 112 16.808 -10.161 38.378 1.00 40.32 C ANISOU 527 CZ2 TRP A 112 5739 3943 5637 -96 673 1017 C ATOM 528 CZ3 TRP A 112 14.648 -9.497 37.476 1.00 39.82 C ANISOU 528 CZ3 TRP A 112 5641 3912 5576 -304 671 844 C ATOM 529 CH2 TRP A 112 16.055 -9.496 37.429 1.00 40.47 C ANISOU 529 CH2 TRP A 112 5730 3993 5652 -187 650 878 C ATOM 530 N LEU A 113 13.538 -14.882 39.288 1.00 40.17 N ANISOU 530 N LEU A 113 5992 3336 5936 -388 1043 1227 N ATOM 531 CA LEU A 113 14.218 -16.185 39.282 1.00 41.38 C ANISOU 531 CA LEU A 113 6244 3293 6186 -322 1121 1313 C ATOM 532 C LEU A 113 15.729 -16.141 39.095 1.00 45.71 C ANISOU 532 C LEU A 113 6795 3840 6734 -159 1086 1344 C ATOM 533 O LEU A 113 16.323 -17.200 38.868 1.00 46.00 O ANISOU 533 O LEU A 113 6908 3699 6872 -96 1155 1389 O ATOM 534 CB LEU A 113 13.603 -17.087 38.184 1.00 41.80 C ANISOU 534 CB LEU A 113 6364 3153 6364 -440 1190 1201 C ATOM 535 CG LEU A 113 12.081 -17.239 38.137 1.00 46.48 C ANISOU 535 CG LEU A 113 6938 3734 6988 -624 1219 1145 C ATOM 536 CD1 LEU A 113 11.660 -17.959 36.867 1.00 46.76 C ANISOU 536 CD1 LEU A 113 7031 3609 7127 -742 1249 998 C ATOM 537 CD2 LEU A 113 11.543 -17.938 39.382 1.00 46.18 C ANISOU 537 CD2 LEU A 113 6935 3641 6972 -651 1309 1305 C ATOM 538 N PHE A 114 16.363 -14.952 39.227 1.00 42.00 N ANISOU 538 N PHE A 114 6239 3558 6160 -88 986 1327 N ATOM 539 CA PHE A 114 17.789 -14.798 38.937 1.00 41.47 C ANISOU 539 CA PHE A 114 6149 3505 6102 53 947 1341 C ATOM 540 C PHE A 114 18.713 -14.510 40.138 1.00 45.22 C ANISOU 540 C PHE A 114 6581 4099 6501 183 887 1499 C ATOM 541 O PHE A 114 19.915 -14.316 39.940 1.00 44.71 O ANISOU 541 O PHE A 114 6473 4062 6451 299 846 1516 O ATOM 542 CB PHE A 114 17.963 -13.728 37.849 1.00 43.28 C ANISOU 542 CB PHE A 114 6316 3831 6297 25 882 1173 C ATOM 543 CG PHE A 114 17.229 -14.090 36.580 1.00 45.12 C ANISOU 543 CG PHE A 114 6600 3946 6597 -90 928 1022 C ATOM 544 CD1 PHE A 114 17.781 -14.986 35.670 1.00 49.22 C ANISOU 544 CD1 PHE A 114 7195 4290 7218 -59 1000 974 C ATOM 545 CD2 PHE A 114 15.970 -13.567 36.313 1.00 47.72 C ANISOU 545 CD2 PHE A 114 6904 4339 6888 -231 901 928 C ATOM 546 CE1 PHE A 114 17.086 -15.356 34.521 1.00 50.56 C ANISOU 546 CE1 PHE A 114 7427 4351 7433 -178 1037 828 C ATOM 547 CE2 PHE A 114 15.272 -13.945 35.167 1.00 50.91 C ANISOU 547 CE2 PHE A 114 7354 4643 7347 -346 926 794 C ATOM 548 CZ PHE A 114 15.843 -14.824 34.272 1.00 49.29 C ANISOU 548 CZ PHE A 114 7236 4268 7224 -324 990 740 C ATOM 549 N GLY A 115 18.188 -14.569 41.354 1.00 42.05 N ANISOU 549 N GLY A 115 6196 3757 6025 164 888 1617 N ATOM 550 CA GLY A 115 18.993 -14.333 42.548 1.00 42.10 C ANISOU 550 CA GLY A 115 6176 3883 5937 274 821 1771 C ATOM 551 C GLY A 115 19.171 -12.876 42.926 1.00 46.33 C ANISOU 551 C GLY A 115 6627 4648 6330 268 709 1718 C ATOM 552 O GLY A 115 18.782 -11.976 42.177 1.00 46.54 O ANISOU 552 O GLY A 115 6605 4739 6339 195 682 1562 O ATOM 553 N HIS A 116 19.773 -12.645 44.101 1.00 42.69 N ANISOU 553 N HIS A 116 6152 4308 5760 343 641 1850 N ATOM 554 CA HIS A 116 20.015 -11.337 44.712 1.00 42.58 C ANISOU 554 CA HIS A 116 6075 4509 5594 339 534 1820 C ATOM 555 C HIS A 116 20.926 -10.421 43.902 1.00 43.14 C ANISOU 555 C HIS A 116 6052 4659 5681 374 452 1707 C ATOM 556 O HIS A 116 20.561 -9.265 43.677 1.00 42.35 O ANISOU 556 O HIS A 116 5909 4671 5512 306 411 1583 O ATOM 557 CB HIS A 116 20.533 -11.506 46.143 1.00 44.50 C ANISOU 557 CB HIS A 116 6343 4846 5718 412 478 2000 C ATOM 558 CG HIS A 116 19.541 -12.177 47.051 1.00 49.20 C ANISOU 558 CG HIS A 116 7036 5397 6261 361 563 2109 C ATOM 559 ND1 HIS A 116 18.723 -11.442 47.894 1.00 51.61 N ANISOU 559 ND1 HIS A 116 7362 5836 6412 283 562 2094 N ATOM 560 CD2 HIS A 116 19.243 -13.494 47.197 1.00 51.79 C ANISOU 560 CD2 HIS A 116 7448 5555 6677 375 663 2228 C ATOM 561 CE1 HIS A 116 17.967 -12.327 48.529 1.00 51.26 C ANISOU 561 CE1 HIS A 116 7407 5708 6364 251 662 2208 C ATOM 562 NE2 HIS A 116 18.243 -13.575 48.143 1.00 51.67 N ANISOU 562 NE2 HIS A 116 7500 5573 6559 301 723 2294 N ATOM 563 N ALA A 117 22.098 -10.919 43.464 1.00 38.22 N ANISOU 563 N ALA A 117 5394 3972 5155 483 436 1752 N ATOM 564 CA ALA A 117 23.072 -10.151 42.674 1.00 36.76 C ANISOU 564 CA ALA A 117 5114 3851 5003 524 373 1658 C ATOM 565 C ALA A 117 22.471 -9.599 41.386 1.00 41.31 C ANISOU 565 C ALA A 117 5686 4389 5623 433 415 1470 C ATOM 566 O ALA A 117 22.613 -8.406 41.126 1.00 42.36 O ANISOU 566 O ALA A 117 5757 4643 5696 399 353 1369 O ATOM 567 CB ALA A 117 24.309 -10.997 42.364 1.00 36.58 C ANISOU 567 CB ALA A 117 5058 3737 5104 660 382 1748 C ATOM 568 N LEU A 118 21.759 -10.447 40.609 1.00 37.27 N ANISOU 568 N LEU A 118 5244 3709 5208 388 518 1424 N ATOM 569 CA LEU A 118 21.151 -10.024 39.341 1.00 36.14 C ANISOU 569 CA LEU A 118 5105 3527 5098 298 549 1252 C ATOM 570 C LEU A 118 19.940 -9.119 39.532 1.00 39.12 C ANISOU 570 C LEU A 118 5477 4004 5382 180 525 1172 C ATOM 571 O LEU A 118 19.587 -8.393 38.606 1.00 39.22 O ANISOU 571 O LEU A 118 5468 4042 5392 119 513 1038 O ATOM 572 CB LEU A 118 20.846 -11.206 38.409 1.00 35.61 C ANISOU 572 CB LEU A 118 5118 3254 5158 280 655 1216 C ATOM 573 CG LEU A 118 22.085 -11.961 37.858 1.00 38.92 C ANISOU 573 CG LEU A 118 5538 3559 5689 401 700 1252 C ATOM 574 CD1 LEU A 118 21.671 -13.139 36.999 1.00 38.62 C ANISOU 574 CD1 LEU A 118 5602 3304 5767 371 816 1206 C ATOM 575 CD2 LEU A 118 23.013 -11.053 37.079 1.00 37.59 C ANISOU 575 CD2 LEU A 118 5290 3474 5517 443 657 1164 C ATOM 576 N CYS A 119 19.350 -9.094 40.742 1.00 35.27 N ANISOU 576 N CYS A 119 5007 3583 4813 156 518 1259 N ATOM 577 CA CYS A 119 18.254 -8.180 41.064 1.00 34.99 C ANISOU 577 CA CYS A 119 4956 3650 4688 60 505 1195 C ATOM 578 C CYS A 119 18.802 -6.723 41.115 1.00 37.52 C ANISOU 578 C CYS A 119 5206 4132 4919 75 414 1127 C ATOM 579 O CYS A 119 18.065 -5.777 40.860 1.00 36.24 O ANISOU 579 O CYS A 119 5018 4037 4715 6 402 1029 O ATOM 580 CB CYS A 119 17.553 -8.587 42.359 1.00 35.48 C ANISOU 580 CB CYS A 119 5064 3733 4685 37 543 1310 C ATOM 581 SG CYS A 119 16.335 -7.387 42.955 1.00 40.05 S ANISOU 581 SG CYS A 119 5615 4452 5150 -59 542 1244 S ATOM 582 N LYS A 120 20.114 -6.554 41.372 1.00 33.97 N ANISOU 582 N LYS A 120 4718 3734 4455 166 351 1176 N ATOM 583 CA LYS A 120 20.739 -5.232 41.317 1.00 33.33 C ANISOU 583 CA LYS A 120 4569 3788 4307 171 267 1105 C ATOM 584 C LYS A 120 21.272 -4.946 39.909 1.00 34.47 C ANISOU 584 C LYS A 120 4674 3885 4537 180 270 1000 C ATOM 585 O LYS A 120 20.999 -3.881 39.385 1.00 33.98 O ANISOU 585 O LYS A 120 4585 3880 4444 129 247 891 O ATOM 586 CB LYS A 120 21.845 -5.078 42.371 1.00 34.98 C ANISOU 586 CB LYS A 120 4745 4104 4443 244 184 1208 C ATOM 587 CG LYS A 120 21.260 -4.828 43.736 1.00 35.71 C ANISOU 587 CG LYS A 120 4882 4289 4399 212 169 1271 C ATOM 588 CD LYS A 120 22.308 -4.652 44.786 1.00 39.66 C ANISOU 588 CD LYS A 120 5354 4917 4798 266 66 1356 C ATOM 589 CE LYS A 120 21.674 -4.451 46.143 1.00 47.90 C ANISOU 589 CE LYS A 120 6464 6047 5687 234 60 1424 C ATOM 590 NZ LYS A 120 21.100 -3.086 46.285 1.00 46.83 N ANISOU 590 NZ LYS A 120 6324 6029 5441 160 33 1305 N ATOM 591 N VAL A 121 21.968 -5.926 39.285 1.00 29.96 N ANISOU 591 N VAL A 121 4111 3200 4073 245 310 1035 N ATOM 592 CA VAL A 121 22.650 -5.826 37.986 1.00 28.97 C ANISOU 592 CA VAL A 121 3959 3019 4028 268 332 950 C ATOM 593 C VAL A 121 21.692 -5.643 36.785 1.00 33.38 C ANISOU 593 C VAL A 121 4563 3513 4607 178 379 818 C ATOM 594 O VAL A 121 21.934 -4.736 35.995 1.00 32.08 O ANISOU 594 O VAL A 121 4366 3395 4428 158 357 724 O ATOM 595 CB VAL A 121 23.632 -7.010 37.783 1.00 32.14 C ANISOU 595 CB VAL A 121 4365 3307 4541 372 380 1032 C ATOM 596 CG1 VAL A 121 24.249 -7.017 36.382 1.00 31.57 C ANISOU 596 CG1 VAL A 121 4282 3160 4553 394 432 938 C ATOM 597 CG2 VAL A 121 24.729 -6.992 38.846 1.00 31.88 C ANISOU 597 CG2 VAL A 121 4261 3364 4488 468 308 1163 C ATOM 598 N ILE A 122 20.646 -6.494 36.620 1.00 31.12 N ANISOU 598 N ILE A 122 4347 3121 4355 122 439 813 N ATOM 599 CA ILE A 122 19.711 -6.397 35.479 1.00 30.91 C ANISOU 599 CA ILE A 122 4358 3039 4346 30 467 692 C ATOM 600 C ILE A 122 18.903 -5.059 35.523 1.00 34.47 C ANISOU 600 C ILE A 122 4768 3617 4714 -41 408 622 C ATOM 601 O ILE A 122 18.988 -4.338 34.527 1.00 34.18 O ANISOU 601 O ILE A 122 4719 3600 4668 -63 389 528 O ATOM 602 CB ILE A 122 18.834 -7.673 35.285 1.00 33.92 C ANISOU 602 CB ILE A 122 4818 3275 4795 -26 539 700 C ATOM 603 CG1 ILE A 122 19.724 -8.847 34.785 1.00 33.93 C ANISOU 603 CG1 ILE A 122 4872 3125 4894 47 610 728 C ATOM 604 CG2 ILE A 122 17.632 -7.410 34.333 1.00 33.70 C ANISOU 604 CG2 ILE A 122 4811 3229 4763 -144 537 580 C ATOM 605 CD1 ILE A 122 19.123 -10.240 34.904 1.00 44.94 C ANISOU 605 CD1 ILE A 122 6350 4360 6365 14 689 772 C ATOM 606 N PRO A 123 18.214 -4.633 36.631 1.00 30.68 N ANISOU 606 N PRO A 123 4265 3223 4168 -68 385 667 N ATOM 607 CA PRO A 123 17.555 -3.304 36.619 1.00 29.24 C ANISOU 607 CA PRO A 123 4042 3149 3920 -118 342 597 C ATOM 608 C PRO A 123 18.519 -2.157 36.320 1.00 30.72 C ANISOU 608 C PRO A 123 4185 3418 4069 -79 288 552 C ATOM 609 O PRO A 123 18.146 -1.205 35.632 1.00 30.28 O ANISOU 609 O PRO A 123 4112 3400 3994 -116 265 468 O ATOM 610 CB PRO A 123 16.966 -3.184 38.026 1.00 30.89 C ANISOU 610 CB PRO A 123 4244 3427 4065 -130 346 668 C ATOM 611 CG PRO A 123 16.748 -4.604 38.443 1.00 35.33 C ANISOU 611 CG PRO A 123 4857 3889 4677 -128 405 757 C ATOM 612 CD PRO A 123 17.947 -5.331 37.909 1.00 31.29 C ANISOU 612 CD PRO A 123 4365 3297 4228 -55 409 783 C ATOM 613 N TYR A 124 19.764 -2.269 36.800 1.00 25.89 N ANISOU 613 N TYR A 124 3552 2831 3454 -5 267 612 N ATOM 614 CA TYR A 124 20.820 -1.293 36.556 1.00 25.38 C ANISOU 614 CA TYR A 124 3435 2839 3369 28 220 577 C ATOM 615 C TYR A 124 21.134 -1.221 35.049 1.00 30.78 C ANISOU 615 C TYR A 124 4127 3458 4110 23 248 495 C ATOM 616 O TYR A 124 21.125 -0.127 34.467 1.00 31.57 O ANISOU 616 O TYR A 124 4209 3605 4182 -5 225 422 O ATOM 617 CB TYR A 124 22.080 -1.655 37.361 1.00 25.55 C ANISOU 617 CB TYR A 124 3419 2895 3394 107 189 672 C ATOM 618 CG TYR A 124 23.298 -0.835 36.998 1.00 26.27 C ANISOU 618 CG TYR A 124 3441 3046 3494 138 148 640 C ATOM 619 CD1 TYR A 124 23.452 0.473 37.466 1.00 27.66 C ANISOU 619 CD1 TYR A 124 3578 3336 3596 105 86 601 C ATOM 620 CD2 TYR A 124 24.311 -1.369 36.208 1.00 27.08 C ANISOU 620 CD2 TYR A 124 3516 3085 3686 197 181 649 C ATOM 621 CE1 TYR A 124 24.578 1.231 37.139 1.00 25.79 C ANISOU 621 CE1 TYR A 124 3273 3149 3377 119 52 571 C ATOM 622 CE2 TYR A 124 25.432 -0.615 35.863 1.00 27.96 C ANISOU 622 CE2 TYR A 124 3552 3253 3818 220 155 623 C ATOM 623 CZ TYR A 124 25.558 0.684 36.332 1.00 32.58 C ANISOU 623 CZ TYR A 124 4095 3951 4331 175 87 585 C ATOM 624 OH TYR A 124 26.676 1.402 36.020 1.00 33.81 O ANISOU 624 OH TYR A 124 4172 4158 4516 186 63 562 O ATOM 625 N LEU A 125 21.342 -2.372 34.411 1.00 25.96 N ANISOU 625 N LEU A 125 3557 2732 3573 50 305 508 N ATOM 626 CA LEU A 125 21.668 -2.405 32.962 1.00 25.04 C ANISOU 626 CA LEU A 125 3469 2545 3499 46 347 429 C ATOM 627 C LEU A 125 20.484 -1.908 32.124 1.00 28.85 C ANISOU 627 C LEU A 125 3993 3023 3947 -42 339 335 C ATOM 628 O LEU A 125 20.729 -1.272 31.099 1.00 29.25 O ANISOU 628 O LEU A 125 4049 3083 3981 -55 338 266 O ATOM 629 CB LEU A 125 22.098 -3.821 32.575 1.00 24.63 C ANISOU 629 CB LEU A 125 3464 2362 3533 95 421 459 C ATOM 630 CG LEU A 125 23.456 -4.255 33.117 1.00 29.45 C ANISOU 630 CG LEU A 125 4019 2972 4200 203 432 548 C ATOM 631 CD1 LEU A 125 23.846 -5.611 32.567 1.00 29.21 C ANISOU 631 CD1 LEU A 125 4045 2789 4266 256 524 572 C ATOM 632 CD2 LEU A 125 24.525 -3.231 32.791 1.00 30.45 C ANISOU 632 CD2 LEU A 125 4070 3174 4325 236 414 517 C ATOM 633 N GLN A 126 19.251 -2.219 32.519 1.00 25.56 N ANISOU 633 N GLN A 126 3594 2602 3517 -101 330 342 N ATOM 634 CA GLN A 126 18.075 -1.723 31.759 1.00 25.18 C ANISOU 634 CA GLN A 126 3561 2564 3443 -182 307 268 C ATOM 635 C GLN A 126 17.996 -0.193 31.856 1.00 29.28 C ANISOU 635 C GLN A 126 4031 3190 3903 -188 255 238 C ATOM 636 O GLN A 126 17.752 0.438 30.837 1.00 30.49 O ANISOU 636 O GLN A 126 4198 3350 4038 -218 235 172 O ATOM 637 CB GLN A 126 16.796 -2.411 32.242 1.00 26.37 C ANISOU 637 CB GLN A 126 3722 2686 3613 -243 316 292 C ATOM 638 CG GLN A 126 15.540 -1.981 31.498 1.00 32.89 C ANISOU 638 CG GLN A 126 4546 3521 4431 -331 285 222 C ATOM 639 CD GLN A 126 15.638 -2.118 29.999 1.00 48.05 C ANISOU 639 CD GLN A 126 6518 5394 6346 -361 275 136 C ATOM 640 OE1 GLN A 126 15.184 -1.265 29.246 1.00 42.01 O ANISOU 640 OE1 GLN A 126 5738 4686 5539 -384 226 87 O ATOM 641 NE2 GLN A 126 16.241 -3.199 29.547 1.00 39.07 N ANISOU 641 NE2 GLN A 126 5452 4148 5245 -361 325 117 N ATOM 642 N THR A 127 18.192 0.367 33.047 1.00 24.41 N ANISOU 642 N THR A 127 3366 2654 3253 -159 232 285 N ATOM 643 CA THR A 127 18.145 1.842 33.240 1.00 23.40 C ANISOU 643 CA THR A 127 3201 2615 3075 -166 193 251 C ATOM 644 C THR A 127 19.319 2.533 32.532 1.00 27.34 C ANISOU 644 C THR A 127 3689 3129 3569 -135 184 220 C ATOM 645 O THR A 127 19.115 3.623 32.013 1.00 27.44 O ANISOU 645 O THR A 127 3696 3173 3557 -154 164 172 O ATOM 646 CB THR A 127 17.852 2.240 34.689 1.00 24.66 C ANISOU 646 CB THR A 127 3330 2849 3189 -161 180 295 C ATOM 647 OG1 THR A 127 18.869 1.718 35.538 1.00 24.31 O ANISOU 647 OG1 THR A 127 3279 2822 3138 -113 176 361 O ATOM 648 CG2 THR A 127 16.487 1.782 35.149 1.00 22.58 C ANISOU 648 CG2 THR A 127 3072 2577 2932 -203 203 316 C ATOM 649 N VAL A 128 20.503 1.917 32.553 1.00 24.45 N ANISOU 649 N VAL A 128 3317 2736 3238 -85 205 253 N ATOM 650 CA VAL A 128 21.718 2.478 31.892 1.00 23.97 C ANISOU 650 CA VAL A 128 3234 2684 3191 -57 213 229 C ATOM 651 C VAL A 128 21.449 2.559 30.390 1.00 29.56 C ANISOU 651 C VAL A 128 3996 3336 3900 -86 243 161 C ATOM 652 O VAL A 128 21.783 3.578 29.796 1.00 30.31 O ANISOU 652 O VAL A 128 4087 3459 3970 -99 236 121 O ATOM 653 CB VAL A 128 22.967 1.629 32.201 1.00 27.20 C ANISOU 653 CB VAL A 128 3609 3069 3655 11 238 288 C ATOM 654 CG1 VAL A 128 24.072 1.837 31.182 1.00 26.05 C ANISOU 654 CG1 VAL A 128 3444 2905 3548 38 277 256 C ATOM 655 CG2 VAL A 128 23.485 1.881 33.599 1.00 27.12 C ANISOU 655 CG2 VAL A 128 3538 3143 3622 37 185 355 C ATOM 656 N SER A 129 20.813 1.523 29.845 1.00 26.66 N ANISOU 656 N SER A 129 3688 2890 3552 -104 272 147 N ATOM 657 CA SER A 129 20.455 1.401 28.413 1.00 26.62 C ANISOU 657 CA SER A 129 3753 2830 3532 -142 293 81 C ATOM 658 C SER A 129 19.473 2.506 28.002 1.00 27.81 C ANISOU 658 C SER A 129 3906 3034 3627 -193 237 43 C ATOM 659 O SER A 129 19.651 3.066 26.923 1.00 27.30 O ANISOU 659 O SER A 129 3877 2968 3528 -205 241 1 O ATOM 660 CB SER A 129 19.907 0.021 28.178 1.00 30.86 C ANISOU 660 CB SER A 129 4351 3272 4102 -165 326 74 C ATOM 661 OG SER A 129 19.119 -0.043 27.012 1.00 46.70 O ANISOU 661 OG SER A 129 6421 5251 6072 -234 308 7 O ATOM 662 N VAL A 130 18.478 2.799 28.838 1.00 22.97 N ANISOU 662 N VAL A 130 3253 2468 3006 -216 194 65 N ATOM 663 CA VAL A 130 17.487 3.877 28.558 1.00 22.38 C ANISOU 663 CA VAL A 130 3163 2443 2897 -248 145 43 C ATOM 664 C VAL A 130 18.222 5.222 28.523 1.00 27.47 C ANISOU 664 C VAL A 130 3788 3134 3517 -221 140 36 C ATOM 665 O VAL A 130 17.948 6.022 27.639 1.00 28.08 O ANISOU 665 O VAL A 130 3892 3213 3564 -234 125 7 O ATOM 666 CB VAL A 130 16.389 3.898 29.636 1.00 25.22 C ANISOU 666 CB VAL A 130 3474 2840 3267 -267 123 73 C ATOM 667 CG1 VAL A 130 15.470 5.091 29.473 1.00 24.18 C ANISOU 667 CG1 VAL A 130 3312 2758 3117 -281 82 56 C ATOM 668 CG2 VAL A 130 15.598 2.605 29.680 1.00 24.98 C ANISOU 668 CG2 VAL A 130 3462 2758 3272 -310 132 79 C ATOM 669 N SER A 131 19.131 5.427 29.471 1.00 22.41 N ANISOU 669 N SER A 131 3104 2526 2886 -187 151 64 N ATOM 670 CA SER A 131 19.939 6.663 29.588 1.00 20.17 C ANISOU 670 CA SER A 131 2795 2281 2588 -174 148 54 C ATOM 671 C SER A 131 20.851 6.824 28.364 1.00 25.35 C ANISOU 671 C SER A 131 3481 2903 3247 -168 183 30 C ATOM 672 O SER A 131 20.928 7.934 27.848 1.00 25.20 O ANISOU 672 O SER A 131 3474 2894 3207 -180 181 10 O ATOM 673 CB SER A 131 20.711 6.616 30.864 1.00 20.22 C ANISOU 673 CB SER A 131 2748 2333 2601 -152 141 86 C ATOM 674 OG SER A 131 21.427 7.811 31.063 1.00 27.23 O ANISOU 674 OG SER A 131 3609 3254 3483 -154 136 69 O ATOM 675 N VAL A 132 21.490 5.739 27.916 1.00 20.49 N ANISOU 675 N VAL A 132 2887 2240 2659 -149 227 34 N ATOM 676 CA VAL A 132 22.379 5.775 26.717 1.00 20.74 C ANISOU 676 CA VAL A 132 2954 2234 2692 -140 283 9 C ATOM 677 C VAL A 132 21.532 6.104 25.490 1.00 26.34 C ANISOU 677 C VAL A 132 3744 2921 3343 -178 274 -30 C ATOM 678 O VAL A 132 21.949 6.942 24.700 1.00 25.29 O ANISOU 678 O VAL A 132 3636 2794 3181 -185 292 -43 O ATOM 679 CB VAL A 132 23.146 4.453 26.530 1.00 24.26 C ANISOU 679 CB VAL A 132 3408 2622 3187 -101 348 19 C ATOM 680 CG1 VAL A 132 23.875 4.410 25.201 1.00 24.68 C ANISOU 680 CG1 VAL A 132 3513 2631 3232 -96 425 -17 C ATOM 681 CG2 VAL A 132 24.112 4.194 27.663 1.00 23.74 C ANISOU 681 CG2 VAL A 132 3251 2590 3180 -54 347 72 C ATOM 682 N ALA A 133 20.352 5.494 25.390 1.00 23.72 N ANISOU 682 N ALA A 133 3450 2570 2993 -208 238 -42 N ATOM 683 CA ALA A 133 19.439 5.717 24.251 1.00 22.04 C ANISOU 683 CA ALA A 133 3305 2350 2720 -250 203 -73 C ATOM 684 C ALA A 133 18.991 7.180 24.204 1.00 27.43 C ANISOU 684 C ALA A 133 3968 3082 3373 -253 158 -60 C ATOM 685 O ALA A 133 19.181 7.811 23.169 1.00 27.56 O ANISOU 685 O ALA A 133 4039 3092 3339 -259 168 -70 O ATOM 686 CB ALA A 133 18.258 4.796 24.364 1.00 21.83 C ANISOU 686 CB ALA A 133 3287 2309 2699 -289 158 -81 C ATOM 687 N VAL A 134 18.438 7.691 25.303 1.00 23.91 N ANISOU 687 N VAL A 134 3452 2677 2956 -244 121 -35 N ATOM 688 CA VAL A 134 17.921 9.057 25.339 1.00 24.52 C ANISOU 688 CA VAL A 134 3511 2785 3019 -239 87 -23 C ATOM 689 C VAL A 134 19.056 10.114 25.199 1.00 28.01 C ANISOU 689 C VAL A 134 3959 3226 3459 -223 129 -22 C ATOM 690 O VAL A 134 18.865 11.106 24.490 1.00 27.67 O ANISOU 690 O VAL A 134 3949 3176 3387 -224 121 -16 O ATOM 691 CB VAL A 134 16.965 9.311 26.554 1.00 28.17 C ANISOU 691 CB VAL A 134 3905 3285 3514 -234 54 -5 C ATOM 692 CG1 VAL A 134 17.678 9.152 27.902 1.00 27.25 C ANISOU 692 CG1 VAL A 134 3741 3190 3421 -213 83 1 C ATOM 693 CG2 VAL A 134 16.310 10.691 26.439 1.00 28.24 C ANISOU 693 CG2 VAL A 134 3906 3310 3515 -229 11 6 C ATOM 694 N LEU A 135 20.226 9.890 25.835 1.00 24.02 N ANISOU 694 N LEU A 135 3416 2722 2987 -210 172 -22 N ATOM 695 CA LEU A 135 21.342 10.820 25.700 1.00 23.64 C ANISOU 695 CA LEU A 135 3360 2673 2950 -209 213 -24 C ATOM 696 C LEU A 135 21.920 10.790 24.282 1.00 26.24 C ANISOU 696 C LEU A 135 3757 2966 3249 -215 265 -32 C ATOM 697 O LEU A 135 22.279 11.847 23.775 1.00 24.81 O ANISOU 697 O LEU A 135 3598 2774 3054 -225 289 -27 O ATOM 698 CB LEU A 135 22.439 10.616 26.761 1.00 23.74 C ANISOU 698 CB LEU A 135 3298 2711 3010 -199 231 -18 C ATOM 699 CG LEU A 135 22.073 10.959 28.220 1.00 27.73 C ANISOU 699 CG LEU A 135 3750 3261 3525 -201 186 -13 C ATOM 700 CD1 LEU A 135 23.171 10.510 29.177 1.00 27.15 C ANISOU 700 CD1 LEU A 135 3610 3223 3483 -191 186 1 C ATOM 701 CD2 LEU A 135 21.778 12.448 28.400 1.00 28.51 C ANISOU 701 CD2 LEU A 135 3855 3362 3614 -218 177 -30 C ATOM 702 N THR A 136 21.921 9.601 23.613 1.00 23.33 N ANISOU 702 N THR A 136 3434 2570 2861 -213 288 -46 N ATOM 703 CA THR A 136 22.397 9.443 22.224 1.00 22.88 C ANISOU 703 CA THR A 136 3462 2476 2756 -221 348 -63 C ATOM 704 C THR A 136 21.501 10.241 21.299 1.00 26.24 C ANISOU 704 C THR A 136 3963 2905 3104 -243 304 -56 C ATOM 705 O THR A 136 22.001 11.009 20.478 1.00 26.22 O ANISOU 705 O THR A 136 4010 2888 3064 -248 349 -47 O ATOM 706 CB THR A 136 22.496 7.952 21.818 1.00 28.27 C ANISOU 706 CB THR A 136 4187 3119 3434 -217 383 -91 C ATOM 707 OG1 THR A 136 23.465 7.315 22.647 1.00 28.68 O ANISOU 707 OG1 THR A 136 4164 3166 3568 -182 429 -80 O ATOM 708 CG2 THR A 136 22.909 7.767 20.359 1.00 21.47 C ANISOU 708 CG2 THR A 136 3433 2219 2504 -229 454 -120 C ATOM 709 N LEU A 137 20.177 10.084 21.457 1.00 23.87 N ANISOU 709 N LEU A 137 3662 2623 2784 -254 218 -53 N ATOM 710 CA LEU A 137 19.194 10.837 20.672 1.00 23.10 C ANISOU 710 CA LEU A 137 3616 2539 2623 -265 155 -33 C ATOM 711 C LEU A 137 19.328 12.340 20.903 1.00 26.47 C ANISOU 711 C LEU A 137 4020 2969 3069 -246 159 4 C ATOM 712 O LEU A 137 19.217 13.105 19.939 1.00 26.88 O ANISOU 712 O LEU A 137 4141 3011 3063 -247 157 30 O ATOM 713 CB LEU A 137 17.755 10.354 20.938 1.00 22.33 C ANISOU 713 CB LEU A 137 3491 2469 2527 -279 60 -32 C ATOM 714 CG LEU A 137 17.403 8.928 20.466 1.00 26.35 C ANISOU 714 CG LEU A 137 4044 2962 3005 -317 44 -73 C ATOM 715 CD1 LEU A 137 15.996 8.575 20.875 1.00 26.46 C ANISOU 715 CD1 LEU A 137 4004 3006 3043 -340 -46 -67 C ATOM 716 CD2 LEU A 137 17.583 8.761 18.945 1.00 25.50 C ANISOU 716 CD2 LEU A 137 4061 2837 2790 -346 53 -96 C ATOM 717 N SER A 138 19.633 12.756 22.161 1.00 22.22 N ANISOU 717 N SER A 138 3397 2440 2607 -231 171 5 N ATOM 718 CA SER A 138 19.833 14.165 22.524 1.00 22.33 C ANISOU 718 CA SER A 138 3392 2444 2650 -221 186 25 C ATOM 719 C SER A 138 21.074 14.734 21.834 1.00 28.30 C ANISOU 719 C SER A 138 4189 3166 3395 -235 266 30 C ATOM 720 O SER A 138 21.018 15.861 21.359 1.00 27.35 O ANISOU 720 O SER A 138 4111 3019 3261 -235 279 59 O ATOM 721 CB SER A 138 19.949 14.347 24.037 1.00 23.13 C ANISOU 721 CB SER A 138 3406 2563 2817 -216 183 9 C ATOM 722 OG SER A 138 18.771 13.963 24.728 1.00 26.17 O ANISOU 722 OG SER A 138 3752 2976 3214 -203 125 11 O ATOM 723 N PHE A 139 22.180 13.956 21.759 1.00 27.32 N ANISOU 723 N PHE A 139 4053 3041 3286 -245 329 7 N ATOM 724 CA PHE A 139 23.428 14.393 21.125 1.00 27.69 C ANISOU 724 CA PHE A 139 4121 3061 3337 -261 422 11 C ATOM 725 C PHE A 139 23.327 14.429 19.597 1.00 29.79 C ANISOU 725 C PHE A 139 4505 3301 3510 -268 457 27 C ATOM 726 O PHE A 139 23.954 15.297 18.997 1.00 30.23 O ANISOU 726 O PHE A 139 4600 3329 3556 -283 523 50 O ATOM 727 CB PHE A 139 24.643 13.598 21.624 1.00 31.01 C ANISOU 727 CB PHE A 139 4468 3493 3822 -260 479 -12 C ATOM 728 CG PHE A 139 25.177 14.195 22.908 1.00 34.91 C ANISOU 728 CG PHE A 139 4859 4011 4395 -272 464 -16 C ATOM 729 CD1 PHE A 139 24.560 13.936 24.125 1.00 38.15 C ANISOU 729 CD1 PHE A 139 5213 4456 4825 -261 389 -24 C ATOM 730 CD2 PHE A 139 26.247 15.087 22.889 1.00 40.85 C ANISOU 730 CD2 PHE A 139 5578 4751 5193 -303 523 -13 C ATOM 731 CE1 PHE A 139 25.012 14.532 25.297 1.00 39.71 C ANISOU 731 CE1 PHE A 139 5335 4681 5074 -279 369 -35 C ATOM 732 CE2 PHE A 139 26.693 15.697 24.067 1.00 43.94 C ANISOU 732 CE2 PHE A 139 5881 5166 5647 -329 496 -27 C ATOM 733 CZ PHE A 139 26.073 15.404 25.263 1.00 41.38 C ANISOU 733 CZ PHE A 139 5515 4881 5327 -316 415 -40 C ATOM 734 N ILE A 140 22.497 13.559 18.973 1.00 24.75 N ANISOU 734 N ILE A 140 3932 2674 2800 -264 409 16 N ATOM 735 CA ILE A 140 22.237 13.608 17.527 1.00 24.59 C ANISOU 735 CA ILE A 140 4039 2641 2664 -277 420 30 C ATOM 736 C ILE A 140 21.523 14.954 17.237 1.00 31.24 C ANISOU 736 C ILE A 140 4915 3479 3476 -269 367 90 C ATOM 737 O ILE A 140 21.975 15.714 16.374 1.00 30.64 O ANISOU 737 O ILE A 140 4916 3375 3349 -277 425 126 O ATOM 738 CB ILE A 140 21.376 12.403 17.031 1.00 27.08 C ANISOU 738 CB ILE A 140 4410 2971 2906 -288 357 -3 C ATOM 739 CG1 ILE A 140 22.154 11.073 17.078 1.00 26.19 C ANISOU 739 CG1 ILE A 140 4295 2838 2818 -290 434 -60 C ATOM 740 CG2 ILE A 140 20.834 12.668 15.612 1.00 27.08 C ANISOU 740 CG2 ILE A 140 4546 2976 2768 -307 328 18 C ATOM 741 CD1 ILE A 140 21.287 9.798 16.903 1.00 23.11 C ANISOU 741 CD1 ILE A 140 3943 2450 2389 -310 372 -104 C ATOM 742 N ALA A 141 20.406 15.231 17.981 1.00 29.17 N ANISOU 742 N ALA A 141 4593 3238 3251 -249 267 105 N ATOM 743 CA ALA A 141 19.592 16.441 17.892 1.00 27.64 C ANISOU 743 CA ALA A 141 4411 3036 3055 -225 213 164 C ATOM 744 C ALA A 141 20.482 17.672 18.020 1.00 30.54 C ANISOU 744 C ALA A 141 4783 3352 3470 -226 297 189 C ATOM 745 O ALA A 141 20.395 18.576 17.193 1.00 29.57 O ANISOU 745 O ALA A 141 4740 3197 3300 -219 311 247 O ATOM 746 CB ALA A 141 18.541 16.439 18.992 1.00 28.15 C ANISOU 746 CB ALA A 141 4380 3127 3191 -200 131 160 C ATOM 747 N LEU A 142 21.371 17.678 19.027 1.00 26.64 N ANISOU 747 N LEU A 142 4207 2850 3066 -242 353 148 N ATOM 748 CA LEU A 142 22.309 18.753 19.310 1.00 26.60 C ANISOU 748 CA LEU A 142 4187 2798 3121 -263 432 156 C ATOM 749 C LEU A 142 23.263 18.978 18.127 1.00 29.54 C ANISOU 749 C LEU A 142 4643 3138 3444 -290 531 181 C ATOM 750 O LEU A 142 23.472 20.118 17.704 1.00 29.13 O ANISOU 750 O LEU A 142 4643 3033 3394 -299 577 227 O ATOM 751 CB LEU A 142 23.076 18.410 20.600 1.00 27.18 C ANISOU 751 CB LEU A 142 4149 2893 3285 -284 451 99 C ATOM 752 CG LEU A 142 23.879 19.525 21.260 1.00 33.54 C ANISOU 752 CG LEU A 142 4914 3661 4170 -319 502 89 C ATOM 753 CD1 LEU A 142 22.963 20.516 22.005 1.00 33.39 C ANISOU 753 CD1 LEU A 142 4891 3611 4183 -300 455 93 C ATOM 754 CD2 LEU A 142 24.905 18.936 22.207 1.00 37.94 C ANISOU 754 CD2 LEU A 142 5367 4259 4792 -347 519 40 C ATOM 755 N ASP A 143 23.802 17.880 17.568 1.00 25.52 N ANISOU 755 N ASP A 143 4153 2654 2889 -300 572 154 N ATOM 756 CA ASP A 143 24.716 17.906 16.435 1.00 24.53 C ANISOU 756 CA ASP A 143 4109 2505 2709 -323 684 170 C ATOM 757 C ASP A 143 24.038 18.477 15.188 1.00 29.47 C ANISOU 757 C ASP A 143 4875 3110 3210 -315 667 234 C ATOM 758 O ASP A 143 24.610 19.345 14.533 1.00 30.21 O ANISOU 758 O ASP A 143 5033 3159 3284 -333 753 281 O ATOM 759 CB ASP A 143 25.262 16.503 16.161 1.00 25.88 C ANISOU 759 CB ASP A 143 4276 2701 2857 -323 731 119 C ATOM 760 CG ASP A 143 26.251 16.476 15.023 1.00 34.61 C ANISOU 760 CG ASP A 143 5462 3781 3909 -343 869 127 C ATOM 761 OD1 ASP A 143 27.416 16.871 15.244 1.00 37.42 O ANISOU 761 OD1 ASP A 143 5751 4117 4350 -365 973 128 O ATOM 762 OD2 ASP A 143 25.857 16.074 13.903 1.00 36.15 O ANISOU 762 OD2 ASP A 143 5786 3978 3972 -342 876 132 O ATOM 763 N ARG A 144 22.825 18.002 14.870 1.00 25.79 N ANISOU 763 N ARG A 144 4455 2681 2664 -290 554 241 N ATOM 764 CA ARG A 144 22.030 18.450 13.727 1.00 25.43 C ANISOU 764 CA ARG A 144 4536 2637 2491 -278 502 308 C ATOM 765 C ARG A 144 21.562 19.879 13.896 1.00 30.43 C ANISOU 765 C ARG A 144 5171 3227 3164 -251 473 387 C ATOM 766 O ARG A 144 21.559 20.613 12.918 1.00 32.20 O ANISOU 766 O ARG A 144 5506 3421 3307 -247 500 461 O ATOM 767 CB ARG A 144 20.819 17.510 13.477 1.00 26.01 C ANISOU 767 CB ARG A 144 4627 2769 2485 -268 368 289 C ATOM 768 CG ARG A 144 21.166 16.041 13.173 1.00 24.81 C ANISOU 768 CG ARG A 144 4502 2643 2281 -298 398 208 C ATOM 769 CD ARG A 144 21.911 15.852 11.868 1.00 27.35 C ANISOU 769 CD ARG A 144 4967 2950 2473 -325 500 208 C ATOM 770 NE ARG A 144 23.340 16.138 12.010 1.00 28.83 N ANISOU 770 NE ARG A 144 5128 3094 2732 -334 663 199 N ATOM 771 CZ ARG A 144 24.085 16.689 11.061 1.00 39.61 C ANISOU 771 CZ ARG A 144 6596 4429 4024 -350 778 237 C ATOM 772 NH1 ARG A 144 23.558 16.986 9.888 1.00 27.52 N ANISOU 772 NH1 ARG A 144 5217 2909 2331 -357 747 288 N ATOM 773 NH2 ARG A 144 25.371 16.931 11.273 1.00 23.77 N ANISOU 773 NH2 ARG A 144 4539 2387 2106 -364 926 229 N ATOM 774 N TRP A 145 21.194 20.289 15.124 1.00 25.33 N ANISOU 774 N TRP A 145 4413 2571 2641 -230 430 372 N ATOM 775 CA TRP A 145 20.732 21.640 15.435 1.00 24.57 C ANISOU 775 CA TRP A 145 4312 2417 2604 -198 415 433 C ATOM 776 C TRP A 145 21.853 22.631 15.233 1.00 29.14 C ANISOU 776 C TRP A 145 4932 2917 3221 -232 544 459 C ATOM 777 O TRP A 145 21.646 23.636 14.568 1.00 29.97 O ANISOU 777 O TRP A 145 5125 2966 3298 -213 560 544 O ATOM 778 CB TRP A 145 20.146 21.702 16.858 1.00 23.47 C ANISOU 778 CB TRP A 145 4049 2286 2581 -174 357 390 C ATOM 779 CG TRP A 145 19.511 23.006 17.215 1.00 24.49 C ANISOU 779 CG TRP A 145 4178 2352 2777 -129 342 444 C ATOM 780 CD1 TRP A 145 18.269 23.445 16.855 1.00 27.20 C ANISOU 780 CD1 TRP A 145 4542 2695 3099 -64 254 517 C ATOM 781 CD2 TRP A 145 20.093 24.054 18.019 1.00 24.50 C ANISOU 781 CD2 TRP A 145 4152 2273 2883 -145 419 426 C ATOM 782 NE1 TRP A 145 18.043 24.707 17.375 1.00 26.23 N ANISOU 782 NE1 TRP A 145 4411 2486 3068 -27 285 551 N ATOM 783 CE2 TRP A 145 19.141 25.096 18.106 1.00 27.57 C ANISOU 783 CE2 TRP A 145 4559 2603 3313 -82 387 488 C ATOM 784 CE3 TRP A 145 21.325 24.204 18.689 1.00 25.41 C ANISOU 784 CE3 TRP A 145 4226 2362 3068 -210 509 362 C ATOM 785 CZ2 TRP A 145 19.374 26.261 18.845 1.00 26.46 C ANISOU 785 CZ2 TRP A 145 4412 2367 3276 -84 452 477 C ATOM 786 CZ3 TRP A 145 21.554 25.365 19.410 1.00 26.48 C ANISOU 786 CZ3 TRP A 145 4350 2413 3298 -224 558 350 C ATOM 787 CH2 TRP A 145 20.589 26.378 19.482 1.00 26.69 C ANISOU 787 CH2 TRP A 145 4412 2370 3359 -163 536 402 C ATOM 788 N TYR A 146 23.058 22.344 15.740 1.00 26.24 N ANISOU 788 N TYR A 146 4503 2547 2920 -283 636 394 N ATOM 789 CA TYR A 146 24.207 23.229 15.495 1.00 25.40 C ANISOU 789 CA TYR A 146 4423 2370 2858 -332 766 416 C ATOM 790 C TYR A 146 24.611 23.227 14.032 1.00 31.38 C ANISOU 790 C TYR A 146 5311 3115 3495 -345 845 475 C ATOM 791 O TYR A 146 24.727 24.295 13.460 1.00 32.62 O ANISOU 791 O TYR A 146 5553 3201 3640 -351 902 552 O ATOM 792 CB TYR A 146 25.410 22.884 16.380 1.00 25.15 C ANISOU 792 CB TYR A 146 4272 2352 2933 -386 834 336 C ATOM 793 CG TYR A 146 25.318 23.514 17.749 1.00 24.10 C ANISOU 793 CG TYR A 146 4044 2195 2918 -397 797 294 C ATOM 794 CD1 TYR A 146 25.471 24.893 17.917 1.00 24.64 C ANISOU 794 CD1 TYR A 146 4139 2171 3051 -423 845 322 C ATOM 795 CD2 TYR A 146 25.058 22.737 18.880 1.00 23.63 C ANISOU 795 CD2 TYR A 146 3879 2199 2900 -385 720 226 C ATOM 796 CE1 TYR A 146 25.352 25.483 19.174 1.00 23.38 C ANISOU 796 CE1 TYR A 146 3910 1985 2989 -438 815 270 C ATOM 797 CE2 TYR A 146 24.951 23.317 20.143 1.00 24.03 C ANISOU 797 CE2 TYR A 146 3858 2232 3038 -399 689 182 C ATOM 798 CZ TYR A 146 25.105 24.687 20.285 1.00 28.81 C ANISOU 798 CZ TYR A 146 4498 2748 3702 -427 737 198 C ATOM 799 OH TYR A 146 25.004 25.250 21.525 1.00 28.56 O ANISOU 799 OH TYR A 146 4411 2694 3746 -447 713 141 O ATOM 800 N ALA A 147 24.764 22.049 13.401 1.00 28.50 N ANISOU 800 N ALA A 147 4979 2812 3036 -348 852 444 N ATOM 801 CA ALA A 147 25.169 21.975 11.991 1.00 28.52 C ANISOU 801 CA ALA A 147 5122 2808 2905 -364 938 490 C ATOM 802 C ALA A 147 24.235 22.751 11.039 1.00 34.26 C ANISOU 802 C ALA A 147 5992 3515 3512 -330 878 598 C ATOM 803 O ALA A 147 24.711 23.475 10.163 1.00 35.34 O ANISOU 803 O ALA A 147 6238 3601 3588 -348 975 671 O ATOM 804 CB ALA A 147 25.280 20.521 11.551 1.00 28.84 C ANISOU 804 CB ALA A 147 5184 2916 2859 -366 940 425 C ATOM 805 N ILE A 148 22.916 22.632 11.249 1.00 31.02 N ANISOU 805 N ILE A 148 5570 3143 3074 -279 718 614 N ATOM 806 CA ILE A 148 21.885 23.215 10.384 1.00 29.80 C ANISOU 806 CA ILE A 148 5529 2989 2806 -235 627 721 C ATOM 807 C ILE A 148 21.449 24.613 10.811 1.00 33.33 C ANISOU 807 C ILE A 148 5959 3355 3350 -192 609 805 C ATOM 808 O ILE A 148 21.355 25.482 9.945 1.00 34.36 O ANISOU 808 O ILE A 148 6209 3436 3410 -174 633 915 O ATOM 809 CB ILE A 148 20.680 22.223 10.256 1.00 31.86 C ANISOU 809 CB ILE A 148 5779 3344 2983 -207 460 696 C ATOM 810 CG1 ILE A 148 21.136 20.886 9.604 1.00 29.96 C ANISOU 810 CG1 ILE A 148 5597 3161 2624 -254 494 617 C ATOM 811 CG2 ILE A 148 19.476 22.843 9.531 1.00 32.86 C ANISOU 811 CG2 ILE A 148 5984 3486 3015 -153 329 812 C ATOM 812 CD1 ILE A 148 20.265 19.711 9.842 1.00 25.03 C ANISOU 812 CD1 ILE A 148 4924 2615 1971 -253 362 549 C ATOM 813 N CYS A 149 21.162 24.837 12.103 1.00 29.21 N ANISOU 813 N CYS A 149 5303 2813 2981 -174 572 756 N ATOM 814 CA CYS A 149 20.652 26.131 12.563 1.00 29.08 C ANISOU 814 CA CYS A 149 5275 2710 3063 -126 560 823 C ATOM 815 C CYS A 149 21.736 27.144 12.982 1.00 35.23 C ANISOU 815 C CYS A 149 6052 3377 3956 -175 706 816 C ATOM 816 O CYS A 149 21.514 28.345 12.817 1.00 34.53 O ANISOU 816 O CYS A 149 6024 3190 3906 -145 734 902 O ATOM 817 CB CYS A 149 19.612 25.938 13.657 1.00 28.56 C ANISOU 817 CB CYS A 149 5086 2676 3089 -75 446 780 C ATOM 818 SG CYS A 149 18.178 24.970 13.125 1.00 32.13 S ANISOU 818 SG CYS A 149 5531 3248 3430 -22 265 806 S ATOM 819 N HIS A 150 22.884 26.686 13.532 1.00 31.44 N ANISOU 819 N HIS A 150 5500 2908 3537 -250 796 719 N ATOM 820 CA HIS A 150 23.958 27.587 13.974 1.00 31.00 C ANISOU 820 CA HIS A 150 5424 2758 3597 -315 925 702 C ATOM 821 C HIS A 150 25.297 27.033 13.481 1.00 38.57 C ANISOU 821 C HIS A 150 6383 3744 4529 -392 1046 667 C ATOM 822 O HIS A 150 26.112 26.581 14.295 1.00 37.59 O ANISOU 822 O HIS A 150 6140 3649 4494 -443 1080 574 O ATOM 823 CB HIS A 150 23.894 27.756 15.501 1.00 31.09 C ANISOU 823 CB HIS A 150 5304 2756 3751 -326 892 610 C ATOM 824 CG HIS A 150 22.571 28.285 15.946 1.00 34.33 C ANISOU 824 CG HIS A 150 5713 3138 4191 -243 794 642 C ATOM 825 ND1 HIS A 150 22.249 29.633 15.821 1.00 35.91 N ANISOU 825 ND1 HIS A 150 5984 3214 4444 -213 830 717 N ATOM 826 CD2 HIS A 150 21.484 27.616 16.390 1.00 35.93 C ANISOU 826 CD2 HIS A 150 5855 3418 4377 -180 672 618 C ATOM 827 CE1 HIS A 150 21.004 29.744 16.248 1.00 35.42 C ANISOU 827 CE1 HIS A 150 5893 3161 4405 -126 731 734 C ATOM 828 NE2 HIS A 150 20.501 28.558 16.601 1.00 35.87 N ANISOU 828 NE2 HIS A 150 5867 3341 4421 -108 633 675 N ATOM 829 N PRO A 151 25.505 27.016 12.128 1.00 39.08 N ANISOU 829 N PRO A 151 6580 3806 4464 -395 1111 746 N ATOM 830 CA PRO A 151 26.660 26.302 11.548 1.00 40.59 C ANISOU 830 CA PRO A 151 6775 4035 4612 -452 1231 710 C ATOM 831 C PRO A 151 28.101 26.713 11.862 1.00 50.91 C ANISOU 831 C PRO A 151 8009 5291 6043 -539 1388 676 C ATOM 832 O PRO A 151 28.974 25.896 11.578 1.00 51.97 O ANISOU 832 O PRO A 151 8107 5476 6164 -572 1471 631 O ATOM 833 CB PRO A 151 26.445 26.454 10.037 1.00 41.55 C ANISOU 833 CB PRO A 151 7081 4150 4557 -434 1270 814 C ATOM 834 CG PRO A 151 25.485 27.553 9.875 1.00 45.00 C ANISOU 834 CG PRO A 151 7599 4518 4981 -383 1201 921 C ATOM 835 CD PRO A 151 24.592 27.453 11.050 1.00 40.44 C ANISOU 835 CD PRO A 151 6902 3960 4502 -335 1060 867 C ATOM 836 N LEU A 152 28.403 27.897 12.384 1.00 51.16 N ANISOU 836 N LEU A 152 8018 5225 6195 -581 1436 695 N ATOM 837 CA LEU A 152 29.841 28.190 12.525 1.00 53.26 C ANISOU 837 CA LEU A 152 8211 5453 6571 -679 1587 665 C ATOM 838 C LEU A 152 30.370 28.251 13.974 1.00 58.45 C ANISOU 838 C LEU A 152 8692 6118 7399 -734 1556 560 C ATOM 839 O LEU A 152 31.437 28.829 14.210 1.00 59.15 O ANISOU 839 O LEU A 152 8716 6156 7601 -826 1662 543 O ATOM 840 CB LEU A 152 30.186 29.488 11.756 1.00 54.08 C ANISOU 840 CB LEU A 152 8437 5432 6679 -723 1715 769 C ATOM 841 CG LEU A 152 29.853 29.484 10.253 1.00 59.67 C ANISOU 841 CG LEU A 152 9334 6133 7203 -680 1762 886 C ATOM 842 CD1 LEU A 152 29.655 30.887 9.729 1.00 59.85 C ANISOU 842 CD1 LEU A 152 9491 6021 7227 -684 1821 1009 C ATOM 843 CD2 LEU A 152 30.864 28.664 9.442 1.00 62.84 C ANISOU 843 CD2 LEU A 152 9749 6593 7534 -720 1901 873 C ATOM 844 N LEU A 153 29.664 27.616 14.921 1.00 53.81 N ANISOU 844 N LEU A 153 8024 5600 6822 -684 1413 492 N ATOM 845 CA LEU A 153 30.056 27.637 16.326 1.00 52.62 C ANISOU 845 CA LEU A 153 7722 5468 6804 -730 1366 396 C ATOM 846 C LEU A 153 30.911 26.446 16.747 1.00 53.97 C ANISOU 846 C LEU A 153 7751 5745 7010 -751 1367 322 C ATOM 847 O LEU A 153 32.029 26.644 17.225 1.00 53.57 O ANISOU 847 O LEU A 153 7588 5695 7072 -833 1428 281 O ATOM 848 CB LEU A 153 28.825 27.788 17.241 1.00 52.48 C ANISOU 848 CB LEU A 153 7702 5450 6788 -668 1225 368 C ATOM 849 CG LEU A 153 28.055 29.083 17.098 1.00 57.57 C ANISOU 849 CG LEU A 153 8453 5973 7447 -647 1228 429 C ATOM 850 CD1 LEU A 153 26.713 28.977 17.742 1.00 57.42 C ANISOU 850 CD1 LEU A 153 8437 5973 7406 -558 1098 419 C ATOM 851 CD2 LEU A 153 28.829 30.261 17.668 1.00 61.24 C ANISOU 851 CD2 LEU A 153 8888 6336 8045 -746 1307 393 C ATOM 852 N PHE A 154 30.382 25.226 16.601 1.00 48.47 N ANISOU 852 N PHE A 154 7054 5136 6227 -679 1297 308 N ATOM 853 CA PHE A 154 31.075 24.009 17.010 1.00 48.07 C ANISOU 853 CA PHE A 154 6877 5177 6211 -679 1295 247 C ATOM 854 C PHE A 154 31.425 23.135 15.810 1.00 55.16 C ANISOU 854 C PHE A 154 7835 6103 7020 -651 1386 274 C ATOM 855 O PHE A 154 30.724 23.171 14.803 1.00 54.63 O ANISOU 855 O PHE A 154 7916 6017 6826 -613 1391 326 O ATOM 856 CB PHE A 154 30.273 23.238 18.086 1.00 48.57 C ANISOU 856 CB PHE A 154 6873 5309 6273 -626 1145 191 C ATOM 857 CG PHE A 154 30.013 24.058 19.334 1.00 48.98 C ANISOU 857 CG PHE A 154 6868 5337 6406 -657 1071 152 C ATOM 858 CD1 PHE A 154 30.969 24.150 20.340 1.00 51.30 C ANISOU 858 CD1 PHE A 154 7024 5659 6808 -725 1069 93 C ATOM 859 CD2 PHE A 154 28.833 24.782 19.480 1.00 48.44 C ANISOU 859 CD2 PHE A 154 6884 5216 6303 -621 1006 173 C ATOM 860 CE1 PHE A 154 30.738 24.936 21.479 1.00 50.94 C ANISOU 860 CE1 PHE A 154 6945 5589 6820 -764 1004 45 C ATOM 861 CE2 PHE A 154 28.622 25.587 20.603 1.00 49.83 C ANISOU 861 CE2 PHE A 154 7023 5358 6551 -650 960 128 C ATOM 862 CZ PHE A 154 29.571 25.654 21.595 1.00 47.78 C ANISOU 862 CZ PHE A 154 6645 5127 6384 -726 960 59 C ATOM 863 N LYS A 155 32.545 22.393 15.899 1.00 53.67 N ANISOU 863 N LYS A 155 7532 5960 6900 -671 1463 238 N ATOM 864 CA LYS A 155 33.010 21.476 14.850 1.00 53.53 C ANISOU 864 CA LYS A 155 7561 5966 6814 -643 1572 247 C ATOM 865 C LYS A 155 32.339 20.106 15.034 1.00 55.47 C ANISOU 865 C LYS A 155 7808 6273 6994 -568 1477 205 C ATOM 866 O LYS A 155 32.459 19.508 16.103 1.00 55.53 O ANISOU 866 O LYS A 155 7685 6330 7085 -552 1398 158 O ATOM 867 CB LYS A 155 34.543 21.318 14.898 1.00 56.79 C ANISOU 867 CB LYS A 155 7833 6391 7353 -691 1710 232 C ATOM 868 CG LYS A 155 35.308 22.327 14.054 1.00 80.27 C ANISOU 868 CG LYS A 155 10849 9298 10351 -764 1870 285 C ATOM 869 CD LYS A 155 36.827 22.086 14.055 1.00 94.87 C ANISOU 869 CD LYS A 155 12536 11170 12340 -811 2014 271 C ATOM 870 CE LYS A 155 37.579 22.797 15.161 1.00105.47 C ANISOU 870 CE LYS A 155 13695 12520 13859 -893 1973 244 C ATOM 871 NZ LYS A 155 39.017 22.406 15.192 1.00112.18 N ANISOU 871 NZ LYS A 155 14361 13411 14853 -928 2094 234 N ATOM 872 N SER A 156 31.640 19.619 14.001 1.00 49.63 N ANISOU 872 N SER A 156 7222 5531 6103 -527 1482 223 N ATOM 873 CA SER A 156 30.984 18.316 14.013 1.00 48.81 C ANISOU 873 CA SER A 156 7142 5473 5931 -469 1405 180 C ATOM 874 C SER A 156 31.872 17.265 13.301 1.00 52.36 C ANISOU 874 C SER A 156 7598 5931 6366 -453 1545 150 C ATOM 875 O SER A 156 31.851 17.166 12.071 1.00 51.18 O ANISOU 875 O SER A 156 7594 5761 6090 -453 1636 167 O ATOM 876 CB SER A 156 29.615 18.411 13.344 1.00 52.21 C ANISOU 876 CB SER A 156 7734 5899 6203 -443 1309 209 C ATOM 877 OG SER A 156 29.018 17.148 13.080 1.00 60.49 O ANISOU 877 OG SER A 156 8831 6984 7168 -405 1255 165 O ATOM 878 N THR A 157 32.665 16.500 14.073 1.00 49.42 N ANISOU 878 N THR A 157 7068 5588 6122 -435 1567 109 N ATOM 879 CA THR A 157 33.534 15.451 13.519 1.00 49.03 C ANISOU 879 CA THR A 157 7003 5537 6087 -405 1708 80 C ATOM 880 C THR A 157 33.192 14.081 14.095 1.00 53.39 C ANISOU 880 C THR A 157 7511 6115 6659 -344 1633 30 C ATOM 881 O THR A 157 32.608 13.989 15.177 1.00 53.13 O ANISOU 881 O THR A 157 7400 6112 6674 -333 1486 22 O ATOM 882 CB THR A 157 35.039 15.788 13.653 1.00 55.90 C ANISOU 882 CB THR A 157 7725 6407 7109 -433 1853 94 C ATOM 883 OG1 THR A 157 35.461 15.685 15.015 1.00 55.17 O ANISOU 883 OG1 THR A 157 7433 6357 7173 -433 1764 83 O ATOM 884 CG2 THR A 157 35.409 17.147 13.073 1.00 53.94 C ANISOU 884 CG2 THR A 157 7527 6121 6848 -504 1946 147 C ATOM 885 N ALA A 158 33.542 13.018 13.357 1.00 50.56 N ANISOU 885 N ALA A 158 7213 5737 6261 -305 1746 -5 N ATOM 886 CA ALA A 158 33.325 11.629 13.759 1.00 50.65 C ANISOU 886 CA ALA A 158 7201 5749 6296 -246 1709 -53 C ATOM 887 C ALA A 158 34.130 11.284 15.021 1.00 55.39 C ANISOU 887 C ALA A 158 7582 6380 7085 -213 1686 -45 C ATOM 888 O ALA A 158 33.647 10.512 15.855 1.00 55.00 O ANISOU 888 O ALA A 158 7486 6344 7067 -176 1577 -60 O ATOM 889 CB ALA A 158 33.700 10.695 12.619 1.00 51.28 C ANISOU 889 CB ALA A 158 7398 5783 6302 -217 1870 -95 C ATOM 890 N ARG A 159 35.332 11.881 15.168 1.00 52.45 N ANISOU 890 N ARG A 159 7073 6021 6835 -232 1781 -15 N ATOM 891 CA ARG A 159 36.230 11.682 16.311 1.00 53.05 C ANISOU 891 CA ARG A 159 6926 6139 7091 -209 1754 2 C ATOM 892 C ARG A 159 35.697 12.363 17.571 1.00 56.33 C ANISOU 892 C ARG A 159 7262 6604 7537 -247 1567 17 C ATOM 893 O ARG A 159 35.890 11.844 18.675 1.00 57.38 O ANISOU 893 O ARG A 159 7262 6778 7760 -214 1478 22 O ATOM 894 CB ARG A 159 37.668 12.121 15.985 1.00 56.15 C ANISOU 894 CB ARG A 159 7192 6536 7606 -228 1917 27 C ATOM 895 CG ARG A 159 38.391 11.125 15.069 1.00 74.30 C ANISOU 895 CG ARG A 159 9516 8792 9921 -163 2113 9 C ATOM 896 CD ARG A 159 39.110 11.786 13.933 1.00 94.16 C ANISOU 896 CD ARG A 159 12077 11280 12420 -206 2307 22 C ATOM 897 NE ARG A 159 39.785 10.797 13.089 1.00108.32 N ANISOU 897 NE ARG A 159 13896 13029 14229 -138 2510 -2 N ATOM 898 CZ ARG A 159 40.662 11.100 12.137 1.00122.37 C ANISOU 898 CZ ARG A 159 15698 14784 16015 -157 2724 7 C ATOM 899 NH1 ARG A 159 40.981 12.366 11.898 1.00108.97 N ANISOU 899 NH1 ARG A 159 13997 13095 14310 -247 2760 47 N ATOM 900 NH2 ARG A 159 41.228 10.141 11.419 1.00107.64 N ANISOU 900 NH2 ARG A 159 13861 12874 14164 -87 2916 -23 N ATOM 901 N ARG A 160 35.003 13.502 17.409 1.00 50.36 N ANISOU 901 N ARG A 160 6595 5839 6700 -311 1511 26 N ATOM 902 CA ARG A 160 34.370 14.219 18.510 1.00 49.17 C ANISOU 902 CA ARG A 160 6400 5722 6562 -346 1349 30 C ATOM 903 C ARG A 160 33.110 13.473 18.939 1.00 49.30 C ANISOU 903 C ARG A 160 6488 5746 6499 -303 1219 11 C ATOM 904 O ARG A 160 32.756 13.508 20.123 1.00 48.95 O ANISOU 904 O ARG A 160 6367 5741 6491 -303 1094 8 O ATOM 905 CB ARG A 160 34.057 15.672 18.121 1.00 52.32 C ANISOU 905 CB ARG A 160 6880 6090 6912 -418 1353 48 C ATOM 906 CG ARG A 160 35.266 16.579 18.306 1.00 69.33 C ANISOU 906 CG ARG A 160 8910 8245 9185 -485 1432 65 C ATOM 907 CD ARG A 160 35.139 17.953 17.665 1.00 87.35 C ANISOU 907 CD ARG A 160 11286 10476 11429 -557 1466 89 C ATOM 908 NE ARG A 160 36.114 18.909 18.192 1.00104.66 N ANISOU 908 NE ARG A 160 13344 12671 13750 -640 1486 92 N ATOM 909 CZ ARG A 160 37.421 18.917 17.933 1.00123.67 C ANISOU 909 CZ ARG A 160 15642 15083 16265 -679 1617 105 C ATOM 910 NH1 ARG A 160 37.946 18.035 17.088 1.00110.40 N ANISOU 910 NH1 ARG A 160 13977 13397 14574 -634 1759 118 N ATOM 911 NH2 ARG A 160 38.210 19.825 18.497 1.00112.55 N ANISOU 911 NH2 ARG A 160 14108 13681 14976 -769 1614 101 N ATOM 912 N ALA A 161 32.447 12.784 17.980 1.00 42.73 N ANISOU 912 N ALA A 161 5802 4878 5554 -272 1252 -6 N ATOM 913 CA ALA A 161 31.261 11.967 18.231 1.00 41.53 C ANISOU 913 CA ALA A 161 5721 4727 5330 -240 1145 -27 C ATOM 914 C ALA A 161 31.642 10.761 19.105 1.00 43.99 C ANISOU 914 C ALA A 161 5924 5056 5735 -185 1125 -36 C ATOM 915 O ALA A 161 30.904 10.437 20.033 1.00 43.43 O ANISOU 915 O ALA A 161 5826 5009 5665 -173 1004 -36 O ATOM 916 CB ALA A 161 30.625 11.517 16.924 1.00 42.04 C ANISOU 916 CB ALA A 161 5965 4752 5258 -236 1192 -49 C ATOM 917 N LEU A 162 32.840 10.179 18.884 1.00 40.18 N ANISOU 917 N LEU A 162 5364 4562 5340 -149 1247 -33 N ATOM 918 CA LEU A 162 33.346 9.069 19.694 1.00 40.21 C ANISOU 918 CA LEU A 162 5254 4577 5449 -84 1237 -24 C ATOM 919 C LEU A 162 33.636 9.497 21.141 1.00 42.65 C ANISOU 919 C LEU A 162 5400 4956 5848 -95 1119 9 C ATOM 920 O LEU A 162 33.415 8.708 22.061 1.00 42.84 O ANISOU 920 O LEU A 162 5372 4999 5906 -52 1038 24 O ATOM 921 CB LEU A 162 34.548 8.370 19.038 1.00 40.57 C ANISOU 921 CB LEU A 162 5253 4587 5574 -31 1408 -25 C ATOM 922 CG LEU A 162 34.266 7.636 17.697 1.00 46.28 C ANISOU 922 CG LEU A 162 6152 5233 6198 -11 1532 -72 C ATOM 923 CD1 LEU A 162 35.553 7.202 17.020 1.00 45.89 C ANISOU 923 CD1 LEU A 162 6052 5149 6234 37 1727 -74 C ATOM 924 CD2 LEU A 162 33.339 6.420 17.884 1.00 49.39 C ANISOU 924 CD2 LEU A 162 6635 5587 6543 25 1468 -103 C ATOM 925 N GLY A 163 34.075 10.747 21.325 1.00 36.67 N ANISOU 925 N GLY A 163 4581 4232 5119 -158 1109 20 N ATOM 926 CA GLY A 163 34.296 11.352 22.636 1.00 35.29 C ANISOU 926 CA GLY A 163 4277 4126 5007 -192 992 37 C ATOM 927 C GLY A 163 32.977 11.585 23.352 1.00 38.75 C ANISOU 927 C GLY A 163 4789 4578 5359 -209 854 24 C ATOM 928 O GLY A 163 32.864 11.337 24.558 1.00 39.27 O ANISOU 928 O GLY A 163 4777 4694 5449 -199 748 35 O ATOM 929 N SER A 164 31.957 12.048 22.605 1.00 33.62 N ANISOU 929 N SER A 164 4286 3884 4602 -233 855 4 N ATOM 930 CA SER A 164 30.610 12.252 23.131 1.00 32.53 C ANISOU 930 CA SER A 164 4219 3753 4388 -242 741 -6 C ATOM 931 C SER A 164 30.018 10.892 23.559 1.00 34.86 C ANISOU 931 C SER A 164 4525 4051 4669 -185 693 -5 C ATOM 932 O SER A 164 29.446 10.811 24.633 1.00 35.23 O ANISOU 932 O SER A 164 4541 4134 4712 -184 595 0 O ATOM 933 CB SER A 164 29.709 12.900 22.085 1.00 34.75 C ANISOU 933 CB SER A 164 4645 3989 4570 -266 759 -14 C ATOM 934 OG SER A 164 30.304 14.056 21.532 1.00 44.74 O ANISOU 934 OG SER A 164 5917 5234 5848 -313 827 -6 O ATOM 935 N ILE A 165 30.188 9.834 22.729 1.00 29.84 N ANISOU 935 N ILE A 165 3939 3372 4027 -143 774 -11 N ATOM 936 CA ILE A 165 29.709 8.465 22.974 1.00 29.90 C ANISOU 936 CA ILE A 165 3970 3358 4032 -93 752 -12 C ATOM 937 C ILE A 165 30.296 7.888 24.289 1.00 34.76 C ANISOU 937 C ILE A 165 4451 4016 4739 -53 702 26 C ATOM 938 O ILE A 165 29.546 7.303 25.077 1.00 34.06 O ANISOU 938 O ILE A 165 4370 3937 4633 -38 623 38 O ATOM 939 CB ILE A 165 29.933 7.546 21.729 1.00 32.29 C ANISOU 939 CB ILE A 165 4364 3592 4315 -63 871 -39 C ATOM 940 CG1 ILE A 165 28.889 7.859 20.622 1.00 31.77 C ANISOU 940 CG1 ILE A 165 4459 3494 4119 -105 868 -75 C ATOM 941 CG2 ILE A 165 29.921 6.056 22.109 1.00 31.03 C ANISOU 941 CG2 ILE A 165 4194 3395 4201 -3 879 -35 C ATOM 942 CD1 ILE A 165 29.337 7.512 19.252 1.00 27.28 C ANISOU 942 CD1 ILE A 165 3990 2871 3503 -100 998 -106 C ATOM 943 N LEU A 166 31.614 8.101 24.535 1.00 31.68 N ANISOU 943 N LEU A 166 3936 3659 4444 -40 743 51 N ATOM 944 CA LEU A 166 32.280 7.665 25.763 1.00 31.79 C ANISOU 944 CA LEU A 166 3810 3728 4541 -3 681 98 C ATOM 945 C LEU A 166 31.715 8.408 26.976 1.00 34.22 C ANISOU 945 C LEU A 166 4091 4105 4807 -51 547 102 C ATOM 946 O LEU A 166 31.528 7.798 28.028 1.00 35.09 O ANISOU 946 O LEU A 166 4162 4249 4921 -21 469 136 O ATOM 947 CB LEU A 166 33.805 7.865 25.677 1.00 32.72 C ANISOU 947 CB LEU A 166 3784 3875 4773 12 747 124 C ATOM 948 CG LEU A 166 34.586 6.720 25.057 1.00 39.69 C ANISOU 948 CG LEU A 166 4640 4703 5738 97 870 143 C ATOM 949 CD1 LEU A 166 35.965 7.181 24.628 1.00 40.69 C ANISOU 949 CD1 LEU A 166 4644 4848 5967 94 969 155 C ATOM 950 CD2 LEU A 166 34.681 5.508 26.008 1.00 42.44 C ANISOU 950 CD2 LEU A 166 4921 5058 6146 181 816 200 C ATOM 951 N GLY A 167 31.444 9.708 26.806 1.00 28.49 N ANISOU 951 N GLY A 167 3398 3391 4038 -123 531 68 N ATOM 952 CA GLY A 167 30.851 10.568 27.827 1.00 27.33 C ANISOU 952 CA GLY A 167 3248 3292 3845 -173 426 54 C ATOM 953 C GLY A 167 29.455 10.110 28.202 1.00 31.44 C ANISOU 953 C GLY A 167 3859 3800 4288 -157 369 51 C ATOM 954 O GLY A 167 29.137 10.048 29.389 1.00 31.41 O ANISOU 954 O GLY A 167 3826 3846 4264 -160 286 63 O ATOM 955 N ILE A 168 28.624 9.741 27.187 1.00 27.08 N ANISOU 955 N ILE A 168 3416 3185 3690 -144 415 34 N ATOM 956 CA ILE A 168 27.267 9.211 27.353 1.00 26.66 C ANISOU 956 CA ILE A 168 3439 3114 3575 -135 370 30 C ATOM 957 C ILE A 168 27.295 7.942 28.220 1.00 29.09 C ANISOU 957 C ILE A 168 3708 3434 3912 -88 341 68 C ATOM 958 O ILE A 168 26.500 7.848 29.153 1.00 29.38 O ANISOU 958 O ILE A 168 3749 3498 3915 -94 276 79 O ATOM 959 CB ILE A 168 26.520 9.014 25.990 1.00 29.67 C ANISOU 959 CB ILE A 168 3935 3432 3904 -140 417 5 C ATOM 960 CG1 ILE A 168 26.165 10.370 25.343 1.00 29.52 C ANISOU 960 CG1 ILE A 168 3969 3407 3841 -183 419 -16 C ATOM 961 CG2 ILE A 168 25.264 8.118 26.123 1.00 28.10 C ANISOU 961 CG2 ILE A 168 3794 3214 3667 -131 375 3 C ATOM 962 CD1 ILE A 168 26.023 10.308 23.803 1.00 33.80 C ANISOU 962 CD1 ILE A 168 4612 3898 4332 -188 483 -31 C ATOM 963 N TRP A 169 28.236 7.002 27.953 1.00 25.07 N ANISOU 963 N TRP A 169 3157 2900 3467 -38 398 94 N ATOM 964 CA TRP A 169 28.395 5.779 28.750 1.00 23.75 C ANISOU 964 CA TRP A 169 2951 2732 3340 18 379 145 C ATOM 965 C TRP A 169 28.873 6.093 30.171 1.00 27.26 C ANISOU 965 C TRP A 169 3296 3266 3797 19 292 189 C ATOM 966 O TRP A 169 28.264 5.609 31.113 1.00 27.73 O ANISOU 966 O TRP A 169 3365 3344 3825 30 235 222 O ATOM 967 CB TRP A 169 29.285 4.753 28.047 1.00 22.48 C ANISOU 967 CB TRP A 169 2775 2511 3257 82 474 162 C ATOM 968 CG TRP A 169 28.566 3.995 26.972 1.00 23.30 C ANISOU 968 CG TRP A 169 3003 2521 3330 85 542 122 C ATOM 969 CD1 TRP A 169 28.532 4.300 25.644 1.00 26.02 C ANISOU 969 CD1 TRP A 169 3426 2820 3639 59 616 67 C ATOM 970 CD2 TRP A 169 27.671 2.875 27.153 1.00 23.34 C ANISOU 970 CD2 TRP A 169 3078 2469 3322 98 533 128 C ATOM 971 NE1 TRP A 169 27.710 3.416 24.976 1.00 25.32 N ANISOU 971 NE1 TRP A 169 3452 2656 3511 55 646 33 N ATOM 972 CE2 TRP A 169 27.160 2.539 25.878 1.00 26.45 C ANISOU 972 CE2 TRP A 169 3588 2785 3674 74 597 67 C ATOM 973 CE3 TRP A 169 27.228 2.140 28.280 1.00 24.78 C ANISOU 973 CE3 TRP A 169 3241 2656 3516 120 477 182 C ATOM 974 CZ2 TRP A 169 26.267 1.474 25.683 1.00 25.57 C ANISOU 974 CZ2 TRP A 169 3568 2601 3548 66 605 48 C ATOM 975 CZ3 TRP A 169 26.357 1.073 28.086 1.00 26.24 C ANISOU 975 CZ3 TRP A 169 3515 2762 3695 118 497 173 C ATOM 976 CH2 TRP A 169 25.889 0.745 26.800 1.00 26.91 C ANISOU 976 CH2 TRP A 169 3707 2767 3750 87 559 103 C ATOM 977 N ALA A 170 29.905 6.963 30.328 1.00 23.75 N ANISOU 977 N ALA A 170 2759 2877 3387 -4 279 186 N ATOM 978 CA ALA A 170 30.408 7.409 31.638 1.00 23.31 C ANISOU 978 CA ALA A 170 2611 2916 3328 -23 183 214 C ATOM 979 C ALA A 170 29.289 8.026 32.515 1.00 28.94 C ANISOU 979 C ALA A 170 3389 3665 3943 -73 109 188 C ATOM 980 O ALA A 170 29.173 7.676 33.688 1.00 29.22 O ANISOU 980 O ALA A 170 3403 3756 3944 -62 37 227 O ATOM 981 CB ALA A 170 31.534 8.407 31.457 1.00 23.37 C ANISOU 981 CB ALA A 170 2525 2968 3388 -67 187 194 C ATOM 982 N VAL A 171 28.454 8.908 31.936 1.00 25.53 N ANISOU 982 N VAL A 171 3037 3197 3464 -121 133 128 N ATOM 983 CA VAL A 171 27.327 9.555 32.628 1.00 25.11 C ANISOU 983 CA VAL A 171 3044 3163 3332 -159 87 98 C ATOM 984 C VAL A 171 26.241 8.522 32.989 1.00 29.62 C ANISOU 984 C VAL A 171 3671 3715 3868 -125 80 129 C ATOM 985 O VAL A 171 25.828 8.450 34.157 1.00 29.11 O ANISOU 985 O VAL A 171 3607 3700 3754 -130 28 147 O ATOM 986 CB VAL A 171 26.770 10.779 31.835 1.00 27.75 C ANISOU 986 CB VAL A 171 3440 3457 3645 -206 120 38 C ATOM 987 CG1 VAL A 171 25.477 11.306 32.430 1.00 27.09 C ANISOU 987 CG1 VAL A 171 3419 3378 3497 -225 91 13 C ATOM 988 CG2 VAL A 171 27.808 11.896 31.769 1.00 27.52 C ANISOU 988 CG2 VAL A 171 3359 3449 3649 -256 123 9 C ATOM 989 N SER A 172 25.788 7.729 31.990 1.00 25.99 N ANISOU 989 N SER A 172 3261 3184 3429 -98 135 132 N ATOM 990 CA SER A 172 24.732 6.724 32.148 1.00 25.48 C ANISOU 990 CA SER A 172 3250 3086 3346 -79 137 155 C ATOM 991 C SER A 172 25.059 5.684 33.203 1.00 28.83 C ANISOU 991 C SER A 172 3638 3534 3782 -38 111 225 C ATOM 992 O SER A 172 24.192 5.342 34.006 1.00 27.93 O ANISOU 992 O SER A 172 3552 3434 3627 -44 88 248 O ATOM 993 CB SER A 172 24.436 6.051 30.815 1.00 29.38 C ANISOU 993 CB SER A 172 3803 3497 3865 -69 198 136 C ATOM 994 OG SER A 172 24.047 7.025 29.860 1.00 34.84 O ANISOU 994 OG SER A 172 4535 4172 4528 -105 212 84 O ATOM 995 N LEU A 173 26.321 5.203 33.218 1.00 25.73 N ANISOU 995 N LEU A 173 3179 3148 3449 7 117 266 N ATOM 996 CA LEU A 173 26.780 4.198 34.175 1.00 24.73 C ANISOU 996 CA LEU A 173 3011 3043 3342 61 87 350 C ATOM 997 C LEU A 173 26.818 4.742 35.602 1.00 28.36 C ANISOU 997 C LEU A 173 3439 3606 3731 37 -1 376 C ATOM 998 O LEU A 173 26.558 4.007 36.529 1.00 29.92 O ANISOU 998 O LEU A 173 3649 3822 3899 64 -29 442 O ATOM 999 CB LEU A 173 28.139 3.592 33.754 1.00 24.02 C ANISOU 999 CB LEU A 173 2843 2934 3348 125 120 392 C ATOM 1000 CG LEU A 173 28.140 2.605 32.559 1.00 27.62 C ANISOU 1000 CG LEU A 173 3347 3274 3873 169 221 383 C ATOM 1001 CD1 LEU A 173 29.540 2.484 31.937 1.00 26.29 C ANISOU 1001 CD1 LEU A 173 3093 3095 3800 221 274 397 C ATOM 1002 CD2 LEU A 173 27.587 1.223 32.945 1.00 28.36 C ANISOU 1002 CD2 LEU A 173 3494 3300 3981 213 239 442 C ATOM 1003 N ALA A 174 27.088 6.031 35.775 1.00 24.60 N ANISOU 1003 N ALA A 174 2935 3191 3220 -17 -38 321 N ATOM 1004 CA ALA A 174 27.151 6.653 37.092 1.00 23.38 C ANISOU 1004 CA ALA A 174 2765 3133 2985 -53 -120 325 C ATOM 1005 C ALA A 174 25.792 7.063 37.644 1.00 26.90 C ANISOU 1005 C ALA A 174 3298 3583 3341 -92 -116 289 C ATOM 1006 O ALA A 174 25.513 6.789 38.810 1.00 27.23 O ANISOU 1006 O ALA A 174 3359 3679 3310 -91 -157 328 O ATOM 1007 CB ALA A 174 28.083 7.854 37.062 1.00 23.62 C ANISOU 1007 CB ALA A 174 2731 3219 3025 -105 -157 272 C ATOM 1008 N ILE A 175 24.952 7.733 36.838 1.00 22.33 N ANISOU 1008 N ILE A 175 2768 2949 2766 -123 -66 220 N ATOM 1009 CA ILE A 175 23.658 8.258 37.300 1.00 21.46 C ANISOU 1009 CA ILE A 175 2723 2842 2590 -154 -52 183 C ATOM 1010 C ILE A 175 22.639 7.146 37.631 1.00 28.16 C ANISOU 1010 C ILE A 175 3613 3664 3424 -129 -26 235 C ATOM 1011 O ILE A 175 21.637 7.426 38.294 1.00 27.88 O ANISOU 1011 O ILE A 175 3616 3646 3332 -149 -13 222 O ATOM 1012 CB ILE A 175 23.071 9.338 36.335 1.00 23.71 C ANISOU 1012 CB ILE A 175 3038 3078 2893 -185 -13 107 C ATOM 1013 CG1 ILE A 175 22.564 8.732 35.014 1.00 23.18 C ANISOU 1013 CG1 ILE A 175 2993 2931 2882 -163 35 112 C ATOM 1014 CG2 ILE A 175 24.099 10.487 36.097 1.00 24.51 C ANISOU 1014 CG2 ILE A 175 3106 3197 3010 -221 -31 59 C ATOM 1015 CD1 ILE A 175 21.818 9.687 34.122 1.00 27.40 C ANISOU 1015 CD1 ILE A 175 3564 3425 3422 -185 61 59 C ATOM 1016 N MET A 176 22.912 5.890 37.208 1.00 25.51 N ANISOU 1016 N MET A 176 3267 3280 3144 -85 -8 295 N ATOM 1017 CA MET A 176 22.009 4.770 37.471 1.00 24.52 C ANISOU 1017 CA MET A 176 3182 3115 3020 -70 24 346 C ATOM 1018 C MET A 176 22.464 3.927 38.657 1.00 28.64 C ANISOU 1018 C MET A 176 3697 3678 3507 -36 -7 439 C ATOM 1019 O MET A 176 21.779 2.969 39.021 1.00 28.04 O ANISOU 1019 O MET A 176 3658 3567 3430 -25 24 495 O ATOM 1020 CB MET A 176 21.756 3.929 36.205 1.00 26.13 C ANISOU 1020 CB MET A 176 3406 3219 3303 -56 75 341 C ATOM 1021 CG MET A 176 20.981 4.686 35.132 1.00 28.34 C ANISOU 1021 CG MET A 176 3708 3467 3592 -95 97 262 C ATOM 1022 SD MET A 176 19.451 5.506 35.728 1.00 31.02 S ANISOU 1022 SD MET A 176 4067 3841 3877 -139 98 230 S ATOM 1023 CE MET A 176 18.943 6.346 34.204 1.00 26.82 C ANISOU 1023 CE MET A 176 3548 3268 3375 -162 107 158 C ATOM 1024 N VAL A 177 23.597 4.314 39.301 1.00 25.34 N ANISOU 1024 N VAL A 177 3230 3338 3059 -24 -72 460 N ATOM 1025 CA VAL A 177 24.089 3.633 40.507 1.00 24.81 C ANISOU 1025 CA VAL A 177 3155 3331 2942 10 -123 558 C ATOM 1026 C VAL A 177 23.016 3.770 41.640 1.00 30.76 C ANISOU 1026 C VAL A 177 3978 4128 3581 -25 -115 567 C ATOM 1027 O VAL A 177 22.708 2.738 42.236 1.00 31.32 O ANISOU 1027 O VAL A 177 4083 4184 3635 4 -99 658 O ATOM 1028 CB VAL A 177 25.537 4.029 40.909 1.00 26.76 C ANISOU 1028 CB VAL A 177 3321 3664 3181 23 -212 579 C ATOM 1029 CG1 VAL A 177 25.951 3.387 42.226 1.00 25.36 C ANISOU 1029 CG1 VAL A 177 3141 3563 2931 57 -282 688 C ATOM 1030 CG2 VAL A 177 26.522 3.647 39.810 1.00 26.29 C ANISOU 1030 CG2 VAL A 177 3189 3551 3250 70 -192 587 C ATOM 1031 N PRO A 178 22.325 4.934 41.856 1.00 28.03 N ANISOU 1031 N PRO A 178 3663 3817 3171 -82 -104 478 N ATOM 1032 CA PRO A 178 21.236 4.970 42.863 1.00 27.61 C ANISOU 1032 CA PRO A 178 3676 3793 3021 -108 -68 487 C ATOM 1033 C PRO A 178 20.103 3.961 42.609 1.00 31.76 C ANISOU 1033 C PRO A 178 4233 4239 3595 -98 13 532 C ATOM 1034 O PRO A 178 19.575 3.404 43.573 1.00 30.47 O ANISOU 1034 O PRO A 178 4115 4096 3365 -98 38 597 O ATOM 1035 CB PRO A 178 20.733 6.417 42.791 1.00 29.24 C ANISOU 1035 CB PRO A 178 3898 4019 3193 -158 -50 371 C ATOM 1036 CG PRO A 178 21.905 7.191 42.279 1.00 33.41 C ANISOU 1036 CG PRO A 178 4374 4567 3753 -169 -111 320 C ATOM 1037 CD PRO A 178 22.530 6.280 41.269 1.00 29.39 C ANISOU 1037 CD PRO A 178 3814 3998 3355 -123 -113 371 C ATOM 1038 N GLN A 179 19.769 3.676 41.321 1.00 28.64 N ANISOU 1038 N GLN A 179 3818 3753 3310 -95 51 502 N ATOM 1039 CA GLN A 179 18.756 2.674 40.949 1.00 27.54 C ANISOU 1039 CA GLN A 179 3702 3532 3231 -100 118 535 C ATOM 1040 C GLN A 179 19.160 1.277 41.447 1.00 32.67 C ANISOU 1040 C GLN A 179 4371 4148 3893 -60 122 650 C ATOM 1041 O GLN A 179 18.318 0.578 42.010 1.00 32.90 O ANISOU 1041 O GLN A 179 4439 4154 3908 -74 174 706 O ATOM 1042 CB GLN A 179 18.531 2.636 39.423 1.00 28.23 C ANISOU 1042 CB GLN A 179 3769 3536 3420 -110 138 475 C ATOM 1043 CG GLN A 179 17.334 1.750 38.996 1.00 34.19 C ANISOU 1043 CG GLN A 179 4544 4211 4234 -138 197 487 C ATOM 1044 CD GLN A 179 15.982 2.287 39.430 1.00 43.98 C ANISOU 1044 CD GLN A 179 5782 5482 5446 -182 235 461 C ATOM 1045 OE1 GLN A 179 15.767 3.496 39.550 1.00 40.48 O ANISOU 1045 OE1 GLN A 179 5318 5075 4987 -196 227 391 O ATOM 1046 NE2 GLN A 179 15.027 1.402 39.670 1.00 30.09 N ANISOU 1046 NE2 GLN A 179 4042 3702 3689 -202 287 520 N ATOM 1047 N ALA A 180 20.434 0.863 41.211 1.00 28.38 N ANISOU 1047 N ALA A 180 3798 3596 3388 -7 77 692 N ATOM 1048 CA ALA A 180 20.989 -0.430 41.639 1.00 27.71 C ANISOU 1048 CA ALA A 180 3726 3473 3331 52 77 813 C ATOM 1049 C ALA A 180 21.018 -0.537 43.178 1.00 33.38 C ANISOU 1049 C ALA A 180 4477 4278 3929 60 45 904 C ATOM 1050 O ALA A 180 20.697 -1.588 43.725 1.00 34.81 O ANISOU 1050 O ALA A 180 4702 4415 4108 81 81 1006 O ATOM 1051 CB ALA A 180 22.390 -0.615 41.064 1.00 28.05 C ANISOU 1051 CB ALA A 180 3709 3505 3443 113 34 830 C ATOM 1052 N ALA A 181 21.330 0.571 43.869 1.00 29.24 N ANISOU 1052 N ALA A 181 3941 3872 3296 36 -18 863 N ATOM 1053 CA ALA A 181 21.384 0.670 45.330 1.00 28.44 C ANISOU 1053 CA ALA A 181 3884 3874 3050 32 -58 927 C ATOM 1054 C ALA A 181 20.061 0.317 46.045 1.00 33.15 C ANISOU 1054 C ALA A 181 4558 4455 3581 -3 29 959 C ATOM 1055 O ALA A 181 20.098 -0.318 47.103 1.00 33.06 O ANISOU 1055 O ALA A 181 4599 4479 3481 17 24 1069 O ATOM 1056 CB ALA A 181 21.828 2.066 45.724 1.00 28.76 C ANISOU 1056 CB ALA A 181 3906 4026 2996 -8 -129 837 C ATOM 1057 N VAL A 182 18.905 0.736 45.481 1.00 29.36 N ANISOU 1057 N VAL A 182 4083 3929 3144 -53 109 869 N ATOM 1058 CA VAL A 182 17.582 0.530 46.078 1.00 28.90 C ANISOU 1058 CA VAL A 182 4077 3860 3044 -92 205 886 C ATOM 1059 C VAL A 182 16.981 -0.849 45.741 1.00 35.04 C ANISOU 1059 C VAL A 182 4870 4523 3921 -88 278 968 C ATOM 1060 O VAL A 182 16.028 -1.262 46.390 1.00 34.99 O ANISOU 1060 O VAL A 182 4907 4507 3881 -118 359 1017 O ATOM 1061 CB VAL A 182 16.578 1.687 45.776 1.00 32.98 C ANISOU 1061 CB VAL A 182 4578 4391 3562 -144 257 761 C ATOM 1062 CG1 VAL A 182 17.091 3.026 46.312 1.00 32.77 C ANISOU 1062 CG1 VAL A 182 4560 4465 3426 -156 203 681 C ATOM 1063 CG2 VAL A 182 16.236 1.782 44.288 1.00 32.80 C ANISOU 1063 CG2 VAL A 182 4496 4282 3685 -155 270 687 C ATOM 1064 N MET A 183 17.517 -1.551 44.722 1.00 32.44 N ANISOU 1064 N MET A 183 4508 4101 3716 -57 261 978 N ATOM 1065 CA MET A 183 16.992 -2.850 44.301 1.00 31.05 C ANISOU 1065 CA MET A 183 4355 3798 3645 -62 332 1039 C ATOM 1066 C MET A 183 17.232 -3.897 45.353 1.00 39.32 C ANISOU 1066 C MET A 183 5462 4832 4645 -24 350 1191 C ATOM 1067 O MET A 183 18.349 -4.039 45.850 1.00 39.38 O ANISOU 1067 O MET A 183 5472 4887 4603 42 277 1266 O ATOM 1068 CB MET A 183 17.569 -3.308 42.957 1.00 32.04 C ANISOU 1068 CB MET A 183 4448 3823 3901 -36 317 1001 C ATOM 1069 CG MET A 183 17.221 -2.422 41.785 1.00 33.99 C ANISOU 1069 CG MET A 183 4650 4067 4198 -77 308 862 C ATOM 1070 SD MET A 183 15.550 -1.757 41.728 1.00 36.07 S ANISOU 1070 SD MET A 183 4901 4350 4454 -164 366 785 S ATOM 1071 CE MET A 183 14.602 -3.232 41.323 1.00 31.94 C ANISOU 1071 CE MET A 183 4405 3690 4040 -213 448 830 C ATOM 1072 N GLU A 184 16.173 -4.606 45.717 1.00 38.32 N ANISOU 1072 N GLU A 184 5380 4645 4534 -68 445 1243 N ATOM 1073 CA GLU A 184 16.245 -5.657 46.708 1.00 39.77 C ANISOU 1073 CA GLU A 184 5635 4800 4675 -39 481 1400 C ATOM 1074 C GLU A 184 15.414 -6.861 46.298 1.00 44.37 C ANISOU 1074 C GLU A 184 6247 5229 5383 -80 586 1443 C ATOM 1075 O GLU A 184 14.328 -6.708 45.727 1.00 41.89 O ANISOU 1075 O GLU A 184 5905 4877 5134 -160 648 1358 O ATOM 1076 CB GLU A 184 15.806 -5.127 48.075 1.00 41.98 C ANISOU 1076 CB GLU A 184 5964 5202 4785 -62 501 1441 C ATOM 1077 CG GLU A 184 16.766 -5.524 49.183 1.00 63.18 C ANISOU 1077 CG GLU A 184 8708 7948 7350 7 440 1587 C ATOM 1078 CD GLU A 184 18.160 -4.920 49.116 1.00 98.69 C ANISOU 1078 CD GLU A 184 13159 12531 11806 74 298 1575 C ATOM 1079 OE1 GLU A 184 19.137 -5.702 49.089 1.00101.67 O ANISOU 1079 OE1 GLU A 184 13533 12868 12231 153 246 1684 O ATOM 1080 OE2 GLU A 184 18.278 -3.673 49.088 1.00 96.55 O ANISOU 1080 OE2 GLU A 184 12852 12364 11469 47 241 1458 O ATOM 1081 N CYS A 185 15.954 -8.059 46.554 1.00 43.81 N ANISOU 1081 N CYS A 185 6228 5065 5354 -24 601 1576 N ATOM 1082 CA CYS A 185 15.281 -9.318 46.279 1.00 45.15 C ANISOU 1082 CA CYS A 185 6444 5071 5642 -63 705 1632 C ATOM 1083 C CYS A 185 14.748 -9.871 47.591 1.00 52.44 C ANISOU 1083 C CYS A 185 7444 6003 6478 -77 780 1777 C ATOM 1084 O CYS A 185 15.513 -10.098 48.533 1.00 52.48 O ANISOU 1084 O CYS A 185 7498 6061 6382 0 738 1908 O ATOM 1085 CB CYS A 185 16.202 -10.307 45.577 1.00 45.85 C ANISOU 1085 CB CYS A 185 6547 5020 5854 11 694 1678 C ATOM 1086 SG CYS A 185 15.358 -11.805 45.004 1.00 50.42 S ANISOU 1086 SG CYS A 185 7190 5369 6600 -54 825 1708 S ATOM 1087 N SER A 186 13.433 -10.033 47.674 1.00 52.00 N ANISOU 1087 N SER A 186 7394 5908 6453 -179 887 1755 N ATOM 1088 CA SER A 186 12.801 -10.533 48.893 1.00 53.82 C ANISOU 1088 CA SER A 186 7700 6146 6604 -206 983 1889 C ATOM 1089 C SER A 186 11.764 -11.600 48.611 1.00 62.09 C ANISOU 1089 C SER A 186 8770 7033 7789 -296 1113 1921 C ATOM 1090 O SER A 186 11.104 -11.573 47.576 1.00 60.91 O ANISOU 1090 O SER A 186 8556 6819 7767 -374 1135 1798 O ATOM 1091 CB SER A 186 12.165 -9.385 49.674 1.00 58.07 C ANISOU 1091 CB SER A 186 8221 6847 6994 -247 1000 1837 C ATOM 1092 OG SER A 186 11.226 -8.679 48.876 1.00 69.95 O ANISOU 1092 OG SER A 186 9636 8362 8580 -328 1029 1682 O ATOM 1093 N SER A 187 11.579 -12.510 49.573 1.00 63.64 N ANISOU 1093 N SER A 187 9059 7170 7951 -292 1200 2088 N ATOM 1094 CA SER A 187 10.567 -13.556 49.460 1.00 65.09 C ANISOU 1094 CA SER A 187 9272 7197 8262 -389 1339 2134 C ATOM 1095 C SER A 187 9.317 -13.129 50.205 1.00 72.02 C ANISOU 1095 C SER A 187 10134 8157 9074 -484 1448 2135 C ATOM 1096 O SER A 187 9.410 -12.645 51.338 1.00 71.18 O ANISOU 1096 O SER A 187 10075 8179 8790 -448 1458 2209 O ATOM 1097 CB SER A 187 11.083 -14.887 49.995 1.00 68.70 C ANISOU 1097 CB SER A 187 9844 7513 8745 -331 1388 2326 C ATOM 1098 OG SER A 187 10.265 -15.949 49.528 1.00 77.27 O ANISOU 1098 OG SER A 187 10952 8411 9996 -433 1511 2339 O ATOM 1099 N VAL A 188 8.149 -13.284 49.551 1.00 71.66 N ANISOU 1099 N VAL A 188 10017 8042 9168 -608 1529 2046 N ATOM 1100 CA VAL A 188 6.831 -12.957 50.116 1.00 72.78 C ANISOU 1100 CA VAL A 188 10115 8244 9293 -709 1653 2039 C ATOM 1101 C VAL A 188 6.496 -13.936 51.285 1.00 78.48 C ANISOU 1101 C VAL A 188 10948 8899 9970 -732 1797 2232 C ATOM 1102 O VAL A 188 5.811 -13.556 52.234 1.00 77.86 O ANISOU 1102 O VAL A 188 10880 8916 9789 -765 1897 2275 O ATOM 1103 CB VAL A 188 5.705 -12.834 49.034 1.00 76.80 C ANISOU 1103 CB VAL A 188 10494 8707 9979 -835 1680 1893 C ATOM 1104 CG1 VAL A 188 6.138 -11.935 47.874 1.00 76.21 C ANISOU 1104 CG1 VAL A 188 10330 8695 9930 -802 1535 1724 C ATOM 1105 CG2 VAL A 188 5.247 -14.197 48.514 1.00 76.83 C ANISOU 1105 CG2 VAL A 188 10521 8507 10163 -928 1752 1929 C ATOM 1106 N LEU A 189 7.047 -15.174 51.209 1.00 76.30 N ANISOU 1106 N LEU A 189 10766 8458 9768 -704 1810 2349 N ATOM 1107 CA LEU A 189 6.959 -16.250 52.191 1.00 76.81 C ANISOU 1107 CA LEU A 189 10956 8425 9804 -706 1931 2553 C ATOM 1108 C LEU A 189 8.407 -16.659 52.561 1.00 81.64 C ANISOU 1108 C LEU A 189 11675 9018 10328 -551 1830 2684 C ATOM 1109 O LEU A 189 8.999 -17.504 51.880 1.00 80.56 O ANISOU 1109 O LEU A 189 11565 8720 10323 -514 1800 2703 O ATOM 1110 CB LEU A 189 6.154 -17.439 51.627 1.00 77.21 C ANISOU 1110 CB LEU A 189 11007 8259 10069 -830 2052 2568 C ATOM 1111 CG LEU A 189 4.627 -17.265 51.579 1.00 82.42 C ANISOU 1111 CG LEU A 189 11566 8934 10818 -993 2177 2492 C ATOM 1112 CD1 LEU A 189 4.014 -18.131 50.493 1.00 82.74 C ANISOU 1112 CD1 LEU A 189 11559 8782 11096 -1121 2215 2416 C ATOM 1113 CD2 LEU A 189 3.984 -17.574 52.931 1.00 84.70 C ANISOU 1113 CD2 LEU A 189 11924 9247 11010 -1034 2346 2653 C ATOM 1114 N PRO A 190 9.006 -16.011 53.604 1.00 79.91 N ANISOU 1114 N PRO A 190 11509 8968 9885 -459 1772 2764 N ATOM 1115 CA PRO A 190 10.427 -16.271 53.951 1.00 80.44 C ANISOU 1115 CA PRO A 190 11650 9047 9865 -308 1649 2886 C ATOM 1116 C PRO A 190 10.857 -17.725 54.190 1.00 86.99 C ANISOU 1116 C PRO A 190 12594 9687 10770 -255 1704 3088 C ATOM 1117 O PRO A 190 11.980 -18.091 53.832 1.00 86.82 O ANISOU 1117 O PRO A 190 12587 9611 10789 -136 1602 3139 O ATOM 1118 CB PRO A 190 10.635 -15.440 55.221 1.00 81.87 C ANISOU 1118 CB PRO A 190 11883 9444 9782 -262 1608 2946 C ATOM 1119 CG PRO A 190 9.637 -14.354 55.130 1.00 85.78 C ANISOU 1119 CG PRO A 190 12293 10056 10244 -362 1661 2779 C ATOM 1120 CD PRO A 190 8.436 -14.946 54.459 1.00 81.18 C ANISOU 1120 CD PRO A 190 11659 9322 9864 -490 1807 2733 C ATOM 1121 N GLU A 191 9.976 -18.540 54.796 1.00 85.19 N ANISOU 1121 N GLU A 191 12445 9355 10568 -338 1873 3209 N ATOM 1122 CA GLU A 191 10.211 -19.950 55.145 1.00 85.73 C ANISOU 1122 CA GLU A 191 12639 9225 10710 -301 1957 3418 C ATOM 1123 C GLU A 191 10.311 -20.914 53.932 1.00 90.23 C ANISOU 1123 C GLU A 191 13193 9549 11543 -317 1980 3364 C ATOM 1124 O GLU A 191 10.655 -22.084 54.125 1.00 90.41 O ANISOU 1124 O GLU A 191 13320 9391 11642 -257 2031 3531 O ATOM 1125 CB GLU A 191 9.159 -20.457 56.165 1.00 87.21 C ANISOU 1125 CB GLU A 191 12916 9374 10843 -401 2148 3558 C ATOM 1126 CG GLU A 191 7.705 -20.125 55.842 1.00 99.37 C ANISOU 1126 CG GLU A 191 14364 10916 12477 -581 2279 3411 C ATOM 1127 CD GLU A 191 7.264 -18.692 56.100 1.00120.08 C ANISOU 1127 CD GLU A 191 16894 13778 14951 -614 2247 3269 C ATOM 1128 OE1 GLU A 191 7.393 -18.225 57.255 1.00122.46 O ANISOU 1128 OE1 GLU A 191 17271 14236 15023 -567 2254 3364 O ATOM 1129 OE2 GLU A 191 6.790 -18.036 55.144 1.00104.05 O ANISOU 1129 OE2 GLU A 191 14725 11778 13033 -685 2216 3063 O ATOM 1130 N LEU A 192 10.039 -20.425 52.700 1.00 86.08 N ANISOU 1130 N LEU A 192 12546 9013 11147 -393 1942 3135 N ATOM 1131 CA LEU A 192 10.079 -21.224 51.465 1.00 85.27 C ANISOU 1131 CA LEU A 192 12429 8692 11276 -427 1960 3046 C ATOM 1132 C LEU A 192 11.195 -20.796 50.500 1.00 86.61 C ANISOU 1132 C LEU A 192 12537 8894 11478 -316 1804 2927 C ATOM 1133 O LEU A 192 11.443 -21.492 49.508 1.00 85.71 O ANISOU 1133 O LEU A 192 12431 8598 11538 -318 1815 2860 O ATOM 1134 CB LEU A 192 8.714 -21.174 50.748 1.00 85.53 C ANISOU 1134 CB LEU A 192 12381 8672 11444 -622 2049 2880 C ATOM 1135 CG LEU A 192 7.514 -21.759 51.495 1.00 90.76 C ANISOU 1135 CG LEU A 192 13088 9260 12136 -759 2230 2981 C ATOM 1136 CD1 LEU A 192 6.221 -21.147 51.001 1.00 90.92 C ANISOU 1136 CD1 LEU A 192 12973 9350 12221 -929 2271 2806 C ATOM 1137 CD2 LEU A 192 7.473 -23.289 51.391 1.00 93.86 C ANISOU 1137 CD2 LEU A 192 13596 9366 12701 -791 2348 3096 C ATOM 1138 N ALA A 193 11.862 -19.658 50.800 1.00 81.60 N ANISOU 1138 N ALA A 193 11845 8484 10676 -226 1667 2896 N ATOM 1139 CA ALA A 193 12.945 -19.047 50.017 1.00 80.48 C ANISOU 1139 CA ALA A 193 11629 8412 10539 -122 1516 2788 C ATOM 1140 C ALA A 193 14.129 -19.978 49.743 1.00 81.86 C ANISOU 1140 C ALA A 193 11858 8434 10812 19 1488 2892 C ATOM 1141 O ALA A 193 14.745 -19.879 48.680 1.00 81.19 O ANISOU 1141 O ALA A 193 11717 8305 10825 62 1427 2770 O ATOM 1142 CB ALA A 193 13.427 -17.782 50.703 1.00 81.21 C ANISOU 1142 CB ALA A 193 11673 8763 10419 -59 1394 2780 C ATOM 1143 N ALA A 194 14.441 -20.874 50.697 1.00 77.00 N ANISOU 1143 N ALA A 194 11351 7734 10170 96 1540 3123 N ATOM 1144 CA ALA A 194 15.535 -21.843 50.591 1.00 76.06 C ANISOU 1144 CA ALA A 194 11288 7458 10152 247 1528 3259 C ATOM 1145 C ALA A 194 15.266 -22.960 49.559 1.00 77.87 C ANISOU 1145 C ALA A 194 11564 7399 10623 199 1648 3200 C ATOM 1146 O ALA A 194 16.227 -23.509 49.006 1.00 78.19 O ANISOU 1146 O ALA A 194 11614 7313 10779 321 1628 3222 O ATOM 1147 CB ALA A 194 15.824 -22.449 51.955 1.00 76.72 C ANISOU 1147 CB ALA A 194 11479 7542 10127 338 1550 3534 C ATOM 1148 N ARG A 195 13.974 -23.296 49.302 1.00 71.12 N ANISOU 1148 N ARG A 195 10736 6437 9848 19 1775 3121 N ATOM 1149 CA ARG A 195 13.600 -24.363 48.361 1.00 69.00 C ANISOU 1149 CA ARG A 195 10526 5892 9801 -58 1892 3053 C ATOM 1150 C ARG A 195 13.132 -23.878 46.976 1.00 67.03 C ANISOU 1150 C ARG A 195 10190 5637 9640 -181 1867 2778 C ATOM 1151 O ARG A 195 13.271 -24.632 46.010 1.00 66.89 O ANISOU 1151 O ARG A 195 10217 5410 9789 -200 1921 2696 O ATOM 1152 CB ARG A 195 12.575 -25.351 48.948 1.00 70.76 C ANISOU 1152 CB ARG A 195 10854 5942 10088 -177 2061 3174 C ATOM 1153 CG ARG A 195 11.680 -24.846 50.081 1.00 81.60 C ANISOU 1153 CG ARG A 195 12219 7482 11303 -266 2099 3253 C ATOM 1154 CD ARG A 195 12.034 -25.538 51.384 1.00 85.64 C ANISOU 1154 CD ARG A 195 12850 7969 11719 -157 2145 3539 C ATOM 1155 NE ARG A 195 10.986 -25.377 52.393 1.00 90.32 N ANISOU 1155 NE ARG A 195 13472 8647 12199 -271 2242 3624 N ATOM 1156 CZ ARG A 195 10.116 -26.323 52.732 1.00100.70 C ANISOU 1156 CZ ARG A 195 14878 9778 13604 -381 2417 3728 C ATOM 1157 NH1 ARG A 195 10.163 -27.517 52.153 1.00 78.74 N ANISOU 1157 NH1 ARG A 195 12178 6708 11031 -396 2510 3758 N ATOM 1158 NH2 ARG A 195 9.199 -26.087 53.660 1.00 93.36 N ANISOU 1158 NH2 ARG A 195 13965 8945 12561 -480 2511 3803 N ATOM 1159 N THR A 196 12.598 -22.645 46.863 1.00 58.56 N ANISOU 1159 N THR A 196 9004 4788 8457 -261 1787 2637 N ATOM 1160 CA THR A 196 12.133 -22.118 45.570 1.00 55.76 C ANISOU 1160 CA THR A 196 8566 4448 8172 -373 1749 2390 C ATOM 1161 C THR A 196 12.293 -20.594 45.436 1.00 55.63 C ANISOU 1161 C THR A 196 8424 4700 8014 -350 1610 2270 C ATOM 1162 O THR A 196 12.283 -19.880 46.441 1.00 54.93 O ANISOU 1162 O THR A 196 8306 4794 7769 -310 1569 2354 O ATOM 1163 CB THR A 196 10.675 -22.576 45.264 1.00 55.70 C ANISOU 1163 CB THR A 196 8562 4334 8267 -586 1859 2312 C ATOM 1164 OG1 THR A 196 10.371 -22.289 43.900 1.00 53.34 O ANISOU 1164 OG1 THR A 196 8202 4014 8049 -683 1813 2085 O ATOM 1165 CG2 THR A 196 9.618 -21.936 46.187 1.00 48.16 C ANISOU 1165 CG2 THR A 196 7548 3549 7202 -681 1887 2353 C ATOM 1166 N ARG A 197 12.407 -20.114 44.180 1.00 49.50 N ANISOU 1166 N ARG A 197 7583 3935 7288 -382 1545 2072 N ATOM 1167 CA ARG A 197 12.470 -18.695 43.805 1.00 48.50 C ANISOU 1167 CA ARG A 197 7341 4028 7058 -379 1423 1935 C ATOM 1168 C ARG A 197 11.092 -18.210 43.292 1.00 51.71 C ANISOU 1168 C ARG A 197 7675 4484 7490 -557 1436 1784 C ATOM 1169 O ARG A 197 10.964 -17.070 42.839 1.00 51.82 O ANISOU 1169 O ARG A 197 7594 4655 7440 -573 1346 1656 O ATOM 1170 CB ARG A 197 13.535 -18.462 42.718 1.00 46.93 C ANISOU 1170 CB ARG A 197 7122 3812 6898 -287 1345 1828 C ATOM 1171 CG ARG A 197 14.954 -18.538 43.235 1.00 52.05 C ANISOU 1171 CG ARG A 197 7787 4489 7501 -99 1296 1961 C ATOM 1172 CD ARG A 197 15.990 -18.431 42.138 1.00 52.44 C ANISOU 1172 CD ARG A 197 7814 4498 7613 -12 1248 1861 C ATOM 1173 NE ARG A 197 17.314 -18.312 42.740 1.00 59.17 N ANISOU 1173 NE ARG A 197 8646 5418 8419 166 1184 1992 N ATOM 1174 CZ ARG A 197 18.453 -18.207 42.065 1.00 69.84 C ANISOU 1174 CZ ARG A 197 9962 6758 9817 278 1142 1951 C ATOM 1175 NH1 ARG A 197 18.451 -18.206 40.736 1.00 53.83 N ANISOU 1175 NH1 ARG A 197 7932 4650 7872 232 1165 1778 N ATOM 1176 NH2 ARG A 197 19.604 -18.108 42.713 1.00 52.68 N ANISOU 1176 NH2 ARG A 197 7752 4658 7607 434 1078 2085 N ATOM 1177 N ALA A 198 10.074 -19.081 43.361 1.00 47.13 N ANISOU 1177 N ALA A 198 7134 3766 7009 -691 1548 1806 N ATOM 1178 CA ALA A 198 8.707 -18.842 42.897 1.00 46.41 C ANISOU 1178 CA ALA A 198 6965 3698 6972 -871 1569 1683 C ATOM 1179 C ALA A 198 8.012 -17.683 43.592 1.00 49.81 C ANISOU 1179 C ALA A 198 7291 4350 7286 -898 1543 1681 C ATOM 1180 O ALA A 198 7.197 -17.008 42.969 1.00 49.12 O ANISOU 1180 O ALA A 198 7099 4345 7219 -997 1504 1545 O ATOM 1181 CB ALA A 198 7.881 -20.099 43.069 1.00 46.93 C ANISOU 1181 CB ALA A 198 7098 3565 7169 -999 1706 1743 C ATOM 1182 N PHE A 199 8.318 -17.464 44.877 1.00 46.40 N ANISOU 1182 N PHE A 199 6890 4012 6730 -810 1568 1832 N ATOM 1183 CA PHE A 199 7.682 -16.429 45.700 1.00 46.36 C ANISOU 1183 CA PHE A 199 6810 4204 6602 -828 1571 1844 C ATOM 1184 C PHE A 199 8.667 -15.260 46.005 1.00 50.86 C ANISOU 1184 C PHE A 199 7355 4959 7009 -688 1451 1832 C ATOM 1185 O PHE A 199 8.423 -14.421 46.879 1.00 52.06 O ANISOU 1185 O PHE A 199 7478 5271 7029 -672 1453 1860 O ATOM 1186 CB PHE A 199 7.028 -17.067 46.949 1.00 47.68 C ANISOU 1186 CB PHE A 199 7038 4332 6746 -873 1714 2012 C ATOM 1187 CG PHE A 199 6.194 -18.292 46.614 1.00 49.04 C ANISOU 1187 CG PHE A 199 7242 4298 7094 -1012 1832 2028 C ATOM 1188 CD1 PHE A 199 4.934 -18.163 46.035 1.00 51.91 C ANISOU 1188 CD1 PHE A 199 7499 4660 7564 -1177 1868 1911 C ATOM 1189 CD2 PHE A 199 6.689 -19.573 46.836 1.00 51.05 C ANISOU 1189 CD2 PHE A 199 7628 4352 7416 -979 1902 2157 C ATOM 1190 CE1 PHE A 199 4.181 -19.296 45.690 1.00 52.79 C ANISOU 1190 CE1 PHE A 199 7635 4578 7843 -1322 1969 1915 C ATOM 1191 CE2 PHE A 199 5.939 -20.704 46.485 1.00 53.73 C ANISOU 1191 CE2 PHE A 199 8005 4484 7926 -1118 2015 2161 C ATOM 1192 CZ PHE A 199 4.684 -20.558 45.930 1.00 51.69 C ANISOU 1192 CZ PHE A 199 7640 4233 7768 -1296 2046 2037 C ATOM 1193 N SER A 200 9.742 -15.168 45.189 1.00 45.40 N ANISOU 1193 N SER A 200 6670 4242 6336 -600 1351 1771 N ATOM 1194 CA SER A 200 10.767 -14.132 45.286 1.00 44.48 C ANISOU 1194 CA SER A 200 6523 4279 6097 -480 1232 1745 C ATOM 1195 C SER A 200 10.424 -12.989 44.361 1.00 45.77 C ANISOU 1195 C SER A 200 6581 4548 6262 -525 1155 1563 C ATOM 1196 O SER A 200 10.022 -13.215 43.222 1.00 44.74 O ANISOU 1196 O SER A 200 6421 4333 6246 -601 1150 1449 O ATOM 1197 CB SER A 200 12.142 -14.692 44.935 1.00 48.75 C ANISOU 1197 CB SER A 200 7119 4733 6672 -356 1180 1791 C ATOM 1198 OG SER A 200 12.665 -15.448 46.013 1.00 62.82 O ANISOU 1198 OG SER A 200 8989 6469 8412 -274 1219 1984 O ATOM 1199 N VAL A 201 10.583 -11.760 44.848 1.00 41.60 N ANISOU 1199 N VAL A 201 6002 4201 5602 -482 1094 1536 N ATOM 1200 CA VAL A 201 10.283 -10.542 44.088 1.00 41.28 C ANISOU 1200 CA VAL A 201 5865 4270 5551 -511 1022 1379 C ATOM 1201 C VAL A 201 11.461 -9.561 44.130 1.00 43.08 C ANISOU 1201 C VAL A 201 6080 4617 5673 -402 912 1351 C ATOM 1202 O VAL A 201 12.052 -9.350 45.197 1.00 42.79 O ANISOU 1202 O VAL A 201 6081 4663 5516 -331 897 1445 O ATOM 1203 CB VAL A 201 8.934 -9.862 44.501 1.00 45.45 C ANISOU 1203 CB VAL A 201 6322 4891 6058 -600 1080 1342 C ATOM 1204 CG1 VAL A 201 7.725 -10.744 44.147 1.00 45.21 C ANISOU 1204 CG1 VAL A 201 6267 4745 6168 -730 1168 1330 C ATOM 1205 CG2 VAL A 201 8.913 -9.443 45.974 1.00 45.52 C ANISOU 1205 CG2 VAL A 201 6368 5008 5921 -563 1131 1445 C ATOM 1206 N CYS A 202 11.791 -8.965 42.969 1.00 37.13 N ANISOU 1206 N CYS A 202 5275 3874 4960 -395 835 1223 N ATOM 1207 CA CYS A 202 12.827 -7.951 42.846 1.00 35.94 C ANISOU 1207 CA CYS A 202 5097 3830 4729 -312 736 1177 C ATOM 1208 C CYS A 202 12.126 -6.601 42.778 1.00 39.32 C ANISOU 1208 C CYS A 202 5452 4384 5104 -353 711 1075 C ATOM 1209 O CYS A 202 11.304 -6.366 41.886 1.00 39.55 O ANISOU 1209 O CYS A 202 5429 4392 5207 -423 714 979 O ATOM 1210 CB CYS A 202 13.695 -8.201 41.617 1.00 36.11 C ANISOU 1210 CB CYS A 202 5118 3772 4832 -274 686 1113 C ATOM 1211 SG CYS A 202 15.038 -7.001 41.408 1.00 39.91 S ANISOU 1211 SG CYS A 202 5555 4375 5234 -179 575 1061 S ATOM 1212 N ASP A 203 12.403 -5.729 43.746 1.00 35.06 N ANISOU 1212 N ASP A 203 4912 3972 4435 -312 688 1098 N ATOM 1213 CA ASP A 203 11.754 -4.424 43.791 1.00 34.42 C ANISOU 1213 CA ASP A 203 4773 4001 4306 -341 680 1006 C ATOM 1214 C ASP A 203 12.606 -3.401 44.530 1.00 35.60 C ANISOU 1214 C ASP A 203 4935 4274 4317 -279 619 1001 C ATOM 1215 O ASP A 203 13.554 -3.762 45.227 1.00 35.66 O ANISOU 1215 O ASP A 203 4995 4303 4252 -222 586 1088 O ATOM 1216 CB ASP A 203 10.350 -4.560 44.442 1.00 36.39 C ANISOU 1216 CB ASP A 203 5007 4258 4561 -413 788 1032 C ATOM 1217 CG ASP A 203 9.329 -3.496 44.070 1.00 47.73 C ANISOU 1217 CG ASP A 203 6357 5757 6022 -457 802 927 C ATOM 1218 OD1 ASP A 203 9.657 -2.614 43.247 1.00 47.80 O ANISOU 1218 OD1 ASP A 203 6324 5797 6043 -435 724 832 O ATOM 1219 OD2 ASP A 203 8.204 -3.546 44.601 1.00 55.45 O ANISOU 1219 OD2 ASP A 203 7307 6750 7014 -509 896 947 O ATOM 1220 N GLU A 204 12.260 -2.129 44.381 1.00 30.42 N ANISOU 1220 N GLU A 204 4233 3698 3627 -292 602 901 N ATOM 1221 CA GLU A 204 12.931 -1.014 45.050 1.00 29.69 C ANISOU 1221 CA GLU A 204 4155 3720 3408 -253 550 871 C ATOM 1222 C GLU A 204 12.571 -0.992 46.536 1.00 35.69 C ANISOU 1222 C GLU A 204 4974 4550 4036 -259 613 939 C ATOM 1223 O GLU A 204 11.422 -1.232 46.900 1.00 35.68 O ANISOU 1223 O GLU A 204 4970 4535 4051 -304 716 958 O ATOM 1224 CB GLU A 204 12.514 0.319 44.414 1.00 29.77 C ANISOU 1224 CB GLU A 204 4105 3770 3437 -269 534 743 C ATOM 1225 CG GLU A 204 12.782 0.448 42.932 1.00 27.26 C ANISOU 1225 CG GLU A 204 3737 3394 3227 -268 475 671 C ATOM 1226 CD GLU A 204 12.271 1.739 42.324 1.00 44.72 C ANISOU 1226 CD GLU A 204 5894 5638 5458 -280 464 564 C ATOM 1227 OE1 GLU A 204 11.798 2.622 43.080 1.00 32.49 O ANISOU 1227 OE1 GLU A 204 4347 4156 3843 -282 503 536 O ATOM 1228 OE2 GLU A 204 12.342 1.867 41.080 1.00 31.83 O ANISOU 1228 OE2 GLU A 204 4226 3961 3905 -285 421 510 O ATOM 1229 N ARG A 205 13.545 -0.687 47.385 1.00 34.79 N ANISOU 1229 N ARG A 205 4912 4518 3788 -219 552 974 N ATOM 1230 CA ARG A 205 13.341 -0.593 48.828 1.00 35.93 C ANISOU 1230 CA ARG A 205 5134 4745 3773 -224 599 1034 C ATOM 1231 C ARG A 205 13.596 0.845 49.244 1.00 39.57 C ANISOU 1231 C ARG A 205 5605 5313 4119 -226 561 930 C ATOM 1232 O ARG A 205 14.703 1.356 49.048 1.00 39.21 O ANISOU 1232 O ARG A 205 5548 5308 4041 -199 449 894 O ATOM 1233 CB ARG A 205 14.260 -1.569 49.594 1.00 38.00 C ANISOU 1233 CB ARG A 205 5465 5016 3956 -180 550 1179 C ATOM 1234 CG ARG A 205 14.119 -1.496 51.117 1.00 56.47 C ANISOU 1234 CG ARG A 205 7903 7452 6100 -186 588 1250 C ATOM 1235 CD ARG A 205 15.250 -2.249 51.809 1.00 79.63 C ANISOU 1235 CD ARG A 205 10896 10417 8943 -130 500 1393 C ATOM 1236 NE ARG A 205 14.938 -3.672 51.913 1.00 96.54 N ANISOU 1236 NE ARG A 205 13072 12454 11153 -119 572 1536 N ATOM 1237 CZ ARG A 205 15.777 -4.628 52.298 1.00112.78 C ANISOU 1237 CZ ARG A 205 15171 14488 13192 -58 517 1685 C ATOM 1238 NH1 ARG A 205 17.039 -4.336 52.604 1.00 99.52 N ANISOU 1238 NH1 ARG A 205 13488 12897 11428 0 374 1716 N ATOM 1239 NH2 ARG A 205 15.372 -5.888 52.343 1.00100.93 N ANISOU 1239 NH2 ARG A 205 13708 12871 11769 -55 604 1808 N ATOM 1240 N TRP A 206 12.563 1.501 49.791 1.00 35.12 N ANISOU 1240 N TRP A 206 5058 4785 3502 -260 664 878 N ATOM 1241 CA TRP A 206 12.668 2.876 50.242 1.00 34.31 C ANISOU 1241 CA TRP A 206 4978 4765 3291 -266 655 770 C ATOM 1242 C TRP A 206 12.428 2.946 51.736 1.00 41.17 C ANISOU 1242 C TRP A 206 5956 5717 3970 -281 723 811 C ATOM 1243 O TRP A 206 11.471 2.352 52.223 1.00 41.29 O ANISOU 1243 O TRP A 206 5994 5713 3983 -300 848 874 O ATOM 1244 CB TRP A 206 11.721 3.798 49.450 1.00 32.13 C ANISOU 1244 CB TRP A 206 4627 4454 3129 -282 718 653 C ATOM 1245 CG TRP A 206 12.005 3.851 47.974 1.00 32.14 C ANISOU 1245 CG TRP A 206 4537 4385 3289 -270 642 607 C ATOM 1246 CD1 TRP A 206 11.401 3.109 47.006 1.00 34.78 C ANISOU 1246 CD1 TRP A 206 4804 4636 3776 -282 663 631 C ATOM 1247 CD2 TRP A 206 13.003 4.648 47.308 1.00 31.51 C ANISOU 1247 CD2 TRP A 206 4436 4316 3221 -252 534 532 C ATOM 1248 NE1 TRP A 206 11.960 3.387 45.778 1.00 33.85 N ANISOU 1248 NE1 TRP A 206 4633 4478 3750 -268 576 576 N ATOM 1249 CE2 TRP A 206 12.933 4.342 45.933 1.00 34.99 C ANISOU 1249 CE2 TRP A 206 4801 4678 3816 -248 502 518 C ATOM 1250 CE3 TRP A 206 13.912 5.634 47.734 1.00 32.60 C ANISOU 1250 CE3 TRP A 206 4612 4521 3253 -249 465 470 C ATOM 1251 CZ2 TRP A 206 13.736 4.982 44.981 1.00 34.16 C ANISOU 1251 CZ2 TRP A 206 4661 4559 3759 -233 416 453 C ATOM 1252 CZ3 TRP A 206 14.740 6.237 46.800 1.00 33.61 C ANISOU 1252 CZ3 TRP A 206 4695 4632 3444 -239 376 407 C ATOM 1253 CH2 TRP A 206 14.640 5.919 45.440 1.00 34.31 C ANISOU 1253 CH2 TRP A 206 4712 4642 3684 -228 358 402 C ATOM 1254 N ALA A 207 13.322 3.645 52.467 1.00 40.11 N ANISOU 1254 N ALA A 207 5891 5677 3671 -279 641 776 N ATOM 1255 CA ALA A 207 13.254 3.832 53.919 1.00 40.51 C ANISOU 1255 CA ALA A 207 6067 5823 3503 -298 687 800 C ATOM 1256 C ALA A 207 12.149 4.809 54.342 1.00 46.12 C ANISOU 1256 C ALA A 207 6807 6547 4172 -326 836 691 C ATOM 1257 O ALA A 207 11.727 4.780 55.493 1.00 47.82 O ANISOU 1257 O ALA A 207 7124 6817 4227 -345 931 720 O ATOM 1258 CB ALA A 207 14.596 4.301 54.448 1.00 41.29 C ANISOU 1258 CB ALA A 207 6220 6020 3448 -297 532 783 C ATOM 1259 N ASP A 208 11.703 5.685 53.437 1.00 42.39 N ANISOU 1259 N ASP A 208 6249 6022 3836 -324 860 572 N ATOM 1260 CA ASP A 208 10.635 6.644 53.692 1.00 42.04 C ANISOU 1260 CA ASP A 208 6210 5972 3791 -334 1007 469 C ATOM 1261 C ASP A 208 9.737 6.774 52.469 1.00 46.59 C ANISOU 1261 C ASP A 208 6648 6456 4598 -319 1059 433 C ATOM 1262 O ASP A 208 10.061 6.219 51.418 1.00 47.05 O ANISOU 1262 O ASP A 208 6622 6460 4793 -309 969 470 O ATOM 1263 CB ASP A 208 11.180 7.999 54.180 1.00 44.13 C ANISOU 1263 CB ASP A 208 6552 6293 3922 -347 974 334 C ATOM 1264 CG ASP A 208 11.960 8.781 53.158 1.00 58.68 C ANISOU 1264 CG ASP A 208 8327 8103 5864 -340 847 246 C ATOM 1265 OD1 ASP A 208 13.205 8.685 53.166 1.00 62.28 O ANISOU 1265 OD1 ASP A 208 8802 8603 6258 -349 695 263 O ATOM 1266 OD2 ASP A 208 11.332 9.496 52.361 1.00 62.20 O ANISOU 1266 OD2 ASP A 208 8699 8482 6451 -323 900 166 O ATOM 1267 N ASP A 209 8.607 7.478 52.606 1.00 42.65 N ANISOU 1267 N ASP A 209 6124 5942 4141 -315 1204 364 N ATOM 1268 CA ASP A 209 7.623 7.635 51.537 1.00 42.66 C ANISOU 1268 CA ASP A 209 5986 5870 4355 -299 1256 338 C ATOM 1269 C ASP A 209 7.864 8.841 50.636 1.00 42.04 C ANISOU 1269 C ASP A 209 5855 5757 4361 -271 1193 223 C ATOM 1270 O ASP A 209 7.263 8.919 49.568 1.00 40.93 O ANISOU 1270 O ASP A 209 5597 5559 4396 -255 1189 215 O ATOM 1271 CB ASP A 209 6.189 7.653 52.117 1.00 46.13 C ANISOU 1271 CB ASP A 209 6397 6307 4823 -301 1455 347 C ATOM 1272 CG ASP A 209 5.927 8.847 53.002 1.00 71.30 C ANISOU 1272 CG ASP A 209 9669 9530 7890 -286 1569 245 C ATOM 1273 OD1 ASP A 209 6.284 8.782 54.207 1.00 75.46 O ANISOU 1273 OD1 ASP A 209 10336 10122 8211 -307 1608 256 O ATOM 1274 OD2 ASP A 209 5.382 9.860 52.489 1.00 80.21 O ANISOU 1274 OD2 ASP A 209 10731 10621 9125 -251 1617 153 O ATOM 1275 N LEU A 210 8.725 9.779 51.056 1.00 37.08 N ANISOU 1275 N LEU A 210 5318 5164 3609 -272 1141 138 N ATOM 1276 CA LEU A 210 9.050 10.981 50.277 1.00 35.53 C ANISOU 1276 CA LEU A 210 5091 4927 3483 -253 1086 31 C ATOM 1277 C LEU A 210 10.192 10.765 49.254 1.00 37.97 C ANISOU 1277 C LEU A 210 5360 5217 3849 -257 912 47 C ATOM 1278 O LEU A 210 10.058 11.217 48.112 1.00 37.80 O ANISOU 1278 O LEU A 210 5258 5137 3969 -235 878 13 O ATOM 1279 CB LEU A 210 9.337 12.185 51.197 1.00 35.41 C ANISOU 1279 CB LEU A 210 5192 4940 3321 -262 1133 -84 C ATOM 1280 CG LEU A 210 9.698 13.515 50.520 1.00 40.37 C ANISOU 1280 CG LEU A 210 5811 5515 4015 -248 1093 -199 C ATOM 1281 CD1 LEU A 210 8.540 14.065 49.682 1.00 40.28 C ANISOU 1281 CD1 LEU A 210 5693 5424 4189 -193 1188 -223 C ATOM 1282 CD2 LEU A 210 10.204 14.529 51.526 1.00 42.86 C ANISOU 1282 CD2 LEU A 210 6264 5860 4160 -280 1115 -312 C ATOM 1283 N ALA A 211 11.297 10.081 49.647 1.00 33.30 N ANISOU 1283 N ALA A 211 4823 4676 3153 -280 807 103 N ATOM 1284 CA ALA A 211 12.447 9.795 48.761 1.00 32.75 C ANISOU 1284 CA ALA A 211 4713 4594 3138 -279 655 125 C ATOM 1285 C ALA A 211 12.054 9.174 47.391 1.00 33.89 C ANISOU 1285 C ALA A 211 4747 4663 3468 -258 635 169 C ATOM 1286 O ALA A 211 12.505 9.732 46.388 1.00 32.29 O ANISOU 1286 O ALA A 211 4500 4423 3346 -249 568 121 O ATOM 1287 CB ALA A 211 13.486 8.938 49.470 1.00 33.70 C ANISOU 1287 CB ALA A 211 4889 4780 3135 -293 566 207 C ATOM 1288 N PRO A 212 11.185 8.107 47.290 1.00 29.48 N ANISOU 1288 N PRO A 212 4147 4079 2977 -258 696 252 N ATOM 1289 CA PRO A 212 10.804 7.594 45.949 1.00 28.51 C ANISOU 1289 CA PRO A 212 3927 3885 3019 -252 668 275 C ATOM 1290 C PRO A 212 10.017 8.595 45.104 1.00 31.76 C ANISOU 1290 C PRO A 212 4268 4258 3540 -235 698 199 C ATOM 1291 O PRO A 212 10.082 8.532 43.887 1.00 31.61 O ANISOU 1291 O PRO A 212 4189 4193 3627 -230 634 193 O ATOM 1292 CB PRO A 212 9.943 6.366 46.268 1.00 29.85 C ANISOU 1292 CB PRO A 212 4080 4040 3224 -272 743 367 C ATOM 1293 CG PRO A 212 9.435 6.597 47.656 1.00 33.65 C ANISOU 1293 CG PRO A 212 4625 4577 3584 -279 854 372 C ATOM 1294 CD PRO A 212 10.554 7.289 48.356 1.00 29.82 C ANISOU 1294 CD PRO A 212 4233 4152 2946 -273 791 328 C ATOM 1295 N LYS A 213 9.284 9.522 45.755 1.00 29.10 N ANISOU 1295 N LYS A 213 3945 3938 3174 -223 797 144 N ATOM 1296 CA LYS A 213 8.503 10.568 45.084 1.00 28.76 C ANISOU 1296 CA LYS A 213 3837 3856 3236 -191 836 80 C ATOM 1297 C LYS A 213 9.433 11.575 44.445 1.00 32.02 C ANISOU 1297 C LYS A 213 4273 4245 3647 -178 751 11 C ATOM 1298 O LYS A 213 9.195 11.970 43.307 1.00 31.91 O ANISOU 1298 O LYS A 213 4195 4185 3744 -156 714 -3 O ATOM 1299 CB LYS A 213 7.541 11.277 46.054 1.00 30.72 C ANISOU 1299 CB LYS A 213 4100 4120 3452 -172 983 40 C ATOM 1300 CG LYS A 213 6.469 10.381 46.644 1.00 30.41 C ANISOU 1300 CG LYS A 213 4019 4099 3436 -187 1093 110 C ATOM 1301 CD LYS A 213 5.641 11.170 47.639 1.00 31.61 C ANISOU 1301 CD LYS A 213 4200 4269 3543 -163 1254 62 C ATOM 1302 CE LYS A 213 4.512 10.358 48.199 1.00 42.73 C ANISOU 1302 CE LYS A 213 5554 5694 4988 -179 1383 131 C ATOM 1303 NZ LYS A 213 3.552 11.215 48.934 1.00 54.90 N ANISOU 1303 NZ LYS A 213 7088 7238 6532 -142 1556 79 N ATOM 1304 N ILE A 214 10.511 11.967 45.159 1.00 28.68 N ANISOU 1304 N ILE A 214 3943 3857 3096 -196 713 -29 N ATOM 1305 CA ILE A 214 11.534 12.902 44.661 1.00 27.40 C ANISOU 1305 CA ILE A 214 3807 3675 2928 -199 634 -95 C ATOM 1306 C ILE A 214 12.346 12.236 43.550 1.00 30.24 C ANISOU 1306 C ILE A 214 4122 4016 3351 -205 520 -49 C ATOM 1307 O ILE A 214 12.489 12.820 42.469 1.00 30.40 O ANISOU 1307 O ILE A 214 4109 3988 3454 -191 483 -77 O ATOM 1308 CB ILE A 214 12.425 13.484 45.809 1.00 29.69 C ANISOU 1308 CB ILE A 214 4202 4016 3062 -233 622 -156 C ATOM 1309 CG1 ILE A 214 11.568 14.318 46.807 1.00 29.63 C ANISOU 1309 CG1 ILE A 214 4254 4010 2992 -225 755 -225 C ATOM 1310 CG2 ILE A 214 13.600 14.310 45.244 1.00 28.46 C ANISOU 1310 CG2 ILE A 214 4060 3839 2913 -252 530 -217 C ATOM 1311 CD1 ILE A 214 12.278 14.721 48.099 1.00 36.82 C ANISOU 1311 CD1 ILE A 214 5286 4983 3721 -270 753 -284 C ATOM 1312 N TYR A 215 12.844 11.004 43.807 1.00 24.32 N ANISOU 1312 N TYR A 215 3378 3299 2562 -221 475 26 N ATOM 1313 CA TYR A 215 13.651 10.246 42.860 1.00 23.12 C ANISOU 1313 CA TYR A 215 3192 3126 2466 -221 385 72 C ATOM 1314 C TYR A 215 12.953 10.012 41.514 1.00 27.89 C ANISOU 1314 C TYR A 215 3728 3668 3202 -208 383 83 C ATOM 1315 O TYR A 215 13.538 10.313 40.459 1.00 26.98 O ANISOU 1315 O TYR A 215 3595 3519 3137 -203 325 62 O ATOM 1316 CB TYR A 215 14.116 8.906 43.472 1.00 23.35 C ANISOU 1316 CB TYR A 215 3242 3188 2442 -229 359 160 C ATOM 1317 CG TYR A 215 14.861 8.050 42.478 1.00 23.77 C ANISOU 1317 CG TYR A 215 3260 3203 2568 -220 288 205 C ATOM 1318 CD1 TYR A 215 16.187 8.326 42.146 1.00 24.82 C ANISOU 1318 CD1 TYR A 215 3391 3348 2692 -216 208 188 C ATOM 1319 CD2 TYR A 215 14.221 7.011 41.806 1.00 24.43 C ANISOU 1319 CD2 TYR A 215 3309 3234 2738 -219 308 256 C ATOM 1320 CE1 TYR A 215 16.870 7.570 41.190 1.00 24.76 C ANISOU 1320 CE1 TYR A 215 3352 3300 2757 -201 163 224 C ATOM 1321 CE2 TYR A 215 14.892 6.251 40.845 1.00 25.77 C ANISOU 1321 CE2 TYR A 215 3461 3358 2972 -210 257 283 C ATOM 1322 CZ TYR A 215 16.215 6.543 40.533 1.00 30.93 C ANISOU 1322 CZ TYR A 215 4116 4023 3614 -196 191 268 C ATOM 1323 OH TYR A 215 16.893 5.811 39.588 1.00 29.50 O ANISOU 1323 OH TYR A 215 3918 3792 3498 -181 159 292 O ATOM 1324 N HIS A 216 11.708 9.478 41.554 1.00 24.11 N ANISOU 1324 N HIS A 216 3209 3177 2773 -208 446 118 N ATOM 1325 CA HIS A 216 10.952 9.140 40.349 1.00 24.01 C ANISOU 1325 CA HIS A 216 3127 3119 2878 -208 432 132 C ATOM 1326 C HIS A 216 10.430 10.361 39.589 1.00 29.94 C ANISOU 1326 C HIS A 216 3841 3845 3691 -182 433 79 C ATOM 1327 O HIS A 216 10.266 10.277 38.367 1.00 31.19 O ANISOU 1327 O HIS A 216 3960 3970 3922 -181 382 84 O ATOM 1328 CB HIS A 216 9.861 8.120 40.640 1.00 24.13 C ANISOU 1328 CB HIS A 216 3100 3131 2935 -230 489 189 C ATOM 1329 CG HIS A 216 10.456 6.767 40.875 1.00 27.22 C ANISOU 1329 CG HIS A 216 3526 3515 3300 -254 467 253 C ATOM 1330 ND1 HIS A 216 11.009 6.023 39.825 1.00 28.64 N ANISOU 1330 ND1 HIS A 216 3702 3648 3531 -264 399 268 N ATOM 1331 CD2 HIS A 216 10.674 6.111 42.039 1.00 27.86 C ANISOU 1331 CD2 HIS A 216 3658 3626 3303 -262 505 306 C ATOM 1332 CE1 HIS A 216 11.476 4.924 40.386 1.00 27.70 C ANISOU 1332 CE1 HIS A 216 3622 3521 3380 -272 405 332 C ATOM 1333 NE2 HIS A 216 11.281 4.925 41.713 1.00 27.78 N ANISOU 1333 NE2 HIS A 216 3664 3579 3312 -271 464 363 N ATOM 1334 N SER A 217 10.276 11.507 40.270 1.00 25.23 N ANISOU 1334 N SER A 217 3268 3258 3058 -159 488 29 N ATOM 1335 CA SER A 217 9.950 12.767 39.600 1.00 25.12 C ANISOU 1335 CA SER A 217 3234 3208 3104 -124 493 -18 C ATOM 1336 C SER A 217 11.188 13.207 38.777 1.00 28.11 C ANISOU 1336 C SER A 217 3651 3560 3470 -130 410 -43 C ATOM 1337 O SER A 217 11.040 13.552 37.612 1.00 27.60 O ANISOU 1337 O SER A 217 3557 3458 3472 -113 371 -39 O ATOM 1338 CB SER A 217 9.545 13.834 40.613 1.00 27.59 C ANISOU 1338 CB SER A 217 3579 3523 3381 -99 588 -72 C ATOM 1339 OG SER A 217 8.306 13.477 41.208 1.00 32.23 O ANISOU 1339 OG SER A 217 4116 4130 3999 -87 679 -45 O ATOM 1340 N CYS A 218 12.402 13.109 39.362 1.00 25.39 N ANISOU 1340 N CYS A 218 3365 3241 3039 -156 381 -59 N ATOM 1341 CA CYS A 218 13.680 13.403 38.686 1.00 25.97 C ANISOU 1341 CA CYS A 218 3463 3298 3105 -171 311 -78 C ATOM 1342 C CYS A 218 13.916 12.424 37.530 1.00 26.84 C ANISOU 1342 C CYS A 218 3541 3390 3267 -174 255 -29 C ATOM 1343 O CYS A 218 14.250 12.854 36.425 1.00 24.79 O ANISOU 1343 O CYS A 218 3279 3092 3046 -168 222 -40 O ATOM 1344 CB CYS A 218 14.851 13.386 39.670 1.00 26.99 C ANISOU 1344 CB CYS A 218 3641 3475 3140 -202 287 -97 C ATOM 1345 SG CYS A 218 14.792 14.707 40.911 1.00 31.37 S ANISOU 1345 SG CYS A 218 4261 4044 3616 -215 344 -183 S ATOM 1346 N PHE A 219 13.719 11.116 37.784 1.00 22.86 N ANISOU 1346 N PHE A 219 3023 2905 2758 -185 252 23 N ATOM 1347 CA PHE A 219 13.875 10.066 36.774 1.00 22.35 C ANISOU 1347 CA PHE A 219 2941 2812 2739 -193 211 61 C ATOM 1348 C PHE A 219 13.092 10.405 35.495 1.00 26.50 C ANISOU 1348 C PHE A 219 3437 3300 3333 -186 195 52 C ATOM 1349 O PHE A 219 13.684 10.422 34.416 1.00 27.21 O ANISOU 1349 O PHE A 219 3541 3361 3436 -188 154 45 O ATOM 1350 CB PHE A 219 13.448 8.691 37.326 1.00 23.57 C ANISOU 1350 CB PHE A 219 3087 2974 2893 -208 231 117 C ATOM 1351 CG PHE A 219 13.988 7.529 36.527 1.00 25.53 C ANISOU 1351 CG PHE A 219 3342 3185 3173 -218 196 148 C ATOM 1352 CD1 PHE A 219 15.209 6.941 36.857 1.00 26.51 C ANISOU 1352 CD1 PHE A 219 3492 3315 3266 -208 176 175 C ATOM 1353 CD2 PHE A 219 13.284 7.024 35.436 1.00 28.12 C ANISOU 1353 CD2 PHE A 219 3649 3471 3563 -237 183 149 C ATOM 1354 CE1 PHE A 219 15.700 5.861 36.128 1.00 26.77 C ANISOU 1354 CE1 PHE A 219 3535 3299 3338 -207 161 202 C ATOM 1355 CE2 PHE A 219 13.803 5.958 34.682 1.00 30.00 C ANISOU 1355 CE2 PHE A 219 3911 3663 3825 -249 163 164 C ATOM 1356 CZ PHE A 219 15.007 5.392 35.033 1.00 26.94 C ANISOU 1356 CZ PHE A 219 3552 3268 3414 -229 161 189 C ATOM 1357 N PHE A 220 11.788 10.701 35.625 1.00 22.14 N ANISOU 1357 N PHE A 220 2841 2752 2820 -177 227 55 N ATOM 1358 CA PHE A 220 10.905 11.022 34.502 1.00 21.73 C ANISOU 1358 CA PHE A 220 2745 2678 2832 -167 198 59 C ATOM 1359 C PHE A 220 11.368 12.233 33.691 1.00 24.75 C ANISOU 1359 C PHE A 220 3155 3033 3217 -140 172 32 C ATOM 1360 O PHE A 220 11.314 12.227 32.461 1.00 23.01 O ANISOU 1360 O PHE A 220 2935 2791 3015 -142 121 43 O ATOM 1361 CB PHE A 220 9.476 11.253 35.009 1.00 23.45 C ANISOU 1361 CB PHE A 220 2893 2914 3102 -152 246 72 C ATOM 1362 CG PHE A 220 8.467 11.736 33.990 1.00 25.02 C ANISOU 1362 CG PHE A 220 3027 3103 3374 -131 210 85 C ATOM 1363 CD1 PHE A 220 8.137 10.954 32.886 1.00 29.08 C ANISOU 1363 CD1 PHE A 220 3516 3614 3918 -166 137 107 C ATOM 1364 CD2 PHE A 220 7.801 12.941 34.169 1.00 27.16 C ANISOU 1364 CD2 PHE A 220 3264 3369 3687 -77 248 77 C ATOM 1365 CE1 PHE A 220 7.197 11.397 31.953 1.00 30.22 C ANISOU 1365 CE1 PHE A 220 3597 3764 4122 -150 85 126 C ATOM 1366 CE2 PHE A 220 6.866 13.391 33.231 1.00 30.20 C ANISOU 1366 CE2 PHE A 220 3578 3750 4145 -47 204 105 C ATOM 1367 CZ PHE A 220 6.556 12.607 32.141 1.00 29.13 C ANISOU 1367 CZ PHE A 220 3412 3626 4029 -85 115 132 C ATOM 1368 N ILE A 221 11.791 13.279 34.386 1.00 21.99 N ANISOU 1368 N ILE A 221 2835 2680 2841 -119 212 -2 N ATOM 1369 CA ILE A 221 12.201 14.520 33.755 1.00 21.85 C ANISOU 1369 CA ILE A 221 2848 2622 2831 -97 204 -25 C ATOM 1370 C ILE A 221 13.537 14.353 33.045 1.00 25.01 C ANISOU 1370 C ILE A 221 3295 3008 3201 -123 164 -31 C ATOM 1371 O ILE A 221 13.637 14.769 31.897 1.00 25.89 O ANISOU 1371 O ILE A 221 3423 3087 3329 -114 136 -21 O ATOM 1372 CB ILE A 221 12.126 15.690 34.777 1.00 24.85 C ANISOU 1372 CB ILE A 221 3250 2990 3202 -75 271 -70 C ATOM 1373 CG1 ILE A 221 10.614 16.040 34.972 1.00 25.26 C ANISOU 1373 CG1 ILE A 221 3241 3038 3317 -28 317 -54 C ATOM 1374 CG2 ILE A 221 12.953 16.929 34.331 1.00 25.34 C ANISOU 1374 CG2 ILE A 221 3366 2999 3263 -70 271 -104 C ATOM 1375 CD1 ILE A 221 10.282 16.850 36.070 1.00 37.93 C ANISOU 1375 CD1 ILE A 221 4863 4633 4915 -4 402 -97 C ATOM 1376 N VAL A 222 14.501 13.669 33.671 1.00 21.71 N ANISOU 1376 N VAL A 222 2893 2616 2739 -151 161 -38 N ATOM 1377 CA VAL A 222 15.854 13.445 33.139 1.00 22.75 C ANISOU 1377 CA VAL A 222 3050 2739 2853 -171 135 -41 C ATOM 1378 C VAL A 222 15.878 12.418 31.986 1.00 29.92 C ANISOU 1378 C VAL A 222 3960 3632 3776 -177 105 -11 C ATOM 1379 O VAL A 222 16.559 12.649 30.984 1.00 30.87 O ANISOU 1379 O VAL A 222 4108 3725 3898 -181 96 -15 O ATOM 1380 CB VAL A 222 16.847 13.093 34.282 1.00 27.01 C ANISOU 1380 CB VAL A 222 3593 3321 3349 -191 136 -51 C ATOM 1381 CG1 VAL A 222 18.195 12.619 33.745 1.00 27.53 C ANISOU 1381 CG1 VAL A 222 3660 3385 3417 -204 112 -41 C ATOM 1382 CG2 VAL A 222 17.047 14.295 35.216 1.00 26.95 C ANISOU 1382 CG2 VAL A 222 3605 3322 3311 -202 159 -100 C ATOM 1383 N THR A 223 15.148 11.299 32.115 1.00 25.89 N ANISOU 1383 N THR A 223 3428 3133 3276 -184 98 14 N ATOM 1384 CA THR A 223 15.165 10.240 31.095 1.00 24.72 C ANISOU 1384 CA THR A 223 3293 2961 3138 -200 74 29 C ATOM 1385 C THR A 223 14.069 10.380 30.024 1.00 26.04 C ANISOU 1385 C THR A 223 3454 3115 3324 -205 40 34 C ATOM 1386 O THR A 223 14.107 9.656 29.019 1.00 25.09 O ANISOU 1386 O THR A 223 3363 2973 3197 -227 15 33 O ATOM 1387 CB THR A 223 15.106 8.841 31.760 1.00 27.86 C ANISOU 1387 CB THR A 223 3680 3364 3541 -214 85 54 C ATOM 1388 OG1 THR A 223 13.823 8.676 32.361 1.00 28.52 O ANISOU 1388 OG1 THR A 223 3724 3467 3645 -223 94 69 O ATOM 1389 CG2 THR A 223 16.222 8.615 32.773 1.00 22.77 C ANISOU 1389 CG2 THR A 223 3039 2741 2871 -203 102 66 C ATOM 1390 N TYR A 224 13.077 11.262 30.243 1.00 20.56 N ANISOU 1390 N TYR A 224 2724 2435 2654 -184 38 39 N ATOM 1391 CA TYR A 224 11.997 11.341 29.277 1.00 19.82 C ANISOU 1391 CA TYR A 224 2606 2341 2584 -186 -10 55 C ATOM 1392 C TYR A 224 11.560 12.774 28.909 1.00 25.86 C ANISOU 1392 C TYR A 224 3363 3098 3366 -141 -18 66 C ATOM 1393 O TYR A 224 11.736 13.163 27.763 1.00 26.13 O ANISOU 1393 O TYR A 224 3436 3114 3378 -137 -56 76 O ATOM 1394 CB TYR A 224 10.780 10.473 29.740 1.00 19.98 C ANISOU 1394 CB TYR A 224 2558 2387 2647 -210 -16 73 C ATOM 1395 CG TYR A 224 9.682 10.356 28.705 1.00 20.52 C ANISOU 1395 CG TYR A 224 2588 2466 2743 -227 -86 90 C ATOM 1396 CD1 TYR A 224 9.683 9.325 27.770 1.00 21.33 C ANISOU 1396 CD1 TYR A 224 2723 2558 2825 -282 -137 80 C ATOM 1397 CD2 TYR A 224 8.662 11.301 28.632 1.00 21.87 C ANISOU 1397 CD2 TYR A 224 2691 2658 2960 -188 -104 115 C ATOM 1398 CE1 TYR A 224 8.693 9.235 26.789 1.00 19.46 C ANISOU 1398 CE1 TYR A 224 2452 2341 2599 -310 -219 92 C ATOM 1399 CE2 TYR A 224 7.677 11.230 27.647 1.00 22.59 C ANISOU 1399 CE2 TYR A 224 2736 2772 3075 -202 -188 140 C ATOM 1400 CZ TYR A 224 7.713 10.207 26.713 1.00 26.32 C ANISOU 1400 CZ TYR A 224 3245 3245 3512 -269 -252 126 C ATOM 1401 OH TYR A 224 6.754 10.139 25.736 1.00 28.53 O ANISOU 1401 OH TYR A 224 3481 3557 3803 -294 -350 146 O ATOM 1402 N LEU A 225 10.944 13.520 29.826 1.00 24.23 N ANISOU 1402 N LEU A 225 3110 2899 3198 -106 22 67 N ATOM 1403 CA LEU A 225 10.307 14.794 29.512 1.00 23.65 C ANISOU 1403 CA LEU A 225 3018 2806 3161 -53 22 85 C ATOM 1404 C LEU A 225 11.245 15.894 29.016 1.00 26.33 C ANISOU 1404 C LEU A 225 3432 3098 3476 -33 34 76 C ATOM 1405 O LEU A 225 10.965 16.447 27.948 1.00 24.19 O ANISOU 1405 O LEU A 225 3176 2807 3208 -9 -8 111 O ATOM 1406 CB LEU A 225 9.449 15.298 30.682 1.00 23.70 C ANISOU 1406 CB LEU A 225 2964 2822 3220 -15 86 80 C ATOM 1407 CG LEU A 225 8.489 16.461 30.367 1.00 28.64 C ANISOU 1407 CG LEU A 225 3545 3424 3913 55 89 111 C ATOM 1408 CD1 LEU A 225 7.406 16.037 29.398 1.00 28.76 C ANISOU 1408 CD1 LEU A 225 3484 3473 3971 59 6 165 C ATOM 1409 CD2 LEU A 225 7.825 16.960 31.616 1.00 32.01 C ANISOU 1409 CD2 LEU A 225 3926 3849 4387 94 180 92 C ATOM 1410 N ALA A 226 12.311 16.248 29.781 1.00 23.36 N ANISOU 1410 N ALA A 226 3099 2704 3074 -47 88 34 N ATOM 1411 CA ALA A 226 13.222 17.313 29.354 1.00 23.08 C ANISOU 1411 CA ALA A 226 3127 2616 3026 -42 108 22 C ATOM 1412 C ALA A 226 13.988 16.962 28.039 1.00 28.10 C ANISOU 1412 C ALA A 226 3813 3242 3622 -68 70 42 C ATOM 1413 O ALA A 226 13.899 17.766 27.107 1.00 28.44 O ANISOU 1413 O ALA A 226 3892 3247 3665 -45 59 74 O ATOM 1414 CB ALA A 226 14.170 17.728 30.477 1.00 23.32 C ANISOU 1414 CB ALA A 226 3182 2639 3041 -67 162 -33 C ATOM 1415 N PRO A 227 14.639 15.782 27.858 1.00 24.03 N ANISOU 1415 N PRO A 227 3306 2754 3070 -109 55 32 N ATOM 1416 CA PRO A 227 15.313 15.540 26.567 1.00 23.03 C ANISOU 1416 CA PRO A 227 3236 2611 2903 -128 39 45 C ATOM 1417 C PRO A 227 14.378 15.489 25.369 1.00 26.30 C ANISOU 1417 C PRO A 227 3667 3028 3297 -115 -21 85 C ATOM 1418 O PRO A 227 14.727 16.061 24.352 1.00 25.96 O ANISOU 1418 O PRO A 227 3686 2958 3221 -111 -24 108 O ATOM 1419 CB PRO A 227 16.091 14.224 26.767 1.00 24.52 C ANISOU 1419 CB PRO A 227 3423 2821 3072 -163 47 22 C ATOM 1420 CG PRO A 227 15.561 13.611 27.979 1.00 29.90 C ANISOU 1420 CG PRO A 227 4047 3536 3777 -163 46 14 C ATOM 1421 CD PRO A 227 14.867 14.665 28.807 1.00 25.91 C ANISOU 1421 CD PRO A 227 3511 3030 3302 -134 63 11 C ATOM 1422 N LEU A 228 13.175 14.883 25.497 1.00 22.72 N ANISOU 1422 N LEU A 228 3157 2610 2864 -112 -71 99 N ATOM 1423 CA LEU A 228 12.220 14.789 24.377 1.00 22.11 C ANISOU 1423 CA LEU A 228 3083 2552 2768 -109 -151 138 C ATOM 1424 C LEU A 228 11.546 16.115 24.041 1.00 27.15 C ANISOU 1424 C LEU A 228 3710 3172 3433 -50 -171 190 C ATOM 1425 O LEU A 228 11.352 16.386 22.855 1.00 27.63 O ANISOU 1425 O LEU A 228 3817 3234 3448 -43 -228 232 O ATOM 1426 CB LEU A 228 11.198 13.661 24.567 1.00 22.15 C ANISOU 1426 CB LEU A 228 3020 2601 2794 -139 -202 134 C ATOM 1427 CG LEU A 228 11.802 12.239 24.501 1.00 26.42 C ANISOU 1427 CG LEU A 228 3595 3142 3301 -199 -193 93 C ATOM 1428 CD1 LEU A 228 10.869 11.245 25.075 1.00 26.43 C ANISOU 1428 CD1 LEU A 228 3523 3172 3346 -231 -216 87 C ATOM 1429 CD2 LEU A 228 12.200 11.848 23.070 1.00 26.48 C ANISOU 1429 CD2 LEU A 228 3695 3140 3227 -233 -230 85 C ATOM 1430 N GLY A 229 11.255 16.945 25.059 1.00 23.00 N ANISOU 1430 N GLY A 229 3136 2626 2975 -5 -121 188 N ATOM 1431 CA GLY A 229 10.726 18.292 24.880 1.00 21.93 C ANISOU 1431 CA GLY A 229 2996 2452 2885 63 -116 236 C ATOM 1432 C GLY A 229 11.753 19.160 24.173 1.00 28.10 C ANISOU 1432 C GLY A 229 3880 3173 3625 65 -84 249 C ATOM 1433 O GLY A 229 11.417 19.849 23.210 1.00 29.31 O ANISOU 1433 O GLY A 229 4067 3304 3765 103 -123 314 O ATOM 1434 N LEU A 230 13.037 19.085 24.601 1.00 24.10 N ANISOU 1434 N LEU A 230 3420 2643 3096 21 -18 195 N ATOM 1435 CA LEU A 230 14.147 19.808 23.961 1.00 24.09 C ANISOU 1435 CA LEU A 230 3506 2584 3062 6 26 202 C ATOM 1436 C LEU A 230 14.395 19.318 22.514 1.00 27.35 C ANISOU 1436 C LEU A 230 3987 3014 3391 -17 -18 238 C ATOM 1437 O LEU A 230 14.579 20.148 21.622 1.00 26.48 O ANISOU 1437 O LEU A 230 3948 2862 3254 0 -11 290 O ATOM 1438 CB LEU A 230 15.451 19.751 24.795 1.00 23.98 C ANISOU 1438 CB LEU A 230 3500 2556 3053 -44 98 135 C ATOM 1439 CG LEU A 230 15.440 20.554 26.114 1.00 28.26 C ANISOU 1439 CG LEU A 230 4014 3068 3657 -33 151 91 C ATOM 1440 CD1 LEU A 230 16.484 20.031 27.075 1.00 28.49 C ANISOU 1440 CD1 LEU A 230 4024 3126 3676 -90 182 26 C ATOM 1441 CD2 LEU A 230 15.612 22.056 25.873 1.00 27.06 C ANISOU 1441 CD2 LEU A 230 3918 2824 3541 -10 201 110 C ATOM 1442 N MET A 231 14.350 17.981 22.278 1.00 24.15 N ANISOU 1442 N MET A 231 3570 2666 2941 -57 -59 213 N ATOM 1443 CA MET A 231 14.534 17.406 20.936 1.00 23.42 C ANISOU 1443 CA MET A 231 3554 2591 2755 -85 -96 231 C ATOM 1444 C MET A 231 13.411 17.836 19.989 1.00 28.00 C ANISOU 1444 C MET A 231 4149 3189 3301 -51 -188 303 C ATOM 1445 O MET A 231 13.704 18.158 18.842 1.00 28.85 O ANISOU 1445 O MET A 231 4351 3284 3327 -54 -198 344 O ATOM 1446 CB MET A 231 14.633 15.879 20.967 1.00 25.05 C ANISOU 1446 CB MET A 231 3747 2839 2930 -135 -115 179 C ATOM 1447 CG MET A 231 15.938 15.361 21.495 1.00 28.18 C ANISOU 1447 CG MET A 231 4151 3219 3337 -164 -31 126 C ATOM 1448 SD MET A 231 15.960 13.550 21.405 1.00 32.11 S ANISOU 1448 SD MET A 231 4648 3744 3807 -210 -48 77 S ATOM 1449 CE MET A 231 15.866 13.105 23.118 1.00 28.45 C ANISOU 1449 CE MET A 231 4079 3298 3432 -203 -30 52 C ATOM 1450 N ALA A 232 12.140 17.865 20.467 1.00 24.00 N ANISOU 1450 N ALA A 232 3547 2715 2856 -15 -253 326 N ATOM 1451 CA ALA A 232 10.967 18.279 19.674 1.00 24.05 C ANISOU 1451 CA ALA A 232 3537 2750 2850 26 -356 405 C ATOM 1452 C ALA A 232 11.157 19.699 19.143 1.00 29.00 C ANISOU 1452 C ALA A 232 4228 3315 3474 86 -332 481 C ATOM 1453 O ALA A 232 10.964 19.947 17.949 1.00 29.32 O ANISOU 1453 O ALA A 232 4341 3368 3432 95 -396 547 O ATOM 1454 CB ALA A 232 9.696 18.198 20.514 1.00 24.72 C ANISOU 1454 CB ALA A 232 3484 2872 3037 62 -399 415 C ATOM 1455 N MET A 233 11.601 20.610 20.025 1.00 26.25 N ANISOU 1455 N MET A 233 3870 2897 3209 120 -234 467 N ATOM 1456 CA MET A 233 11.893 22.012 19.712 1.00 26.37 C ANISOU 1456 CA MET A 233 3950 2827 3244 172 -184 529 C ATOM 1457 C MET A 233 13.080 22.167 18.755 1.00 29.64 C ANISOU 1457 C MET A 233 4494 3205 3561 126 -138 540 C ATOM 1458 O MET A 233 13.008 22.977 17.832 1.00 29.74 O ANISOU 1458 O MET A 233 4584 3180 3534 161 -151 627 O ATOM 1459 CB MET A 233 12.091 22.817 21.000 1.00 29.08 C ANISOU 1459 CB MET A 233 4253 3100 3698 199 -86 486 C ATOM 1460 CG MET A 233 10.817 22.925 21.816 1.00 32.91 C ANISOU 1460 CG MET A 233 4622 3604 4279 263 -112 494 C ATOM 1461 SD MET A 233 10.973 24.020 23.226 1.00 37.54 S ANISOU 1461 SD MET A 233 5189 4095 4978 301 13 441 S ATOM 1462 CE MET A 233 11.758 22.924 24.399 1.00 34.81 C ANISOU 1462 CE MET A 233 4815 3803 4607 208 57 319 C ATOM 1463 N ALA A 234 14.140 21.363 18.942 1.00 25.91 N ANISOU 1463 N ALA A 234 4043 2748 3052 53 -82 460 N ATOM 1464 CA ALA A 234 15.318 21.358 18.076 1.00 25.58 C ANISOU 1464 CA ALA A 234 4110 2681 2928 5 -20 461 C ATOM 1465 C ALA A 234 14.920 20.960 16.653 1.00 31.45 C ANISOU 1465 C ALA A 234 4937 3470 3542 0 -99 518 C ATOM 1466 O ALA A 234 15.251 21.678 15.704 1.00 31.59 O ANISOU 1466 O ALA A 234 5059 3449 3494 9 -75 586 O ATOM 1467 CB ALA A 234 16.358 20.381 18.607 1.00 25.78 C ANISOU 1467 CB ALA A 234 4113 2727 2954 -60 41 367 C ATOM 1468 N TYR A 235 14.160 19.841 16.516 1.00 27.82 N ANISOU 1468 N TYR A 235 4436 3091 3042 -19 -196 491 N ATOM 1469 CA TYR A 235 13.694 19.322 15.236 1.00 27.93 C ANISOU 1469 CA TYR A 235 4528 3161 2922 -39 -290 526 C ATOM 1470 C TYR A 235 12.684 20.230 14.554 1.00 35.11 C ANISOU 1470 C TYR A 235 5452 4080 3807 25 -389 642 C ATOM 1471 O TYR A 235 12.671 20.287 13.323 1.00 34.59 O ANISOU 1471 O TYR A 235 5498 4037 3609 14 -437 697 O ATOM 1472 CB TYR A 235 13.193 17.890 15.364 1.00 28.34 C ANISOU 1472 CB TYR A 235 4531 3286 2953 -90 -362 455 C ATOM 1473 CG TYR A 235 14.351 16.913 15.422 1.00 28.83 C ANISOU 1473 CG TYR A 235 4639 3335 2981 -153 -267 363 C ATOM 1474 CD1 TYR A 235 15.202 16.746 14.335 1.00 29.45 C ANISOU 1474 CD1 TYR A 235 4853 3399 2937 -188 -214 357 C ATOM 1475 CD2 TYR A 235 14.614 16.178 16.579 1.00 29.21 C ANISOU 1475 CD2 TYR A 235 4596 3380 3122 -171 -223 289 C ATOM 1476 CE1 TYR A 235 16.288 15.881 14.395 1.00 29.78 C ANISOU 1476 CE1 TYR A 235 4926 3421 2966 -233 -112 277 C ATOM 1477 CE2 TYR A 235 15.697 15.304 16.650 1.00 29.82 C ANISOU 1477 CE2 TYR A 235 4707 3440 3183 -214 -135 217 C ATOM 1478 CZ TYR A 235 16.532 15.160 15.554 1.00 35.52 C ANISOU 1478 CZ TYR A 235 5553 4146 3800 -241 -77 211 C ATOM 1479 OH TYR A 235 17.597 14.297 15.609 1.00 32.81 O ANISOU 1479 OH TYR A 235 5231 3780 3454 -272 20 144 O ATOM 1480 N PHE A 236 11.896 20.994 15.331 1.00 33.43 N ANISOU 1480 N PHE A 236 5136 3845 3721 97 -410 685 N ATOM 1481 CA PHE A 236 10.976 21.958 14.747 1.00 34.47 C ANISOU 1481 CA PHE A 236 5269 3973 3854 177 -494 809 C ATOM 1482 C PHE A 236 11.779 23.080 14.059 1.00 37.03 C ANISOU 1482 C PHE A 236 5728 4210 4130 202 -413 885 C ATOM 1483 O PHE A 236 11.417 23.517 12.961 1.00 37.95 O ANISOU 1483 O PHE A 236 5927 4341 4153 233 -486 992 O ATOM 1484 CB PHE A 236 10.000 22.514 15.801 1.00 37.65 C ANISOU 1484 CB PHE A 236 5527 4359 4420 257 -508 831 C ATOM 1485 CG PHE A 236 9.071 23.564 15.238 1.00 40.99 C ANISOU 1485 CG PHE A 236 5940 4765 4868 359 -584 970 C ATOM 1486 CD1 PHE A 236 7.923 23.199 14.536 1.00 45.54 C ANISOU 1486 CD1 PHE A 236 6460 5439 5402 381 -750 1040 C ATOM 1487 CD2 PHE A 236 9.373 24.919 15.355 1.00 44.54 C ANISOU 1487 CD2 PHE A 236 6439 5100 5385 431 -494 1035 C ATOM 1488 CE1 PHE A 236 7.086 24.171 13.981 1.00 46.64 C ANISOU 1488 CE1 PHE A 236 6584 5569 5568 484 -830 1183 C ATOM 1489 CE2 PHE A 236 8.537 25.888 14.794 1.00 47.38 C ANISOU 1489 CE2 PHE A 236 6796 5435 5774 537 -561 1177 C ATOM 1490 CZ PHE A 236 7.389 25.506 14.130 1.00 45.44 C ANISOU 1490 CZ PHE A 236 6482 5294 5488 569 -732 1255 C ATOM 1491 N GLN A 237 12.886 23.520 14.689 1.00 31.14 N ANISOU 1491 N GLN A 237 5009 3378 3445 180 -265 832 N ATOM 1492 CA GLN A 237 13.775 24.544 14.134 1.00 29.09 C ANISOU 1492 CA GLN A 237 4871 3025 3158 184 -164 891 C ATOM 1493 C GLN A 237 14.566 24.023 12.936 1.00 34.26 C ANISOU 1493 C GLN A 237 5662 3709 3646 118 -142 896 C ATOM 1494 O GLN A 237 14.774 24.775 11.985 1.00 35.04 O ANISOU 1494 O GLN A 237 5880 3767 3667 136 -123 995 O ATOM 1495 CB GLN A 237 14.705 25.104 15.201 1.00 29.31 C ANISOU 1495 CB GLN A 237 4871 2960 3307 163 -21 822 C ATOM 1496 CG GLN A 237 13.968 25.912 16.274 1.00 26.93 C ANISOU 1496 CG GLN A 237 4474 2602 3156 235 -17 829 C ATOM 1497 CD GLN A 237 14.862 26.927 16.929 1.00 37.98 C ANISOU 1497 CD GLN A 237 5904 3879 4648 220 121 800 C ATOM 1498 OE1 GLN A 237 16.049 26.700 17.175 1.00 39.14 O ANISOU 1498 OE1 GLN A 237 6073 4011 4788 139 209 725 O ATOM 1499 NE2 GLN A 237 14.322 28.084 17.219 1.00 29.25 N ANISOU 1499 NE2 GLN A 237 4797 2680 3638 297 144 859 N ATOM 1500 N ILE A 238 15.001 22.744 12.972 1.00 30.84 N ANISOU 1500 N ILE A 238 5219 3342 3158 44 -137 792 N ATOM 1501 CA ILE A 238 15.707 22.100 11.858 1.00 31.03 C ANISOU 1501 CA ILE A 238 5371 3397 3022 -18 -107 777 C ATOM 1502 C ILE A 238 14.721 22.019 10.670 1.00 38.89 C ANISOU 1502 C ILE A 238 6444 4461 3870 2 -252 864 C ATOM 1503 O ILE A 238 15.095 22.382 9.547 1.00 39.90 O ANISOU 1503 O ILE A 238 6719 4579 3862 -7 -227 933 O ATOM 1504 CB ILE A 238 16.296 20.710 12.253 1.00 32.66 C ANISOU 1504 CB ILE A 238 5539 3647 3224 -88 -70 644 C ATOM 1505 CG1 ILE A 238 17.494 20.855 13.212 1.00 32.16 C ANISOU 1505 CG1 ILE A 238 5421 3521 3278 -112 76 576 C ATOM 1506 CG2 ILE A 238 16.674 19.887 11.022 1.00 31.50 C ANISOU 1506 CG2 ILE A 238 5525 3543 2899 -143 -65 623 C ATOM 1507 CD1 ILE A 238 17.727 19.619 14.116 1.00 32.11 C ANISOU 1507 CD1 ILE A 238 5315 3553 3330 -148 84 462 C ATOM 1508 N PHE A 239 13.455 21.613 10.947 1.00 36.25 N ANISOU 1508 N PHE A 239 6007 4200 3567 28 -403 868 N ATOM 1509 CA PHE A 239 12.388 21.509 9.957 1.00 37.01 C ANISOU 1509 CA PHE A 239 6141 4379 3543 44 -572 948 C ATOM 1510 C PHE A 239 12.184 22.837 9.245 1.00 41.64 C ANISOU 1510 C PHE A 239 6808 4921 4091 120 -591 1105 C ATOM 1511 O PHE A 239 12.135 22.853 8.016 1.00 41.66 O ANISOU 1511 O PHE A 239 6947 4966 3917 106 -652 1175 O ATOM 1512 CB PHE A 239 11.064 20.993 10.571 1.00 39.58 C ANISOU 1512 CB PHE A 239 6301 4779 3957 63 -718 931 C ATOM 1513 CG PHE A 239 9.856 21.205 9.678 1.00 42.42 C ANISOU 1513 CG PHE A 239 6661 5221 4236 100 -907 1042 C ATOM 1514 CD1 PHE A 239 9.611 20.363 8.594 1.00 46.57 C ANISOU 1514 CD1 PHE A 239 7277 5841 4576 28 -1023 1027 C ATOM 1515 CD2 PHE A 239 8.992 22.278 9.889 1.00 45.09 C ANISOU 1515 CD2 PHE A 239 6915 5540 4679 209 -968 1166 C ATOM 1516 CE1 PHE A 239 8.526 20.594 7.736 1.00 47.49 C ANISOU 1516 CE1 PHE A 239 7394 6044 4605 57 -1214 1136 C ATOM 1517 CE2 PHE A 239 7.910 22.507 9.031 1.00 47.77 C ANISOU 1517 CE2 PHE A 239 7245 5961 4946 252 -1152 1285 C ATOM 1518 CZ PHE A 239 7.682 21.659 7.965 1.00 46.07 C ANISOU 1518 CZ PHE A 239 7114 5853 4538 172 -1283 1271 C ATOM 1519 N ARG A 240 12.061 23.944 10.016 1.00 38.52 N ANISOU 1519 N ARG A 240 6339 4437 3857 200 -535 1161 N ATOM 1520 CA ARG A 240 11.877 25.289 9.470 1.00 38.51 C ANISOU 1520 CA ARG A 240 6411 4366 3854 284 -533 1316 C ATOM 1521 C ARG A 240 13.055 25.712 8.608 1.00 44.27 C ANISOU 1521 C ARG A 240 7326 5033 4463 243 -407 1353 C ATOM 1522 O ARG A 240 12.843 26.314 7.568 1.00 44.66 O ANISOU 1522 O ARG A 240 7492 5079 4397 280 -453 1487 O ATOM 1523 CB ARG A 240 11.592 26.322 10.570 1.00 37.39 C ANISOU 1523 CB ARG A 240 6161 4121 3924 369 -470 1342 C ATOM 1524 CG ARG A 240 10.207 26.149 11.174 1.00 46.87 C ANISOU 1524 CG ARG A 240 7194 5382 5233 441 -604 1362 C ATOM 1525 CD ARG A 240 9.489 27.443 11.489 1.00 67.29 C ANISOU 1525 CD ARG A 240 9732 7881 7956 570 -604 1483 C ATOM 1526 NE ARG A 240 8.039 27.251 11.569 1.00 87.54 N ANISOU 1526 NE ARG A 240 12142 10528 10590 645 -758 1534 N ATOM 1527 CZ ARG A 240 7.157 27.655 10.656 1.00108.29 C ANISOU 1527 CZ ARG A 240 14765 13198 13182 730 -900 1689 C ATOM 1528 NH1 ARG A 240 7.565 28.298 9.565 1.00 96.02 N ANISOU 1528 NH1 ARG A 240 13371 11607 11507 756 -908 1816 N ATOM 1529 NH2 ARG A 240 5.861 27.425 10.830 1.00 99.03 N ANISOU 1529 NH2 ARG A 240 13424 12108 12096 792 -1035 1725 N ATOM 1530 N LYS A 241 14.282 25.365 9.009 1.00 42.06 N ANISOU 1530 N LYS A 241 7067 4709 4205 167 -250 1241 N ATOM 1531 CA LYS A 241 15.490 25.705 8.262 1.00 41.98 C ANISOU 1531 CA LYS A 241 7213 4638 4098 118 -106 1264 C ATOM 1532 C LYS A 241 15.622 24.896 6.964 1.00 47.86 C ANISOU 1532 C LYS A 241 8102 5472 4610 62 -148 1268 C ATOM 1533 O LYS A 241 15.853 25.487 5.913 1.00 47.97 O ANISOU 1533 O LYS A 241 8272 5464 4491 69 -121 1377 O ATOM 1534 CB LYS A 241 16.736 25.537 9.147 1.00 43.49 C ANISOU 1534 CB LYS A 241 7355 4766 4404 55 67 1142 C ATOM 1535 CG LYS A 241 18.003 26.165 8.577 1.00 46.90 C ANISOU 1535 CG LYS A 241 7914 5112 4795 12 240 1178 C ATOM 1536 CD LYS A 241 18.114 27.644 8.904 1.00 51.79 C ANISOU 1536 CD LYS A 241 8541 5599 5540 58 315 1268 C ATOM 1537 CE LYS A 241 19.468 28.188 8.543 1.00 63.48 C ANISOU 1537 CE LYS A 241 10119 6989 7011 -5 502 1284 C ATOM 1538 NZ LYS A 241 19.574 29.630 8.871 1.00 79.20 N ANISOU 1538 NZ LYS A 241 12122 8835 9134 28 580 1363 N ATOM 1539 N LEU A 242 15.462 23.573 7.030 1.00 45.81 N ANISOU 1539 N LEU A 242 7802 5306 4296 4 -208 1149 N ATOM 1540 CA LEU A 242 15.641 22.682 5.848 1.00 45.75 C ANISOU 1540 CA LEU A 242 7937 5378 4068 -61 -238 1121 C ATOM 1541 C LEU A 242 14.495 22.816 4.836 1.00 52.74 C ANISOU 1541 C LEU A 242 8902 6349 4788 -32 -429 1232 C ATOM 1542 O LEU A 242 14.774 22.765 3.632 1.00 52.13 O ANISOU 1542 O LEU A 242 9005 6303 4500 -67 -423 1274 O ATOM 1543 CB LEU A 242 15.754 21.235 6.337 1.00 44.83 C ANISOU 1543 CB LEU A 242 7758 5316 3957 -132 -237 955 C ATOM 1544 CG LEU A 242 17.074 20.861 7.000 1.00 47.56 C ANISOU 1544 CG LEU A 242 8058 5599 4414 -172 -50 843 C ATOM 1545 CD1 LEU A 242 17.098 19.382 7.327 1.00 47.24 C ANISOU 1545 CD1 LEU A 242 7969 5612 4367 -228 -70 702 C ATOM 1546 CD2 LEU A 242 18.248 21.220 6.109 1.00 48.12 C ANISOU 1546 CD2 LEU A 242 8277 5614 4393 -205 128 866 C ATOM 1547 N TRP A 243 13.263 22.982 5.309 1.00 51.90 N ANISOU 1547 N TRP A 243 8659 6286 4774 29 -597 1280 N ATOM 1548 CA TRP A 243 12.088 23.078 4.448 1.00 53.38 C ANISOU 1548 CA TRP A 243 8880 6570 4831 62 -806 1391 C ATOM 1549 C TRP A 243 11.572 24.506 4.253 1.00 65.61 C ANISOU 1549 C TRP A 243 10436 8067 6427 176 -849 1582 C ATOM 1550 O TRP A 243 10.498 24.702 3.679 1.00 65.23 O ANISOU 1550 O TRP A 243 10384 8099 6302 224 -1038 1695 O ATOM 1551 CB TRP A 243 10.984 22.143 4.951 1.00 51.13 C ANISOU 1551 CB TRP A 243 8434 6386 4607 44 -979 1318 C ATOM 1552 CG TRP A 243 11.240 20.714 4.610 1.00 51.29 C ANISOU 1552 CG TRP A 243 8511 6477 4500 -73 -992 1169 C ATOM 1553 CD1 TRP A 243 10.930 20.085 3.442 1.00 53.97 C ANISOU 1553 CD1 TRP A 243 8985 6912 4608 -140 -1110 1164 C ATOM 1554 CD2 TRP A 243 11.899 19.741 5.431 1.00 50.89 C ANISOU 1554 CD2 TRP A 243 8398 6396 4542 -136 -873 1003 C ATOM 1555 NE1 TRP A 243 11.344 18.776 3.485 1.00 53.42 N ANISOU 1555 NE1 TRP A 243 8945 6864 4489 -243 -1063 996 N ATOM 1556 CE2 TRP A 243 11.934 18.534 4.699 1.00 54.62 C ANISOU 1556 CE2 TRP A 243 8972 6938 4843 -236 -919 902 C ATOM 1557 CE3 TRP A 243 12.478 19.775 6.712 1.00 51.62 C ANISOU 1557 CE3 TRP A 243 8365 6407 4840 -119 -735 932 C ATOM 1558 CZ2 TRP A 243 12.494 17.361 5.218 1.00 53.50 C ANISOU 1558 CZ2 TRP A 243 8802 6777 4746 -308 -827 741 C ATOM 1559 CZ3 TRP A 243 13.046 18.619 7.217 1.00 52.87 C ANISOU 1559 CZ3 TRP A 243 8495 6562 5032 -190 -655 781 C ATOM 1560 CH2 TRP A 243 13.046 17.427 6.477 1.00 53.51 C ANISOU 1560 CH2 TRP A 243 8672 6702 4956 -278 -698 691 C ATOM 1561 N GLY A 244 12.366 25.484 4.672 1.00 68.72 N ANISOU 1561 N GLY A 244 10847 8325 6938 215 -675 1619 N ATOM 1562 CA GLY A 244 12.023 26.890 4.531 1.00 71.40 C ANISOU 1562 CA GLY A 244 11207 8582 7341 324 -679 1795 C ATOM 1563 C GLY A 244 12.460 27.478 3.209 1.00 82.62 C ANISOU 1563 C GLY A 244 12849 9985 8558 326 -653 1933 C ATOM 1564 O GLY A 244 12.889 26.748 2.301 1.00 82.15 O ANISOU 1564 O GLY A 244 12931 10004 8278 244 -662 1898 O ATOM 1565 N ARG A 245 12.322 28.825 3.108 1.00 84.51 N ANISOU 1565 N ARG A 245 13124 10115 8871 423 -615 2097 N ATOM 1566 CA ARG A 245 12.644 29.651 1.944 1.00 86.76 C ANISOU 1566 CA ARG A 245 13615 10357 8993 449 -581 2268 C ATOM 1567 C ARG A 245 14.106 29.506 1.535 1.00 95.27 C ANISOU 1567 C ARG A 245 14850 11376 9972 345 -362 2203 C ATOM 1568 O ARG A 245 15.010 29.695 2.356 1.00 95.00 O ANISOU 1568 O ARG A 245 14763 11233 10101 310 -178 2111 O ATOM 1569 CB ARG A 245 12.283 31.125 2.201 1.00 88.93 C ANISOU 1569 CB ARG A 245 13870 10495 9425 579 -559 2441 C ATOM 1570 CG ARG A 245 10.795 31.427 2.059 1.00104.45 C ANISOU 1570 CG ARG A 245 15747 12534 11404 702 -795 2585 C ATOM 1571 CD ARG A 245 10.441 32.773 2.661 1.00119.02 C ANISOU 1571 CD ARG A 245 17512 14227 13482 839 -750 2704 C ATOM 1572 NE ARG A 245 9.023 33.092 2.480 1.00131.39 N ANISOU 1572 NE ARG A 245 18991 15864 15066 971 -971 2863 N ATOM 1573 CZ ARG A 245 8.565 34.043 1.672 1.00147.76 C ANISOU 1573 CZ ARG A 245 21151 17872 17118 1091 -1015 3092 C ATOM 1574 NH1 ARG A 245 9.408 34.794 0.973 1.00135.34 N ANISOU 1574 NH1 ARG A 245 19765 16152 15505 1091 -845 3186 N ATOM 1575 NH2 ARG A 245 7.261 34.260 1.567 1.00135.48 N ANISOU 1575 NH2 ARG A 245 19489 16395 15591 1215 -1228 3233 N ATOM 1576 N GLN A 246 14.325 29.129 0.268 1.00 95.10 N ANISOU 1576 N GLN A 246 15019 11434 9681 291 -385 2244 N ATOM 1577 CA GLN A 246 15.649 28.903 -0.308 1.00 96.41 C ANISOU 1577 CA GLN A 246 15349 11565 9720 193 -179 2189 C ATOM 1578 C GLN A 246 16.379 30.231 -0.517 1.00102.27 C ANISOU 1578 C GLN A 246 16198 12146 10512 219 8 2323 C ATOM 1579 O GLN A 246 15.827 31.152 -1.130 1.00102.30 O ANISOU 1579 O GLN A 246 16289 12112 10468 304 -59 2519 O ATOM 1580 CB GLN A 246 15.547 28.128 -1.640 1.00 98.12 C ANISOU 1580 CB GLN A 246 15752 11915 9614 132 -261 2198 C ATOM 1581 CG GLN A 246 15.007 26.695 -1.509 1.00116.85 C ANISOU 1581 CG GLN A 246 18041 14435 11922 76 -421 2041 C ATOM 1582 CD GLN A 246 13.505 26.563 -1.684 1.00136.58 C ANISOU 1582 CD GLN A 246 20478 17052 14363 137 -711 2130 C ATOM 1583 OE1 GLN A 246 12.736 27.536 -1.624 1.00131.49 O ANISOU 1583 OE1 GLN A 246 19770 16373 13817 247 -808 2290 O ATOM 1584 NE2 GLN A 246 13.052 25.334 -1.897 1.00128.04 N ANISOU 1584 NE2 GLN A 246 19409 16111 13131 64 -855 2024 N ATOM 1585 N ILE A 247 17.618 30.322 0.004 1.00 99.49 N ANISOU 1585 N ILE A 247 15836 11698 10266 145 241 2220 N ATOM 1586 CA ILE A 247 18.490 31.496 -0.136 1.00 99.32 C ANISOU 1586 CA ILE A 247 15909 11518 10309 138 449 2318 C ATOM 1587 C ILE A 247 19.286 31.370 -1.455 1.00102.49 C ANISOU 1587 C ILE A 247 16548 11942 10451 73 568 2382 C ATOM 1588 O ILE A 247 19.917 30.334 -1.680 1.00102.07 O ANISOU 1588 O ILE A 247 16526 11967 10289 -15 638 2246 O ATOM 1589 CB ILE A 247 19.376 31.778 1.130 1.00102.49 C ANISOU 1589 CB ILE A 247 16160 11803 10978 89 629 2185 C ATOM 1590 CG1 ILE A 247 18.530 31.973 2.422 1.00103.00 C ANISOU 1590 CG1 ILE A 247 16334 11710 11090 45 867 2264 C ATOM 1591 CG2 ILE A 247 20.354 32.947 0.927 1.00103.10 C ANISOU 1591 CG2 ILE A 247 16127 11967 11078 2 667 1968 C ATOM 1592 CD1 ILE A 247 17.511 33.118 2.385 1.00110.95 C ANISOU 1592 CD1 ILE A 247 17354 12557 12244 126 882 2419 C ATOM 1593 N PRO A 248 19.257 32.399 -2.341 1.00 98.44 N ANISOU 1593 N PRO A 248 16210 11359 9835 118 600 2590 N ATOM 1594 CA PRO A 248 20.001 32.294 -3.614 1.00 97.83 C ANISOU 1594 CA PRO A 248 16373 11305 9492 54 724 2658 C ATOM 1595 C PRO A 248 21.531 32.271 -3.492 1.00 99.16 C ANISOU 1595 C PRO A 248 16565 11385 9726 -53 1020 2565 C ATOM 1596 O PRO A 248 22.080 32.518 -2.412 1.00 98.73 O ANISOU 1596 O PRO A 248 16348 11232 9934 -77 1132 2474 O ATOM 1597 CB PRO A 248 19.505 33.536 -4.369 1.00 99.80 C ANISOU 1597 CB PRO A 248 16780 11484 9657 143 679 2920 C ATOM 1598 CG PRO A 248 19.107 34.493 -3.300 1.00104.41 C ANISOU 1598 CG PRO A 248 17202 11928 10539 227 663 2965 C ATOM 1599 CD PRO A 248 18.559 33.651 -2.184 1.00100.01 C ANISOU 1599 CD PRO A 248 16405 11449 10146 233 532 2778 C ATOM 1600 N GLY A 249 22.192 31.946 -4.606 1.00 93.15 N ANISOU 1600 N GLY A 249 16003 10669 8719 -119 1142 2587 N ATOM 1601 CA GLY A 249 23.647 31.882 -4.711 1.00 91.49 C ANISOU 1601 CA GLY A 249 15833 10391 8537 -220 1433 2516 C ATOM 1602 C GLY A 249 24.321 30.657 -4.119 1.00 91.42 C ANISOU 1602 C GLY A 249 15675 10442 8617 -294 1507 2278 C ATOM 1603 O GLY A 249 25.553 30.579 -4.143 1.00 91.63 O ANISOU 1603 O GLY A 249 15692 10411 8712 -372 1750 2213 O ATOM 1604 N THR A 250 23.531 29.688 -3.592 1.00 83.71 N ANISOU 1604 N THR A 250 14577 9579 7649 -269 1305 2152 N ATOM 1605 CA THR A 250 24.043 28.454 -2.980 1.00 81.36 C ANISOU 1605 CA THR A 250 14137 9339 7437 -325 1351 1934 C ATOM 1606 C THR A 250 24.662 27.508 -4.021 1.00 80.35 C ANISOU 1606 C THR A 250 14172 9288 7068 -394 1473 1860 C ATOM 1607 O THR A 250 24.066 27.239 -5.074 1.00 80.30 O ANISOU 1607 O THR A 250 14355 9372 6784 -388 1370 1916 O ATOM 1608 CB THR A 250 22.989 27.766 -2.099 1.00 86.74 C ANISOU 1608 CB THR A 250 14640 10099 8217 -279 1111 1835 C ATOM 1609 OG1 THR A 250 21.740 27.728 -2.791 1.00 87.81 O ANISOU 1609 OG1 THR A 250 14879 10329 8157 -226 880 1930 O ATOM 1610 CG2 THR A 250 22.821 28.453 -0.747 1.00 82.85 C ANISOU 1610 CG2 THR A 250 13937 9515 8027 -236 1080 1831 C ATOM 1611 N THR A 251 25.872 27.039 -3.699 1.00 71.72 N ANISOU 1611 N THR A 251 13005 8158 6086 -459 1696 1736 N ATOM 1612 CA THR A 251 26.702 26.156 -4.558 1.00 68.56 C ANISOU 1612 CA THR A 251 12727 7802 5519 -523 1876 1644 C ATOM 1613 C THR A 251 26.078 24.765 -4.702 1.00 68.04 C ANISOU 1613 C THR A 251 12667 7858 5328 -529 1741 1490 C ATOM 1614 O THR A 251 25.051 24.510 -4.066 1.00 67.17 O ANISOU 1614 O THR A 251 12414 7791 5314 -493 1527 1432 O ATOM 1615 CB THR A 251 28.111 26.041 -3.973 1.00 66.33 C ANISOU 1615 CB THR A 251 12302 7440 5460 -576 2137 1558 C ATOM 1616 OG1 THR A 251 27.978 25.538 -2.646 1.00 62.00 O ANISOU 1616 OG1 THR A 251 11499 6898 5161 -563 2054 1421 O ATOM 1617 CG2 THR A 251 28.834 27.367 -3.933 1.00 59.42 C ANISOU 1617 CG2 THR A 251 11439 6438 4698 -596 2304 1697 C ATOM 1618 N SER A 252 26.672 23.928 -5.557 1.00 61.08 N ANISOU 1618 N SER A 252 11950 7018 4240 -580 1888 1418 N ATOM 1619 CA SER A 252 26.214 22.533 -5.785 1.00 59.02 C ANISOU 1619 CA SER A 252 11732 6849 3842 -604 1820 1256 C ATOM 1620 C SER A 252 26.388 21.731 -4.493 1.00 58.54 C ANISOU 1620 C SER A 252 11408 6783 4050 -593 1776 1095 C ATOM 1621 O SER A 252 25.497 20.949 -4.164 1.00 58.46 O ANISOU 1621 O SER A 252 11352 6843 4018 -583 1571 1014 O ATOM 1622 CB SER A 252 26.976 21.898 -6.918 1.00 61.30 C ANISOU 1622 CB SER A 252 12216 7140 3935 -659 2074 1200 C ATOM 1623 OG SER A 252 28.231 21.406 -6.477 1.00 68.81 O ANISOU 1623 OG SER A 252 13125 8121 4898 -684 2130 1003 O ATOM 1624 N GLU A 286 26.361 23.010 -1.520 1.00 51.81 N ANISOU 1624 N GLU A 286 9984 5820 3881 -513 1607 1094 N ATOM 1625 CA GLU A 286 25.359 23.466 -0.509 1.00 51.52 C ANISOU 1625 CA GLU A 286 9802 5786 3986 -460 1388 1129 C ATOM 1626 C GLU A 286 23.966 22.904 -0.852 1.00 56.13 C ANISOU 1626 C GLU A 286 10443 6471 4411 -435 1136 1123 C ATOM 1627 O GLU A 286 23.285 22.451 0.066 1.00 55.69 O ANISOU 1627 O GLU A 286 10231 6451 4478 -415 990 1043 O ATOM 1628 CB GLU A 286 25.373 24.985 -0.375 1.00 52.80 C ANISOU 1628 CB GLU A 286 9970 5861 4231 -432 1405 1291 C ATOM 1629 CG GLU A 286 26.496 25.480 0.508 1.00 66.05 C ANISOU 1629 CG GLU A 286 11518 7437 6141 -464 1605 1273 C ATOM 1630 CD GLU A 286 26.573 26.991 0.590 1.00102.91 C ANISOU 1630 CD GLU A 286 16264 11999 10838 -470 1718 1428 C ATOM 1631 OE1 GLU A 286 26.443 27.640 -0.465 1.00 97.83 O ANISOU 1631 OE1 GLU A 286 15822 11357 9991 -454 1703 1562 O ATOM 1632 OE2 GLU A 286 26.743 27.513 1.709 1.00106.89 O ANISOU 1632 OE2 GLU A 286 16632 12415 11568 -495 1822 1416 O ATOM 1633 N VAL A 287 23.638 22.815 -2.138 1.00 53.23 N ANISOU 1633 N VAL A 287 10300 6156 3769 -443 1088 1205 N ATOM 1634 CA VAL A 287 22.340 22.234 -2.590 1.00 53.32 C ANISOU 1634 CA VAL A 287 10389 6276 3595 -433 841 1209 C ATOM 1635 C VAL A 287 22.272 20.729 -2.284 1.00 56.80 C ANISOU 1635 C VAL A 287 10779 6780 4023 -477 797 1019 C ATOM 1636 O VAL A 287 21.222 20.283 -1.808 1.00 56.43 O ANISOU 1636 O VAL A 287 10629 6793 4021 -462 585 978 O ATOM 1637 CB VAL A 287 22.132 22.515 -4.087 1.00 57.14 C ANISOU 1637 CB VAL A 287 11146 6805 3758 -448 827 1328 C ATOM 1638 CG1 VAL A 287 21.046 21.641 -4.682 1.00 57.25 C ANISOU 1638 CG1 VAL A 287 11234 6946 3571 -453 559 1322 C ATOM 1639 CG2 VAL A 287 21.836 23.981 -4.335 1.00 56.70 C ANISOU 1639 CG2 VAL A 287 11144 6679 3720 -398 858 1533 C ATOM 1640 N LYS A 288 23.353 19.987 -2.551 1.00 52.39 N ANISOU 1640 N LYS A 288 10292 6199 3415 -528 1009 905 N ATOM 1641 CA LYS A 288 23.413 18.513 -2.336 1.00 51.42 C ANISOU 1641 CA LYS A 288 10143 6110 3287 -567 1015 722 C ATOM 1642 C LYS A 288 23.323 18.136 -0.854 1.00 52.97 C ANISOU 1642 C LYS A 288 10075 6277 3774 -540 973 640 C ATOM 1643 O LYS A 288 22.579 17.203 -0.538 1.00 52.67 O ANISOU 1643 O LYS A 288 9977 6283 3750 -554 843 537 O ATOM 1644 CB LYS A 288 24.713 17.944 -2.910 1.00 54.01 C ANISOU 1644 CB LYS A 288 10596 6399 3526 -610 1287 635 C ATOM 1645 CG LYS A 288 24.654 17.533 -4.372 1.00 71.01 C ANISOU 1645 CG LYS A 288 13043 8599 5338 -654 1324 664 C ATOM 1646 CD LYS A 288 26.022 17.318 -4.974 1.00 85.48 C ANISOU 1646 CD LYS A 288 14986 10377 7116 -683 1639 605 C ATOM 1647 CE LYS A 288 25.961 16.840 -6.406 1.00105.71 C ANISOU 1647 CE LYS A 288 17854 12980 9330 -725 1695 657 C ATOM 1648 NZ LYS A 288 26.874 17.616 -7.277 1.00118.91 N ANISOU 1648 NZ LYS A 288 19629 14592 10959 -748 2029 622 N ATOM 1649 N GLN A 289 24.043 18.855 0.009 1.00 47.85 N ANISOU 1649 N GLN A 289 9276 5552 3351 -509 1085 686 N ATOM 1650 CA GLN A 289 24.065 18.568 1.466 1.00 47.44 C ANISOU 1650 CA GLN A 289 8980 5474 3571 -483 1055 621 C ATOM 1651 C GLN A 289 22.661 18.769 2.036 1.00 53.89 C ANISOU 1651 C GLN A 289 9696 6336 4443 -447 801 660 C ATOM 1652 O GLN A 289 22.236 17.953 2.850 1.00 52.87 O ANISOU 1652 O GLN A 289 9430 6229 4430 -443 712 568 O ATOM 1653 CB GLN A 289 25.072 19.484 2.157 1.00 48.14 C ANISOU 1653 CB GLN A 289 8953 5479 3861 -472 1221 667 C ATOM 1654 CG GLN A 289 25.329 19.128 3.612 1.00 45.64 C ANISOU 1654 CG GLN A 289 8393 5140 3808 -453 1200 592 C ATOM 1655 CD GLN A 289 26.210 20.145 4.290 1.00 51.96 C ANISOU 1655 CD GLN A 289 9075 5866 4803 -453 1326 639 C ATOM 1656 OE1 GLN A 289 25.973 21.345 4.215 1.00 41.72 O ANISOU 1656 OE1 GLN A 289 7809 4525 3519 -442 1318 754 O ATOM 1657 NE2 GLN A 289 27.240 19.665 4.962 1.00 37.07 N ANISOU 1657 NE2 GLN A 289 7047 3960 3080 -466 1441 551 N ATOM 1658 N MET A 290 21.983 19.816 1.576 1.00 53.19 N ANISOU 1658 N MET A 290 9678 6258 4274 -416 692 803 N ATOM 1659 CA MET A 290 20.612 20.187 2.001 1.00 54.07 C ANISOU 1659 CA MET A 290 9704 6411 4427 -369 459 868 C ATOM 1660 C MET A 290 19.622 19.076 1.627 1.00 53.97 C ANISOU 1660 C MET A 290 9714 6499 4291 -398 274 790 C ATOM 1661 O MET A 290 18.759 18.777 2.452 1.00 53.16 O ANISOU 1661 O MET A 290 9452 6424 4321 -381 139 747 O ATOM 1662 CB MET A 290 20.246 21.512 1.323 1.00 57.73 C ANISOU 1662 CB MET A 290 10271 6855 4810 -325 419 1051 C ATOM 1663 CG MET A 290 18.854 21.590 0.763 1.00 63.62 C ANISOU 1663 CG MET A 290 11081 7691 5402 -297 178 1138 C ATOM 1664 SD MET A 290 17.694 22.003 2.046 1.00 70.60 S ANISOU 1664 SD MET A 290 11726 8584 6515 -221 -21 1171 S ATOM 1665 CE MET A 290 18.400 23.537 2.638 1.00 67.76 C ANISOU 1665 CE MET A 290 11352 8095 6299 -144 84 1337 C ATOM 1666 N ARG A 291 19.745 18.497 0.430 1.00 48.53 N ANISOU 1666 N ARG A 291 9227 5861 3353 -452 284 760 N ATOM 1667 CA ARG A 291 18.848 17.400 -0.021 1.00 47.24 C ANISOU 1667 CA ARG A 291 9120 5788 3042 -503 122 672 C ATOM 1668 C ARG A 291 19.092 16.159 0.838 1.00 45.90 C ANISOU 1668 C ARG A 291 8830 5599 3010 -536 169 501 C ATOM 1669 O ARG A 291 18.115 15.514 1.230 1.00 45.27 O ANISOU 1669 O ARG A 291 8665 5572 2963 -555 -1 443 O ATOM 1670 CB ARG A 291 19.068 17.133 -1.510 1.00 50.36 C ANISOU 1670 CB ARG A 291 9783 6226 3127 -561 160 668 C ATOM 1671 CG ARG A 291 18.726 18.332 -2.381 1.00 69.69 C ANISOU 1671 CG ARG A 291 12360 8723 5396 -534 39 843 C ATOM 1672 CD ARG A 291 18.742 18.073 -3.873 1.00 91.57 C ANISOU 1672 CD ARG A 291 15411 11542 7841 -597 85 834 C ATOM 1673 NE ARG A 291 18.245 19.243 -4.580 1.00107.13 N ANISOU 1673 NE ARG A 291 17526 13519 9661 -560 78 1023 N ATOM 1674 CZ ARG A 291 16.964 19.490 -4.820 1.00124.63 C ANISOU 1674 CZ ARG A 291 19829 15828 11695 -549 -148 1142 C ATOM 1675 NH1 ARG A 291 16.038 18.636 -4.420 1.00116.11 N ANISOU 1675 NH1 ARG A 291 18702 14853 10564 -582 -393 1084 N ATOM 1676 NH2 ARG A 291 16.614 20.586 -5.466 1.00109.47 N ANISOU 1676 NH2 ARG A 291 18046 13900 9648 -507 -133 1326 N ATOM 1677 N ALA A 292 20.364 15.869 1.108 1.00 39.36 N ANISOU 1677 N ALA A 292 7986 4694 2274 -540 400 430 N ATOM 1678 CA ALA A 292 20.780 14.723 1.941 1.00 37.88 C ANISOU 1678 CA ALA A 292 7686 4473 2234 -556 478 286 C ATOM 1679 C ALA A 292 20.276 14.923 3.371 1.00 41.66 C ANISOU 1679 C ALA A 292 7926 4943 2961 -512 379 296 C ATOM 1680 O ALA A 292 19.767 13.967 3.951 1.00 41.83 O ANISOU 1680 O ALA A 292 7862 4985 3046 -531 289 208 O ATOM 1681 CB ALA A 292 22.279 14.612 1.907 1.00 37.88 C ANISOU 1681 CB ALA A 292 7706 4396 2289 -554 745 243 C ATOM 1682 N ARG A 293 20.392 16.150 3.880 1.00 37.29 N ANISOU 1682 N ARG A 293 7276 4356 2538 -459 399 402 N ATOM 1683 CA ARG A 293 19.986 16.522 5.259 1.00 36.27 C ANISOU 1683 CA ARG A 293 6937 4212 2632 -413 326 421 C ATOM 1684 C ARG A 293 18.478 16.342 5.459 1.00 41.27 C ANISOU 1684 C ARG A 293 7504 4913 3265 -402 96 442 C ATOM 1685 O ARG A 293 18.101 15.884 6.528 1.00 41.99 O ANISOU 1685 O ARG A 293 7433 5006 3515 -390 40 393 O ATOM 1686 CB ARG A 293 20.437 17.950 5.566 1.00 32.90 C ANISOU 1686 CB ARG A 293 6469 3727 2306 -368 398 532 C ATOM 1687 CG ARG A 293 21.861 18.043 6.086 1.00 31.66 C ANISOU 1687 CG ARG A 293 6259 3499 2270 -378 609 490 C ATOM 1688 CD ARG A 293 22.342 19.470 6.141 1.00 34.60 C ANISOU 1688 CD ARG A 293 6629 3810 2709 -354 684 600 C ATOM 1689 NE ARG A 293 23.625 19.582 6.806 1.00 41.05 N ANISOU 1689 NE ARG A 293 7356 4565 3674 -371 863 558 N ATOM 1690 CZ ARG A 293 24.213 20.729 7.096 1.00 47.71 C ANISOU 1690 CZ ARG A 293 8168 5343 4619 -369 952 626 C ATOM 1691 NH1 ARG A 293 23.631 21.865 6.766 1.00 32.55 N ANISOU 1691 NH1 ARG A 293 6308 3393 2667 -341 892 743 N ATOM 1692 NH2 ARG A 293 25.377 20.740 7.708 1.00 32.00 N ANISOU 1692 NH2 ARG A 293 6081 3311 2768 -396 1101 579 N ATOM 1693 N ARG A 294 17.659 16.690 4.467 1.00 36.89 N ANISOU 1693 N ARG A 294 7068 4418 2532 -408 -38 519 N ATOM 1694 CA ARG A 294 16.183 16.554 4.579 1.00 36.78 C ANISOU 1694 CA ARG A 294 6987 4482 2507 -401 -268 548 C ATOM 1695 C ARG A 294 15.804 15.086 4.802 1.00 42.60 C ANISOU 1695 C ARG A 294 7684 5257 3245 -466 -331 409 C ATOM 1696 O ARG A 294 14.908 14.830 5.601 1.00 43.47 O ANISOU 1696 O ARG A 294 7635 5392 3490 -456 -442 391 O ATOM 1697 CB ARG A 294 15.513 17.090 3.315 1.00 34.02 C ANISOU 1697 CB ARG A 294 6789 4198 1941 -402 -395 656 C ATOM 1698 CG ARG A 294 15.585 18.600 3.169 1.00 39.93 C ANISOU 1698 CG ARG A 294 7534 4912 2726 -320 -398 823 C ATOM 1699 CD ARG A 294 14.704 19.031 2.021 1.00 46.64 C ANISOU 1699 CD ARG A 294 8523 5837 3359 -315 -551 941 C ATOM 1700 NE ARG A 294 14.869 20.419 1.640 1.00 55.26 N ANISOU 1700 NE ARG A 294 9653 6878 4467 -236 -520 1110 N ATOM 1701 CZ ARG A 294 14.069 21.049 0.797 1.00 74.87 C ANISOU 1701 CZ ARG A 294 12228 9414 6806 -198 -663 1258 C ATOM 1702 NH1 ARG A 294 13.047 20.412 0.258 1.00 64.52 N ANISOU 1702 NH1 ARG A 294 10972 8222 5319 -240 -860 1252 N ATOM 1703 NH2 ARG A 294 14.284 22.314 0.498 1.00 63.54 N ANISOU 1703 NH2 ARG A 294 10827 7910 5406 -120 -615 1415 N ATOM 1704 N LYS A 295 16.471 14.174 4.098 1.00 38.61 N ANISOU 1704 N LYS A 295 7327 4745 2599 -533 -240 308 N ATOM 1705 CA LYS A 295 16.250 12.730 4.211 1.00 37.68 C ANISOU 1705 CA LYS A 295 7207 4639 2470 -602 -268 165 C ATOM 1706 C LYS A 295 16.622 12.216 5.609 1.00 40.80 C ANISOU 1706 C LYS A 295 7422 4976 3104 -579 -188 98 C ATOM 1707 O LYS A 295 15.838 11.488 6.218 1.00 41.57 O ANISOU 1707 O LYS A 295 7415 5096 3282 -605 -295 45 O ATOM 1708 CB LYS A 295 17.044 11.976 3.127 1.00 39.85 C ANISOU 1708 CB LYS A 295 7696 4894 2553 -665 -141 73 C ATOM 1709 CG LYS A 295 16.557 12.219 1.707 1.00 40.31 C ANISOU 1709 CG LYS A 295 7955 5024 2337 -708 -243 118 C ATOM 1710 CD LYS A 295 17.464 11.536 0.706 1.00 46.57 C ANISOU 1710 CD LYS A 295 8967 5785 2941 -764 -79 21 C ATOM 1711 CE LYS A 295 17.012 11.770 -0.706 1.00 63.95 C ANISOU 1711 CE LYS A 295 11386 8065 4846 -815 -183 62 C ATOM 1712 NZ LYS A 295 17.738 10.897 -1.660 1.00 78.60 N ANISOU 1712 NZ LYS A 295 13468 9894 6504 -884 -33 -62 N ATOM 1713 N THR A 296 17.799 12.629 6.125 1.00 35.61 N ANISOU 1713 N THR A 296 6723 4248 2560 -533 -6 108 N ATOM 1714 CA THR A 296 18.301 12.261 7.452 1.00 34.70 C ANISOU 1714 CA THR A 296 6442 4082 2659 -505 75 59 C ATOM 1715 C THR A 296 17.422 12.837 8.561 1.00 38.76 C ANISOU 1715 C THR A 296 6777 4620 3329 -462 -48 119 C ATOM 1716 O THR A 296 17.083 12.101 9.489 1.00 38.83 O ANISOU 1716 O THR A 296 6667 4628 3457 -468 -83 63 O ATOM 1717 CB THR A 296 19.789 12.627 7.592 1.00 35.37 C ANISOU 1717 CB THR A 296 6532 4099 2807 -475 286 61 C ATOM 1718 OG1 THR A 296 20.510 11.963 6.565 1.00 34.24 O ANISOU 1718 OG1 THR A 296 6552 3936 2523 -513 408 -4 O ATOM 1719 CG2 THR A 296 20.380 12.222 8.931 1.00 32.39 C ANISOU 1719 CG2 THR A 296 5987 3680 2638 -447 360 16 C ATOM 1720 N ALA A 297 17.056 14.140 8.468 1.00 34.74 N ANISOU 1720 N ALA A 297 6254 4126 2821 -415 -103 235 N ATOM 1721 CA ALA A 297 16.215 14.806 9.469 1.00 34.15 C ANISOU 1721 CA ALA A 297 6018 4064 2891 -365 -203 296 C ATOM 1722 C ALA A 297 14.857 14.126 9.569 1.00 38.55 C ANISOU 1722 C ALA A 297 6512 4691 3444 -391 -380 274 C ATOM 1723 O ALA A 297 14.411 13.835 10.682 1.00 37.99 O ANISOU 1723 O ALA A 297 6292 4621 3521 -379 -411 248 O ATOM 1724 CB ALA A 297 16.047 16.279 9.141 1.00 34.64 C ANISOU 1724 CB ALA A 297 6107 4117 2938 -308 -223 424 C ATOM 1725 N LYS A 298 14.235 13.815 8.402 1.00 35.39 N ANISOU 1725 N LYS A 298 6228 4350 2867 -438 -493 280 N ATOM 1726 CA LYS A 298 12.946 13.130 8.319 1.00 35.43 C ANISOU 1726 CA LYS A 298 6180 4430 2852 -484 -673 256 C ATOM 1727 C LYS A 298 13.031 11.782 9.044 1.00 38.59 C ANISOU 1727 C LYS A 298 6517 4806 3341 -539 -634 131 C ATOM 1728 O LYS A 298 12.151 11.475 9.850 1.00 39.59 O ANISOU 1728 O LYS A 298 6496 4959 3587 -542 -722 124 O ATOM 1729 CB LYS A 298 12.514 12.967 6.847 1.00 39.02 C ANISOU 1729 CB LYS A 298 6800 4951 3075 -542 -786 268 C ATOM 1730 CG LYS A 298 11.153 12.305 6.675 1.00 64.12 C ANISOU 1730 CG LYS A 298 9914 8219 6229 -600 -996 250 C ATOM 1731 CD LYS A 298 10.831 12.045 5.212 1.00 81.06 C ANISOU 1731 CD LYS A 298 12239 10436 8126 -677 -1110 238 C ATOM 1732 CE LYS A 298 9.662 11.096 5.062 1.00 98.92 C ANISOU 1732 CE LYS A 298 14434 12779 10373 -765 -1306 186 C ATOM 1733 NZ LYS A 298 9.378 10.785 3.634 1.00111.40 N ANISOU 1733 NZ LYS A 298 16198 14434 11695 -856 -1429 159 N ATOM 1734 N MET A 299 14.131 11.020 8.822 1.00 33.33 N ANISOU 1734 N MET A 299 5953 4081 2630 -572 -486 39 N ATOM 1735 CA MET A 299 14.365 9.737 9.484 1.00 31.93 C ANISOU 1735 CA MET A 299 5732 3860 2540 -613 -426 -71 C ATOM 1736 C MET A 299 14.522 9.905 10.995 1.00 35.47 C ANISOU 1736 C MET A 299 6001 4277 3200 -555 -373 -54 C ATOM 1737 O MET A 299 13.927 9.138 11.755 1.00 35.30 O ANISOU 1737 O MET A 299 5881 4259 3275 -581 -421 -94 O ATOM 1738 CB MET A 299 15.591 9.026 8.901 1.00 34.29 C ANISOU 1738 CB MET A 299 6177 4094 2759 -638 -260 -157 C ATOM 1739 CG MET A 299 15.833 7.672 9.514 1.00 38.05 C ANISOU 1739 CG MET A 299 6620 4513 3325 -671 -194 -263 C ATOM 1740 SD MET A 299 17.312 6.851 8.913 1.00 42.81 S ANISOU 1740 SD MET A 299 7373 5026 3866 -679 21 -359 S ATOM 1741 CE MET A 299 18.549 7.597 9.925 1.00 39.00 C ANISOU 1741 CE MET A 299 6769 4502 3548 -582 175 -296 C ATOM 1742 N LEU A 300 15.331 10.894 11.425 1.00 32.05 N ANISOU 1742 N LEU A 300 5534 3812 2832 -486 -273 4 N ATOM 1743 CA LEU A 300 15.605 11.173 12.835 1.00 31.00 C ANISOU 1743 CA LEU A 300 5250 3651 2878 -435 -218 19 C ATOM 1744 C LEU A 300 14.373 11.616 13.590 1.00 34.63 C ANISOU 1744 C LEU A 300 5573 4155 3430 -411 -342 71 C ATOM 1745 O LEU A 300 14.203 11.201 14.732 1.00 34.88 O ANISOU 1745 O LEU A 300 5489 4179 3586 -404 -332 46 O ATOM 1746 CB LEU A 300 16.744 12.176 13.000 1.00 30.64 C ANISOU 1746 CB LEU A 300 5211 3562 2867 -385 -92 62 C ATOM 1747 CG LEU A 300 18.119 11.693 12.575 1.00 34.39 C ANISOU 1747 CG LEU A 300 5773 3988 3307 -398 64 9 C ATOM 1748 CD1 LEU A 300 19.100 12.864 12.498 1.00 34.17 C ANISOU 1748 CD1 LEU A 300 5757 3927 3297 -363 171 66 C ATOM 1749 CD2 LEU A 300 18.611 10.513 13.450 1.00 34.48 C ANISOU 1749 CD2 LEU A 300 5712 3966 3422 -404 129 -67 C ATOM 1750 N MET A 301 13.491 12.400 12.946 1.00 30.54 N ANISOU 1750 N MET A 301 5068 3686 2849 -396 -458 146 N ATOM 1751 CA MET A 301 12.228 12.846 13.535 1.00 31.03 C ANISOU 1751 CA MET A 301 4995 3795 3001 -365 -577 203 C ATOM 1752 C MET A 301 11.319 11.630 13.821 1.00 35.52 C ANISOU 1752 C MET A 301 5494 4402 3601 -430 -665 142 C ATOM 1753 O MET A 301 10.683 11.564 14.884 1.00 34.62 O ANISOU 1753 O MET A 301 5237 4299 3620 -412 -686 148 O ATOM 1754 CB MET A 301 11.521 13.865 12.626 1.00 33.69 C ANISOU 1754 CB MET A 301 5369 4176 3257 -331 -688 304 C ATOM 1755 CG MET A 301 12.152 15.258 12.645 1.00 37.84 C ANISOU 1755 CG MET A 301 5923 4650 3803 -254 -606 386 C ATOM 1756 SD MET A 301 11.410 16.332 11.386 1.00 42.90 S ANISOU 1756 SD MET A 301 6644 5334 4321 -214 -731 518 S ATOM 1757 CE MET A 301 12.788 17.460 11.051 1.00 39.95 C ANISOU 1757 CE MET A 301 6387 4868 3922 -170 -565 570 C ATOM 1758 N VAL A 302 11.320 10.637 12.903 1.00 31.80 N ANISOU 1758 N VAL A 302 5132 3942 3008 -512 -701 75 N ATOM 1759 CA VAL A 302 10.542 9.395 13.052 1.00 30.93 C ANISOU 1759 CA VAL A 302 4979 3855 2920 -594 -776 4 C ATOM 1760 C VAL A 302 11.098 8.546 14.226 1.00 34.11 C ANISOU 1760 C VAL A 302 5319 4192 3448 -597 -657 -59 C ATOM 1761 O VAL A 302 10.312 8.097 15.054 1.00 34.21 O ANISOU 1761 O VAL A 302 5209 4220 3570 -616 -700 -65 O ATOM 1762 CB VAL A 302 10.392 8.614 11.717 1.00 33.90 C ANISOU 1762 CB VAL A 302 5506 4254 3122 -689 -847 -59 C ATOM 1763 CG1 VAL A 302 9.699 7.262 11.921 1.00 33.40 C ANISOU 1763 CG1 VAL A 302 5407 4190 3093 -788 -905 -148 C ATOM 1764 CG2 VAL A 302 9.631 9.448 10.685 1.00 33.42 C ANISOU 1764 CG2 VAL A 302 5481 4278 2941 -685 -1001 22 C ATOM 1765 N VAL A 303 12.439 8.403 14.332 1.00 29.26 N ANISOU 1765 N VAL A 303 4780 3511 2828 -572 -507 -94 N ATOM 1766 CA VAL A 303 13.118 7.671 15.412 1.00 28.23 C ANISOU 1766 CA VAL A 303 4596 3320 2810 -561 -394 -137 C ATOM 1767 C VAL A 303 12.737 8.303 16.760 1.00 33.18 C ANISOU 1767 C VAL A 303 5065 3965 3578 -503 -398 -80 C ATOM 1768 O VAL A 303 12.337 7.585 17.674 1.00 34.63 O ANISOU 1768 O VAL A 303 5164 4140 3853 -521 -396 -100 O ATOM 1769 CB VAL A 303 14.675 7.569 15.206 1.00 31.08 C ANISOU 1769 CB VAL A 303 5050 3616 3145 -532 -239 -169 C ATOM 1770 CG1 VAL A 303 15.372 6.889 16.381 1.00 30.18 C ANISOU 1770 CG1 VAL A 303 4864 3450 3155 -507 -139 -194 C ATOM 1771 CG2 VAL A 303 15.026 6.841 13.908 1.00 30.82 C ANISOU 1771 CG2 VAL A 303 5182 3557 2972 -589 -214 -238 C ATOM 1772 N VAL A 304 12.819 9.637 16.866 1.00 29.15 N ANISOU 1772 N VAL A 304 4524 3473 3079 -438 -398 -11 N ATOM 1773 CA VAL A 304 12.476 10.383 18.085 1.00 28.28 C ANISOU 1773 CA VAL A 304 4283 3373 3089 -381 -390 36 C ATOM 1774 C VAL A 304 10.982 10.220 18.436 1.00 33.55 C ANISOU 1774 C VAL A 304 4839 4093 3815 -397 -500 58 C ATOM 1775 O VAL A 304 10.663 9.953 19.597 1.00 34.48 O ANISOU 1775 O VAL A 304 4855 4211 4036 -389 -473 54 O ATOM 1776 CB VAL A 304 12.945 11.871 18.006 1.00 29.75 C ANISOU 1776 CB VAL A 304 4483 3549 3273 -314 -355 97 C ATOM 1777 CG1 VAL A 304 12.439 12.698 19.193 1.00 28.29 C ANISOU 1777 CG1 VAL A 304 4176 3369 3202 -257 -351 137 C ATOM 1778 CG2 VAL A 304 14.464 11.946 17.909 1.00 28.91 C ANISOU 1778 CG2 VAL A 304 4453 3390 3141 -306 -231 71 C ATOM 1779 N LEU A 305 10.086 10.328 17.437 1.00 29.77 N ANISOU 1779 N LEU A 305 4377 3664 3269 -425 -621 83 N ATOM 1780 CA LEU A 305 8.654 10.147 17.662 1.00 29.87 C ANISOU 1780 CA LEU A 305 4269 3737 3345 -448 -734 107 C ATOM 1781 C LEU A 305 8.312 8.709 18.119 1.00 32.85 C ANISOU 1781 C LEU A 305 4609 4105 3769 -531 -733 38 C ATOM 1782 O LEU A 305 7.522 8.556 19.048 1.00 33.09 O ANISOU 1782 O LEU A 305 4508 4156 3911 -530 -741 54 O ATOM 1783 CB LEU A 305 7.810 10.596 16.448 1.00 30.45 C ANISOU 1783 CB LEU A 305 4364 3875 3332 -460 -881 156 C ATOM 1784 CG LEU A 305 6.297 10.296 16.503 1.00 36.62 C ANISOU 1784 CG LEU A 305 5007 4731 4175 -498 -1019 180 C ATOM 1785 CD1 LEU A 305 5.595 11.075 17.619 1.00 37.28 C ANISOU 1785 CD1 LEU A 305 4922 4830 4413 -416 -1001 246 C ATOM 1786 CD2 LEU A 305 5.635 10.568 15.174 1.00 40.37 C ANISOU 1786 CD2 LEU A 305 5526 5277 4536 -526 -1179 220 C ATOM 1787 N VAL A 306 8.927 7.679 17.503 1.00 28.25 N ANISOU 1787 N VAL A 306 4146 3484 3105 -600 -707 -37 N ATOM 1788 CA VAL A 306 8.726 6.270 17.866 1.00 28.50 C ANISOU 1788 CA VAL A 306 4169 3481 3179 -682 -690 -105 C ATOM 1789 C VAL A 306 9.293 5.993 19.292 1.00 32.26 C ANISOU 1789 C VAL A 306 4583 3907 3767 -639 -565 -104 C ATOM 1790 O VAL A 306 8.651 5.273 20.062 1.00 32.64 O ANISOU 1790 O VAL A 306 4547 3952 3903 -677 -565 -111 O ATOM 1791 CB VAL A 306 9.236 5.290 16.763 1.00 32.83 C ANISOU 1791 CB VAL A 306 4878 3988 3609 -762 -686 -190 C ATOM 1792 CG1 VAL A 306 9.190 3.826 17.218 1.00 32.05 C ANISOU 1792 CG1 VAL A 306 4784 3825 3569 -837 -640 -262 C ATOM 1793 CG2 VAL A 306 8.426 5.466 15.476 1.00 32.67 C ANISOU 1793 CG2 VAL A 306 4907 4035 3471 -822 -836 -192 C ATOM 1794 N PHE A 307 10.442 6.611 19.655 1.00 27.18 N ANISOU 1794 N PHE A 307 3975 3232 3120 -563 -465 -88 N ATOM 1795 CA PHE A 307 11.026 6.512 21.001 1.00 26.41 C ANISOU 1795 CA PHE A 307 3821 3103 3112 -517 -364 -77 C ATOM 1796 C PHE A 307 10.057 7.133 22.041 1.00 32.01 C ANISOU 1796 C PHE A 307 4390 3859 3913 -485 -389 -25 C ATOM 1797 O PHE A 307 9.807 6.526 23.091 1.00 32.28 O ANISOU 1797 O PHE A 307 4360 3884 4022 -496 -350 -25 O ATOM 1798 CB PHE A 307 12.409 7.208 21.058 1.00 27.20 C ANISOU 1798 CB PHE A 307 3976 3174 3185 -452 -275 -69 C ATOM 1799 CG PHE A 307 13.134 7.043 22.384 1.00 27.56 C ANISOU 1799 CG PHE A 307 3972 3196 3305 -413 -186 -62 C ATOM 1800 CD1 PHE A 307 12.868 7.896 23.455 1.00 29.61 C ANISOU 1800 CD1 PHE A 307 4140 3486 3623 -366 -177 -22 C ATOM 1801 CD2 PHE A 307 14.075 6.028 22.564 1.00 28.13 C ANISOU 1801 CD2 PHE A 307 4089 3214 3385 -419 -111 -94 C ATOM 1802 CE1 PHE A 307 13.503 7.717 24.690 1.00 29.94 C ANISOU 1802 CE1 PHE A 307 4145 3516 3713 -339 -108 -16 C ATOM 1803 CE2 PHE A 307 14.743 5.875 23.786 1.00 30.44 C ANISOU 1803 CE2 PHE A 307 4332 3495 3738 -380 -46 -75 C ATOM 1804 CZ PHE A 307 14.435 6.705 24.849 1.00 28.75 C ANISOU 1804 CZ PHE A 307 4035 3323 3565 -346 -51 -38 C ATOM 1805 N ALA A 308 9.516 8.342 21.729 1.00 28.56 N ANISOU 1805 N ALA A 308 3915 3468 3471 -441 -446 23 N ATOM 1806 CA ALA A 308 8.559 9.079 22.560 1.00 27.62 C ANISOU 1806 CA ALA A 308 3666 3388 3438 -397 -462 72 C ATOM 1807 C ALA A 308 7.310 8.220 22.837 1.00 32.67 C ANISOU 1807 C ALA A 308 4207 4061 4145 -460 -516 70 C ATOM 1808 O ALA A 308 6.886 8.119 23.986 1.00 32.80 O ANISOU 1808 O ALA A 308 4133 4084 4247 -447 -465 84 O ATOM 1809 CB ALA A 308 8.163 10.377 21.876 1.00 27.57 C ANISOU 1809 CB ALA A 308 3652 3413 3412 -341 -524 126 C ATOM 1810 N LEU A 309 6.767 7.557 21.800 1.00 29.55 N ANISOU 1810 N LEU A 309 3837 3686 3706 -536 -614 47 N ATOM 1811 CA LEU A 309 5.593 6.692 21.897 1.00 29.99 C ANISOU 1811 CA LEU A 309 3798 3771 3824 -618 -678 38 C ATOM 1812 C LEU A 309 5.847 5.376 22.646 1.00 34.46 C ANISOU 1812 C LEU A 309 4379 4281 4434 -680 -598 -7 C ATOM 1813 O LEU A 309 5.012 4.998 23.466 1.00 34.88 O ANISOU 1813 O LEU A 309 4320 4349 4584 -708 -583 10 O ATOM 1814 CB LEU A 309 4.994 6.424 20.505 1.00 30.61 C ANISOU 1814 CB LEU A 309 3910 3891 3828 -693 -820 20 C ATOM 1815 CG LEU A 309 4.339 7.628 19.792 1.00 36.46 C ANISOU 1815 CG LEU A 309 4601 4706 4546 -638 -931 89 C ATOM 1816 CD1 LEU A 309 4.163 7.350 18.319 1.00 37.26 C ANISOU 1816 CD1 LEU A 309 4793 4842 4523 -710 -1062 65 C ATOM 1817 CD2 LEU A 309 2.977 7.964 20.396 1.00 38.31 C ANISOU 1817 CD2 LEU A 309 4639 5005 4913 -621 -981 148 C ATOM 1818 N CYS A 310 6.987 4.688 22.382 1.00 30.66 N ANISOU 1818 N CYS A 310 4032 3730 3888 -697 -537 -58 N ATOM 1819 CA CYS A 310 7.353 3.420 23.041 1.00 29.50 C ANISOU 1819 CA CYS A 310 3915 3513 3782 -742 -454 -92 C ATOM 1820 C CYS A 310 7.633 3.555 24.533 1.00 29.74 C ANISOU 1820 C CYS A 310 3883 3533 3885 -681 -352 -49 C ATOM 1821 O CYS A 310 7.393 2.613 25.287 1.00 28.52 O ANISOU 1821 O CYS A 310 3702 3343 3791 -722 -304 -48 O ATOM 1822 CB CYS A 310 8.522 2.744 22.332 1.00 29.70 C ANISOU 1822 CB CYS A 310 4094 3463 3728 -757 -409 -150 C ATOM 1823 SG CYS A 310 8.118 2.088 20.700 1.00 34.02 S ANISOU 1823 SG CYS A 310 4744 4003 4181 -867 -510 -226 S ATOM 1824 N TYR A 311 8.199 4.690 24.936 1.00 25.39 N ANISOU 1824 N TYR A 311 3324 3006 3318 -588 -318 -16 N ATOM 1825 CA TYR A 311 8.596 4.977 26.314 1.00 24.58 C ANISOU 1825 CA TYR A 311 3182 2902 3257 -529 -228 16 C ATOM 1826 C TYR A 311 7.562 5.769 27.098 1.00 28.53 C ANISOU 1826 C TYR A 311 3561 3460 3821 -498 -229 59 C ATOM 1827 O TYR A 311 7.743 5.946 28.297 1.00 28.50 O ANISOU 1827 O TYR A 311 3527 3458 3841 -460 -153 80 O ATOM 1828 CB TYR A 311 9.978 5.668 26.337 1.00 24.44 C ANISOU 1828 CB TYR A 311 3236 2866 3183 -459 -181 13 C ATOM 1829 CG TYR A 311 11.118 4.701 26.100 1.00 25.81 C ANISOU 1829 CG TYR A 311 3504 2976 3326 -472 -134 -17 C ATOM 1830 CD1 TYR A 311 11.549 4.399 24.811 1.00 27.42 C ANISOU 1830 CD1 TYR A 311 3800 3149 3470 -500 -158 -59 C ATOM 1831 CD2 TYR A 311 11.778 4.095 27.166 1.00 26.82 C ANISOU 1831 CD2 TYR A 311 3634 3076 3482 -451 -60 0 C ATOM 1832 CE1 TYR A 311 12.578 3.483 24.587 1.00 26.92 C ANISOU 1832 CE1 TYR A 311 3820 3017 3391 -504 -98 -89 C ATOM 1833 CE2 TYR A 311 12.847 3.220 26.955 1.00 27.79 C ANISOU 1833 CE2 TYR A 311 3833 3135 3592 -447 -13 -18 C ATOM 1834 CZ TYR A 311 13.248 2.920 25.663 1.00 33.56 C ANISOU 1834 CZ TYR A 311 4647 3826 4278 -471 -25 -65 C ATOM 1835 OH TYR A 311 14.285 2.040 25.449 1.00 33.72 O ANISOU 1835 OH TYR A 311 4739 3776 4298 -459 38 -85 O ATOM 1836 N LEU A 312 6.478 6.230 26.438 1.00 26.06 N ANISOU 1836 N LEU A 312 3175 3194 3532 -512 -313 73 N ATOM 1837 CA LEU A 312 5.398 6.972 27.095 1.00 26.66 C ANISOU 1837 CA LEU A 312 3121 3322 3687 -475 -308 115 C ATOM 1838 C LEU A 312 4.632 6.104 28.119 1.00 30.75 C ANISOU 1838 C LEU A 312 3555 3843 4286 -523 -251 128 C ATOM 1839 O LEU A 312 4.554 6.540 29.269 1.00 30.22 O ANISOU 1839 O LEU A 312 3445 3786 4250 -473 -164 152 O ATOM 1840 CB LEU A 312 4.443 7.670 26.102 1.00 26.82 C ANISOU 1840 CB LEU A 312 3071 3394 3723 -468 -419 141 C ATOM 1841 CG LEU A 312 3.256 8.460 26.710 1.00 31.77 C ANISOU 1841 CG LEU A 312 3545 4073 4454 -417 -411 191 C ATOM 1842 CD1 LEU A 312 3.714 9.768 27.328 1.00 31.55 C ANISOU 1842 CD1 LEU A 312 3532 4034 4424 -307 -337 211 C ATOM 1843 CD2 LEU A 312 2.227 8.776 25.661 1.00 33.72 C ANISOU 1843 CD2 LEU A 312 3705 4378 4730 -431 -543 223 C ATOM 1844 N PRO A 313 4.102 4.891 27.805 1.00 27.85 N ANISOU 1844 N PRO A 313 3172 3461 3950 -624 -284 111 N ATOM 1845 CA PRO A 313 3.380 4.141 28.847 1.00 27.50 C ANISOU 1845 CA PRO A 313 3045 3414 3990 -670 -213 133 C ATOM 1846 C PRO A 313 4.225 3.810 30.097 1.00 30.12 C ANISOU 1846 C PRO A 313 3441 3704 4298 -636 -90 147 C ATOM 1847 O PRO A 313 3.764 4.100 31.196 1.00 29.88 O ANISOU 1847 O PRO A 313 3342 3700 4309 -606 -12 181 O ATOM 1848 CB PRO A 313 2.856 2.908 28.104 1.00 28.90 C ANISOU 1848 CB PRO A 313 3223 3565 4194 -794 -278 102 C ATOM 1849 CG PRO A 313 2.805 3.317 26.684 1.00 32.55 C ANISOU 1849 CG PRO A 313 3711 4055 4601 -807 -408 74 C ATOM 1850 CD PRO A 313 4.032 4.170 26.515 1.00 29.06 C ANISOU 1850 CD PRO A 313 3377 3599 4066 -709 -384 70 C ATOM 1851 N ILE A 314 5.452 3.286 29.945 1.00 25.67 N ANISOU 1851 N ILE A 314 3005 3082 3666 -632 -73 123 N ATOM 1852 CA ILE A 314 6.317 2.932 31.091 1.00 25.23 C ANISOU 1852 CA ILE A 314 3007 2994 3583 -596 24 146 C ATOM 1853 C ILE A 314 6.655 4.144 32.000 1.00 28.73 C ANISOU 1853 C ILE A 314 3436 3484 3994 -505 73 165 C ATOM 1854 O ILE A 314 6.639 3.999 33.228 1.00 27.31 O ANISOU 1854 O ILE A 314 3248 3313 3814 -490 153 197 O ATOM 1855 CB ILE A 314 7.584 2.153 30.660 1.00 27.96 C ANISOU 1855 CB ILE A 314 3477 3269 3877 -599 27 123 C ATOM 1856 CG1 ILE A 314 8.245 1.451 31.873 1.00 28.65 C ANISOU 1856 CG1 ILE A 314 3607 3322 3958 -577 116 165 C ATOM 1857 CG2 ILE A 314 8.594 3.009 29.834 1.00 27.03 C ANISOU 1857 CG2 ILE A 314 3424 3158 3689 -542 -14 90 C ATOM 1858 CD1 ILE A 314 9.177 0.269 31.514 1.00 35.65 C ANISOU 1858 CD1 ILE A 314 4591 4118 4835 -593 134 156 C ATOM 1859 N SER A 315 6.954 5.318 31.383 1.00 24.90 N ANISOU 1859 N SER A 315 2960 3025 3477 -451 26 145 N ATOM 1860 CA SER A 315 7.301 6.579 32.048 1.00 23.74 C ANISOU 1860 CA SER A 315 2812 2908 3301 -373 66 148 C ATOM 1861 C SER A 315 6.132 7.112 32.840 1.00 28.46 C ANISOU 1861 C SER A 315 3309 3548 3958 -354 115 171 C ATOM 1862 O SER A 315 6.302 7.484 34.002 1.00 28.84 O ANISOU 1862 O SER A 315 3366 3609 3983 -319 196 178 O ATOM 1863 CB SER A 315 7.747 7.617 31.021 1.00 24.25 C ANISOU 1863 CB SER A 315 2908 2973 3333 -333 5 126 C ATOM 1864 OG SER A 315 8.965 7.189 30.434 1.00 23.70 O ANISOU 1864 OG SER A 315 2934 2865 3205 -342 -13 104 O ATOM 1865 N VAL A 316 4.937 7.124 32.217 1.00 25.03 N ANISOU 1865 N VAL A 316 2775 3135 3598 -380 69 183 N ATOM 1866 CA VAL A 316 3.690 7.570 32.825 1.00 23.89 C ANISOU 1866 CA VAL A 316 2509 3032 3536 -361 117 210 C ATOM 1867 C VAL A 316 3.286 6.627 33.960 1.00 29.88 C ANISOU 1867 C VAL A 316 3241 3791 4321 -407 213 233 C ATOM 1868 O VAL A 316 3.031 7.096 35.071 1.00 30.53 O ANISOU 1868 O VAL A 316 3302 3894 4405 -365 313 245 O ATOM 1869 CB VAL A 316 2.576 7.805 31.767 1.00 26.56 C ANISOU 1869 CB VAL A 316 2735 3403 3955 -376 23 225 C ATOM 1870 CG1 VAL A 316 1.212 8.064 32.422 1.00 25.44 C ANISOU 1870 CG1 VAL A 316 2439 3305 3924 -361 83 260 C ATOM 1871 CG2 VAL A 316 2.954 8.977 30.863 1.00 26.34 C ANISOU 1871 CG2 VAL A 316 2741 3376 3892 -308 -49 218 C ATOM 1872 N LEU A 317 3.279 5.308 33.706 1.00 26.84 N ANISOU 1872 N LEU A 317 2873 3375 3949 -492 191 239 N ATOM 1873 CA LEU A 317 2.939 4.310 34.724 1.00 26.53 C ANISOU 1873 CA LEU A 317 2823 3323 3936 -544 284 272 C ATOM 1874 C LEU A 317 3.869 4.381 35.943 1.00 30.63 C ANISOU 1874 C LEU A 317 3440 3834 4365 -496 373 286 C ATOM 1875 O LEU A 317 3.384 4.271 37.068 1.00 31.07 O ANISOU 1875 O LEU A 317 3469 3909 4428 -496 476 319 O ATOM 1876 CB LEU A 317 2.912 2.884 34.143 1.00 26.73 C ANISOU 1876 CB LEU A 317 2872 3293 3989 -645 243 271 C ATOM 1877 CG LEU A 317 1.738 2.536 33.202 1.00 31.36 C ANISOU 1877 CG LEU A 317 3346 3895 4674 -727 165 261 C ATOM 1878 CD1 LEU A 317 1.988 1.242 32.492 1.00 31.35 C ANISOU 1878 CD1 LEU A 317 3412 3825 4676 -826 116 236 C ATOM 1879 CD2 LEU A 317 0.440 2.433 33.943 1.00 33.28 C ANISOU 1879 CD2 LEU A 317 3446 4176 5022 -760 239 301 C ATOM 1880 N ASN A 318 5.184 4.618 35.730 1.00 26.30 N ANISOU 1880 N ASN A 318 2999 3265 3728 -456 334 262 N ATOM 1881 CA ASN A 318 6.171 4.742 36.814 1.00 25.79 C ANISOU 1881 CA ASN A 318 3023 3206 3571 -413 392 274 C ATOM 1882 C ASN A 318 5.881 5.948 37.725 1.00 31.26 C ANISOU 1882 C ASN A 318 3694 3949 4235 -355 460 263 C ATOM 1883 O ASN A 318 5.917 5.814 38.948 1.00 30.86 O ANISOU 1883 O ASN A 318 3674 3918 4133 -349 545 288 O ATOM 1884 CB ASN A 318 7.591 4.820 36.257 1.00 19.73 C ANISOU 1884 CB ASN A 318 2347 2412 2737 -386 327 249 C ATOM 1885 CG ASN A 318 8.651 4.822 37.326 1.00 30.90 C ANISOU 1885 CG ASN A 318 3839 3840 4062 -351 364 267 C ATOM 1886 OD1 ASN A 318 8.771 3.872 38.107 1.00 26.59 O ANISOU 1886 OD1 ASN A 318 3325 3282 3497 -370 408 317 O ATOM 1887 ND2 ASN A 318 9.438 5.892 37.384 1.00 25.60 N ANISOU 1887 ND2 ASN A 318 3199 3193 3334 -303 342 231 N ATOM 1888 N VAL A 319 5.571 7.111 37.123 1.00 28.06 N ANISOU 1888 N VAL A 319 3243 3558 3859 -312 428 228 N ATOM 1889 CA VAL A 319 5.213 8.334 37.843 1.00 28.34 C ANISOU 1889 CA VAL A 319 3259 3623 3886 -253 499 207 C ATOM 1890 C VAL A 319 3.913 8.136 38.635 1.00 33.72 C ANISOU 1890 C VAL A 319 3850 4331 4631 -264 604 238 C ATOM 1891 O VAL A 319 3.876 8.451 39.818 1.00 34.14 O ANISOU 1891 O VAL A 319 3937 4405 4630 -241 707 235 O ATOM 1892 CB VAL A 319 5.123 9.540 36.875 1.00 31.94 C ANISOU 1892 CB VAL A 319 3685 4071 4380 -201 440 176 C ATOM 1893 CG1 VAL A 319 4.427 10.735 37.527 1.00 32.17 C ANISOU 1893 CG1 VAL A 319 3672 4114 4438 -137 528 159 C ATOM 1894 CG2 VAL A 319 6.495 9.928 36.381 1.00 30.78 C ANISOU 1894 CG2 VAL A 319 3638 3899 4157 -187 374 144 C ATOM 1895 N LEU A 320 2.860 7.603 37.994 1.00 31.17 N ANISOU 1895 N LEU A 320 3413 4010 4418 -305 579 265 N ATOM 1896 CA LEU A 320 1.575 7.376 38.644 1.00 30.65 C ANISOU 1896 CA LEU A 320 3236 3971 4436 -323 680 298 C ATOM 1897 C LEU A 320 1.697 6.423 39.829 1.00 33.41 C ANISOU 1897 C LEU A 320 3644 4320 4730 -367 782 334 C ATOM 1898 O LEU A 320 1.066 6.644 40.863 1.00 33.75 O ANISOU 1898 O LEU A 320 3659 4390 4775 -352 912 349 O ATOM 1899 CB LEU A 320 0.531 6.874 37.627 1.00 31.60 C ANISOU 1899 CB LEU A 320 3219 4099 4690 -377 609 321 C ATOM 1900 CG LEU A 320 0.111 7.847 36.493 1.00 37.03 C ANISOU 1900 CG LEU A 320 3824 4802 5445 -329 509 306 C ATOM 1901 CD1 LEU A 320 -0.871 7.175 35.567 1.00 37.27 C ANISOU 1901 CD1 LEU A 320 3723 4851 5588 -402 423 330 C ATOM 1902 CD2 LEU A 320 -0.536 9.126 37.041 1.00 38.08 C ANISOU 1902 CD2 LEU A 320 3886 4957 5625 -233 598 304 C ATOM 1903 N LYS A 321 2.548 5.398 39.703 1.00 29.42 N ANISOU 1903 N LYS A 321 3229 3780 4168 -415 732 352 N ATOM 1904 CA LYS A 321 2.776 4.421 40.763 1.00 29.07 C ANISOU 1904 CA LYS A 321 3255 3727 4065 -453 815 402 C ATOM 1905 C LYS A 321 3.620 5.003 41.912 1.00 33.32 C ANISOU 1905 C LYS A 321 3907 4294 4459 -398 872 394 C ATOM 1906 O LYS A 321 3.206 4.971 43.067 1.00 33.44 O ANISOU 1906 O LYS A 321 3937 4336 4431 -397 993 422 O ATOM 1907 CB LYS A 321 3.445 3.169 40.176 1.00 30.51 C ANISOU 1907 CB LYS A 321 3496 3850 4247 -510 739 426 C ATOM 1908 CG LYS A 321 3.779 2.111 41.199 1.00 32.95 C ANISOU 1908 CG LYS A 321 3888 4135 4495 -539 814 493 C ATOM 1909 CD LYS A 321 4.662 1.034 40.612 1.00 36.17 C ANISOU 1909 CD LYS A 321 4371 4472 4899 -569 740 511 C ATOM 1910 CE LYS A 321 5.105 0.075 41.684 1.00 36.08 C ANISOU 1910 CE LYS A 321 4449 4435 4826 -579 813 592 C ATOM 1911 NZ LYS A 321 5.557 -1.213 41.107 1.00 42.67 N ANISOU 1911 NZ LYS A 321 5333 5176 5703 -621 774 622 N ATOM 1912 N ARG A 322 4.800 5.524 41.584 1.00 30.30 N ANISOU 1912 N ARG A 322 3605 3907 3999 -358 786 355 N ATOM 1913 CA ARG A 322 5.791 6.000 42.540 1.00 29.82 C ANISOU 1913 CA ARG A 322 3656 3876 3798 -321 805 341 C ATOM 1914 C ARG A 322 5.554 7.372 43.130 1.00 34.86 C ANISOU 1914 C ARG A 322 4300 4550 4394 -270 869 283 C ATOM 1915 O ARG A 322 5.899 7.588 44.292 1.00 34.14 O ANISOU 1915 O ARG A 322 4293 4494 4184 -260 933 279 O ATOM 1916 CB ARG A 322 7.187 5.949 41.911 1.00 27.98 C ANISOU 1916 CB ARG A 322 3491 3622 3516 -308 686 324 C ATOM 1917 CG ARG A 322 7.605 4.552 41.451 1.00 29.58 C ANISOU 1917 CG ARG A 322 3713 3777 3748 -347 637 379 C ATOM 1918 CD ARG A 322 7.851 3.614 42.606 1.00 22.35 C ANISOU 1918 CD ARG A 322 2864 2868 2760 -363 695 454 C ATOM 1919 NE ARG A 322 8.293 2.323 42.113 1.00 28.50 N ANISOU 1919 NE ARG A 322 3666 3582 3578 -390 654 506 N ATOM 1920 CZ ARG A 322 8.482 1.266 42.883 1.00 38.77 C ANISOU 1920 CZ ARG A 322 5023 4863 4844 -404 696 589 C ATOM 1921 NH1 ARG A 322 8.285 1.348 44.192 1.00 25.16 N ANISOU 1921 NH1 ARG A 322 3342 3190 3028 -398 776 634 N ATOM 1922 NH2 ARG A 322 8.875 0.118 42.354 1.00 25.52 N ANISOU 1922 NH2 ARG A 322 3368 3108 3219 -423 665 631 N ATOM 1923 N VAL A 323 5.014 8.304 42.342 1.00 32.47 N ANISOU 1923 N VAL A 323 3921 4236 4181 -237 851 237 N ATOM 1924 CA VAL A 323 4.762 9.675 42.791 1.00 32.09 C ANISOU 1924 CA VAL A 323 3879 4200 4113 -180 919 177 C ATOM 1925 C VAL A 323 3.320 9.853 43.288 1.00 38.76 C ANISOU 1925 C VAL A 323 4628 5060 5040 -165 1053 191 C ATOM 1926 O VAL A 323 3.110 10.509 44.308 1.00 39.68 O ANISOU 1926 O VAL A 323 4788 5193 5094 -135 1170 158 O ATOM 1927 CB VAL A 323 5.144 10.715 41.695 1.00 33.57 C ANISOU 1927 CB VAL A 323 4053 4356 4346 -139 828 126 C ATOM 1928 CG1 VAL A 323 4.988 12.151 42.197 1.00 32.33 C ANISOU 1928 CG1 VAL A 323 3922 4191 4170 -79 905 61 C ATOM 1929 CG2 VAL A 323 6.553 10.464 41.153 1.00 32.57 C ANISOU 1929 CG2 VAL A 323 4006 4216 4155 -158 708 118 C ATOM 1930 N PHE A 324 2.331 9.286 42.574 1.00 35.62 N ANISOU 1930 N PHE A 324 4098 4655 4780 -189 1040 234 N ATOM 1931 CA PHE A 324 0.919 9.486 42.904 1.00 35.34 C ANISOU 1931 CA PHE A 324 3937 4637 4854 -173 1161 252 C ATOM 1932 C PHE A 324 0.247 8.313 43.652 1.00 41.14 C ANISOU 1932 C PHE A 324 4637 5391 5603 -239 1261 317 C ATOM 1933 O PHE A 324 -0.960 8.363 43.889 1.00 40.40 O ANISOU 1933 O PHE A 324 4420 5314 5616 -236 1366 339 O ATOM 1934 CB PHE A 324 0.131 9.873 41.639 1.00 36.93 C ANISOU 1934 CB PHE A 324 3988 4828 5214 -150 1082 258 C ATOM 1935 CG PHE A 324 0.564 11.222 41.109 1.00 38.43 C ANISOU 1935 CG PHE A 324 4208 4993 5398 -70 1030 204 C ATOM 1936 CD1 PHE A 324 -0.028 12.385 41.566 1.00 41.83 C ANISOU 1936 CD1 PHE A 324 4608 5417 5869 12 1139 172 C ATOM 1937 CD2 PHE A 324 1.600 11.330 40.184 1.00 39.65 C ANISOU 1937 CD2 PHE A 324 4434 5124 5509 -76 886 185 C ATOM 1938 CE1 PHE A 324 0.385 13.632 41.089 1.00 42.67 C ANISOU 1938 CE1 PHE A 324 4752 5484 5976 84 1099 127 C ATOM 1939 CE2 PHE A 324 2.049 12.582 39.751 1.00 42.90 C ANISOU 1939 CE2 PHE A 324 4885 5504 5912 -9 850 141 C ATOM 1940 CZ PHE A 324 1.447 13.726 40.220 1.00 41.43 C ANISOU 1940 CZ PHE A 324 4671 5304 5769 68 955 113 C ATOM 1941 N GLY A 325 1.027 7.303 44.057 1.00 38.35 N ANISOU 1941 N GLY A 325 4390 5032 5148 -294 1237 352 N ATOM 1942 CA GLY A 325 0.523 6.173 44.842 1.00 37.36 C ANISOU 1942 CA GLY A 325 4261 4913 5019 -357 1338 423 C ATOM 1943 C GLY A 325 -0.612 5.370 44.244 1.00 40.30 C ANISOU 1943 C GLY A 325 4479 5273 5560 -422 1347 470 C ATOM 1944 O GLY A 325 -1.462 4.836 44.965 1.00 41.16 O ANISOU 1944 O GLY A 325 4535 5393 5709 -461 1482 519 O ATOM 1945 N MET A 326 -0.587 5.213 42.931 1.00 36.14 N ANISOU 1945 N MET A 326 3885 4720 5125 -444 1202 457 N ATOM 1946 CA MET A 326 -1.593 4.468 42.193 1.00 35.28 C ANISOU 1946 CA MET A 326 3629 4602 5175 -520 1174 489 C ATOM 1947 C MET A 326 -1.284 2.970 42.064 1.00 39.30 C ANISOU 1947 C MET A 326 4192 5060 5681 -619 1141 535 C ATOM 1948 O MET A 326 -0.167 2.526 42.354 1.00 38.65 O ANISOU 1948 O MET A 326 4259 4946 5479 -614 1114 545 O ATOM 1949 CB MET A 326 -1.805 5.126 40.817 1.00 37.74 C ANISOU 1949 CB MET A 326 3842 4918 5578 -495 1031 448 C ATOM 1950 CG MET A 326 -2.488 6.485 40.920 1.00 42.59 C ANISOU 1950 CG MET A 326 4361 5572 6249 -401 1085 424 C ATOM 1951 SD MET A 326 -2.841 7.317 39.362 1.00 48.05 S ANISOU 1951 SD MET A 326 4937 6273 7045 -357 921 399 S ATOM 1952 CE MET A 326 -3.981 6.210 38.646 1.00 44.59 C ANISOU 1952 CE MET A 326 4320 5854 6767 -469 864 443 C ATOM 1953 N PHE A 327 -2.314 2.199 41.646 1.00 36.83 N ANISOU 1953 N PHE A 327 3748 4734 5511 -709 1146 564 N ATOM 1954 CA PHE A 327 -2.337 0.769 41.309 1.00 36.89 C ANISOU 1954 CA PHE A 327 3771 4678 5567 -823 1113 598 C ATOM 1955 C PHE A 327 -2.083 -0.206 42.491 1.00 45.06 C ANISOU 1955 C PHE A 327 4914 5673 6535 -862 1244 671 C ATOM 1956 O PHE A 327 -1.719 -1.363 42.251 1.00 44.54 O ANISOU 1956 O PHE A 327 4916 5532 6476 -933 1212 699 O ATOM 1957 CB PHE A 327 -1.371 0.472 40.138 1.00 37.80 C ANISOU 1957 CB PHE A 327 3971 4744 5646 -831 943 554 C ATOM 1958 CG PHE A 327 -1.301 1.524 39.056 1.00 37.88 C ANISOU 1958 CG PHE A 327 3928 4793 5673 -775 814 491 C ATOM 1959 CD1 PHE A 327 -2.440 1.897 38.341 1.00 40.67 C ANISOU 1959 CD1 PHE A 327 4107 5188 6158 -800 767 479 C ATOM 1960 CD2 PHE A 327 -0.105 2.162 38.767 1.00 38.39 C ANISOU 1960 CD2 PHE A 327 4110 4853 5624 -696 739 451 C ATOM 1961 CE1 PHE A 327 -2.367 2.886 37.342 1.00 41.00 C ANISOU 1961 CE1 PHE A 327 4108 5264 6206 -740 645 436 C ATOM 1962 CE2 PHE A 327 -0.030 3.135 37.765 1.00 40.14 C ANISOU 1962 CE2 PHE A 327 4293 5102 5857 -644 630 403 C ATOM 1963 CZ PHE A 327 -1.160 3.492 37.060 1.00 38.49 C ANISOU 1963 CZ PHE A 327 3925 4931 5768 -663 582 399 C ATOM 1964 N ARG A 328 -2.372 0.215 43.736 1.00 44.87 N ANISOU 1964 N ARG A 328 4902 5693 6452 -819 1398 704 N ATOM 1965 CA ARG A 328 -2.160 -0.617 44.927 1.00 45.61 C ANISOU 1965 CA ARG A 328 5107 5761 6460 -848 1529 784 C ATOM 1966 C ARG A 328 -3.360 -1.493 45.302 1.00 54.38 C ANISOU 1966 C ARG A 328 6115 6850 7697 -953 1662 850 C ATOM 1967 O ARG A 328 -3.201 -2.394 46.134 1.00 55.55 O ANISOU 1967 O ARG A 328 6361 6956 7789 -994 1760 930 O ATOM 1968 CB ARG A 328 -1.702 0.235 46.127 1.00 44.26 C ANISOU 1968 CB ARG A 328 5041 5652 6125 -755 1627 784 C ATOM 1969 CG ARG A 328 -0.644 1.271 45.761 1.00 53.83 C ANISOU 1969 CG ARG A 328 6333 6890 7231 -661 1504 710 C ATOM 1970 CD ARG A 328 0.437 1.441 46.803 1.00 65.70 C ANISOU 1970 CD ARG A 328 8015 8416 8532 -609 1530 729 C ATOM 1971 NE ARG A 328 -0.001 2.232 47.954 1.00 69.91 N ANISOU 1971 NE ARG A 328 8570 9012 8980 -567 1679 719 N ATOM 1972 CZ ARG A 328 0.417 3.464 48.236 1.00 73.58 C ANISOU 1972 CZ ARG A 328 9082 9523 9351 -491 1671 643 C ATOM 1973 NH1 ARG A 328 -0.019 4.085 49.322 1.00 59.29 N ANISOU 1973 NH1 ARG A 328 7307 7761 7459 -461 1824 629 N ATOM 1974 NH2 ARG A 328 1.284 4.078 47.440 1.00 49.19 N ANISOU 1974 NH2 ARG A 328 6015 6427 6249 -449 1520 579 N ATOM 1975 N GLN A 329 -4.550 -1.257 44.701 1.00 53.00 N ANISOU 1975 N GLN A 329 5741 6703 7695 -997 1664 826 N ATOM 1976 CA GLN A 329 -5.755 -2.042 45.024 1.00 53.54 C ANISOU 1976 CA GLN A 329 5681 6757 7906 -1108 1792 885 C ATOM 1977 C GLN A 329 -5.759 -3.398 44.350 1.00 59.73 C ANISOU 1977 C GLN A 329 6472 7446 8777 -1239 1721 908 C ATOM 1978 O GLN A 329 -5.549 -3.477 43.140 1.00 59.77 O ANISOU 1978 O GLN A 329 6447 7426 8835 -1266 1550 848 O ATOM 1979 CB GLN A 329 -7.067 -1.285 44.702 1.00 54.69 C ANISOU 1979 CB GLN A 329 5587 6975 8219 -1107 1825 858 C ATOM 1980 CG GLN A 329 -7.210 0.082 45.370 1.00 70.45 C ANISOU 1980 CG GLN A 329 7564 9050 10154 -975 1921 831 C ATOM 1981 CD GLN A 329 -6.971 0.076 46.865 1.00 95.96 C ANISOU 1981 CD GLN A 329 10930 12291 13241 -940 2120 879 C ATOM 1982 OE1 GLN A 329 -7.607 -0.676 47.624 1.00 97.25 O ANISOU 1982 OE1 GLN A 329 11069 12439 13442 -1017 2279 953 O ATOM 1983 NE2 GLN A 329 -6.046 0.924 47.317 1.00 79.92 N ANISOU 1983 NE2 GLN A 329 9046 10286 11034 -829 2114 839 N ATOM 1984 N ALA A 330 -6.034 -4.461 45.134 1.00 57.90 N ANISOU 1984 N ALA A 330 6285 7155 8561 -1324 1861 994 N ATOM 1985 CA ALA A 330 -6.097 -5.858 44.682 1.00 57.69 C ANISOU 1985 CA ALA A 330 6281 7015 8624 -1460 1834 1025 C ATOM 1986 C ALA A 330 -7.185 -6.109 43.617 1.00 60.03 C ANISOU 1986 C ALA A 330 6368 7310 9130 -1584 1758 977 C ATOM 1987 O ALA A 330 -7.008 -6.981 42.769 1.00 59.84 O ANISOU 1987 O ALA A 330 6372 7197 9166 -1682 1655 951 O ATOM 1988 CB ALA A 330 -6.316 -6.771 45.869 1.00 58.49 C ANISOU 1988 CB ALA A 330 6458 7061 8705 -1517 2029 1139 C ATOM 1989 N SER A 331 -8.284 -5.330 43.642 1.00 55.16 N ANISOU 1989 N SER A 331 5543 6791 8622 -1577 1803 963 N ATOM 1990 CA SER A 331 -9.378 -5.430 42.670 1.00 54.46 C ANISOU 1990 CA SER A 331 5228 6730 8735 -1686 1717 924 C ATOM 1991 C SER A 331 -8.903 -5.117 41.234 1.00 59.48 C ANISOU 1991 C SER A 331 5866 7371 9363 -1673 1472 830 C ATOM 1992 O SER A 331 -9.345 -5.764 40.292 1.00 60.08 O ANISOU 1992 O SER A 331 5866 7412 9552 -1803 1360 793 O ATOM 1993 CB SER A 331 -10.547 -4.530 43.074 1.00 56.30 C ANISOU 1993 CB SER A 331 5238 7075 9079 -1648 1823 939 C ATOM 1994 OG SER A 331 -10.244 -3.149 42.975 1.00 63.25 O ANISOU 1994 OG SER A 331 6113 8040 9879 -1484 1774 894 O ATOM 1995 N ASP A 332 -7.920 -4.208 41.103 1.00 56.21 N ANISOU 1995 N ASP A 332 5564 6992 8801 -1524 1395 790 N ATOM 1996 CA ASP A 332 -7.332 -3.769 39.836 1.00 55.92 C ANISOU 1996 CA ASP A 332 5554 6966 8726 -1488 1182 709 C ATOM 1997 C ASP A 332 -6.174 -4.631 39.307 1.00 58.87 C ANISOU 1997 C ASP A 332 6131 7231 9004 -1520 1089 680 C ATOM 1998 O ASP A 332 -5.758 -4.430 38.161 1.00 57.75 O ANISOU 1998 O ASP A 332 6014 7090 8840 -1514 920 609 O ATOM 1999 CB ASP A 332 -6.873 -2.304 39.964 1.00 57.96 C ANISOU 1999 CB ASP A 332 5832 7307 8884 -1315 1161 683 C ATOM 2000 CG ASP A 332 -7.981 -1.317 40.262 1.00 69.07 C ANISOU 2000 CG ASP A 332 7035 8814 10396 -1262 1234 697 C ATOM 2001 OD1 ASP A 332 -9.106 -1.519 39.759 1.00 71.08 O ANISOU 2001 OD1 ASP A 332 7086 9103 10819 -1348 1198 701 O ATOM 2002 OD2 ASP A 332 -7.719 -0.335 40.986 1.00 74.69 O ANISOU 2002 OD2 ASP A 332 7788 9567 11023 -1133 1325 702 O ATOM 2003 N ARG A 333 -5.657 -5.574 40.133 1.00 55.80 N ANISOU 2003 N ARG A 333 5889 6751 8561 -1548 1205 739 N ATOM 2004 CA ARG A 333 -4.503 -6.461 39.870 1.00 55.22 C ANISOU 2004 CA ARG A 333 6017 6561 8403 -1559 1157 733 C ATOM 2005 C ARG A 333 -4.335 -6.879 38.392 1.00 56.53 C ANISOU 2005 C ARG A 333 6194 6675 8612 -1636 983 644 C ATOM 2006 O ARG A 333 -3.252 -6.704 37.837 1.00 55.51 O ANISOU 2006 O ARG A 333 6196 6519 8378 -1563 889 600 O ATOM 2007 CB ARG A 333 -4.547 -7.702 40.789 1.00 56.85 C ANISOU 2007 CB ARG A 333 6309 6662 8631 -1637 1310 823 C ATOM 2008 CG ARG A 333 -3.204 -8.399 40.980 1.00 73.13 C ANISOU 2008 CG ARG A 333 8593 8615 10578 -1589 1305 852 C ATOM 2009 CD ARG A 333 -3.366 -9.737 41.677 1.00 92.81 C ANISOU 2009 CD ARG A 333 11161 10982 13121 -1683 1441 944 C ATOM 2010 NE ARG A 333 -2.150 -10.554 41.592 1.00107.28 N ANISOU 2010 NE ARG A 333 13191 12691 14880 -1645 1417 968 N ATOM 2011 CZ ARG A 333 -2.031 -11.787 42.084 1.00120.13 C ANISOU 2011 CZ ARG A 333 14924 14182 16540 -1705 1521 1053 C ATOM 2012 NH1 ARG A 333 -3.053 -12.364 42.710 1.00105.66 N ANISOU 2012 NH1 ARG A 333 13024 12318 14805 -1817 1659 1122 N ATOM 2013 NH2 ARG A 333 -0.889 -12.451 41.956 1.00102.46 N ANISOU 2013 NH2 ARG A 333 12855 11832 14243 -1650 1493 1076 N ATOM 2014 N GLU A 334 -5.408 -7.413 37.773 1.00 51.52 N ANISOU 2014 N GLU A 334 5420 6028 8127 -1787 944 615 N ATOM 2015 CA GLU A 334 -5.442 -7.877 36.388 1.00 50.43 C ANISOU 2015 CA GLU A 334 5286 5846 8031 -1889 782 524 C ATOM 2016 C GLU A 334 -5.191 -6.749 35.381 1.00 51.93 C ANISOU 2016 C GLU A 334 5443 6133 8156 -1802 613 451 C ATOM 2017 O GLU A 334 -4.379 -6.931 34.477 1.00 51.07 O ANISOU 2017 O GLU A 334 5461 5973 7971 -1797 504 385 O ATOM 2018 CB GLU A 334 -6.759 -8.620 36.115 1.00 51.82 C ANISOU 2018 CB GLU A 334 5299 6007 8385 -2079 782 515 C ATOM 2019 CG GLU A 334 -6.839 -9.350 34.786 1.00 66.06 C ANISOU 2019 CG GLU A 334 7139 7732 10228 -2223 639 420 C ATOM 2020 CD GLU A 334 -7.947 -10.389 34.729 1.00 96.85 C ANISOU 2020 CD GLU A 334 10916 11582 14302 -2434 669 417 C ATOM 2021 OE1 GLU A 334 -9.029 -10.088 34.169 1.00 92.39 O ANISOU 2021 OE1 GLU A 334 10153 11113 13839 -2524 559 378 O ATOM 2022 OE2 GLU A 334 -7.734 -11.506 35.253 1.00 91.50 O ANISOU 2022 OE2 GLU A 334 10336 10766 13663 -2512 801 460 O ATOM 2023 N ALA A 335 -5.871 -5.593 35.540 1.00 47.92 N ANISOU 2023 N ALA A 335 4772 5757 7678 -1730 603 467 N ATOM 2024 CA ALA A 335 -5.733 -4.412 34.664 1.00 46.94 C ANISOU 2024 CA ALA A 335 4605 5729 7503 -1638 455 417 C ATOM 2025 C ALA A 335 -4.338 -3.798 34.760 1.00 49.54 C ANISOU 2025 C ALA A 335 5115 6043 7665 -1488 448 405 C ATOM 2026 O ALA A 335 -3.761 -3.392 33.743 1.00 49.60 O ANISOU 2026 O ALA A 335 5184 6061 7601 -1452 313 346 O ATOM 2027 CB ALA A 335 -6.784 -3.368 35.021 1.00 47.41 C ANISOU 2027 CB ALA A 335 4451 5912 7651 -1582 482 455 C ATOM 2028 N VAL A 336 -3.803 -3.741 35.991 1.00 44.84 N ANISOU 2028 N VAL A 336 4603 5429 7006 -1407 593 464 N ATOM 2029 CA VAL A 336 -2.479 -3.207 36.311 1.00 44.39 C ANISOU 2029 CA VAL A 336 4706 5363 6798 -1272 603 464 C ATOM 2030 C VAL A 336 -1.387 -4.111 35.707 1.00 48.96 C ANISOU 2030 C VAL A 336 5458 5833 7311 -1300 547 430 C ATOM 2031 O VAL A 336 -0.477 -3.601 35.050 1.00 48.60 O ANISOU 2031 O VAL A 336 5497 5793 7175 -1226 459 384 O ATOM 2032 CB VAL A 336 -2.340 -2.971 37.839 1.00 47.37 C ANISOU 2032 CB VAL A 336 5115 5759 7125 -1199 770 538 C ATOM 2033 CG1 VAL A 336 -0.900 -2.670 38.247 1.00 46.94 C ANISOU 2033 CG1 VAL A 336 5235 5685 6914 -1086 775 542 C ATOM 2034 CG2 VAL A 336 -3.278 -1.859 38.298 1.00 46.78 C ANISOU 2034 CG2 VAL A 336 4884 5790 7100 -1144 826 552 C ATOM 2035 N TYR A 337 -1.519 -5.442 35.884 1.00 46.54 N ANISOU 2035 N TYR A 337 5200 5423 7061 -1408 606 452 N ATOM 2036 CA TYR A 337 -0.605 -6.448 35.337 1.00 46.68 C ANISOU 2036 CA TYR A 337 5377 5316 7043 -1441 575 422 C ATOM 2037 C TYR A 337 -0.486 -6.298 33.819 1.00 45.50 C ANISOU 2037 C TYR A 337 5236 5168 6884 -1478 418 321 C ATOM 2038 O TYR A 337 0.625 -6.220 33.330 1.00 44.65 O ANISOU 2038 O TYR A 337 5257 5024 6685 -1411 373 285 O ATOM 2039 CB TYR A 337 -1.047 -7.884 35.716 1.00 50.04 C ANISOU 2039 CB TYR A 337 5828 5620 7562 -1570 669 461 C ATOM 2040 CG TYR A 337 -0.426 -8.965 34.850 1.00 55.61 C ANISOU 2040 CG TYR A 337 6669 6186 8274 -1639 623 403 C ATOM 2041 CD1 TYR A 337 0.853 -9.452 35.117 1.00 58.29 C ANISOU 2041 CD1 TYR A 337 7180 6430 8536 -1555 667 430 C ATOM 2042 CD2 TYR A 337 -1.107 -9.485 33.750 1.00 57.31 C ANISOU 2042 CD2 TYR A 337 6839 6364 8570 -1786 535 319 C ATOM 2043 CE1 TYR A 337 1.453 -10.398 34.288 1.00 60.21 C ANISOU 2043 CE1 TYR A 337 7551 6537 8791 -1604 638 371 C ATOM 2044 CE2 TYR A 337 -0.511 -10.419 32.905 1.00 58.60 C ANISOU 2044 CE2 TYR A 337 7143 6394 8727 -1847 499 249 C ATOM 2045 CZ TYR A 337 0.762 -10.887 33.189 1.00 70.27 C ANISOU 2045 CZ TYR A 337 8794 7767 10137 -1753 562 276 C ATOM 2046 OH TYR A 337 1.329 -11.847 32.384 1.00 76.59 O ANISOU 2046 OH TYR A 337 9736 8422 10944 -1807 548 206 O ATOM 2047 N ALA A 338 -1.625 -6.266 33.089 1.00 39.05 N ANISOU 2047 N ALA A 338 4280 4399 6158 -1586 335 279 N ATOM 2048 CA ALA A 338 -1.680 -6.139 31.631 1.00 37.42 C ANISOU 2048 CA ALA A 338 4076 4209 5932 -1639 173 186 C ATOM 2049 C ALA A 338 -1.000 -4.857 31.128 1.00 40.56 C ANISOU 2049 C ALA A 338 4499 4692 6219 -1501 89 164 C ATOM 2050 O ALA A 338 -0.131 -4.944 30.252 1.00 41.42 O ANISOU 2050 O ALA A 338 4738 4759 6242 -1483 22 104 O ATOM 2051 CB ALA A 338 -3.121 -6.206 31.151 1.00 37.69 C ANISOU 2051 CB ALA A 338 3927 4307 6088 -1772 97 166 C ATOM 2052 N ALA A 339 -1.359 -3.684 31.718 1.00 34.27 N ANISOU 2052 N ALA A 339 3589 4005 5426 -1403 110 212 N ATOM 2053 CA ALA A 339 -0.817 -2.365 31.382 1.00 33.21 C ANISOU 2053 CA ALA A 339 3468 3947 5203 -1271 48 202 C ATOM 2054 C ALA A 339 0.715 -2.302 31.538 1.00 36.83 C ANISOU 2054 C ALA A 339 4106 4349 5539 -1174 84 194 C ATOM 2055 O ALA A 339 1.395 -1.845 30.617 1.00 36.25 O ANISOU 2055 O ALA A 339 4106 4282 5387 -1132 -2 147 O ATOM 2056 CB ALA A 339 -1.485 -1.281 32.223 1.00 33.49 C ANISOU 2056 CB ALA A 339 3366 4079 5280 -1186 108 259 C ATOM 2057 N PHE A 340 1.249 -2.781 32.688 1.00 32.06 N ANISOU 2057 N PHE A 340 3570 3692 4921 -1142 210 246 N ATOM 2058 CA PHE A 340 2.683 -2.801 32.966 1.00 30.89 C ANISOU 2058 CA PHE A 340 3571 3495 4672 -1052 244 252 C ATOM 2059 C PHE A 340 3.423 -3.783 32.043 1.00 38.09 C ANISOU 2059 C PHE A 340 4609 4301 5562 -1100 205 199 C ATOM 2060 O PHE A 340 4.480 -3.442 31.523 1.00 38.23 O ANISOU 2060 O PHE A 340 4718 4309 5500 -1030 170 168 O ATOM 2061 CB PHE A 340 2.944 -3.107 34.446 1.00 31.27 C ANISOU 2061 CB PHE A 340 3647 3524 4709 -1011 376 331 C ATOM 2062 CG PHE A 340 2.947 -1.873 35.323 1.00 30.96 C ANISOU 2062 CG PHE A 340 3562 3581 4620 -910 418 363 C ATOM 2063 CD1 PHE A 340 1.760 -1.371 35.852 1.00 32.76 C ANISOU 2063 CD1 PHE A 340 3656 3880 4911 -923 464 388 C ATOM 2064 CD2 PHE A 340 4.138 -1.222 35.632 1.00 30.55 C ANISOU 2064 CD2 PHE A 340 3598 3547 4464 -804 416 365 C ATOM 2065 CE1 PHE A 340 1.761 -0.219 36.653 1.00 33.04 C ANISOU 2065 CE1 PHE A 340 3662 3992 4899 -828 516 406 C ATOM 2066 CE2 PHE A 340 4.140 -0.075 36.440 1.00 33.08 C ANISOU 2066 CE2 PHE A 340 3887 3947 4733 -722 455 380 C ATOM 2067 CZ PHE A 340 2.953 0.424 36.937 1.00 31.50 C ANISOU 2067 CZ PHE A 340 3571 3807 4590 -733 508 397 C ATOM 2068 N THR A 341 2.839 -4.970 31.799 1.00 35.83 N ANISOU 2068 N THR A 341 4327 3934 5354 -1225 216 183 N ATOM 2069 CA THR A 341 3.389 -6.003 30.918 1.00 35.43 C ANISOU 2069 CA THR A 341 4402 3764 5295 -1287 193 121 C ATOM 2070 C THR A 341 3.511 -5.472 29.465 1.00 39.65 C ANISOU 2070 C THR A 341 4959 4338 5769 -1298 64 31 C ATOM 2071 O THR A 341 4.554 -5.662 28.844 1.00 39.81 O ANISOU 2071 O THR A 341 5106 4299 5720 -1256 57 -12 O ATOM 2072 CB THR A 341 2.566 -7.294 31.088 1.00 39.94 C ANISOU 2072 CB THR A 341 4960 4241 5973 -1430 241 124 C ATOM 2073 OG1 THR A 341 2.771 -7.773 32.411 1.00 42.16 O ANISOU 2073 OG1 THR A 341 5264 4474 6282 -1394 373 219 O ATOM 2074 CG2 THR A 341 2.938 -8.379 30.122 1.00 36.29 C ANISOU 2074 CG2 THR A 341 4625 3647 5516 -1515 219 43 C ATOM 2075 N PHE A 342 2.471 -4.780 28.948 1.00 35.41 N ANISOU 2075 N PHE A 342 4298 3902 5255 -1345 -35 10 N ATOM 2076 CA PHE A 342 2.491 -4.214 27.599 1.00 34.82 C ANISOU 2076 CA PHE A 342 4241 3877 5111 -1354 -167 -60 C ATOM 2077 C PHE A 342 3.535 -3.095 27.516 1.00 37.53 C ANISOU 2077 C PHE A 342 4637 4269 5354 -1207 -170 -46 C ATOM 2078 O PHE A 342 4.251 -3.002 26.517 1.00 37.97 O ANISOU 2078 O PHE A 342 4797 4306 5324 -1193 -220 -102 O ATOM 2079 CB PHE A 342 1.088 -3.723 27.177 1.00 36.67 C ANISOU 2079 CB PHE A 342 4311 4218 5404 -1428 -277 -63 C ATOM 2080 CG PHE A 342 1.080 -2.968 25.865 1.00 39.08 C ANISOU 2080 CG PHE A 342 4629 4595 5624 -1419 -423 -112 C ATOM 2081 CD1 PHE A 342 1.267 -3.635 24.660 1.00 42.11 C ANISOU 2081 CD1 PHE A 342 5126 4930 5945 -1514 -503 -201 C ATOM 2082 CD2 PHE A 342 0.944 -1.578 25.839 1.00 42.42 C ANISOU 2082 CD2 PHE A 342 4970 5127 6021 -1312 -470 -67 C ATOM 2083 CE1 PHE A 342 1.304 -2.933 23.450 1.00 43.04 C ANISOU 2083 CE1 PHE A 342 5274 5118 5963 -1504 -635 -239 C ATOM 2084 CE2 PHE A 342 0.967 -0.879 24.625 1.00 45.26 C ANISOU 2084 CE2 PHE A 342 5354 5548 6295 -1298 -602 -97 C ATOM 2085 CZ PHE A 342 1.146 -1.562 23.440 1.00 42.94 C ANISOU 2085 CZ PHE A 342 5173 5216 5928 -1395 -686 -180 C ATOM 2086 N SER A 343 3.632 -2.264 28.580 1.00 32.75 N ANISOU 2086 N SER A 343 3966 3722 4757 -1105 -107 24 N ATOM 2087 CA SER A 343 4.581 -1.144 28.663 1.00 31.37 C ANISOU 2087 CA SER A 343 3830 3590 4499 -975 -102 39 C ATOM 2088 C SER A 343 6.041 -1.617 28.665 1.00 34.17 C ANISOU 2088 C SER A 343 4330 3861 4790 -924 -45 25 C ATOM 2089 O SER A 343 6.909 -0.911 28.149 1.00 32.89 O ANISOU 2089 O SER A 343 4227 3717 4553 -854 -71 4 O ATOM 2090 CB SER A 343 4.268 -0.239 29.854 1.00 32.81 C ANISOU 2090 CB SER A 343 3916 3843 4706 -896 -42 104 C ATOM 2091 OG SER A 343 4.957 -0.614 31.037 1.00 35.09 O ANISOU 2091 OG SER A 343 4256 4092 4984 -851 67 149 O ATOM 2092 N HIS A 344 6.307 -2.814 29.245 1.00 30.29 N ANISOU 2092 N HIS A 344 3894 3277 4338 -957 35 42 N ATOM 2093 CA HIS A 344 7.640 -3.429 29.276 1.00 29.23 C ANISOU 2093 CA HIS A 344 3886 3054 4168 -905 95 39 C ATOM 2094 C HIS A 344 7.997 -3.962 27.908 1.00 35.21 C ANISOU 2094 C HIS A 344 4743 3743 4893 -955 52 -47 C ATOM 2095 O HIS A 344 9.125 -3.778 27.486 1.00 36.30 O ANISOU 2095 O HIS A 344 4962 3859 4972 -886 67 -67 O ATOM 2096 CB HIS A 344 7.707 -4.553 30.314 1.00 29.15 C ANISOU 2096 CB HIS A 344 3901 2958 4217 -921 193 98 C ATOM 2097 CG HIS A 344 7.525 -4.079 31.724 1.00 31.84 C ANISOU 2097 CG HIS A 344 4170 3363 4564 -865 249 184 C ATOM 2098 ND1 HIS A 344 7.179 -4.952 32.736 1.00 33.15 N ANISOU 2098 ND1 HIS A 344 4333 3478 4784 -898 332 251 N ATOM 2099 CD2 HIS A 344 7.608 -2.831 32.238 1.00 32.83 C ANISOU 2099 CD2 HIS A 344 4237 3595 4643 -788 237 208 C ATOM 2100 CE1 HIS A 344 7.099 -4.216 33.828 1.00 32.20 C ANISOU 2100 CE1 HIS A 344 4158 3442 4635 -837 368 312 C ATOM 2101 NE2 HIS A 344 7.342 -2.936 33.573 1.00 32.36 N ANISOU 2101 NE2 HIS A 344 4145 3555 4597 -771 313 283 N ATOM 2102 N TRP A 345 7.049 -4.629 27.214 1.00 33.25 N ANISOU 2102 N TRP A 345 4491 3462 4681 -1081 4 -101 N ATOM 2103 CA TRP A 345 7.253 -5.149 25.866 1.00 33.36 C ANISOU 2103 CA TRP A 345 4613 3415 4648 -1147 -41 -197 C ATOM 2104 C TRP A 345 7.552 -4.028 24.883 1.00 38.05 C ANISOU 2104 C TRP A 345 5221 4095 5141 -1102 -125 -232 C ATOM 2105 O TRP A 345 8.428 -4.189 24.026 1.00 37.86 O ANISOU 2105 O TRP A 345 5318 4021 5046 -1083 -113 -289 O ATOM 2106 CB TRP A 345 6.053 -5.991 25.389 1.00 32.01 C ANISOU 2106 CB TRP A 345 4421 3210 4533 -1308 -94 -251 C ATOM 2107 CG TRP A 345 6.182 -6.449 23.961 1.00 32.95 C ANISOU 2107 CG TRP A 345 4659 3279 4583 -1389 -155 -363 C ATOM 2108 CD1 TRP A 345 6.915 -7.502 23.492 1.00 35.58 C ANISOU 2108 CD1 TRP A 345 5146 3469 4903 -1417 -86 -430 C ATOM 2109 CD2 TRP A 345 5.637 -5.792 22.807 1.00 32.93 C ANISOU 2109 CD2 TRP A 345 4641 3370 4501 -1443 -293 -419 C ATOM 2110 NE1 TRP A 345 6.798 -7.590 22.124 1.00 35.03 N ANISOU 2110 NE1 TRP A 345 5166 3398 4745 -1498 -168 -537 N ATOM 2111 CE2 TRP A 345 6.030 -6.543 21.673 1.00 36.86 C ANISOU 2111 CE2 TRP A 345 5298 3781 4928 -1516 -303 -528 C ATOM 2112 CE3 TRP A 345 4.845 -4.639 22.620 1.00 33.75 C ANISOU 2112 CE3 TRP A 345 4617 3622 4586 -1430 -408 -384 C ATOM 2113 CZ2 TRP A 345 5.653 -6.182 20.368 1.00 35.86 C ANISOU 2113 CZ2 TRP A 345 5211 3721 4694 -1586 -433 -602 C ATOM 2114 CZ3 TRP A 345 4.476 -4.285 21.331 1.00 35.00 C ANISOU 2114 CZ3 TRP A 345 4804 3843 4651 -1490 -541 -445 C ATOM 2115 CH2 TRP A 345 4.873 -5.053 20.224 1.00 35.68 C ANISOU 2115 CH2 TRP A 345 5056 3851 4651 -1571 -558 -553 C ATOM 2116 N LEU A 346 6.826 -2.907 25.010 1.00 34.95 N ANISOU 2116 N LEU A 346 4709 3824 4745 -1080 -199 -195 N ATOM 2117 CA LEU A 346 6.932 -1.752 24.136 1.00 34.92 C ANISOU 2117 CA LEU A 346 4706 3906 4655 -1037 -284 -209 C ATOM 2118 C LEU A 346 8.340 -1.175 24.125 1.00 37.35 C ANISOU 2118 C LEU A 346 5095 4201 4897 -922 -222 -199 C ATOM 2119 O LEU A 346 8.822 -0.826 23.052 1.00 38.00 O ANISOU 2119 O LEU A 346 5259 4288 4890 -913 -258 -242 O ATOM 2120 CB LEU A 346 5.888 -0.722 24.553 1.00 35.95 C ANISOU 2120 CB LEU A 346 4681 4151 4828 -1019 -347 -152 C ATOM 2121 CG LEU A 346 5.250 0.133 23.475 1.00 41.83 C ANISOU 2121 CG LEU A 346 5390 4984 5518 -1034 -479 -165 C ATOM 2122 CD1 LEU A 346 4.625 -0.710 22.384 1.00 42.18 C ANISOU 2122 CD1 LEU A 346 5477 5014 5537 -1169 -576 -237 C ATOM 2123 CD2 LEU A 346 4.186 1.024 24.085 1.00 44.82 C ANISOU 2123 CD2 LEU A 346 5599 5460 5973 -1002 -517 -97 C ATOM 2124 N VAL A 347 9.026 -1.143 25.297 1.00 31.28 N ANISOU 2124 N VAL A 347 4305 3412 4165 -841 -129 -143 N ATOM 2125 CA VAL A 347 10.407 -0.670 25.440 1.00 29.75 C ANISOU 2125 CA VAL A 347 4168 3209 3928 -738 -70 -128 C ATOM 2126 C VAL A 347 11.305 -1.518 24.544 1.00 34.76 C ANISOU 2126 C VAL A 347 4935 3749 4525 -752 -29 -189 C ATOM 2127 O VAL A 347 12.071 -0.974 23.736 1.00 36.50 O ANISOU 2127 O VAL A 347 5217 3978 4674 -713 -30 -218 O ATOM 2128 CB VAL A 347 10.880 -0.668 26.924 1.00 32.30 C ANISOU 2128 CB VAL A 347 4443 3532 4297 -668 8 -57 C ATOM 2129 CG1 VAL A 347 12.404 -0.534 27.037 1.00 31.91 C ANISOU 2129 CG1 VAL A 347 4452 3455 4218 -580 68 -47 C ATOM 2130 CG2 VAL A 347 10.196 0.431 27.714 1.00 31.55 C ANISOU 2130 CG2 VAL A 347 4239 3535 4215 -636 -17 -9 C ATOM 2131 N TYR A 348 11.147 -2.854 24.643 1.00 30.15 N ANISOU 2131 N TYR A 348 4398 3067 3992 -812 15 -213 N ATOM 2132 CA TYR A 348 11.923 -3.818 23.864 1.00 29.23 C ANISOU 2132 CA TYR A 348 4413 2837 3857 -827 74 -277 C ATOM 2133 C TYR A 348 11.593 -3.760 22.386 1.00 33.27 C ANISOU 2133 C TYR A 348 5007 3353 4280 -903 6 -370 C ATOM 2134 O TYR A 348 12.512 -3.866 21.578 1.00 33.15 O ANISOU 2134 O TYR A 348 5100 3291 4204 -874 54 -419 O ATOM 2135 CB TYR A 348 11.805 -5.234 24.443 1.00 28.92 C ANISOU 2135 CB TYR A 348 4406 2677 3906 -868 147 -271 C ATOM 2136 CG TYR A 348 12.378 -5.312 25.838 1.00 28.74 C ANISOU 2136 CG TYR A 348 4327 2646 3945 -775 219 -172 C ATOM 2137 CD1 TYR A 348 13.690 -4.927 26.096 1.00 30.04 C ANISOU 2137 CD1 TYR A 348 4504 2818 4093 -658 271 -135 C ATOM 2138 CD2 TYR A 348 11.587 -5.691 26.916 1.00 29.55 C ANISOU 2138 CD2 TYR A 348 4359 2750 4118 -808 230 -108 C ATOM 2139 CE1 TYR A 348 14.206 -4.936 27.385 1.00 30.13 C ANISOU 2139 CE1 TYR A 348 4461 2842 4147 -577 316 -41 C ATOM 2140 CE2 TYR A 348 12.098 -5.719 28.212 1.00 30.49 C ANISOU 2140 CE2 TYR A 348 4438 2875 4270 -725 288 -12 C ATOM 2141 CZ TYR A 348 13.411 -5.343 28.440 1.00 36.52 C ANISOU 2141 CZ TYR A 348 5217 3652 5008 -610 323 21 C ATOM 2142 OH TYR A 348 13.935 -5.361 29.704 1.00 38.40 O ANISOU 2142 OH TYR A 348 5417 3907 5266 -532 362 117 O ATOM 2143 N ALA A 349 10.304 -3.519 22.038 1.00 29.56 N ANISOU 2143 N ALA A 349 4481 2952 3799 -996 -106 -387 N ATOM 2144 CA ALA A 349 9.819 -3.352 20.666 1.00 28.85 C ANISOU 2144 CA ALA A 349 4456 2895 3611 -1078 -205 -463 C ATOM 2145 C ALA A 349 10.539 -2.181 19.995 1.00 33.54 C ANISOU 2145 C ALA A 349 5087 3556 4100 -996 -221 -454 C ATOM 2146 O ALA A 349 10.772 -2.224 18.789 1.00 33.90 O ANISOU 2146 O ALA A 349 5250 3592 4040 -1033 -244 -522 O ATOM 2147 CB ALA A 349 8.316 -3.111 20.656 1.00 28.83 C ANISOU 2147 CB ALA A 349 4340 2979 3637 -1169 -333 -451 C ATOM 2148 N ASN A 350 10.928 -1.157 20.776 1.00 30.67 N ANISOU 2148 N ASN A 350 4635 3255 3763 -891 -199 -372 N ATOM 2149 CA ASN A 350 11.651 -0.003 20.254 1.00 31.10 C ANISOU 2149 CA ASN A 350 4717 3362 3736 -815 -200 -354 C ATOM 2150 C ASN A 350 13.030 -0.382 19.688 1.00 33.77 C ANISOU 2150 C ASN A 350 5184 3622 4026 -774 -93 -399 C ATOM 2151 O ASN A 350 13.422 0.171 18.661 1.00 31.82 O ANISOU 2151 O ASN A 350 5017 3396 3675 -768 -103 -425 O ATOM 2152 CB ASN A 350 11.736 1.127 21.277 1.00 33.83 C ANISOU 2152 CB ASN A 350 4944 3777 4131 -725 -194 -268 C ATOM 2153 CG ASN A 350 12.336 2.382 20.698 1.00 42.38 C ANISOU 2153 CG ASN A 350 6053 4909 5139 -662 -203 -249 C ATOM 2154 OD1 ASN A 350 13.512 2.677 20.886 1.00 36.92 O ANISOU 2154 OD1 ASN A 350 5390 4195 4444 -594 -119 -237 O ATOM 2155 ND2 ASN A 350 11.549 3.123 19.955 1.00 33.85 N ANISOU 2155 ND2 ASN A 350 4963 3897 4001 -686 -306 -240 N ATOM 2156 N SER A 351 13.737 -1.348 20.328 1.00 31.11 N ANISOU 2156 N SER A 351 4865 3191 3763 -746 14 -402 N ATOM 2157 CA SER A 351 15.048 -1.854 19.870 1.00 31.04 C ANISOU 2157 CA SER A 351 4962 3096 3737 -698 133 -440 C ATOM 2158 C SER A 351 14.907 -2.535 18.497 1.00 36.88 C ANISOU 2158 C SER A 351 5854 3777 4383 -781 133 -546 C ATOM 2159 O SER A 351 15.810 -2.430 17.663 1.00 36.76 O ANISOU 2159 O SER A 351 5938 3732 4297 -749 205 -586 O ATOM 2160 CB SER A 351 15.621 -2.853 20.869 1.00 33.33 C ANISOU 2160 CB SER A 351 5231 3294 4139 -653 231 -411 C ATOM 2161 OG SER A 351 15.834 -2.228 22.123 1.00 42.83 O ANISOU 2161 OG SER A 351 6310 4559 5406 -579 229 -318 O ATOM 2162 N ALA A 352 13.756 -3.205 18.268 1.00 32.36 N ANISOU 2162 N ALA A 352 5297 3189 3808 -894 54 -594 N ATOM 2163 CA ALA A 352 13.423 -3.856 17.015 1.00 32.24 C ANISOU 2163 CA ALA A 352 5427 3128 3694 -999 28 -704 C ATOM 2164 C ALA A 352 12.983 -2.825 15.952 1.00 38.08 C ANISOU 2164 C ALA A 352 6198 3981 4288 -1032 -88 -716 C ATOM 2165 O ALA A 352 13.252 -3.020 14.767 1.00 38.63 O ANISOU 2165 O ALA A 352 6418 4027 4232 -1075 -76 -797 O ATOM 2166 CB ALA A 352 12.315 -4.870 17.238 1.00 32.67 C ANISOU 2166 CB ALA A 352 5468 3135 3809 -1119 -28 -745 C ATOM 2167 N ALA A 353 12.298 -1.744 16.369 1.00 34.03 N ANISOU 2167 N ALA A 353 5551 3588 3790 -1009 -195 -632 N ATOM 2168 CA ALA A 353 11.761 -0.707 15.489 1.00 33.42 C ANISOU 2168 CA ALA A 353 5482 3621 3593 -1029 -319 -616 C ATOM 2169 C ALA A 353 12.816 0.120 14.728 1.00 37.45 C ANISOU 2169 C ALA A 353 6087 4147 3994 -955 -257 -606 C ATOM 2170 O ALA A 353 12.663 0.321 13.520 1.00 37.97 O ANISOU 2170 O ALA A 353 6268 4246 3912 -1005 -314 -647 O ATOM 2171 CB ALA A 353 10.834 0.211 16.275 1.00 33.98 C ANISOU 2171 CB ALA A 353 5376 3795 3739 -1002 -421 -520 C ATOM 2172 N ASN A 354 13.859 0.613 15.428 1.00 32.66 N ANISOU 2172 N ASN A 354 5434 3523 3455 -845 -145 -550 N ATOM 2173 CA ASN A 354 14.907 1.477 14.864 1.00 32.00 C ANISOU 2173 CA ASN A 354 5413 3452 3295 -774 -71 -529 C ATOM 2174 C ASN A 354 15.565 0.912 13.595 1.00 35.73 C ANISOU 2174 C ASN A 354 6073 3865 3639 -809 7 -619 C ATOM 2175 O ASN A 354 15.525 1.631 12.599 1.00 36.37 O ANISOU 2175 O ASN A 354 6236 4001 3582 -822 -34 -615 O ATOM 2176 CB ASN A 354 15.932 1.872 15.914 1.00 28.84 C ANISOU 2176 CB ASN A 354 4919 3032 3008 -669 37 -467 C ATOM 2177 CG ASN A 354 15.305 2.645 17.027 1.00 39.77 C ANISOU 2177 CG ASN A 354 6144 4483 4484 -635 -36 -384 C ATOM 2178 OD1 ASN A 354 14.396 3.458 16.816 1.00 34.26 O ANISOU 2178 OD1 ASN A 354 5405 3863 3750 -652 -148 -347 O ATOM 2179 ND2 ASN A 354 15.748 2.385 18.236 1.00 35.36 N ANISOU 2179 ND2 ASN A 354 5496 3896 4043 -585 27 -352 N ATOM 2180 N PRO A 355 16.091 -0.343 13.535 1.00 32.23 N ANISOU 2180 N PRO A 355 5712 3310 3225 -828 117 -700 N ATOM 2181 CA PRO A 355 16.628 -0.850 12.253 1.00 32.27 C ANISOU 2181 CA PRO A 355 5910 3257 3093 -865 199 -798 C ATOM 2182 C PRO A 355 15.574 -0.898 11.130 1.00 37.18 C ANISOU 2182 C PRO A 355 6646 3934 3549 -985 58 -860 C ATOM 2183 O PRO A 355 15.920 -0.613 9.987 1.00 38.86 O ANISOU 2183 O PRO A 355 7005 4162 3599 -1002 83 -898 O ATOM 2184 CB PRO A 355 17.139 -2.247 12.606 1.00 33.68 C ANISOU 2184 CB PRO A 355 6132 3297 3368 -863 328 -868 C ATOM 2185 CG PRO A 355 17.349 -2.210 14.075 1.00 38.46 C ANISOU 2185 CG PRO A 355 6563 3897 4155 -784 349 -779 C ATOM 2186 CD PRO A 355 16.235 -1.363 14.589 1.00 33.94 C ANISOU 2186 CD PRO A 355 5862 3440 3594 -811 183 -706 C ATOM 2187 N ILE A 356 14.291 -1.199 11.451 1.00 31.60 N ANISOU 2187 N ILE A 356 5865 3264 2877 -1070 -94 -863 N ATOM 2188 CA ILE A 356 13.182 -1.214 10.479 1.00 31.68 C ANISOU 2188 CA ILE A 356 5948 3345 2743 -1191 -262 -911 C ATOM 2189 C ILE A 356 12.936 0.223 9.936 1.00 35.73 C ANISOU 2189 C ILE A 356 6440 3989 3146 -1154 -368 -820 C ATOM 2190 O ILE A 356 12.698 0.387 8.738 1.00 35.33 O ANISOU 2190 O ILE A 356 6527 3987 2910 -1216 -440 -858 O ATOM 2191 CB ILE A 356 11.882 -1.886 11.042 1.00 34.86 C ANISOU 2191 CB ILE A 356 6244 3758 3242 -1291 -393 -928 C ATOM 2192 CG1 ILE A 356 12.143 -3.339 11.512 1.00 34.93 C ANISOU 2192 CG1 ILE A 356 6297 3618 3356 -1332 -277 -1016 C ATOM 2193 CG2 ILE A 356 10.717 -1.845 10.019 1.00 34.56 C ANISOU 2193 CG2 ILE A 356 6260 3813 3059 -1422 -589 -971 C ATOM 2194 CD1 ILE A 356 10.993 -3.951 12.411 1.00 37.66 C ANISOU 2194 CD1 ILE A 356 6502 3960 3847 -1410 -368 -1004 C ATOM 2195 N ILE A 357 13.035 1.245 10.812 1.00 31.56 N ANISOU 2195 N ILE A 357 5754 3512 2726 -1052 -370 -701 N ATOM 2196 CA ILE A 357 12.912 2.662 10.444 1.00 30.73 C ANISOU 2196 CA ILE A 357 5623 3506 2547 -998 -444 -601 C ATOM 2197 C ILE A 357 14.059 3.043 9.467 1.00 36.04 C ANISOU 2197 C ILE A 357 6463 4154 3078 -962 -323 -617 C ATOM 2198 O ILE A 357 13.777 3.635 8.422 1.00 36.78 O ANISOU 2198 O ILE A 357 6655 4314 3004 -988 -404 -597 O ATOM 2199 CB ILE A 357 12.859 3.606 11.688 1.00 32.82 C ANISOU 2199 CB ILE A 357 5693 3804 2974 -899 -444 -487 C ATOM 2200 CG1 ILE A 357 11.590 3.342 12.548 1.00 32.16 C ANISOU 2200 CG1 ILE A 357 5447 3760 3012 -937 -567 -464 C ATOM 2201 CG2 ILE A 357 12.965 5.096 11.268 1.00 32.03 C ANISOU 2201 CG2 ILE A 357 5591 3775 2803 -831 -482 -387 C ATOM 2202 CD1 ILE A 357 11.616 3.955 13.972 1.00 36.52 C ANISOU 2202 CD1 ILE A 357 5822 4320 3735 -847 -529 -379 C ATOM 2203 N TYR A 358 15.321 2.655 9.779 1.00 31.53 N ANISOU 2203 N TYR A 358 5923 3488 2568 -904 -130 -649 N ATOM 2204 CA TYR A 358 16.476 2.947 8.918 1.00 31.58 C ANISOU 2204 CA TYR A 358 6073 3464 2462 -868 14 -665 C ATOM 2205 C TYR A 358 16.304 2.309 7.547 1.00 39.65 C ANISOU 2205 C TYR A 358 7311 4477 3280 -963 3 -769 C ATOM 2206 O TYR A 358 16.603 2.930 6.526 1.00 40.79 O ANISOU 2206 O TYR A 358 7586 4658 3256 -965 21 -755 O ATOM 2207 CB TYR A 358 17.831 2.517 9.546 1.00 31.63 C ANISOU 2207 CB TYR A 358 6049 3372 2598 -790 222 -683 C ATOM 2208 CG TYR A 358 18.068 2.905 10.998 1.00 30.98 C ANISOU 2208 CG TYR A 358 5763 3291 2715 -709 236 -601 C ATOM 2209 CD1 TYR A 358 17.511 4.063 11.534 1.00 31.03 C ANISOU 2209 CD1 TYR A 358 5646 3381 2762 -678 127 -500 C ATOM 2210 CD2 TYR A 358 18.878 2.128 11.823 1.00 31.46 C ANISOU 2210 CD2 TYR A 358 5764 3269 2921 -659 362 -622 C ATOM 2211 CE1 TYR A 358 17.695 4.399 12.872 1.00 30.22 C ANISOU 2211 CE1 TYR A 358 5374 3280 2826 -613 140 -437 C ATOM 2212 CE2 TYR A 358 19.080 2.462 13.162 1.00 31.55 C ANISOU 2212 CE2 TYR A 358 5601 3292 3095 -593 363 -547 C ATOM 2213 CZ TYR A 358 18.488 3.601 13.680 1.00 36.07 C ANISOU 2213 CZ TYR A 358 6063 3950 3691 -575 254 -461 C ATOM 2214 OH TYR A 358 18.677 3.937 14.996 1.00 35.45 O ANISOU 2214 OH TYR A 358 5829 3884 3756 -517 257 -399 O ATOM 2215 N ASN A 359 15.786 1.083 7.521 1.00 37.90 N ANISOU 2215 N ASN A 359 7132 4203 3064 -1050 -30 -874 N ATOM 2216 CA ASN A 359 15.525 0.358 6.288 1.00 38.22 C ANISOU 2216 CA ASN A 359 7383 4228 2911 -1160 -53 -994 C ATOM 2217 C ASN A 359 14.574 1.117 5.362 1.00 44.00 C ANISOU 2217 C ASN A 359 8174 5091 3452 -1225 -251 -955 C ATOM 2218 O ASN A 359 14.835 1.186 4.174 1.00 44.72 O ANISOU 2218 O ASN A 359 8461 5197 3332 -1266 -228 -1003 O ATOM 2219 CB ASN A 359 14.957 -1.021 6.599 1.00 35.98 C ANISOU 2219 CB ASN A 359 7106 3867 2699 -1252 -79 -1105 C ATOM 2220 CG ASN A 359 14.792 -1.848 5.365 1.00 49.87 C ANISOU 2220 CG ASN A 359 9096 5593 4260 -1375 -87 -1250 C ATOM 2221 OD1 ASN A 359 15.762 -2.360 4.801 1.00 45.29 O ANISOU 2221 OD1 ASN A 359 8681 4917 3611 -1361 95 -1338 O ATOM 2222 ND2 ASN A 359 13.563 -1.971 4.905 1.00 39.86 N ANISOU 2222 ND2 ASN A 359 7844 4407 2893 -1498 -299 -1279 N ATOM 2223 N PHE A 360 13.487 1.685 5.898 1.00 41.67 N ANISOU 2223 N PHE A 360 7713 4892 3228 -1231 -440 -865 N ATOM 2224 CA PHE A 360 12.502 2.387 5.081 1.00 41.80 C ANISOU 2224 CA PHE A 360 7758 5038 3085 -1284 -648 -812 C ATOM 2225 C PHE A 360 12.820 3.855 4.819 1.00 45.63 C ANISOU 2225 C PHE A 360 8232 5593 3511 -1185 -652 -673 C ATOM 2226 O PHE A 360 12.388 4.372 3.793 1.00 45.67 O ANISOU 2226 O PHE A 360 8345 5684 3322 -1222 -770 -639 O ATOM 2227 CB PHE A 360 11.085 2.230 5.672 1.00 43.50 C ANISOU 2227 CB PHE A 360 7798 5323 3407 -1344 -856 -785 C ATOM 2228 CG PHE A 360 10.545 0.825 5.521 1.00 45.42 C ANISOU 2228 CG PHE A 360 8097 5516 3645 -1483 -897 -929 C ATOM 2229 CD1 PHE A 360 10.201 0.322 4.266 1.00 48.51 C ANISOU 2229 CD1 PHE A 360 8681 5935 3815 -1612 -986 -1033 C ATOM 2230 CD2 PHE A 360 10.401 -0.005 6.627 1.00 47.38 C ANISOU 2230 CD2 PHE A 360 8218 5683 4103 -1492 -842 -963 C ATOM 2231 CE1 PHE A 360 9.731 -0.986 4.121 1.00 49.13 C ANISOU 2231 CE1 PHE A 360 8822 5952 3892 -1752 -1017 -1178 C ATOM 2232 CE2 PHE A 360 9.927 -1.313 6.480 1.00 50.49 C ANISOU 2232 CE2 PHE A 360 8673 6011 4501 -1627 -867 -1096 C ATOM 2233 CZ PHE A 360 9.596 -1.794 5.227 1.00 48.26 C ANISOU 2233 CZ PHE A 360 8580 5750 4007 -1759 -954 -1207 C ATOM 2234 N LEU A 361 13.564 4.523 5.712 1.00 41.87 N ANISOU 2234 N LEU A 361 7635 5080 3195 -1068 -529 -590 N ATOM 2235 CA LEU A 361 13.836 5.953 5.555 1.00 41.47 C ANISOU 2235 CA LEU A 361 7564 5080 3112 -979 -527 -456 C ATOM 2236 C LEU A 361 15.308 6.320 5.224 1.00 46.12 C ANISOU 2236 C LEU A 361 8264 5603 3657 -916 -306 -453 C ATOM 2237 O LEU A 361 15.632 7.512 5.123 1.00 46.31 O ANISOU 2237 O LEU A 361 8277 5653 3666 -847 -283 -342 O ATOM 2238 CB LEU A 361 13.330 6.723 6.788 1.00 41.23 C ANISOU 2238 CB LEU A 361 7299 5076 3288 -901 -590 -349 C ATOM 2239 CG LEU A 361 11.815 6.668 7.022 1.00 45.59 C ANISOU 2239 CG LEU A 361 7725 5713 3884 -947 -810 -319 C ATOM 2240 CD1 LEU A 361 11.471 7.161 8.386 1.00 45.55 C ANISOU 2240 CD1 LEU A 361 7498 5708 4101 -871 -817 -243 C ATOM 2241 CD2 LEU A 361 11.059 7.473 5.988 1.00 48.40 C ANISOU 2241 CD2 LEU A 361 8142 6175 4073 -963 -983 -238 C ATOM 2242 N SER A 362 16.169 5.312 5.000 1.00 41.57 N ANISOU 2242 N SER A 362 7796 4937 3060 -942 -142 -571 N ATOM 2243 CA SER A 362 17.557 5.506 4.606 1.00 40.10 C ANISOU 2243 CA SER A 362 7713 4689 2835 -890 80 -580 C ATOM 2244 C SER A 362 17.904 4.526 3.516 1.00 46.26 C ANISOU 2244 C SER A 362 8717 5423 3436 -964 170 -713 C ATOM 2245 O SER A 362 17.939 3.316 3.754 1.00 48.07 O ANISOU 2245 O SER A 362 8962 5578 3723 -1004 218 -828 O ATOM 2246 CB SER A 362 18.499 5.338 5.791 1.00 41.31 C ANISOU 2246 CB SER A 362 7715 4763 3220 -808 237 -573 C ATOM 2247 OG SER A 362 19.846 5.255 5.355 1.00 46.62 O ANISOU 2247 OG SER A 362 8480 5367 3865 -771 461 -605 O ATOM 2248 N GLY A 363 18.144 5.049 2.318 1.00 42.59 N ANISOU 2248 N GLY A 363 8435 4996 2749 -983 198 -696 N ATOM 2249 CA GLY A 363 18.544 4.273 1.150 1.00 41.62 C ANISOU 2249 CA GLY A 363 8559 4835 2418 -1052 302 -821 C ATOM 2250 C GLY A 363 19.885 3.599 1.343 1.00 45.67 C ANISOU 2250 C GLY A 363 9099 5225 3030 -1001 577 -900 C ATOM 2251 O GLY A 363 20.118 2.521 0.799 1.00 46.04 O ANISOU 2251 O GLY A 363 9299 5201 2993 -1054 674 -1041 O ATOM 2252 N LYS A 364 20.763 4.215 2.152 1.00 43.35 N ANISOU 2252 N LYS A 364 8646 4901 2925 -897 701 -812 N ATOM 2253 CA LYS A 364 22.106 3.721 2.481 1.00 43.67 C ANISOU 2253 CA LYS A 364 8658 4836 3100 -828 956 -857 C ATOM 2254 C LYS A 364 22.034 2.470 3.340 1.00 45.06 C ANISOU 2254 C LYS A 364 8743 4927 3452 -826 973 -947 C ATOM 2255 O LYS A 364 22.672 1.482 3.004 1.00 45.10 O ANISOU 2255 O LYS A 364 8851 4834 3449 -826 1142 -1057 O ATOM 2256 CB LYS A 364 22.958 4.822 3.154 1.00 47.30 C ANISOU 2256 CB LYS A 364 8952 5305 3714 -732 1044 -729 C ATOM 2257 CG LYS A 364 23.375 5.943 2.215 1.00 70.48 C ANISOU 2257 CG LYS A 364 12005 8286 6489 -727 1111 -650 C ATOM 2258 CD LYS A 364 24.701 6.553 2.631 1.00 87.95 C ANISOU 2258 CD LYS A 364 14102 10458 8855 -645 1308 -584 C ATOM 2259 CE LYS A 364 25.017 7.812 1.862 1.00103.72 C ANISOU 2259 CE LYS A 364 16192 12496 10719 -644 1366 -485 C ATOM 2260 NZ LYS A 364 26.284 8.438 2.322 1.00114.89 N ANISOU 2260 NZ LYS A 364 17475 13873 12306 -579 1549 -421 N ATOM 2261 N PHE A 365 21.223 2.494 4.422 1.00 40.14 N ANISOU 2261 N PHE A 365 7937 4334 2980 -823 806 -899 N ATOM 2262 CA PHE A 365 21.008 1.329 5.293 1.00 38.19 C ANISOU 2262 CA PHE A 365 7604 4010 2896 -828 802 -967 C ATOM 2263 C PHE A 365 20.223 0.248 4.543 1.00 42.05 C ANISOU 2263 C PHE A 365 8267 4467 3244 -944 735 -1103 C ATOM 2264 O PHE A 365 20.603 -0.921 4.605 1.00 42.05 O ANISOU 2264 O PHE A 365 8323 4351 3303 -950 857 -1209 O ATOM 2265 CB PHE A 365 20.310 1.718 6.619 1.00 38.45 C ANISOU 2265 CB PHE A 365 7407 4092 3110 -801 646 -874 C ATOM 2266 CG PHE A 365 21.223 2.264 7.705 1.00 38.15 C ANISOU 2266 CG PHE A 365 7183 4041 3270 -691 742 -782 C ATOM 2267 CD1 PHE A 365 22.103 1.427 8.384 1.00 38.76 C ANISOU 2267 CD1 PHE A 365 7195 4022 3508 -631 892 -815 C ATOM 2268 CD2 PHE A 365 21.173 3.607 8.073 1.00 38.99 C ANISOU 2268 CD2 PHE A 365 7181 4229 3406 -650 675 -663 C ATOM 2269 CE1 PHE A 365 22.942 1.929 9.387 1.00 38.69 C ANISOU 2269 CE1 PHE A 365 7011 4015 3673 -538 961 -730 C ATOM 2270 CE2 PHE A 365 22.002 4.106 9.088 1.00 40.97 C ANISOU 2270 CE2 PHE A 365 7266 4470 3832 -565 754 -590 C ATOM 2271 CZ PHE A 365 22.879 3.262 9.739 1.00 38.68 C ANISOU 2271 CZ PHE A 365 6907 4100 3689 -513 888 -624 C ATOM 2272 N ARG A 366 19.181 0.642 3.777 1.00 38.45 N ANISOU 2272 N ARG A 366 7902 4109 2597 -1035 548 -1102 N ATOM 2273 CA ARG A 366 18.357 -0.285 2.985 1.00 38.75 C ANISOU 2273 CA ARG A 366 8112 4138 2474 -1168 454 -1233 C ATOM 2274 C ARG A 366 19.206 -1.141 2.062 1.00 44.88 C ANISOU 2274 C ARG A 366 9117 4807 3128 -1190 663 -1374 C ATOM 2275 O ARG A 366 18.992 -2.342 1.978 1.00 45.36 O ANISOU 2275 O ARG A 366 9264 4775 3194 -1260 689 -1507 O ATOM 2276 CB ARG A 366 17.314 0.490 2.171 1.00 37.28 C ANISOU 2276 CB ARG A 366 7993 4093 2077 -1246 230 -1186 C ATOM 2277 CG ARG A 366 16.249 -0.385 1.520 1.00 35.58 C ANISOU 2277 CG ARG A 366 7905 3897 1717 -1399 70 -1308 C ATOM 2278 CD ARG A 366 15.145 0.374 0.791 1.00 40.24 C ANISOU 2278 CD ARG A 366 8516 4645 2128 -1473 -191 -1242 C ATOM 2279 NE ARG A 366 14.780 1.665 1.370 1.00 58.02 N ANISOU 2279 NE ARG A 366 10574 6997 4475 -1383 -301 -1060 N ATOM 2280 CZ ARG A 366 15.114 2.840 0.849 1.00 78.36 C ANISOU 2280 CZ ARG A 366 13197 9641 6936 -1321 -292 -948 C ATOM 2281 NH1 ARG A 366 15.825 2.898 -0.268 1.00 72.66 N ANISOU 2281 NH1 ARG A 366 12706 8908 5991 -1339 -176 -992 N ATOM 2282 NH2 ARG A 366 14.725 3.966 1.432 1.00 69.35 N ANISOU 2282 NH2 ARG A 366 11878 8571 5903 -1240 -386 -791 N ATOM 2283 N GLU A 367 20.185 -0.516 1.383 1.00 42.88 N ANISOU 2283 N GLU A 367 8963 4559 2772 -1131 825 -1344 N ATOM 2284 CA GLU A 367 21.132 -1.137 0.456 1.00 42.13 C ANISOU 2284 CA GLU A 367 9084 4369 2554 -1133 1061 -1463 C ATOM 2285 C GLU A 367 21.987 -2.187 1.180 1.00 46.66 C ANISOU 2285 C GLU A 367 9592 4785 3351 -1061 1266 -1532 C ATOM 2286 O GLU A 367 22.235 -3.254 0.630 1.00 46.64 O ANISOU 2286 O GLU A 367 9762 4672 3287 -1102 1394 -1680 O ATOM 2287 CB GLU A 367 22.023 -0.028 -0.106 1.00 43.08 C ANISOU 2287 CB GLU A 367 9248 4538 2582 -1062 1193 -1371 C ATOM 2288 CG GLU A 367 22.835 -0.413 -1.315 1.00 49.38 C ANISOU 2288 CG GLU A 367 10314 5284 3165 -1088 1398 -1479 C ATOM 2289 CD GLU A 367 23.395 0.795 -2.026 1.00 59.83 C ANISOU 2289 CD GLU A 367 11700 6684 4348 -1050 1476 -1373 C ATOM 2290 OE1 GLU A 367 24.301 1.451 -1.464 1.00 62.59 O ANISOU 2290 OE1 GLU A 367 11890 7020 4872 -944 1606 -1269 O ATOM 2291 OE2 GLU A 367 22.910 1.099 -3.138 1.00 50.37 O ANISOU 2291 OE2 GLU A 367 10712 5561 2866 -1131 1400 -1389 O ATOM 2292 N GLN A 368 22.421 -1.878 2.412 1.00 44.21 N ANISOU 2292 N GLN A 368 9037 4466 3296 -952 1294 -1422 N ATOM 2293 CA GLN A 368 23.256 -2.755 3.227 1.00 44.56 C ANISOU 2293 CA GLN A 368 8983 4376 3572 -864 1468 -1450 C ATOM 2294 C GLN A 368 22.466 -3.963 3.753 1.00 48.66 C ANISOU 2294 C GLN A 368 9495 4813 4182 -927 1383 -1536 C ATOM 2295 O GLN A 368 22.946 -5.094 3.657 1.00 47.87 O ANISOU 2295 O GLN A 368 9485 4568 4135 -915 1545 -1644 O ATOM 2296 CB GLN A 368 23.917 -1.959 4.366 1.00 46.08 C ANISOU 2296 CB GLN A 368 8919 4606 3984 -742 1494 -1298 C ATOM 2297 CG GLN A 368 24.920 -0.887 3.912 1.00 48.72 C ANISOU 2297 CG GLN A 368 9251 4991 4271 -676 1627 -1221 C ATOM 2298 CD GLN A 368 26.035 -1.428 3.076 1.00 62.39 C ANISOU 2298 CD GLN A 368 11132 6626 5947 -640 1896 -1309 C ATOM 2299 OE1 GLN A 368 26.691 -2.408 3.427 1.00 59.23 O ANISOU 2299 OE1 GLN A 368 10707 6106 5694 -579 2054 -1368 O ATOM 2300 NE2 GLN A 368 26.265 -0.794 1.945 1.00 58.91 N ANISOU 2300 NE2 GLN A 368 10854 6235 5295 -673 1961 -1314 N ATOM 2301 N PHE A 369 21.242 -3.721 4.274 1.00 45.32 N ANISOU 2301 N PHE A 369 8969 4475 3775 -996 1136 -1487 N ATOM 2302 CA PHE A 369 20.343 -4.767 4.767 1.00 44.39 C ANISOU 2302 CA PHE A 369 8835 4294 3738 -1077 1033 -1558 C ATOM 2303 C PHE A 369 19.948 -5.688 3.607 1.00 50.05 C ANISOU 2303 C PHE A 369 9813 4943 4260 -1208 1046 -1735 C ATOM 2304 O PHE A 369 19.968 -6.904 3.776 1.00 49.84 O ANISOU 2304 O PHE A 369 9847 4773 4316 -1238 1129 -1841 O ATOM 2305 CB PHE A 369 19.095 -4.166 5.443 1.00 45.03 C ANISOU 2305 CB PHE A 369 8749 4500 3860 -1128 771 -1463 C ATOM 2306 CG PHE A 369 19.313 -3.233 6.620 1.00 45.89 C ANISOU 2306 CG PHE A 369 8613 4680 4145 -1017 735 -1300 C ATOM 2307 CD1 PHE A 369 20.453 -3.332 7.415 1.00 48.92 C ANISOU 2307 CD1 PHE A 369 8886 4991 4709 -889 906 -1249 C ATOM 2308 CD2 PHE A 369 18.357 -2.288 6.962 1.00 46.70 C ANISOU 2308 CD2 PHE A 369 8589 4917 4237 -1042 526 -1202 C ATOM 2309 CE1 PHE A 369 20.644 -2.474 8.506 1.00 49.07 C ANISOU 2309 CE1 PHE A 369 8689 5080 4877 -801 863 -1110 C ATOM 2310 CE2 PHE A 369 18.545 -1.441 8.057 1.00 48.93 C ANISOU 2310 CE2 PHE A 369 8661 5255 4675 -946 501 -1066 C ATOM 2311 CZ PHE A 369 19.681 -1.546 8.828 1.00 47.10 C ANISOU 2311 CZ PHE A 369 8336 4955 4605 -833 666 -1026 C ATOM 2312 N LYS A 370 19.661 -5.116 2.414 1.00 47.60 N ANISOU 2312 N LYS A 370 9669 4729 3688 -1284 978 -1768 N ATOM 2313 CA LYS A 370 19.322 -5.876 1.205 1.00 48.25 C ANISOU 2313 CA LYS A 370 10025 4767 3542 -1418 984 -1941 C ATOM 2314 C LYS A 370 20.488 -6.800 0.810 1.00 54.29 C ANISOU 2314 C LYS A 370 10952 5356 4322 -1365 1285 -2065 C ATOM 2315 O LYS A 370 20.252 -7.966 0.514 1.00 53.88 O ANISOU 2315 O LYS A 370 11049 5179 4244 -1451 1332 -2222 O ATOM 2316 CB LYS A 370 18.915 -4.940 0.048 1.00 50.80 C ANISOU 2316 CB LYS A 370 10487 5243 3573 -1488 858 -1923 C ATOM 2317 CG LYS A 370 18.326 -5.666 -1.156 1.00 68.07 C ANISOU 2317 CG LYS A 370 12947 7419 5498 -1655 796 -2097 C ATOM 2318 CD LYS A 370 17.718 -4.706 -2.157 1.00 80.62 C ANISOU 2318 CD LYS A 370 14646 9183 6803 -1725 619 -2051 C ATOM 2319 CE LYS A 370 17.023 -5.436 -3.289 1.00 91.40 C ANISOU 2319 CE LYS A 370 16277 10552 7898 -1906 526 -2227 C ATOM 2320 NZ LYS A 370 16.230 -4.511 -4.146 1.00 98.37 N ANISOU 2320 NZ LYS A 370 17233 11627 8514 -1986 288 -2162 N ATOM 2321 N ALA A 371 21.735 -6.296 0.878 1.00 53.00 N ANISOU 2321 N ALA A 371 10741 5173 4222 -1221 1494 -1993 N ATOM 2322 CA ALA A 371 22.956 -7.056 0.596 1.00 54.33 C ANISOU 2322 CA ALA A 371 11019 5180 4442 -1139 1800 -2084 C ATOM 2323 C ALA A 371 23.164 -8.180 1.618 1.00 61.34 C ANISOU 2323 C ALA A 371 11797 5907 5603 -1080 1888 -2109 C ATOM 2324 O ALA A 371 23.587 -9.267 1.242 1.00 60.70 O ANISOU 2324 O ALA A 371 11870 5659 5534 -1079 2076 -2247 O ATOM 2325 CB ALA A 371 24.162 -6.123 0.598 1.00 55.15 C ANISOU 2325 CB ALA A 371 11039 5327 4587 -999 1972 -1970 C ATOM 2326 N ALA A 372 22.866 -7.909 2.907 1.00 61.65 N ANISOU 2326 N ALA A 372 11577 5990 5857 -1027 1757 -1974 N ATOM 2327 CA ALA A 372 22.983 -8.863 4.013 1.00 62.64 C ANISOU 2327 CA ALA A 372 11576 5983 6242 -968 1810 -1963 C ATOM 2328 C ALA A 372 22.060 -10.052 3.826 1.00 70.61 C ANISOU 2328 C ALA A 372 12726 6882 7221 -1106 1744 -2108 C ATOM 2329 O ALA A 372 22.522 -11.177 3.956 1.00 71.02 O ANISOU 2329 O ALA A 372 12847 6748 7388 -1071 1917 -2192 O ATOM 2330 CB ALA A 372 22.702 -8.175 5.340 1.00 63.22 C ANISOU 2330 CB ALA A 372 11366 6159 6498 -905 1656 -1787 C ATOM 2331 N PHE A 373 20.785 -9.815 3.466 1.00 70.75 N ANISOU 2331 N PHE A 373 12790 7006 7083 -1265 1502 -2141 N ATOM 2332 CA PHE A 373 19.801 -10.880 3.259 1.00 73.07 C ANISOU 2332 CA PHE A 373 13207 7212 7343 -1424 1412 -2281 C ATOM 2333 C PHE A 373 19.859 -11.543 1.878 1.00 84.24 C ANISOU 2333 C PHE A 373 14940 8539 8529 -1536 1511 -2488 C ATOM 2334 O PHE A 373 19.418 -12.683 1.763 1.00 83.89 O ANISOU 2334 O PHE A 373 15018 8351 8507 -1639 1529 -2627 O ATOM 2335 CB PHE A 373 18.372 -10.391 3.558 1.00 74.68 C ANISOU 2335 CB PHE A 373 13296 7571 7509 -1550 1102 -2225 C ATOM 2336 CG PHE A 373 18.141 -9.916 4.978 1.00 76.19 C ANISOU 2336 CG PHE A 373 13193 7826 7928 -1465 1004 -2048 C ATOM 2337 CD1 PHE A 373 18.222 -10.800 6.050 1.00 79.39 C ANISOU 2337 CD1 PHE A 373 13497 8095 8573 -1423 1073 -2028 C ATOM 2338 CD2 PHE A 373 17.797 -8.596 5.240 1.00 77.55 C ANISOU 2338 CD2 PHE A 373 13206 8191 8070 -1434 839 -1904 C ATOM 2339 CE1 PHE A 373 18.020 -10.355 7.361 1.00 79.90 C ANISOU 2339 CE1 PHE A 373 13307 8224 8827 -1347 988 -1867 C ATOM 2340 CE2 PHE A 373 17.585 -8.158 6.549 1.00 80.04 C ANISOU 2340 CE2 PHE A 373 13268 8561 8585 -1360 760 -1754 C ATOM 2341 CZ PHE A 373 17.692 -9.040 7.599 1.00 78.33 C ANISOU 2341 CZ PHE A 373 12957 8218 8588 -1321 833 -1739 C ATOM 2342 N SER A 374 20.383 -10.850 0.839 1.00 86.79 N ANISOU 2342 N SER A 374 15406 8941 8629 -1522 1579 -2511 N ATOM 2343 CA SER A 374 20.461 -11.374 -0.533 1.00 89.37 C ANISOU 2343 CA SER A 374 16054 9204 8699 -1629 1676 -2706 C ATOM 2344 C SER A 374 21.749 -12.089 -0.899 1.00101.11 C ANISOU 2344 C SER A 374 17686 10498 10233 -1524 2020 -2806 C ATOM 2345 O SER A 374 21.675 -13.037 -1.684 1.00101.40 O ANISOU 2345 O SER A 374 17968 10393 10166 -1620 2118 -3000 O ATOM 2346 CB SER A 374 20.196 -10.285 -1.569 1.00 92.41 C ANISOU 2346 CB SER A 374 16547 9781 8785 -1687 1561 -2682 C ATOM 2347 OG SER A 374 18.971 -9.612 -1.331 1.00101.69 O ANISOU 2347 OG SER A 374 17589 11137 9910 -1777 1241 -2586 O ATOM 2348 N TRP A 375 22.929 -11.619 -0.455 1.00103.51 N ANISOU 2348 N TRP A 375 17859 10798 10674 -1335 2210 -2686 N ATOM 2349 CA TRP A 375 24.157 -12.303 -0.882 1.00106.34 C ANISOU 2349 CA TRP A 375 18355 10977 11075 -1231 2548 -2784 C ATOM 2350 C TRP A 375 25.188 -12.544 0.228 1.00112.92 C ANISOU 2350 C TRP A 375 18962 11702 12242 -1030 2729 -2668 C ATOM 2351 O TRP A 375 25.999 -13.466 0.091 1.00113.35 O ANISOU 2351 O TRP A 375 19111 11558 12400 -954 2984 -2762 O ATOM 2352 CB TRP A 375 24.821 -11.630 -2.104 1.00106.10 C ANISOU 2352 CB TRP A 375 18503 11018 10793 -1218 2691 -2820 C ATOM 2353 CG TRP A 375 25.119 -10.162 -1.989 1.00107.87 C ANISOU 2353 CG TRP A 375 18563 11441 10981 -1147 2615 -2634 C ATOM 2354 CD1 TRP A 375 26.147 -9.586 -1.302 1.00110.92 C ANISOU 2354 CD1 TRP A 375 18738 11844 11564 -972 2757 -2485 C ATOM 2355 CD2 TRP A 375 24.496 -9.107 -2.738 1.00108.10 C ANISOU 2355 CD2 TRP A 375 18669 11666 10738 -1250 2419 -2594 C ATOM 2356 NE1 TRP A 375 26.158 -8.225 -1.517 1.00110.67 N ANISOU 2356 NE1 TRP A 375 18640 11998 11411 -968 2656 -2356 N ATOM 2357 CE2 TRP A 375 25.159 -7.905 -2.402 1.00112.21 C ANISOU 2357 CE2 TRP A 375 19012 12303 11320 -1129 2452 -2414 C ATOM 2358 CE3 TRP A 375 23.423 -9.056 -3.647 1.00109.63 C ANISOU 2358 CE3 TRP A 375 19058 11951 10647 -1434 2205 -2687 C ATOM 2359 CZ2 TRP A 375 24.781 -6.665 -2.936 1.00111.69 C ANISOU 2359 CZ2 TRP A 375 18967 12426 11047 -1179 2293 -2320 C ATOM 2360 CZ3 TRP A 375 23.043 -7.826 -4.167 1.00111.23 C ANISOU 2360 CZ3 TRP A 375 19269 12354 10641 -1476 2034 -2584 C ATOM 2361 CH2 TRP A 375 23.718 -6.649 -3.812 1.00111.88 C ANISOU 2361 CH2 TRP A 375 19182 12534 10796 -1346 2084 -2401 C ATOM 2362 N TRP A 376 25.160 -11.757 1.313 1.00110.35 N ANISOU 2362 N TRP A 376 18347 11499 12083 -943 2601 -2470 N ATOM 2363 CA TRP A 376 26.100 -11.962 2.414 1.00110.82 C ANISOU 2363 CA TRP A 376 18180 11479 12449 -760 2736 -2348 C ATOM 2364 C TRP A 376 25.775 -13.280 3.137 1.00114.57 C ANISOU 2364 C TRP A 376 18646 11770 13115 -769 2745 -2400 C ATOM 2365 O TRP A 376 26.694 -14.009 3.512 1.00114.07 O ANISOU 2365 O TRP A 376 18550 11543 13249 -633 2963 -2398 O ATOM 2366 CB TRP A 376 26.123 -10.748 3.359 1.00110.16 C ANISOU 2366 CB TRP A 376 17812 11579 12465 -692 2573 -2139 C ATOM 2367 CG TRP A 376 27.290 -10.728 4.304 1.00111.57 C ANISOU 2367 CG TRP A 376 17768 11715 12909 -501 2724 -2010 C ATOM 2368 CD1 TRP A 376 28.612 -10.642 3.976 1.00114.55 C ANISOU 2368 CD1 TRP A 376 18138 12042 13343 -370 2981 -2000 C ATOM 2369 CD2 TRP A 376 27.232 -10.762 5.737 1.00111.59 C ANISOU 2369 CD2 TRP A 376 17518 11726 13155 -423 2625 -1869 C ATOM 2370 NE1 TRP A 376 29.384 -10.673 5.114 1.00114.16 N ANISOU 2370 NE1 TRP A 376 17839 11969 13566 -215 3037 -1864 N ATOM 2371 CE2 TRP A 376 28.562 -10.722 6.212 1.00115.64 C ANISOU 2371 CE2 TRP A 376 17879 12196 13861 -245 2817 -1779 C ATOM 2372 CE3 TRP A 376 26.181 -10.826 6.671 1.00112.86 C ANISOU 2372 CE3 TRP A 376 17564 11932 13387 -488 2394 -1807 C ATOM 2373 CZ2 TRP A 376 28.872 -10.749 7.578 1.00114.95 C ANISOU 2373 CZ2 TRP A 376 17541 12116 14020 -134 2770 -1631 C ATOM 2374 CZ3 TRP A 376 26.489 -10.860 8.022 1.00114.41 C ANISOU 2374 CZ3 TRP A 376 17523 12127 13822 -376 2366 -1664 C ATOM 2375 CH2 TRP A 376 27.820 -10.825 8.464 1.00115.09 C ANISOU 2375 CH2 TRP A 376 17472 12175 14082 -202 2545 -1577 C ATOM 2376 N LEU A 377 24.459 -13.597 3.265 1.00111.15 N ANISOU 2376 N LEU A 377 18255 11361 12617 -933 2516 -2449 N ATOM 2377 CA LEU A 377 23.862 -14.823 3.826 1.00110.88 C ANISOU 2377 CA LEU A 377 18248 11159 12722 -993 2493 -2515 C ATOM 2378 C LEU A 377 22.335 -14.868 3.592 1.00114.84 C ANISOU 2378 C LEU A 377 18820 11737 13076 -1213 2222 -2588 C ATOM 2379 O LEU A 377 21.623 -14.007 4.112 1.00114.38 O ANISOU 2379 O LEU A 377 18587 11859 13014 -1250 1989 -2465 O ATOM 2380 CB LEU A 377 24.226 -15.127 5.306 1.00110.83 C ANISOU 2380 CB LEU A 377 17992 11086 13031 -848 2517 -2357 C ATOM 2381 CG LEU A 377 24.266 -13.993 6.339 1.00115.15 C ANISOU 2381 CG LEU A 377 18247 11825 13681 -763 2362 -2142 C ATOM 2382 CD1 LEU A 377 22.938 -13.850 7.058 1.00115.08 C ANISOU 2382 CD1 LEU A 377 18130 11898 13699 -880 2098 -2088 C ATOM 2383 CD2 LEU A 377 25.332 -14.271 7.376 1.00117.47 C ANISOU 2383 CD2 LEU A 377 18357 12037 14240 -560 2517 -2012 C ATOM 2384 N PRO A 378 21.808 -15.837 2.797 1.00111.41 N ANISOU 2384 N PRO A 378 18638 11169 12522 -1366 2249 -2791 N ATOM 2385 CA PRO A 378 20.352 -15.875 2.558 1.00114.09 C ANISOU 2385 CA PRO A 378 19029 11591 12728 -1587 1980 -2861 C ATOM 2386 C PRO A 378 19.559 -16.385 3.762 1.00122.69 C ANISOU 2386 C PRO A 378 19942 12633 14043 -1624 1850 -2786 C ATOM 2387 O PRO A 378 19.085 -15.595 4.580 1.00 74.35 O ANISOU 2387 O PRO A 378 13581 6668 8002 -1594 1674 -2619 O ATOM 2388 CB PRO A 378 20.205 -16.804 1.340 1.00115.43 C ANISOU 2388 CB PRO A 378 19534 11616 12709 -1732 2080 -3111 C ATOM 2389 CG PRO A 378 21.616 -17.110 0.873 1.00118.91 C ANISOU 2389 CG PRO A 378 20103 11917 13162 -1575 2412 -3165 C ATOM 2390 CD PRO A 378 22.490 -16.923 2.068 1.00113.85 C ANISOU 2390 CD PRO A 378 19197 11249 12811 -1351 2522 -2970 C TER 2391 PRO A 378 ATOM 2392 N ASP B 29 0.971 49.750 60.703 1.00 94.59 N ANISOU 2392 N ASP B 29 10112 11945 13882 751 2151 -4535 N ATOM 2393 CA ASP B 29 1.786 49.163 59.639 1.00 93.99 C ANISOU 2393 CA ASP B 29 10115 11818 13779 710 1999 -4288 C ATOM 2394 C ASP B 29 1.745 49.967 58.331 1.00 95.34 C ANISOU 2394 C ASP B 29 10235 11720 14270 752 1911 -4189 C ATOM 2395 O ASP B 29 2.703 49.899 57.557 1.00 94.98 O ANISOU 2395 O ASP B 29 10257 11600 14232 718 1787 -4060 O ATOM 2396 CB ASP B 29 1.421 47.680 59.402 1.00 96.15 C ANISOU 2396 CB ASP B 29 10426 12244 13863 680 1994 -4059 C ATOM 2397 CG ASP B 29 0.027 47.432 58.848 1.00109.40 C ANISOU 2397 CG ASP B 29 12001 13871 15696 732 2051 -3953 C ATOM 2398 OD1 ASP B 29 -0.961 47.832 59.512 1.00110.63 O ANISOU 2398 OD1 ASP B 29 12064 14046 15925 777 2183 -4109 O ATOM 2399 OD2 ASP B 29 -0.078 46.822 57.760 1.00115.79 O ANISOU 2399 OD2 ASP B 29 12819 14625 16550 726 1964 -3722 O ATOM 2400 N GLU B 30 0.646 50.727 58.089 1.00 89.39 N ANISOU 2400 N GLU B 30 9361 10824 13779 827 1975 -4243 N ATOM 2401 CA GLU B 30 0.480 51.559 56.889 1.00 87.63 C ANISOU 2401 CA GLU B 30 9079 10342 13874 878 1899 -4147 C ATOM 2402 C GLU B 30 1.470 52.745 56.857 1.00 86.49 C ANISOU 2402 C GLU B 30 8951 10034 13878 873 1852 -4283 C ATOM 2403 O GLU B 30 1.867 53.176 55.767 1.00 85.72 O ANISOU 2403 O GLU B 30 8859 9752 13958 882 1750 -4147 O ATOM 2404 CB GLU B 30 -0.974 52.031 56.720 1.00 89.02 C ANISOU 2404 CB GLU B 30 9114 10420 14289 965 1983 -4176 C ATOM 2405 CG GLU B 30 -1.378 52.188 55.262 1.00100.72 C ANISOU 2405 CG GLU B 30 10548 11710 16011 1011 1882 -3953 C ATOM 2406 CD GLU B 30 -2.821 52.586 55.015 1.00126.96 C ANISOU 2406 CD GLU B 30 13726 14945 19567 1097 1948 -3953 C ATOM 2407 OE1 GLU B 30 -3.191 53.737 55.342 1.00115.71 O ANISOU 2407 OE1 GLU B 30 12208 13387 18368 1159 2019 -4137 O ATOM 2408 OE2 GLU B 30 -3.579 51.748 54.475 1.00127.62 O ANISOU 2408 OE2 GLU B 30 13783 15088 19620 1104 1925 -3772 O ATOM 2409 N PHE B 31 1.883 53.246 58.046 1.00 78.81 N ANISOU 2409 N PHE B 31 7987 9131 12824 855 1924 -4551 N ATOM 2410 CA PHE B 31 2.859 54.330 58.163 1.00 76.69 C ANISOU 2410 CA PHE B 31 7733 8724 12684 839 1885 -4711 C ATOM 2411 C PHE B 31 4.236 53.839 57.714 1.00 77.49 C ANISOU 2411 C PHE B 31 7947 8855 12639 762 1755 -4575 C ATOM 2412 O PHE B 31 4.897 54.537 56.944 1.00 76.12 O ANISOU 2412 O PHE B 31 7776 8488 12657 757 1674 -4527 O ATOM 2413 CB PHE B 31 2.915 54.886 59.596 1.00 78.14 C ANISOU 2413 CB PHE B 31 7900 9006 12786 834 1993 -5042 C ATOM 2414 CG PHE B 31 3.928 55.987 59.801 1.00 79.53 C ANISOU 2414 CG PHE B 31 8084 9043 13092 811 1952 -5233 C ATOM 2415 CD1 PHE B 31 3.656 57.288 59.397 1.00 82.98 C ANISOU 2415 CD1 PHE B 31 8426 9215 13886 868 1971 -5336 C ATOM 2416 CD2 PHE B 31 5.152 55.725 60.400 1.00 81.92 C ANISOU 2416 CD2 PHE B 31 8481 9473 13171 732 1892 -5307 C ATOM 2417 CE1 PHE B 31 4.593 58.308 59.592 1.00 84.27 C ANISOU 2417 CE1 PHE B 31 8592 9239 14188 841 1936 -5517 C ATOM 2418 CE2 PHE B 31 6.095 56.741 60.579 1.00 85.07 C ANISOU 2418 CE2 PHE B 31 8879 9740 13704 705 1850 -5488 C ATOM 2419 CZ PHE B 31 5.807 58.027 60.179 1.00 83.33 C ANISOU 2419 CZ PHE B 31 8565 9252 13844 757 1875 -5594 C ATOM 2420 N LEU B 32 4.648 52.630 58.186 1.00 72.74 N ANISOU 2420 N LEU B 32 7436 8494 11709 703 1739 -4507 N ATOM 2421 CA LEU B 32 5.923 51.970 57.862 1.00 71.81 C ANISOU 2421 CA LEU B 32 7425 8439 11419 631 1623 -4374 C ATOM 2422 C LEU B 32 6.030 51.728 56.374 1.00 70.15 C ANISOU 2422 C LEU B 32 7228 8087 11340 637 1523 -4097 C ATOM 2423 O LEU B 32 7.099 51.937 55.817 1.00 68.33 O ANISOU 2423 O LEU B 32 7045 7770 11149 600 1430 -4033 O ATOM 2424 CB LEU B 32 6.097 50.650 58.633 1.00 72.67 C ANISOU 2424 CB LEU B 32 7614 8829 11167 582 1638 -4334 C ATOM 2425 CG LEU B 32 6.251 50.800 60.150 1.00 79.19 C ANISOU 2425 CG LEU B 32 8450 9833 11805 564 1723 -4600 C ATOM 2426 CD1 LEU B 32 5.345 49.820 60.902 1.00 79.95 C ANISOU 2426 CD1 LEU B 32 8554 10156 11667 568 1820 -4569 C ATOM 2427 CD2 LEU B 32 7.705 50.680 60.574 1.00 83.25 C ANISOU 2427 CD2 LEU B 32 9048 10429 12155 496 1638 -4674 C ATOM 2428 N ARG B 33 4.904 51.347 55.732 1.00 64.44 N ANISOU 2428 N ARG B 33 6455 7334 10697 687 1545 -3944 N ATOM 2429 CA ARG B 33 4.765 51.127 54.293 1.00 63.36 C ANISOU 2429 CA ARG B 33 6319 7068 10688 704 1456 -3685 C ATOM 2430 C ARG B 33 5.118 52.422 53.532 1.00 66.63 C ANISOU 2430 C ARG B 33 6692 7222 11404 734 1410 -3695 C ATOM 2431 O ARG B 33 5.929 52.375 52.608 1.00 64.38 O ANISOU 2431 O ARG B 33 6459 6853 11148 705 1313 -3538 O ATOM 2432 CB ARG B 33 3.337 50.657 53.969 1.00 62.19 C ANISOU 2432 CB ARG B 33 6101 6942 10587 758 1501 -3577 C ATOM 2433 CG ARG B 33 3.184 50.008 52.599 1.00 71.74 C ANISOU 2433 CG ARG B 33 7332 8096 11832 763 1402 -3295 C ATOM 2434 CD ARG B 33 1.838 49.325 52.413 1.00 84.86 C ANISOU 2434 CD ARG B 33 8927 9817 13498 802 1441 -3198 C ATOM 2435 NE ARG B 33 1.687 48.136 53.256 1.00 97.81 N ANISOU 2435 NE ARG B 33 10609 11690 14864 757 1494 -3201 N ATOM 2436 CZ ARG B 33 1.922 46.888 52.858 1.00117.43 C ANISOU 2436 CZ ARG B 33 13165 14283 17169 712 1434 -3016 C ATOM 2437 NH1 ARG B 33 2.318 46.641 51.614 1.00104.30 N ANISOU 2437 NH1 ARG B 33 11542 12530 15559 705 1319 -2822 N ATOM 2438 NH2 ARG B 33 1.757 45.876 53.700 1.00107.63 N ANISOU 2438 NH2 ARG B 33 11955 13242 15697 674 1492 -3025 N ATOM 2439 N TYR B 34 4.545 53.579 53.955 1.00 64.97 N ANISOU 2439 N TYR B 34 6387 6881 11417 789 1485 -3885 N ATOM 2440 CA TYR B 34 4.836 54.882 53.354 1.00 65.36 C ANISOU 2440 CA TYR B 34 6390 6670 11775 819 1453 -3911 C ATOM 2441 C TYR B 34 6.245 55.376 53.702 1.00 65.57 C ANISOU 2441 C TYR B 34 6473 6662 11779 753 1413 -4030 C ATOM 2442 O TYR B 34 6.884 55.971 52.844 1.00 64.75 O ANISOU 2442 O TYR B 34 6377 6379 11848 745 1344 -3932 O ATOM 2443 CB TYR B 34 3.747 55.929 53.667 1.00 68.63 C ANISOU 2443 CB TYR B 34 6679 6943 12455 903 1545 -4072 C ATOM 2444 CG TYR B 34 2.412 55.598 53.028 1.00 73.85 C ANISOU 2444 CG TYR B 34 7268 7585 13208 974 1560 -3917 C ATOM 2445 CD1 TYR B 34 2.340 55.119 51.721 1.00 76.82 C ANISOU 2445 CD1 TYR B 34 7666 7902 13619 983 1459 -3631 C ATOM 2446 CD2 TYR B 34 1.224 55.732 53.739 1.00 75.38 C ANISOU 2446 CD2 TYR B 34 7368 7828 13446 1030 1675 -4062 C ATOM 2447 CE1 TYR B 34 1.121 54.763 51.145 1.00 78.68 C ANISOU 2447 CE1 TYR B 34 7832 8133 13930 1044 1461 -3493 C ATOM 2448 CE2 TYR B 34 -0.005 55.408 53.164 1.00 76.99 C ANISOU 2448 CE2 TYR B 34 7493 8016 13742 1094 1684 -3922 C ATOM 2449 CZ TYR B 34 -0.050 54.910 51.869 1.00 87.10 C ANISOU 2449 CZ TYR B 34 8797 9243 15053 1099 1571 -3638 C ATOM 2450 OH TYR B 34 -1.252 54.572 51.286 1.00 91.03 O ANISOU 2450 OH TYR B 34 9214 9732 15641 1159 1568 -3504 O ATOM 2451 N LEU B 35 6.753 55.069 54.914 1.00 60.30 N ANISOU 2451 N LEU B 35 5848 6176 10889 703 1452 -4224 N ATOM 2452 CA LEU B 35 8.108 55.435 55.335 1.00 60.10 C ANISOU 2452 CA LEU B 35 5872 6148 10815 635 1407 -4351 C ATOM 2453 C LEU B 35 9.161 54.626 54.561 1.00 58.41 C ANISOU 2453 C LEU B 35 5750 5980 10462 573 1296 -4127 C ATOM 2454 O LEU B 35 10.230 55.145 54.258 1.00 58.82 O ANISOU 2454 O LEU B 35 5821 5922 10605 531 1236 -4134 O ATOM 2455 CB LEU B 35 8.278 55.309 56.870 1.00 61.30 C ANISOU 2455 CB LEU B 35 6040 6502 10749 605 1474 -4621 C ATOM 2456 CG LEU B 35 9.649 55.679 57.503 1.00 67.48 C ANISOU 2456 CG LEU B 35 6869 7320 11450 531 1424 -4788 C ATOM 2457 CD1 LEU B 35 9.865 57.192 57.590 1.00 67.38 C ANISOU 2457 CD1 LEU B 35 6785 7076 11740 543 1440 -4995 C ATOM 2458 CD2 LEU B 35 9.782 55.082 58.892 1.00 72.28 C ANISOU 2458 CD2 LEU B 35 7520 8201 11743 499 1469 -4966 C ATOM 2459 N TRP B 36 8.882 53.341 54.346 1.00 50.52 N ANISOU 2459 N TRP B 36 4801 5129 9265 568 1273 -3926 N ATOM 2460 CA TRP B 36 9.796 52.481 53.553 1.00 48.45 C ANISOU 2460 CA TRP B 36 4624 4916 8868 518 1176 -3705 C ATOM 2461 C TRP B 36 9.789 52.905 52.081 1.00 52.19 C ANISOU 2461 C TRP B 36 5083 5174 9574 542 1115 -3498 C ATOM 2462 O TRP B 36 10.860 53.115 51.516 1.00 51.45 O ANISOU 2462 O TRP B 36 5023 4993 9533 501 1051 -3438 O ATOM 2463 CB TRP B 36 9.362 51.020 53.687 1.00 45.65 C ANISOU 2463 CB TRP B 36 4321 4781 8244 509 1179 -3571 C ATOM 2464 CG TRP B 36 10.026 50.128 52.688 1.00 45.68 C ANISOU 2464 CG TRP B 36 4403 4822 8132 469 1087 -3332 C ATOM 2465 CD1 TRP B 36 9.524 49.707 51.494 1.00 48.31 C ANISOU 2465 CD1 TRP B 36 4743 5108 8503 493 1046 -3098 C ATOM 2466 CD2 TRP B 36 11.348 49.576 52.786 1.00 45.37 C ANISOU 2466 CD2 TRP B 36 4440 4868 7930 401 1021 -3312 C ATOM 2467 NE1 TRP B 36 10.434 48.918 50.852 1.00 48.09 N ANISOU 2467 NE1 TRP B 36 4797 5136 8341 443 968 -2940 N ATOM 2468 CE2 TRP B 36 11.561 48.817 51.620 1.00 49.24 C ANISOU 2468 CE2 TRP B 36 4982 5360 8367 388 952 -3063 C ATOM 2469 CE3 TRP B 36 12.362 49.641 53.745 1.00 46.33 C ANISOU 2469 CE3 TRP B 36 4587 5068 7949 350 1010 -3486 C ATOM 2470 CZ2 TRP B 36 12.751 48.132 51.391 1.00 48.07 C ANISOU 2470 CZ2 TRP B 36 4907 5282 8076 330 881 -2981 C ATOM 2471 CZ3 TRP B 36 13.537 48.963 53.517 1.00 47.51 C ANISOU 2471 CZ3 TRP B 36 4804 5288 7959 292 931 -3399 C ATOM 2472 CH2 TRP B 36 13.725 48.218 52.356 1.00 48.04 C ANISOU 2472 CH2 TRP B 36 4919 5349 7985 284 872 -3149 C ATOM 2473 N ARG B 37 8.593 53.080 51.525 1.00 49.08 N ANISOU 2473 N ARG B 37 4632 4698 9317 611 1137 -3392 N ATOM 2474 CA ARG B 37 8.381 53.434 50.099 1.00 49.15 C ANISOU 2474 CA ARG B 37 4621 4517 9537 648 1082 -3185 C ATOM 2475 C ARG B 37 8.878 54.840 49.760 1.00 53.22 C ANISOU 2475 C ARG B 37 5094 4789 10337 656 1074 -3247 C ATOM 2476 O ARG B 37 9.461 55.015 48.685 1.00 52.74 O ANISOU 2476 O ARG B 37 5062 4610 10364 641 1007 -3074 O ATOM 2477 CB ARG B 37 6.889 53.339 49.784 1.00 49.34 C ANISOU 2477 CB ARG B 37 4574 4521 9653 727 1117 -3115 C ATOM 2478 CG ARG B 37 6.485 53.994 48.474 1.00 56.94 C ANISOU 2478 CG ARG B 37 5492 5279 10864 785 1067 -2929 C ATOM 2479 CD ARG B 37 5.064 54.494 48.578 1.00 67.34 C ANISOU 2479 CD ARG B 37 6697 6521 12369 870 1131 -3001 C ATOM 2480 NE ARG B 37 4.644 55.226 47.399 1.00 78.04 N ANISOU 2480 NE ARG B 37 7996 7652 14004 935 1087 -2860 N ATOM 2481 CZ ARG B 37 3.717 56.169 47.412 1.00 98.62 C ANISOU 2481 CZ ARG B 37 10494 10104 16875 1012 1135 -2949 C ATOM 2482 NH1 ARG B 37 3.132 56.498 48.549 1.00 85.86 N ANISOU 2482 NH1 ARG B 37 8812 8532 15278 1034 1238 -3193 N ATOM 2483 NH2 ARG B 37 3.391 56.793 46.295 1.00 94.01 N ANISOU 2483 NH2 ARG B 37 9863 9318 16538 1071 1084 -2794 N ATOM 2484 N ASP B 38 8.624 55.810 50.635 1.00 49.83 N ANISOU 2484 N ASP B 38 4595 4282 10056 680 1145 -3490 N ATOM 2485 CA ASP B 38 8.996 57.213 50.326 1.00 49.72 C ANISOU 2485 CA ASP B 38 4527 4020 10345 693 1147 -3567 C ATOM 2486 C ASP B 38 10.322 57.623 50.979 1.00 54.21 C ANISOU 2486 C ASP B 38 5120 4578 10899 618 1141 -3758 C ATOM 2487 O ASP B 38 10.830 58.675 50.601 1.00 53.12 O ANISOU 2487 O ASP B 38 4940 4222 11023 617 1138 -3813 O ATOM 2488 CB ASP B 38 7.832 58.159 50.630 1.00 51.03 C ANISOU 2488 CB ASP B 38 4583 4056 10751 778 1226 -3704 C ATOM 2489 CG ASP B 38 6.618 57.928 49.748 1.00 57.58 C ANISOU 2489 CG ASP B 38 5368 4846 11665 857 1218 -3505 C ATOM 2490 OD1 ASP B 38 6.803 57.646 48.559 1.00 57.77 O ANISOU 2490 OD1 ASP B 38 5436 4841 11675 855 1137 -3241 O ATOM 2491 OD2 ASP B 38 5.500 58.038 50.259 1.00 58.17 O ANISOU 2491 OD2 ASP B 38 5360 4920 11822 922 1291 -3618 O ATOM 2492 N TYR B 39 10.861 56.845 51.920 1.00 51.15 N ANISOU 2492 N TYR B 39 4797 4417 10220 555 1134 -3851 N ATOM 2493 CA TYR B 39 12.132 57.301 52.534 1.00 51.62 C ANISOU 2493 CA TYR B 39 4874 4476 10264 484 1115 -4033 C ATOM 2494 C TYR B 39 13.184 56.200 52.735 1.00 55.42 C ANISOU 2494 C TYR B 39 5448 5168 10442 407 1051 -3970 C ATOM 2495 O TYR B 39 14.243 56.293 52.121 1.00 55.99 O ANISOU 2495 O TYR B 39 5551 5168 10556 359 987 -3861 O ATOM 2496 CB TYR B 39 11.905 58.066 53.840 1.00 53.87 C ANISOU 2496 CB TYR B 39 5101 4770 10598 494 1192 -4371 C ATOM 2497 CG TYR B 39 13.205 58.486 54.471 1.00 57.06 C ANISOU 2497 CG TYR B 39 5517 5169 10995 417 1159 -4563 C ATOM 2498 CD1 TYR B 39 14.048 59.365 53.821 1.00 59.42 C ANISOU 2498 CD1 TYR B 39 5792 5242 11542 385 1116 -4532 C ATOM 2499 CD2 TYR B 39 13.626 57.956 55.673 1.00 58.25 C ANISOU 2499 CD2 TYR B 39 5706 5551 10875 372 1163 -4753 C ATOM 2500 CE1 TYR B 39 15.265 59.733 54.361 1.00 60.37 C ANISOU 2500 CE1 TYR B 39 5918 5362 11657 307 1077 -4698 C ATOM 2501 CE2 TYR B 39 14.841 58.313 56.228 1.00 59.53 C ANISOU 2501 CE2 TYR B 39 5878 5722 11017 298 1115 -4919 C ATOM 2502 CZ TYR B 39 15.664 59.203 55.569 1.00 67.79 C ANISOU 2502 CZ TYR B 39 6893 6538 12327 265 1072 -4895 C ATOM 2503 OH TYR B 39 16.859 59.568 56.107 1.00 71.72 O ANISOU 2503 OH TYR B 39 7388 7038 12824 189 1023 -5067 O ATOM 2504 N LEU B 40 12.887 55.194 53.555 1.00 50.32 N ANISOU 2504 N LEU B 40 4841 4772 9505 396 1073 -4043 N ATOM 2505 CA LEU B 40 13.895 54.180 53.961 1.00 49.44 C ANISOU 2505 CA LEU B 40 4812 4870 9103 330 1016 -4003 C ATOM 2506 C LEU B 40 14.494 53.446 52.759 1.00 51.55 C ANISOU 2506 C LEU B 40 5138 5124 9326 304 938 -3723 C ATOM 2507 O LEU B 40 15.713 53.292 52.741 1.00 51.11 O ANISOU 2507 O LEU B 40 5120 5098 9203 243 877 -3710 O ATOM 2508 CB LEU B 40 13.226 53.187 54.910 1.00 50.02 C ANISOU 2508 CB LEU B 40 4919 5204 8884 337 1058 -4059 C ATOM 2509 CG LEU B 40 12.802 53.754 56.257 1.00 56.08 C ANISOU 2509 CG LEU B 40 5639 6037 9630 360 1146 -4342 C ATOM 2510 CD1 LEU B 40 11.961 52.745 57.013 1.00 57.42 C ANISOU 2510 CD1 LEU B 40 5837 6438 9540 379 1201 -4318 C ATOM 2511 CD2 LEU B 40 14.017 54.142 57.075 1.00 59.09 C ANISOU 2511 CD2 LEU B 40 6027 6467 9955 302 1121 -4582 C ATOM 2512 N TYR B 41 13.683 53.033 51.790 1.00 45.80 N ANISOU 2512 N TYR B 41 4413 4356 8632 351 939 -3505 N ATOM 2513 CA TYR B 41 14.244 52.362 50.628 1.00 43.25 C ANISOU 2513 CA TYR B 41 4147 4021 8264 328 869 -3248 C ATOM 2514 C TYR B 41 14.991 53.326 49.659 1.00 46.48 C ANISOU 2514 C TYR B 41 4536 4201 8922 313 834 -3172 C ATOM 2515 O TYR B 41 16.153 53.046 49.390 1.00 44.66 O ANISOU 2515 O TYR B 41 4348 3991 8629 255 782 -3111 O ATOM 2516 CB TYR B 41 13.216 51.500 49.878 1.00 42.41 C ANISOU 2516 CB TYR B 41 4060 3968 8087 374 868 -3038 C ATOM 2517 CG TYR B 41 13.802 50.933 48.598 1.00 41.07 C ANISOU 2517 CG TYR B 41 3947 3767 7893 353 798 -2786 C ATOM 2518 CD1 TYR B 41 14.805 49.966 48.636 1.00 41.99 C ANISOU 2518 CD1 TYR B 41 4134 4022 7799 296 749 -2722 C ATOM 2519 CD2 TYR B 41 13.394 51.406 47.354 1.00 40.78 C ANISOU 2519 CD2 TYR B 41 3889 3560 8044 393 780 -2617 C ATOM 2520 CE1 TYR B 41 15.373 49.469 47.466 1.00 41.42 C ANISOU 2520 CE1 TYR B 41 4111 3920 7706 278 694 -2505 C ATOM 2521 CE2 TYR B 41 13.973 50.937 46.180 1.00 41.20 C ANISOU 2521 CE2 TYR B 41 3998 3591 8067 373 721 -2396 C ATOM 2522 CZ TYR B 41 14.953 49.961 46.242 1.00 45.61 C ANISOU 2522 CZ TYR B 41 4626 4290 8415 315 682 -2347 C ATOM 2523 OH TYR B 41 15.498 49.479 45.093 1.00 44.05 O ANISOU 2523 OH TYR B 41 4480 4075 8183 298 634 -2140 O ATOM 2524 N PRO B 42 14.377 54.410 49.091 1.00 44.28 N ANISOU 2524 N PRO B 42 4193 3705 8925 363 861 -3156 N ATOM 2525 CA PRO B 42 15.115 55.239 48.118 1.00 44.24 C ANISOU 2525 CA PRO B 42 4178 3489 9144 345 830 -3050 C ATOM 2526 C PRO B 42 16.351 55.970 48.634 1.00 48.88 C ANISOU 2526 C PRO B 42 4747 4005 9820 278 821 -3217 C ATOM 2527 O PRO B 42 17.324 56.126 47.890 1.00 47.76 O ANISOU 2527 O PRO B 42 4625 3778 9746 234 782 -3097 O ATOM 2528 CB PRO B 42 14.062 56.246 47.620 1.00 46.02 C ANISOU 2528 CB PRO B 42 4330 3507 9647 421 867 -3023 C ATOM 2529 CG PRO B 42 12.761 55.709 48.036 1.00 50.47 C ANISOU 2529 CG PRO B 42 4876 4189 10111 481 904 -3052 C ATOM 2530 CD PRO B 42 12.991 54.910 49.262 1.00 45.91 C ANISOU 2530 CD PRO B 42 4333 3845 9267 441 922 -3218 C ATOM 2531 N LYS B 43 16.305 56.435 49.886 1.00 46.65 N ANISOU 2531 N LYS B 43 4424 3758 9541 270 858 -3493 N ATOM 2532 CA LYS B 43 17.376 57.220 50.480 1.00 47.45 C ANISOU 2532 CA LYS B 43 4496 3789 9746 208 847 -3690 C ATOM 2533 C LYS B 43 18.371 56.417 51.328 1.00 55.87 C ANISOU 2533 C LYS B 43 5610 5074 10544 138 803 -3791 C ATOM 2534 O LYS B 43 19.410 56.968 51.706 1.00 57.57 O ANISOU 2534 O LYS B 43 5801 5239 10833 77 776 -3928 O ATOM 2535 CB LYS B 43 16.799 58.390 51.296 1.00 48.70 C ANISOU 2535 CB LYS B 43 4573 3824 10109 239 910 -3953 C ATOM 2536 CG LYS B 43 15.737 59.232 50.580 1.00 55.45 C ANISOU 2536 CG LYS B 43 5366 4454 11246 318 956 -3874 C ATOM 2537 CD LYS B 43 16.324 60.294 49.674 1.00 58.27 C ANISOU 2537 CD LYS B 43 5690 4542 11908 302 939 -3767 C ATOM 2538 CE LYS B 43 15.265 61.226 49.149 1.00 59.60 C ANISOU 2538 CE LYS B 43 5790 4486 12369 384 982 -3717 C ATOM 2539 NZ LYS B 43 15.517 62.635 49.552 1.00 66.70 N ANISOU 2539 NZ LYS B 43 6605 5167 13570 380 1023 -3947 N ATOM 2540 N GLN B 44 18.079 55.139 51.635 1.00 52.73 N ANISOU 2540 N GLN B 44 5273 4913 9848 146 792 -3725 N ATOM 2541 CA GLN B 44 18.967 54.365 52.499 1.00 52.32 C ANISOU 2541 CA GLN B 44 5265 5074 9540 87 747 -3816 C ATOM 2542 C GLN B 44 19.266 52.952 52.031 1.00 56.07 C ANISOU 2542 C GLN B 44 5818 5714 9771 73 699 -3594 C ATOM 2543 O GLN B 44 20.412 52.668 51.698 1.00 55.15 O ANISOU 2543 O GLN B 44 5724 5606 9625 21 641 -3519 O ATOM 2544 CB GLN B 44 18.425 54.335 53.946 1.00 53.65 C ANISOU 2544 CB GLN B 44 5423 5402 9560 101 789 -4067 C ATOM 2545 CG GLN B 44 18.680 55.599 54.752 1.00 70.25 C ANISOU 2545 CG GLN B 44 7457 7398 11839 85 813 -4359 C ATOM 2546 CD GLN B 44 18.227 55.443 56.182 1.00102.37 C ANISOU 2546 CD GLN B 44 11527 11659 15712 94 853 -4602 C ATOM 2547 OE1 GLN B 44 18.510 54.438 56.847 1.00103.23 O ANISOU 2547 OE1 GLN B 44 11691 12005 15526 68 820 -4611 O ATOM 2548 NE2 GLN B 44 17.517 56.442 56.694 1.00 93.53 N ANISOU 2548 NE2 GLN B 44 10345 10441 14752 134 927 -4804 N ATOM 2549 N TYR B 45 18.260 52.056 52.035 1.00 54.07 N ANISOU 2549 N TYR B 45 5600 5592 9353 119 725 -3497 N ATOM 2550 CA TYR B 45 18.448 50.630 51.720 1.00 54.50 C ANISOU 2550 CA TYR B 45 5727 5815 9165 107 685 -3308 C ATOM 2551 C TYR B 45 18.670 50.338 50.227 1.00 55.18 C ANISOU 2551 C TYR B 45 5841 5798 9326 110 652 -3043 C ATOM 2552 O TYR B 45 19.225 49.282 49.930 1.00 55.49 O ANISOU 2552 O TYR B 45 5937 5953 9193 84 608 -2910 O ATOM 2553 CB TYR B 45 17.331 49.762 52.342 1.00 57.33 C ANISOU 2553 CB TYR B 45 6109 6349 9326 147 729 -3309 C ATOM 2554 CG TYR B 45 17.415 49.857 53.850 1.00 62.99 C ANISOU 2554 CG TYR B 45 6818 7216 9899 130 751 -3554 C ATOM 2555 CD1 TYR B 45 16.667 50.803 54.550 1.00 65.75 C ANISOU 2555 CD1 TYR B 45 7109 7513 10360 161 820 -3765 C ATOM 2556 CD2 TYR B 45 18.379 49.143 54.558 1.00 65.28 C ANISOU 2556 CD2 TYR B 45 7154 7685 9966 81 697 -3589 C ATOM 2557 CE1 TYR B 45 16.838 50.996 55.921 1.00 67.74 C ANISOU 2557 CE1 TYR B 45 7355 7902 10482 142 839 -4008 C ATOM 2558 CE2 TYR B 45 18.562 49.332 55.930 1.00 66.97 C ANISOU 2558 CE2 TYR B 45 7361 8037 10047 63 706 -3820 C ATOM 2559 CZ TYR B 45 17.783 50.254 56.609 1.00 77.21 C ANISOU 2559 CZ TYR B 45 8606 9291 11439 92 779 -4033 C ATOM 2560 OH TYR B 45 17.948 50.436 57.963 1.00 82.31 O ANISOU 2560 OH TYR B 45 9250 10086 11939 74 791 -4270 O ATOM 2561 N ALA B 46 18.366 51.287 49.308 1.00 49.53 N ANISOU 2561 N ALA B 46 5087 4867 8865 137 670 -2972 N ATOM 2562 CA ALA B 46 18.659 51.103 47.881 1.00 48.86 C ANISOU 2562 CA ALA B 46 5030 4687 8847 136 639 -2726 C ATOM 2563 C ALA B 46 20.179 51.166 47.671 1.00 54.22 C ANISOU 2563 C ALA B 46 5720 5340 9539 67 596 -2711 C ATOM 2564 O ALA B 46 20.688 50.479 46.798 1.00 52.58 O ANISOU 2564 O ALA B 46 5559 5159 9259 51 564 -2524 O ATOM 2565 CB ALA B 46 17.971 52.161 47.038 1.00 49.09 C ANISOU 2565 CB ALA B 46 5013 4496 9143 184 668 -2657 C ATOM 2566 N TRP B 47 20.893 51.950 48.525 1.00 52.64 N ANISOU 2566 N TRP B 47 5475 5099 9428 26 595 -2921 N ATOM 2567 CA TRP B 47 22.346 52.120 48.523 1.00 53.00 C ANISOU 2567 CA TRP B 47 5511 5120 9507 -44 554 -2949 C ATOM 2568 C TRP B 47 23.093 50.962 49.153 1.00 53.39 C ANISOU 2568 C TRP B 47 5605 5391 9289 -81 503 -2967 C ATOM 2569 O TRP B 47 24.172 50.624 48.675 1.00 52.14 O ANISOU 2569 O TRP B 47 5459 5239 9111 -125 464 -2873 O ATOM 2570 CB TRP B 47 22.734 53.425 49.193 1.00 53.00 C ANISOU 2570 CB TRP B 47 5436 4985 9714 -73 567 -3178 C ATOM 2571 CG TRP B 47 22.341 54.606 48.376 1.00 55.41 C ANISOU 2571 CG TRP B 47 5695 5036 10323 -48 609 -3123 C ATOM 2572 CD1 TRP B 47 21.278 55.434 48.588 1.00 58.68 C ANISOU 2572 CD1 TRP B 47 6065 5335 10896 6 659 -3215 C ATOM 2573 CD2 TRP B 47 22.959 55.044 47.162 1.00 55.88 C ANISOU 2573 CD2 TRP B 47 5748 4925 10561 -70 606 -2941 C ATOM 2574 NE1 TRP B 47 21.234 56.403 47.614 1.00 58.74 N ANISOU 2574 NE1 TRP B 47 6036 5101 11180 19 681 -3105 N ATOM 2575 CE2 TRP B 47 22.263 56.196 46.731 1.00 60.37 C ANISOU 2575 CE2 TRP B 47 6267 5272 11401 -30 651 -2934 C ATOM 2576 CE3 TRP B 47 24.057 54.593 46.410 1.00 57.47 C ANISOU 2576 CE3 TRP B 47 5976 5138 10723 -120 575 -2785 C ATOM 2577 CZ2 TRP B 47 22.608 56.884 45.563 1.00 59.88 C ANISOU 2577 CZ2 TRP B 47 6188 5004 11559 -38 664 -2760 C ATOM 2578 CZ3 TRP B 47 24.400 55.276 45.254 1.00 59.38 C ANISOU 2578 CZ3 TRP B 47 6200 5182 11177 -131 596 -2622 C ATOM 2579 CH2 TRP B 47 23.683 56.410 44.843 1.00 60.12 C ANISOU 2579 CH2 TRP B 47 6251 5061 11530 -91 638 -2606 C ATOM 2580 N VAL B 48 22.528 50.362 50.225 1.00 48.41 N ANISOU 2580 N VAL B 48 4994 4941 8458 -62 507 -3081 N ATOM 2581 CA VAL B 48 23.063 49.177 50.906 1.00 47.47 C ANISOU 2581 CA VAL B 48 4922 5048 8068 -86 460 -3086 C ATOM 2582 C VAL B 48 23.060 48.050 49.855 1.00 48.29 C ANISOU 2582 C VAL B 48 5085 5196 8067 -74 443 -2825 C ATOM 2583 O VAL B 48 24.046 47.315 49.729 1.00 49.05 O ANISOU 2583 O VAL B 48 5208 5373 8058 -109 394 -2754 O ATOM 2584 CB VAL B 48 22.229 48.812 52.167 1.00 51.97 C ANISOU 2584 CB VAL B 48 5504 5789 8453 -58 486 -3229 C ATOM 2585 CG1 VAL B 48 22.799 47.593 52.880 1.00 52.03 C ANISOU 2585 CG1 VAL B 48 5560 6026 8184 -83 434 -3224 C ATOM 2586 CG2 VAL B 48 22.154 49.988 53.130 1.00 51.95 C ANISOU 2586 CG2 VAL B 48 5442 5729 8567 -63 514 -3495 C ATOM 2587 N LEU B 49 21.974 47.995 49.047 1.00 41.48 N ANISOU 2587 N LEU B 49 4238 4267 7255 -23 482 -2688 N ATOM 2588 CA LEU B 49 21.776 47.062 47.933 1.00 39.70 C ANISOU 2588 CA LEU B 49 4065 4060 6958 -4 472 -2449 C ATOM 2589 C LEU B 49 22.821 47.280 46.803 1.00 41.90 C ANISOU 2589 C LEU B 49 4347 4223 7352 -37 449 -2315 C ATOM 2590 O LEU B 49 23.398 46.305 46.326 1.00 40.69 O ANISOU 2590 O LEU B 49 4239 4149 7074 -52 419 -2182 O ATOM 2591 CB LEU B 49 20.326 47.162 47.410 1.00 38.95 C ANISOU 2591 CB LEU B 49 3970 3908 6922 57 514 -2369 C ATOM 2592 CG LEU B 49 19.953 46.313 46.191 1.00 42.18 C ANISOU 2592 CG LEU B 49 4427 4322 7276 81 501 -2133 C ATOM 2593 CD1 LEU B 49 20.266 44.821 46.422 1.00 40.72 C ANISOU 2593 CD1 LEU B 49 4302 4326 6844 65 470 -2064 C ATOM 2594 CD2 LEU B 49 18.487 46.553 45.790 1.00 42.79 C ANISOU 2594 CD2 LEU B 49 4486 4339 7431 142 534 -2083 C ATOM 2595 N ILE B 50 23.059 48.548 46.392 1.00 37.88 N ANISOU 2595 N ILE B 50 3788 3523 7083 -48 469 -2348 N ATOM 2596 CA ILE B 50 24.066 48.901 45.381 1.00 37.70 C ANISOU 2596 CA ILE B 50 3758 3379 7188 -84 461 -2230 C ATOM 2597 C ILE B 50 25.480 48.484 45.863 1.00 41.64 C ANISOU 2597 C ILE B 50 4251 3970 7601 -145 417 -2292 C ATOM 2598 O ILE B 50 26.221 47.846 45.106 1.00 42.10 O ANISOU 2598 O ILE B 50 4338 4052 7606 -166 401 -2147 O ATOM 2599 CB ILE B 50 23.980 50.421 45.015 1.00 40.09 C ANISOU 2599 CB ILE B 50 4000 3451 7782 -84 496 -2268 C ATOM 2600 CG1 ILE B 50 22.674 50.713 44.249 1.00 40.14 C ANISOU 2600 CG1 ILE B 50 4016 3364 7874 -17 529 -2149 C ATOM 2601 CG2 ILE B 50 25.223 50.899 44.216 1.00 38.23 C ANISOU 2601 CG2 ILE B 50 3745 3093 7688 -137 495 -2181 C ATOM 2602 CD1 ILE B 50 22.182 52.154 44.298 1.00 44.16 C ANISOU 2602 CD1 ILE B 50 4458 3671 8649 4 566 -2238 C ATOM 2603 N ALA B 51 25.828 48.831 47.126 1.00 37.08 N ANISOU 2603 N ALA B 51 3634 3449 7006 -172 398 -2513 N ATOM 2604 CA ALA B 51 27.121 48.531 47.753 1.00 36.48 C ANISOU 2604 CA ALA B 51 3539 3467 6855 -229 345 -2603 C ATOM 2605 C ALA B 51 27.414 47.014 47.786 1.00 40.69 C ANISOU 2605 C ALA B 51 4132 4192 7136 -224 305 -2492 C ATOM 2606 O ALA B 51 28.529 46.614 47.442 1.00 39.87 O ANISOU 2606 O ALA B 51 4023 4108 7016 -260 273 -2427 O ATOM 2607 CB ALA B 51 27.186 49.132 49.155 1.00 36.68 C ANISOU 2607 CB ALA B 51 3520 3539 6879 -248 327 -2866 C ATOM 2608 N ALA B 52 26.400 46.182 48.150 1.00 37.49 N ANISOU 2608 N ALA B 52 3778 3916 6550 -178 313 -2465 N ATOM 2609 CA ALA B 52 26.479 44.712 48.233 1.00 36.90 C ANISOU 2609 CA ALA B 52 3762 4016 6243 -167 282 -2358 C ATOM 2610 C ALA B 52 26.771 44.102 46.856 1.00 42.59 C ANISOU 2610 C ALA B 52 4518 4688 6976 -163 287 -2137 C ATOM 2611 O ALA B 52 27.588 43.183 46.736 1.00 41.41 O ANISOU 2611 O ALA B 52 4389 4628 6719 -180 251 -2065 O ATOM 2612 CB ALA B 52 25.181 44.146 48.795 1.00 36.80 C ANISOU 2612 CB ALA B 52 3786 4110 6085 -121 306 -2367 C ATOM 2613 N TYR B 53 26.126 44.659 45.817 1.00 39.78 N ANISOU 2613 N TYR B 53 4166 4190 6758 -139 330 -2035 N ATOM 2614 CA TYR B 53 26.285 44.269 44.424 1.00 39.01 C ANISOU 2614 CA TYR B 53 4103 4034 6685 -132 343 -1832 C ATOM 2615 C TYR B 53 27.631 44.734 43.871 1.00 43.03 C ANISOU 2615 C TYR B 53 4579 4455 7317 -181 340 -1803 C ATOM 2616 O TYR B 53 28.231 44.003 43.099 1.00 43.20 O ANISOU 2616 O TYR B 53 4629 4508 7278 -190 335 -1671 O ATOM 2617 CB TYR B 53 25.126 44.827 43.587 1.00 39.39 C ANISOU 2617 CB TYR B 53 4161 3963 6843 -89 383 -1744 C ATOM 2618 CG TYR B 53 24.044 43.825 43.261 1.00 39.54 C ANISOU 2618 CG TYR B 53 4236 4070 6719 -43 383 -1635 C ATOM 2619 CD1 TYR B 53 24.238 42.861 42.284 1.00 41.22 C ANISOU 2619 CD1 TYR B 53 4500 4324 6836 -39 373 -1467 C ATOM 2620 CD2 TYR B 53 22.799 43.888 43.877 1.00 40.00 C ANISOU 2620 CD2 TYR B 53 4288 4160 6750 -5 399 -1703 C ATOM 2621 CE1 TYR B 53 23.232 41.968 41.939 1.00 41.94 C ANISOU 2621 CE1 TYR B 53 4637 4486 6811 -1 369 -1374 C ATOM 2622 CE2 TYR B 53 21.784 42.991 43.545 1.00 40.59 C ANISOU 2622 CE2 TYR B 53 4404 4307 6713 33 399 -1601 C ATOM 2623 CZ TYR B 53 22.016 42.019 42.586 1.00 49.43 C ANISOU 2623 CZ TYR B 53 5576 5467 7740 33 380 -1440 C ATOM 2624 OH TYR B 53 21.030 41.134 42.225 1.00 51.75 O ANISOU 2624 OH TYR B 53 5906 5825 7933 65 376 -1347 O ATOM 2625 N VAL B 54 28.103 45.940 44.275 1.00 40.54 N ANISOU 2625 N VAL B 54 4196 4027 7179 -215 347 -1933 N ATOM 2626 CA VAL B 54 29.409 46.510 43.884 1.00 39.77 C ANISOU 2626 CA VAL B 54 4050 3836 7227 -270 349 -1929 C ATOM 2627 C VAL B 54 30.551 45.669 44.480 1.00 42.90 C ANISOU 2627 C VAL B 54 4434 4372 7494 -305 295 -1976 C ATOM 2628 O VAL B 54 31.462 45.281 43.744 1.00 43.73 O ANISOU 2628 O VAL B 54 4538 4472 7607 -328 299 -1866 O ATOM 2629 CB VAL B 54 29.539 48.035 44.198 1.00 42.84 C ANISOU 2629 CB VAL B 54 4364 4056 7856 -300 369 -2064 C ATOM 2630 CG1 VAL B 54 30.981 48.513 44.075 1.00 42.81 C ANISOU 2630 CG1 VAL B 54 4296 3981 7988 -368 362 -2093 C ATOM 2631 CG2 VAL B 54 28.636 48.861 43.285 1.00 42.05 C ANISOU 2631 CG2 VAL B 54 4273 3789 7917 -265 424 -1961 C ATOM 2632 N ALA B 55 30.466 45.345 45.793 1.00 37.42 N ANISOU 2632 N ALA B 55 3733 3812 6672 -304 248 -2132 N ATOM 2633 CA ALA B 55 31.447 44.510 46.501 1.00 36.51 C ANISOU 2633 CA ALA B 55 3607 3847 6419 -329 184 -2180 C ATOM 2634 C ALA B 55 31.614 43.136 45.812 1.00 39.07 C ANISOU 2634 C ALA B 55 3989 4265 6593 -305 179 -1998 C ATOM 2635 O ALA B 55 32.729 42.729 45.511 1.00 39.22 O ANISOU 2635 O ALA B 55 3984 4303 6614 -332 157 -1950 O ATOM 2636 CB ALA B 55 31.022 44.329 47.953 1.00 36.71 C ANISOU 2636 CB ALA B 55 3635 4013 6301 -318 141 -2348 C ATOM 2637 N VAL B 56 30.491 42.476 45.505 1.00 34.50 N ANISOU 2637 N VAL B 56 3479 3729 5902 -256 202 -1900 N ATOM 2638 CA VAL B 56 30.411 41.158 44.849 1.00 33.46 C ANISOU 2638 CA VAL B 56 3409 3677 5628 -229 202 -1737 C ATOM 2639 C VAL B 56 30.944 41.215 43.404 1.00 36.65 C ANISOU 2639 C VAL B 56 3817 3976 6130 -239 241 -1585 C ATOM 2640 O VAL B 56 31.716 40.346 43.012 1.00 36.56 O ANISOU 2640 O VAL B 56 3817 4021 6054 -244 229 -1504 O ATOM 2641 CB VAL B 56 28.971 40.601 44.972 1.00 36.46 C ANISOU 2641 CB VAL B 56 3849 4116 5887 -179 218 -1697 C ATOM 2642 CG1 VAL B 56 28.596 39.716 43.811 1.00 36.96 C ANISOU 2642 CG1 VAL B 56 3972 4181 5892 -152 239 -1514 C ATOM 2643 CG2 VAL B 56 28.784 39.868 46.285 1.00 35.70 C ANISOU 2643 CG2 VAL B 56 3765 4184 5617 -170 176 -1787 C ATOM 2644 N PHE B 57 30.581 42.261 42.641 1.00 33.19 N ANISOU 2644 N PHE B 57 3369 3388 5854 -241 290 -1549 N ATOM 2645 CA PHE B 57 31.036 42.482 41.266 1.00 32.99 C ANISOU 2645 CA PHE B 57 3349 3258 5927 -252 336 -1402 C ATOM 2646 C PHE B 57 32.575 42.576 41.202 1.00 38.07 C ANISOU 2646 C PHE B 57 3934 3886 6643 -303 332 -1420 C ATOM 2647 O PHE B 57 33.187 41.908 40.369 1.00 38.33 O ANISOU 2647 O PHE B 57 3985 3940 6637 -306 352 -1300 O ATOM 2648 CB PHE B 57 30.378 43.760 40.702 1.00 34.11 C ANISOU 2648 CB PHE B 57 3479 3236 6245 -246 382 -1381 C ATOM 2649 CG PHE B 57 30.802 44.199 39.321 1.00 34.82 C ANISOU 2649 CG PHE B 57 3574 3209 6449 -259 436 -1227 C ATOM 2650 CD1 PHE B 57 30.223 43.636 38.187 1.00 36.02 C ANISOU 2650 CD1 PHE B 57 3795 3371 6520 -222 460 -1058 C ATOM 2651 CD2 PHE B 57 31.726 45.226 39.154 1.00 35.61 C ANISOU 2651 CD2 PHE B 57 3608 3185 6739 -309 465 -1251 C ATOM 2652 CE1 PHE B 57 30.599 44.055 36.908 1.00 36.13 C ANISOU 2652 CE1 PHE B 57 3818 3288 6620 -233 512 -911 C ATOM 2653 CE2 PHE B 57 32.099 45.648 37.876 1.00 38.48 C ANISOU 2653 CE2 PHE B 57 3976 3440 7202 -322 525 -1097 C ATOM 2654 CZ PHE B 57 31.526 45.063 36.760 1.00 36.23 C ANISOU 2654 CZ PHE B 57 3767 3180 6816 -282 549 -925 C ATOM 2655 N VAL B 58 33.185 43.384 42.105 1.00 34.33 N ANISOU 2655 N VAL B 58 3385 3382 6275 -344 306 -1577 N ATOM 2656 CA VAL B 58 34.639 43.600 42.169 1.00 33.46 C ANISOU 2656 CA VAL B 58 3201 3252 6260 -399 294 -1618 C ATOM 2657 C VAL B 58 35.373 42.333 42.623 1.00 37.04 C ANISOU 2657 C VAL B 58 3655 3864 6553 -395 239 -1620 C ATOM 2658 O VAL B 58 36.310 41.918 41.952 1.00 37.29 O ANISOU 2658 O VAL B 58 3667 3895 6606 -412 257 -1534 O ATOM 2659 CB VAL B 58 35.037 44.855 42.997 1.00 36.31 C ANISOU 2659 CB VAL B 58 3476 3527 6793 -447 275 -1797 C ATOM 2660 CG1 VAL B 58 36.562 44.986 43.093 1.00 36.14 C ANISOU 2660 CG1 VAL B 58 3368 3496 6870 -507 255 -1842 C ATOM 2661 CG2 VAL B 58 34.432 46.125 42.398 1.00 35.70 C ANISOU 2661 CG2 VAL B 58 3390 3264 6908 -451 338 -1774 C ATOM 2662 N VAL B 59 34.937 41.710 43.733 1.00 33.27 N ANISOU 2662 N VAL B 59 3200 3523 5918 -371 177 -1709 N ATOM 2663 CA VAL B 59 35.563 40.490 44.252 1.00 32.46 C ANISOU 2663 CA VAL B 59 3100 3571 5661 -361 117 -1703 C ATOM 2664 C VAL B 59 35.480 39.342 43.218 1.00 36.58 C ANISOU 2664 C VAL B 59 3684 4124 6089 -326 151 -1523 C ATOM 2665 O VAL B 59 36.489 38.667 42.989 1.00 37.13 O ANISOU 2665 O VAL B 59 3728 4236 6145 -334 137 -1478 O ATOM 2666 CB VAL B 59 35.020 40.117 45.659 1.00 35.80 C ANISOU 2666 CB VAL B 59 3541 4133 5928 -341 51 -1822 C ATOM 2667 CG1 VAL B 59 35.551 38.760 46.137 1.00 35.44 C ANISOU 2667 CG1 VAL B 59 3508 4242 5715 -321 -10 -1783 C ATOM 2668 CG2 VAL B 59 35.352 41.221 46.674 1.00 35.11 C ANISOU 2668 CG2 VAL B 59 3382 4026 5931 -381 11 -2019 C ATOM 2669 N ALA B 60 34.315 39.164 42.552 1.00 31.48 N ANISOU 2669 N ALA B 60 3114 3452 5395 -289 195 -1428 N ATOM 2670 CA ALA B 60 34.153 38.127 41.528 1.00 29.37 C ANISOU 2670 CA ALA B 60 2908 3209 5040 -258 227 -1272 C ATOM 2671 C ALA B 60 35.040 38.327 40.287 1.00 35.07 C ANISOU 2671 C ALA B 60 3609 3845 5869 -280 284 -1172 C ATOM 2672 O ALA B 60 35.663 37.363 39.848 1.00 34.82 O ANISOU 2672 O ALA B 60 3587 3868 5776 -271 288 -1101 O ATOM 2673 CB ALA B 60 32.704 37.984 41.126 1.00 28.96 C ANISOU 2673 CB ALA B 60 2932 3148 4924 -218 252 -1208 C ATOM 2674 N LEU B 61 35.120 39.557 39.729 1.00 33.10 N ANISOU 2674 N LEU B 61 3331 3462 5783 -309 334 -1165 N ATOM 2675 CA LEU B 61 35.951 39.800 38.543 1.00 33.96 C ANISOU 2675 CA LEU B 61 3420 3491 5991 -333 401 -1060 C ATOM 2676 C LEU B 61 37.431 39.642 38.830 1.00 36.46 C ANISOU 2676 C LEU B 61 3654 3831 6367 -372 387 -1107 C ATOM 2677 O LEU B 61 38.133 39.015 38.038 1.00 35.98 O ANISOU 2677 O LEU B 61 3594 3787 6290 -371 426 -1016 O ATOM 2678 CB LEU B 61 35.657 41.146 37.853 1.00 34.69 C ANISOU 2678 CB LEU B 61 3503 3429 6249 -354 461 -1021 C ATOM 2679 CG LEU B 61 34.262 41.317 37.199 1.00 40.21 C ANISOU 2679 CG LEU B 61 4281 4089 6908 -311 485 -932 C ATOM 2680 CD1 LEU B 61 34.131 42.689 36.589 1.00 40.05 C ANISOU 2680 CD1 LEU B 61 4238 3909 7071 -332 538 -892 C ATOM 2681 CD2 LEU B 61 33.996 40.254 36.130 1.00 42.88 C ANISOU 2681 CD2 LEU B 61 4698 4487 7107 -276 512 -785 C ATOM 2682 N VAL B 62 37.902 40.157 39.977 1.00 32.92 N ANISOU 2682 N VAL B 62 3133 3393 5984 -404 329 -1255 N ATOM 2683 CA VAL B 62 39.322 40.048 40.356 1.00 32.51 C ANISOU 2683 CA VAL B 62 2986 3368 5998 -443 300 -1315 C ATOM 2684 C VAL B 62 39.671 38.577 40.647 1.00 35.85 C ANISOU 2684 C VAL B 62 3428 3934 6259 -406 251 -1287 C ATOM 2685 O VAL B 62 40.558 38.027 40.003 1.00 35.55 O ANISOU 2685 O VAL B 62 3363 3905 6240 -409 282 -1215 O ATOM 2686 CB VAL B 62 39.708 40.999 41.522 1.00 35.37 C ANISOU 2686 CB VAL B 62 3263 3709 6469 -488 239 -1493 C ATOM 2687 CG1 VAL B 62 41.162 40.782 41.944 1.00 35.36 C ANISOU 2687 CG1 VAL B 62 3159 3751 6524 -524 193 -1555 C ATOM 2688 CG2 VAL B 62 39.462 42.462 41.146 1.00 34.49 C ANISOU 2688 CG2 VAL B 62 3124 3430 6551 -526 296 -1515 C ATOM 2689 N GLY B 63 38.923 37.961 41.561 1.00 31.90 N ANISOU 2689 N GLY B 63 2976 3539 5608 -370 185 -1336 N ATOM 2690 CA GLY B 63 39.119 36.583 41.979 1.00 31.56 C ANISOU 2690 CA GLY B 63 2954 3627 5411 -333 131 -1310 C ATOM 2691 C GLY B 63 39.122 35.571 40.856 1.00 35.96 C ANISOU 2691 C GLY B 63 3565 4191 5908 -299 187 -1164 C ATOM 2692 O GLY B 63 39.991 34.695 40.815 1.00 36.71 O ANISOU 2692 O GLY B 63 3628 4341 5979 -288 170 -1134 O ATOM 2693 N ASN B 64 38.150 35.684 39.939 1.00 32.17 N ANISOU 2693 N ASN B 64 3163 3656 5405 -281 250 -1077 N ATOM 2694 CA ASN B 64 37.987 34.753 38.827 1.00 31.20 C ANISOU 2694 CA ASN B 64 3103 3542 5212 -249 302 -949 C ATOM 2695 C ASN B 64 39.006 34.961 37.712 1.00 34.71 C ANISOU 2695 C ASN B 64 3508 3921 5761 -272 378 -882 C ATOM 2696 O ASN B 64 39.362 33.985 37.050 1.00 33.78 O ANISOU 2696 O ASN B 64 3410 3838 5586 -248 407 -810 O ATOM 2697 CB ASN B 64 36.559 34.750 38.311 1.00 28.38 C ANISOU 2697 CB ASN B 64 2838 3164 4780 -220 328 -888 C ATOM 2698 CG ASN B 64 35.619 34.047 39.255 1.00 39.09 C ANISOU 2698 CG ASN B 64 4240 4610 6003 -187 266 -925 C ATOM 2699 OD1 ASN B 64 35.690 32.831 39.439 1.00 32.27 O ANISOU 2699 OD1 ASN B 64 3400 3828 5035 -159 237 -897 O ATOM 2700 ND2 ASN B 64 34.718 34.792 39.887 1.00 26.87 N ANISOU 2700 ND2 ASN B 64 2702 3047 4462 -190 248 -989 N ATOM 2701 N THR B 65 39.501 36.202 37.520 1.00 32.39 N ANISOU 2701 N THR B 65 3153 3531 5625 -320 415 -908 N ATOM 2702 CA THR B 65 40.563 36.502 36.548 1.00 32.41 C ANISOU 2702 CA THR B 65 3103 3468 5742 -351 496 -847 C ATOM 2703 C THR B 65 41.837 35.826 37.056 1.00 36.45 C ANISOU 2703 C THR B 65 3529 4045 6275 -358 460 -895 C ATOM 2704 O THR B 65 42.546 35.193 36.272 1.00 37.13 O ANISOU 2704 O THR B 65 3603 4143 6363 -349 515 -826 O ATOM 2705 CB THR B 65 40.746 38.021 36.351 1.00 35.90 C ANISOU 2705 CB THR B 65 3494 3784 6361 -405 541 -866 C ATOM 2706 OG1 THR B 65 39.558 38.543 35.773 1.00 37.85 O ANISOU 2706 OG1 THR B 65 3823 3972 6586 -388 575 -800 O ATOM 2707 CG2 THR B 65 41.907 38.360 35.441 1.00 31.20 C ANISOU 2707 CG2 THR B 65 2833 3124 5897 -445 629 -804 C ATOM 2708 N LEU B 66 42.084 35.915 38.381 1.00 31.99 N ANISOU 2708 N LEU B 66 2907 3531 5717 -369 363 -1015 N ATOM 2709 CA LEU B 66 43.248 35.314 39.030 1.00 31.35 C ANISOU 2709 CA LEU B 66 2737 3520 5656 -371 304 -1068 C ATOM 2710 C LEU B 66 43.262 33.791 38.913 1.00 34.24 C ANISOU 2710 C LEU B 66 3147 3979 5884 -313 286 -1004 C ATOM 2711 O LEU B 66 44.329 33.211 38.748 1.00 34.52 O ANISOU 2711 O LEU B 66 3114 4039 5962 -309 290 -991 O ATOM 2712 CB LEU B 66 43.360 35.758 40.495 1.00 31.31 C ANISOU 2712 CB LEU B 66 2674 3561 5662 -392 193 -1211 C ATOM 2713 CG LEU B 66 43.671 37.240 40.747 1.00 35.11 C ANISOU 2713 CG LEU B 66 3080 3946 6314 -456 199 -1306 C ATOM 2714 CD1 LEU B 66 43.808 37.502 42.213 1.00 35.41 C ANISOU 2714 CD1 LEU B 66 3067 4053 6335 -471 83 -1459 C ATOM 2715 CD2 LEU B 66 44.922 37.702 40.020 1.00 35.42 C ANISOU 2715 CD2 LEU B 66 3018 3906 6535 -504 264 -1282 C ATOM 2716 N VAL B 67 42.081 33.149 38.956 1.00 29.69 N ANISOU 2716 N VAL B 67 2677 3446 5158 -270 272 -964 N ATOM 2717 CA VAL B 67 41.947 31.696 38.800 1.00 27.90 C ANISOU 2717 CA VAL B 67 2501 3292 4809 -215 260 -900 C ATOM 2718 C VAL B 67 42.342 31.320 37.367 1.00 32.19 C ANISOU 2718 C VAL B 67 3060 3791 5381 -207 364 -805 C ATOM 2719 O VAL B 67 43.147 30.407 37.182 1.00 31.89 O ANISOU 2719 O VAL B 67 2987 3787 5345 -183 369 -781 O ATOM 2720 CB VAL B 67 40.533 31.185 39.176 1.00 28.89 C ANISOU 2720 CB VAL B 67 2730 3464 4783 -179 225 -884 C ATOM 2721 CG1 VAL B 67 40.358 29.703 38.829 1.00 27.36 C ANISOU 2721 CG1 VAL B 67 2590 3322 4484 -128 227 -809 C ATOM 2722 CG2 VAL B 67 40.245 31.429 40.650 1.00 28.11 C ANISOU 2722 CG2 VAL B 67 2612 3430 4639 -184 127 -980 C ATOM 2723 N CYS B 68 41.785 32.036 36.368 1.00 29.61 N ANISOU 2723 N CYS B 68 2784 3389 5076 -224 446 -751 N ATOM 2724 CA CYS B 68 42.079 31.829 34.951 1.00 30.91 C ANISOU 2724 CA CYS B 68 2974 3516 5252 -220 553 -659 C ATOM 2725 C CYS B 68 43.559 32.020 34.659 1.00 35.80 C ANISOU 2725 C CYS B 68 3486 4111 6006 -249 603 -666 C ATOM 2726 O CYS B 68 44.136 31.180 33.977 1.00 34.97 O ANISOU 2726 O CYS B 68 3375 4029 5885 -225 655 -623 O ATOM 2727 CB CYS B 68 41.217 32.727 34.074 1.00 31.91 C ANISOU 2727 CB CYS B 68 3170 3573 5381 -236 617 -599 C ATOM 2728 SG CYS B 68 39.453 32.351 34.163 1.00 36.39 S ANISOU 2728 SG CYS B 68 3861 4171 5795 -195 571 -577 S ATOM 2729 N LEU B 69 44.176 33.085 35.220 1.00 33.04 N ANISOU 2729 N LEU B 69 3043 3716 5793 -300 585 -731 N ATOM 2730 CA LEU B 69 45.590 33.392 35.046 1.00 33.46 C ANISOU 2730 CA LEU B 69 2975 3740 5999 -336 626 -748 C ATOM 2731 C LEU B 69 46.530 32.361 35.698 1.00 35.82 C ANISOU 2731 C LEU B 69 3195 4116 6298 -309 562 -792 C ATOM 2732 O LEU B 69 47.506 31.958 35.072 1.00 35.51 O ANISOU 2732 O LEU B 69 3094 4073 6323 -306 628 -760 O ATOM 2733 CB LEU B 69 45.905 34.815 35.539 1.00 34.14 C ANISOU 2733 CB LEU B 69 2981 3750 6239 -402 613 -816 C ATOM 2734 CG LEU B 69 45.568 35.956 34.572 1.00 39.80 C ANISOU 2734 CG LEU B 69 3729 4358 7035 -441 716 -748 C ATOM 2735 CD1 LEU B 69 45.687 37.318 35.269 1.00 39.90 C ANISOU 2735 CD1 LEU B 69 3669 4290 7203 -501 682 -835 C ATOM 2736 CD2 LEU B 69 46.471 35.920 33.329 1.00 42.63 C ANISOU 2736 CD2 LEU B 69 4053 4679 7465 -458 847 -656 C ATOM 2737 N ALA B 70 46.219 31.937 36.942 1.00 31.37 N ANISOU 2737 N ALA B 70 2634 3624 5662 -285 437 -859 N ATOM 2738 CA ALA B 70 46.992 30.983 37.734 1.00 30.10 C ANISOU 2738 CA ALA B 70 2403 3542 5491 -253 353 -895 C ATOM 2739 C ALA B 70 47.147 29.641 37.031 1.00 36.19 C ANISOU 2739 C ALA B 70 3210 4344 6196 -196 398 -819 C ATOM 2740 O ALA B 70 48.239 29.074 37.029 1.00 37.02 O ANISOU 2740 O ALA B 70 3224 4469 6373 -180 397 -822 O ATOM 2741 CB ALA B 70 46.341 30.783 39.105 1.00 29.75 C ANISOU 2741 CB ALA B 70 2387 3574 5342 -235 221 -959 C ATOM 2742 N VAL B 71 46.059 29.131 36.449 1.00 32.98 N ANISOU 2742 N VAL B 71 2930 3940 5662 -164 435 -757 N ATOM 2743 CA VAL B 71 46.014 27.841 35.757 1.00 33.04 C ANISOU 2743 CA VAL B 71 2986 3970 5597 -110 478 -695 C ATOM 2744 C VAL B 71 46.690 27.928 34.394 1.00 41.54 C ANISOU 2744 C VAL B 71 4041 4997 6743 -120 613 -648 C ATOM 2745 O VAL B 71 47.573 27.122 34.097 1.00 41.77 O ANISOU 2745 O VAL B 71 4013 5040 6816 -92 644 -640 O ATOM 2746 CB VAL B 71 44.564 27.275 35.701 1.00 35.38 C ANISOU 2746 CB VAL B 71 3419 4288 5735 -77 457 -659 C ATOM 2747 CG1 VAL B 71 44.488 25.962 34.920 1.00 35.37 C ANISOU 2747 CG1 VAL B 71 3470 4299 5669 -26 505 -606 C ATOM 2748 CG2 VAL B 71 43.995 27.092 37.106 1.00 34.78 C ANISOU 2748 CG2 VAL B 71 3354 4271 5588 -64 332 -702 C ATOM 2749 N TRP B 72 46.304 28.920 33.585 1.00 42.01 N ANISOU 2749 N TRP B 72 4142 5000 6819 -160 696 -614 N ATOM 2750 CA TRP B 72 46.836 29.143 32.248 1.00 44.84 C ANISOU 2750 CA TRP B 72 4494 5318 7226 -176 835 -557 C ATOM 2751 C TRP B 72 48.383 29.333 32.221 1.00 45.58 C ANISOU 2751 C TRP B 72 4440 5395 7484 -201 880 -583 C ATOM 2752 O TRP B 72 49.047 28.730 31.374 1.00 44.82 O ANISOU 2752 O TRP B 72 4321 5304 7404 -181 974 -551 O ATOM 2753 CB TRP B 72 46.071 30.316 31.581 1.00 46.45 C ANISOU 2753 CB TRP B 72 4766 5462 7420 -216 896 -509 C ATOM 2754 CG TRP B 72 46.647 30.866 30.311 1.00 49.97 C ANISOU 2754 CG TRP B 72 5197 5862 7929 -247 1040 -441 C ATOM 2755 CD1 TRP B 72 47.179 30.162 29.270 1.00 53.46 C ANISOU 2755 CD1 TRP B 72 5647 6325 8341 -224 1144 -397 C ATOM 2756 CD2 TRP B 72 46.660 32.238 29.910 1.00 51.32 C ANISOU 2756 CD2 TRP B 72 5351 5955 8191 -304 1101 -404 C ATOM 2757 NE1 TRP B 72 47.652 31.025 28.308 1.00 53.75 N ANISOU 2757 NE1 TRP B 72 5662 6313 8449 -267 1269 -335 N ATOM 2758 CE2 TRP B 72 47.323 32.305 28.661 1.00 55.92 C ANISOU 2758 CE2 TRP B 72 5923 6522 8801 -317 1245 -330 C ATOM 2759 CE3 TRP B 72 46.213 33.435 30.506 1.00 54.02 C ANISOU 2759 CE3 TRP B 72 5681 6236 8607 -347 1053 -428 C ATOM 2760 CZ2 TRP B 72 47.549 33.516 27.992 1.00 56.28 C ANISOU 2760 CZ2 TRP B 72 5948 6492 8942 -373 1341 -265 C ATOM 2761 CZ3 TRP B 72 46.446 34.640 29.848 1.00 56.42 C ANISOU 2761 CZ3 TRP B 72 5961 6454 9022 -401 1144 -371 C ATOM 2762 CH2 TRP B 72 47.100 34.674 28.604 1.00 57.22 C ANISOU 2762 CH2 TRP B 72 6054 6540 9146 -414 1287 -283 C ATOM 2763 N ARG B 73 48.946 30.110 33.163 1.00 39.59 N ANISOU 2763 N ARG B 73 3578 4621 6845 -242 811 -647 N ATOM 2764 CA ARG B 73 50.376 30.428 33.171 1.00 38.46 C ANISOU 2764 CA ARG B 73 3281 4455 6876 -275 848 -677 C ATOM 2765 C ARG B 73 51.282 29.488 34.024 1.00 40.77 C ANISOU 2765 C ARG B 73 3469 4809 7214 -237 757 -732 C ATOM 2766 O ARG B 73 52.494 29.693 34.052 1.00 40.98 O ANISOU 2766 O ARG B 73 3357 4821 7393 -261 781 -759 O ATOM 2767 CB ARG B 73 50.600 31.910 33.569 1.00 37.78 C ANISOU 2767 CB ARG B 73 3125 4304 6926 -352 836 -719 C ATOM 2768 CG ARG B 73 49.767 32.967 32.802 1.00 53.30 C ANISOU 2768 CG ARG B 73 5177 6194 8879 -391 920 -659 C ATOM 2769 CD ARG B 73 49.812 32.861 31.273 1.00 74.20 C ANISOU 2769 CD ARG B 73 7879 8817 11495 -386 1079 -551 C ATOM 2770 NE ARG B 73 51.051 33.386 30.688 1.00 93.09 N ANISOU 2770 NE ARG B 73 10153 11162 14054 -434 1191 -531 N ATOM 2771 CZ ARG B 73 51.156 34.568 30.082 1.00114.89 C ANISOU 2771 CZ ARG B 73 12898 13839 16918 -496 1283 -481 C ATOM 2772 NH1 ARG B 73 50.097 35.364 29.973 1.00108.57 N ANISOU 2772 NH1 ARG B 73 12191 12988 16073 -513 1273 -445 N ATOM 2773 NH2 ARG B 73 52.322 34.965 29.588 1.00 99.95 N ANISOU 2773 NH2 ARG B 73 10889 11906 15183 -541 1390 -461 N ATOM 2774 N ASN B 74 50.730 28.465 34.679 1.00 36.49 N ANISOU 2774 N ASN B 74 2986 4330 6550 -178 658 -740 N ATOM 2775 CA ASN B 74 51.537 27.517 35.454 1.00 35.57 C ANISOU 2775 CA ASN B 74 2777 4269 6469 -134 569 -773 C ATOM 2776 C ASN B 74 51.231 26.078 35.076 1.00 38.99 C ANISOU 2776 C ASN B 74 3282 4733 6801 -58 585 -725 C ATOM 2777 O ASN B 74 50.129 25.599 35.328 1.00 38.35 O ANISOU 2777 O ASN B 74 3318 4676 6577 -29 537 -704 O ATOM 2778 CB ASN B 74 51.361 27.709 36.956 1.00 33.27 C ANISOU 2778 CB ASN B 74 2457 4029 6153 -138 404 -838 C ATOM 2779 CG ASN B 74 51.744 29.055 37.470 1.00 38.20 C ANISOU 2779 CG ASN B 74 2997 4626 6891 -210 371 -910 C ATOM 2780 OD1 ASN B 74 52.904 29.346 37.720 1.00 39.34 O ANISOU 2780 OD1 ASN B 74 2997 4765 7184 -236 353 -955 O ATOM 2781 ND2 ASN B 74 50.760 29.908 37.680 1.00 28.70 N ANISOU 2781 ND2 ASN B 74 1876 3400 5629 -245 358 -928 N ATOM 2782 N HIS B 75 52.226 25.377 34.509 1.00 36.59 N ANISOU 2782 N HIS B 75 2897 4423 6581 -27 652 -713 N ATOM 2783 CA HIS B 75 52.134 23.966 34.094 1.00 36.66 C ANISOU 2783 CA HIS B 75 2953 4448 6528 47 677 -679 C ATOM 2784 C HIS B 75 51.674 23.029 35.221 1.00 37.00 C ANISOU 2784 C HIS B 75 3026 4541 6490 101 531 -680 C ATOM 2785 O HIS B 75 50.882 22.116 34.966 1.00 36.72 O ANISOU 2785 O HIS B 75 3097 4509 6346 145 537 -646 O ATOM 2786 CB HIS B 75 53.460 23.485 33.477 1.00 38.64 C ANISOU 2786 CB HIS B 75 3080 4683 6920 71 764 -684 C ATOM 2787 CG HIS B 75 54.494 23.160 34.510 1.00 44.07 C ANISOU 2787 CG HIS B 75 3618 5400 7727 94 652 -721 C ATOM 2788 ND1 HIS B 75 54.616 21.874 35.030 1.00 46.73 N ANISOU 2788 ND1 HIS B 75 3942 5765 8048 171 572 -710 N ATOM 2789 CD2 HIS B 75 55.330 23.986 35.191 1.00 46.99 C ANISOU 2789 CD2 HIS B 75 3853 5776 8224 49 592 -767 C ATOM 2790 CE1 HIS B 75 55.540 21.956 35.979 1.00 46.64 C ANISOU 2790 CE1 HIS B 75 3790 5784 8149 174 465 -742 C ATOM 2791 NE2 HIS B 75 56.007 23.204 36.104 1.00 47.01 N ANISOU 2791 NE2 HIS B 75 3756 5820 8283 100 472 -784 N ATOM 2792 N HIS B 76 52.160 23.261 36.459 1.00 32.21 N ANISOU 2792 N HIS B 76 2328 3974 5936 94 400 -718 N ATOM 2793 CA HIS B 76 51.824 22.444 37.638 1.00 32.03 C ANISOU 2793 CA HIS B 76 2324 4011 5836 142 254 -710 C ATOM 2794 C HIS B 76 50.343 22.575 38.066 1.00 36.93 C ANISOU 2794 C HIS B 76 3091 4654 6288 133 206 -695 C ATOM 2795 O HIS B 76 49.826 21.696 38.760 1.00 37.91 O ANISOU 2795 O HIS B 76 3265 4818 6321 178 123 -665 O ATOM 2796 CB HIS B 76 52.796 22.728 38.809 1.00 32.09 C ANISOU 2796 CB HIS B 76 2189 4068 5936 135 126 -757 C ATOM 2797 CG HIS B 76 52.558 24.038 39.506 1.00 34.82 C ANISOU 2797 CG HIS B 76 2525 4434 6272 66 64 -819 C ATOM 2798 ND1 HIS B 76 53.139 25.213 39.061 1.00 35.83 N ANISOU 2798 ND1 HIS B 76 2577 4515 6523 -2 131 -866 N ATOM 2799 CD2 HIS B 76 51.831 24.304 40.615 1.00 34.96 C ANISOU 2799 CD2 HIS B 76 2595 4511 6178 56 -54 -845 C ATOM 2800 CE1 HIS B 76 52.728 26.152 39.895 1.00 34.38 C ANISOU 2800 CE1 HIS B 76 2403 4354 6305 -50 49 -925 C ATOM 2801 NE2 HIS B 76 51.946 25.653 40.849 1.00 34.41 N ANISOU 2801 NE2 HIS B 76 2483 4428 6164 -16 -62 -919 N ATOM 2802 N MET B 77 49.673 23.668 37.626 1.00 34.20 N ANISOU 2802 N MET B 77 2807 4278 5909 75 264 -711 N ATOM 2803 CA MET B 77 48.258 23.987 37.907 1.00 33.66 C ANISOU 2803 CA MET B 77 2867 4221 5700 59 236 -704 C ATOM 2804 C MET B 77 47.300 23.363 36.901 1.00 36.72 C ANISOU 2804 C MET B 77 3381 4578 5991 84 321 -648 C ATOM 2805 O MET B 77 46.099 23.339 37.152 1.00 37.47 O ANISOU 2805 O MET B 77 3579 4687 5969 85 291 -634 O ATOM 2806 CB MET B 77 48.019 25.507 37.863 1.00 36.09 C ANISOU 2806 CB MET B 77 3173 4499 6040 -12 260 -748 C ATOM 2807 CG MET B 77 48.794 26.314 38.878 1.00 40.08 C ANISOU 2807 CG MET B 77 3564 5031 6634 -49 170 -823 C ATOM 2808 SD MET B 77 48.418 25.932 40.582 1.00 44.21 S ANISOU 2808 SD MET B 77 4094 5655 7048 -23 -3 -859 S ATOM 2809 CE MET B 77 46.765 26.696 40.720 1.00 40.59 C ANISOU 2809 CE MET B 77 3777 5189 6457 -51 6 -869 C ATOM 2810 N ARG B 78 47.811 22.910 35.750 1.00 32.88 N ANISOU 2810 N ARG B 78 2884 4054 5556 102 429 -623 N ATOM 2811 CA ARG B 78 47.020 22.361 34.653 1.00 32.01 C ANISOU 2811 CA ARG B 78 2886 3917 5360 122 517 -584 C ATOM 2812 C ARG B 78 46.546 20.918 34.903 1.00 34.26 C ANISOU 2812 C ARG B 78 3225 4218 5574 183 471 -557 C ATOM 2813 O ARG B 78 46.867 20.013 34.142 1.00 35.13 O ANISOU 2813 O ARG B 78 3338 4305 5705 222 535 -546 O ATOM 2814 CB ARG B 78 47.777 22.515 33.312 1.00 29.92 C ANISOU 2814 CB ARG B 78 2589 3613 5166 113 659 -576 C ATOM 2815 CG ARG B 78 47.912 23.982 32.883 1.00 38.05 C ANISOU 2815 CG ARG B 78 3600 4613 6245 46 723 -580 C ATOM 2816 CD ARG B 78 48.590 24.152 31.535 1.00 45.37 C ANISOU 2816 CD ARG B 78 4505 5508 7224 35 874 -558 C ATOM 2817 NE ARG B 78 49.273 25.443 31.441 1.00 52.92 N ANISOU 2817 NE ARG B 78 5380 6433 8294 -28 923 -564 N ATOM 2818 CZ ARG B 78 50.549 25.602 31.091 1.00 70.05 C ANISOU 2818 CZ ARG B 78 7431 8586 10600 -42 999 -574 C ATOM 2819 NH1 ARG B 78 51.289 24.553 30.745 1.00 53.74 N ANISOU 2819 NH1 ARG B 78 5314 6534 8570 7 1041 -581 N ATOM 2820 NH2 ARG B 78 51.091 26.812 31.068 1.00 58.57 N ANISOU 2820 NH2 ARG B 78 5902 7094 9256 -105 1039 -577 N ATOM 2821 N THR B 79 45.753 20.717 35.963 1.00 29.67 N ANISOU 2821 N THR B 79 2688 3674 4912 191 364 -549 N ATOM 2822 CA THR B 79 45.132 19.429 36.313 1.00 27.91 C ANISOU 2822 CA THR B 79 2524 3461 4620 241 316 -513 C ATOM 2823 C THR B 79 43.717 19.438 35.722 1.00 30.58 C ANISOU 2823 C THR B 79 2993 3783 4843 227 353 -495 C ATOM 2824 O THR B 79 43.209 20.520 35.404 1.00 30.01 O ANISOU 2824 O THR B 79 2957 3706 4738 182 384 -508 O ATOM 2825 CB THR B 79 45.137 19.197 37.841 1.00 33.20 C ANISOU 2825 CB THR B 79 3160 4188 5267 257 182 -505 C ATOM 2826 OG1 THR B 79 44.142 20.007 38.463 1.00 34.25 O ANISOU 2826 OG1 THR B 79 3352 4355 5306 218 137 -518 O ATOM 2827 CG2 THR B 79 46.509 19.460 38.485 1.00 29.54 C ANISOU 2827 CG2 THR B 79 2558 3751 4914 260 128 -532 C ATOM 2828 N VAL B 80 43.086 18.253 35.561 1.00 27.95 N ANISOU 2828 N VAL B 80 2724 3437 4460 266 349 -466 N ATOM 2829 CA VAL B 80 41.713 18.087 35.037 1.00 27.37 C ANISOU 2829 CA VAL B 80 2766 3349 4283 256 372 -451 C ATOM 2830 C VAL B 80 40.711 18.937 35.835 1.00 30.53 C ANISOU 2830 C VAL B 80 3209 3786 4607 220 312 -450 C ATOM 2831 O VAL B 80 39.943 19.696 35.229 1.00 30.75 O ANISOU 2831 O VAL B 80 3295 3803 4586 188 352 -456 O ATOM 2832 CB VAL B 80 41.282 16.592 34.942 1.00 31.05 C ANISOU 2832 CB VAL B 80 3276 3791 4731 301 362 -425 C ATOM 2833 CG1 VAL B 80 39.793 16.439 34.605 1.00 30.34 C ANISOU 2833 CG1 VAL B 80 3296 3693 4540 286 367 -414 C ATOM 2834 CG2 VAL B 80 42.126 15.868 33.913 1.00 30.40 C ANISOU 2834 CG2 VAL B 80 3164 3664 4721 335 442 -444 C ATOM 2835 N THR B 81 40.771 18.856 37.186 1.00 25.89 N ANISOU 2835 N THR B 81 2586 3244 4008 227 218 -443 N ATOM 2836 CA THR B 81 39.926 19.628 38.097 1.00 25.35 C ANISOU 2836 CA THR B 81 2547 3219 3867 197 161 -454 C ATOM 2837 C THR B 81 40.086 21.126 37.850 1.00 29.02 C ANISOU 2837 C THR B 81 2989 3676 4362 149 192 -500 C ATOM 2838 O THR B 81 39.070 21.818 37.730 1.00 28.91 O ANISOU 2838 O THR B 81 3033 3656 4294 123 204 -507 O ATOM 2839 CB THR B 81 40.190 19.247 39.564 1.00 29.82 C ANISOU 2839 CB THR B 81 3070 3848 4414 215 60 -442 C ATOM 2840 OG1 THR B 81 39.910 17.861 39.731 1.00 30.41 O ANISOU 2840 OG1 THR B 81 3174 3915 4466 258 39 -383 O ATOM 2841 CG2 THR B 81 39.346 20.056 40.553 1.00 27.08 C ANISOU 2841 CG2 THR B 81 2750 3555 3982 185 7 -465 C ATOM 2842 N ASN B 82 41.346 21.617 37.746 1.00 25.38 N ANISOU 2842 N ASN B 82 2437 3206 3998 139 206 -528 N ATOM 2843 CA ASN B 82 41.632 23.043 37.553 1.00 25.38 C ANISOU 2843 CA ASN B 82 2402 3188 4054 91 236 -570 C ATOM 2844 C ASN B 82 41.184 23.571 36.201 1.00 29.63 C ANISOU 2844 C ASN B 82 2997 3670 4589 70 337 -552 C ATOM 2845 O ASN B 82 40.806 24.736 36.133 1.00 29.14 O ANISOU 2845 O ASN B 82 2946 3589 4538 31 352 -570 O ATOM 2846 CB ASN B 82 43.083 23.375 37.835 1.00 25.38 C ANISOU 2846 CB ASN B 82 2283 3193 4170 82 223 -604 C ATOM 2847 CG ASN B 82 43.440 23.276 39.292 1.00 32.51 C ANISOU 2847 CG ASN B 82 3126 4162 5065 89 106 -635 C ATOM 2848 OD1 ASN B 82 42.583 23.100 40.158 1.00 26.43 O ANISOU 2848 OD1 ASN B 82 2407 3439 4196 96 40 -633 O ATOM 2849 ND2 ASN B 82 44.724 23.392 39.594 1.00 28.44 N ANISOU 2849 ND2 ASN B 82 2497 3657 4651 87 78 -664 N ATOM 2850 N TYR B 83 41.148 22.713 35.155 1.00 26.66 N ANISOU 2850 N TYR B 83 2663 3271 4194 97 401 -516 N ATOM 2851 CA TYR B 83 40.613 23.081 33.840 1.00 27.14 C ANISOU 2851 CA TYR B 83 2793 3296 4223 83 490 -492 C ATOM 2852 C TYR B 83 39.098 23.338 33.979 1.00 29.30 C ANISOU 2852 C TYR B 83 3157 3575 4401 74 457 -479 C ATOM 2853 O TYR B 83 38.595 24.346 33.477 1.00 29.31 O ANISOU 2853 O TYR B 83 3190 3552 4396 45 491 -470 O ATOM 2854 CB TYR B 83 40.893 21.974 32.819 1.00 29.90 C ANISOU 2854 CB TYR B 83 3168 3633 4560 118 555 -473 C ATOM 2855 CG TYR B 83 42.218 22.103 32.091 1.00 34.39 C ANISOU 2855 CG TYR B 83 3665 4183 5220 116 639 -480 C ATOM 2856 CD1 TYR B 83 43.235 22.917 32.583 1.00 37.56 C ANISOU 2856 CD1 TYR B 83 3963 4581 5726 89 634 -501 C ATOM 2857 CD2 TYR B 83 42.454 21.413 30.910 1.00 36.27 C ANISOU 2857 CD2 TYR B 83 3932 4409 5442 138 727 -472 C ATOM 2858 CE1 TYR B 83 44.451 23.046 31.912 1.00 39.29 C ANISOU 2858 CE1 TYR B 83 4107 4782 6041 84 719 -506 C ATOM 2859 CE2 TYR B 83 43.663 21.542 30.224 1.00 37.89 C ANISOU 2859 CE2 TYR B 83 4068 4601 5729 136 818 -479 C ATOM 2860 CZ TYR B 83 44.663 22.350 30.736 1.00 46.81 C ANISOU 2860 CZ TYR B 83 5090 5724 6971 109 815 -492 C ATOM 2861 OH TYR B 83 45.858 22.465 30.069 1.00 51.51 O ANISOU 2861 OH TYR B 83 5607 6306 7658 105 911 -497 O ATOM 2862 N PHE B 84 38.395 22.452 34.719 1.00 23.95 N ANISOU 2862 N PHE B 84 2513 2928 3661 99 391 -475 N ATOM 2863 CA PHE B 84 36.967 22.599 35.009 1.00 23.18 C ANISOU 2863 CA PHE B 84 2487 2841 3482 92 357 -466 C ATOM 2864 C PHE B 84 36.719 23.789 35.923 1.00 27.38 C ANISOU 2864 C PHE B 84 2991 3386 4027 61 316 -499 C ATOM 2865 O PHE B 84 35.776 24.522 35.681 1.00 28.33 O ANISOU 2865 O PHE B 84 3155 3488 4120 44 327 -497 O ATOM 2866 CB PHE B 84 36.368 21.320 35.606 1.00 23.94 C ANISOU 2866 CB PHE B 84 2614 2962 3520 122 305 -448 C ATOM 2867 CG PHE B 84 36.136 20.166 34.655 1.00 24.10 C ANISOU 2867 CG PHE B 84 2682 2956 3517 148 342 -424 C ATOM 2868 CD1 PHE B 84 35.295 20.306 33.550 1.00 25.67 C ANISOU 2868 CD1 PHE B 84 2951 3134 3669 139 386 -415 C ATOM 2869 CD2 PHE B 84 36.691 18.916 34.906 1.00 23.37 C ANISOU 2869 CD2 PHE B 84 2567 2862 3450 183 326 -413 C ATOM 2870 CE1 PHE B 84 35.073 19.234 32.681 1.00 25.55 C ANISOU 2870 CE1 PHE B 84 2980 3100 3628 161 415 -410 C ATOM 2871 CE2 PHE B 84 36.437 17.837 34.055 1.00 25.23 C ANISOU 2871 CE2 PHE B 84 2846 3066 3673 206 360 -406 C ATOM 2872 CZ PHE B 84 35.642 18.009 32.943 1.00 23.30 C ANISOU 2872 CZ PHE B 84 2670 2805 3378 193 405 -411 C ATOM 2873 N LEU B 85 37.583 24.026 36.937 1.00 23.41 N ANISOU 2873 N LEU B 85 2412 2911 3571 55 268 -536 N ATOM 2874 CA LEU B 85 37.464 25.206 37.809 1.00 23.12 C ANISOU 2874 CA LEU B 85 2343 2887 3555 24 230 -588 C ATOM 2875 C LEU B 85 37.661 26.503 37.005 1.00 26.84 C ANISOU 2875 C LEU B 85 2800 3295 4102 -12 292 -599 C ATOM 2876 O LEU B 85 37.020 27.506 37.321 1.00 26.64 O ANISOU 2876 O LEU B 85 2785 3255 4083 -36 283 -629 O ATOM 2877 CB LEU B 85 38.431 25.150 39.004 1.00 22.85 C ANISOU 2877 CB LEU B 85 2228 2904 3552 24 159 -632 C ATOM 2878 CG LEU B 85 38.231 24.042 40.044 1.00 25.35 C ANISOU 2878 CG LEU B 85 2553 3289 3789 57 85 -615 C ATOM 2879 CD1 LEU B 85 39.247 24.177 41.131 1.00 25.19 C ANISOU 2879 CD1 LEU B 85 2448 3324 3799 56 11 -658 C ATOM 2880 CD2 LEU B 85 36.808 24.061 40.643 1.00 24.62 C ANISOU 2880 CD2 LEU B 85 2531 3229 3596 56 61 -613 C ATOM 2881 N VAL B 86 38.499 26.472 35.929 1.00 24.16 N ANISOU 2881 N VAL B 86 2440 2918 3822 -15 363 -569 N ATOM 2882 CA VAL B 86 38.642 27.628 35.016 1.00 24.25 C ANISOU 2882 CA VAL B 86 2447 2866 3900 -49 436 -555 C ATOM 2883 C VAL B 86 37.288 27.863 34.292 1.00 28.48 C ANISOU 2883 C VAL B 86 3077 3379 4364 -45 461 -511 C ATOM 2884 O VAL B 86 36.818 29.000 34.238 1.00 29.53 O ANISOU 2884 O VAL B 86 3216 3471 4533 -69 471 -514 O ATOM 2885 CB VAL B 86 39.852 27.525 34.040 1.00 27.78 C ANISOU 2885 CB VAL B 86 2849 3287 4420 -54 517 -528 C ATOM 2886 CG1 VAL B 86 39.758 28.543 32.902 1.00 27.05 C ANISOU 2886 CG1 VAL B 86 2778 3134 4364 -83 604 -484 C ATOM 2887 CG2 VAL B 86 41.145 27.719 34.795 1.00 27.22 C ANISOU 2887 CG2 VAL B 86 2665 3225 4452 -69 489 -579 C ATOM 2888 N ASN B 87 36.644 26.780 33.808 1.00 23.25 N ANISOU 2888 N ASN B 87 2484 2743 3609 -12 462 -475 N ATOM 2889 CA ASN B 87 35.342 26.856 33.148 1.00 22.81 C ANISOU 2889 CA ASN B 87 2512 2676 3480 -5 472 -437 C ATOM 2890 C ASN B 87 34.254 27.465 34.056 1.00 27.40 C ANISOU 2890 C ASN B 87 3105 3260 4045 -12 415 -466 C ATOM 2891 O ASN B 87 33.461 28.301 33.597 1.00 26.98 O ANISOU 2891 O ASN B 87 3084 3172 3996 -22 430 -444 O ATOM 2892 CB ASN B 87 34.918 25.507 32.614 1.00 20.78 C ANISOU 2892 CB ASN B 87 2312 2446 3138 27 473 -412 C ATOM 2893 CG ASN B 87 33.895 25.646 31.528 1.00 37.86 C ANISOU 2893 CG ASN B 87 4552 4595 5237 30 499 -369 C ATOM 2894 OD1 ASN B 87 34.076 26.434 30.582 1.00 26.73 O ANISOU 2894 OD1 ASN B 87 3154 3156 3845 16 555 -334 O ATOM 2895 ND2 ASN B 87 32.804 24.895 31.641 1.00 25.14 N ANISOU 2895 ND2 ASN B 87 2992 3005 3554 48 457 -367 N ATOM 2896 N LEU B 88 34.269 27.091 35.354 1.00 23.79 N ANISOU 2896 N LEU B 88 2618 2848 3574 -7 352 -513 N ATOM 2897 CA LEU B 88 33.385 27.636 36.382 1.00 24.08 C ANISOU 2897 CA LEU B 88 2655 2902 3594 -14 303 -555 C ATOM 2898 C LEU B 88 33.641 29.155 36.519 1.00 29.70 C ANISOU 2898 C LEU B 88 3323 3563 4399 -46 318 -594 C ATOM 2899 O LEU B 88 32.688 29.923 36.537 1.00 31.05 O ANISOU 2899 O LEU B 88 3517 3705 4577 -51 318 -602 O ATOM 2900 CB LEU B 88 33.613 26.885 37.706 1.00 24.26 C ANISOU 2900 CB LEU B 88 2650 2993 3575 -3 240 -591 C ATOM 2901 CG LEU B 88 32.745 27.242 38.916 1.00 28.66 C ANISOU 2901 CG LEU B 88 3209 3591 4089 -7 193 -640 C ATOM 2902 CD1 LEU B 88 31.255 27.158 38.598 1.00 28.51 C ANISOU 2902 CD1 LEU B 88 3252 3563 4018 3 204 -612 C ATOM 2903 CD2 LEU B 88 33.077 26.329 40.085 1.00 30.17 C ANISOU 2903 CD2 LEU B 88 3381 3861 4221 8 136 -653 C ATOM 2904 N SER B 89 34.916 29.585 36.512 1.00 26.55 N ANISOU 2904 N SER B 89 2859 3143 4086 -68 335 -616 N ATOM 2905 CA SER B 89 35.306 30.999 36.526 1.00 26.38 C ANISOU 2905 CA SER B 89 2788 3058 4177 -104 357 -652 C ATOM 2906 C SER B 89 34.844 31.736 35.257 1.00 29.21 C ANISOU 2906 C SER B 89 3188 3341 4572 -111 424 -582 C ATOM 2907 O SER B 89 34.422 32.874 35.369 1.00 28.58 O ANISOU 2907 O SER B 89 3097 3203 4559 -129 429 -601 O ATOM 2908 CB SER B 89 36.814 31.146 36.704 1.00 29.03 C ANISOU 2908 CB SER B 89 3039 3389 4604 -128 363 -683 C ATOM 2909 OG SER B 89 37.174 30.838 38.039 1.00 34.43 O ANISOU 2909 OG SER B 89 3675 4138 5267 -126 286 -759 O ATOM 2910 N LEU B 90 34.888 31.089 34.070 1.00 26.71 N ANISOU 2910 N LEU B 90 2918 3025 4206 -95 473 -502 N ATOM 2911 CA LEU B 90 34.403 31.695 32.813 1.00 26.65 C ANISOU 2911 CA LEU B 90 2959 2963 4204 -97 530 -422 C ATOM 2912 C LEU B 90 32.876 31.916 32.850 1.00 29.93 C ANISOU 2912 C LEU B 90 3431 3373 4567 -77 495 -409 C ATOM 2913 O LEU B 90 32.405 32.983 32.450 1.00 28.48 O ANISOU 2913 O LEU B 90 3256 3126 4440 -86 515 -377 O ATOM 2914 CB LEU B 90 34.817 30.900 31.558 1.00 26.05 C ANISOU 2914 CB LEU B 90 2922 2906 4069 -82 589 -352 C ATOM 2915 CG LEU B 90 36.313 30.798 31.265 1.00 30.68 C ANISOU 2915 CG LEU B 90 3448 3487 4721 -100 645 -352 C ATOM 2916 CD1 LEU B 90 36.574 29.829 30.141 1.00 31.15 C ANISOU 2916 CD1 LEU B 90 3553 3580 4702 -78 700 -301 C ATOM 2917 CD2 LEU B 90 36.927 32.160 30.949 1.00 31.05 C ANISOU 2917 CD2 LEU B 90 3446 3457 4894 -141 701 -330 C ATOM 2918 N ALA B 91 32.142 30.936 33.381 1.00 27.16 N ANISOU 2918 N ALA B 91 3113 3084 4121 -52 445 -431 N ATOM 2919 CA ALA B 91 30.675 31.036 33.546 1.00 27.60 C ANISOU 2919 CA ALA B 91 3209 3144 4133 -34 409 -429 C ATOM 2920 C ALA B 91 30.377 32.140 34.563 1.00 33.34 C ANISOU 2920 C ALA B 91 3892 3837 4939 -49 386 -495 C ATOM 2921 O ALA B 91 29.487 32.939 34.312 1.00 33.67 O ANISOU 2921 O ALA B 91 3946 3830 5017 -44 389 -478 O ATOM 2922 CB ALA B 91 30.122 29.716 34.012 1.00 28.02 C ANISOU 2922 CB ALA B 91 3290 3270 4087 -12 366 -446 C ATOM 2923 N ASP B 92 31.144 32.178 35.651 1.00 30.39 N ANISOU 2923 N ASP B 92 3462 3489 4598 -66 363 -575 N ATOM 2924 CA ASP B 92 30.975 33.178 36.699 1.00 30.50 C ANISOU 2924 CA ASP B 92 3428 3480 4680 -82 340 -662 C ATOM 2925 C ASP B 92 31.348 34.586 36.231 1.00 36.25 C ANISOU 2925 C ASP B 92 4123 4105 5546 -108 380 -659 C ATOM 2926 O ASP B 92 30.658 35.525 36.618 1.00 38.58 O ANISOU 2926 O ASP B 92 4405 4352 5903 -110 374 -700 O ATOM 2927 CB ASP B 92 31.697 32.742 37.983 1.00 31.77 C ANISOU 2927 CB ASP B 92 3543 3711 4817 -92 294 -748 C ATOM 2928 CG ASP B 92 30.932 31.638 38.727 1.00 38.99 C ANISOU 2928 CG ASP B 92 4492 4717 5605 -65 252 -756 C ATOM 2929 OD1 ASP B 92 29.801 31.299 38.301 1.00 37.66 O ANISOU 2929 OD1 ASP B 92 4376 4550 5384 -44 258 -708 O ATOM 2930 OD2 ASP B 92 31.455 31.126 39.731 1.00 42.52 O ANISOU 2930 OD2 ASP B 92 4911 5233 6010 -67 210 -806 O ATOM 2931 N VAL B 93 32.332 34.731 35.325 1.00 31.79 N ANISOU 2931 N VAL B 93 3544 3500 5034 -126 428 -601 N ATOM 2932 CA VAL B 93 32.706 36.033 34.748 1.00 32.32 C ANISOU 2932 CA VAL B 93 3580 3460 5239 -154 478 -574 C ATOM 2933 C VAL B 93 31.630 36.506 33.754 1.00 38.46 C ANISOU 2933 C VAL B 93 4416 4184 6014 -132 502 -479 C ATOM 2934 O VAL B 93 31.329 37.691 33.725 1.00 38.56 O ANISOU 2934 O VAL B 93 4407 4105 6138 -143 516 -479 O ATOM 2935 CB VAL B 93 34.148 36.054 34.168 1.00 36.18 C ANISOU 2935 CB VAL B 93 4027 3928 5791 -185 530 -542 C ATOM 2936 CG1 VAL B 93 34.382 37.239 33.226 1.00 35.95 C ANISOU 2936 CG1 VAL B 93 3987 3788 5885 -210 598 -468 C ATOM 2937 CG2 VAL B 93 35.164 36.082 35.296 1.00 36.10 C ANISOU 2937 CG2 VAL B 93 3935 3943 5839 -213 494 -652 C ATOM 2938 N LEU B 94 31.036 35.581 32.972 1.00 36.63 N ANISOU 2938 N LEU B 94 4254 4006 5658 -101 501 -403 N ATOM 2939 CA LEU B 94 29.960 35.888 32.027 1.00 36.30 C ANISOU 2939 CA LEU B 94 4268 3932 5591 -75 508 -313 C ATOM 2940 C LEU B 94 28.747 36.492 32.792 1.00 39.19 C ANISOU 2940 C LEU B 94 4623 4269 5997 -58 464 -366 C ATOM 2941 O LEU B 94 28.221 37.529 32.378 1.00 40.25 O ANISOU 2941 O LEU B 94 4754 4319 6218 -52 477 -323 O ATOM 2942 CB LEU B 94 29.548 34.622 31.241 1.00 36.17 C ANISOU 2942 CB LEU B 94 4322 3996 5426 -47 499 -253 C ATOM 2943 CG LEU B 94 28.267 34.713 30.371 1.00 40.05 C ANISOU 2943 CG LEU B 94 4872 4480 5865 -16 482 -173 C ATOM 2944 CD1 LEU B 94 28.443 35.682 29.208 1.00 40.37 C ANISOU 2944 CD1 LEU B 94 4929 4451 5958 -20 530 -65 C ATOM 2945 CD2 LEU B 94 27.855 33.360 29.874 1.00 38.42 C ANISOU 2945 CD2 LEU B 94 4723 4359 5516 6 459 -153 C ATOM 2946 N ALA B 95 28.387 35.882 33.921 1.00 32.19 N ANISOU 2946 N ALA B 95 3726 3451 5054 -50 418 -458 N ATOM 2947 CA ALA B 95 27.261 36.354 34.754 1.00 30.50 C ANISOU 2947 CA ALA B 95 3497 3227 4867 -33 386 -523 C ATOM 2948 C ALA B 95 27.602 37.711 35.375 1.00 33.55 C ANISOU 2948 C ALA B 95 3820 3526 5403 -56 399 -602 C ATOM 2949 O ALA B 95 26.822 38.637 35.210 1.00 32.35 O ANISOU 2949 O ALA B 95 3658 3299 5336 -42 402 -599 O ATOM 2950 CB ALA B 95 26.962 35.335 35.820 1.00 30.47 C ANISOU 2950 CB ALA B 95 3497 3326 4756 -24 346 -595 C ATOM 2951 N THR B 96 28.750 37.797 36.046 1.00 32.16 N ANISOU 2951 N THR B 96 3596 3355 5269 -92 403 -673 N ATOM 2952 CA THR B 96 29.212 39.013 36.736 1.00 32.58 C ANISOU 2952 CA THR B 96 3582 3329 5469 -122 410 -768 C ATOM 2953 C THR B 96 29.364 40.222 35.810 1.00 36.62 C ANISOU 2953 C THR B 96 4079 3703 6133 -134 459 -695 C ATOM 2954 O THR B 96 28.895 41.304 36.154 1.00 35.76 O ANISOU 2954 O THR B 96 3937 3503 6146 -134 462 -745 O ATOM 2955 CB THR B 96 30.504 38.738 37.522 1.00 41.12 C ANISOU 2955 CB THR B 96 4613 4459 6551 -158 394 -855 C ATOM 2956 OG1 THR B 96 30.302 37.593 38.360 1.00 43.22 O ANISOU 2956 OG1 THR B 96 4898 4853 6671 -140 348 -902 O ATOM 2957 CG2 THR B 96 30.943 39.936 38.373 1.00 36.10 C ANISOU 2957 CG2 THR B 96 3903 3753 6060 -192 389 -981 C ATOM 2958 N ALA B 97 30.026 40.049 34.657 1.00 34.26 N ANISOU 2958 N ALA B 97 3803 3385 5831 -145 500 -576 N ATOM 2959 CA ALA B 97 30.282 41.152 33.729 1.00 34.39 C ANISOU 2959 CA ALA B 97 3807 3275 5985 -161 554 -486 C ATOM 2960 C ALA B 97 29.057 41.654 32.965 1.00 39.22 C ANISOU 2960 C ALA B 97 4463 3828 6612 -121 556 -387 C ATOM 2961 O ALA B 97 28.861 42.858 32.892 1.00 39.45 O ANISOU 2961 O ALA B 97 4460 3734 6797 -126 575 -377 O ATOM 2962 CB ALA B 97 31.404 40.786 32.754 1.00 34.71 C ANISOU 2962 CB ALA B 97 3858 3327 6005 -185 608 -389 C ATOM 2963 N ILE B 98 28.254 40.754 32.384 1.00 37.26 N ANISOU 2963 N ILE B 98 4281 3660 6215 -82 533 -314 N ATOM 2964 CA ILE B 98 27.125 41.127 31.521 1.00 37.18 C ANISOU 2964 CA ILE B 98 4313 3609 6207 -41 525 -205 C ATOM 2965 C ILE B 98 25.767 41.157 32.225 1.00 38.26 C ANISOU 2965 C ILE B 98 4444 3756 6339 -3 473 -272 C ATOM 2966 O ILE B 98 24.986 42.076 31.974 1.00 39.35 O ANISOU 2966 O ILE B 98 4569 3803 6580 22 470 -233 O ATOM 2967 CB ILE B 98 27.110 40.198 30.259 1.00 40.82 C ANISOU 2967 CB ILE B 98 4849 4147 6514 -24 532 -77 C ATOM 2968 CG1 ILE B 98 28.319 40.512 29.345 1.00 41.69 C ANISOU 2968 CG1 ILE B 98 4964 4221 6657 -57 602 15 C ATOM 2969 CG2 ILE B 98 25.815 40.312 29.449 1.00 42.31 C ANISOU 2969 CG2 ILE B 98 5084 4329 6663 23 499 23 C ATOM 2970 CD1 ILE B 98 29.317 39.509 29.327 1.00 47.81 C ANISOU 2970 CD1 ILE B 98 5744 5082 7338 -80 624 -14 C ATOM 2971 N CYS B 99 25.481 40.181 33.082 1.00 32.18 N ANISOU 2971 N CYS B 99 3678 3092 5458 3 437 -364 N ATOM 2972 CA CYS B 99 24.158 40.060 33.684 1.00 31.40 C ANISOU 2972 CA CYS B 99 3574 3019 5336 39 397 -418 C ATOM 2973 C CYS B 99 23.986 40.795 35.020 1.00 35.10 C ANISOU 2973 C CYS B 99 3979 3450 5906 32 396 -565 C ATOM 2974 O CYS B 99 22.934 41.404 35.206 1.00 34.34 O ANISOU 2974 O CYS B 99 3863 3304 5881 63 386 -584 O ATOM 2975 CB CYS B 99 23.755 38.592 33.786 1.00 31.06 C ANISOU 2975 CB CYS B 99 3573 3107 5120 52 365 -420 C ATOM 2976 SG CYS B 99 24.088 37.635 32.276 1.00 34.69 S ANISOU 2976 SG CYS B 99 4108 3620 5453 56 369 -278 S ATOM 2977 N LEU B 100 24.984 40.759 35.927 1.00 31.44 N ANISOU 2977 N LEU B 100 3482 3012 5451 -6 403 -673 N ATOM 2978 CA LEU B 100 24.924 41.432 37.239 1.00 31.09 C ANISOU 2978 CA LEU B 100 3380 2947 5486 -17 398 -831 C ATOM 2979 C LEU B 100 24.497 42.922 37.150 1.00 35.63 C ANISOU 2979 C LEU B 100 3911 3371 6257 -8 421 -849 C ATOM 2980 O LEU B 100 23.558 43.270 37.872 1.00 34.73 O ANISOU 2980 O LEU B 100 3772 3248 6176 18 413 -937 O ATOM 2981 CB LEU B 100 26.254 41.269 38.025 1.00 31.11 C ANISOU 2981 CB LEU B 100 3350 2992 5477 -64 395 -928 C ATOM 2982 CG LEU B 100 26.320 41.768 39.480 1.00 35.11 C ANISOU 2982 CG LEU B 100 3803 3514 6024 -79 380 -1109 C ATOM 2983 CD1 LEU B 100 27.398 41.041 40.235 1.00 34.63 C ANISOU 2983 CD1 LEU B 100 3730 3558 5871 -112 353 -1179 C ATOM 2984 CD2 LEU B 100 26.588 43.280 39.559 1.00 36.80 C ANISOU 2984 CD2 LEU B 100 3957 3578 6447 -100 406 -1174 C ATOM 2985 N PRO B 101 25.149 43.822 36.339 1.00 32.87 N ANISOU 2985 N PRO B 101 3547 2897 6046 -27 453 -772 N ATOM 2986 CA PRO B 101 24.678 45.227 36.291 1.00 32.35 C ANISOU 2986 CA PRO B 101 3437 2674 6182 -15 474 -786 C ATOM 2987 C PRO B 101 23.197 45.383 35.907 1.00 37.55 C ANISOU 2987 C PRO B 101 4110 3306 6851 47 458 -723 C ATOM 2988 O PRO B 101 22.495 46.202 36.505 1.00 36.56 O ANISOU 2988 O PRO B 101 3937 3105 6848 69 461 -812 O ATOM 2989 CB PRO B 101 25.626 45.895 35.285 1.00 33.38 C ANISOU 2989 CB PRO B 101 3563 2694 6426 -46 514 -669 C ATOM 2990 CG PRO B 101 26.842 44.992 35.241 1.00 37.38 C ANISOU 2990 CG PRO B 101 4086 3300 6816 -88 519 -666 C ATOM 2991 CD PRO B 101 26.287 43.615 35.408 1.00 33.43 C ANISOU 2991 CD PRO B 101 3639 2959 6105 -60 480 -663 C ATOM 2992 N ALA B 102 22.709 44.569 34.936 1.00 35.18 N ANISOU 2992 N ALA B 102 3870 3072 6424 75 439 -581 N ATOM 2993 CA ALA B 102 21.308 44.589 34.496 1.00 34.65 C ANISOU 2993 CA ALA B 102 3815 2995 6354 133 411 -512 C ATOM 2994 C ALA B 102 20.365 44.110 35.599 1.00 41.07 C ANISOU 2994 C ALA B 102 4606 3891 7107 156 390 -641 C ATOM 2995 O ALA B 102 19.315 44.720 35.805 1.00 42.70 O ANISOU 2995 O ALA B 102 4775 4038 7412 197 386 -667 O ATOM 2996 CB ALA B 102 21.132 43.747 33.249 1.00 34.62 C ANISOU 2996 CB ALA B 102 3880 3060 6212 148 389 -348 C ATOM 2997 N SER B 103 20.756 43.038 36.320 1.00 37.85 N ANISOU 2997 N SER B 103 4217 3618 6546 130 381 -718 N ATOM 2998 CA SER B 103 20.003 42.470 37.442 1.00 38.07 C ANISOU 2998 CA SER B 103 4229 3743 6494 143 370 -835 C ATOM 2999 C SER B 103 19.946 43.465 38.605 1.00 40.65 C ANISOU 2999 C SER B 103 4490 4010 6944 139 395 -1001 C ATOM 3000 O SER B 103 18.915 43.592 39.241 1.00 40.12 O ANISOU 3000 O SER B 103 4393 3957 6894 170 400 -1076 O ATOM 3001 CB SER B 103 20.610 41.133 37.873 1.00 42.29 C ANISOU 3001 CB SER B 103 4801 4423 6845 114 357 -859 C ATOM 3002 OG SER B 103 20.057 40.667 39.096 1.00 54.29 O ANISOU 3002 OG SER B 103 6304 6036 8289 119 355 -974 O ATOM 3003 N LEU B 104 21.036 44.205 38.827 1.00 37.88 N ANISOU 3003 N LEU B 104 4114 3588 6690 101 414 -1058 N ATOM 3004 CA LEU B 104 21.120 45.232 39.855 1.00 37.80 C ANISOU 3004 CA LEU B 104 4042 3510 6813 91 435 -1226 C ATOM 3005 C LEU B 104 20.092 46.325 39.572 1.00 43.53 C ANISOU 3005 C LEU B 104 4726 4094 7718 137 452 -1217 C ATOM 3006 O LEU B 104 19.349 46.701 40.472 1.00 44.35 O ANISOU 3006 O LEU B 104 4787 4196 7867 160 466 -1350 O ATOM 3007 CB LEU B 104 22.553 45.809 39.900 1.00 37.33 C ANISOU 3007 CB LEU B 104 3960 3385 6839 35 446 -1266 C ATOM 3008 CG LEU B 104 22.808 47.093 40.699 1.00 40.87 C ANISOU 3008 CG LEU B 104 4338 3717 7473 17 467 -1426 C ATOM 3009 CD1 LEU B 104 22.453 46.922 42.167 1.00 41.29 C ANISOU 3009 CD1 LEU B 104 4367 3872 7450 18 462 -1626 C ATOM 3010 CD2 LEU B 104 24.229 47.510 40.573 1.00 39.95 C ANISOU 3010 CD2 LEU B 104 4200 3538 7442 -42 474 -1436 C ATOM 3011 N LEU B 105 20.039 46.811 38.324 1.00 39.53 N ANISOU 3011 N LEU B 105 4232 3476 7313 154 452 -1056 N ATOM 3012 CA LEU B 105 19.115 47.867 37.928 1.00 38.70 C ANISOU 3012 CA LEU B 105 4086 3225 7393 202 462 -1019 C ATOM 3013 C LEU B 105 17.655 47.465 37.996 1.00 42.25 C ANISOU 3013 C LEU B 105 4530 3730 7794 262 443 -1009 C ATOM 3014 O LEU B 105 16.825 48.298 38.349 1.00 41.92 O ANISOU 3014 O LEU B 105 4430 3599 7899 301 459 -1079 O ATOM 3015 CB LEU B 105 19.473 48.433 36.559 1.00 38.89 C ANISOU 3015 CB LEU B 105 4131 3128 7519 205 464 -831 C ATOM 3016 CG LEU B 105 20.495 49.554 36.614 1.00 44.30 C ANISOU 3016 CG LEU B 105 4776 3664 8391 163 500 -869 C ATOM 3017 CD1 LEU B 105 21.333 49.587 35.366 1.00 45.20 C ANISOU 3017 CD1 LEU B 105 4932 3734 8508 138 511 -683 C ATOM 3018 CD2 LEU B 105 19.840 50.906 36.892 1.00 45.94 C ANISOU 3018 CD2 LEU B 105 4913 3696 8845 198 521 -933 C ATOM 3019 N VAL B 106 17.336 46.198 37.705 1.00 38.44 N ANISOU 3019 N VAL B 106 4099 3391 7116 266 413 -933 N ATOM 3020 CA VAL B 106 15.958 45.695 37.800 1.00 37.05 C ANISOU 3020 CA VAL B 106 3911 3279 6887 315 394 -926 C ATOM 3021 C VAL B 106 15.567 45.625 39.288 1.00 42.63 C ANISOU 3021 C VAL B 106 4575 4053 7571 313 425 -1122 C ATOM 3022 O VAL B 106 14.465 46.046 39.655 1.00 40.66 O ANISOU 3022 O VAL B 106 4271 3770 7407 358 440 -1178 O ATOM 3023 CB VAL B 106 15.755 44.332 37.082 1.00 39.11 C ANISOU 3023 CB VAL B 106 4236 3670 6954 313 353 -803 C ATOM 3024 CG1 VAL B 106 14.368 43.777 37.348 1.00 38.38 C ANISOU 3024 CG1 VAL B 106 4120 3649 6815 353 337 -818 C ATOM 3025 CG2 VAL B 106 15.983 44.461 35.585 1.00 38.76 C ANISOU 3025 CG2 VAL B 106 4234 3568 6925 323 324 -614 C ATOM 3026 N ASP B 107 16.487 45.118 40.146 1.00 40.47 N ANISOU 3026 N ASP B 107 4321 3874 7182 263 437 -1226 N ATOM 3027 CA ASP B 107 16.237 45.001 41.582 1.00 40.63 C ANISOU 3027 CA ASP B 107 4309 3979 7148 257 467 -1408 C ATOM 3028 C ASP B 107 16.108 46.370 42.284 1.00 45.87 C ANISOU 3028 C ASP B 107 4904 4524 8002 269 506 -1563 C ATOM 3029 O ASP B 107 15.388 46.472 43.274 1.00 45.61 O ANISOU 3029 O ASP B 107 4831 4536 7961 288 538 -1701 O ATOM 3030 CB ASP B 107 17.283 44.094 42.239 1.00 41.67 C ANISOU 3030 CB ASP B 107 4483 4248 7102 204 457 -1459 C ATOM 3031 CG ASP B 107 17.164 42.622 41.845 1.00 48.65 C ANISOU 3031 CG ASP B 107 5426 5264 7795 199 428 -1344 C ATOM 3032 OD1 ASP B 107 16.153 42.250 41.184 1.00 49.27 O ANISOU 3032 OD1 ASP B 107 5509 5343 7866 235 416 -1244 O ATOM 3033 OD2 ASP B 107 18.063 41.840 42.213 1.00 49.57 O ANISOU 3033 OD2 ASP B 107 5578 5480 7777 161 415 -1357 O ATOM 3034 N ILE B 108 16.734 47.424 41.738 1.00 42.94 N ANISOU 3034 N ILE B 108 4514 3994 7806 260 508 -1538 N ATOM 3035 CA ILE B 108 16.624 48.773 42.293 1.00 43.33 C ANISOU 3035 CA ILE B 108 4494 3903 8065 272 544 -1680 C ATOM 3036 C ILE B 108 15.378 49.503 41.784 1.00 47.69 C ANISOU 3036 C ILE B 108 4998 4330 8791 341 555 -1625 C ATOM 3037 O ILE B 108 14.611 50.030 42.583 1.00 48.28 O ANISOU 3037 O ILE B 108 5015 4378 8953 374 591 -1768 O ATOM 3038 CB ILE B 108 17.909 49.628 42.046 1.00 46.33 C ANISOU 3038 CB ILE B 108 4866 4160 8579 224 546 -1693 C ATOM 3039 CG1 ILE B 108 19.121 49.067 42.778 1.00 46.55 C ANISOU 3039 CG1 ILE B 108 4917 4308 8463 159 535 -1795 C ATOM 3040 CG2 ILE B 108 17.691 51.138 42.373 1.00 45.65 C ANISOU 3040 CG2 ILE B 108 4703 3883 8760 242 582 -1811 C ATOM 3041 CD1 ILE B 108 20.264 49.485 42.084 1.00 59.40 C ANISOU 3041 CD1 ILE B 108 6550 5846 10173 115 527 -1725 C ATOM 3042 N THR B 109 15.210 49.570 40.456 1.00 45.06 N ANISOU 3042 N THR B 109 4688 3921 8513 365 523 -1420 N ATOM 3043 CA THR B 109 14.188 50.363 39.773 1.00 45.05 C ANISOU 3043 CA THR B 109 4641 3779 8696 432 519 -1333 C ATOM 3044 C THR B 109 12.854 49.639 39.510 1.00 50.92 C ANISOU 3044 C THR B 109 5379 4611 9357 486 494 -1262 C ATOM 3045 O THR B 109 11.858 50.315 39.228 1.00 50.56 O ANISOU 3045 O THR B 109 5275 4461 9473 549 493 -1234 O ATOM 3046 CB THR B 109 14.763 50.931 38.444 1.00 48.40 C ANISOU 3046 CB THR B 109 5091 4071 9228 429 495 -1139 C ATOM 3047 OG1 THR B 109 14.780 49.888 37.463 1.00 47.42 O ANISOU 3047 OG1 THR B 109 5039 4057 8922 425 449 -960 O ATOM 3048 CG2 THR B 109 16.165 51.557 38.599 1.00 44.69 C ANISOU 3048 CG2 THR B 109 4625 3515 8842 367 521 -1190 C ATOM 3049 N GLU B 110 12.839 48.282 39.533 1.00 47.86 N ANISOU 3049 N GLU B 110 5046 4403 8736 463 471 -1224 N ATOM 3050 CA GLU B 110 11.683 47.431 39.206 1.00 47.57 C ANISOU 3050 CA GLU B 110 5009 4460 8607 501 442 -1147 C ATOM 3051 C GLU B 110 11.317 47.520 37.709 1.00 52.76 C ANISOU 3051 C GLU B 110 5685 5051 9312 538 382 -932 C ATOM 3052 O GLU B 110 10.227 47.102 37.315 1.00 54.92 O ANISOU 3052 O GLU B 110 5937 5362 9568 581 348 -865 O ATOM 3053 CB GLU B 110 10.462 47.730 40.111 1.00 48.57 C ANISOU 3053 CB GLU B 110 5052 4588 8815 548 482 -1283 C ATOM 3054 CG GLU B 110 10.061 46.547 40.960 1.00 55.33 C ANISOU 3054 CG GLU B 110 5919 5628 9476 528 501 -1358 C ATOM 3055 CD GLU B 110 8.834 46.752 41.821 1.00 75.71 C ANISOU 3055 CD GLU B 110 8418 8225 12125 572 551 -1482 C ATOM 3056 OE1 GLU B 110 8.991 46.888 43.057 1.00 54.18 O ANISOU 3056 OE1 GLU B 110 5671 5555 9358 553 612 -1660 O ATOM 3057 OE2 GLU B 110 7.713 46.761 41.262 1.00 74.82 O ANISOU 3057 OE2 GLU B 110 8255 8074 12099 627 529 -1403 O ATOM 3058 N SER B 111 12.227 48.058 36.879 1.00 47.49 N ANISOU 3058 N SER B 111 5054 4289 8700 519 368 -825 N ATOM 3059 CA SER B 111 12.026 48.259 35.443 1.00 45.76 C ANISOU 3059 CA SER B 111 4861 4006 8520 550 316 -615 C ATOM 3060 C SER B 111 13.208 47.815 34.594 1.00 46.37 C ANISOU 3060 C SER B 111 5025 4119 8475 500 301 -493 C ATOM 3061 O SER B 111 14.333 47.771 35.083 1.00 45.91 O ANISOU 3061 O SER B 111 4990 4077 8378 443 338 -570 O ATOM 3062 CB SER B 111 11.679 49.713 35.142 1.00 46.83 C ANISOU 3062 CB SER B 111 4935 3942 8916 599 324 -580 C ATOM 3063 OG SER B 111 12.756 50.548 35.518 1.00 54.95 O ANISOU 3063 OG SER B 111 5957 4864 10057 559 375 -656 O ATOM 3064 N TRP B 112 12.934 47.490 33.314 1.00 40.70 N ANISOU 3064 N TRP B 112 4351 3420 7695 523 246 -305 N ATOM 3065 CA TRP B 112 13.919 47.075 32.316 1.00 38.69 C ANISOU 3065 CA TRP B 112 4179 3202 7321 485 234 -169 C ATOM 3066 C TRP B 112 14.375 48.275 31.497 1.00 42.50 C ANISOU 3066 C TRP B 112 4660 3523 7967 497 246 -41 C ATOM 3067 O TRP B 112 13.592 48.846 30.735 1.00 41.14 O ANISOU 3067 O TRP B 112 4468 3273 7889 554 207 83 O ATOM 3068 CB TRP B 112 13.353 45.996 31.400 1.00 36.22 C ANISOU 3068 CB TRP B 112 3919 3014 6830 502 169 -50 C ATOM 3069 CG TRP B 112 14.413 45.420 30.509 1.00 36.15 C ANISOU 3069 CG TRP B 112 3997 3066 6674 459 169 58 C ATOM 3070 CD1 TRP B 112 14.615 45.701 29.193 1.00 38.82 C ANISOU 3070 CD1 TRP B 112 4382 3371 6999 472 145 239 C ATOM 3071 CD2 TRP B 112 15.485 44.550 30.905 1.00 35.07 C ANISOU 3071 CD2 TRP B 112 3905 3026 6394 397 202 -12 C ATOM 3072 NE1 TRP B 112 15.713 45.013 28.728 1.00 38.23 N ANISOU 3072 NE1 TRP B 112 4379 3373 6775 422 167 279 N ATOM 3073 CE2 TRP B 112 16.265 44.298 29.758 1.00 38.98 C ANISOU 3073 CE2 TRP B 112 4472 3544 6797 377 200 127 C ATOM 3074 CE3 TRP B 112 15.824 43.903 32.104 1.00 35.71 C ANISOU 3074 CE3 TRP B 112 3974 3186 6409 361 231 -173 C ATOM 3075 CZ2 TRP B 112 17.378 43.450 29.780 1.00 37.57 C ANISOU 3075 CZ2 TRP B 112 4343 3453 6479 323 229 102 C ATOM 3076 CZ3 TRP B 112 16.907 43.040 32.115 1.00 36.75 C ANISOU 3076 CZ3 TRP B 112 4159 3407 6399 309 249 -186 C ATOM 3077 CH2 TRP B 112 17.678 42.831 30.966 1.00 37.13 C ANISOU 3077 CH2 TRP B 112 4269 3464 6374 292 250 -54 C ATOM 3078 N LEU B 113 15.645 48.660 31.666 1.00 40.19 N ANISOU 3078 N LEU B 113 4382 3177 7712 442 299 -68 N ATOM 3079 CA LEU B 113 16.203 49.845 31.012 1.00 40.95 C ANISOU 3079 CA LEU B 113 4469 3106 7982 441 326 43 C ATOM 3080 C LEU B 113 17.144 49.566 29.837 1.00 46.07 C ANISOU 3080 C LEU B 113 5196 3786 8523 407 333 214 C ATOM 3081 O LEU B 113 17.800 50.503 29.382 1.00 46.50 O ANISOU 3081 O LEU B 113 5244 3709 8714 390 373 298 O ATOM 3082 CB LEU B 113 16.924 50.731 32.065 1.00 41.24 C ANISOU 3082 CB LEU B 113 4446 3025 8199 404 389 -120 C ATOM 3083 CG LEU B 113 16.172 51.058 33.382 1.00 46.51 C ANISOU 3083 CG LEU B 113 5037 3671 8964 428 400 -329 C ATOM 3084 CD1 LEU B 113 17.093 51.712 34.382 1.00 47.39 C ANISOU 3084 CD1 LEU B 113 5107 3709 9191 375 455 -505 C ATOM 3085 CD2 LEU B 113 14.967 51.941 33.142 1.00 47.22 C ANISOU 3085 CD2 LEU B 113 5068 3633 9243 505 380 -283 C ATOM 3086 N PHE B 114 17.183 48.319 29.311 1.00 42.96 N ANISOU 3086 N PHE B 114 4871 3558 7893 397 300 270 N ATOM 3087 CA PHE B 114 18.133 47.908 28.262 1.00 43.02 C ANISOU 3087 CA PHE B 114 4954 3618 7772 362 317 407 C ATOM 3088 C PHE B 114 17.550 47.558 26.871 1.00 45.76 C ANISOU 3088 C PHE B 114 5364 4026 7996 402 261 603 C ATOM 3089 O PHE B 114 18.307 47.149 25.981 1.00 45.22 O ANISOU 3089 O PHE B 114 5364 4018 7802 375 280 711 O ATOM 3090 CB PHE B 114 18.983 46.734 28.777 1.00 45.41 C ANISOU 3090 CB PHE B 114 5290 4062 7900 305 338 296 C ATOM 3091 CG PHE B 114 19.721 47.093 30.044 1.00 47.72 C ANISOU 3091 CG PHE B 114 5528 4307 8297 261 387 118 C ATOM 3092 CD1 PHE B 114 20.910 47.808 29.996 1.00 51.26 C ANISOU 3092 CD1 PHE B 114 5961 4659 8856 213 447 127 C ATOM 3093 CD2 PHE B 114 19.202 46.755 31.290 1.00 50.40 C ANISOU 3093 CD2 PHE B 114 5826 4697 8626 266 373 -59 C ATOM 3094 CE1 PHE B 114 21.570 48.175 31.172 1.00 52.26 C ANISOU 3094 CE1 PHE B 114 6031 4743 9083 171 480 -48 C ATOM 3095 CE2 PHE B 114 19.855 47.131 32.461 1.00 53.26 C ANISOU 3095 CE2 PHE B 114 6139 5023 9075 227 411 -228 C ATOM 3096 CZ PHE B 114 21.044 47.824 32.394 1.00 51.26 C ANISOU 3096 CZ PHE B 114 5870 4677 8929 179 459 -226 C ATOM 3097 N GLY B 115 16.244 47.739 26.688 1.00 41.77 N ANISOU 3097 N GLY B 115 4833 3509 7530 467 195 643 N ATOM 3098 CA GLY B 115 15.588 47.471 25.412 1.00 41.33 C ANISOU 3098 CA GLY B 115 4827 3513 7363 511 126 821 C ATOM 3099 C GLY B 115 15.183 46.033 25.162 1.00 44.28 C ANISOU 3099 C GLY B 115 5250 4071 7504 508 70 795 C ATOM 3100 O GLY B 115 15.539 45.136 25.926 1.00 42.86 O ANISOU 3100 O GLY B 115 5075 3980 7229 468 92 653 O ATOM 3101 N HIS B 116 14.459 45.818 24.047 1.00 42.48 N ANISOU 3101 N HIS B 116 5058 3899 7183 552 -7 938 N ATOM 3102 CA HIS B 116 13.875 44.549 23.619 1.00 43.55 C ANISOU 3102 CA HIS B 116 5235 4198 7114 558 -78 931 C ATOM 3103 C HIS B 116 14.891 43.436 23.372 1.00 47.08 C ANISOU 3103 C HIS B 116 5761 4770 7359 500 -41 899 C ATOM 3104 O HIS B 116 14.706 42.336 23.912 1.00 47.61 O ANISOU 3104 O HIS B 116 5829 4938 7323 479 -56 778 O ATOM 3105 CB HIS B 116 12.970 44.743 22.394 1.00 45.62 C ANISOU 3105 CB HIS B 116 5518 4483 7333 617 -173 1102 C ATOM 3106 CG HIS B 116 11.786 45.614 22.676 1.00 50.72 C ANISOU 3106 CG HIS B 116 6076 5027 8169 684 -227 1118 C ATOM 3107 ND1 HIS B 116 10.547 45.073 22.995 1.00 53.59 N ANISOU 3107 ND1 HIS B 116 6388 5453 8522 718 -305 1049 N ATOM 3108 CD2 HIS B 116 11.694 46.968 22.698 1.00 53.59 C ANISOU 3108 CD2 HIS B 116 6389 5226 8747 720 -209 1192 C ATOM 3109 CE1 HIS B 116 9.740 46.113 23.191 1.00 53.45 C ANISOU 3109 CE1 HIS B 116 6288 5312 8708 778 -332 1082 C ATOM 3110 NE2 HIS B 116 10.387 47.276 23.025 1.00 53.70 N ANISOU 3110 NE2 HIS B 116 6319 5201 8883 783 -277 1167 N ATOM 3111 N ALA B 117 15.951 43.705 22.573 1.00 40.95 N ANISOU 3111 N ALA B 117 5044 3981 6533 473 12 1009 N ATOM 3112 CA ALA B 117 16.987 42.715 22.256 1.00 39.22 C ANISOU 3112 CA ALA B 117 4895 3871 6135 422 57 987 C ATOM 3113 C ALA B 117 17.673 42.177 23.503 1.00 42.84 C ANISOU 3113 C ALA B 117 5323 4341 6611 372 116 807 C ATOM 3114 O ALA B 117 17.767 40.957 23.647 1.00 44.33 O ANISOU 3114 O ALA B 117 5542 4646 6654 351 105 728 O ATOM 3115 CB ALA B 117 18.015 43.297 21.299 1.00 39.37 C ANISOU 3115 CB ALA B 117 4967 3856 6137 403 121 1135 C ATOM 3116 N LEU B 118 18.098 43.067 24.429 1.00 37.24 N ANISOU 3116 N LEU B 118 4553 3513 6085 356 171 741 N ATOM 3117 CA LEU B 118 18.785 42.654 25.654 1.00 36.27 C ANISOU 3117 CA LEU B 118 4398 3403 5980 311 219 572 C ATOM 3118 C LEU B 118 17.860 41.977 26.663 1.00 38.92 C ANISOU 3118 C LEU B 118 4695 3797 6297 325 174 432 C ATOM 3119 O LEU B 118 18.346 41.237 27.524 1.00 38.38 O ANISOU 3119 O LEU B 118 4621 3788 6173 290 199 308 O ATOM 3120 CB LEU B 118 19.593 43.796 26.293 1.00 36.24 C ANISOU 3120 CB LEU B 118 4342 3262 6166 284 289 534 C ATOM 3121 CG LEU B 118 20.807 44.284 25.482 1.00 41.20 C ANISOU 3121 CG LEU B 118 5003 3842 6809 249 356 650 C ATOM 3122 CD1 LEU B 118 21.506 45.438 26.178 1.00 42.00 C ANISOU 3122 CD1 LEU B 118 5039 3794 7124 220 418 600 C ATOM 3123 CD2 LEU B 118 21.807 43.162 25.208 1.00 42.27 C ANISOU 3123 CD2 LEU B 118 5192 4100 6771 207 391 630 C ATOM 3124 N CYS B 119 16.531 42.151 26.514 1.00 35.36 N ANISOU 3124 N CYS B 119 4218 3338 5880 376 108 461 N ATOM 3125 CA CYS B 119 15.550 41.463 27.356 1.00 34.84 C ANISOU 3125 CA CYS B 119 4112 3334 5792 390 68 344 C ATOM 3126 C CYS B 119 15.565 39.947 27.022 1.00 36.21 C ANISOU 3126 C CYS B 119 4342 3654 5761 370 38 330 C ATOM 3127 O CYS B 119 15.262 39.127 27.880 1.00 34.81 O ANISOU 3127 O CYS B 119 4144 3541 5540 357 33 218 O ATOM 3128 CB CYS B 119 14.158 42.085 27.225 1.00 35.11 C ANISOU 3128 CB CYS B 119 4092 3315 5933 451 8 385 C ATOM 3129 SG CYS B 119 12.846 41.169 28.074 1.00 39.12 S ANISOU 3129 SG CYS B 119 4547 3908 6409 469 -38 262 S ATOM 3130 N LYS B 120 15.987 39.582 25.802 1.00 32.34 N ANISOU 3130 N LYS B 120 3924 3214 5149 364 27 440 N ATOM 3131 CA LYS B 120 16.141 38.174 25.432 1.00 31.69 C ANISOU 3131 CA LYS B 120 3897 3260 4883 342 6 418 C ATOM 3132 C LYS B 120 17.561 37.686 25.739 1.00 36.64 C ANISOU 3132 C LYS B 120 4556 3914 5452 292 80 365 C ATOM 3133 O LYS B 120 17.703 36.629 26.333 1.00 38.24 O ANISOU 3133 O LYS B 120 4761 4186 5582 269 83 268 O ATOM 3134 CB LYS B 120 15.779 37.928 23.962 1.00 32.62 C ANISOU 3134 CB LYS B 120 4075 3436 4883 366 -54 545 C ATOM 3135 CG LYS B 120 14.285 37.892 23.769 1.00 30.12 C ANISOU 3135 CG LYS B 120 3722 3133 4591 412 -147 563 C ATOM 3136 CD LYS B 120 13.880 37.651 22.346 1.00 33.34 C ANISOU 3136 CD LYS B 120 4187 3617 4863 433 -221 673 C ATOM 3137 CE LYS B 120 12.374 37.661 22.203 1.00 29.77 C ANISOU 3137 CE LYS B 120 3686 3175 4450 481 -324 696 C ATOM 3138 NZ LYS B 120 11.767 36.429 22.763 1.00 34.86 N ANISOU 3138 NZ LYS B 120 4314 3908 5022 464 -367 586 N ATOM 3139 N VAL B 121 18.598 38.483 25.391 1.00 31.33 N ANISOU 3139 N VAL B 121 3897 3178 4829 275 140 428 N ATOM 3140 CA VAL B 121 20.021 38.153 25.511 1.00 30.37 C ANISOU 3140 CA VAL B 121 3798 3074 4669 229 213 396 C ATOM 3141 C VAL B 121 20.520 38.018 26.974 1.00 33.28 C ANISOU 3141 C VAL B 121 4113 3427 5106 200 245 249 C ATOM 3142 O VAL B 121 21.156 37.000 27.280 1.00 31.21 O ANISOU 3142 O VAL B 121 3867 3239 4751 173 262 184 O ATOM 3143 CB VAL B 121 20.890 39.139 24.678 1.00 33.91 C ANISOU 3143 CB VAL B 121 4265 3449 5170 220 270 516 C ATOM 3144 CG1 VAL B 121 22.384 38.909 24.888 1.00 33.12 C ANISOU 3144 CG1 VAL B 121 4169 3355 5060 171 351 477 C ATOM 3145 CG2 VAL B 121 20.551 39.032 23.198 1.00 33.97 C ANISOU 3145 CG2 VAL B 121 4341 3505 5060 245 240 661 C ATOM 3146 N ILE B 122 20.257 39.019 27.860 1.00 29.78 N ANISOU 3146 N ILE B 122 3605 2891 4820 206 254 196 N ATOM 3147 CA ILE B 122 20.774 39.009 29.248 1.00 28.82 C ANISOU 3147 CA ILE B 122 3434 2760 4758 177 284 54 C ATOM 3148 C ILE B 122 20.128 37.856 30.070 1.00 31.19 C ANISOU 3148 C ILE B 122 3728 3158 4963 180 248 -44 C ATOM 3149 O ILE B 122 20.912 37.059 30.600 1.00 30.92 O ANISOU 3149 O ILE B 122 3702 3186 4860 150 267 -110 O ATOM 3150 CB ILE B 122 20.751 40.415 29.932 1.00 31.60 C ANISOU 3150 CB ILE B 122 3719 2986 5302 180 307 11 C ATOM 3151 CG1 ILE B 122 21.845 41.308 29.276 1.00 30.22 C ANISOU 3151 CG1 ILE B 122 3548 2721 5213 154 362 92 C ATOM 3152 CG2 ILE B 122 20.977 40.331 31.463 1.00 32.97 C ANISOU 3152 CG2 ILE B 122 3841 3173 5513 158 320 -155 C ATOM 3153 CD1 ILE B 122 21.639 42.747 29.376 1.00 34.93 C ANISOU 3153 CD1 ILE B 122 4096 3174 6001 167 378 113 C ATOM 3154 N PRO B 123 18.787 37.620 30.085 1.00 28.45 N ANISOU 3154 N PRO B 123 3371 2836 4604 214 197 -44 N ATOM 3155 CA PRO B 123 18.254 36.444 30.812 1.00 27.66 C ANISOU 3155 CA PRO B 123 3267 2829 4414 210 173 -126 C ATOM 3156 C PRO B 123 18.792 35.125 30.257 1.00 29.84 C ANISOU 3156 C PRO B 123 3603 3196 4540 190 166 -101 C ATOM 3157 O PRO B 123 19.094 34.209 31.025 1.00 30.32 O ANISOU 3157 O PRO B 123 3663 3318 4540 169 174 -175 O ATOM 3158 CB PRO B 123 16.739 36.572 30.610 1.00 29.09 C ANISOU 3158 CB PRO B 123 3422 3005 4626 250 121 -102 C ATOM 3159 CG PRO B 123 16.538 38.062 30.467 1.00 33.54 C ANISOU 3159 CG PRO B 123 3948 3454 5343 276 130 -64 C ATOM 3160 CD PRO B 123 17.670 38.433 29.558 1.00 30.02 C ANISOU 3160 CD PRO B 123 3549 2973 4885 259 159 26 C ATOM 3161 N TYR B 124 18.974 35.059 28.933 1.00 24.35 N ANISOU 3161 N TYR B 124 2959 2506 3786 197 156 2 N ATOM 3162 CA TYR B 124 19.540 33.906 28.248 1.00 24.53 C ANISOU 3162 CA TYR B 124 3041 2607 3674 181 157 23 C ATOM 3163 C TYR B 124 20.966 33.597 28.737 1.00 28.69 C ANISOU 3163 C TYR B 124 3569 3143 4188 146 214 -25 C ATOM 3164 O TYR B 124 21.221 32.473 29.162 1.00 28.42 O ANISOU 3164 O TYR B 124 3544 3171 4081 132 212 -81 O ATOM 3165 CB TYR B 124 19.525 34.134 26.733 1.00 25.79 C ANISOU 3165 CB TYR B 124 3254 2769 3777 197 143 142 C ATOM 3166 CG TYR B 124 20.320 33.117 25.952 1.00 27.00 C ANISOU 3166 CG TYR B 124 3469 2994 3797 179 163 159 C ATOM 3167 CD1 TYR B 124 19.821 31.832 25.725 1.00 28.70 C ANISOU 3167 CD1 TYR B 124 3712 3287 3904 180 121 123 C ATOM 3168 CD2 TYR B 124 21.559 33.444 25.408 1.00 27.28 C ANISOU 3168 CD2 TYR B 124 3530 3013 3823 162 228 205 C ATOM 3169 CE1 TYR B 124 20.552 30.891 24.998 1.00 29.00 C ANISOU 3169 CE1 TYR B 124 3805 3384 3828 166 143 125 C ATOM 3170 CE2 TYR B 124 22.291 32.514 24.667 1.00 27.94 C ANISOU 3170 CE2 TYR B 124 3666 3162 3786 149 255 213 C ATOM 3171 CZ TYR B 124 21.782 31.242 24.465 1.00 31.11 C ANISOU 3171 CZ TYR B 124 4098 3641 4083 153 211 169 C ATOM 3172 OH TYR B 124 22.486 30.357 23.697 1.00 29.67 O ANISOU 3172 OH TYR B 124 3966 3517 3790 144 241 167 O ATOM 3173 N LEU B 125 21.852 34.596 28.713 1.00 24.68 N ANISOU 3173 N LEU B 125 3046 2568 3761 133 263 -2 N ATOM 3174 CA LEU B 125 23.257 34.396 29.150 1.00 23.73 C ANISOU 3174 CA LEU B 125 2914 2453 3649 99 315 -48 C ATOM 3175 C LEU B 125 23.305 34.047 30.635 1.00 27.05 C ANISOU 3175 C LEU B 125 3289 2896 4092 86 307 -166 C ATOM 3176 O LEU B 125 24.221 33.336 31.027 1.00 26.57 O ANISOU 3176 O LEU B 125 3229 2881 3985 66 323 -207 O ATOM 3177 CB LEU B 125 24.085 35.648 28.855 1.00 23.57 C ANISOU 3177 CB LEU B 125 2876 2348 3733 83 368 1 C ATOM 3178 CG LEU B 125 24.297 35.966 27.381 1.00 27.56 C ANISOU 3178 CG LEU B 125 3431 2838 4204 90 392 132 C ATOM 3179 CD1 LEU B 125 25.039 37.278 27.221 1.00 27.72 C ANISOU 3179 CD1 LEU B 125 3419 2754 4358 73 446 183 C ATOM 3180 CD2 LEU B 125 25.038 34.840 26.685 1.00 28.25 C ANISOU 3180 CD2 LEU B 125 3570 3009 4156 80 419 153 C ATOM 3181 N GLN B 126 22.404 34.618 31.433 1.00 23.97 N ANISOU 3181 N GLN B 126 2860 2481 3769 99 283 -218 N ATOM 3182 CA GLN B 126 22.365 34.319 32.885 1.00 24.13 C ANISOU 3182 CA GLN B 126 2839 2533 3794 89 277 -329 C ATOM 3183 C GLN B 126 22.011 32.841 33.103 1.00 28.54 C ANISOU 3183 C GLN B 126 3423 3185 4234 91 251 -346 C ATOM 3184 O GLN B 126 22.664 32.208 33.913 1.00 30.39 O ANISOU 3184 O GLN B 126 3648 3468 4432 74 256 -404 O ATOM 3185 CB GLN B 126 21.388 35.276 33.570 1.00 25.69 C ANISOU 3185 CB GLN B 126 2990 2683 4088 108 266 -378 C ATOM 3186 CG GLN B 126 21.263 35.072 35.070 1.00 32.94 C ANISOU 3186 CG GLN B 126 3869 3646 5003 98 267 -499 C ATOM 3187 CD GLN B 126 22.595 35.033 35.772 1.00 52.12 C ANISOU 3187 CD GLN B 126 6280 6093 7429 66 286 -565 C ATOM 3188 OE1 GLN B 126 23.470 35.852 35.531 1.00 50.68 O ANISOU 3188 OE1 GLN B 126 6073 5844 7338 49 309 -579 O ATOM 3189 NE2 GLN B 126 22.762 34.066 36.653 1.00 40.80 N ANISOU 3189 NE2 GLN B 126 4856 4749 5897 56 274 -604 N ATOM 3190 N THR B 127 21.013 32.324 32.389 1.00 22.87 N ANISOU 3190 N THR B 127 2736 2491 3463 111 219 -295 N ATOM 3191 CA THR B 127 20.610 30.896 32.504 1.00 21.65 C ANISOU 3191 CA THR B 127 2603 2411 3213 109 195 -309 C ATOM 3192 C THR B 127 21.692 29.967 31.942 1.00 24.75 C ANISOU 3192 C THR B 127 3038 2837 3529 96 209 -284 C ATOM 3193 O THR B 127 21.839 28.872 32.470 1.00 23.55 O ANISOU 3193 O THR B 127 2891 2734 3322 87 204 -316 O ATOM 3194 CB THR B 127 19.181 30.630 32.022 1.00 25.47 C ANISOU 3194 CB THR B 127 3092 2906 3681 130 152 -278 C ATOM 3195 OG1 THR B 127 19.054 31.051 30.671 1.00 26.69 O ANISOU 3195 OG1 THR B 127 3279 3032 3828 145 136 -196 O ATOM 3196 CG2 THR B 127 18.137 31.301 32.886 1.00 22.02 C ANISOU 3196 CG2 THR B 127 2600 2448 3319 144 145 -323 C ATOM 3197 N VAL B 128 22.363 30.388 30.868 1.00 21.93 N ANISOU 3197 N VAL B 128 2709 2451 3173 95 232 -225 N ATOM 3198 CA VAL B 128 23.449 29.587 30.231 1.00 22.27 C ANISOU 3198 CA VAL B 128 2787 2522 3153 84 260 -205 C ATOM 3199 C VAL B 128 24.574 29.412 31.252 1.00 27.79 C ANISOU 3199 C VAL B 128 3450 3230 3879 65 286 -266 C ATOM 3200 O VAL B 128 25.060 28.291 31.392 1.00 28.74 O ANISOU 3200 O VAL B 128 3579 3392 3947 62 285 -288 O ATOM 3201 CB VAL B 128 23.957 30.260 28.943 1.00 25.12 C ANISOU 3201 CB VAL B 128 3180 2853 3512 86 292 -126 C ATOM 3202 CG1 VAL B 128 25.348 29.785 28.567 1.00 24.41 C ANISOU 3202 CG1 VAL B 128 3107 2784 3386 71 343 -123 C ATOM 3203 CG2 VAL B 128 22.998 30.070 27.787 1.00 24.66 C ANISOU 3203 CG2 VAL B 128 3169 2814 3388 107 255 -65 C ATOM 3204 N SER B 129 24.888 30.483 31.980 1.00 23.89 N ANISOU 3204 N SER B 129 2911 2694 3473 55 301 -296 N ATOM 3205 CA SER B 129 25.936 30.537 33.027 1.00 24.13 C ANISOU 3205 CA SER B 129 2896 2731 3540 36 313 -361 C ATOM 3206 C SER B 129 25.613 29.587 34.188 1.00 27.23 C ANISOU 3206 C SER B 129 3279 3188 3880 38 281 -418 C ATOM 3207 O SER B 129 26.539 28.943 34.684 1.00 27.06 O ANISOU 3207 O SER B 129 3246 3202 3834 31 282 -441 O ATOM 3208 CB SER B 129 26.103 31.961 33.479 1.00 29.59 C ANISOU 3208 CB SER B 129 3541 3358 4342 24 327 -393 C ATOM 3209 OG SER B 129 26.639 32.024 34.781 1.00 44.47 O ANISOU 3209 OG SER B 129 5379 5265 6251 10 315 -482 O ATOM 3210 N VAL B 130 24.354 29.527 34.628 1.00 24.34 N ANISOU 3210 N VAL B 130 2914 2838 3497 50 253 -433 N ATOM 3211 CA VAL B 130 23.957 28.594 35.723 1.00 23.12 C ANISOU 3211 CA VAL B 130 2752 2745 3288 51 231 -471 C ATOM 3212 C VAL B 130 24.142 27.153 35.232 1.00 25.78 C ANISOU 3212 C VAL B 130 3126 3117 3552 55 223 -434 C ATOM 3213 O VAL B 130 24.617 26.331 35.997 1.00 25.95 O ANISOU 3213 O VAL B 130 3140 3181 3541 51 216 -452 O ATOM 3214 CB VAL B 130 22.501 28.828 36.162 1.00 26.93 C ANISOU 3214 CB VAL B 130 3222 3232 3779 62 216 -489 C ATOM 3215 CG1 VAL B 130 22.115 27.907 37.299 1.00 25.76 C ANISOU 3215 CG1 VAL B 130 3068 3150 3568 60 204 -514 C ATOM 3216 CG2 VAL B 130 22.236 30.278 36.517 1.00 27.20 C ANISOU 3216 CG2 VAL B 130 3215 3223 3896 62 228 -539 C ATOM 3217 N SER B 131 23.750 26.892 33.989 1.00 20.92 N ANISOU 3217 N SER B 131 2550 2484 2914 63 222 -383 N ATOM 3218 CA SER B 131 23.860 25.557 33.355 1.00 21.07 C ANISOU 3218 CA SER B 131 2606 2526 2874 67 216 -360 C ATOM 3219 C SER B 131 25.333 25.148 33.223 1.00 25.87 C ANISOU 3219 C SER B 131 3213 3136 3479 63 244 -361 C ATOM 3220 O SER B 131 25.645 24.009 33.556 1.00 25.07 O ANISOU 3220 O SER B 131 3116 3059 3351 66 238 -368 O ATOM 3221 CB SER B 131 23.160 25.579 32.031 1.00 24.84 C ANISOU 3221 CB SER B 131 3124 2989 3323 75 205 -318 C ATOM 3222 OG SER B 131 23.262 24.336 31.375 1.00 32.27 O ANISOU 3222 OG SER B 131 4102 3949 4210 77 202 -311 O ATOM 3223 N VAL B 132 26.198 26.072 32.793 1.00 20.78 N ANISOU 3223 N VAL B 132 2557 2463 2876 57 276 -352 N ATOM 3224 CA VAL B 132 27.659 25.802 32.654 1.00 19.13 C ANISOU 3224 CA VAL B 132 2333 2254 2682 53 309 -356 C ATOM 3225 C VAL B 132 28.237 25.533 34.043 1.00 23.22 C ANISOU 3225 C VAL B 132 2805 2800 3218 49 289 -401 C ATOM 3226 O VAL B 132 28.988 24.581 34.182 1.00 23.48 O ANISOU 3226 O VAL B 132 2833 2854 3235 56 289 -403 O ATOM 3227 CB VAL B 132 28.390 26.954 31.937 1.00 21.79 C ANISOU 3227 CB VAL B 132 2660 2549 3071 41 355 -332 C ATOM 3228 CG1 VAL B 132 29.898 26.818 32.036 1.00 20.80 C ANISOU 3228 CG1 VAL B 132 2500 2426 2979 34 390 -345 C ATOM 3229 CG2 VAL B 132 27.978 27.062 30.487 1.00 21.39 C ANISOU 3229 CG2 VAL B 132 2662 2485 2980 49 375 -274 C ATOM 3230 N ALA B 133 27.818 26.316 35.036 1.00 20.80 N ANISOU 3230 N ALA B 133 2465 2496 2941 39 270 -438 N ATOM 3231 CA ALA B 133 28.304 26.174 36.424 1.00 20.26 C ANISOU 3231 CA ALA B 133 2355 2469 2873 35 243 -486 C ATOM 3232 C ALA B 133 27.988 24.796 37.015 1.00 24.08 C ANISOU 3232 C ALA B 133 2857 3001 3293 48 216 -472 C ATOM 3233 O ALA B 133 28.908 24.153 37.502 1.00 24.35 O ANISOU 3233 O ALA B 133 2874 3059 3320 54 206 -470 O ATOM 3234 CB ALA B 133 27.759 27.291 37.272 1.00 20.03 C ANISOU 3234 CB ALA B 133 2299 2440 2871 25 230 -536 C ATOM 3235 N VAL B 134 26.729 24.372 36.954 1.00 20.93 N ANISOU 3235 N VAL B 134 2487 2608 2857 53 206 -455 N ATOM 3236 CA VAL B 134 26.291 23.088 37.512 1.00 21.48 C ANISOU 3236 CA VAL B 134 2571 2713 2878 60 186 -436 C ATOM 3237 C VAL B 134 26.765 21.879 36.668 1.00 24.23 C ANISOU 3237 C VAL B 134 2943 3043 3218 71 193 -401 C ATOM 3238 O VAL B 134 27.107 20.846 37.247 1.00 22.91 O ANISOU 3238 O VAL B 134 2769 2897 3037 80 179 -387 O ATOM 3239 CB VAL B 134 24.749 23.050 37.791 1.00 25.49 C ANISOU 3239 CB VAL B 134 3092 3229 3365 57 179 -432 C ATOM 3240 CG1 VAL B 134 23.922 23.208 36.515 1.00 24.91 C ANISOU 3240 CG1 VAL B 134 3055 3120 3290 60 181 -401 C ATOM 3241 CG2 VAL B 134 24.372 21.776 38.523 1.00 25.18 C ANISOU 3241 CG2 VAL B 134 3045 3240 3284 56 164 -423 C ATOM 3242 N LEU B 135 26.818 22.011 35.322 1.00 22.08 N ANISOU 3242 N LEU B 135 2701 2734 2956 73 216 -388 N ATOM 3243 CA LEU B 135 27.315 20.921 34.482 1.00 23.03 C ANISOU 3243 CA LEU B 135 2843 2838 3068 85 230 -373 C ATOM 3244 C LEU B 135 28.814 20.755 34.714 1.00 26.51 C ANISOU 3244 C LEU B 135 3249 3281 3541 94 245 -379 C ATOM 3245 O LEU B 135 29.269 19.616 34.767 1.00 26.51 O ANISOU 3245 O LEU B 135 3249 3279 3546 110 243 -370 O ATOM 3246 CB LEU B 135 26.985 21.037 32.981 1.00 23.83 C ANISOU 3246 CB LEU B 135 2988 2914 3152 86 252 -363 C ATOM 3247 CG LEU B 135 25.497 20.881 32.580 1.00 28.52 C ANISOU 3247 CG LEU B 135 3613 3506 3715 81 225 -355 C ATOM 3248 CD1 LEU B 135 25.293 21.247 31.115 1.00 28.82 C ANISOU 3248 CD1 LEU B 135 3692 3533 3725 83 238 -344 C ATOM 3249 CD2 LEU B 135 24.967 19.473 32.880 1.00 29.05 C ANISOU 3249 CD2 LEU B 135 3690 3574 3773 82 203 -357 C ATOM 3250 N THR B 136 29.561 21.875 34.952 1.00 22.86 N ANISOU 3250 N THR B 136 2752 2821 3115 85 257 -397 N ATOM 3251 CA THR B 136 31.005 21.852 35.252 1.00 22.04 C ANISOU 3251 CA THR B 136 2599 2722 3055 90 266 -409 C ATOM 3252 C THR B 136 31.227 21.121 36.572 1.00 24.59 C ANISOU 3252 C THR B 136 2892 3083 3367 101 219 -410 C ATOM 3253 O THR B 136 32.068 20.221 36.640 1.00 24.23 O ANISOU 3253 O THR B 136 2827 3038 3342 120 216 -397 O ATOM 3254 CB THR B 136 31.611 23.273 35.255 1.00 24.36 C ANISOU 3254 CB THR B 136 2855 3002 3399 69 284 -433 C ATOM 3255 OG1 THR B 136 31.473 23.828 33.949 1.00 23.01 O ANISOU 3255 OG1 THR B 136 2715 2794 3233 63 332 -412 O ATOM 3256 CG2 THR B 136 33.089 23.277 35.646 1.00 20.82 C ANISOU 3256 CG2 THR B 136 2342 2561 3006 70 287 -451 C ATOM 3257 N LEU B 137 30.463 21.491 37.604 1.00 20.02 N ANISOU 3257 N LEU B 137 2310 2540 2756 91 185 -421 N ATOM 3258 CA LEU B 137 30.528 20.831 38.908 1.00 20.93 C ANISOU 3258 CA LEU B 137 2406 2707 2840 100 141 -412 C ATOM 3259 C LEU B 137 30.177 19.349 38.808 1.00 24.95 C ANISOU 3259 C LEU B 137 2945 3206 3331 119 136 -362 C ATOM 3260 O LEU B 137 30.827 18.542 39.471 1.00 23.92 O ANISOU 3260 O LEU B 137 2791 3095 3203 138 109 -335 O ATOM 3261 CB LEU B 137 29.644 21.533 39.965 1.00 20.72 C ANISOU 3261 CB LEU B 137 2378 2727 2769 85 119 -438 C ATOM 3262 CG LEU B 137 30.086 22.942 40.383 1.00 24.92 C ANISOU 3262 CG LEU B 137 2870 3270 3328 67 114 -501 C ATOM 3263 CD1 LEU B 137 29.080 23.544 41.345 1.00 24.31 C ANISOU 3263 CD1 LEU B 137 2796 3235 3207 56 102 -537 C ATOM 3264 CD2 LEU B 137 31.510 22.958 40.986 1.00 24.82 C ANISOU 3264 CD2 LEU B 137 2802 3287 3340 71 83 -522 C ATOM 3265 N SER B 138 29.198 18.989 37.937 1.00 22.91 N ANISOU 3265 N SER B 138 2732 2911 3063 115 158 -349 N ATOM 3266 CA SER B 138 28.785 17.600 37.698 1.00 22.87 C ANISOU 3266 CA SER B 138 2753 2879 3056 127 157 -312 C ATOM 3267 C SER B 138 29.917 16.808 37.036 1.00 29.40 C ANISOU 3267 C SER B 138 3571 3670 3931 150 173 -308 C ATOM 3268 O SER B 138 30.135 15.663 37.421 1.00 31.15 O ANISOU 3268 O SER B 138 3785 3878 4171 169 158 -275 O ATOM 3269 CB SER B 138 27.526 17.522 36.836 1.00 24.78 C ANISOU 3269 CB SER B 138 3039 3093 3284 113 171 -316 C ATOM 3270 OG SER B 138 26.401 18.137 37.439 1.00 27.40 O ANISOU 3270 OG SER B 138 3372 3454 3585 95 159 -319 O ATOM 3271 N PHE B 139 30.645 17.406 36.072 1.00 26.69 N ANISOU 3271 N PHE B 139 3222 3307 3612 151 208 -338 N ATOM 3272 CA PHE B 139 31.749 16.732 35.380 1.00 27.27 C ANISOU 3272 CA PHE B 139 3281 3348 3734 175 237 -343 C ATOM 3273 C PHE B 139 33.000 16.589 36.265 1.00 27.82 C ANISOU 3273 C PHE B 139 3286 3437 3847 194 214 -333 C ATOM 3274 O PHE B 139 33.703 15.598 36.128 1.00 27.14 O ANISOU 3274 O PHE B 139 3180 3323 3807 223 219 -322 O ATOM 3275 CB PHE B 139 32.050 17.380 34.014 1.00 31.05 C ANISOU 3275 CB PHE B 139 3777 3806 4214 167 293 -372 C ATOM 3276 CG PHE B 139 31.144 16.818 32.942 1.00 35.02 C ANISOU 3276 CG PHE B 139 4341 4283 4681 165 311 -380 C ATOM 3277 CD1 PHE B 139 29.830 17.266 32.812 1.00 38.53 C ANISOU 3277 CD1 PHE B 139 4825 4738 5078 144 292 -376 C ATOM 3278 CD2 PHE B 139 31.572 15.778 32.121 1.00 40.41 C ANISOU 3278 CD2 PHE B 139 5038 4933 5385 186 342 -398 C ATOM 3279 CE1 PHE B 139 28.969 16.706 31.867 1.00 40.51 C ANISOU 3279 CE1 PHE B 139 5125 4969 5297 140 295 -388 C ATOM 3280 CE2 PHE B 139 30.705 15.208 31.176 1.00 44.33 C ANISOU 3280 CE2 PHE B 139 5589 5409 5845 181 349 -419 C ATOM 3281 CZ PHE B 139 29.410 15.684 31.055 1.00 42.20 C ANISOU 3281 CZ PHE B 139 5355 5154 5523 157 321 -412 C ATOM 3282 N ILE B 140 33.240 17.522 37.211 1.00 23.58 N ANISOU 3282 N ILE B 140 2713 2948 3300 181 182 -342 N ATOM 3283 CA ILE B 140 34.334 17.398 38.192 1.00 22.87 C ANISOU 3283 CA ILE B 140 2559 2891 3241 198 141 -334 C ATOM 3284 C ILE B 140 34.018 16.159 39.079 1.00 27.97 C ANISOU 3284 C ILE B 140 3212 3549 3867 222 96 -278 C ATOM 3285 O ILE B 140 34.865 15.275 39.222 1.00 28.75 O ANISOU 3285 O ILE B 140 3276 3631 4016 255 81 -250 O ATOM 3286 CB ILE B 140 34.501 18.678 39.074 1.00 24.58 C ANISOU 3286 CB ILE B 140 2739 3161 3438 174 108 -368 C ATOM 3287 CG1 ILE B 140 35.049 19.860 38.266 1.00 23.91 C ANISOU 3287 CG1 ILE B 140 2632 3051 3401 151 153 -413 C ATOM 3288 CG2 ILE B 140 35.398 18.390 40.278 1.00 24.72 C ANISOU 3288 CG2 ILE B 140 2697 3231 3464 192 45 -357 C ATOM 3289 CD1 ILE B 140 34.941 21.240 38.972 1.00 24.31 C ANISOU 3289 CD1 ILE B 140 2658 3134 3446 119 131 -460 C ATOM 3290 N ALA B 141 32.785 16.117 39.652 1.00 25.03 N ANISOU 3290 N ALA B 141 2880 3201 3428 206 79 -257 N ATOM 3291 CA ALA B 141 32.260 15.037 40.496 1.00 24.13 C ANISOU 3291 CA ALA B 141 2781 3099 3289 219 47 -193 C ATOM 3292 C ALA B 141 32.422 13.696 39.787 1.00 27.29 C ANISOU 3292 C ALA B 141 3193 3424 3753 245 67 -161 C ATOM 3293 O ALA B 141 32.949 12.755 40.374 1.00 27.33 O ANISOU 3293 O ALA B 141 3173 3421 3790 276 38 -107 O ATOM 3294 CB ALA B 141 30.790 15.287 40.813 1.00 23.89 C ANISOU 3294 CB ALA B 141 2794 3091 3193 190 53 -187 C ATOM 3295 N LEU B 142 32.018 13.638 38.514 1.00 23.94 N ANISOU 3295 N LEU B 142 2803 2943 3348 235 116 -198 N ATOM 3296 CA LEU B 142 32.105 12.460 37.667 1.00 25.77 C ANISOU 3296 CA LEU B 142 3051 3100 3640 256 142 -195 C ATOM 3297 C LEU B 142 33.561 12.007 37.497 1.00 29.59 C ANISOU 3297 C LEU B 142 3484 3559 4202 295 148 -198 C ATOM 3298 O LEU B 142 33.855 10.823 37.656 1.00 29.89 O ANISOU 3298 O LEU B 142 3509 3548 4300 327 139 -161 O ATOM 3299 CB LEU B 142 31.451 12.784 36.304 1.00 26.87 C ANISOU 3299 CB LEU B 142 3237 3208 3763 234 188 -251 C ATOM 3300 CG LEU B 142 31.160 11.617 35.357 1.00 31.88 C ANISOU 3300 CG LEU B 142 3903 3771 4441 244 215 -269 C ATOM 3301 CD1 LEU B 142 29.923 10.850 35.807 1.00 32.96 C ANISOU 3301 CD1 LEU B 142 4066 3884 4573 227 190 -232 C ATOM 3302 CD2 LEU B 142 30.937 12.123 33.956 1.00 32.87 C ANISOU 3302 CD2 LEU B 142 4065 3888 4535 229 257 -332 C ATOM 3303 N ASP B 143 34.473 12.963 37.243 1.00 26.00 N ANISOU 3303 N ASP B 143 2993 3132 3755 294 163 -237 N ATOM 3304 CA ASP B 143 35.901 12.717 37.071 1.00 25.56 C ANISOU 3304 CA ASP B 143 2874 3059 3779 328 174 -247 C ATOM 3305 C ASP B 143 36.525 12.153 38.346 1.00 27.54 C ANISOU 3305 C ASP B 143 3071 3334 4059 360 106 -186 C ATOM 3306 O ASP B 143 37.253 11.169 38.277 1.00 27.18 O ANISOU 3306 O ASP B 143 2990 3242 4095 403 105 -164 O ATOM 3307 CB ASP B 143 36.618 14.012 36.638 1.00 27.79 C ANISOU 3307 CB ASP B 143 3123 3371 4063 309 204 -296 C ATOM 3308 CG ASP B 143 38.085 13.793 36.379 1.00 40.99 C ANISOU 3308 CG ASP B 143 4721 5026 5828 341 225 -311 C ATOM 3309 OD1 ASP B 143 38.416 13.235 35.313 1.00 45.67 O ANISOU 3309 OD1 ASP B 143 5321 5567 6466 360 288 -338 O ATOM 3310 OD2 ASP B 143 38.903 14.146 37.260 1.00 41.76 O ANISOU 3310 OD2 ASP B 143 4750 5163 5954 349 177 -300 O ATOM 3311 N ARG B 144 36.249 12.783 39.497 1.00 23.17 N ANISOU 3311 N ARG B 144 2510 2855 3438 342 50 -162 N ATOM 3312 CA ARG B 144 36.747 12.361 40.812 1.00 22.95 C ANISOU 3312 CA ARG B 144 2439 2874 3408 369 -25 -99 C ATOM 3313 C ARG B 144 36.164 11.038 41.251 1.00 27.53 C ANISOU 3313 C ARG B 144 3047 3418 3994 392 -44 -16 C ATOM 3314 O ARG B 144 36.875 10.240 41.839 1.00 28.26 O ANISOU 3314 O ARG B 144 3097 3503 4138 435 -87 45 O ATOM 3315 CB ARG B 144 36.487 13.447 41.887 1.00 23.03 C ANISOU 3315 CB ARG B 144 2443 2983 3324 339 -74 -109 C ATOM 3316 CG ARG B 144 37.144 14.807 41.627 1.00 29.25 C ANISOU 3316 CG ARG B 144 3191 3800 4123 314 -64 -189 C ATOM 3317 CD ARG B 144 38.663 14.755 41.675 1.00 33.05 C ANISOU 3317 CD ARG B 144 3583 4283 4691 343 -90 -199 C ATOM 3318 NE ARG B 144 39.229 14.266 40.419 1.00 31.97 N ANISOU 3318 NE ARG B 144 3432 4064 4650 364 -22 -216 N ATOM 3319 CZ ARG B 144 40.334 13.537 40.316 1.00 40.97 C ANISOU 3319 CZ ARG B 144 4506 5175 5886 408 -30 -198 C ATOM 3320 NH1 ARG B 144 41.029 13.206 41.407 1.00 26.81 N ANISOU 3320 NH1 ARG B 144 2651 3427 4107 439 -115 -153 N ATOM 3321 NH2 ARG B 144 40.763 13.142 39.125 1.00 26.93 N ANISOU 3321 NH2 ARG B 144 2721 3325 4187 425 46 -226 N ATOM 3322 N TRP B 145 34.878 10.797 40.961 1.00 25.49 N ANISOU 3322 N TRP B 145 2857 3133 3697 365 -13 -10 N ATOM 3323 CA TRP B 145 34.180 9.558 41.303 1.00 25.21 C ANISOU 3323 CA TRP B 145 2850 3050 3678 376 -21 67 C ATOM 3324 C TRP B 145 34.792 8.392 40.536 1.00 29.45 C ANISOU 3324 C TRP B 145 3369 3483 4338 416 4 72 C ATOM 3325 O TRP B 145 35.105 7.384 41.149 1.00 29.98 O ANISOU 3325 O TRP B 145 3413 3517 4459 453 -28 153 O ATOM 3326 CB TRP B 145 32.672 9.689 41.046 1.00 23.37 C ANISOU 3326 CB TRP B 145 2681 2810 3388 331 10 55 C ATOM 3327 CG TRP B 145 31.855 8.528 41.507 1.00 24.37 C ANISOU 3327 CG TRP B 145 2833 2894 3533 331 5 138 C ATOM 3328 CD1 TRP B 145 31.463 8.250 42.787 1.00 26.98 C ANISOU 3328 CD1 TRP B 145 3165 3278 3809 330 -31 230 C ATOM 3329 CD2 TRP B 145 31.311 7.488 40.683 1.00 24.42 C ANISOU 3329 CD2 TRP B 145 2865 2795 3618 330 40 135 C ATOM 3330 NE1 TRP B 145 30.725 7.084 42.812 1.00 26.01 N ANISOU 3330 NE1 TRP B 145 3064 3081 3736 326 -15 296 N ATOM 3331 CE2 TRP B 145 30.596 6.610 41.533 1.00 27.49 C ANISOU 3331 CE2 TRP B 145 3266 3167 4012 324 25 233 C ATOM 3332 CE3 TRP B 145 31.354 7.214 39.303 1.00 25.72 C ANISOU 3332 CE3 TRP B 145 3045 2879 3847 330 85 55 C ATOM 3333 CZ2 TRP B 145 29.920 5.487 41.049 1.00 27.08 C ANISOU 3333 CZ2 TRP B 145 3235 3010 4044 316 52 251 C ATOM 3334 CZ3 TRP B 145 30.676 6.103 38.826 1.00 27.13 C ANISOU 3334 CZ3 TRP B 145 3247 2963 4096 324 105 61 C ATOM 3335 CH2 TRP B 145 29.980 5.247 39.693 1.00 27.64 C ANISOU 3335 CH2 TRP B 145 3318 3001 4183 316 88 157 C ATOM 3336 N TYR B 146 35.013 8.535 39.224 1.00 25.63 N ANISOU 3336 N TYR B 146 2893 2948 3898 414 62 -13 N ATOM 3337 CA TYR B 146 35.664 7.484 38.452 1.00 25.57 C ANISOU 3337 CA TYR B 146 2864 2844 4007 454 95 -29 C ATOM 3338 C TYR B 146 37.118 7.310 38.887 1.00 33.91 C ANISOU 3338 C TYR B 146 3839 3907 5139 506 65 -4 C ATOM 3339 O TYR B 146 37.499 6.191 39.180 1.00 34.98 O ANISOU 3339 O TYR B 146 3946 3979 5365 550 46 53 O ATOM 3340 CB TYR B 146 35.576 7.727 36.933 1.00 24.80 C ANISOU 3340 CB TYR B 146 2797 2707 3918 439 169 -133 C ATOM 3341 CG TYR B 146 34.280 7.221 36.344 1.00 24.09 C ANISOU 3341 CG TYR B 146 2775 2568 3808 408 192 -153 C ATOM 3342 CD1 TYR B 146 34.017 5.848 36.249 1.00 24.92 C ANISOU 3342 CD1 TYR B 146 2888 2578 4002 428 195 -132 C ATOM 3343 CD2 TYR B 146 33.299 8.105 35.907 1.00 23.38 C ANISOU 3343 CD2 TYR B 146 2736 2522 3623 360 206 -194 C ATOM 3344 CE1 TYR B 146 32.804 5.377 35.744 1.00 20.94 C ANISOU 3344 CE1 TYR B 146 2438 2027 3490 394 210 -157 C ATOM 3345 CE2 TYR B 146 32.089 7.644 35.390 1.00 23.79 C ANISOU 3345 CE2 TYR B 146 2843 2535 3663 331 217 -214 C ATOM 3346 CZ TYR B 146 31.846 6.280 35.310 1.00 28.65 C ANISOU 3346 CZ TYR B 146 3462 3059 4365 345 219 -200 C ATOM 3347 OH TYR B 146 30.651 5.832 34.794 1.00 28.83 O ANISOU 3347 OH TYR B 146 3530 3040 4384 312 225 -229 O ATOM 3348 N ALA B 147 37.915 8.396 38.991 1.00 30.16 N ANISOU 3348 N ALA B 147 3319 3503 4637 500 56 -40 N ATOM 3349 CA ALA B 147 39.325 8.286 39.387 1.00 29.52 C ANISOU 3349 CA ALA B 147 3148 3432 4637 547 23 -23 C ATOM 3350 C ALA B 147 39.540 7.578 40.740 1.00 33.86 C ANISOU 3350 C ALA B 147 3664 4003 5197 584 -66 88 C ATOM 3351 O ALA B 147 40.417 6.718 40.853 1.00 33.57 O ANISOU 3351 O ALA B 147 3568 3916 5271 641 -86 128 O ATOM 3352 CB ALA B 147 39.982 9.661 39.400 1.00 30.12 C ANISOU 3352 CB ALA B 147 3182 3586 4677 522 20 -79 C ATOM 3353 N ILE B 148 38.707 7.913 41.740 1.00 29.64 N ANISOU 3353 N ILE B 148 3170 3542 4549 554 -116 142 N ATOM 3354 CA ILE B 148 38.828 7.413 43.109 1.00 29.39 C ANISOU 3354 CA ILE B 148 3116 3559 4490 582 -202 254 C ATOM 3355 C ILE B 148 38.026 6.127 43.376 1.00 34.90 C ANISOU 3355 C ILE B 148 3860 4186 5216 596 -200 352 C ATOM 3356 O ILE B 148 38.573 5.199 43.974 1.00 36.48 O ANISOU 3356 O ILE B 148 4020 4357 5482 648 -248 448 O ATOM 3357 CB ILE B 148 38.478 8.558 44.116 1.00 31.86 C ANISOU 3357 CB ILE B 148 3443 4007 4657 542 -253 251 C ATOM 3358 CG1 ILE B 148 39.474 9.746 43.956 1.00 31.38 C ANISOU 3358 CG1 ILE B 148 3318 4003 4600 532 -266 160 C ATOM 3359 CG2 ILE B 148 38.370 8.057 45.586 1.00 31.67 C ANISOU 3359 CG2 ILE B 148 3416 4054 4564 564 -338 373 C ATOM 3360 CD1 ILE B 148 39.012 11.056 44.467 1.00 28.98 C ANISOU 3360 CD1 ILE B 148 3036 3801 4175 480 -283 107 C ATOM 3361 N CYS B 149 36.753 6.064 42.961 1.00 31.43 N ANISOU 3361 N CYS B 149 3494 3714 4733 552 -148 334 N ATOM 3362 CA CYS B 149 35.906 4.906 43.253 1.00 31.05 C ANISOU 3362 CA CYS B 149 3485 3597 4716 554 -144 426 C ATOM 3363 C CYS B 149 35.936 3.796 42.199 1.00 37.04 C ANISOU 3363 C CYS B 149 4246 4207 5622 577 -90 401 C ATOM 3364 O CYS B 149 35.772 2.637 42.578 1.00 37.14 O ANISOU 3364 O CYS B 149 4257 4143 5712 603 -103 495 O ATOM 3365 CB CYS B 149 34.479 5.348 43.550 1.00 30.48 C ANISOU 3365 CB CYS B 149 3479 3574 4527 494 -125 431 C ATOM 3366 SG CYS B 149 34.344 6.463 44.967 1.00 33.99 S ANISOU 3366 SG CYS B 149 3925 4191 4800 471 -184 466 S ATOM 3367 N HIS B 150 36.119 4.122 40.896 1.00 34.73 N ANISOU 3367 N HIS B 150 3957 3872 5367 568 -29 276 N ATOM 3368 CA HIS B 150 36.171 3.109 39.822 1.00 34.62 C ANISOU 3368 CA HIS B 150 3947 3724 5484 589 26 227 C ATOM 3369 C HIS B 150 37.352 3.417 38.896 1.00 41.12 C ANISOU 3369 C HIS B 150 4722 4534 6369 620 64 129 C ATOM 3370 O HIS B 150 37.143 3.804 37.741 1.00 40.71 O ANISOU 3370 O HIS B 150 4701 4470 6297 594 127 20 O ATOM 3371 CB HIS B 150 34.825 3.067 39.095 1.00 34.84 C ANISOU 3371 CB HIS B 150 4048 3716 5474 533 73 170 C ATOM 3372 CG HIS B 150 33.698 2.781 40.031 1.00 38.22 C ANISOU 3372 CG HIS B 150 4512 4160 5850 500 44 267 C ATOM 3373 ND1 HIS B 150 33.437 1.499 40.473 1.00 39.58 N ANISOU 3373 ND1 HIS B 150 4681 4238 6119 518 33 361 N ATOM 3374 CD2 HIS B 150 32.858 3.635 40.656 1.00 40.25 C ANISOU 3374 CD2 HIS B 150 4801 4517 5974 453 28 289 C ATOM 3375 CE1 HIS B 150 32.422 1.604 41.309 1.00 38.72 C ANISOU 3375 CE1 HIS B 150 4605 4179 5929 478 17 438 C ATOM 3376 NE2 HIS B 150 32.034 2.868 41.448 1.00 39.51 N ANISOU 3376 NE2 HIS B 150 4727 4398 5888 440 14 393 N ATOM 3377 N PRO B 151 38.605 3.285 39.413 1.00 41.71 N ANISOU 3377 N PRO B 151 4717 4620 6511 675 25 171 N ATOM 3378 CA PRO B 151 39.784 3.788 38.688 1.00 43.25 C ANISOU 3378 CA PRO B 151 4853 4826 6756 699 61 83 C ATOM 3379 C PRO B 151 40.193 3.253 37.309 1.00 52.49 C ANISOU 3379 C PRO B 151 6014 5899 8031 722 149 -20 C ATOM 3380 O PRO B 151 40.966 3.965 36.652 1.00 55.17 O ANISOU 3380 O PRO B 151 6319 6273 8371 723 194 -99 O ATOM 3381 CB PRO B 151 40.937 3.522 39.669 1.00 44.33 C ANISOU 3381 CB PRO B 151 4897 4984 6961 758 -13 167 C ATOM 3382 CG PRO B 151 40.424 2.551 40.627 1.00 47.61 C ANISOU 3382 CG PRO B 151 5329 5362 7399 779 -71 295 C ATOM 3383 CD PRO B 151 38.993 2.907 40.784 1.00 43.04 C ANISOU 3383 CD PRO B 151 4842 4819 6691 712 -62 304 C ATOM 3384 N LEU B 152 39.778 2.080 36.857 1.00 50.06 N ANISOU 3384 N LEU B 152 5731 5476 7814 741 179 -27 N ATOM 3385 CA LEU B 152 40.370 1.675 35.568 1.00 51.81 C ANISOU 3385 CA LEU B 152 5935 5621 8131 768 265 -142 C ATOM 3386 C LEU B 152 39.391 1.613 34.379 1.00 56.69 C ANISOU 3386 C LEU B 152 6638 6206 8696 722 334 -248 C ATOM 3387 O LEU B 152 39.673 0.937 33.384 1.00 55.85 O ANISOU 3387 O LEU B 152 6528 6016 8675 747 401 -340 O ATOM 3388 CB LEU B 152 41.135 0.338 35.719 1.00 52.60 C ANISOU 3388 CB LEU B 152 5968 5597 8419 845 260 -106 C ATOM 3389 CG LEU B 152 42.274 0.326 36.769 1.00 57.89 C ANISOU 3389 CG LEU B 152 6540 6296 9159 903 186 -3 C ATOM 3390 CD1 LEU B 152 42.545 -1.079 37.278 1.00 58.31 C ANISOU 3390 CD1 LEU B 152 6553 6225 9377 968 150 87 C ATOM 3391 CD2 LEU B 152 43.538 1.056 36.268 1.00 58.61 C ANISOU 3391 CD2 LEU B 152 6550 6435 9283 928 224 -77 C ATOM 3392 N LEU B 153 38.297 2.386 34.441 1.00 53.26 N ANISOU 3392 N LEU B 153 6274 5843 8118 657 318 -245 N ATOM 3393 CA LEU B 153 37.289 2.394 33.383 1.00 52.20 C ANISOU 3393 CA LEU B 153 6219 5691 7923 611 366 -337 C ATOM 3394 C LEU B 153 37.503 3.469 32.319 1.00 52.92 C ANISOU 3394 C LEU B 153 6334 5857 7917 585 427 -435 C ATOM 3395 O LEU B 153 37.611 3.135 31.134 1.00 53.19 O ANISOU 3395 O LEU B 153 6389 5853 7968 591 495 -540 O ATOM 3396 CB LEU B 153 35.872 2.485 33.977 1.00 52.15 C ANISOU 3396 CB LEU B 153 6273 5706 7836 558 317 -277 C ATOM 3397 CG LEU B 153 35.446 1.293 34.807 1.00 56.71 C ANISOU 3397 CG LEU B 153 6842 6193 8511 573 276 -187 C ATOM 3398 CD1 LEU B 153 34.245 1.624 35.627 1.00 56.65 C ANISOU 3398 CD1 LEU B 153 6875 6237 8411 522 229 -106 C ATOM 3399 CD2 LEU B 153 35.202 0.061 33.930 1.00 60.08 C ANISOU 3399 CD2 LEU B 153 7286 6487 9054 583 319 -264 C ATOM 3400 N PHE B 154 37.537 4.742 32.727 1.00 45.88 N ANISOU 3400 N PHE B 154 5440 5071 6921 556 405 -403 N ATOM 3401 CA PHE B 154 37.691 5.862 31.802 1.00 44.25 C ANISOU 3401 CA PHE B 154 5255 4934 6623 527 460 -474 C ATOM 3402 C PHE B 154 39.004 6.588 32.026 1.00 51.29 C ANISOU 3402 C PHE B 154 6070 5874 7543 549 475 -464 C ATOM 3403 O PHE B 154 39.499 6.598 33.154 1.00 51.14 O ANISOU 3403 O PHE B 154 5993 5872 7566 569 413 -389 O ATOM 3404 CB PHE B 154 36.471 6.817 31.884 1.00 44.04 C ANISOU 3404 CB PHE B 154 5297 4977 6460 466 431 -460 C ATOM 3405 CG PHE B 154 35.163 6.136 31.542 1.00 43.98 C ANISOU 3405 CG PHE B 154 5357 4924 6430 440 420 -480 C ATOM 3406 CD1 PHE B 154 34.763 5.983 30.220 1.00 45.82 C ANISOU 3406 CD1 PHE B 154 5641 5141 6626 425 471 -575 C ATOM 3407 CD2 PHE B 154 34.356 5.598 32.541 1.00 44.05 C ANISOU 3407 CD2 PHE B 154 5373 4907 6457 429 359 -405 C ATOM 3408 CE1 PHE B 154 33.570 5.319 29.905 1.00 46.12 C ANISOU 3408 CE1 PHE B 154 5734 5137 6654 399 452 -604 C ATOM 3409 CE2 PHE B 154 33.179 4.910 32.221 1.00 45.57 C ANISOU 3409 CE2 PHE B 154 5616 5049 6650 401 351 -427 C ATOM 3410 CZ PHE B 154 32.791 4.779 30.908 1.00 43.63 C ANISOU 3410 CZ PHE B 154 5416 4785 6376 386 393 -530 C ATOM 3411 N LYS B 155 39.588 7.159 30.945 1.00 50.35 N ANISOU 3411 N LYS B 155 5947 5779 7404 546 557 -539 N ATOM 3412 CA LYS B 155 40.850 7.914 31.006 1.00 50.43 C ANISOU 3412 CA LYS B 155 5878 5832 7451 559 584 -538 C ATOM 3413 C LYS B 155 40.560 9.375 31.362 1.00 53.32 C ANISOU 3413 C LYS B 155 6258 6285 7715 507 559 -508 C ATOM 3414 O LYS B 155 39.800 10.032 30.658 1.00 53.08 O ANISOU 3414 O LYS B 155 6299 6285 7584 466 589 -536 O ATOM 3415 CB LYS B 155 41.613 7.832 29.671 1.00 53.06 C ANISOU 3415 CB LYS B 155 6196 6150 7816 579 698 -627 C ATOM 3416 CG LYS B 155 42.614 6.682 29.586 1.00 77.10 C ANISOU 3416 CG LYS B 155 9165 9117 11014 646 726 -653 C ATOM 3417 CD LYS B 155 43.265 6.586 28.187 1.00 92.75 C ANISOU 3417 CD LYS B 155 11139 11086 13018 665 853 -756 C ATOM 3418 CE LYS B 155 44.479 7.471 27.973 1.00105.38 C ANISOU 3418 CE LYS B 155 12661 12739 14640 664 918 -765 C ATOM 3419 NZ LYS B 155 45.032 7.328 26.596 1.00111.09 N ANISOU 3419 NZ LYS B 155 13388 13459 15362 679 1054 -863 N ATOM 3420 N SER B 156 41.161 9.873 32.453 1.00 49.26 N ANISOU 3420 N SER B 156 5676 5809 7234 511 499 -455 N ATOM 3421 CA SER B 156 41.011 11.254 32.919 1.00 48.76 C ANISOU 3421 CA SER B 156 5610 5818 7097 465 469 -435 C ATOM 3422 C SER B 156 42.200 12.099 32.424 1.00 50.15 C ANISOU 3422 C SER B 156 5716 6018 7320 460 532 -469 C ATOM 3423 O SER B 156 43.253 12.102 33.066 1.00 51.12 O ANISOU 3423 O SER B 156 5743 6149 7532 485 503 -454 O ATOM 3424 CB SER B 156 40.908 11.277 34.450 1.00 53.15 C ANISOU 3424 CB SER B 156 6134 6407 7653 468 362 -366 C ATOM 3425 OG SER B 156 41.010 12.575 35.015 1.00 61.89 O ANISOU 3425 OG SER B 156 7218 7581 8714 430 330 -362 O ATOM 3426 N THR B 157 42.050 12.792 31.281 1.00 43.99 N ANISOU 3426 N THR B 157 4979 5251 6485 429 617 -510 N ATOM 3427 CA THR B 157 43.130 13.652 30.752 1.00 43.74 C ANISOU 3427 CA THR B 157 4882 5239 6497 417 690 -533 C ATOM 3428 C THR B 157 42.684 15.101 30.617 1.00 46.73 C ANISOU 3428 C THR B 157 5294 5660 6799 359 699 -522 C ATOM 3429 O THR B 157 41.492 15.370 30.541 1.00 45.70 O ANISOU 3429 O THR B 157 5251 5542 6570 332 674 -510 O ATOM 3430 CB THR B 157 43.761 13.116 29.440 1.00 51.60 C ANISOU 3430 CB THR B 157 5874 6206 7526 443 809 -589 C ATOM 3431 OG1 THR B 157 42.852 13.286 28.354 1.00 53.30 O ANISOU 3431 OG1 THR B 157 6196 6431 7625 418 863 -614 O ATOM 3432 CG2 THR B 157 44.238 11.657 29.547 1.00 47.48 C ANISOU 3432 CG2 THR B 157 5310 5627 7105 506 806 -609 C ATOM 3433 N ALA B 158 43.640 16.033 30.614 1.00 43.76 N ANISOU 3433 N ALA B 158 4841 5302 6483 339 732 -525 N ATOM 3434 CA ALA B 158 43.401 17.465 30.470 1.00 44.31 C ANISOU 3434 CA ALA B 158 4926 5398 6512 283 749 -513 C ATOM 3435 C ALA B 158 42.782 17.793 29.100 1.00 51.56 C ANISOU 3435 C ALA B 158 5935 6317 7338 262 839 -516 C ATOM 3436 O ALA B 158 41.944 18.696 29.008 1.00 52.22 O ANISOU 3436 O ALA B 158 6076 6414 7350 224 825 -493 O ATOM 3437 CB ALA B 158 44.699 18.229 30.657 1.00 44.65 C ANISOU 3437 CB ALA B 158 4855 5446 6665 268 777 -520 C ATOM 3438 N ARG B 159 43.185 17.057 28.048 1.00 48.77 N ANISOU 3438 N ARG B 159 5594 5952 6985 290 929 -546 N ATOM 3439 CA ARG B 159 42.680 17.229 26.690 1.00 49.38 C ANISOU 3439 CA ARG B 159 5759 6043 6961 276 1015 -554 C ATOM 3440 C ARG B 159 41.253 16.724 26.541 1.00 53.62 C ANISOU 3440 C ARG B 159 6405 6582 7387 277 959 -556 C ATOM 3441 O ARG B 159 40.483 17.293 25.765 1.00 55.71 O ANISOU 3441 O ARG B 159 6749 6870 7549 251 983 -541 O ATOM 3442 CB ARG B 159 43.622 16.594 25.642 1.00 52.68 C ANISOU 3442 CB ARG B 159 6151 6457 7409 305 1134 -598 C ATOM 3443 CG ARG B 159 44.977 17.304 25.463 1.00 70.18 C ANISOU 3443 CG ARG B 159 8264 8678 9725 292 1219 -592 C ATOM 3444 CD ARG B 159 44.925 18.695 24.807 1.00 91.51 C ANISOU 3444 CD ARG B 159 10990 11404 12375 239 1288 -547 C ATOM 3445 NE ARG B 159 46.261 19.280 24.635 1.00107.70 N ANISOU 3445 NE ARG B 159 12931 13452 14540 225 1376 -542 N ATOM 3446 CZ ARG B 159 46.572 20.557 24.864 1.00121.16 C ANISOU 3446 CZ ARG B 159 14593 15153 16290 175 1388 -498 C ATOM 3447 NH1 ARG B 159 45.648 21.408 25.296 1.00104.76 N ANISOU 3447 NH1 ARG B 159 12574 13074 14155 139 1318 -456 N ATOM 3448 NH2 ARG B 159 47.813 20.988 24.669 1.00107.53 N ANISOU 3448 NH2 ARG B 159 12758 13419 14681 160 1473 -497 N ATOM 3449 N ARG B 160 40.887 15.684 27.299 1.00 47.34 N ANISOU 3449 N ARG B 160 5610 5761 6617 306 883 -568 N ATOM 3450 CA ARG B 160 39.531 15.153 27.307 1.00 46.07 C ANISOU 3450 CA ARG B 160 5537 5595 6372 304 824 -570 C ATOM 3451 C ARG B 160 38.630 16.096 28.106 1.00 46.43 C ANISOU 3451 C ARG B 160 5606 5662 6374 267 746 -522 C ATOM 3452 O ARG B 160 37.438 16.192 27.810 1.00 47.20 O ANISOU 3452 O ARG B 160 5780 5769 6384 250 718 -516 O ATOM 3453 CB ARG B 160 39.499 13.724 27.881 1.00 48.85 C ANISOU 3453 CB ARG B 160 5875 5903 6785 344 776 -589 C ATOM 3454 CG ARG B 160 39.877 12.672 26.835 1.00 65.68 C ANISOU 3454 CG ARG B 160 8019 8004 8932 378 852 -654 C ATOM 3455 CD ARG B 160 40.039 11.276 27.409 1.00 82.79 C ANISOU 3455 CD ARG B 160 10162 10109 11185 421 810 -670 C ATOM 3456 NE ARG B 160 40.453 10.300 26.387 1.00 97.70 N ANISOU 3456 NE ARG B 160 12045 11961 13113 458 894 -746 N ATOM 3457 CZ ARG B 160 39.657 9.721 25.493 1.00115.10 C ANISOU 3457 CZ ARG B 160 14326 14157 15250 457 931 -812 C ATOM 3458 NH1 ARG B 160 38.367 10.038 25.434 1.00 98.11 N ANISOU 3458 NH1 ARG B 160 12260 12032 12983 419 888 -805 N ATOM 3459 NH2 ARG B 160 40.150 8.844 24.628 1.00106.12 N ANISOU 3459 NH2 ARG B 160 13176 12988 14158 494 1010 -893 N ATOM 3460 N ALA B 161 39.205 16.797 29.117 1.00 38.95 N ANISOU 3460 N ALA B 161 4585 4722 5491 257 708 -496 N ATOM 3461 CA ALA B 161 38.503 17.778 29.953 1.00 36.74 C ANISOU 3461 CA ALA B 161 4313 4462 5182 224 641 -465 C ATOM 3462 C ALA B 161 38.118 18.981 29.089 1.00 39.19 C ANISOU 3462 C ALA B 161 4667 4785 5438 188 690 -450 C ATOM 3463 O ALA B 161 36.999 19.468 29.224 1.00 39.15 O ANISOU 3463 O ALA B 161 4715 4789 5371 168 648 -431 O ATOM 3464 CB ALA B 161 39.360 18.205 31.133 1.00 36.72 C ANISOU 3464 CB ALA B 161 4219 4469 5263 221 596 -458 C ATOM 3465 N LEU B 162 38.988 19.379 28.127 1.00 34.32 N ANISOU 3465 N LEU B 162 4031 4169 4841 183 784 -453 N ATOM 3466 CA LEU B 162 38.710 20.468 27.187 1.00 33.65 C ANISOU 3466 CA LEU B 162 3989 4094 4704 152 841 -422 C ATOM 3467 C LEU B 162 37.562 20.115 26.228 1.00 37.31 C ANISOU 3467 C LEU B 162 4558 4574 5046 156 845 -419 C ATOM 3468 O LEU B 162 36.776 20.988 25.878 1.00 37.63 O ANISOU 3468 O LEU B 162 4646 4622 5028 133 836 -381 O ATOM 3469 CB LEU B 162 39.975 20.926 26.439 1.00 33.83 C ANISOU 3469 CB LEU B 162 3959 4115 4779 144 949 -418 C ATOM 3470 CG LEU B 162 41.081 21.584 27.305 1.00 38.86 C ANISOU 3470 CG LEU B 162 4484 4736 5546 127 944 -419 C ATOM 3471 CD1 LEU B 162 42.346 21.775 26.516 1.00 39.46 C ANISOU 3471 CD1 LEU B 162 4500 4808 5683 123 1059 -419 C ATOM 3472 CD2 LEU B 162 40.627 22.932 27.913 1.00 40.53 C ANISOU 3472 CD2 LEU B 162 4688 4936 5777 86 896 -390 C ATOM 3473 N GLY B 163 37.452 18.837 25.862 1.00 32.60 N ANISOU 3473 N GLY B 163 3989 3977 4420 186 849 -461 N ATOM 3474 CA GLY B 163 36.366 18.322 25.040 1.00 31.63 C ANISOU 3474 CA GLY B 163 3958 3870 4190 191 837 -477 C ATOM 3475 C GLY B 163 35.058 18.321 25.819 1.00 35.37 C ANISOU 3475 C GLY B 163 4463 4337 4638 181 735 -461 C ATOM 3476 O GLY B 163 34.012 18.671 25.270 1.00 34.72 O ANISOU 3476 O GLY B 163 4445 4274 4472 167 713 -445 O ATOM 3477 N SER B 164 35.113 17.947 27.121 1.00 30.55 N ANISOU 3477 N SER B 164 3803 3706 4099 188 673 -462 N ATOM 3478 CA SER B 164 33.963 17.962 28.013 1.00 29.79 C ANISOU 3478 CA SER B 164 3724 3609 3987 177 586 -446 C ATOM 3479 C SER B 164 33.485 19.416 28.192 1.00 31.74 C ANISOU 3479 C SER B 164 3974 3869 4215 148 571 -407 C ATOM 3480 O SER B 164 32.289 19.655 28.119 1.00 30.68 O ANISOU 3480 O SER B 164 3885 3742 4029 137 529 -394 O ATOM 3481 CB SER B 164 34.312 17.364 29.372 1.00 32.75 C ANISOU 3481 CB SER B 164 4041 3969 4434 191 535 -445 C ATOM 3482 OG SER B 164 34.927 16.099 29.234 1.00 42.19 O ANISOU 3482 OG SER B 164 5221 5139 5671 223 554 -473 O ATOM 3483 N ILE B 165 34.425 20.373 28.385 1.00 27.62 N ANISOU 3483 N ILE B 165 3400 3345 3749 135 606 -392 N ATOM 3484 CA ILE B 165 34.167 21.815 28.556 1.00 26.95 C ANISOU 3484 CA ILE B 165 3308 3258 3676 107 601 -361 C ATOM 3485 C ILE B 165 33.423 22.393 27.329 1.00 33.05 C ANISOU 3485 C ILE B 165 4149 4036 4371 98 629 -326 C ATOM 3486 O ILE B 165 32.455 23.130 27.512 1.00 32.09 O ANISOU 3486 O ILE B 165 4050 3911 4232 86 588 -302 O ATOM 3487 CB ILE B 165 35.472 22.591 28.933 1.00 28.34 C ANISOU 3487 CB ILE B 165 3404 3420 3944 93 639 -361 C ATOM 3488 CG1 ILE B 165 35.853 22.349 30.411 1.00 27.78 C ANISOU 3488 CG1 ILE B 165 3266 3353 3936 97 575 -389 C ATOM 3489 CG2 ILE B 165 35.366 24.085 28.628 1.00 26.61 C ANISOU 3489 CG2 ILE B 165 3184 3183 3745 62 665 -325 C ATOM 3490 CD1 ILE B 165 37.296 22.515 30.713 1.00 29.97 C ANISOU 3490 CD1 ILE B 165 3456 3624 4305 94 603 -405 C ATOM 3491 N LEU B 166 33.844 22.019 26.095 1.00 30.70 N ANISOU 3491 N LEU B 166 3887 3755 4025 107 697 -325 N ATOM 3492 CA LEU B 166 33.185 22.447 24.852 1.00 30.86 C ANISOU 3492 CA LEU B 166 3979 3796 3951 102 721 -288 C ATOM 3493 C LEU B 166 31.767 21.881 24.760 1.00 31.97 C ANISOU 3493 C LEU B 166 4178 3952 4018 111 646 -301 C ATOM 3494 O LEU B 166 30.862 22.593 24.326 1.00 31.84 O ANISOU 3494 O LEU B 166 4201 3945 3953 103 619 -259 O ATOM 3495 CB LEU B 166 33.998 22.060 23.608 1.00 31.77 C ANISOU 3495 CB LEU B 166 4118 3937 4015 112 814 -294 C ATOM 3496 CG LEU B 166 35.071 23.061 23.200 1.00 38.58 C ANISOU 3496 CG LEU B 166 4942 4792 4922 94 904 -249 C ATOM 3497 CD1 LEU B 166 36.090 22.422 22.288 1.00 39.69 C ANISOU 3497 CD1 LEU B 166 5081 4958 5040 108 1003 -276 C ATOM 3498 CD2 LEU B 166 34.466 24.279 22.520 1.00 43.22 C ANISOU 3498 CD2 LEU B 166 5575 5385 5460 76 915 -168 C ATOM 3499 N GLY B 167 31.596 20.627 25.187 1.00 26.33 N ANISOU 3499 N GLY B 167 3461 3235 3309 125 612 -354 N ATOM 3500 CA GLY B 167 30.310 19.942 25.244 1.00 25.90 C ANISOU 3500 CA GLY B 167 3447 3186 3209 129 541 -374 C ATOM 3501 C GLY B 167 29.354 20.625 26.207 1.00 28.95 C ANISOU 3501 C GLY B 167 3815 3561 3624 116 473 -347 C ATOM 3502 O GLY B 167 28.185 20.821 25.867 1.00 29.56 O ANISOU 3502 O GLY B 167 3929 3650 3654 111 428 -333 O ATOM 3503 N ILE B 168 29.861 21.026 27.407 1.00 25.24 N ANISOU 3503 N ILE B 168 3285 3072 3233 110 466 -343 N ATOM 3504 CA ILE B 168 29.103 21.757 28.451 1.00 25.22 C ANISOU 3504 CA ILE B 168 3258 3063 3263 98 414 -328 C ATOM 3505 C ILE B 168 28.561 23.087 27.874 1.00 27.87 C ANISOU 3505 C ILE B 168 3612 3393 3583 88 417 -285 C ATOM 3506 O ILE B 168 27.385 23.374 28.068 1.00 27.09 O ANISOU 3506 O ILE B 168 3525 3294 3473 86 369 -276 O ATOM 3507 CB ILE B 168 29.923 21.958 29.765 1.00 27.82 C ANISOU 3507 CB ILE B 168 3520 3384 3667 94 409 -343 C ATOM 3508 CG1 ILE B 168 30.105 20.633 30.515 1.00 26.44 C ANISOU 3508 CG1 ILE B 168 3328 3214 3504 109 383 -368 C ATOM 3509 CG2 ILE B 168 29.300 23.035 30.688 1.00 29.37 C ANISOU 3509 CG2 ILE B 168 3690 3575 3893 80 373 -337 C ATOM 3510 CD1 ILE B 168 31.349 20.594 31.421 1.00 27.83 C ANISOU 3510 CD1 ILE B 168 3440 3391 3743 114 389 -379 C ATOM 3511 N TRP B 169 29.395 23.846 27.120 1.00 24.12 N ANISOU 3511 N TRP B 169 3138 2911 3115 83 478 -254 N ATOM 3512 CA TRP B 169 28.970 25.088 26.469 1.00 24.17 C ANISOU 3512 CA TRP B 169 3165 2905 3114 76 487 -196 C ATOM 3513 C TRP B 169 27.947 24.821 25.358 1.00 29.19 C ANISOU 3513 C TRP B 169 3868 3570 3651 87 461 -171 C ATOM 3514 O TRP B 169 26.914 25.472 25.343 1.00 28.39 O ANISOU 3514 O TRP B 169 3778 3461 3549 89 416 -139 O ATOM 3515 CB TRP B 169 30.162 25.915 25.974 1.00 22.81 C ANISOU 3515 CB TRP B 169 2972 2714 2980 63 565 -160 C ATOM 3516 CG TRP B 169 30.831 26.677 27.076 1.00 23.59 C ANISOU 3516 CG TRP B 169 2998 2774 3191 45 570 -178 C ATOM 3517 CD1 TRP B 169 31.916 26.283 27.805 1.00 26.17 C ANISOU 3517 CD1 TRP B 169 3268 3100 3575 41 587 -222 C ATOM 3518 CD2 TRP B 169 30.402 27.930 27.636 1.00 23.46 C ANISOU 3518 CD2 TRP B 169 2954 2715 3245 32 548 -161 C ATOM 3519 NE1 TRP B 169 32.189 27.211 28.785 1.00 25.76 N ANISOU 3519 NE1 TRP B 169 3156 3015 3616 22 573 -239 N ATOM 3520 CE2 TRP B 169 31.276 28.233 28.704 1.00 27.04 C ANISOU 3520 CE2 TRP B 169 3335 3147 3790 15 553 -207 C ATOM 3521 CE3 TRP B 169 29.321 28.795 27.379 1.00 24.76 C ANISOU 3521 CE3 TRP B 169 3142 2855 3409 35 520 -117 C ATOM 3522 CZ2 TRP B 169 31.150 29.399 29.469 1.00 26.46 C ANISOU 3522 CZ2 TRP B 169 3219 3030 3807 -2 536 -220 C ATOM 3523 CZ3 TRP B 169 29.199 29.951 28.136 1.00 26.35 C ANISOU 3523 CZ3 TRP B 169 3298 3004 3711 22 509 -123 C ATOM 3524 CH2 TRP B 169 30.111 30.250 29.161 1.00 26.93 C ANISOU 3524 CH2 TRP B 169 3304 3056 3872 2 519 -179 C ATOM 3525 N ALA B 170 28.194 23.821 24.481 1.00 26.43 N ANISOU 3525 N ALA B 170 3562 3257 3225 96 483 -194 N ATOM 3526 CA ALA B 170 27.272 23.418 23.409 1.00 25.55 C ANISOU 3526 CA ALA B 170 3515 3184 3009 106 450 -187 C ATOM 3527 C ALA B 170 25.884 23.049 23.974 1.00 28.80 C ANISOU 3527 C ALA B 170 3923 3593 3426 107 360 -210 C ATOM 3528 O ALA B 170 24.879 23.500 23.430 1.00 29.16 O ANISOU 3528 O ALA B 170 3996 3653 3429 111 313 -176 O ATOM 3529 CB ALA B 170 27.846 22.251 22.618 1.00 26.05 C ANISOU 3529 CB ALA B 170 3613 3281 3003 114 489 -238 C ATOM 3530 N VAL B 171 25.830 22.255 25.060 1.00 23.09 N ANISOU 3530 N VAL B 171 3163 2852 2759 104 337 -261 N ATOM 3531 CA VAL B 171 24.573 21.850 25.708 1.00 21.65 C ANISOU 3531 CA VAL B 171 2968 2665 2592 101 266 -281 C ATOM 3532 C VAL B 171 23.874 23.065 26.359 1.00 27.50 C ANISOU 3532 C VAL B 171 3676 3386 3384 98 237 -243 C ATOM 3533 O VAL B 171 22.690 23.305 26.108 1.00 28.72 O ANISOU 3533 O VAL B 171 3839 3548 3524 101 184 -228 O ATOM 3534 CB VAL B 171 24.794 20.661 26.715 1.00 23.62 C ANISOU 3534 CB VAL B 171 3188 2900 2887 98 260 -332 C ATOM 3535 CG1 VAL B 171 23.549 20.382 27.553 1.00 21.84 C ANISOU 3535 CG1 VAL B 171 2940 2668 2691 90 200 -340 C ATOM 3536 CG2 VAL B 171 25.242 19.394 25.986 1.00 23.06 C ANISOU 3536 CG2 VAL B 171 3149 2835 2776 104 279 -377 C ATOM 3537 N SER B 172 24.614 23.825 27.186 1.00 24.04 N ANISOU 3537 N SER B 172 3197 2923 3014 93 270 -235 N ATOM 3538 CA SER B 172 24.102 24.995 27.911 1.00 24.08 C ANISOU 3538 CA SER B 172 3165 2902 3083 91 252 -216 C ATOM 3539 C SER B 172 23.528 26.063 26.990 1.00 28.23 C ANISOU 3539 C SER B 172 3713 3416 3597 99 242 -156 C ATOM 3540 O SER B 172 22.461 26.597 27.272 1.00 27.93 O ANISOU 3540 O SER B 172 3658 3366 3590 106 199 -145 O ATOM 3541 CB SER B 172 25.192 25.588 28.797 1.00 25.91 C ANISOU 3541 CB SER B 172 3351 3110 3385 81 292 -231 C ATOM 3542 OG SER B 172 25.662 24.606 29.708 1.00 31.41 O ANISOU 3542 OG SER B 172 4024 3822 4087 78 290 -277 O ATOM 3543 N LEU B 173 24.220 26.352 25.874 1.00 24.54 N ANISOU 3543 N LEU B 173 3282 2955 3086 101 283 -111 N ATOM 3544 CA LEU B 173 23.793 27.346 24.897 1.00 23.97 C ANISOU 3544 CA LEU B 173 3238 2875 2993 112 278 -34 C ATOM 3545 C LEU B 173 22.516 26.928 24.171 1.00 29.49 C ANISOU 3545 C LEU B 173 3974 3612 3618 127 207 -21 C ATOM 3546 O LEU B 173 21.699 27.785 23.850 1.00 30.33 O ANISOU 3546 O LEU B 173 4079 3705 3740 141 169 35 O ATOM 3547 CB LEU B 173 24.923 27.687 23.903 1.00 23.64 C ANISOU 3547 CB LEU B 173 3230 2841 2913 107 350 17 C ATOM 3548 CG LEU B 173 26.084 28.564 24.423 1.00 27.09 C ANISOU 3548 CG LEU B 173 3621 3227 3446 90 418 31 C ATOM 3549 CD1 LEU B 173 27.356 28.400 23.521 1.00 26.85 C ANISOU 3549 CD1 LEU B 173 3615 3217 3369 82 503 57 C ATOM 3550 CD2 LEU B 173 25.681 30.048 24.548 1.00 23.60 C ANISOU 3550 CD2 LEU B 173 3154 2723 3091 91 412 93 C ATOM 3551 N ALA B 174 22.309 25.621 23.961 1.00 25.66 N ANISOU 3551 N ALA B 174 3513 3170 3068 124 183 -76 N ATOM 3552 CA ALA B 174 21.126 25.111 23.279 1.00 24.58 C ANISOU 3552 CA ALA B 174 3404 3071 2864 133 110 -81 C ATOM 3553 C ALA B 174 19.911 24.972 24.182 1.00 27.02 C ANISOU 3553 C ALA B 174 3664 3363 3239 132 46 -110 C ATOM 3554 O ALA B 174 18.827 25.397 23.798 1.00 26.01 O ANISOU 3554 O ALA B 174 3532 3243 3107 145 -15 -79 O ATOM 3555 CB ALA B 174 21.443 23.779 22.623 1.00 25.10 C ANISOU 3555 CB ALA B 174 3513 3181 2841 127 115 -138 C ATOM 3556 N ILE B 175 20.071 24.369 25.375 1.00 23.85 N ANISOU 3556 N ILE B 175 3223 2943 2896 118 62 -167 N ATOM 3557 CA ILE B 175 18.945 24.088 26.281 1.00 23.30 C ANISOU 3557 CA ILE B 175 3107 2865 2881 114 15 -198 C ATOM 3558 C ILE B 175 18.328 25.360 26.877 1.00 27.70 C ANISOU 3558 C ILE B 175 3618 3390 3517 125 5 -166 C ATOM 3559 O ILE B 175 17.214 25.293 27.410 1.00 27.20 O ANISOU 3559 O ILE B 175 3514 3324 3496 126 -35 -183 O ATOM 3560 CB ILE B 175 19.303 23.024 27.375 1.00 26.08 C ANISOU 3560 CB ILE B 175 3436 3212 3263 96 38 -254 C ATOM 3561 CG1 ILE B 175 20.261 23.595 28.453 1.00 26.53 C ANISOU 3561 CG1 ILE B 175 3461 3246 3373 94 91 -257 C ATOM 3562 CG2 ILE B 175 19.846 21.716 26.731 1.00 24.81 C ANISOU 3562 CG2 ILE B 175 3316 3069 3043 89 47 -290 C ATOM 3563 CD1 ILE B 175 20.496 22.701 29.634 1.00 30.47 C ANISOU 3563 CD1 ILE B 175 3932 3747 3897 81 103 -297 C ATOM 3564 N MET B 176 19.019 26.525 26.753 1.00 24.58 N ANISOU 3564 N MET B 176 3224 2965 3150 134 43 -123 N ATOM 3565 CA MET B 176 18.515 27.801 27.288 1.00 22.79 C ANISOU 3565 CA MET B 176 2952 2693 3013 147 38 -100 C ATOM 3566 C MET B 176 17.861 28.668 26.213 1.00 26.71 C ANISOU 3566 C MET B 176 3465 3180 3505 172 -2 -22 C ATOM 3567 O MET B 176 17.342 29.748 26.530 1.00 25.68 O ANISOU 3567 O MET B 176 3294 3002 3461 189 -11 3 O ATOM 3568 CB MET B 176 19.591 28.552 28.084 1.00 24.00 C ANISOU 3568 CB MET B 176 3081 2807 3232 138 100 -113 C ATOM 3569 CG MET B 176 19.996 27.826 29.364 1.00 26.37 C ANISOU 3569 CG MET B 176 3351 3122 3545 119 122 -186 C ATOM 3570 SD MET B 176 18.614 27.283 30.417 1.00 28.97 S ANISOU 3570 SD MET B 176 3636 3471 3899 119 83 -236 S ATOM 3571 CE MET B 176 19.539 26.424 31.703 1.00 24.54 C ANISOU 3571 CE MET B 176 3062 2937 3326 98 119 -293 C ATOM 3572 N VAL B 177 17.829 28.167 24.950 1.00 23.23 N ANISOU 3572 N VAL B 177 3080 2784 2962 176 -29 13 N ATOM 3573 CA VAL B 177 17.140 28.856 23.850 1.00 23.32 C ANISOU 3573 CA VAL B 177 3112 2802 2944 202 -81 95 C ATOM 3574 C VAL B 177 15.612 28.988 24.200 1.00 29.61 C ANISOU 3574 C VAL B 177 3854 3592 3804 220 -158 86 C ATOM 3575 O VAL B 177 15.089 30.091 24.034 1.00 31.31 O ANISOU 3575 O VAL B 177 4045 3768 4083 248 -182 149 O ATOM 3576 CB VAL B 177 17.440 28.259 22.449 1.00 26.19 C ANISOU 3576 CB VAL B 177 3552 3233 3165 203 -96 125 C ATOM 3577 CG1 VAL B 177 16.623 28.954 21.374 1.00 25.83 C ANISOU 3577 CG1 VAL B 177 3528 3208 3081 233 -163 216 C ATOM 3578 CG2 VAL B 177 18.920 28.382 22.125 1.00 26.02 C ANISOU 3578 CG2 VAL B 177 3572 3211 3105 190 -6 144 C ATOM 3579 N PRO B 178 14.908 27.978 24.801 1.00 25.90 N ANISOU 3579 N PRO B 178 3354 3147 3340 206 -189 10 N ATOM 3580 CA PRO B 178 13.499 28.213 25.198 1.00 25.56 C ANISOU 3580 CA PRO B 178 3245 3092 3375 221 -249 3 C ATOM 3581 C PRO B 178 13.314 29.370 26.191 1.00 29.81 C ANISOU 3581 C PRO B 178 3720 3564 4041 238 -215 6 C ATOM 3582 O PRO B 178 12.313 30.079 26.088 1.00 29.80 O ANISOU 3582 O PRO B 178 3674 3540 4110 267 -262 38 O ATOM 3583 CB PRO B 178 13.069 26.869 25.793 1.00 27.01 C ANISOU 3583 CB PRO B 178 3408 3307 3549 193 -260 -79 C ATOM 3584 CG PRO B 178 13.990 25.859 25.156 1.00 30.81 C ANISOU 3584 CG PRO B 178 3959 3827 3922 171 -242 -100 C ATOM 3585 CD PRO B 178 15.304 26.575 25.082 1.00 26.29 C ANISOU 3585 CD PRO B 178 3422 3231 3336 175 -171 -64 C ATOM 3586 N GLN B 179 14.294 29.607 27.106 1.00 27.10 N ANISOU 3586 N GLN B 179 3372 3191 3732 221 -138 -30 N ATOM 3587 CA GLN B 179 14.271 30.740 28.060 1.00 27.10 C ANISOU 3587 CA GLN B 179 3319 3128 3851 233 -100 -45 C ATOM 3588 C GLN B 179 14.260 32.073 27.317 1.00 31.70 C ANISOU 3588 C GLN B 179 3903 3653 4489 265 -110 41 C ATOM 3589 O GLN B 179 13.468 32.944 27.667 1.00 32.13 O ANISOU 3589 O GLN B 179 3901 3658 4650 292 -126 47 O ATOM 3590 CB GLN B 179 15.481 30.705 29.026 1.00 28.24 C ANISOU 3590 CB GLN B 179 3466 3262 4004 207 -25 -100 C ATOM 3591 CG GLN B 179 15.392 31.726 30.180 1.00 29.56 C ANISOU 3591 CG GLN B 179 3571 3374 4285 214 11 -146 C ATOM 3592 CD GLN B 179 14.253 31.458 31.164 1.00 38.03 C ANISOU 3592 CD GLN B 179 4584 4464 5402 219 0 -208 C ATOM 3593 OE1 GLN B 179 13.816 30.320 31.365 1.00 34.92 O ANISOU 3593 OE1 GLN B 179 4189 4124 4954 197 2 -251 O ATOM 3594 NE2 GLN B 179 13.741 32.498 31.805 1.00 28.56 N ANISOU 3594 NE2 GLN B 179 3329 3215 4309 247 -6 -212 N ATOM 3595 N ALA B 180 15.156 32.237 26.309 1.00 27.77 N ANISOU 3595 N ALA B 180 3468 3159 3924 262 -96 110 N ATOM 3596 CA ALA B 180 15.260 33.446 25.482 1.00 27.23 C ANISOU 3596 CA ALA B 180 3413 3038 3897 288 -99 215 C ATOM 3597 C ALA B 180 13.965 33.677 24.667 1.00 30.86 C ANISOU 3597 C ALA B 180 3861 3508 4357 327 -189 284 C ATOM 3598 O ALA B 180 13.496 34.805 24.569 1.00 32.16 O ANISOU 3598 O ALA B 180 3991 3606 4624 361 -206 345 O ATOM 3599 CB ALA B 180 16.472 33.348 24.557 1.00 27.56 C ANISOU 3599 CB ALA B 180 3527 3101 3842 271 -58 273 C ATOM 3600 N ALA B 181 13.369 32.601 24.145 1.00 26.13 N ANISOU 3600 N ALA B 181 3283 2990 3655 323 -251 267 N ATOM 3601 CA ALA B 181 12.126 32.611 23.370 1.00 25.23 C ANISOU 3601 CA ALA B 181 3154 2906 3526 356 -352 317 C ATOM 3602 C ALA B 181 10.913 33.228 24.098 1.00 29.10 C ANISOU 3602 C ALA B 181 3550 3345 4163 386 -387 299 C ATOM 3603 O ALA B 181 10.131 33.923 23.462 1.00 28.92 O ANISOU 3603 O ALA B 181 3504 3304 4182 428 -455 379 O ATOM 3604 CB ALA B 181 11.792 31.197 22.935 1.00 25.51 C ANISOU 3604 CB ALA B 181 3220 3034 3440 333 -402 265 C ATOM 3605 N VAL B 182 10.753 32.962 25.409 1.00 26.28 N ANISOU 3605 N VAL B 182 3136 2968 3880 368 -342 197 N ATOM 3606 CA VAL B 182 9.617 33.433 26.225 1.00 25.89 C ANISOU 3606 CA VAL B 182 2991 2878 3968 393 -357 159 C ATOM 3607 C VAL B 182 9.821 34.850 26.778 1.00 32.05 C ANISOU 3607 C VAL B 182 3731 3557 4889 420 -308 174 C ATOM 3608 O VAL B 182 8.852 35.463 27.219 1.00 32.58 O ANISOU 3608 O VAL B 182 3719 3579 5081 454 -326 161 O ATOM 3609 CB VAL B 182 9.203 32.440 27.352 1.00 28.13 C ANISOU 3609 CB VAL B 182 3231 3199 4259 361 -330 45 C ATOM 3610 CG1 VAL B 182 8.813 31.088 26.768 1.00 27.57 C ANISOU 3610 CG1 VAL B 182 3185 3209 4080 336 -389 31 C ATOM 3611 CG2 VAL B 182 10.299 32.281 28.418 1.00 27.60 C ANISOU 3611 CG2 VAL B 182 3183 3122 4183 326 -234 -25 C ATOM 3612 N MET B 183 11.063 35.363 26.774 1.00 28.96 N ANISOU 3612 N MET B 183 3386 3126 4490 405 -243 194 N ATOM 3613 CA MET B 183 11.355 36.698 27.303 1.00 28.12 C ANISOU 3613 CA MET B 183 3242 2914 4528 423 -193 198 C ATOM 3614 C MET B 183 10.737 37.766 26.449 1.00 36.20 C ANISOU 3614 C MET B 183 4246 3872 5638 476 -246 313 C ATOM 3615 O MET B 183 10.899 37.764 25.227 1.00 36.38 O ANISOU 3615 O MET B 183 4326 3921 5577 487 -291 426 O ATOM 3616 CB MET B 183 12.860 36.947 27.460 1.00 29.18 C ANISOU 3616 CB MET B 183 3425 3021 4642 388 -115 192 C ATOM 3617 CG MET B 183 13.549 36.046 28.458 1.00 31.44 C ANISOU 3617 CG MET B 183 3719 3360 4866 342 -62 77 C ATOM 3618 SD MET B 183 12.647 35.681 30.001 1.00 33.97 S ANISOU 3618 SD MET B 183 3961 3701 5246 340 -48 -58 S ATOM 3619 CE MET B 183 12.766 37.241 30.836 1.00 30.56 C ANISOU 3619 CE MET B 183 3467 3154 4993 360 4 -102 C ATOM 3620 N GLU B 184 9.999 38.662 27.088 1.00 35.98 N ANISOU 3620 N GLU B 184 4135 3761 5774 512 -241 285 N ATOM 3621 CA GLU B 184 9.346 39.753 26.396 1.00 37.36 C ANISOU 3621 CA GLU B 184 4277 3856 6062 570 -292 395 C ATOM 3622 C GLU B 184 9.460 41.040 27.168 1.00 43.74 C ANISOU 3622 C GLU B 184 5024 4531 7064 591 -233 361 C ATOM 3623 O GLU B 184 9.373 41.035 28.400 1.00 41.38 O ANISOU 3623 O GLU B 184 4672 4218 6833 578 -178 225 O ATOM 3624 CB GLU B 184 7.885 39.409 26.112 1.00 39.12 C ANISOU 3624 CB GLU B 184 4443 4122 6298 609 -385 409 C ATOM 3625 CG GLU B 184 7.466 39.706 24.683 1.00 57.33 C ANISOU 3625 CG GLU B 184 6776 6435 8573 653 -482 568 C ATOM 3626 CD GLU B 184 8.146 38.892 23.595 1.00 89.21 C ANISOU 3626 CD GLU B 184 10921 10570 12405 623 -512 642 C ATOM 3627 OE1 GLU B 184 8.783 39.506 22.705 1.00 88.80 O ANISOU 3627 OE1 GLU B 184 10926 10487 12326 635 -510 767 O ATOM 3628 OE2 GLU B 184 8.045 37.643 23.632 1.00 82.78 O ANISOU 3628 OE2 GLU B 184 10132 9861 11460 587 -531 573 O ATOM 3629 N CYS B 185 9.715 42.143 26.434 1.00 45.28 N ANISOU 3629 N CYS B 185 5230 4628 7345 622 -239 484 N ATOM 3630 CA CYS B 185 9.805 43.481 26.996 1.00 47.46 C ANISOU 3630 CA CYS B 185 5447 4756 7830 646 -188 467 C ATOM 3631 C CYS B 185 8.517 44.209 26.676 1.00 55.86 C ANISOU 3631 C CYS B 185 6436 5752 9038 721 -257 534 C ATOM 3632 O CYS B 185 8.161 44.365 25.507 1.00 55.49 O ANISOU 3632 O CYS B 185 6413 5712 8958 757 -334 689 O ATOM 3633 CB CYS B 185 11.022 44.236 26.475 1.00 48.45 C ANISOU 3633 CB CYS B 185 5627 4802 7981 625 -139 559 C ATOM 3634 SG CYS B 185 11.316 45.814 27.317 1.00 53.16 S ANISOU 3634 SG CYS B 185 6149 5202 8847 640 -65 507 S ATOM 3635 N SER B 186 7.789 44.602 27.711 1.00 56.70 N ANISOU 3635 N SER B 186 6448 5801 9296 746 -231 416 N ATOM 3636 CA SER B 186 6.528 45.308 27.539 1.00 58.88 C ANISOU 3636 CA SER B 186 6634 6005 9734 822 -290 462 C ATOM 3637 C SER B 186 6.452 46.544 28.421 1.00 66.98 C ANISOU 3637 C SER B 186 7578 6874 10998 852 -223 382 C ATOM 3638 O SER B 186 6.904 46.507 29.565 1.00 65.17 O ANISOU 3638 O SER B 186 7331 6640 10790 814 -138 221 O ATOM 3639 CB SER B 186 5.347 44.374 27.783 1.00 62.71 C ANISOU 3639 CB SER B 186 7066 6597 10165 835 -343 397 C ATOM 3640 OG SER B 186 5.412 43.764 29.059 1.00 70.62 O ANISOU 3640 OG SER B 186 8041 7650 11142 793 -268 219 O ATOM 3641 N SER B 187 5.953 47.654 27.863 1.00 68.82 N ANISOU 3641 N SER B 187 7764 6976 11406 919 -260 496 N ATOM 3642 CA SER B 187 5.798 48.918 28.588 1.00 70.70 C ANISOU 3642 CA SER B 187 7918 7044 11899 956 -202 427 C ATOM 3643 C SER B 187 4.461 48.942 29.350 1.00 77.11 C ANISOU 3643 C SER B 187 8612 7853 12831 1008 -211 314 C ATOM 3644 O SER B 187 3.648 48.025 29.190 1.00 77.36 O ANISOU 3644 O SER B 187 8628 8009 12754 1015 -270 314 O ATOM 3645 CB SER B 187 5.910 50.103 27.633 1.00 75.64 C ANISOU 3645 CB SER B 187 8545 7519 12676 1006 -233 609 C ATOM 3646 OG SER B 187 4.999 49.984 26.554 1.00 88.35 O ANISOU 3646 OG SER B 187 10141 9158 14270 1069 -347 772 O ATOM 3647 N VAL B 188 4.255 49.962 30.211 1.00 74.69 N ANISOU 3647 N VAL B 188 8220 7407 12752 1041 -146 206 N ATOM 3648 CA VAL B 188 3.019 50.116 30.995 1.00114.89 C ANISOU 3648 CA VAL B 188 13190 12482 17980 1094 -136 87 C ATOM 3649 C VAL B 188 2.348 51.452 30.648 1.00142.72 C ANISOU 3649 C VAL B 188 16624 15821 21782 1186 -162 165 C ATOM 3650 O VAL B 188 1.662 51.552 29.631 1.00103.41 O ANISOU 3650 O VAL B 188 11639 10825 16828 1239 -263 348 O ATOM 3651 CB VAL B 188 3.228 49.931 32.530 1.00118.81 C ANISOU 3651 CB VAL B 188 13656 13013 18475 1051 -23 -156 C ATOM 3652 CG1 VAL B 188 1.915 50.112 33.295 1.00118.58 C ANISOU 3652 CG1 VAL B 188 13498 12969 18590 1109 -1 -274 C ATOM 3653 CG2 VAL B 188 3.848 48.569 32.853 1.00118.54 C ANISOU 3653 CG2 VAL B 188 13707 13161 18171 967 -5 -214 C ATOM 3654 N PHE B 199 8.792 52.374 33.208 1.00 73.23 N ANISOU 3654 N PHE B 199 8092 6892 12838 838 224 -284 N ATOM 3655 CA PHE B 199 7.657 51.949 32.393 1.00 73.01 C ANISOU 3655 CA PHE B 199 8059 6910 12772 898 137 -120 C ATOM 3656 C PHE B 199 7.774 50.536 31.800 1.00 71.88 C ANISOU 3656 C PHE B 199 8001 6964 12347 860 84 -39 C ATOM 3657 O PHE B 199 6.754 49.857 31.705 1.00 71.25 O ANISOU 3657 O PHE B 199 7892 6982 12196 890 35 -35 O ATOM 3658 CB PHE B 199 7.387 52.955 31.263 1.00 75.92 C ANISOU 3658 CB PHE B 199 8422 7118 13307 950 93 85 C ATOM 3659 CG PHE B 199 7.415 54.399 31.706 1.00 78.81 C ANISOU 3659 CG PHE B 199 8710 7265 13971 983 147 22 C ATOM 3660 CD1 PHE B 199 6.311 54.975 32.322 1.00 82.79 C ANISOU 3660 CD1 PHE B 199 9103 7677 14677 1061 147 -51 C ATOM 3661 CD2 PHE B 199 8.558 55.176 31.531 1.00 82.11 C ANISOU 3661 CD2 PHE B 199 9157 7561 14479 935 202 25 C ATOM 3662 CE1 PHE B 199 6.343 56.304 32.750 1.00 84.22 C ANISOU 3662 CE1 PHE B 199 9209 7645 15146 1093 200 -122 C ATOM 3663 CE2 PHE B 199 8.593 56.506 31.965 1.00 85.49 C ANISOU 3663 CE2 PHE B 199 9509 7775 15198 962 253 -46 C ATOM 3664 CZ PHE B 199 7.484 57.063 32.567 1.00 83.83 C ANISOU 3664 CZ PHE B 199 9194 7472 15186 1042 252 -121 C ATOM 3665 N SER B 200 8.970 50.140 31.314 1.00 64.01 N ANISOU 3665 N SER B 200 7099 6014 11205 798 91 32 N ATOM 3666 CA SER B 200 9.170 48.831 30.682 1.00 61.02 C ANISOU 3666 CA SER B 200 6805 5810 10569 762 44 108 C ATOM 3667 C SER B 200 9.524 47.731 31.652 1.00 57.59 C ANISOU 3667 C SER B 200 6394 5520 9967 703 84 -53 C ATOM 3668 O SER B 200 10.291 47.949 32.575 1.00 56.57 O ANISOU 3668 O SER B 200 6261 5367 9866 661 154 -187 O ATOM 3669 CB SER B 200 10.216 48.913 29.577 1.00 65.03 C ANISOU 3669 CB SER B 200 7403 6304 11003 732 35 274 C ATOM 3670 OG SER B 200 9.641 49.410 28.381 1.00 76.14 O ANISOU 3670 OG SER B 200 8806 7635 12487 791 -29 468 O ATOM 3671 N VAL B 201 8.965 46.546 31.440 1.00 50.77 N ANISOU 3671 N VAL B 201 5554 4804 8933 699 36 -36 N ATOM 3672 CA VAL B 201 9.229 45.341 32.236 1.00 48.58 C ANISOU 3672 CA VAL B 201 5305 4673 8481 645 64 -157 C ATOM 3673 C VAL B 201 9.669 44.191 31.319 1.00 45.69 C ANISOU 3673 C VAL B 201 5030 4429 7900 611 17 -52 C ATOM 3674 O VAL B 201 9.060 43.958 30.273 1.00 43.94 O ANISOU 3674 O VAL B 201 4823 4235 7639 642 -58 76 O ATOM 3675 CB VAL B 201 8.005 44.964 33.139 1.00 52.91 C ANISOU 3675 CB VAL B 201 5774 5277 9055 671 71 -277 C ATOM 3676 CG1 VAL B 201 7.969 43.485 33.510 1.00 52.88 C ANISOU 3676 CG1 VAL B 201 5806 5439 8847 626 68 -328 C ATOM 3677 CG2 VAL B 201 7.936 45.834 34.385 1.00 52.56 C ANISOU 3677 CG2 VAL B 201 5657 5150 9161 680 149 -442 C ATOM 3678 N CYS B 202 10.731 43.481 31.723 1.00 39.18 N ANISOU 3678 N CYS B 202 4264 3681 6943 548 58 -112 N ATOM 3679 CA CYS B 202 11.229 42.296 31.028 1.00 36.64 C ANISOU 3679 CA CYS B 202 4026 3477 6419 512 28 -45 C ATOM 3680 C CYS B 202 10.743 41.080 31.817 1.00 38.08 C ANISOU 3680 C CYS B 202 4197 3784 6488 490 29 -150 C ATOM 3681 O CYS B 202 11.061 40.932 32.997 1.00 37.92 O ANISOU 3681 O CYS B 202 4157 3787 6464 462 86 -281 O ATOM 3682 CB CYS B 202 12.747 42.312 30.909 1.00 35.98 C ANISOU 3682 CB CYS B 202 4006 3387 6278 460 74 -35 C ATOM 3683 SG CYS B 202 13.436 40.898 30.015 1.00 39.37 S ANISOU 3683 SG CYS B 202 4534 3951 6472 420 48 41 S ATOM 3684 N ASP B 203 9.938 40.238 31.185 1.00 32.01 N ANISOU 3684 N ASP B 203 3437 3093 5633 503 -36 -91 N ATOM 3685 CA ASP B 203 9.405 39.069 31.860 1.00 31.31 C ANISOU 3685 CA ASP B 203 3334 3112 5451 481 -35 -174 C ATOM 3686 C ASP B 203 9.039 37.978 30.866 1.00 31.94 C ANISOU 3686 C ASP B 203 3457 3280 5399 475 -108 -93 C ATOM 3687 O ASP B 203 8.968 38.227 29.663 1.00 31.58 O ANISOU 3687 O ASP B 203 3442 3217 5341 498 -167 25 O ATOM 3688 CB ASP B 203 8.190 39.463 32.747 1.00 33.70 C ANISOU 3688 CB ASP B 203 3535 3389 5880 517 -19 -260 C ATOM 3689 CG ASP B 203 7.880 38.539 33.932 1.00 48.62 C ANISOU 3689 CG ASP B 203 5400 5372 7703 485 26 -380 C ATOM 3690 OD1 ASP B 203 8.652 37.557 34.160 1.00 49.29 O ANISOU 3690 OD1 ASP B 203 5545 5537 7644 435 44 -400 O ATOM 3691 OD2 ASP B 203 6.874 38.790 34.626 1.00 55.89 O ANISOU 3691 OD2 ASP B 203 6236 6284 8714 512 47 -448 O ATOM 3692 N GLU B 204 8.823 36.764 31.375 1.00 26.98 N ANISOU 3692 N GLU B 204 2832 2747 4671 442 -102 -156 N ATOM 3693 CA GLU B 204 8.427 35.608 30.583 1.00 26.42 C ANISOU 3693 CA GLU B 204 2794 2760 4484 429 -168 -108 C ATOM 3694 C GLU B 204 6.969 35.769 30.135 1.00 32.36 C ANISOU 3694 C GLU B 204 3476 3506 5314 472 -241 -72 C ATOM 3695 O GLU B 204 6.124 36.222 30.915 1.00 30.01 O ANISOU 3695 O GLU B 204 3091 3178 5135 497 -218 -130 O ATOM 3696 CB GLU B 204 8.549 34.325 31.408 1.00 27.07 C ANISOU 3696 CB GLU B 204 2887 2928 4472 381 -133 -192 C ATOM 3697 CG GLU B 204 9.931 34.034 31.963 1.00 28.28 C ANISOU 3697 CG GLU B 204 3099 3098 4547 340 -69 -234 C ATOM 3698 CD GLU B 204 10.000 32.791 32.830 1.00 41.83 C ANISOU 3698 CD GLU B 204 4820 4893 6180 299 -38 -304 C ATOM 3699 OE1 GLU B 204 8.988 32.055 32.914 1.00 34.26 O ANISOU 3699 OE1 GLU B 204 3824 3976 5216 296 -64 -315 O ATOM 3700 OE2 GLU B 204 11.076 32.548 33.420 1.00 36.24 O ANISOU 3700 OE2 GLU B 204 4149 4202 5416 270 11 -342 O ATOM 3701 N ARG B 205 6.679 35.388 28.887 1.00 31.57 N ANISOU 3701 N ARG B 205 3409 3441 5145 482 -328 20 N ATOM 3702 CA ARG B 205 5.334 35.454 28.334 1.00 32.49 C ANISOU 3702 CA ARG B 205 3459 3564 5322 522 -416 61 C ATOM 3703 C ARG B 205 4.886 34.043 28.032 1.00 36.67 C ANISOU 3703 C ARG B 205 4000 4191 5742 487 -467 39 C ATOM 3704 O ARG B 205 5.515 33.357 27.221 1.00 37.82 O ANISOU 3704 O ARG B 205 4230 4389 5751 461 -498 75 O ATOM 3705 CB ARG B 205 5.279 36.341 27.067 1.00 35.56 C ANISOU 3705 CB ARG B 205 3870 3909 5731 571 -491 195 C ATOM 3706 CG ARG B 205 3.861 36.484 26.508 1.00 52.84 C ANISOU 3706 CG ARG B 205 5980 6104 7994 619 -596 243 C ATOM 3707 CD ARG B 205 3.575 37.865 25.970 1.00 75.17 C ANISOU 3707 CD ARG B 205 8773 8838 10950 687 -633 345 C ATOM 3708 NE ARG B 205 3.996 37.960 24.577 1.00 93.71 N ANISOU 3708 NE ARG B 205 11206 11211 13189 699 -706 482 N ATOM 3709 CZ ARG B 205 4.195 39.089 23.904 1.00113.70 C ANISOU 3709 CZ ARG B 205 13752 13666 15784 746 -726 604 C ATOM 3710 NH1 ARG B 205 4.587 39.050 22.641 1.00103.25 N ANISOU 3710 NH1 ARG B 205 12512 12385 14332 752 -786 730 N ATOM 3711 NH2 ARG B 205 4.041 40.266 24.501 1.00102.31 N ANISOU 3711 NH2 ARG B 205 12242 12100 14531 785 -679 601 N ATOM 3712 N TRP B 206 3.816 33.601 28.691 1.00 32.34 N ANISOU 3712 N TRP B 206 3364 3664 5261 484 -470 -27 N ATOM 3713 CA TRP B 206 3.287 32.258 28.472 1.00 31.01 C ANISOU 3713 CA TRP B 206 3190 3576 5017 446 -517 -55 C ATOM 3714 C TRP B 206 1.884 32.371 27.910 1.00 37.85 C ANISOU 3714 C TRP B 206 3966 4447 5967 482 -616 -24 C ATOM 3715 O TRP B 206 1.076 33.132 28.443 1.00 37.98 O ANISOU 3715 O TRP B 206 3885 4416 6130 521 -602 -40 O ATOM 3716 CB TRP B 206 3.340 31.411 29.765 1.00 27.81 C ANISOU 3716 CB TRP B 206 2762 3200 4606 398 -427 -155 C ATOM 3717 CG TRP B 206 4.731 31.206 30.303 1.00 27.05 C ANISOU 3717 CG TRP B 206 2751 3107 4420 364 -343 -184 C ATOM 3718 CD1 TRP B 206 5.366 31.953 31.258 1.00 29.60 C ANISOU 3718 CD1 TRP B 206 3073 3389 4785 369 -256 -225 C ATOM 3719 CD2 TRP B 206 5.684 30.222 29.865 1.00 26.26 C ANISOU 3719 CD2 TRP B 206 2744 3053 4180 322 -346 -176 C ATOM 3720 NE1 TRP B 206 6.658 31.495 31.442 1.00 28.32 N ANISOU 3720 NE1 TRP B 206 2995 3249 4517 332 -210 -237 N ATOM 3721 CE2 TRP B 206 6.871 30.422 30.611 1.00 29.71 C ANISOU 3721 CE2 TRP B 206 3228 3475 4584 304 -260 -207 C ATOM 3722 CE3 TRP B 206 5.633 29.153 28.950 1.00 26.56 C ANISOU 3722 CE3 TRP B 206 2827 3144 4123 297 -412 -157 C ATOM 3723 CZ2 TRP B 206 7.991 29.589 30.469 1.00 28.34 C ANISOU 3723 CZ2 TRP B 206 3138 3335 4293 267 -238 -210 C ATOM 3724 CZ3 TRP B 206 6.750 28.355 28.789 1.00 27.20 C ANISOU 3724 CZ3 TRP B 206 2995 3253 4087 260 -384 -166 C ATOM 3725 CH2 TRP B 206 7.914 28.576 29.538 1.00 27.66 C ANISOU 3725 CH2 TRP B 206 3093 3293 4122 248 -297 -188 C ATOM 3726 N ALA B 207 1.606 31.648 26.800 1.00 35.96 N ANISOU 3726 N ALA B 207 3757 4268 5639 472 -720 16 N ATOM 3727 CA ALA B 207 0.285 31.634 26.145 1.00 35.56 C ANISOU 3727 CA ALA B 207 3620 4237 5654 502 -836 45 C ATOM 3728 C ALA B 207 -0.738 30.851 26.960 1.00 40.35 C ANISOU 3728 C ALA B 207 4122 4866 6345 472 -819 -42 C ATOM 3729 O ALA B 207 -1.938 31.061 26.802 1.00 42.54 O ANISOU 3729 O ALA B 207 4291 5139 6734 503 -886 -35 O ATOM 3730 CB ALA B 207 0.403 31.043 24.751 1.00 36.18 C ANISOU 3730 CB ALA B 207 3770 4383 5593 493 -950 99 C ATOM 3731 N ASP B 208 -0.275 29.935 27.821 1.00 36.81 N ANISOU 3731 N ASP B 208 3700 4439 5845 413 -729 -117 N ATOM 3732 CA ASP B 208 -1.148 29.152 28.698 1.00 36.70 C ANISOU 3732 CA ASP B 208 3593 4445 5906 377 -690 -192 C ATOM 3733 C ASP B 208 -0.533 29.018 30.084 1.00 36.66 C ANISOU 3733 C ASP B 208 3603 4429 5899 347 -546 -254 C ATOM 3734 O ASP B 208 0.661 29.230 30.233 1.00 35.90 O ANISOU 3734 O ASP B 208 3601 4322 5719 341 -493 -247 O ATOM 3735 CB ASP B 208 -1.500 27.780 28.088 1.00 39.77 C ANISOU 3735 CB ASP B 208 3990 4893 6229 324 -763 -213 C ATOM 3736 CG ASP B 208 -0.379 26.787 28.132 1.00 54.38 C ANISOU 3736 CG ASP B 208 5952 6769 7939 269 -717 -237 C ATOM 3737 OD1 ASP B 208 0.446 26.795 27.207 1.00 60.45 O ANISOU 3737 OD1 ASP B 208 6822 7553 8592 274 -761 -198 O ATOM 3738 OD2 ASP B 208 -0.318 26.009 29.102 1.00 58.40 O ANISOU 3738 OD2 ASP B 208 6447 7283 8458 222 -633 -291 O ATOM 3739 N ASP B 209 -1.346 28.662 31.086 1.00 31.11 N ANISOU 3739 N ASP B 209 2805 3734 5283 327 -485 -312 N ATOM 3740 CA ASP B 209 -0.924 28.523 32.480 1.00 30.02 C ANISOU 3740 CA ASP B 209 2669 3599 5138 301 -349 -370 C ATOM 3741 C ASP B 209 -0.213 27.217 32.808 1.00 30.76 C ANISOU 3741 C ASP B 209 2837 3734 5114 234 -308 -390 C ATOM 3742 O ASP B 209 0.497 27.183 33.808 1.00 30.68 O ANISOU 3742 O ASP B 209 2865 3731 5059 217 -209 -420 O ATOM 3743 CB ASP B 209 -2.123 28.727 33.434 1.00 31.74 C ANISOU 3743 CB ASP B 209 2751 3814 5494 310 -289 -420 C ATOM 3744 CG ASP B 209 -3.138 27.611 33.361 1.00 42.64 C ANISOU 3744 CG ASP B 209 4055 5230 6916 267 -321 -433 C ATOM 3745 OD1 ASP B 209 -3.778 27.454 32.282 1.00 45.86 O ANISOU 3745 OD1 ASP B 209 4428 5640 7357 277 -442 -400 O ATOM 3746 OD2 ASP B 209 -3.303 26.895 34.375 1.00 44.14 O ANISOU 3746 OD2 ASP B 209 4218 5449 7105 221 -227 -473 O ATOM 3747 N LEU B 210 -0.426 26.140 32.017 1.00 26.05 N ANISOU 3747 N LEU B 210 2257 3164 4475 197 -384 -376 N ATOM 3748 CA LEU B 210 0.221 24.840 32.257 1.00 26.08 C ANISOU 3748 CA LEU B 210 2328 3195 4387 136 -351 -392 C ATOM 3749 C LEU B 210 1.702 24.785 31.783 1.00 29.43 C ANISOU 3749 C LEU B 210 2885 3619 4676 134 -352 -370 C ATOM 3750 O LEU B 210 2.554 24.264 32.523 1.00 28.80 O ANISOU 3750 O LEU B 210 2860 3549 4535 105 -276 -385 O ATOM 3751 CB LEU B 210 -0.601 23.689 31.673 1.00 26.53 C ANISOU 3751 CB LEU B 210 2341 3270 4469 93 -423 -403 C ATOM 3752 CG LEU B 210 -0.029 22.265 31.846 1.00 33.34 C ANISOU 3752 CG LEU B 210 3263 4144 5260 30 -395 -419 C ATOM 3753 CD1 LEU B 210 0.044 21.842 33.325 1.00 33.62 C ANISOU 3753 CD1 LEU B 210 3273 4185 5318 -3 -267 -436 C ATOM 3754 CD2 LEU B 210 -0.803 21.246 30.999 1.00 36.39 C ANISOU 3754 CD2 LEU B 210 3612 4536 5677 -8 -490 -437 C ATOM 3755 N ALA B 211 2.009 25.330 30.576 1.00 25.61 N ANISOU 3755 N ALA B 211 2452 3129 4150 167 -437 -328 N ATOM 3756 CA ALA B 211 3.386 25.357 30.018 1.00 24.91 C ANISOU 3756 CA ALA B 211 2483 3041 3940 169 -435 -303 C ATOM 3757 C ALA B 211 4.460 25.908 30.999 1.00 28.40 C ANISOU 3757 C ALA B 211 2967 3465 4359 174 -331 -312 C ATOM 3758 O ALA B 211 5.462 25.206 31.173 1.00 28.60 O ANISOU 3758 O ALA B 211 3063 3503 4299 144 -293 -322 O ATOM 3759 CB ALA B 211 3.422 26.112 28.697 1.00 25.60 C ANISOU 3759 CB ALA B 211 2603 3125 3998 210 -527 -246 C ATOM 3760 N PRO B 212 4.279 27.083 31.707 1.00 24.10 N ANISOU 3760 N PRO B 212 2374 2890 3894 209 -283 -320 N ATOM 3761 CA PRO B 212 5.317 27.526 32.676 1.00 22.95 C ANISOU 3761 CA PRO B 212 2266 2733 3721 207 -191 -345 C ATOM 3762 C PRO B 212 5.503 26.573 33.861 1.00 27.21 C ANISOU 3762 C PRO B 212 2803 3309 4228 163 -114 -390 C ATOM 3763 O PRO B 212 6.592 26.516 34.408 1.00 26.58 O ANISOU 3763 O PRO B 212 2780 3237 4084 151 -62 -403 O ATOM 3764 CB PRO B 212 4.803 28.887 33.147 1.00 24.64 C ANISOU 3764 CB PRO B 212 2412 2905 4046 252 -165 -359 C ATOM 3765 CG PRO B 212 3.324 28.859 32.894 1.00 28.35 C ANISOU 3765 CG PRO B 212 2785 3376 4612 268 -215 -356 C ATOM 3766 CD PRO B 212 3.173 28.071 31.639 1.00 24.08 C ANISOU 3766 CD PRO B 212 2279 2858 4013 254 -313 -311 C ATOM 3767 N LYS B 213 4.454 25.826 34.269 1.00 24.61 N ANISOU 3767 N LYS B 213 2404 3002 3944 140 -108 -409 N ATOM 3768 CA LYS B 213 4.567 24.851 35.360 1.00 24.78 C ANISOU 3768 CA LYS B 213 2424 3059 3934 97 -35 -434 C ATOM 3769 C LYS B 213 5.420 23.667 34.912 1.00 28.92 C ANISOU 3769 C LYS B 213 3029 3593 4366 61 -56 -413 C ATOM 3770 O LYS B 213 6.270 23.210 35.676 1.00 28.86 O ANISOU 3770 O LYS B 213 3065 3603 4296 41 1 -418 O ATOM 3771 CB LYS B 213 3.189 24.354 35.821 1.00 27.88 C ANISOU 3771 CB LYS B 213 2716 3467 4411 78 -19 -450 C ATOM 3772 CG LYS B 213 2.253 25.461 36.301 1.00 31.26 C ANISOU 3772 CG LYS B 213 3050 3883 4944 116 10 -478 C ATOM 3773 CD LYS B 213 0.984 24.886 36.863 1.00 38.67 C ANISOU 3773 CD LYS B 213 3885 4842 5964 92 43 -495 C ATOM 3774 CE LYS B 213 -0.006 25.987 37.102 1.00 59.00 C ANISOU 3774 CE LYS B 213 6358 7399 8659 137 58 -525 C ATOM 3775 NZ LYS B 213 -1.253 25.476 37.725 1.00 77.52 N ANISOU 3775 NZ LYS B 213 8592 9768 11093 114 106 -545 N ATOM 3776 N ILE B 214 5.204 23.176 33.668 1.00 24.30 N ANISOU 3776 N ILE B 214 2463 2999 3772 55 -142 -393 N ATOM 3777 CA ILE B 214 5.988 22.073 33.121 1.00 23.91 C ANISOU 3777 CA ILE B 214 2488 2953 3644 25 -164 -385 C ATOM 3778 C ILE B 214 7.452 22.520 32.939 1.00 27.04 C ANISOU 3778 C ILE B 214 2973 3345 3957 43 -144 -372 C ATOM 3779 O ILE B 214 8.361 21.833 33.409 1.00 26.32 O ANISOU 3779 O ILE B 214 2928 3259 3811 22 -102 -375 O ATOM 3780 CB ILE B 214 5.365 21.465 31.824 1.00 26.70 C ANISOU 3780 CB ILE B 214 2838 3303 4003 13 -262 -384 C ATOM 3781 CG1 ILE B 214 3.952 20.860 32.111 1.00 27.66 C ANISOU 3781 CG1 ILE B 214 2862 3427 4222 -15 -277 -403 C ATOM 3782 CG2 ILE B 214 6.315 20.427 31.195 1.00 24.87 C ANISOU 3782 CG2 ILE B 214 2692 3070 3687 -11 -278 -390 C ATOM 3783 CD1 ILE B 214 3.136 20.477 30.913 1.00 30.56 C ANISOU 3783 CD1 ILE B 214 3203 3795 4614 -23 -385 -413 C ATOM 3784 N TYR B 215 7.660 23.696 32.298 1.00 22.28 N ANISOU 3784 N TYR B 215 2385 2726 3354 82 -173 -353 N ATOM 3785 CA TYR B 215 8.989 24.241 32.032 1.00 20.51 C ANISOU 3785 CA TYR B 215 2234 2493 3067 98 -153 -337 C ATOM 3786 C TYR B 215 9.819 24.454 33.303 1.00 25.01 C ANISOU 3786 C TYR B 215 2811 3067 3626 92 -71 -359 C ATOM 3787 O TYR B 215 10.963 23.982 33.371 1.00 23.94 O ANISOU 3787 O TYR B 215 2731 2937 3426 79 -47 -358 O ATOM 3788 CB TYR B 215 8.897 25.542 31.215 1.00 20.77 C ANISOU 3788 CB TYR B 215 2268 2500 3123 140 -192 -301 C ATOM 3789 CG TYR B 215 10.245 26.199 31.037 1.00 22.60 C ANISOU 3789 CG TYR B 215 2564 2715 3309 151 -159 -282 C ATOM 3790 CD1 TYR B 215 11.171 25.698 30.119 1.00 23.69 C ANISOU 3790 CD1 TYR B 215 2777 2865 3359 142 -174 -259 C ATOM 3791 CD2 TYR B 215 10.640 27.264 31.851 1.00 22.93 C ANISOU 3791 CD2 TYR B 215 2585 2728 3399 168 -106 -295 C ATOM 3792 CE1 TYR B 215 12.444 26.247 30.004 1.00 23.98 C ANISOU 3792 CE1 TYR B 215 2863 2885 3362 148 -135 -242 C ATOM 3793 CE2 TYR B 215 11.907 27.838 31.727 1.00 22.81 C ANISOU 3793 CE2 TYR B 215 2619 2692 3355 172 -74 -281 C ATOM 3794 CZ TYR B 215 12.809 27.320 30.808 1.00 30.80 C ANISOU 3794 CZ TYR B 215 3701 3717 4284 161 -87 -250 C ATOM 3795 OH TYR B 215 14.066 27.871 30.677 1.00 26.11 O ANISOU 3795 OH TYR B 215 3147 3102 3671 162 -49 -235 O ATOM 3796 N HIS B 216 9.241 25.159 34.307 1.00 22.86 N ANISOU 3796 N HIS B 216 2476 2794 3416 103 -29 -386 N ATOM 3797 CA HIS B 216 9.933 25.496 35.552 1.00 22.51 C ANISOU 3797 CA HIS B 216 2433 2763 3356 100 43 -419 C ATOM 3798 C HIS B 216 10.139 24.303 36.469 1.00 26.43 C ANISOU 3798 C HIS B 216 2937 3301 3804 65 83 -427 C ATOM 3799 O HIS B 216 11.111 24.312 37.227 1.00 26.31 O ANISOU 3799 O HIS B 216 2951 3306 3740 60 123 -441 O ATOM 3800 CB HIS B 216 9.280 26.684 36.256 1.00 22.73 C ANISOU 3800 CB HIS B 216 2397 2779 3462 126 75 -455 C ATOM 3801 CG HIS B 216 9.577 27.963 35.528 1.00 25.20 C ANISOU 3801 CG HIS B 216 2718 3038 3818 162 49 -441 C ATOM 3802 ND1 HIS B 216 10.850 28.524 35.544 1.00 26.72 N ANISOU 3802 ND1 HIS B 216 2959 3212 3981 165 69 -444 N ATOM 3803 CD2 HIS B 216 8.798 28.679 34.691 1.00 25.93 C ANISOU 3803 CD2 HIS B 216 2778 3091 3982 194 0 -412 C ATOM 3804 CE1 HIS B 216 10.778 29.590 34.767 1.00 25.94 C ANISOU 3804 CE1 HIS B 216 2856 3058 3941 195 41 -416 C ATOM 3805 NE2 HIS B 216 9.557 29.729 34.245 1.00 26.15 N ANISOU 3805 NE2 HIS B 216 2837 3073 4028 217 -3 -392 N ATOM 3806 N SER B 217 9.319 23.241 36.328 1.00 23.01 N ANISOU 3806 N SER B 217 2481 2878 3385 40 67 -413 N ATOM 3807 CA SER B 217 9.533 21.988 37.050 1.00 22.57 C ANISOU 3807 CA SER B 217 2437 2848 3291 6 101 -403 C ATOM 3808 C SER B 217 10.778 21.312 36.462 1.00 25.61 C ANISOU 3808 C SER B 217 2899 3221 3612 -1 80 -383 C ATOM 3809 O SER B 217 11.630 20.879 37.225 1.00 26.00 O ANISOU 3809 O SER B 217 2975 3290 3614 -10 117 -377 O ATOM 3810 CB SER B 217 8.310 21.082 36.955 1.00 25.10 C ANISOU 3810 CB SER B 217 2706 3166 3664 -22 88 -393 C ATOM 3811 OG SER B 217 7.230 21.645 37.682 1.00 29.91 O ANISOU 3811 OG SER B 217 3236 3792 4335 -17 125 -413 O ATOM 3812 N CYS B 218 10.918 21.296 35.117 1.00 23.26 N ANISOU 3812 N CYS B 218 2634 2895 3308 7 21 -374 N ATOM 3813 CA CYS B 218 12.097 20.764 34.408 1.00 24.14 C ANISOU 3813 CA CYS B 218 2815 2995 3361 6 6 -364 C ATOM 3814 C CYS B 218 13.346 21.583 34.742 1.00 27.70 C ANISOU 3814 C CYS B 218 3298 3451 3777 25 38 -366 C ATOM 3815 O CYS B 218 14.376 21.004 35.076 1.00 28.28 O ANISOU 3815 O CYS B 218 3403 3529 3811 18 61 -361 O ATOM 3816 CB CYS B 218 11.874 20.706 32.897 1.00 25.00 C ANISOU 3816 CB CYS B 218 2950 3087 3461 13 -59 -360 C ATOM 3817 SG CYS B 218 10.594 19.539 32.381 1.00 29.36 S ANISOU 3817 SG CYS B 218 3468 3632 4054 -18 -110 -373 S ATOM 3818 N PHE B 219 13.246 22.929 34.670 1.00 23.29 N ANISOU 3818 N PHE B 219 2722 2883 3243 50 39 -373 N ATOM 3819 CA PHE B 219 14.354 23.839 34.964 1.00 21.99 C ANISOU 3819 CA PHE B 219 2577 2713 3066 64 68 -381 C ATOM 3820 C PHE B 219 14.976 23.505 36.325 1.00 28.23 C ANISOU 3820 C PHE B 219 3360 3536 3829 51 113 -402 C ATOM 3821 O PHE B 219 16.190 23.329 36.397 1.00 26.81 O ANISOU 3821 O PHE B 219 3214 3360 3613 50 124 -400 O ATOM 3822 CB PHE B 219 13.903 25.319 34.909 1.00 22.10 C ANISOU 3822 CB PHE B 219 2558 2701 3138 89 67 -391 C ATOM 3823 CG PHE B 219 15.058 26.291 34.890 1.00 22.28 C ANISOU 3823 CG PHE B 219 2602 2702 3163 100 89 -396 C ATOM 3824 CD1 PHE B 219 15.554 26.782 33.690 1.00 24.44 C ANISOU 3824 CD1 PHE B 219 2911 2941 3432 112 68 -357 C ATOM 3825 CD2 PHE B 219 15.659 26.714 36.075 1.00 23.23 C ANISOU 3825 CD2 PHE B 219 2704 2836 3287 96 130 -441 C ATOM 3826 CE1 PHE B 219 16.645 27.667 33.674 1.00 25.00 C ANISOU 3826 CE1 PHE B 219 2995 2985 3518 116 95 -358 C ATOM 3827 CE2 PHE B 219 16.760 27.582 36.057 1.00 24.89 C ANISOU 3827 CE2 PHE B 219 2927 3021 3511 100 147 -452 C ATOM 3828 CZ PHE B 219 17.247 28.053 34.856 1.00 23.23 C ANISOU 3828 CZ PHE B 219 2747 2768 3312 109 132 -409 C ATOM 3829 N PHE B 220 14.139 23.408 37.398 1.00 25.69 N ANISOU 3829 N PHE B 220 2994 3244 3522 43 140 -421 N ATOM 3830 CA PHE B 220 14.586 23.107 38.766 1.00 24.93 C ANISOU 3830 CA PHE B 220 2892 3197 3385 33 182 -436 C ATOM 3831 C PHE B 220 15.317 21.772 38.888 1.00 26.89 C ANISOU 3831 C PHE B 220 3175 3457 3584 16 179 -399 C ATOM 3832 O PHE B 220 16.328 21.685 39.579 1.00 25.02 O ANISOU 3832 O PHE B 220 2954 3248 3305 17 193 -402 O ATOM 3833 CB PHE B 220 13.384 23.134 39.737 1.00 25.99 C ANISOU 3833 CB PHE B 220 2972 3365 3538 26 217 -454 C ATOM 3834 CG PHE B 220 13.665 22.714 41.165 1.00 26.64 C ANISOU 3834 CG PHE B 220 3050 3512 3560 13 262 -459 C ATOM 3835 CD1 PHE B 220 14.571 23.421 41.954 1.00 28.79 C ANISOU 3835 CD1 PHE B 220 3331 3819 3791 22 279 -500 C ATOM 3836 CD2 PHE B 220 12.993 21.641 41.735 1.00 27.56 C ANISOU 3836 CD2 PHE B 220 3151 3658 3662 -10 287 -422 C ATOM 3837 CE1 PHE B 220 14.832 23.032 43.268 1.00 29.36 C ANISOU 3837 CE1 PHE B 220 3401 3963 3789 12 312 -503 C ATOM 3838 CE2 PHE B 220 13.255 21.248 43.052 1.00 29.78 C ANISOU 3838 CE2 PHE B 220 3434 4008 3875 -20 329 -412 C ATOM 3839 CZ PHE B 220 14.155 21.959 43.815 1.00 28.49 C ANISOU 3839 CZ PHE B 220 3282 3888 3653 -7 339 -453 C ATOM 3840 N ILE B 221 14.773 20.730 38.251 1.00 23.82 N ANISOU 3840 N ILE B 221 2794 3047 3212 2 159 -369 N ATOM 3841 CA ILE B 221 15.326 19.388 38.337 1.00 22.98 C ANISOU 3841 CA ILE B 221 2715 2937 3081 -13 158 -334 C ATOM 3842 C ILE B 221 16.630 19.278 37.562 1.00 27.18 C ANISOU 3842 C ILE B 221 3293 3444 3592 0 140 -333 C ATOM 3843 O ILE B 221 17.592 18.742 38.103 1.00 27.06 O ANISOU 3843 O ILE B 221 3293 3440 3549 2 151 -316 O ATOM 3844 CB ILE B 221 14.247 18.346 37.963 1.00 25.08 C ANISOU 3844 CB ILE B 221 2964 3179 3388 -37 146 -314 C ATOM 3845 CG1 ILE B 221 13.257 18.248 39.174 1.00 24.67 C ANISOU 3845 CG1 ILE B 221 2861 3164 3348 -54 188 -303 C ATOM 3846 CG2 ILE B 221 14.861 16.958 37.601 1.00 23.72 C ANISOU 3846 CG2 ILE B 221 2826 2972 3214 -49 134 -286 C ATOM 3847 CD1 ILE B 221 12.021 17.601 38.943 1.00 29.78 C ANISOU 3847 CD1 ILE B 221 3471 3791 4053 -79 184 -291 C ATOM 3848 N VAL B 222 16.688 19.852 36.352 1.00 23.69 N ANISOU 3848 N VAL B 222 2869 2972 3160 12 114 -347 N ATOM 3849 CA VAL B 222 17.856 19.807 35.468 1.00 23.06 C ANISOU 3849 CA VAL B 222 2831 2871 3059 23 107 -346 C ATOM 3850 C VAL B 222 19.012 20.708 35.955 1.00 25.91 C ANISOU 3850 C VAL B 222 3191 3245 3406 36 128 -357 C ATOM 3851 O VAL B 222 20.170 20.291 35.897 1.00 23.95 O ANISOU 3851 O VAL B 222 2962 2994 3143 41 137 -352 O ATOM 3852 CB VAL B 222 17.453 20.095 33.987 1.00 26.18 C ANISOU 3852 CB VAL B 222 3249 3241 3456 29 75 -349 C ATOM 3853 CG1 VAL B 222 18.672 20.270 33.092 1.00 26.00 C ANISOU 3853 CG1 VAL B 222 3268 3206 3404 42 82 -348 C ATOM 3854 CG2 VAL B 222 16.556 18.994 33.433 1.00 25.39 C ANISOU 3854 CG2 VAL B 222 3151 3127 3367 12 44 -351 C ATOM 3855 N THR B 223 18.708 21.935 36.413 1.00 23.99 N ANISOU 3855 N THR B 223 2922 3013 3181 42 137 -379 N ATOM 3856 CA THR B 223 19.744 22.899 36.826 1.00 23.66 C ANISOU 3856 CA THR B 223 2873 2976 3142 50 154 -401 C ATOM 3857 C THR B 223 20.076 22.846 38.324 1.00 26.26 C ANISOU 3857 C THR B 223 3177 3353 3447 45 170 -423 C ATOM 3858 O THR B 223 21.056 23.478 38.748 1.00 24.50 O ANISOU 3858 O THR B 223 2945 3140 3224 47 176 -449 O ATOM 3859 CB THR B 223 19.362 24.332 36.404 1.00 27.69 C ANISOU 3859 CB THR B 223 3368 3457 3695 60 155 -418 C ATOM 3860 OG1 THR B 223 18.242 24.748 37.179 1.00 29.32 O ANISOU 3860 OG1 THR B 223 3537 3679 3924 60 161 -442 O ATOM 3861 CG2 THR B 223 19.024 24.454 34.923 1.00 23.70 C ANISOU 3861 CG2 THR B 223 2891 2916 3199 68 133 -385 C ATOM 3862 N TYR B 224 19.258 22.138 39.133 1.00 21.72 N ANISOU 3862 N TYR B 224 2589 2813 2851 36 176 -412 N ATOM 3863 CA TYR B 224 19.517 22.146 40.563 1.00 21.09 C ANISOU 3863 CA TYR B 224 2490 2793 2730 32 191 -429 C ATOM 3864 C TYR B 224 19.384 20.773 41.246 1.00 26.74 C ANISOU 3864 C TYR B 224 3212 3542 3406 23 195 -379 C ATOM 3865 O TYR B 224 20.386 20.256 41.721 1.00 27.46 O ANISOU 3865 O TYR B 224 3312 3656 3464 27 186 -359 O ATOM 3866 CB TYR B 224 18.648 23.233 41.275 1.00 21.18 C ANISOU 3866 CB TYR B 224 2465 2829 2752 33 214 -481 C ATOM 3867 CG TYR B 224 18.985 23.420 42.738 1.00 21.21 C ANISOU 3867 CG TYR B 224 2453 2907 2698 30 230 -515 C ATOM 3868 CD1 TYR B 224 18.382 22.632 43.719 1.00 22.51 C ANISOU 3868 CD1 TYR B 224 2611 3133 2808 21 252 -489 C ATOM 3869 CD2 TYR B 224 19.945 24.352 43.143 1.00 20.13 C ANISOU 3869 CD2 TYR B 224 2307 2784 2559 35 224 -573 C ATOM 3870 CE1 TYR B 224 18.759 22.730 45.059 1.00 22.95 C ANISOU 3870 CE1 TYR B 224 2660 3273 2788 19 264 -514 C ATOM 3871 CE2 TYR B 224 20.302 24.486 44.490 1.00 20.08 C ANISOU 3871 CE2 TYR B 224 2287 2857 2485 31 229 -613 C ATOM 3872 CZ TYR B 224 19.715 23.663 45.440 1.00 27.33 C ANISOU 3872 CZ TYR B 224 3206 3847 3330 26 248 -581 C ATOM 3873 OH TYR B 224 20.080 23.765 46.758 1.00 28.23 O ANISOU 3873 OH TYR B 224 3314 4055 3359 24 251 -614 O ATOM 3874 N LEU B 225 18.175 20.218 41.357 1.00 24.41 N ANISOU 3874 N LEU B 225 2905 3248 3120 10 209 -355 N ATOM 3875 CA LEU B 225 17.929 19.031 42.171 1.00 24.25 C ANISOU 3875 CA LEU B 225 2885 3259 3070 -3 224 -301 C ATOM 3876 C LEU B 225 18.655 17.766 41.737 1.00 26.99 C ANISOU 3876 C LEU B 225 3260 3568 3427 -2 203 -248 C ATOM 3877 O LEU B 225 19.337 17.179 42.589 1.00 26.46 O ANISOU 3877 O LEU B 225 3199 3536 3320 3 204 -209 O ATOM 3878 CB LEU B 225 16.431 18.761 42.340 1.00 24.52 C ANISOU 3878 CB LEU B 225 2891 3295 3130 -22 250 -288 C ATOM 3879 CG LEU B 225 16.040 17.738 43.423 1.00 30.14 C ANISOU 3879 CG LEU B 225 3594 4049 3808 -40 282 -228 C ATOM 3880 CD1 LEU B 225 16.413 18.230 44.821 1.00 30.79 C ANISOU 3880 CD1 LEU B 225 3671 4224 3805 -33 308 -240 C ATOM 3881 CD2 LEU B 225 14.562 17.479 43.393 1.00 34.06 C ANISOU 3881 CD2 LEU B 225 4055 4536 4352 -62 311 -217 C ATOM 3882 N ALA B 226 18.486 17.307 40.464 1.00 22.58 N ANISOU 3882 N ALA B 226 2718 2942 2919 -5 185 -246 N ATOM 3883 CA ALA B 226 19.153 16.083 40.005 1.00 21.17 C ANISOU 3883 CA ALA B 226 2563 2719 2762 -2 171 -210 C ATOM 3884 C ALA B 226 20.698 16.195 40.019 1.00 25.23 C ANISOU 3884 C ALA B 226 3092 3239 3257 22 160 -213 C ATOM 3885 O ALA B 226 21.311 15.330 40.647 1.00 25.55 O ANISOU 3885 O ALA B 226 3133 3285 3290 29 157 -167 O ATOM 3886 CB ALA B 226 18.626 15.632 38.650 1.00 21.58 C ANISOU 3886 CB ALA B 226 2630 2707 2863 -11 154 -226 C ATOM 3887 N PRO B 227 21.370 17.251 39.464 1.00 21.63 N ANISOU 3887 N PRO B 227 2639 2782 2796 34 154 -259 N ATOM 3888 CA PRO B 227 22.844 17.268 39.537 1.00 21.16 C ANISOU 3888 CA PRO B 227 2581 2727 2732 54 146 -260 C ATOM 3889 C PRO B 227 23.396 17.358 40.950 1.00 26.38 C ANISOU 3889 C PRO B 227 3220 3452 3349 60 139 -245 C ATOM 3890 O PRO B 227 24.351 16.658 41.233 1.00 27.62 O ANISOU 3890 O PRO B 227 3374 3611 3508 75 124 -213 O ATOM 3891 CB PRO B 227 23.264 18.449 38.658 1.00 22.80 C ANISOU 3891 CB PRO B 227 2792 2918 2952 58 149 -308 C ATOM 3892 CG PRO B 227 22.065 19.236 38.413 1.00 27.07 C ANISOU 3892 CG PRO B 227 3330 3459 3496 46 154 -329 C ATOM 3893 CD PRO B 227 20.858 18.391 38.668 1.00 22.92 C ANISOU 3893 CD PRO B 227 2803 2932 2972 32 154 -303 C ATOM 3894 N LEU B 228 22.775 18.144 41.844 1.00 23.50 N ANISOU 3894 N LEU B 228 2839 3144 2945 50 147 -267 N ATOM 3895 CA LEU B 228 23.257 18.291 43.229 1.00 23.74 C ANISOU 3895 CA LEU B 228 2852 3253 2913 54 137 -263 C ATOM 3896 C LEU B 228 22.996 17.050 44.096 1.00 27.99 C ANISOU 3896 C LEU B 228 3396 3822 3416 54 138 -183 C ATOM 3897 O LEU B 228 23.865 16.701 44.898 1.00 29.13 O ANISOU 3897 O LEU B 228 3535 4013 3521 68 113 -151 O ATOM 3898 CB LEU B 228 22.758 19.579 43.908 1.00 23.51 C ANISOU 3898 CB LEU B 228 2805 3278 2851 45 151 -328 C ATOM 3899 CG LEU B 228 23.330 20.867 43.306 1.00 28.12 C ANISOU 3899 CG LEU B 228 3376 3833 3475 48 145 -400 C ATOM 3900 CD1 LEU B 228 22.522 22.039 43.709 1.00 28.13 C ANISOU 3900 CD1 LEU B 228 3359 3856 3472 39 166 -465 C ATOM 3901 CD2 LEU B 228 24.814 21.065 43.689 1.00 29.38 C ANISOU 3901 CD2 LEU B 228 3519 4018 3625 57 115 -419 C ATOM 3902 N GLY B 229 21.859 16.380 43.891 1.00 22.07 N ANISOU 3902 N GLY B 229 2654 3042 2688 37 162 -146 N ATOM 3903 CA GLY B 229 21.548 15.112 44.546 1.00 21.61 C ANISOU 3903 CA GLY B 229 2600 2990 2619 32 171 -58 C ATOM 3904 C GLY B 229 22.531 14.040 44.117 1.00 27.19 C ANISOU 3904 C GLY B 229 3318 3639 3373 52 145 -8 C ATOM 3905 O GLY B 229 23.078 13.333 44.966 1.00 28.33 O ANISOU 3905 O GLY B 229 3460 3813 3489 66 131 62 O ATOM 3906 N LEU B 230 22.829 13.957 42.798 1.00 23.74 N ANISOU 3906 N LEU B 230 2892 3124 3005 57 139 -45 N ATOM 3907 CA LEU B 230 23.828 13.018 42.248 1.00 23.48 C ANISOU 3907 CA LEU B 230 2865 3029 3028 80 122 -19 C ATOM 3908 C LEU B 230 25.255 13.340 42.746 1.00 26.86 C ANISOU 3908 C LEU B 230 3276 3499 3432 109 93 -19 C ATOM 3909 O LEU B 230 25.985 12.418 43.122 1.00 25.98 O ANISOU 3909 O LEU B 230 3156 3373 3341 132 74 42 O ATOM 3910 CB LEU B 230 23.786 12.951 40.698 1.00 23.22 C ANISOU 3910 CB LEU B 230 2849 2917 3057 78 129 -73 C ATOM 3911 CG LEU B 230 22.536 12.287 40.080 1.00 26.92 C ANISOU 3911 CG LEU B 230 3329 3329 3569 52 142 -71 C ATOM 3912 CD1 LEU B 230 22.347 12.728 38.655 1.00 26.10 C ANISOU 3912 CD1 LEU B 230 3244 3188 3487 47 142 -141 C ATOM 3913 CD2 LEU B 230 22.565 10.753 40.216 1.00 25.61 C ANISOU 3913 CD2 LEU B 230 3164 3099 3466 53 143 -9 C ATOM 3914 N MET B 231 25.635 14.641 42.784 1.00 22.96 N ANISOU 3914 N MET B 231 2769 3052 2902 108 87 -86 N ATOM 3915 CA MET B 231 26.959 15.074 43.277 1.00 22.85 C ANISOU 3915 CA MET B 231 2729 3081 2871 130 55 -100 C ATOM 3916 C MET B 231 27.135 14.741 44.756 1.00 29.74 C ANISOU 3916 C MET B 231 3589 4037 3674 138 25 -42 C ATOM 3917 O MET B 231 28.214 14.282 45.123 1.00 30.87 O ANISOU 3917 O MET B 231 3712 4193 3825 165 -12 -7 O ATOM 3918 CB MET B 231 27.214 16.570 43.054 1.00 24.35 C ANISOU 3918 CB MET B 231 2905 3298 3050 119 57 -186 C ATOM 3919 CG MET B 231 27.501 16.924 41.631 1.00 27.97 C ANISOU 3919 CG MET B 231 3370 3684 3571 119 79 -229 C ATOM 3920 SD MET B 231 27.845 18.694 41.513 1.00 32.37 S ANISOU 3920 SD MET B 231 3906 4264 4130 105 84 -312 S ATOM 3921 CE MET B 231 26.426 19.277 40.655 1.00 28.30 C ANISOU 3921 CE MET B 231 3421 3711 3621 85 117 -335 C ATOM 3922 N ALA B 232 26.081 14.955 45.595 1.00 26.70 N ANISOU 3922 N ALA B 232 3215 3712 3218 118 42 -30 N ATOM 3923 CA ALA B 232 26.099 14.663 47.041 1.00 26.71 C ANISOU 3923 CA ALA B 232 3212 3809 3127 124 23 29 C ATOM 3924 C ALA B 232 26.435 13.192 47.279 1.00 30.21 C ANISOU 3924 C ALA B 232 3661 4220 3599 145 6 146 C ATOM 3925 O ALA B 232 27.314 12.891 48.085 1.00 30.03 O ANISOU 3925 O ALA B 232 3623 4252 3537 171 -40 195 O ATOM 3926 CB ALA B 232 24.756 15.002 47.679 1.00 27.21 C ANISOU 3926 CB ALA B 232 3287 3926 3123 96 65 25 C ATOM 3927 N MET B 233 25.775 12.292 46.520 1.00 26.24 N ANISOU 3927 N MET B 233 3174 3622 3174 136 39 185 N ATOM 3928 CA MET B 233 25.976 10.843 46.560 1.00 25.51 C ANISOU 3928 CA MET B 233 3086 3466 3142 153 32 290 C ATOM 3929 C MET B 233 27.371 10.446 46.073 1.00 30.94 C ANISOU 3929 C MET B 233 3752 4103 3900 193 -7 291 C ATOM 3930 O MET B 233 28.006 9.588 46.689 1.00 32.80 O ANISOU 3930 O MET B 233 3977 4341 4146 223 -39 382 O ATOM 3931 CB MET B 233 24.864 10.119 45.795 1.00 27.18 C ANISOU 3931 CB MET B 233 3314 3583 3431 126 77 304 C ATOM 3932 CG MET B 233 23.508 10.285 46.463 1.00 30.72 C ANISOU 3932 CG MET B 233 3770 4081 3822 89 118 328 C ATOM 3933 SD MET B 233 22.166 9.348 45.699 1.00 35.32 S ANISOU 3933 SD MET B 233 4358 4554 4507 52 163 350 S ATOM 3934 CE MET B 233 21.766 10.359 44.329 1.00 31.81 C ANISOU 3934 CE MET B 233 3917 4075 4095 38 167 213 C ATOM 3935 N ALA B 234 27.868 11.087 45.006 1.00 25.92 N ANISOU 3935 N ALA B 234 3109 3427 3311 196 -2 196 N ATOM 3936 CA ALA B 234 29.208 10.836 44.457 1.00 24.65 C ANISOU 3936 CA ALA B 234 2921 3222 3223 232 -27 181 C ATOM 3937 C ALA B 234 30.271 11.178 45.508 1.00 29.02 C ANISOU 3937 C ALA B 234 3438 3864 3723 258 -84 204 C ATOM 3938 O ALA B 234 31.142 10.353 45.789 1.00 28.62 O ANISOU 3938 O ALA B 234 3362 3795 3717 296 -120 270 O ATOM 3939 CB ALA B 234 29.428 11.686 43.205 1.00 25.44 C ANISOU 3939 CB ALA B 234 3022 3285 3360 221 0 74 C ATOM 3940 N TYR B 235 30.172 12.386 46.115 1.00 25.91 N ANISOU 3940 N TYR B 235 3039 3568 3238 238 -97 147 N ATOM 3941 CA TYR B 235 31.103 12.870 47.131 1.00 25.17 C ANISOU 3941 CA TYR B 235 2910 3573 3082 255 -159 145 C ATOM 3942 C TYR B 235 31.025 12.092 48.424 1.00 31.62 C ANISOU 3942 C TYR B 235 3731 4461 3822 273 -198 258 C ATOM 3943 O TYR B 235 32.047 11.942 49.086 1.00 30.85 O ANISOU 3943 O TYR B 235 3598 4416 3707 304 -264 291 O ATOM 3944 CB TYR B 235 30.946 14.377 47.353 1.00 25.70 C ANISOU 3944 CB TYR B 235 2969 3711 3082 226 -158 38 C ATOM 3945 CG TYR B 235 31.629 15.160 46.255 1.00 25.25 C ANISOU 3945 CG TYR B 235 2887 3596 3109 221 -143 -53 C ATOM 3946 CD1 TYR B 235 33.012 15.099 46.083 1.00 25.79 C ANISOU 3946 CD1 TYR B 235 2905 3655 3240 247 -181 -62 C ATOM 3947 CD2 TYR B 235 30.895 15.941 45.371 1.00 25.17 C ANISOU 3947 CD2 TYR B 235 2901 3542 3120 191 -89 -123 C ATOM 3948 CE1 TYR B 235 33.644 15.792 45.060 1.00 25.90 C ANISOU 3948 CE1 TYR B 235 2893 3614 3333 240 -155 -138 C ATOM 3949 CE2 TYR B 235 31.517 16.632 44.336 1.00 25.99 C ANISOU 3949 CE2 TYR B 235 2986 3593 3297 186 -69 -190 C ATOM 3950 CZ TYR B 235 32.894 16.555 44.187 1.00 33.03 C ANISOU 3950 CZ TYR B 235 3828 4475 4247 209 -97 -197 C ATOM 3951 OH TYR B 235 33.538 17.232 43.186 1.00 34.84 O ANISOU 3951 OH TYR B 235 4035 4655 4548 201 -67 -257 O ATOM 3952 N PHE B 236 29.844 11.538 48.764 1.00 31.32 N ANISOU 3952 N PHE B 236 3733 4422 3746 254 -160 325 N ATOM 3953 CA PHE B 236 29.723 10.681 49.940 1.00 32.47 C ANISOU 3953 CA PHE B 236 3888 4627 3822 270 -186 454 C ATOM 3954 C PHE B 236 30.548 9.381 49.715 1.00 35.40 C ANISOU 3954 C PHE B 236 4239 4912 4299 315 -217 556 C ATOM 3955 O PHE B 236 31.225 8.917 50.634 1.00 36.98 O ANISOU 3955 O PHE B 236 4422 5171 4458 350 -278 648 O ATOM 3956 CB PHE B 236 28.254 10.381 50.265 1.00 35.62 C ANISOU 3956 CB PHE B 236 4327 5033 4174 235 -123 503 C ATOM 3957 CG PHE B 236 28.098 9.436 51.431 1.00 39.47 C ANISOU 3957 CG PHE B 236 4828 5575 4594 249 -138 655 C ATOM 3958 CD1 PHE B 236 28.131 9.908 52.737 1.00 44.41 C ANISOU 3958 CD1 PHE B 236 5459 6355 5059 250 -167 679 C ATOM 3959 CD2 PHE B 236 27.949 8.063 51.224 1.00 42.99 C ANISOU 3959 CD2 PHE B 236 5280 5917 5137 261 -122 776 C ATOM 3960 CE1 PHE B 236 28.008 9.026 53.816 1.00 46.04 C ANISOU 3960 CE1 PHE B 236 5681 6620 5191 264 -179 835 C ATOM 3961 CE2 PHE B 236 27.838 7.182 52.303 1.00 46.06 C ANISOU 3961 CE2 PHE B 236 5680 6350 5470 275 -134 934 C ATOM 3962 CZ PHE B 236 27.856 7.670 53.590 1.00 44.71 C ANISOU 3962 CZ PHE B 236 5520 6342 5127 276 -161 969 C ATOM 3963 N GLN B 237 30.519 8.829 48.493 1.00 28.82 N ANISOU 3963 N GLN B 237 3407 3942 3602 318 -180 535 N ATOM 3964 CA GLN B 237 31.287 7.645 48.131 1.00 27.89 C ANISOU 3964 CA GLN B 237 3265 3724 3608 362 -199 607 C ATOM 3965 C GLN B 237 32.785 7.939 48.047 1.00 32.46 C ANISOU 3965 C GLN B 237 3789 4320 4225 405 -257 571 C ATOM 3966 O GLN B 237 33.587 7.092 48.441 1.00 33.46 O ANISOU 3966 O GLN B 237 3884 4427 4403 452 -305 663 O ATOM 3967 CB GLN B 237 30.772 7.030 46.830 1.00 28.94 C ANISOU 3967 CB GLN B 237 3417 3714 3867 349 -137 570 C ATOM 3968 CG GLN B 237 29.377 6.434 46.967 1.00 27.86 C ANISOU 3968 CG GLN B 237 3320 3542 3725 311 -89 628 C ATOM 3969 CD GLN B 237 29.137 5.352 45.940 1.00 45.57 C ANISOU 3969 CD GLN B 237 5569 5630 6116 313 -53 632 C ATOM 3970 OE1 GLN B 237 29.641 5.378 44.799 1.00 34.12 O ANISOU 3970 OE1 GLN B 237 4108 4105 4749 325 -40 542 O ATOM 3971 NE2 GLN B 237 28.339 4.377 46.327 1.00 35.70 N ANISOU 3971 NE2 GLN B 237 4333 4329 4900 299 -31 734 N ATOM 3972 N ILE B 238 33.169 9.128 47.533 1.00 28.24 N ANISOU 3972 N ILE B 238 3236 3816 3676 388 -253 443 N ATOM 3973 CA ILE B 238 34.571 9.562 47.471 1.00 27.81 C ANISOU 3973 CA ILE B 238 3119 3786 3660 419 -303 397 C ATOM 3974 C ILE B 238 35.082 9.701 48.924 1.00 36.99 C ANISOU 3974 C ILE B 238 4256 5079 4719 439 -391 460 C ATOM 3975 O ILE B 238 36.164 9.197 49.242 1.00 37.22 O ANISOU 3975 O ILE B 238 4233 5111 4798 487 -454 514 O ATOM 3976 CB ILE B 238 34.748 10.862 46.641 1.00 28.90 C ANISOU 3976 CB ILE B 238 3248 3928 3805 387 -271 255 C ATOM 3977 CG1 ILE B 238 34.526 10.607 45.137 1.00 27.99 C ANISOU 3977 CG1 ILE B 238 3151 3691 3794 380 -197 202 C ATOM 3978 CG2 ILE B 238 36.122 11.518 46.894 1.00 27.75 C ANISOU 3978 CG2 ILE B 238 3031 3838 3677 407 -330 206 C ATOM 3979 CD1 ILE B 238 34.065 11.877 44.349 1.00 27.97 C ANISOU 3979 CD1 ILE B 238 3169 3693 3766 335 -147 88 C ATOM 3980 N PHE B 239 34.259 10.324 49.807 1.00 36.83 N ANISOU 3980 N PHE B 239 4273 5167 4554 404 -393 454 N ATOM 3981 CA PHE B 239 34.555 10.510 51.228 1.00 37.64 C ANISOU 3981 CA PHE B 239 4364 5413 4523 416 -470 503 C ATOM 3982 C PHE B 239 34.847 9.178 51.901 1.00 41.94 C ANISOU 3982 C PHE B 239 4904 5953 5076 463 -517 671 C ATOM 3983 O PHE B 239 35.854 9.073 52.600 1.00 42.25 O ANISOU 3983 O PHE B 239 4899 6063 5092 503 -607 714 O ATOM 3984 CB PHE B 239 33.428 11.267 51.963 1.00 39.56 C ANISOU 3984 CB PHE B 239 4657 5761 4613 370 -441 468 C ATOM 3985 CG PHE B 239 33.525 11.177 53.469 1.00 42.24 C ANISOU 3985 CG PHE B 239 5002 6252 4796 383 -507 545 C ATOM 3986 CD1 PHE B 239 34.422 11.972 54.174 1.00 45.79 C ANISOU 3986 CD1 PHE B 239 5410 6820 5167 392 -591 479 C ATOM 3987 CD2 PHE B 239 32.733 10.280 54.184 1.00 45.69 C ANISOU 3987 CD2 PHE B 239 5483 6714 5161 386 -487 684 C ATOM 3988 CE1 PHE B 239 34.537 11.863 55.563 1.00 46.69 C ANISOU 3988 CE1 PHE B 239 5533 7088 5120 406 -661 549 C ATOM 3989 CE2 PHE B 239 32.843 10.183 55.575 1.00 48.61 C ANISOU 3989 CE2 PHE B 239 5864 7236 5370 401 -546 765 C ATOM 3990 CZ PHE B 239 33.743 10.979 56.253 1.00 46.28 C ANISOU 3990 CZ PHE B 239 5532 7069 4984 412 -636 694 C ATOM 3991 N ARG B 240 33.974 8.166 51.690 1.00 37.09 N ANISOU 3991 N ARG B 240 4334 5253 4506 460 -459 766 N ATOM 3992 CA ARG B 240 34.145 6.832 52.260 1.00 36.31 C ANISOU 3992 CA ARG B 240 4234 5123 4438 503 -491 938 C ATOM 3993 C ARG B 240 35.416 6.165 51.771 1.00 41.71 C ANISOU 3993 C ARG B 240 4855 5717 5275 563 -539 966 C ATOM 3994 O ARG B 240 36.095 5.515 52.564 1.00 43.13 O ANISOU 3994 O ARG B 240 5007 5932 5449 612 -615 1088 O ATOM 3995 CB ARG B 240 32.919 5.943 52.003 1.00 36.33 C ANISOU 3995 CB ARG B 240 4288 5028 4486 478 -409 1016 C ATOM 3996 CG ARG B 240 31.723 6.351 52.870 1.00 47.15 C ANISOU 3996 CG ARG B 240 5711 6507 5696 433 -373 1050 C ATOM 3997 CD ARG B 240 30.812 5.202 53.284 1.00 69.00 C ANISOU 3997 CD ARG B 240 8513 9211 8493 425 -325 1203 C ATOM 3998 NE ARG B 240 31.468 4.122 54.026 1.00 86.36 N ANISOU 3998 NE ARG B 240 10697 11402 10715 478 -384 1380 N ATOM 3999 CZ ARG B 240 31.627 2.888 53.557 1.00100.02 C ANISOU 3999 CZ ARG B 240 12416 12977 12609 504 -370 1477 C ATOM 4000 NH1 ARG B 240 31.168 2.562 52.353 1.00 87.00 N ANISOU 4000 NH1 ARG B 240 10773 11176 11106 479 -300 1405 N ATOM 4001 NH2 ARG B 240 32.240 1.968 54.290 1.00 80.41 N ANISOU 4001 NH2 ARG B 240 9916 10489 10148 557 -428 1646 N ATOM 4002 N LYS B 241 35.766 6.354 50.484 1.00 37.10 N ANISOU 4002 N LYS B 241 4247 5025 4824 561 -496 854 N ATOM 4003 CA LYS B 241 36.959 5.768 49.888 1.00 35.99 C ANISOU 4003 CA LYS B 241 4042 4793 4841 616 -524 859 C ATOM 4004 C LYS B 241 38.244 6.449 50.396 1.00 41.64 C ANISOU 4004 C LYS B 241 4684 5609 5530 646 -616 823 C ATOM 4005 O LYS B 241 39.165 5.760 50.799 1.00 41.39 O ANISOU 4005 O LYS B 241 4596 5568 5560 706 -687 913 O ATOM 4006 CB LYS B 241 36.871 5.810 48.350 1.00 37.91 C ANISOU 4006 CB LYS B 241 4287 4904 5214 601 -438 743 C ATOM 4007 CG LYS B 241 37.912 4.960 47.629 1.00 52.04 C ANISOU 4007 CG LYS B 241 6016 6572 7183 659 -440 754 C ATOM 4008 CD LYS B 241 37.442 3.526 47.489 1.00 66.81 C ANISOU 4008 CD LYS B 241 7911 8315 9158 683 -411 859 C ATOM 4009 CE LYS B 241 38.320 2.718 46.590 1.00 79.76 C ANISOU 4009 CE LYS B 241 9496 9820 10987 738 -395 842 C ATOM 4010 NZ LYS B 241 37.812 1.326 46.472 1.00 94.49 N ANISOU 4010 NZ LYS B 241 11385 11547 12969 758 -364 934 N ATOM 4011 N LEU B 242 38.303 7.788 50.381 1.00 38.90 N ANISOU 4011 N LEU B 242 4330 5350 5100 605 -619 694 N ATOM 4012 CA LEU B 242 39.492 8.539 50.796 1.00 38.46 C ANISOU 4012 CA LEU B 242 4198 5385 5030 622 -703 637 C ATOM 4013 C LEU B 242 39.753 8.532 52.294 1.00 45.84 C ANISOU 4013 C LEU B 242 5122 6470 5826 643 -813 724 C ATOM 4014 O LEU B 242 40.914 8.515 52.703 1.00 46.48 O ANISOU 4014 O LEU B 242 5126 6597 5939 685 -907 741 O ATOM 4015 CB LEU B 242 39.440 9.987 50.279 1.00 37.57 C ANISOU 4015 CB LEU B 242 4081 5304 4888 567 -666 470 C ATOM 4016 CG LEU B 242 39.537 10.214 48.767 1.00 39.97 C ANISOU 4016 CG LEU B 242 4377 5482 5326 551 -573 373 C ATOM 4017 CD1 LEU B 242 39.536 11.675 48.475 1.00 39.22 C ANISOU 4017 CD1 LEU B 242 4277 5432 5193 499 -549 233 C ATOM 4018 CD2 LEU B 242 40.795 9.559 48.159 1.00 39.61 C ANISOU 4018 CD2 LEU B 242 4250 5354 5445 607 -588 386 C ATOM 4019 N TRP B 243 38.690 8.568 53.108 1.00 43.82 N ANISOU 4019 N TRP B 243 4939 6297 5413 613 -802 775 N ATOM 4020 CA TRP B 243 38.786 8.591 54.568 1.00 44.13 C ANISOU 4020 CA TRP B 243 4983 6499 5286 628 -897 857 C ATOM 4021 C TRP B 243 38.490 7.228 55.223 1.00 52.88 C ANISOU 4021 C TRP B 243 6120 7592 6378 670 -917 1062 C ATOM 4022 O TRP B 243 38.390 7.145 56.448 1.00 52.96 O ANISOU 4022 O TRP B 243 6149 7741 6233 682 -985 1155 O ATOM 4023 CB TRP B 243 37.918 9.714 55.149 1.00 41.85 C ANISOU 4023 CB TRP B 243 4747 6338 4817 567 -874 765 C ATOM 4024 CG TRP B 243 38.542 11.069 54.981 1.00 42.07 C ANISOU 4024 CG TRP B 243 4725 6420 4838 539 -904 589 C ATOM 4025 CD1 TRP B 243 39.444 11.661 55.817 1.00 44.81 C ANISOU 4025 CD1 TRP B 243 5017 6899 5110 550 -1015 544 C ATOM 4026 CD2 TRP B 243 38.349 11.984 53.886 1.00 41.57 C ANISOU 4026 CD2 TRP B 243 4659 6276 4860 495 -824 437 C ATOM 4027 NE1 TRP B 243 39.810 12.896 55.326 1.00 44.17 N ANISOU 4027 NE1 TRP B 243 4896 6815 5073 512 -1005 370 N ATOM 4028 CE2 TRP B 243 39.153 13.121 54.141 1.00 45.44 C ANISOU 4028 CE2 TRP B 243 5089 6845 5330 478 -886 308 C ATOM 4029 CE3 TRP B 243 37.580 11.954 52.709 1.00 42.22 C ANISOU 4029 CE3 TRP B 243 4782 6227 5034 467 -710 400 C ATOM 4030 CZ2 TRP B 243 39.202 14.221 53.266 1.00 44.07 C ANISOU 4030 CZ2 TRP B 243 4898 6617 5232 435 -830 156 C ATOM 4031 CZ3 TRP B 243 37.632 13.039 51.845 1.00 43.35 C ANISOU 4031 CZ3 TRP B 243 4910 6327 5235 429 -661 253 C ATOM 4032 CH2 TRP B 243 38.435 14.156 52.125 1.00 43.90 C ANISOU 4032 CH2 TRP B 243 4921 6469 5290 413 -717 138 C ATOM 4033 N GLY B 244 38.425 6.173 54.409 1.00 52.82 N ANISOU 4033 N GLY B 244 6114 7417 6537 695 -861 1131 N ATOM 4034 CA GLY B 244 38.242 4.795 54.866 1.00 54.29 C ANISOU 4034 CA GLY B 244 6319 7550 6760 738 -874 1329 C ATOM 4035 C GLY B 244 39.555 4.108 55.214 1.00 63.14 C ANISOU 4035 C GLY B 244 7359 8664 7967 819 -984 1429 C ATOM 4036 O GLY B 244 40.573 4.782 55.415 1.00 62.98 O ANISOU 4036 O GLY B 244 7275 8739 7917 837 -1073 1362 O ATOM 4037 N ARG B 245 39.550 2.754 55.263 1.00 62.27 N ANISOU 4037 N ARG B 245 7245 8430 7984 868 -978 1585 N ATOM 4038 CA ARG B 245 40.709 1.900 55.582 1.00102.25 C ANISOU 4038 CA ARG B 245 12230 13458 13161 954 -1077 1704 C ATOM 4039 C ARG B 245 41.939 2.156 54.698 1.00121.66 C ANISOU 4039 C ARG B 245 14591 15847 15786 986 -1097 1574 C ATOM 4040 O ARG B 245 41.858 2.081 53.475 1.00 81.14 O ANISOU 4040 O ARG B 245 9457 10577 10797 970 -1001 1468 O ATOM 4041 CB ARG B 245 40.322 0.413 55.529 1.00103.38 C ANISOU 4041 CB ARG B 245 12393 13447 13438 993 -1042 1881 C ATOM 4042 CG ARG B 245 39.492 -0.055 56.716 1.00114.74 C ANISOU 4042 CG ARG B 245 13898 14974 14725 990 -1064 2076 C ATOM 4043 CD ARG B 245 39.091 -1.506 56.559 1.00125.72 C ANISOU 4043 CD ARG B 245 15311 16185 16272 1013 -1006 2235 C ATOM 4044 NE ARG B 245 38.248 -1.957 57.665 1.00136.20 N ANISOU 4044 NE ARG B 245 16703 17592 17456 1004 -1013 2434 N ATOM 4045 CZ ARG B 245 36.950 -2.227 57.563 1.00153.04 C ANISOU 4045 CZ ARG B 245 18910 19679 19560 944 -907 2477 C ATOM 4046 NH1 ARG B 245 36.330 -2.109 56.394 1.00141.08 N ANISOU 4046 NH1 ARG B 245 17417 18039 18150 890 -796 2334 N ATOM 4047 NH2 ARG B 245 36.265 -2.627 58.625 1.00141.58 N ANISOU 4047 NH2 ARG B 245 17510 18310 17975 938 -912 2668 N ATOM 4048 N PRO B 248 49.109 1.743 53.423 1.00 82.02 N ANISOU 4048 N PRO B 248 8933 10700 11529 1315 -1468 1461 N ATOM 4049 CA PRO B 248 50.316 0.957 53.134 1.00 81.72 C ANISOU 4049 CA PRO B 248 8766 10563 11722 1409 -1514 1509 C ATOM 4050 C PRO B 248 51.570 1.836 53.092 1.00 84.68 C ANISOU 4050 C PRO B 248 9006 11019 12148 1417 -1587 1388 C ATOM 4051 O PRO B 248 52.039 2.229 52.015 1.00 84.07 O ANISOU 4051 O PRO B 248 8872 10862 12208 1401 -1496 1240 O ATOM 4052 CB PRO B 248 49.992 0.294 51.787 1.00 83.64 C ANISOU 4052 CB PRO B 248 9032 10595 12151 1413 -1356 1454 C ATOM 4053 CG PRO B 248 48.922 1.188 51.153 1.00 88.22 C ANISOU 4053 CG PRO B 248 9723 11192 12604 1308 -1233 1312 C ATOM 4054 CD PRO B 248 48.425 2.172 52.188 1.00 83.54 C ANISOU 4054 CD PRO B 248 9187 10795 11759 1248 -1306 1308 C ATOM 4055 N GLY B 249 52.082 2.153 54.281 1.00 80.59 N ANISOU 4055 N GLY B 249 8441 10667 11513 1437 -1750 1452 N ATOM 4056 CA GLY B 249 53.261 2.994 54.464 1.00 80.07 C ANISOU 4056 CA GLY B 249 8240 10701 11481 1440 -1847 1349 C ATOM 4057 C GLY B 249 52.904 4.462 54.363 1.00 83.37 C ANISOU 4057 C GLY B 249 8693 11230 11754 1337 -1815 1167 C ATOM 4058 O GLY B 249 51.755 4.844 54.619 1.00 83.26 O ANISOU 4058 O GLY B 249 8811 11266 11557 1269 -1760 1149 O ATOM 4059 N THR B 250 53.893 5.299 54.001 1.00 79.15 N ANISOU 4059 N THR B 250 8032 10731 11311 1325 -1849 1033 N ATOM 4060 CA THR B 250 53.743 6.750 53.841 1.00 78.23 C ANISOU 4060 CA THR B 250 7923 10705 11096 1229 -1824 852 C ATOM 4061 C THR B 250 54.605 7.371 52.741 1.00 80.23 C ANISOU 4061 C THR B 250 8072 10867 11545 1206 -1731 696 C ATOM 4062 O THR B 250 54.248 8.424 52.201 1.00 80.08 O ANISOU 4062 O THR B 250 8097 10851 11479 1122 -1636 555 O ATOM 4063 CB THR B 250 53.987 7.546 55.139 1.00 84.93 C ANISOU 4063 CB THR B 250 8734 11760 11777 1214 -2001 843 C ATOM 4064 OG1 THR B 250 55.312 7.310 55.631 1.00 83.21 O ANISOU 4064 OG1 THR B 250 8397 11584 11635 1305 -2160 961 O ATOM 4065 CG2 THR B 250 52.942 7.256 56.208 1.00 83.56 C ANISOU 4065 CG2 THR B 250 8710 11706 11331 1170 -2021 891 C ATOM 4066 N THR B 251 55.743 6.715 52.418 1.00 74.26 N ANISOU 4066 N THR B 251 7175 10030 11009 1283 -1754 725 N ATOM 4067 CA THR B 251 56.694 7.203 51.414 1.00 72.83 C ANISOU 4067 CA THR B 251 6878 9769 11026 1269 -1665 588 C ATOM 4068 C THR B 251 56.193 6.819 49.999 1.00 73.93 C ANISOU 4068 C THR B 251 7082 9737 11272 1259 -1460 544 C ATOM 4069 O THR B 251 56.576 7.485 49.031 1.00 73.36 O ANISOU 4069 O THR B 251 6959 9615 11299 1218 -1352 412 O ATOM 4070 CB THR B 251 58.166 6.804 51.675 1.00 77.33 C ANISOU 4070 CB THR B 251 7253 10342 11785 1351 -1781 622 C ATOM 4071 OG1 THR B 251 58.303 5.385 51.752 1.00 76.83 O ANISOU 4071 OG1 THR B 251 7175 10184 11833 1455 -1801 776 O ATOM 4072 CG2 THR B 251 58.728 7.433 52.944 1.00 75.24 C ANISOU 4072 CG2 THR B 251 6912 10260 11415 1345 -1983 625 C ATOM 4073 N SER B 252 55.316 5.793 49.879 1.00 68.21 N ANISOU 4073 N SER B 252 6470 8926 10520 1292 -1407 650 N ATOM 4074 CA SER B 252 54.785 5.354 48.578 1.00 67.03 C ANISOU 4074 CA SER B 252 6388 8620 10461 1284 -1224 604 C ATOM 4075 C SER B 252 53.983 6.450 47.839 1.00 66.47 C ANISOU 4075 C SER B 252 6414 8560 10282 1179 -1098 467 C ATOM 4076 O SER B 252 53.393 7.326 48.484 1.00 64.56 O ANISOU 4076 O SER B 252 6239 8434 9859 1114 -1146 442 O ATOM 4077 CB SER B 252 53.976 4.064 48.714 1.00 71.23 C ANISOU 4077 CB SER B 252 7016 9063 10986 1333 -1209 744 C ATOM 4078 OG SER B 252 52.774 4.247 49.445 1.00 79.98 O ANISOU 4078 OG SER B 252 8267 10247 11874 1282 -1232 799 O ATOM 4079 N ALA B 253 54.007 6.411 46.486 1.00 60.68 N ANISOU 4079 N ALA B 253 5685 7708 9662 1167 -939 378 N ATOM 4080 CA ALA B 253 53.318 7.375 45.622 1.00 59.65 C ANISOU 4080 CA ALA B 253 5641 7573 9451 1077 -811 257 C ATOM 4081 C ALA B 253 51.782 7.379 45.839 1.00 62.62 C ANISOU 4081 C ALA B 253 6189 7964 9638 1029 -785 293 C ATOM 4082 O ALA B 253 51.149 8.430 45.726 1.00 61.72 O ANISOU 4082 O ALA B 253 6144 7904 9402 949 -746 216 O ATOM 4083 CB ALA B 253 53.649 7.100 44.162 1.00 60.00 C ANISOU 4083 CB ALA B 253 5658 7490 9647 1088 -651 177 C ATOM 4084 N GLU B 286 51.258 6.209 46.215 1.00 58.13 N ANISOU 4084 N GLU B 286 5682 7346 9060 1078 -811 414 N ATOM 4085 CA GLU B 286 49.816 5.961 46.467 1.00 56.86 C ANISOU 4085 CA GLU B 286 5670 7186 8747 1042 -788 468 C ATOM 4086 C GLU B 286 49.384 6.669 47.756 1.00 59.03 C ANISOU 4086 C GLU B 286 5988 7615 8826 1005 -900 511 C ATOM 4087 O GLU B 286 48.324 7.298 47.734 1.00 58.43 O ANISOU 4087 O GLU B 286 6021 7576 8605 939 -857 479 O ATOM 4088 CB GLU B 286 49.551 4.455 46.482 1.00 57.99 C ANISOU 4088 CB GLU B 286 5847 7213 8973 1108 -776 587 C ATOM 4089 CG GLU B 286 49.583 3.822 45.100 1.00 69.41 C ANISOU 4089 CG GLU B 286 7277 8503 10593 1136 -646 523 C ATOM 4090 CD GLU B 286 50.952 3.462 44.540 1.00 92.49 C ANISOU 4090 CD GLU B 286 10051 11369 13720 1205 -645 493 C ATOM 4091 OE1 GLU B 286 51.871 3.211 45.333 1.00 88.82 O ANISOU 4091 OE1 GLU B 286 9486 10950 13310 1263 -768 574 O ATOM 4092 OE2 GLU B 286 51.092 3.431 43.308 1.00 85.54 O ANISOU 4092 OE2 GLU B 286 9153 10401 12946 1204 -520 388 O ATOM 4093 N VAL B 287 50.166 6.554 48.829 1.00 55.21 N ANISOU 4093 N VAL B 287 5415 7226 8337 1046 -1044 573 N ATOM 4094 CA VAL B 287 49.857 7.254 50.112 1.00 54.99 C ANISOU 4094 CA VAL B 287 5415 7363 8116 1014 -1161 599 C ATOM 4095 C VAL B 287 49.952 8.770 49.900 1.00 56.97 C ANISOU 4095 C VAL B 287 5656 7689 8302 931 -1137 438 C ATOM 4096 O VAL B 287 49.116 9.500 50.448 1.00 55.93 O ANISOU 4096 O VAL B 287 5610 7644 7997 871 -1142 406 O ATOM 4097 CB VAL B 287 50.797 6.795 51.239 1.00 59.67 C ANISOU 4097 CB VAL B 287 5913 8039 8720 1086 -1330 713 C ATOM 4098 CG1 VAL B 287 50.732 7.728 52.434 1.00 59.78 C ANISOU 4098 CG1 VAL B 287 5947 8241 8527 1048 -1453 708 C ATOM 4099 CG2 VAL B 287 50.498 5.372 51.664 1.00 59.57 C ANISOU 4099 CG2 VAL B 287 5933 7951 8749 1160 -1351 890 C ATOM 4100 N LYS B 288 50.958 9.214 49.146 1.00 51.93 N ANISOU 4100 N LYS B 288 4910 7006 7815 929 -1100 338 N ATOM 4101 CA LYS B 288 51.163 10.654 48.853 1.00 50.56 C ANISOU 4101 CA LYS B 288 4708 6873 7629 854 -1063 190 C ATOM 4102 C LYS B 288 49.972 11.171 48.040 1.00 50.57 C ANISOU 4102 C LYS B 288 4838 6823 7553 786 -924 125 C ATOM 4103 O LYS B 288 49.488 12.266 48.339 1.00 49.38 O ANISOU 4103 O LYS B 288 4729 6746 7286 719 -929 50 O ATOM 4104 CB LYS B 288 52.486 10.819 48.098 1.00 53.67 C ANISOU 4104 CB LYS B 288 4955 7207 8229 874 -1032 120 C ATOM 4105 CG LYS B 288 53.078 12.221 48.080 1.00 75.64 C ANISOU 4105 CG LYS B 288 7652 10065 11025 813 -1065 -5 C ATOM 4106 CD LYS B 288 52.435 13.130 47.057 1.00 92.16 C ANISOU 4106 CD LYS B 288 9806 12108 13105 731 -921 -118 C ATOM 4107 CE LYS B 288 52.764 14.594 47.252 1.00105.34 C ANISOU 4107 CE LYS B 288 11419 13852 14751 659 -960 -233 C ATOM 4108 NZ LYS B 288 51.660 15.462 46.779 1.00112.45 N ANISOU 4108 NZ LYS B 288 12401 14704 15623 583 -825 -318 N ATOM 4109 N GLN B 289 49.526 10.382 47.061 1.00 45.77 N ANISOU 4109 N GLN B 289 4289 6090 7011 805 -807 152 N ATOM 4110 CA GLN B 289 48.388 10.718 46.165 1.00 45.30 C ANISOU 4110 CA GLN B 289 4348 5974 6891 751 -679 101 C ATOM 4111 C GLN B 289 47.085 10.811 46.964 1.00 50.00 C ANISOU 4111 C GLN B 289 5062 6638 7300 717 -711 147 C ATOM 4112 O GLN B 289 46.286 11.698 46.680 1.00 49.51 O ANISOU 4112 O GLN B 289 5070 6596 7147 653 -656 77 O ATOM 4113 CB GLN B 289 48.233 9.638 45.101 1.00 46.11 C ANISOU 4113 CB GLN B 289 4479 5936 7104 789 -571 126 C ATOM 4114 CG GLN B 289 47.158 9.968 44.080 1.00 52.14 C ANISOU 4114 CG GLN B 289 5354 6645 7811 733 -444 64 C ATOM 4115 CD GLN B 289 46.917 8.851 43.100 1.00 64.75 C ANISOU 4115 CD GLN B 289 6987 8116 9497 767 -348 76 C ATOM 4116 OE1 GLN B 289 46.827 7.685 43.466 1.00 56.03 O ANISOU 4116 OE1 GLN B 289 5901 6963 8427 817 -376 167 O ATOM 4117 NE2 GLN B 289 46.804 9.210 41.836 1.00 56.46 N ANISOU 4117 NE2 GLN B 289 5952 7013 8488 738 -231 -16 N ATOM 4118 N MET B 290 46.892 9.900 47.912 1.00 47.15 N ANISOU 4118 N MET B 290 4715 6310 6888 764 -797 270 N ATOM 4119 CA MET B 290 45.679 9.881 48.760 1.00 47.54 C ANISOU 4119 CA MET B 290 4866 6433 6766 743 -833 338 C ATOM 4120 C MET B 290 45.526 11.150 49.600 1.00 48.02 C ANISOU 4120 C MET B 290 4928 6637 6682 690 -899 266 C ATOM 4121 O MET B 290 44.421 11.673 49.654 1.00 46.99 O ANISOU 4121 O MET B 290 4887 6540 6429 637 -855 232 O ATOM 4122 CB MET B 290 45.714 8.671 49.691 1.00 51.28 C ANISOU 4122 CB MET B 290 5332 6905 7246 814 -912 499 C ATOM 4123 CG MET B 290 44.553 8.653 50.642 1.00 57.41 C ANISOU 4123 CG MET B 290 6127 7829 7856 817 -1031 578 C ATOM 4124 SD MET B 290 44.602 7.197 51.669 1.00 64.38 S ANISOU 4124 SD MET B 290 7160 8740 8562 769 -974 631 S ATOM 4125 CE MET B 290 44.537 7.950 53.292 1.00 61.18 C ANISOU 4125 CE MET B 290 6784 8186 8275 831 -933 795 C ATOM 4126 N ARG B 291 46.611 11.622 50.211 1.00 43.09 N ANISOU 4126 N ARG B 291 4196 6091 6086 702 -999 229 N ATOM 4127 CA ARG B 291 46.574 12.851 51.042 1.00 41.97 C ANISOU 4127 CA ARG B 291 4037 6081 5828 653 -1072 141 C ATOM 4128 C ARG B 291 46.306 14.088 50.174 1.00 44.45 C ANISOU 4128 C ARG B 291 4372 6359 6157 580 -974 -3 C ATOM 4129 O ARG B 291 45.627 15.005 50.647 1.00 44.82 O ANISOU 4129 O ARG B 291 4474 6480 6074 528 -978 -65 O ATOM 4130 CB ARG B 291 47.911 13.024 51.763 1.00 43.04 C ANISOU 4130 CB ARG B 291 4039 6292 6022 686 -1203 130 C ATOM 4131 CG ARG B 291 48.179 11.943 52.797 1.00 63.77 C ANISOU 4131 CG ARG B 291 6656 9005 8570 750 -1334 273 C ATOM 4132 CD ARG B 291 49.458 12.112 53.587 1.00 88.49 C ANISOU 4132 CD ARG B 291 9648 12215 11760 786 -1477 265 C ATOM 4133 NE ARG B 291 49.623 11.013 54.526 1.00107.19 N ANISOU 4133 NE ARG B 291 12029 14758 13939 791 -1622 304 N ATOM 4134 CZ ARG B 291 49.051 10.960 55.723 1.00127.43 C ANISOU 4134 CZ ARG B 291 14570 17447 16402 738 -1691 181 C ATOM 4135 NH1 ARG B 291 48.289 11.957 56.139 1.00116.18 N ANISOU 4135 NH1 ARG B 291 13104 15980 15061 675 -1629 19 N ATOM 4136 NH2 ARG B 291 49.251 9.916 56.504 1.00117.11 N ANISOU 4136 NH2 ARG B 291 13281 16306 14909 747 -1821 218 N ATOM 4137 N ALA B 292 46.837 14.081 48.952 1.00 38.45 N ANISOU 4137 N ALA B 292 3570 5483 5555 578 -879 -51 N ATOM 4138 CA ALA B 292 46.638 15.163 47.964 1.00 36.86 C ANISOU 4138 CA ALA B 292 3387 5230 5388 514 -774 -166 C ATOM 4139 C ALA B 292 45.162 15.134 47.560 1.00 40.08 C ANISOU 4139 C ALA B 292 3930 5605 5695 482 -686 -156 C ATOM 4140 O ALA B 292 44.562 16.202 47.473 1.00 42.39 O ANISOU 4140 O ALA B 292 4263 5926 5917 425 -659 -235 O ATOM 4141 CB ALA B 292 47.529 15.021 46.760 1.00 37.02 C ANISOU 4141 CB ALA B 292 3338 5141 5588 530 -689 -193 C ATOM 4142 N ARG B 293 44.621 13.939 47.326 1.00 33.66 N ANISOU 4142 N ARG B 293 3178 4728 4882 520 -646 -61 N ATOM 4143 CA ARG B 293 43.212 13.745 46.906 1.00 32.67 C ANISOU 4143 CA ARG B 293 3171 4563 4679 496 -568 -39 C ATOM 4144 C ARG B 293 42.255 14.224 48.001 1.00 36.16 C ANISOU 4144 C ARG B 293 3680 5108 4952 466 -613 -29 C ATOM 4145 O ARG B 293 41.262 14.855 47.658 1.00 36.93 O ANISOU 4145 O ARG B 293 3852 5193 4988 422 -546 -71 O ATOM 4146 CB ARG B 293 42.983 12.283 46.525 1.00 30.34 C ANISOU 4146 CB ARG B 293 2909 4181 4439 546 -535 62 C ATOM 4147 CG ARG B 293 43.435 11.953 45.114 1.00 31.32 C ANISOU 4147 CG ARG B 293 3014 4184 4701 557 -437 23 C ATOM 4148 CD ARG B 293 43.440 10.473 44.826 1.00 38.18 C ANISOU 4148 CD ARG B 293 3898 4966 5644 613 -420 111 C ATOM 4149 NE ARG B 293 43.535 10.209 43.403 1.00 40.36 N ANISOU 4149 NE ARG B 293 4175 5132 6029 617 -312 57 N ATOM 4150 CZ ARG B 293 43.331 9.023 42.856 1.00 54.70 C ANISOU 4150 CZ ARG B 293 6011 6849 7925 657 -269 99 C ATOM 4151 NH1 ARG B 293 43.022 7.990 43.616 1.00 32.61 N ANISOU 4151 NH1 ARG B 293 3229 4036 5126 696 -324 207 N ATOM 4152 NH2 ARG B 293 43.432 8.871 41.554 1.00 47.12 N ANISOU 4152 NH2 ARG B 293 5054 5803 7046 658 -170 32 N ATOM 4153 N ARG B 294 42.573 13.947 49.262 1.00 31.38 N ANISOU 4153 N ARG B 294 3047 4608 4270 492 -724 27 N ATOM 4154 CA ARG B 294 41.725 14.379 50.400 1.00 30.79 C ANISOU 4154 CA ARG B 294 3028 4652 4019 468 -772 34 C ATOM 4155 C ARG B 294 41.608 15.905 50.403 1.00 36.82 C ANISOU 4155 C ARG B 294 3788 5464 4739 406 -759 -109 C ATOM 4156 O ARG B 294 40.499 16.402 50.585 1.00 37.83 O ANISOU 4156 O ARG B 294 3989 5617 4765 370 -716 -138 O ATOM 4157 CB ARG B 294 42.338 13.906 51.717 1.00 29.38 C ANISOU 4157 CB ARG B 294 2807 4588 3767 510 -902 115 C ATOM 4158 CG ARG B 294 42.280 12.404 51.930 1.00 35.95 C ANISOU 4158 CG ARG B 294 3672 5392 4597 566 -916 280 C ATOM 4159 CD ARG B 294 42.745 12.082 53.330 1.00 50.70 C ANISOU 4159 CD ARG B 294 5505 7390 6370 606 -1051 367 C ATOM 4160 NE ARG B 294 42.811 10.656 53.588 1.00 66.25 N ANISOU 4160 NE ARG B 294 7485 9312 8375 668 -1072 539 N ATOM 4161 CZ ARG B 294 42.943 10.118 54.790 1.00 81.56 C ANISOU 4161 CZ ARG B 294 9416 11350 10221 711 -1178 663 C ATOM 4162 NH1 ARG B 294 43.013 10.894 55.855 1.00 70.02 N ANISOU 4162 NH1 ARG B 294 7940 10057 8608 697 -1277 626 N ATOM 4163 NH2 ARG B 294 42.995 8.808 54.927 1.00 69.17 N ANISOU 4163 NH2 ARG B 294 7857 9716 8710 767 -1186 825 N ATOM 4164 N LYS B 295 42.723 16.605 50.203 1.00 33.80 N ANISOU 4164 N LYS B 295 3313 5080 4448 395 -789 -199 N ATOM 4165 CA LYS B 295 42.747 18.071 50.176 1.00 33.25 C ANISOU 4165 CA LYS B 295 3223 5036 4375 336 -779 -339 C ATOM 4166 C LYS B 295 41.861 18.622 49.052 1.00 37.70 C ANISOU 4166 C LYS B 295 3850 5500 4975 296 -651 -386 C ATOM 4167 O LYS B 295 41.065 19.528 49.303 1.00 37.53 O ANISOU 4167 O LYS B 295 3873 5508 4878 253 -629 -457 O ATOM 4168 CB LYS B 295 44.183 18.593 50.032 1.00 35.02 C ANISOU 4168 CB LYS B 295 3324 5256 4725 333 -829 -409 C ATOM 4169 CG LYS B 295 45.056 18.342 51.246 1.00 40.10 C ANISOU 4169 CG LYS B 295 3894 6019 5322 364 -975 -389 C ATOM 4170 CD LYS B 295 46.475 18.787 50.993 1.00 51.00 C ANISOU 4170 CD LYS B 295 5141 7384 6854 362 -1019 -455 C ATOM 4171 CE LYS B 295 47.361 18.505 52.182 1.00 68.22 C ANISOU 4171 CE LYS B 295 7242 9688 8990 396 -1178 -436 C ATOM 4172 NZ LYS B 295 48.721 19.078 51.999 1.00 86.85 N ANISOU 4172 NZ LYS B 295 9458 12037 11504 385 -1227 -517 N ATOM 4173 N THR B 296 41.976 18.056 47.835 1.00 33.89 N ANISOU 4173 N THR B 296 3372 4902 4602 312 -570 -347 N ATOM 4174 CA THR B 296 41.175 18.456 46.670 1.00 33.37 C ANISOU 4174 CA THR B 296 3369 4744 4568 281 -455 -377 C ATOM 4175 C THR B 296 39.691 18.123 46.862 1.00 36.87 C ANISOU 4175 C THR B 296 3916 5196 4897 274 -422 -333 C ATOM 4176 O THR B 296 38.848 18.981 46.579 1.00 36.08 O ANISOU 4176 O THR B 296 3861 5082 4764 234 -370 -391 O ATOM 4177 CB THR B 296 41.759 17.854 45.381 1.00 37.78 C ANISOU 4177 CB THR B 296 3902 5194 5257 305 -384 -350 C ATOM 4178 OG1 THR B 296 43.113 18.282 45.269 1.00 39.50 O ANISOU 4178 OG1 THR B 296 4013 5411 5583 305 -409 -398 O ATOM 4179 CG2 THR B 296 40.989 18.284 44.122 1.00 33.58 C ANISOU 4179 CG2 THR B 296 3435 4579 4747 274 -271 -380 C ATOM 4180 N ALA B 297 39.373 16.882 47.341 1.00 32.70 N ANISOU 4180 N ALA B 297 3420 4684 4319 314 -450 -227 N ATOM 4181 CA ALA B 297 37.991 16.448 47.582 1.00 31.21 C ANISOU 4181 CA ALA B 297 3321 4504 4033 306 -418 -174 C ATOM 4182 C ALA B 297 37.324 17.340 48.611 1.00 33.10 C ANISOU 4182 C ALA B 297 3585 4848 4143 273 -446 -227 C ATOM 4183 O ALA B 297 36.199 17.786 48.372 1.00 32.68 O ANISOU 4183 O ALA B 297 3589 4778 4048 242 -386 -257 O ATOM 4184 CB ALA B 297 37.954 15.006 48.044 1.00 31.97 C ANISOU 4184 CB ALA B 297 3432 4602 4113 353 -450 -47 C ATOM 4185 N LYS B 298 38.035 17.652 49.725 1.00 28.63 N ANISOU 4185 N LYS B 298 2970 4389 3518 279 -538 -249 N ATOM 4186 CA LYS B 298 37.551 18.532 50.797 1.00 28.34 C ANISOU 4186 CA LYS B 298 2949 4466 3352 250 -573 -318 C ATOM 4187 C LYS B 298 37.215 19.896 50.212 1.00 32.66 C ANISOU 4187 C LYS B 298 3497 4969 3943 201 -514 -446 C ATOM 4188 O LYS B 298 36.141 20.402 50.505 1.00 33.51 O ANISOU 4188 O LYS B 298 3656 5103 3972 176 -477 -483 O ATOM 4189 CB LYS B 298 38.580 18.644 51.935 1.00 30.80 C ANISOU 4189 CB LYS B 298 3197 4897 3608 265 -691 -335 C ATOM 4190 CG LYS B 298 38.145 19.509 53.107 1.00 48.08 C ANISOU 4190 CG LYS B 298 5403 7218 5647 237 -732 -416 C ATOM 4191 CD LYS B 298 39.260 19.682 54.128 1.00 67.00 C ANISOU 4191 CD LYS B 298 7729 9733 7997 249 -858 -454 C ATOM 4192 CE LYS B 298 38.962 20.807 55.095 1.00 89.63 C ANISOU 4192 CE LYS B 298 10605 12719 10731 213 -891 -578 C ATOM 4193 NZ LYS B 298 40.075 21.033 56.059 1.00104.85 N ANISOU 4193 NZ LYS B 298 12460 14768 12612 219 -1024 -633 N ATOM 4194 N MET B 299 38.084 20.452 49.326 1.00 27.80 N ANISOU 4194 N MET B 299 2824 4277 3463 189 -497 -505 N ATOM 4195 CA MET B 299 37.840 21.742 48.668 1.00 27.02 C ANISOU 4195 CA MET B 299 2722 4118 3426 145 -439 -610 C ATOM 4196 C MET B 299 36.603 21.674 47.760 1.00 31.12 C ANISOU 4196 C MET B 299 3318 4557 3949 135 -342 -581 C ATOM 4197 O MET B 299 35.774 22.581 47.795 1.00 31.74 O ANISOU 4197 O MET B 299 3425 4633 4001 105 -307 -646 O ATOM 4198 CB MET B 299 39.064 22.199 47.865 1.00 28.59 C ANISOU 4198 CB MET B 299 2842 4248 3773 136 -432 -653 C ATOM 4199 CG MET B 299 38.872 23.545 47.220 1.00 31.99 C ANISOU 4199 CG MET B 299 3266 4613 4276 89 -372 -747 C ATOM 4200 SD MET B 299 40.247 24.096 46.201 1.00 36.47 S ANISOU 4200 SD MET B 299 3742 5094 5023 71 -343 -785 S ATOM 4201 CE MET B 299 39.912 23.231 44.696 1.00 33.32 C ANISOU 4201 CE MET B 299 3396 4592 4671 97 -243 -687 C ATOM 4202 N LEU B 300 36.498 20.607 46.944 1.00 26.49 N ANISOU 4202 N LEU B 300 2759 3903 3403 162 -303 -490 N ATOM 4203 CA LEU B 300 35.390 20.398 46.006 1.00 25.68 C ANISOU 4203 CA LEU B 300 2724 3725 3307 155 -222 -459 C ATOM 4204 C LEU B 300 34.054 20.217 46.703 1.00 29.96 C ANISOU 4204 C LEU B 300 3327 4318 3739 149 -214 -436 C ATOM 4205 O LEU B 300 33.060 20.750 46.223 1.00 30.45 O ANISOU 4205 O LEU B 300 3427 4343 3799 127 -159 -465 O ATOM 4206 CB LEU B 300 35.670 19.247 45.040 1.00 24.66 C ANISOU 4206 CB LEU B 300 2605 3519 3247 185 -190 -382 C ATOM 4207 CG LEU B 300 36.800 19.483 44.063 1.00 28.14 C ANISOU 4207 CG LEU B 300 2993 3894 3803 188 -164 -410 C ATOM 4208 CD1 LEU B 300 37.183 18.214 43.379 1.00 27.62 C ANISOU 4208 CD1 LEU B 300 2929 3771 3794 226 -143 -341 C ATOM 4209 CD2 LEU B 300 36.482 20.632 43.093 1.00 29.14 C ANISOU 4209 CD2 LEU B 300 3135 3965 3975 151 -97 -473 C ATOM 4210 N MET B 301 34.041 19.526 47.851 1.00 26.83 N ANISOU 4210 N MET B 301 2935 4009 3251 168 -268 -382 N ATOM 4211 CA MET B 301 32.837 19.333 48.663 1.00 27.73 C ANISOU 4211 CA MET B 301 3099 4186 3250 161 -257 -354 C ATOM 4212 C MET B 301 32.332 20.687 49.187 1.00 32.06 C ANISOU 4212 C MET B 301 3646 4787 3747 129 -248 -467 C ATOM 4213 O MET B 301 31.124 20.929 49.175 1.00 31.60 O ANISOU 4213 O MET B 301 3629 4726 3652 113 -197 -478 O ATOM 4214 CB MET B 301 33.097 18.366 49.822 1.00 30.70 C ANISOU 4214 CB MET B 301 3476 4655 3534 190 -319 -266 C ATOM 4215 CG MET B 301 33.168 16.904 49.397 1.00 35.47 C ANISOU 4215 CG MET B 301 4096 5195 4186 222 -311 -141 C ATOM 4216 SD MET B 301 33.690 15.845 50.771 1.00 41.32 S ANISOU 4216 SD MET B 301 4825 6040 4835 261 -396 -23 S ATOM 4217 CE MET B 301 34.475 14.522 49.902 1.00 38.18 C ANISOU 4217 CE MET B 301 4408 5523 4576 305 -397 77 C ATOM 4218 N VAL B 302 33.263 21.593 49.573 1.00 28.89 N ANISOU 4218 N VAL B 302 3191 4424 3360 118 -297 -558 N ATOM 4219 CA VAL B 302 32.932 22.942 50.057 1.00 28.30 C ANISOU 4219 CA VAL B 302 3107 4388 3259 86 -293 -683 C ATOM 4220 C VAL B 302 32.320 23.779 48.910 1.00 32.13 C ANISOU 4220 C VAL B 302 3603 4759 3844 63 -216 -731 C ATOM 4221 O VAL B 302 31.280 24.400 49.121 1.00 31.47 O ANISOU 4221 O VAL B 302 3546 4683 3727 48 -177 -780 O ATOM 4222 CB VAL B 302 34.123 23.631 50.792 1.00 30.49 C ANISOU 4222 CB VAL B 302 3317 4732 3534 77 -373 -773 C ATOM 4223 CG1 VAL B 302 33.809 25.089 51.153 1.00 29.87 C ANISOU 4223 CG1 VAL B 302 3223 4667 3460 41 -362 -920 C ATOM 4224 CG2 VAL B 302 34.502 22.850 52.044 1.00 29.44 C ANISOU 4224 CG2 VAL B 302 3181 4733 3271 102 -454 -722 C ATOM 4225 N VAL B 303 32.923 23.724 47.691 1.00 27.62 N ANISOU 4225 N VAL B 303 3016 4087 3392 65 -192 -706 N ATOM 4226 CA VAL B 303 32.441 24.436 46.496 1.00 25.74 C ANISOU 4226 CA VAL B 303 2793 3743 3245 47 -124 -729 C ATOM 4227 C VAL B 303 31.005 23.983 46.190 1.00 29.59 C ANISOU 4227 C VAL B 303 3343 4210 3689 53 -74 -677 C ATOM 4228 O VAL B 303 30.128 24.822 46.014 1.00 29.51 O ANISOU 4228 O VAL B 303 3348 4173 3693 37 -36 -724 O ATOM 4229 CB VAL B 303 33.405 24.296 45.274 1.00 27.34 C ANISOU 4229 CB VAL B 303 2970 3857 3561 51 -103 -699 C ATOM 4230 CG1 VAL B 303 32.838 24.970 44.026 1.00 25.78 C ANISOU 4230 CG1 VAL B 303 2797 3561 3435 35 -33 -705 C ATOM 4231 CG2 VAL B 303 34.799 24.856 45.584 1.00 27.62 C ANISOU 4231 CG2 VAL B 303 2929 3908 3657 40 -148 -759 C ATOM 4232 N VAL B 304 30.760 22.657 46.184 1.00 26.42 N ANISOU 4232 N VAL B 304 2972 3820 3244 75 -76 -581 N ATOM 4233 CA VAL B 304 29.433 22.067 45.920 1.00 25.21 C ANISOU 4233 CA VAL B 304 2871 3648 3060 77 -34 -526 C ATOM 4234 C VAL B 304 28.414 22.474 47.006 1.00 30.14 C ANISOU 4234 C VAL B 304 3508 4350 3595 66 -26 -562 C ATOM 4235 O VAL B 304 27.298 22.877 46.673 1.00 29.64 O ANISOU 4235 O VAL B 304 3464 4256 3543 55 19 -580 O ATOM 4236 CB VAL B 304 29.514 20.533 45.681 1.00 27.51 C ANISOU 4236 CB VAL B 304 3184 3922 3345 100 -39 -420 C ATOM 4237 CG1 VAL B 304 28.126 19.906 45.541 1.00 27.06 C ANISOU 4237 CG1 VAL B 304 3171 3849 3260 96 1 -369 C ATOM 4238 CG2 VAL B 304 30.361 20.225 44.445 1.00 26.34 C ANISOU 4238 CG2 VAL B 304 3027 3690 3293 111 -28 -402 C ATOM 4239 N LEU B 305 28.807 22.423 48.283 1.00 28.65 N ANISOU 4239 N LEU B 305 3304 4265 3317 70 -70 -578 N ATOM 4240 CA LEU B 305 27.926 22.828 49.376 1.00 29.68 C ANISOU 4240 CA LEU B 305 3445 4484 3348 60 -57 -623 C ATOM 4241 C LEU B 305 27.566 24.334 49.310 1.00 31.63 C ANISOU 4241 C LEU B 305 3672 4709 3637 39 -31 -749 C ATOM 4242 O LEU B 305 26.403 24.672 49.493 1.00 29.96 O ANISOU 4242 O LEU B 305 3476 4504 3403 33 16 -775 O ATOM 4243 CB LEU B 305 28.489 22.419 50.760 1.00 30.62 C ANISOU 4243 CB LEU B 305 3556 4735 3345 70 -115 -610 C ATOM 4244 CG LEU B 305 27.722 22.936 51.992 1.00 37.05 C ANISOU 4244 CG LEU B 305 4379 5662 4035 60 -101 -673 C ATOM 4245 CD1 LEU B 305 26.292 22.339 52.077 1.00 37.58 C ANISOU 4245 CD1 LEU B 305 4487 5737 4057 58 -33 -604 C ATOM 4246 CD2 LEU B 305 28.506 22.689 53.262 1.00 40.83 C ANISOU 4246 CD2 LEU B 305 4847 6275 4390 70 -173 -674 C ATOM 4247 N VAL B 306 28.550 25.213 49.015 1.00 27.73 N ANISOU 4247 N VAL B 306 3140 4179 3219 30 -58 -824 N ATOM 4248 CA VAL B 306 28.344 26.661 48.883 1.00 27.52 C ANISOU 4248 CA VAL B 306 3089 4109 3261 10 -36 -942 C ATOM 4249 C VAL B 306 27.444 26.956 47.642 1.00 31.27 C ANISOU 4249 C VAL B 306 3584 4469 3828 9 26 -913 C ATOM 4250 O VAL B 306 26.582 27.821 47.722 1.00 31.67 O ANISOU 4250 O VAL B 306 3631 4499 3901 2 61 -977 O ATOM 4251 CB VAL B 306 29.692 27.460 48.924 1.00 31.08 C ANISOU 4251 CB VAL B 306 3486 4545 3780 -6 -82 -1022 C ATOM 4252 CG1 VAL B 306 29.504 28.945 48.606 1.00 30.36 C ANISOU 4252 CG1 VAL B 306 3366 4377 3791 -28 -52 -1132 C ATOM 4253 CG2 VAL B 306 30.364 27.301 50.285 1.00 31.00 C ANISOU 4253 CG2 VAL B 306 3452 4664 3662 -5 -151 -1068 C ATOM 4254 N PHE B 307 27.616 26.211 46.534 1.00 26.94 N ANISOU 4254 N PHE B 307 3055 3853 3329 18 36 -820 N ATOM 4255 CA PHE B 307 26.785 26.332 45.330 1.00 25.23 C ANISOU 4255 CA PHE B 307 2863 3544 3180 20 82 -782 C ATOM 4256 C PHE B 307 25.320 25.935 45.669 1.00 30.22 C ANISOU 4256 C PHE B 307 3521 4205 3755 25 112 -757 C ATOM 4257 O PHE B 307 24.381 26.648 45.285 1.00 29.04 O ANISOU 4257 O PHE B 307 3371 4011 3652 23 146 -786 O ATOM 4258 CB PHE B 307 27.333 25.441 44.183 1.00 25.26 C ANISOU 4258 CB PHE B 307 2885 3490 3221 29 82 -694 C ATOM 4259 CG PHE B 307 26.596 25.594 42.870 1.00 25.62 C ANISOU 4259 CG PHE B 307 2957 3451 3326 31 120 -659 C ATOM 4260 CD1 PHE B 307 25.423 24.876 42.618 1.00 27.97 C ANISOU 4260 CD1 PHE B 307 3288 3747 3594 37 137 -608 C ATOM 4261 CD2 PHE B 307 27.066 26.465 41.887 1.00 26.57 C ANISOU 4261 CD2 PHE B 307 3068 3496 3533 24 137 -673 C ATOM 4262 CE1 PHE B 307 24.715 25.054 41.418 1.00 28.50 C ANISOU 4262 CE1 PHE B 307 3376 3744 3708 39 160 -581 C ATOM 4263 CE2 PHE B 307 26.384 26.610 40.672 1.00 28.71 C ANISOU 4263 CE2 PHE B 307 3367 3699 3842 28 166 -633 C ATOM 4264 CZ PHE B 307 25.201 25.923 40.455 1.00 27.23 C ANISOU 4264 CZ PHE B 307 3211 3518 3618 36 171 -591 C ATOM 4265 N ALA B 308 25.141 24.791 46.390 1.00 26.32 N ANISOU 4265 N ALA B 308 3046 3786 3170 32 102 -698 N ATOM 4266 CA ALA B 308 23.848 24.273 46.829 1.00 24.00 C ANISOU 4266 CA ALA B 308 2770 3528 2820 33 135 -665 C ATOM 4267 C ALA B 308 23.105 25.324 47.670 1.00 29.67 C ANISOU 4267 C ALA B 308 3468 4292 3512 26 162 -761 C ATOM 4268 O ALA B 308 21.928 25.582 47.417 1.00 28.70 O ANISOU 4268 O ALA B 308 3344 4141 3420 26 204 -769 O ATOM 4269 CB ALA B 308 24.038 22.998 47.623 1.00 23.57 C ANISOU 4269 CB ALA B 308 2733 3549 2674 39 117 -586 C ATOM 4270 N LEU B 309 23.811 25.973 48.621 1.00 27.61 N ANISOU 4270 N LEU B 309 3186 4098 3205 22 137 -845 N ATOM 4271 CA LEU B 309 23.262 27.014 49.495 1.00 27.71 C ANISOU 4271 CA LEU B 309 3177 4159 3191 16 162 -959 C ATOM 4272 C LEU B 309 22.954 28.331 48.770 1.00 32.38 C ANISOU 4272 C LEU B 309 3743 4649 3910 13 186 -1039 C ATOM 4273 O LEU B 309 21.889 28.891 49.012 1.00 33.89 O ANISOU 4273 O LEU B 309 3922 4838 4114 16 232 -1091 O ATOM 4274 CB LEU B 309 24.172 27.256 50.710 1.00 27.94 C ANISOU 4274 CB LEU B 309 3193 4297 3128 11 118 -1032 C ATOM 4275 CG LEU B 309 24.282 26.096 51.730 1.00 32.93 C ANISOU 4275 CG LEU B 309 3850 5054 3609 17 97 -957 C ATOM 4276 CD1 LEU B 309 25.484 26.277 52.620 1.00 33.00 C ANISOU 4276 CD1 LEU B 309 3841 5153 3544 15 28 -1012 C ATOM 4277 CD2 LEU B 309 23.012 25.965 52.589 1.00 36.28 C ANISOU 4277 CD2 LEU B 309 4286 5560 3937 17 158 -964 C ATOM 4278 N CYS B 310 23.850 28.813 47.882 1.00 27.48 N ANISOU 4278 N CYS B 310 3111 3942 3389 8 162 -1043 N ATOM 4279 CA CYS B 310 23.654 30.064 47.124 1.00 28.39 C ANISOU 4279 CA CYS B 310 3203 3949 3635 6 183 -1099 C ATOM 4280 C CYS B 310 22.513 30.016 46.117 1.00 31.42 C ANISOU 4280 C CYS B 310 3601 4256 4081 19 219 -1035 C ATOM 4281 O CYS B 310 21.908 31.047 45.828 1.00 29.68 O ANISOU 4281 O CYS B 310 3359 3969 3949 24 245 -1086 O ATOM 4282 CB CYS B 310 24.948 30.505 46.449 1.00 29.65 C ANISOU 4282 CB CYS B 310 3346 4041 3878 -7 154 -1102 C ATOM 4283 SG CYS B 310 26.210 31.103 47.597 1.00 34.69 S ANISOU 4283 SG CYS B 310 3942 4744 4493 -27 107 -1222 S ATOM 4284 N TYR B 311 22.290 28.840 45.516 1.00 28.16 N ANISOU 4284 N TYR B 311 3221 3844 3634 24 215 -926 N ATOM 4285 CA TYR B 311 21.276 28.624 44.486 1.00 27.00 C ANISOU 4285 CA TYR B 311 3088 3634 3536 35 235 -860 C ATOM 4286 C TYR B 311 19.963 28.065 45.028 1.00 30.43 C ANISOU 4286 C TYR B 311 3522 4120 3920 40 265 -845 C ATOM 4287 O TYR B 311 19.005 27.957 44.264 1.00 30.23 O ANISOU 4287 O TYR B 311 3497 4047 3943 47 277 -803 O ATOM 4288 CB TYR B 311 21.843 27.744 43.358 1.00 26.57 C ANISOU 4288 CB TYR B 311 3066 3539 3490 35 214 -764 C ATOM 4289 CG TYR B 311 22.765 28.493 42.430 1.00 27.01 C ANISOU 4289 CG TYR B 311 3118 3518 3626 32 206 -767 C ATOM 4290 CD1 TYR B 311 24.124 28.621 42.714 1.00 28.49 C ANISOU 4290 CD1 TYR B 311 3293 3719 3813 22 186 -794 C ATOM 4291 CD2 TYR B 311 22.289 29.060 41.250 1.00 27.56 C ANISOU 4291 CD2 TYR B 311 3195 3504 3773 40 217 -736 C ATOM 4292 CE1 TYR B 311 24.973 29.345 41.875 1.00 29.05 C ANISOU 4292 CE1 TYR B 311 3353 3717 3968 15 189 -794 C ATOM 4293 CE2 TYR B 311 23.144 29.738 40.374 1.00 27.80 C ANISOU 4293 CE2 TYR B 311 3224 3466 3874 35 218 -725 C ATOM 4294 CZ TYR B 311 24.482 29.887 40.695 1.00 32.72 C ANISOU 4294 CZ TYR B 311 3830 4098 4503 21 209 -755 C ATOM 4295 OH TYR B 311 25.323 30.569 39.839 1.00 32.80 O ANISOU 4295 OH TYR B 311 3833 4039 4591 12 220 -740 O ATOM 4296 N LEU B 312 19.912 27.705 46.331 1.00 26.24 N ANISOU 4296 N LEU B 312 2988 3691 3292 34 275 -875 N ATOM 4297 CA LEU B 312 18.702 27.193 46.968 1.00 25.79 C ANISOU 4297 CA LEU B 312 2925 3691 3182 35 316 -860 C ATOM 4298 C LEU B 312 17.572 28.253 47.026 1.00 29.87 C ANISOU 4298 C LEU B 312 3403 4177 3771 45 359 -935 C ATOM 4299 O LEU B 312 16.484 27.945 46.544 1.00 30.00 O ANISOU 4299 O LEU B 312 3408 4163 3827 50 380 -890 O ATOM 4300 CB LEU B 312 18.963 26.569 48.357 1.00 25.64 C ANISOU 4300 CB LEU B 312 2915 3797 3029 27 322 -864 C ATOM 4301 CG LEU B 312 17.730 26.007 49.110 1.00 29.67 C ANISOU 4301 CG LEU B 312 3419 4377 3478 24 378 -840 C ATOM 4302 CD1 LEU B 312 17.236 24.705 48.482 1.00 28.58 C ANISOU 4302 CD1 LEU B 312 3300 4211 3350 17 379 -716 C ATOM 4303 CD2 LEU B 312 18.064 25.750 50.555 1.00 31.94 C ANISOU 4303 CD2 LEU B 312 3715 4797 3625 18 387 -865 C ATOM 4304 N PRO B 313 17.759 29.496 47.543 1.00 25.77 N ANISOU 4304 N PRO B 313 2855 3653 3282 50 371 -1050 N ATOM 4305 CA PRO B 313 16.621 30.438 47.556 1.00 25.24 C ANISOU 4305 CA PRO B 313 2745 3546 3299 66 415 -1118 C ATOM 4306 C PRO B 313 16.018 30.733 46.177 1.00 28.46 C ANISOU 4306 C PRO B 313 3142 3837 3834 81 405 -1061 C ATOM 4307 O PRO B 313 14.820 30.598 46.036 1.00 28.52 O ANISOU 4307 O PRO B 313 3124 3837 3874 92 433 -1042 O ATOM 4308 CB PRO B 313 17.204 31.691 48.239 1.00 25.99 C ANISOU 4308 CB PRO B 313 2816 3640 3420 66 419 -1254 C ATOM 4309 CG PRO B 313 18.302 31.161 49.086 1.00 29.72 C ANISOU 4309 CG PRO B 313 3315 4211 3765 48 389 -1266 C ATOM 4310 CD PRO B 313 18.936 30.109 48.199 1.00 25.83 C ANISOU 4310 CD PRO B 313 2860 3693 3260 41 345 -1134 C ATOM 4311 N ILE B 314 16.830 31.063 45.163 1.00 25.65 N ANISOU 4311 N ILE B 314 2804 3399 3542 81 364 -1027 N ATOM 4312 CA ILE B 314 16.330 31.403 43.816 1.00 24.94 C ANISOU 4312 CA ILE B 314 2710 3207 3558 97 348 -966 C ATOM 4313 C ILE B 314 15.583 30.239 43.150 1.00 30.10 C ANISOU 4313 C ILE B 314 3382 3873 4183 97 336 -866 C ATOM 4314 O ILE B 314 14.558 30.478 42.514 1.00 30.30 O ANISOU 4314 O ILE B 314 3383 3852 4280 114 336 -842 O ATOM 4315 CB ILE B 314 17.443 32.000 42.913 1.00 26.35 C ANISOU 4315 CB ILE B 314 2908 3305 3799 94 316 -944 C ATOM 4316 CG1 ILE B 314 16.840 32.765 41.707 1.00 24.54 C ANISOU 4316 CG1 ILE B 314 2666 2970 3688 117 308 -900 C ATOM 4317 CG2 ILE B 314 18.519 30.948 42.488 1.00 26.99 C ANISOU 4317 CG2 ILE B 314 3037 3415 3803 76 285 -870 C ATOM 4318 CD1 ILE B 314 17.922 33.557 40.833 1.00 28.19 C ANISOU 4318 CD1 ILE B 314 3142 3345 4224 113 291 -876 C ATOM 4319 N SER B 315 16.081 28.996 43.313 1.00 26.28 N ANISOU 4319 N SER B 315 2935 3448 3602 78 322 -811 N ATOM 4320 CA SER B 315 15.490 27.774 42.759 1.00 25.21 C ANISOU 4320 CA SER B 315 2817 3320 3441 72 310 -725 C ATOM 4321 C SER B 315 14.150 27.482 43.390 1.00 29.96 C ANISOU 4321 C SER B 315 3381 3963 4041 71 348 -734 C ATOM 4322 O SER B 315 13.196 27.193 42.675 1.00 30.54 O ANISOU 4322 O SER B 315 3436 4002 4164 75 339 -693 O ATOM 4323 CB SER B 315 16.436 26.594 42.964 1.00 26.73 C ANISOU 4323 CB SER B 315 3052 3559 3546 54 293 -675 C ATOM 4324 OG SER B 315 17.607 26.796 42.194 1.00 23.74 O ANISOU 4324 OG SER B 315 2702 3135 3182 55 261 -659 O ATOM 4325 N VAL B 316 14.075 27.574 44.732 1.00 26.44 N ANISOU 4325 N VAL B 316 2917 3595 3534 66 393 -791 N ATOM 4326 CA VAL B 316 12.867 27.360 45.508 1.00 25.66 C ANISOU 4326 CA VAL B 316 2778 3548 3424 64 447 -808 C ATOM 4327 C VAL B 316 11.838 28.449 45.204 1.00 30.05 C ANISOU 4327 C VAL B 316 3276 4048 4094 89 467 -863 C ATOM 4328 O VAL B 316 10.700 28.120 44.880 1.00 29.89 O ANISOU 4328 O VAL B 316 3219 4014 4124 91 478 -830 O ATOM 4329 CB VAL B 316 13.165 27.179 47.025 1.00 28.26 C ANISOU 4329 CB VAL B 316 3111 3988 3637 52 492 -854 C ATOM 4330 CG1 VAL B 316 11.876 27.152 47.850 1.00 26.79 C ANISOU 4330 CG1 VAL B 316 2877 3859 3442 52 565 -882 C ATOM 4331 CG2 VAL B 316 13.965 25.898 47.258 1.00 27.68 C ANISOU 4331 CG2 VAL B 316 3088 3966 3463 32 468 -771 C ATOM 4332 N LEU B 317 12.243 29.734 45.259 1.00 27.13 N ANISOU 4332 N LEU B 317 2893 3637 3779 107 467 -943 N ATOM 4333 CA LEU B 317 11.348 30.861 44.954 1.00 26.56 C ANISOU 4333 CA LEU B 317 2763 3494 3834 138 483 -994 C ATOM 4334 C LEU B 317 10.761 30.772 43.530 1.00 31.83 C ANISOU 4334 C LEU B 317 3423 4079 4593 152 433 -910 C ATOM 4335 O LEU B 317 9.575 31.053 43.354 1.00 33.49 O ANISOU 4335 O LEU B 317 3575 4263 4887 173 447 -915 O ATOM 4336 CB LEU B 317 12.048 32.207 45.164 1.00 25.95 C ANISOU 4336 CB LEU B 317 2679 3369 3814 152 485 -1088 C ATOM 4337 CG LEU B 317 12.317 32.644 46.598 1.00 29.75 C ANISOU 4337 CG LEU B 317 3146 3926 4231 147 537 -1209 C ATOM 4338 CD1 LEU B 317 13.275 33.797 46.624 1.00 28.83 C ANISOU 4338 CD1 LEU B 317 3031 3752 4172 150 520 -1292 C ATOM 4339 CD2 LEU B 317 11.029 32.990 47.324 1.00 31.41 C ANISOU 4339 CD2 LEU B 317 3293 4166 4477 165 607 -1279 C ATOM 4340 N ASN B 318 11.577 30.341 42.535 1.00 26.71 N ANISOU 4340 N ASN B 318 2829 3396 3922 142 376 -834 N ATOM 4341 CA ASN B 318 11.139 30.180 41.141 1.00 25.90 C ANISOU 4341 CA ASN B 318 2731 3231 3878 154 321 -754 C ATOM 4342 C ASN B 318 10.037 29.117 41.009 1.00 28.99 C ANISOU 4342 C ASN B 318 3098 3657 4261 143 318 -708 C ATOM 4343 O ASN B 318 9.041 29.346 40.329 1.00 29.17 O ANISOU 4343 O ASN B 318 3078 3639 4365 162 294 -686 O ATOM 4344 CB ASN B 318 12.324 29.855 40.227 1.00 22.89 C ANISOU 4344 CB ASN B 318 2418 2825 3455 142 274 -694 C ATOM 4345 CG ASN B 318 11.950 29.792 38.775 1.00 37.89 C ANISOU 4345 CG ASN B 318 4329 4670 5396 155 219 -618 C ATOM 4346 OD1 ASN B 318 11.469 30.778 38.198 1.00 31.76 O ANISOU 4346 OD1 ASN B 318 3525 3832 4711 184 201 -612 O ATOM 4347 ND2 ASN B 318 12.170 28.624 38.152 1.00 26.62 N ANISOU 4347 ND2 ASN B 318 2945 3266 3902 135 187 -559 N ATOM 4348 N VAL B 319 10.216 27.971 41.669 1.00 24.60 N ANISOU 4348 N VAL B 319 2564 3170 3612 111 341 -691 N ATOM 4349 CA VAL B 319 9.252 26.874 41.694 1.00 24.23 C ANISOU 4349 CA VAL B 319 2492 3154 3560 91 348 -649 C ATOM 4350 C VAL B 319 7.949 27.320 42.378 1.00 29.50 C ANISOU 4350 C VAL B 319 3076 3840 4293 103 402 -696 C ATOM 4351 O VAL B 319 6.883 27.117 41.820 1.00 29.75 O ANISOU 4351 O VAL B 319 3059 3847 4398 107 383 -670 O ATOM 4352 CB VAL B 319 9.858 25.601 42.353 1.00 26.29 C ANISOU 4352 CB VAL B 319 2796 3478 3714 57 367 -613 C ATOM 4353 CG1 VAL B 319 8.780 24.580 42.691 1.00 25.43 C ANISOU 4353 CG1 VAL B 319 2648 3401 3613 32 397 -578 C ATOM 4354 CG2 VAL B 319 10.913 24.989 41.448 1.00 25.45 C ANISOU 4354 CG2 VAL B 319 2758 3342 3570 48 310 -560 C ATOM 4355 N LEU B 320 8.036 27.936 43.564 1.00 25.68 N ANISOU 4355 N LEU B 320 2572 3400 3783 110 468 -771 N ATOM 4356 CA LEU B 320 6.867 28.385 44.309 1.00 26.11 C ANISOU 4356 CA LEU B 320 2546 3479 3894 123 535 -830 C ATOM 4357 C LEU B 320 6.051 29.409 43.520 1.00 31.24 C ANISOU 4357 C LEU B 320 3134 4046 4689 164 508 -850 C ATOM 4358 O LEU B 320 4.824 29.347 43.521 1.00 30.80 O ANISOU 4358 O LEU B 320 3003 3989 4710 172 529 -851 O ATOM 4359 CB LEU B 320 7.277 28.934 45.687 1.00 26.30 C ANISOU 4359 CB LEU B 320 2572 3571 3849 125 608 -922 C ATOM 4360 CG LEU B 320 7.895 27.931 46.699 1.00 31.01 C ANISOU 4360 CG LEU B 320 3219 4271 4294 90 643 -900 C ATOM 4361 CD1 LEU B 320 8.287 28.651 47.968 1.00 31.46 C ANISOU 4361 CD1 LEU B 320 3276 4399 4281 97 703 -1004 C ATOM 4362 CD2 LEU B 320 6.935 26.780 47.041 1.00 30.98 C ANISOU 4362 CD2 LEU B 320 3184 4318 4268 62 688 -836 C ATOM 4363 N LYS B 321 6.736 30.300 42.786 1.00 27.83 N ANISOU 4363 N LYS B 321 2732 3542 4301 188 457 -853 N ATOM 4364 CA LYS B 321 6.094 31.320 41.965 1.00 26.89 C ANISOU 4364 CA LYS B 321 2562 3335 4321 231 421 -854 C ATOM 4365 C LYS B 321 5.476 30.733 40.690 1.00 30.56 C ANISOU 4365 C LYS B 321 3018 3767 4825 233 343 -762 C ATOM 4366 O LYS B 321 4.287 30.912 40.445 1.00 32.23 O ANISOU 4366 O LYS B 321 3152 3958 5136 255 335 -759 O ATOM 4367 CB LYS B 321 7.118 32.421 41.623 1.00 28.10 C ANISOU 4367 CB LYS B 321 2755 3420 4504 252 397 -876 C ATOM 4368 CG LYS B 321 6.594 33.497 40.707 1.00 27.10 C ANISOU 4368 CG LYS B 321 2585 3191 4521 299 354 -855 C ATOM 4369 CD LYS B 321 7.711 34.398 40.194 1.00 31.69 C ANISOU 4369 CD LYS B 321 3215 3699 5128 309 327 -848 C ATOM 4370 CE LYS B 321 7.139 35.384 39.196 1.00 36.14 C ANISOU 4370 CE LYS B 321 3739 4159 5834 357 280 -802 C ATOM 4371 NZ LYS B 321 7.970 36.595 38.992 1.00 46.44 N ANISOU 4371 NZ LYS B 321 5062 5373 7212 374 281 -817 N ATOM 4372 N ARG B 322 6.279 30.025 39.897 1.00 25.89 N ANISOU 4372 N ARG B 322 2504 3175 4158 210 285 -693 N ATOM 4373 CA ARG B 322 5.911 29.503 38.585 1.00 24.95 C ANISOU 4373 CA ARG B 322 2394 3030 4055 210 202 -615 C ATOM 4374 C ARG B 322 5.115 28.230 38.576 1.00 26.92 C ANISOU 4374 C ARG B 322 2618 3324 4287 177 195 -587 C ATOM 4375 O ARG B 322 4.289 28.068 37.697 1.00 26.72 O ANISOU 4375 O ARG B 322 2555 3277 4321 185 133 -552 O ATOM 4376 CB ARG B 322 7.160 29.329 37.715 1.00 24.90 C ANISOU 4376 CB ARG B 322 2481 3004 3974 200 152 -564 C ATOM 4377 CG ARG B 322 7.967 30.610 37.498 1.00 28.84 C ANISOU 4377 CG ARG B 322 3005 3445 4508 229 152 -576 C ATOM 4378 CD ARG B 322 7.259 31.607 36.619 1.00 22.51 C ANISOU 4378 CD ARG B 322 2161 2572 3819 274 104 -543 C ATOM 4379 NE ARG B 322 8.096 32.791 36.407 1.00 28.56 N ANISOU 4379 NE ARG B 322 2953 3272 4626 296 109 -543 N ATOM 4380 CZ ARG B 322 7.703 33.883 35.750 1.00 40.66 C ANISOU 4380 CZ ARG B 322 4454 4727 6268 339 77 -511 C ATOM 4381 NH1 ARG B 322 6.480 33.958 35.242 1.00 29.62 N ANISOU 4381 NH1 ARG B 322 2996 3315 4944 369 31 -478 N ATOM 4382 NH2 ARG B 322 8.525 34.913 35.609 1.00 28.77 N ANISOU 4382 NH2 ARG B 322 2972 3154 4807 353 89 -508 N ATOM 4383 N VAL B 323 5.368 27.316 39.501 1.00 24.84 N ANISOU 4383 N VAL B 323 2371 3120 3945 138 251 -599 N ATOM 4384 CA VAL B 323 4.663 26.024 39.577 1.00 24.85 C ANISOU 4384 CA VAL B 323 2348 3156 3939 100 255 -568 C ATOM 4385 C VAL B 323 3.495 26.073 40.553 1.00 29.99 C ANISOU 4385 C VAL B 323 2904 3840 4650 97 330 -606 C ATOM 4386 O VAL B 323 2.428 25.544 40.237 1.00 30.62 O ANISOU 4386 O VAL B 323 2918 3916 4799 83 312 -586 O ATOM 4387 CB VAL B 323 5.640 24.855 39.908 1.00 27.90 C ANISOU 4387 CB VAL B 323 2811 3579 4211 59 269 -537 C ATOM 4388 CG1 VAL B 323 4.946 23.498 39.871 1.00 27.35 C ANISOU 4388 CG1 VAL B 323 2718 3525 4151 16 268 -499 C ATOM 4389 CG2 VAL B 323 6.848 24.865 38.982 1.00 27.58 C ANISOU 4389 CG2 VAL B 323 2857 3507 4114 65 208 -509 C ATOM 4390 N PHE B 324 3.678 26.702 41.728 1.00 27.33 N ANISOU 4390 N PHE B 324 2555 3539 4289 108 414 -666 N ATOM 4391 CA PHE B 324 2.632 26.708 42.761 1.00 27.91 C ANISOU 4391 CA PHE B 324 2544 3658 4402 103 504 -707 C ATOM 4392 C PHE B 324 1.809 28.000 42.857 1.00 33.46 C ANISOU 4392 C PHE B 324 3161 4328 5226 153 527 -774 C ATOM 4393 O PHE B 324 0.966 28.092 43.754 1.00 32.77 O ANISOU 4393 O PHE B 324 2998 4281 5172 153 614 -820 O ATOM 4394 CB PHE B 324 3.242 26.325 44.132 1.00 29.32 C ANISOU 4394 CB PHE B 324 2762 3920 4458 77 593 -729 C ATOM 4395 CG PHE B 324 3.715 24.890 44.138 1.00 30.79 C ANISOU 4395 CG PHE B 324 3007 4137 4556 29 581 -652 C ATOM 4396 CD1 PHE B 324 2.830 23.845 44.428 1.00 33.73 C ANISOU 4396 CD1 PHE B 324 3332 4535 4950 -9 619 -607 C ATOM 4397 CD2 PHE B 324 5.014 24.569 43.765 1.00 32.86 C ANISOU 4397 CD2 PHE B 324 3364 4389 4733 23 529 -620 C ATOM 4398 CE1 PHE B 324 3.254 22.508 44.377 1.00 35.04 C ANISOU 4398 CE1 PHE B 324 3549 4711 5055 -52 606 -532 C ATOM 4399 CE2 PHE B 324 5.431 23.237 43.692 1.00 35.86 C ANISOU 4399 CE2 PHE B 324 3792 4782 5051 -16 515 -549 C ATOM 4400 CZ PHE B 324 4.551 22.214 44.003 1.00 34.32 C ANISOU 4400 CZ PHE B 324 3552 4606 4881 -53 552 -505 C ATOM 4401 N GLY B 325 2.007 28.941 41.921 1.00 31.65 N ANISOU 4401 N GLY B 325 2938 4023 5066 194 454 -772 N ATOM 4402 CA GLY B 325 1.252 30.196 41.864 1.00 32.37 C ANISOU 4402 CA GLY B 325 2946 4061 5293 248 463 -824 C ATOM 4403 C GLY B 325 1.237 31.034 43.129 1.00 39.46 C ANISOU 4403 C GLY B 325 3810 4983 6198 268 568 -929 C ATOM 4404 O GLY B 325 0.222 31.668 43.455 1.00 39.77 O ANISOU 4404 O GLY B 325 3751 5006 6354 302 613 -984 O ATOM 4405 N MET B 326 2.369 31.040 43.852 1.00 36.91 N ANISOU 4405 N MET B 326 3566 4705 5753 248 606 -964 N ATOM 4406 CA MET B 326 2.542 31.767 45.104 1.00 36.47 C ANISOU 4406 CA MET B 326 3497 4689 5672 260 700 -1076 C ATOM 4407 C MET B 326 2.979 33.198 44.875 1.00 39.89 C ANISOU 4407 C MET B 326 3927 5036 6195 305 681 -1141 C ATOM 4408 O MET B 326 3.361 33.559 43.757 1.00 39.45 O ANISOU 4408 O MET B 326 3899 4896 6195 323 595 -1082 O ATOM 4409 CB MET B 326 3.531 31.016 46.008 1.00 38.90 C ANISOU 4409 CB MET B 326 3888 5092 5802 215 737 -1079 C ATOM 4410 CG MET B 326 2.868 29.880 46.748 1.00 43.11 C ANISOU 4410 CG MET B 326 4397 5718 6263 177 804 -1047 C ATOM 4411 SD MET B 326 3.987 28.931 47.769 1.00 47.85 S ANISOU 4411 SD MET B 326 5092 6432 6656 131 841 -1031 S ATOM 4412 CE MET B 326 4.263 30.052 49.119 1.00 44.65 C ANISOU 4412 CE MET B 326 4675 6086 6206 156 928 -1183 C ATOM 4413 N PHE B 327 2.931 34.010 45.949 1.00 36.36 N ANISOU 4413 N PHE B 327 3447 4610 5758 323 766 -1264 N ATOM 4414 CA PHE B 327 3.347 35.421 46.028 1.00 36.05 C ANISOU 4414 CA PHE B 327 3397 4489 5812 362 770 -1356 C ATOM 4415 C PHE B 327 2.420 36.387 45.227 1.00 46.60 C ANISOU 4415 C PHE B 327 4645 5705 7354 421 740 -1349 C ATOM 4416 O PHE B 327 2.834 37.503 44.901 1.00 48.02 O ANISOU 4416 O PHE B 327 4825 5784 7635 454 714 -1381 O ATOM 4417 CB PHE B 327 4.860 35.607 45.659 1.00 35.27 C ANISOU 4417 CB PHE B 327 3397 4359 5644 344 709 -1335 C ATOM 4418 CG PHE B 327 5.786 34.531 46.189 1.00 33.93 C ANISOU 4418 CG PHE B 327 3311 4296 5283 291 711 -1307 C ATOM 4419 CD1 PHE B 327 5.868 34.270 47.555 1.00 35.10 C ANISOU 4419 CD1 PHE B 327 3463 4558 5316 270 792 -1391 C ATOM 4420 CD2 PHE B 327 6.552 33.755 45.322 1.00 33.55 C ANISOU 4420 CD2 PHE B 327 3337 4241 5171 264 633 -1195 C ATOM 4421 CE1 PHE B 327 6.684 33.238 48.041 1.00 34.89 C ANISOU 4421 CE1 PHE B 327 3511 4631 5116 226 788 -1350 C ATOM 4422 CE2 PHE B 327 7.382 32.728 45.815 1.00 34.99 C ANISOU 4422 CE2 PHE B 327 3588 4515 5191 221 635 -1165 C ATOM 4423 CZ PHE B 327 7.432 32.475 47.167 1.00 32.28 C ANISOU 4423 CZ PHE B 327 3246 4279 4740 203 708 -1236 C ATOM 4424 N ARG B 328 1.162 35.966 44.959 1.00 46.17 N ANISOU 4424 N ARG B 328 4510 5661 7372 434 746 -1309 N ATOM 4425 CA ARG B 328 0.127 36.760 44.263 1.00 47.37 C ANISOU 4425 CA ARG B 328 4563 5712 7723 493 714 -1298 C ATOM 4426 C ARG B 328 -0.787 37.471 45.301 1.00 55.47 C ANISOU 4426 C ARG B 328 5481 6743 8851 530 827 -1431 C ATOM 4427 O ARG B 328 -2.000 37.249 45.352 1.00 55.16 O ANISOU 4427 O ARG B 328 5342 6718 8899 548 856 -1429 O ATOM 4428 CB ARG B 328 -0.682 35.884 43.280 1.00 45.77 C ANISOU 4428 CB ARG B 328 4330 5514 7549 486 637 -1175 C ATOM 4429 CG ARG B 328 0.155 35.317 42.147 1.00 53.15 C ANISOU 4429 CG ARG B 328 5364 6431 8401 460 525 -1056 C ATOM 4430 CD ARG B 328 -0.617 34.325 41.314 1.00 64.97 C ANISOU 4430 CD ARG B 328 6835 7950 9900 443 454 -956 C ATOM 4431 NE ARG B 328 -0.667 34.747 39.916 1.00 86.30 N ANISOU 4431 NE ARG B 328 9552 10571 12665 474 334 -863 N ATOM 4432 CZ ARG B 328 0.013 34.170 38.929 1.00107.79 C ANISOU 4432 CZ ARG B 328 12363 13304 15290 445 249 -772 C ATOM 4433 NH1 ARG B 328 -0.092 34.628 37.686 1.00 95.26 N ANISOU 4433 NH1 ARG B 328 10788 11652 13754 478 146 -690 N ATOM 4434 NH2 ARG B 328 0.792 33.121 39.174 1.00 96.38 N ANISOU 4434 NH2 ARG B 328 10992 11934 13695 386 267 -762 N ATOM 4435 N GLN B 329 -0.170 38.317 46.140 1.00 55.26 N ANISOU 4435 N GLN B 329 5473 6707 8816 540 890 -1557 N ATOM 4436 CA GLN B 329 -0.822 39.078 47.213 1.00 56.49 C ANISOU 4436 CA GLN B 329 5542 6870 9050 575 1006 -1712 C ATOM 4437 C GLN B 329 -0.109 40.413 47.415 1.00 63.73 C ANISOU 4437 C GLN B 329 6473 7690 10052 607 1013 -1821 C ATOM 4438 O GLN B 329 1.117 40.483 47.319 1.00 64.16 O ANISOU 4438 O GLN B 329 6623 7736 10017 577 971 -1813 O ATOM 4439 CB GLN B 329 -0.864 38.278 48.535 1.00 58.09 C ANISOU 4439 CB GLN B 329 5760 7233 9077 529 1118 -1785 C ATOM 4440 CG GLN B 329 0.523 37.972 49.129 1.00 88.88 C ANISOU 4440 CG GLN B 329 9790 11223 12756 467 1095 -1753 C ATOM 4441 CD GLN B 329 0.481 37.190 50.420 1.00119.45 C ANISOU 4441 CD GLN B 329 13685 15225 16473 441 1204 -1876 C ATOM 4442 OE1 GLN B 329 -0.515 36.529 50.756 1.00118.39 O ANISOU 4442 OE1 GLN B 329 13496 15186 16300 434 1305 -1914 O ATOM 4443 NE2 GLN B 329 1.580 37.232 51.165 1.00110.11 N ANISOU 4443 NE2 GLN B 329 12585 14057 15194 423 1185 -1937 N ATOM 4444 N ALA B 330 -0.874 41.466 47.700 1.00 62.27 N ANISOU 4444 N ALA B 330 6185 7424 10049 667 1069 -1925 N ATOM 4445 CA ALA B 330 -0.342 42.810 47.895 1.00 63.05 C ANISOU 4445 CA ALA B 330 6279 7409 10267 703 1082 -2041 C ATOM 4446 C ALA B 330 0.214 43.054 49.305 1.00 67.43 C ANISOU 4446 C ALA B 330 6865 8052 10704 676 1183 -2224 C ATOM 4447 O ALA B 330 1.089 43.914 49.470 1.00 66.76 O ANISOU 4447 O ALA B 330 6816 7895 10654 677 1173 -2309 O ATOM 4448 CB ALA B 330 -1.420 43.836 47.574 1.00 63.89 C ANISOU 4448 CB ALA B 330 6257 7385 10634 783 1099 -2080 C ATOM 4449 N SER B 331 -0.302 42.309 50.311 1.00 63.96 N ANISOU 4449 N SER B 331 6409 7768 10126 651 1280 -2283 N ATOM 4450 CA SER B 331 0.043 42.451 51.728 1.00 63.81 C ANISOU 4450 CA SER B 331 6412 7862 9970 628 1385 -2458 C ATOM 4451 C SER B 331 1.543 42.350 52.066 1.00 68.86 C ANISOU 4451 C SER B 331 7173 8550 10439 576 1341 -2484 C ATOM 4452 O SER B 331 2.041 43.231 52.780 1.00 69.79 O ANISOU 4452 O SER B 331 7294 8647 10575 583 1377 -2649 O ATOM 4453 CB SER B 331 -0.754 41.477 52.593 1.00 65.82 C ANISOU 4453 CB SER B 331 6640 8286 10083 604 1487 -2467 C ATOM 4454 OG SER B 331 -0.355 40.132 52.400 1.00 70.79 O ANISOU 4454 OG SER B 331 7349 9017 10530 544 1438 -2314 O ATOM 4455 N ASP B 332 2.246 41.279 51.643 1.00 63.86 N ANISOU 4455 N ASP B 332 6631 7988 9644 523 1268 -2338 N ATOM 4456 CA ASP B 332 3.661 41.129 52.010 1.00 63.43 C ANISOU 4456 CA ASP B 332 6681 7989 9430 476 1228 -2363 C ATOM 4457 C ASP B 332 4.628 41.375 50.840 1.00 62.49 C ANISOU 4457 C ASP B 332 6616 7744 9382 469 1108 -2258 C ATOM 4458 O ASP B 332 5.733 40.827 50.817 1.00 61.64 O ANISOU 4458 O ASP B 332 6597 7689 9133 423 1054 -2207 O ATOM 4459 CB ASP B 332 3.909 39.764 52.680 1.00 66.34 C ANISOU 4459 CB ASP B 332 7117 8542 9549 421 1248 -2300 C ATOM 4460 CG ASP B 332 3.698 39.781 54.184 1.00 83.61 C ANISOU 4460 CG ASP B 332 9291 10878 11597 412 1365 -2452 C ATOM 4461 OD1 ASP B 332 4.620 40.236 54.910 1.00 85.37 O ANISOU 4461 OD1 ASP B 332 9561 11150 11725 395 1368 -2576 O ATOM 4462 OD2 ASP B 332 2.613 39.338 54.637 1.00 89.43 O ANISOU 4462 OD2 ASP B 332 9971 11689 12321 421 1453 -2449 O ATOM 4463 N ARG B 333 4.243 42.296 49.955 1.00 54.78 N ANISOU 4463 N ARG B 333 5583 6601 8629 517 1072 -2228 N ATOM 4464 CA ARG B 333 4.958 42.589 48.687 1.00 52.21 C ANISOU 4464 CA ARG B 333 5295 6140 8403 521 970 -2118 C ATOM 4465 C ARG B 333 6.411 43.025 48.917 1.00 51.55 C ANISOU 4465 C ARG B 333 5284 6041 8260 483 937 -2173 C ATOM 4466 O ARG B 333 7.271 42.545 48.177 1.00 51.22 O ANISOU 4466 O ARG B 333 5314 5996 8150 450 860 -2050 O ATOM 4467 CB ARG B 333 4.198 43.690 47.947 1.00 50.48 C ANISOU 4467 CB ARG B 333 4988 5747 8444 587 962 -2120 C ATOM 4468 CG ARG B 333 4.507 43.764 46.463 1.00 57.18 C ANISOU 4468 CG ARG B 333 5862 6488 9374 598 855 -1934 C ATOM 4469 CD ARG B 333 4.505 45.186 45.958 1.00 58.54 C ANISOU 4469 CD ARG B 333 5991 6471 9781 647 833 -1949 C ATOM 4470 NE ARG B 333 4.673 45.242 44.517 1.00 68.90 N ANISOU 4470 NE ARG B 333 7333 7698 11147 657 733 -1755 N ATOM 4471 CZ ARG B 333 5.782 45.635 43.908 1.00 81.94 C ANISOU 4471 CZ ARG B 333 9047 9268 12819 637 678 -1690 C ATOM 4472 NH1 ARG B 333 6.829 46.014 44.618 1.00 58.64 N ANISOU 4472 NH1 ARG B 333 6125 6295 9861 606 709 -1809 N ATOM 4473 NH2 ARG B 333 5.836 45.659 42.591 1.00 70.98 N ANISOU 4473 NH2 ARG B 333 7688 7821 11461 648 594 -1509 N ATOM 4474 N GLU B 334 6.671 43.886 49.899 1.00 43.76 N ANISOU 4474 N GLU B 334 4275 5049 7302 486 995 -2366 N ATOM 4475 CA GLU B 334 8.012 44.356 50.204 1.00 41.72 C ANISOU 4475 CA GLU B 334 4068 4774 7008 449 967 -2449 C ATOM 4476 C GLU B 334 8.934 43.202 50.596 1.00 42.66 C ANISOU 4476 C GLU B 334 4276 5054 6878 389 936 -2400 C ATOM 4477 O GLU B 334 10.062 43.162 50.121 1.00 42.21 O ANISOU 4477 O GLU B 334 4273 4964 6799 357 868 -2344 O ATOM 4478 CB GLU B 334 7.996 45.452 51.288 1.00 42.56 C ANISOU 4478 CB GLU B 334 4125 4861 7186 464 1040 -2687 C ATOM 4479 CG GLU B 334 7.260 46.728 50.898 1.00 46.45 C ANISOU 4479 CG GLU B 334 4527 5167 7955 525 1068 -2748 C ATOM 4480 CD GLU B 334 5.767 46.793 51.194 1.00 57.63 C ANISOU 4480 CD GLU B 334 5855 6594 9448 581 1147 -2787 C ATOM 4481 OE1 GLU B 334 5.118 45.736 51.376 1.00 45.21 O ANISOU 4481 OE1 GLU B 334 4287 5159 7730 573 1174 -2719 O ATOM 4482 OE2 GLU B 334 5.242 47.925 51.234 1.00 54.42 O ANISOU 4482 OE2 GLU B 334 5368 6047 9263 633 1185 -2885 O ATOM 4483 N ALA B 335 8.443 42.274 51.447 1.00 36.88 N ANISOU 4483 N ALA B 335 3553 4490 5970 376 989 -2414 N ATOM 4484 CA ALA B 335 9.157 41.094 51.944 1.00 36.26 C ANISOU 4484 CA ALA B 335 3551 4573 5652 326 968 -2361 C ATOM 4485 C ALA B 335 9.419 40.091 50.817 1.00 41.48 C ANISOU 4485 C ALA B 335 4263 5220 6276 308 890 -2148 C ATOM 4486 O ALA B 335 10.476 39.471 50.779 1.00 42.22 O ANISOU 4486 O ALA B 335 4425 5371 6246 270 837 -2091 O ATOM 4487 CB ALA B 335 8.347 40.426 53.045 1.00 36.38 C ANISOU 4487 CB ALA B 335 3552 4752 5518 324 1056 -2414 C ATOM 4488 N VAL B 336 8.446 39.931 49.910 1.00 37.98 N ANISOU 4488 N VAL B 336 3782 4706 5943 338 883 -2038 N ATOM 4489 CA VAL B 336 8.501 39.030 48.760 1.00 37.03 C ANISOU 4489 CA VAL B 336 3700 4565 5803 327 812 -1848 C ATOM 4490 C VAL B 336 9.573 39.504 47.780 1.00 41.38 C ANISOU 4490 C VAL B 336 4292 5004 6425 319 733 -1788 C ATOM 4491 O VAL B 336 10.447 38.726 47.404 1.00 41.41 O ANISOU 4491 O VAL B 336 4364 5048 6322 285 681 -1697 O ATOM 4492 CB VAL B 336 7.090 38.894 48.110 1.00 39.11 C ANISOU 4492 CB VAL B 336 3898 4782 6179 364 822 -1772 C ATOM 4493 CG1 VAL B 336 7.168 38.286 46.710 1.00 38.37 C ANISOU 4493 CG1 VAL B 336 3839 4635 6104 359 734 -1594 C ATOM 4494 CG2 VAL B 336 6.159 38.089 49.009 1.00 38.19 C ANISOU 4494 CG2 VAL B 336 3750 4797 5965 357 900 -1797 C ATOM 4495 N TYR B 337 9.523 40.791 47.411 1.00 38.70 N ANISOU 4495 N TYR B 337 3909 4523 6271 351 731 -1841 N ATOM 4496 CA TYR B 337 10.466 41.416 46.491 1.00 38.46 C ANISOU 4496 CA TYR B 337 3907 4371 6335 346 670 -1785 C ATOM 4497 C TYR B 337 11.877 41.500 47.084 1.00 39.20 C ANISOU 4497 C TYR B 337 4048 4504 6341 300 657 -1862 C ATOM 4498 O TYR B 337 12.832 41.369 46.319 1.00 37.47 O ANISOU 4498 O TYR B 337 3876 4244 6118 277 602 -1771 O ATOM 4499 CB TYR B 337 9.935 42.775 45.987 1.00 40.87 C ANISOU 4499 CB TYR B 337 4146 4506 6876 395 678 -1815 C ATOM 4500 CG TYR B 337 8.944 42.631 44.843 1.00 44.99 C ANISOU 4500 CG TYR B 337 4641 4964 7490 435 642 -1668 C ATOM 4501 CD1 TYR B 337 7.636 42.210 45.073 1.00 47.30 C ANISOU 4501 CD1 TYR B 337 4879 5310 7784 464 675 -1668 C ATOM 4502 CD2 TYR B 337 9.333 42.856 43.524 1.00 46.73 C ANISOU 4502 CD2 TYR B 337 4889 5081 7784 442 574 -1525 C ATOM 4503 CE1 TYR B 337 6.734 42.039 44.024 1.00 48.98 C ANISOU 4503 CE1 TYR B 337 5061 5471 8077 499 630 -1537 C ATOM 4504 CE2 TYR B 337 8.438 42.692 42.467 1.00 47.98 C ANISOU 4504 CE2 TYR B 337 5027 5196 8009 479 530 -1389 C ATOM 4505 CZ TYR B 337 7.135 42.299 42.724 1.00 59.11 C ANISOU 4505 CZ TYR B 337 6376 6656 9426 508 553 -1400 C ATOM 4506 OH TYR B 337 6.245 42.145 41.688 1.00 64.94 O ANISOU 4506 OH TYR B 337 7086 7355 10233 545 499 -1273 O ATOM 4507 N ALA B 338 12.016 41.637 48.437 1.00 33.71 N ANISOU 4507 N ALA B 338 3343 3903 5564 286 707 -2025 N ATOM 4508 CA ALA B 338 13.334 41.644 49.102 1.00 32.26 C ANISOU 4508 CA ALA B 338 3198 3776 5282 242 685 -2106 C ATOM 4509 C ALA B 338 13.939 40.225 49.053 1.00 35.59 C ANISOU 4509 C ALA B 338 3689 4327 5505 207 644 -1989 C ATOM 4510 O ALA B 338 15.139 40.092 48.814 1.00 34.88 O ANISOU 4510 O ALA B 338 3638 4233 5380 175 593 -1960 O ATOM 4511 CB ALA B 338 13.211 42.119 50.550 1.00 32.27 C ANISOU 4511 CB ALA B 338 3169 3857 5233 240 744 -2312 C ATOM 4512 N ALA B 339 13.092 39.162 49.245 1.00 31.92 N ANISOU 4512 N ALA B 339 3235 3967 4928 212 668 -1918 N ATOM 4513 CA ALA B 339 13.532 37.754 49.209 1.00 30.28 C ANISOU 4513 CA ALA B 339 3089 3870 4548 183 635 -1801 C ATOM 4514 C ALA B 339 14.056 37.411 47.829 1.00 33.49 C ANISOU 4514 C ALA B 339 3529 4192 5002 177 570 -1648 C ATOM 4515 O ALA B 339 15.126 36.818 47.724 1.00 33.88 O ANISOU 4515 O ALA B 339 3628 4281 4965 148 526 -1597 O ATOM 4516 CB ALA B 339 12.394 36.821 49.593 1.00 30.49 C ANISOU 4516 CB ALA B 339 3106 3996 4484 190 683 -1757 C ATOM 4517 N PHE B 340 13.336 37.843 46.767 1.00 29.31 N ANISOU 4517 N PHE B 340 2972 3547 4616 207 562 -1579 N ATOM 4518 CA PHE B 340 13.737 37.643 45.371 1.00 27.91 C ANISOU 4518 CA PHE B 340 2829 3289 4488 206 504 -1437 C ATOM 4519 C PHE B 340 15.020 38.388 45.056 1.00 31.64 C ANISOU 4519 C PHE B 340 3318 3685 5020 188 475 -1457 C ATOM 4520 O PHE B 340 15.866 37.854 44.364 1.00 31.56 O ANISOU 4520 O PHE B 340 3353 3674 4962 167 435 -1365 O ATOM 4521 CB PHE B 340 12.618 38.047 44.398 1.00 28.79 C ANISOU 4521 CB PHE B 340 2902 3303 4733 246 499 -1367 C ATOM 4522 CG PHE B 340 11.654 36.924 44.111 1.00 29.47 C ANISOU 4522 CG PHE B 340 2990 3455 4751 251 494 -1277 C ATOM 4523 CD1 PHE B 340 10.511 36.746 44.892 1.00 31.82 C ANISOU 4523 CD1 PHE B 340 3237 3811 5041 266 547 -1334 C ATOM 4524 CD2 PHE B 340 11.883 36.041 43.060 1.00 28.99 C ANISOU 4524 CD2 PHE B 340 2978 3398 4638 239 440 -1141 C ATOM 4525 CE1 PHE B 340 9.630 35.687 44.644 1.00 31.80 C ANISOU 4525 CE1 PHE B 340 3229 3865 4989 264 545 -1252 C ATOM 4526 CE2 PHE B 340 10.994 34.991 42.804 1.00 31.39 C ANISOU 4526 CE2 PHE B 340 3278 3756 4891 239 432 -1070 C ATOM 4527 CZ PHE B 340 9.871 34.825 43.595 1.00 30.17 C ANISOU 4527 CZ PHE B 340 3069 3653 4740 249 483 -1123 C ATOM 4528 N THR B 341 15.195 39.589 45.603 1.00 29.51 N ANISOU 4528 N THR B 341 3007 3352 4856 194 501 -1587 N ATOM 4529 CA THR B 341 16.420 40.373 45.404 1.00 29.73 C ANISOU 4529 CA THR B 341 3037 3298 4959 170 478 -1621 C ATOM 4530 C THR B 341 17.588 39.733 46.132 1.00 34.31 C ANISOU 4530 C THR B 341 3653 3990 5395 128 457 -1663 C ATOM 4531 O THR B 341 18.671 39.673 45.573 1.00 35.21 O ANISOU 4531 O THR B 341 3791 4071 5517 103 421 -1606 O ATOM 4532 CB THR B 341 16.157 41.826 45.759 1.00 31.97 C ANISOU 4532 CB THR B 341 3260 3471 5416 189 512 -1751 C ATOM 4533 OG1 THR B 341 15.322 42.286 44.717 1.00 33.43 O ANISOU 4533 OG1 THR B 341 3423 3538 5740 229 511 -1655 O ATOM 4534 CG2 THR B 341 17.426 42.679 45.807 1.00 28.39 C ANISOU 4534 CG2 THR B 341 2800 2940 5048 156 496 -1820 C ATOM 4535 N PHE B 342 17.357 39.227 47.359 1.00 31.78 N ANISOU 4535 N PHE B 342 3333 3804 4939 121 478 -1753 N ATOM 4536 CA PHE B 342 18.391 38.555 48.135 1.00 31.30 C ANISOU 4536 CA PHE B 342 3302 3862 4726 87 449 -1785 C ATOM 4537 C PHE B 342 18.854 37.275 47.417 1.00 34.69 C ANISOU 4537 C PHE B 342 3786 4337 5059 75 410 -1623 C ATOM 4538 O PHE B 342 20.059 37.007 47.362 1.00 34.52 O ANISOU 4538 O PHE B 342 3784 4336 4997 49 369 -1606 O ATOM 4539 CB PHE B 342 17.918 38.256 49.569 1.00 33.21 C ANISOU 4539 CB PHE B 342 3538 4248 4831 87 484 -1898 C ATOM 4540 CG PHE B 342 18.941 37.471 50.361 1.00 35.45 C ANISOU 4540 CG PHE B 342 3857 4668 4943 56 445 -1910 C ATOM 4541 CD1 PHE B 342 20.145 38.054 50.752 1.00 38.08 C ANISOU 4541 CD1 PHE B 342 4179 4999 5292 29 405 -2007 C ATOM 4542 CD2 PHE B 342 18.711 36.148 50.698 1.00 38.55 C ANISOU 4542 CD2 PHE B 342 4289 5186 5172 55 444 -1818 C ATOM 4543 CE1 PHE B 342 21.093 37.328 51.472 1.00 38.91 C ANISOU 4543 CE1 PHE B 342 4310 5233 5242 6 358 -2013 C ATOM 4544 CE2 PHE B 342 19.663 35.420 51.413 1.00 41.81 C ANISOU 4544 CE2 PHE B 342 4732 5720 5433 33 402 -1815 C ATOM 4545 CZ PHE B 342 20.851 36.014 51.793 1.00 39.18 C ANISOU 4545 CZ PHE B 342 4386 5391 5111 10 355 -1911 C ATOM 4546 N SER B 343 17.898 36.528 46.814 1.00 28.93 N ANISOU 4546 N SER B 343 3073 3614 4308 95 421 -1511 N ATOM 4547 CA SER B 343 18.170 35.307 46.058 1.00 27.09 C ANISOU 4547 CA SER B 343 2886 3409 3996 87 388 -1365 C ATOM 4548 C SER B 343 19.008 35.579 44.784 1.00 31.77 C ANISOU 4548 C SER B 343 3496 3898 4676 81 354 -1284 C ATOM 4549 O SER B 343 19.822 34.732 44.380 1.00 30.13 O ANISOU 4549 O SER B 343 3325 3721 4401 64 323 -1207 O ATOM 4550 CB SER B 343 16.861 34.607 45.719 1.00 27.13 C ANISOU 4550 CB SER B 343 2893 3430 3983 108 408 -1287 C ATOM 4551 OG SER B 343 16.302 35.121 44.524 1.00 27.30 O ANISOU 4551 OG SER B 343 2903 3339 4131 130 399 -1222 O ATOM 4552 N HIS B 344 18.787 36.761 44.147 1.00 29.82 N ANISOU 4552 N HIS B 344 3220 3527 4584 95 364 -1297 N ATOM 4553 CA HIS B 344 19.523 37.208 42.951 1.00 28.80 C ANISOU 4553 CA HIS B 344 3102 3291 4548 89 344 -1219 C ATOM 4554 C HIS B 344 20.931 37.542 43.346 1.00 34.60 C ANISOU 4554 C HIS B 344 3831 4026 5291 55 331 -1281 C ATOM 4555 O HIS B 344 21.872 37.059 42.710 1.00 35.73 O ANISOU 4555 O HIS B 344 4000 4167 5407 37 310 -1204 O ATOM 4556 CB HIS B 344 18.863 38.435 42.300 1.00 28.16 C ANISOU 4556 CB HIS B 344 2988 3077 4635 115 361 -1214 C ATOM 4557 CG HIS B 344 17.492 38.161 41.780 1.00 30.95 C ANISOU 4557 CG HIS B 344 3339 3424 4996 151 363 -1144 C ATOM 4558 ND1 HIS B 344 16.644 39.191 41.412 1.00 32.41 N ANISOU 4558 ND1 HIS B 344 3483 3505 5327 186 376 -1148 N ATOM 4559 CD2 HIS B 344 16.847 36.979 41.610 1.00 31.79 C ANISOU 4559 CD2 HIS B 344 3473 3613 4995 157 350 -1073 C ATOM 4560 CE1 HIS B 344 15.525 38.605 41.019 1.00 31.23 C ANISOU 4560 CE1 HIS B 344 3334 3385 5148 211 366 -1080 C ATOM 4561 NE2 HIS B 344 15.595 37.277 41.142 1.00 31.32 N ANISOU 4561 NE2 HIS B 344 3384 3506 5008 193 353 -1039 N ATOM 4562 N TRP B 345 21.081 38.324 44.436 1.00 31.17 N ANISOU 4562 N TRP B 345 3356 3599 4889 45 344 -1429 N ATOM 4563 CA TRP B 345 22.390 38.710 44.948 1.00 30.77 C ANISOU 4563 CA TRP B 345 3286 3552 4852 10 324 -1512 C ATOM 4564 C TRP B 345 23.227 37.487 45.351 1.00 36.25 C ANISOU 4564 C TRP B 345 4012 4374 5389 -9 288 -1480 C ATOM 4565 O TRP B 345 24.427 37.461 45.068 1.00 36.51 O ANISOU 4565 O TRP B 345 4041 4391 5442 -35 263 -1462 O ATOM 4566 CB TRP B 345 22.273 39.692 46.109 1.00 29.01 C ANISOU 4566 CB TRP B 345 3016 3329 4679 4 339 -1693 C ATOM 4567 CG TRP B 345 23.597 40.056 46.705 1.00 29.71 C ANISOU 4567 CG TRP B 345 3080 3435 4775 -36 308 -1792 C ATOM 4568 CD1 TRP B 345 24.488 40.962 46.218 1.00 32.37 C ANISOU 4568 CD1 TRP B 345 3382 3654 5262 -63 302 -1814 C ATOM 4569 CD2 TRP B 345 24.215 39.459 47.858 1.00 29.71 C ANISOU 4569 CD2 TRP B 345 3083 3581 4624 -55 273 -1873 C ATOM 4570 NE1 TRP B 345 25.598 41.018 47.034 1.00 31.65 N ANISOU 4570 NE1 TRP B 345 3266 3625 5136 -99 264 -1920 N ATOM 4571 CE2 TRP B 345 25.462 40.095 48.041 1.00 33.20 C ANISOU 4571 CE2 TRP B 345 3486 3987 5140 -93 240 -1955 C ATOM 4572 CE3 TRP B 345 23.837 38.437 48.753 1.00 30.89 C ANISOU 4572 CE3 TRP B 345 3263 3890 4584 -45 265 -1877 C ATOM 4573 CZ2 TRP B 345 26.335 39.749 49.081 1.00 32.25 C ANISOU 4573 CZ2 TRP B 345 3355 3991 4907 -118 190 -2045 C ATOM 4574 CZ3 TRP B 345 24.701 38.097 49.784 1.00 32.05 C ANISOU 4574 CZ3 TRP B 345 3406 4159 4613 -67 219 -1955 C ATOM 4575 CH2 TRP B 345 25.937 38.742 49.934 1.00 32.63 C ANISOU 4575 CH2 TRP B 345 3440 4200 4759 -101 177 -2039 C ATOM 4576 N LEU B 346 22.590 36.471 45.989 1.00 33.05 N ANISOU 4576 N LEU B 346 3632 4088 4836 4 288 -1465 N ATOM 4577 CA LEU B 346 23.242 35.225 46.426 1.00 32.89 C ANISOU 4577 CA LEU B 346 3643 4188 4667 -7 254 -1421 C ATOM 4578 C LEU B 346 23.875 34.442 45.290 1.00 34.95 C ANISOU 4578 C LEU B 346 3935 4417 4926 -10 235 -1284 C ATOM 4579 O LEU B 346 24.884 33.776 45.518 1.00 34.38 O ANISOU 4579 O LEU B 346 3870 4403 4789 -24 201 -1265 O ATOM 4580 CB LEU B 346 22.269 34.306 47.176 1.00 33.18 C ANISOU 4580 CB LEU B 346 3702 4338 4567 9 270 -1407 C ATOM 4581 CG LEU B 346 22.354 34.246 48.692 1.00 37.96 C ANISOU 4581 CG LEU B 346 4299 5073 5053 0 264 -1516 C ATOM 4582 CD1 LEU B 346 21.434 33.154 49.211 1.00 38.22 C ANISOU 4582 CD1 LEU B 346 4360 5210 4953 14 288 -1457 C ATOM 4583 CD2 LEU B 346 23.772 33.990 49.168 1.00 38.78 C ANISOU 4583 CD2 LEU B 346 4400 5235 5098 -22 207 -1536 C ATOM 4584 N VAL B 347 23.260 34.484 44.084 1.00 30.36 N ANISOU 4584 N VAL B 347 3372 3752 4413 6 254 -1190 N ATOM 4585 CA VAL B 347 23.776 33.823 42.885 1.00 29.66 C ANISOU 4585 CA VAL B 347 3316 3629 4324 5 244 -1068 C ATOM 4586 C VAL B 347 25.111 34.469 42.543 1.00 34.99 C ANISOU 4586 C VAL B 347 3967 4246 5082 -19 237 -1085 C ATOM 4587 O VAL B 347 26.102 33.765 42.379 1.00 35.62 O ANISOU 4587 O VAL B 347 4055 4359 5119 -30 218 -1045 O ATOM 4588 CB VAL B 347 22.777 33.871 41.694 1.00 32.60 C ANISOU 4588 CB VAL B 347 3711 3932 4745 28 261 -977 C ATOM 4589 CG1 VAL B 347 23.462 33.520 40.364 1.00 31.82 C ANISOU 4589 CG1 VAL B 347 3643 3785 4662 24 257 -870 C ATOM 4590 CG2 VAL B 347 21.583 32.954 41.940 1.00 31.95 C ANISOU 4590 CG2 VAL B 347 3649 3915 4577 46 263 -945 C ATOM 4591 N TYR B 348 25.139 35.809 42.489 1.00 31.36 N ANISOU 4591 N TYR B 348 3470 3694 4751 -27 255 -1148 N ATOM 4592 CA TYR B 348 26.327 36.609 42.191 1.00 30.45 C ANISOU 4592 CA TYR B 348 3321 3505 4745 -56 256 -1171 C ATOM 4593 C TYR B 348 27.400 36.521 43.293 1.00 33.51 C ANISOU 4593 C TYR B 348 3672 3965 5095 -84 221 -1274 C ATOM 4594 O TYR B 348 28.590 36.515 42.977 1.00 33.30 O ANISOU 4594 O TYR B 348 3623 3917 5110 -108 211 -1258 O ATOM 4595 CB TYR B 348 25.920 38.062 41.871 1.00 30.58 C ANISOU 4595 CB TYR B 348 3305 3391 4924 -56 286 -1207 C ATOM 4596 CG TYR B 348 25.085 38.167 40.612 1.00 30.46 C ANISOU 4596 CG TYR B 348 3321 3300 4951 -29 309 -1084 C ATOM 4597 CD1 TYR B 348 25.559 37.677 39.392 1.00 31.47 C ANISOU 4597 CD1 TYR B 348 3486 3410 5063 -30 316 -954 C ATOM 4598 CD2 TYR B 348 23.808 38.730 40.642 1.00 30.75 C ANISOU 4598 CD2 TYR B 348 3352 3294 5040 1 323 -1099 C ATOM 4599 CE1 TYR B 348 24.782 37.738 38.239 1.00 31.17 C ANISOU 4599 CE1 TYR B 348 3481 3318 5043 -4 329 -841 C ATOM 4600 CE2 TYR B 348 23.039 38.838 39.483 1.00 30.95 C ANISOU 4600 CE2 TYR B 348 3402 3255 5102 29 332 -981 C ATOM 4601 CZ TYR B 348 23.525 38.322 38.289 1.00 37.88 C ANISOU 4601 CZ TYR B 348 4322 4125 5946 25 331 -852 C ATOM 4602 OH TYR B 348 22.775 38.398 37.148 1.00 40.34 O ANISOU 4602 OH TYR B 348 4661 4389 6275 53 332 -738 O ATOM 4603 N ALA B 349 26.978 36.406 44.572 1.00 29.66 N ANISOU 4603 N ALA B 349 3176 3570 4522 -79 202 -1374 N ATOM 4604 CA ALA B 349 27.878 36.233 45.714 1.00 29.13 C ANISOU 4604 CA ALA B 349 3081 3597 4390 -100 157 -1471 C ATOM 4605 C ALA B 349 28.662 34.899 45.547 1.00 34.10 C ANISOU 4605 C ALA B 349 3733 4306 4917 -98 123 -1376 C ATOM 4606 O ALA B 349 29.821 34.817 45.949 1.00 34.41 O ANISOU 4606 O ALA B 349 3737 4381 4954 -119 83 -1415 O ATOM 4607 CB ALA B 349 27.082 36.236 47.015 1.00 29.40 C ANISOU 4607 CB ALA B 349 3117 3730 4324 -90 152 -1575 C ATOM 4608 N ASN B 350 28.043 33.883 44.903 1.00 29.92 N ANISOU 4608 N ASN B 350 3256 3793 4319 -73 139 -1254 N ATOM 4609 CA ASN B 350 28.689 32.601 44.653 1.00 29.29 C ANISOU 4609 CA ASN B 350 3199 3769 4160 -65 115 -1162 C ATOM 4610 C ASN B 350 29.912 32.734 43.726 1.00 32.74 C ANISOU 4610 C ASN B 350 3612 4138 4690 -82 118 -1120 C ATOM 4611 O ASN B 350 30.908 32.052 43.959 1.00 31.49 O ANISOU 4611 O ASN B 350 3436 4032 4496 -85 84 -1106 O ATOM 4612 CB ASN B 350 27.692 31.553 44.142 1.00 27.29 C ANISOU 4612 CB ASN B 350 3002 3534 3832 -39 135 -1056 C ATOM 4613 CG ASN B 350 28.309 30.180 44.026 1.00 33.85 C ANISOU 4613 CG ASN B 350 3855 4422 4586 -29 110 -974 C ATOM 4614 OD1 ASN B 350 28.701 29.734 42.951 1.00 28.14 O ANISOU 4614 OD1 ASN B 350 3147 3649 3895 -24 124 -895 O ATOM 4615 ND2 ASN B 350 28.457 29.497 45.139 1.00 21.45 N ANISOU 4615 ND2 ASN B 350 2283 2954 2912 -24 74 -991 N ATOM 4616 N SER B 351 29.846 33.627 42.705 1.00 31.31 N ANISOU 4616 N SER B 351 3425 3842 4628 -91 161 -1096 N ATOM 4617 CA SER B 351 30.951 33.910 41.766 1.00 31.96 C ANISOU 4617 CA SER B 351 3482 3852 4809 -111 181 -1053 C ATOM 4618 C SER B 351 32.145 34.491 42.523 1.00 36.02 C ANISOU 4618 C SER B 351 3925 4375 5388 -144 149 -1152 C ATOM 4619 O SER B 351 33.290 34.184 42.194 1.00 37.66 O ANISOU 4619 O SER B 351 4101 4581 5629 -157 144 -1125 O ATOM 4620 CB SER B 351 30.513 34.883 40.675 1.00 35.78 C ANISOU 4620 CB SER B 351 3975 4216 5405 -115 233 -1008 C ATOM 4621 OG SER B 351 29.465 34.335 39.895 1.00 45.84 O ANISOU 4621 OG SER B 351 5311 5486 6620 -84 253 -915 O ATOM 4622 N ALA B 352 31.867 35.295 43.561 1.00 32.60 N ANISOU 4622 N ALA B 352 3460 3955 4970 -157 125 -1276 N ATOM 4623 CA ALA B 352 32.866 35.908 44.435 1.00 32.39 C ANISOU 4623 CA ALA B 352 3363 3945 4998 -191 83 -1397 C ATOM 4624 C ALA B 352 33.445 34.877 45.439 1.00 34.08 C ANISOU 4624 C ALA B 352 3568 4301 5078 -182 13 -1420 C ATOM 4625 O ALA B 352 34.624 34.940 45.771 1.00 33.04 O ANISOU 4625 O ALA B 352 3377 4192 4986 -205 -30 -1466 O ATOM 4626 CB ALA B 352 32.238 37.092 45.175 1.00 32.98 C ANISOU 4626 CB ALA B 352 3415 3988 5129 -203 84 -1530 C ATOM 4627 N ALA B 353 32.604 33.940 45.914 1.00 30.01 N ANISOU 4627 N ALA B 353 3109 3880 4413 -149 0 -1382 N ATOM 4628 CA ALA B 353 32.952 32.922 46.905 1.00 28.83 C ANISOU 4628 CA ALA B 353 2962 3867 4123 -134 -63 -1383 C ATOM 4629 C ALA B 353 34.020 31.896 46.450 1.00 32.02 C ANISOU 4629 C ALA B 353 3354 4291 4522 -124 -88 -1289 C ATOM 4630 O ALA B 353 34.954 31.626 47.205 1.00 30.94 O ANISOU 4630 O ALA B 353 3172 4231 4355 -129 -154 -1328 O ATOM 4631 CB ALA B 353 31.689 32.202 47.369 1.00 29.18 C ANISOU 4631 CB ALA B 353 3073 3987 4030 -104 -51 -1345 C ATOM 4632 N ASN B 354 33.850 31.300 45.248 1.00 28.05 N ANISOU 4632 N ASN B 354 2888 3726 4044 -108 -37 -1171 N ATOM 4633 CA ASN B 354 34.723 30.245 44.718 1.00 28.37 C ANISOU 4633 CA ASN B 354 2922 3777 4081 -91 -46 -1081 C ATOM 4634 C ASN B 354 36.225 30.585 44.748 1.00 31.62 C ANISOU 4634 C ASN B 354 3248 4176 4589 -115 -77 -1123 C ATOM 4635 O ASN B 354 36.965 29.793 45.348 1.00 29.60 O ANISOU 4635 O ASN B 354 2964 3999 4285 -99 -137 -1113 O ATOM 4636 CB ASN B 354 34.274 29.784 43.337 1.00 29.21 C ANISOU 4636 CB ASN B 354 3079 3808 4211 -76 21 -974 C ATOM 4637 CG ASN B 354 32.894 29.206 43.378 1.00 37.20 C ANISOU 4637 CG ASN B 354 4163 4844 5126 -52 37 -927 C ATOM 4638 OD1 ASN B 354 32.524 28.530 44.326 1.00 29.49 O ANISOU 4638 OD1 ASN B 354 3205 3955 4046 -36 -1 -928 O ATOM 4639 ND2 ASN B 354 32.092 29.477 42.373 1.00 34.52 N ANISOU 4639 ND2 ASN B 354 3865 4431 4819 -49 91 -883 N ATOM 4640 N PRO B 355 36.711 31.739 44.214 1.00 29.67 N ANISOU 4640 N PRO B 355 2953 3836 4482 -151 -43 -1171 N ATOM 4641 CA PRO B 355 38.158 32.052 44.349 1.00 29.05 C ANISOU 4641 CA PRO B 355 2780 3751 4504 -178 -75 -1219 C ATOM 4642 C PRO B 355 38.620 32.165 45.813 1.00 33.46 C ANISOU 4642 C PRO B 355 3287 4414 5013 -188 -174 -1329 C ATOM 4643 O PRO B 355 39.723 31.735 46.123 1.00 33.85 O ANISOU 4643 O PRO B 355 3273 4510 5079 -187 -229 -1333 O ATOM 4644 CB PRO B 355 38.294 33.385 43.616 1.00 30.76 C ANISOU 4644 CB PRO B 355 2966 3845 4879 -221 -13 -1252 C ATOM 4645 CG PRO B 355 37.106 33.432 42.698 1.00 35.33 C ANISOU 4645 CG PRO B 355 3628 4361 5435 -203 60 -1172 C ATOM 4646 CD PRO B 355 36.005 32.806 43.472 1.00 30.66 C ANISOU 4646 CD PRO B 355 3100 3855 4693 -170 25 -1177 C ATOM 4647 N ILE B 356 37.762 32.688 46.719 1.00 31.41 N ANISOU 4647 N ILE B 356 3054 4197 4682 -193 -198 -1416 N ATOM 4648 CA ILE B 356 38.052 32.796 48.163 1.00 31.35 C ANISOU 4648 CA ILE B 356 3011 4306 4593 -200 -292 -1528 C ATOM 4649 C ILE B 356 38.185 31.375 48.778 1.00 33.59 C ANISOU 4649 C ILE B 356 3322 4719 4724 -157 -354 -1449 C ATOM 4650 O ILE B 356 39.066 31.156 49.606 1.00 33.93 O ANISOU 4650 O ILE B 356 3309 4851 4733 -157 -443 -1492 O ATOM 4651 CB ILE B 356 37.024 33.707 48.918 1.00 34.63 C ANISOU 4651 CB ILE B 356 3454 4736 4969 -214 -286 -1644 C ATOM 4652 CG1 ILE B 356 36.974 35.141 48.308 1.00 34.51 C ANISOU 4652 CG1 ILE B 356 3403 4576 5133 -255 -229 -1719 C ATOM 4653 CG2 ILE B 356 37.331 33.758 50.439 1.00 36.47 C ANISOU 4653 CG2 ILE B 356 3657 5111 5090 -219 -384 -1765 C ATOM 4654 CD1 ILE B 356 35.738 36.024 48.780 1.00 36.54 C ANISOU 4654 CD1 ILE B 356 3695 4812 5375 -258 -196 -1815 C ATOM 4655 N ILE B 357 37.330 30.416 48.339 1.00 29.30 N ANISOU 4655 N ILE B 357 2858 4178 4097 -119 -309 -1329 N ATOM 4656 CA ILE B 357 37.370 29.014 48.767 1.00 29.32 C ANISOU 4656 CA ILE B 357 2890 4274 3975 -77 -352 -1233 C ATOM 4657 C ILE B 357 38.719 28.384 48.330 1.00 33.30 C ANISOU 4657 C ILE B 357 3331 4764 4557 -66 -384 -1177 C ATOM 4658 O ILE B 357 39.391 27.774 49.161 1.00 32.88 O ANISOU 4658 O ILE B 357 3243 4807 4442 -46 -469 -1169 O ATOM 4659 CB ILE B 357 36.129 28.194 48.269 1.00 32.34 C ANISOU 4659 CB ILE B 357 3365 4638 4283 -47 -288 -1124 C ATOM 4660 CG1 ILE B 357 34.801 28.715 48.889 1.00 32.23 C ANISOU 4660 CG1 ILE B 357 3402 4658 4184 -54 -264 -1180 C ATOM 4661 CG2 ILE B 357 36.317 26.671 48.524 1.00 32.51 C ANISOU 4661 CG2 ILE B 357 3410 4728 4215 -5 -325 -1009 C ATOM 4662 CD1 ILE B 357 33.481 28.220 48.194 1.00 34.74 C ANISOU 4662 CD1 ILE B 357 3797 4929 4472 -36 -189 -1092 C ATOM 4663 N TYR B 358 39.136 28.591 47.052 1.00 29.71 N ANISOU 4663 N TYR B 358 2856 4194 4239 -77 -315 -1141 N ATOM 4664 CA TYR B 358 40.408 28.054 46.525 1.00 28.60 C ANISOU 4664 CA TYR B 358 2648 4030 4189 -66 -325 -1093 C ATOM 4665 C TYR B 358 41.593 28.602 47.312 1.00 34.74 C ANISOU 4665 C TYR B 358 3320 4855 5025 -91 -411 -1189 C ATOM 4666 O TYR B 358 42.528 27.864 47.632 1.00 34.39 O ANISOU 4666 O TYR B 358 3218 4863 4985 -67 -475 -1159 O ATOM 4667 CB TYR B 358 40.602 28.316 45.004 1.00 28.10 C ANISOU 4667 CB TYR B 358 2583 3840 4252 -79 -222 -1046 C ATOM 4668 CG TYR B 358 39.418 28.016 44.103 1.00 28.02 C ANISOU 4668 CG TYR B 358 2673 3776 4198 -63 -139 -970 C ATOM 4669 CD1 TYR B 358 38.504 27.006 44.422 1.00 28.43 C ANISOU 4669 CD1 TYR B 358 2800 3881 4122 -26 -153 -907 C ATOM 4670 CD2 TYR B 358 39.216 28.734 42.925 1.00 28.42 C ANISOU 4670 CD2 TYR B 358 2740 3723 4337 -86 -50 -955 C ATOM 4671 CE1 TYR B 358 37.391 26.757 43.621 1.00 27.53 C ANISOU 4671 CE1 TYR B 358 2768 3718 3973 -16 -85 -847 C ATOM 4672 CE2 TYR B 358 38.111 28.488 42.110 1.00 29.71 C ANISOU 4672 CE2 TYR B 358 2991 3845 4453 -71 13 -889 C ATOM 4673 CZ TYR B 358 37.200 27.496 42.462 1.00 34.98 C ANISOU 4673 CZ TYR B 358 3725 4566 4998 -37 -8 -841 C ATOM 4674 OH TYR B 358 36.113 27.250 41.661 1.00 30.57 O ANISOU 4674 OH TYR B 358 3245 3969 4402 -25 47 -783 O ATOM 4675 N ASN B 359 41.535 29.889 47.650 1.00 32.21 N ANISOU 4675 N ASN B 359 2970 4515 4755 -138 -416 -1310 N ATOM 4676 CA ASN B 359 42.571 30.543 48.429 1.00 31.87 C ANISOU 4676 CA ASN B 359 2823 4513 4772 -170 -502 -1425 C ATOM 4677 C ASN B 359 42.783 29.869 49.785 1.00 38.94 C ANISOU 4677 C ASN B 359 3708 5564 5522 -142 -625 -1443 C ATOM 4678 O ASN B 359 43.921 29.677 50.180 1.00 40.71 O ANISOU 4678 O ASN B 359 3843 5837 5790 -142 -707 -1466 O ATOM 4679 CB ASN B 359 42.228 32.009 48.628 1.00 29.72 C ANISOU 4679 CB ASN B 359 2535 4188 4567 -224 -483 -1558 C ATOM 4680 CG ASN B 359 43.325 32.756 49.311 1.00 48.19 C ANISOU 4680 CG ASN B 359 4762 6556 6992 -266 -568 -1691 C ATOM 4681 OD1 ASN B 359 44.354 33.067 48.717 1.00 42.27 O ANISOU 4681 OD1 ASN B 359 3923 5735 6404 -294 -554 -1697 O ATOM 4682 ND2 ASN B 359 43.135 33.037 50.579 1.00 44.14 N ANISOU 4682 ND2 ASN B 359 4248 6153 6370 -272 -657 -1801 N ATOM 4683 N PHE B 360 41.700 29.513 50.498 1.00 36.56 N ANISOU 4683 N PHE B 360 3495 5346 5051 -118 -638 -1429 N ATOM 4684 CA PHE B 360 41.819 28.915 51.823 1.00 35.55 C ANISOU 4684 CA PHE B 360 3368 5377 4763 -92 -750 -1438 C ATOM 4685 C PHE B 360 41.993 27.398 51.817 1.00 37.28 C ANISOU 4685 C PHE B 360 3611 5644 4908 -33 -777 -1283 C ATOM 4686 O PHE B 360 42.584 26.869 52.754 1.00 37.40 O ANISOU 4686 O PHE B 360 3591 5776 4842 -9 -885 -1273 O ATOM 4687 CB PHE B 360 40.637 29.340 52.724 1.00 37.58 C ANISOU 4687 CB PHE B 360 3698 5711 4869 -99 -749 -1509 C ATOM 4688 CG PHE B 360 40.712 30.797 53.127 1.00 39.64 C ANISOU 4688 CG PHE B 360 3914 5954 5192 -153 -760 -1691 C ATOM 4689 CD1 PHE B 360 41.695 31.247 54.006 1.00 42.80 C ANISOU 4689 CD1 PHE B 360 4228 6436 5599 -177 -871 -1812 C ATOM 4690 CD2 PHE B 360 39.817 31.726 52.611 1.00 42.33 C ANISOU 4690 CD2 PHE B 360 4292 6192 5598 -180 -664 -1745 C ATOM 4691 CE1 PHE B 360 41.791 32.605 54.344 1.00 43.81 C ANISOU 4691 CE1 PHE B 360 4308 6534 5803 -231 -881 -1992 C ATOM 4692 CE2 PHE B 360 39.909 33.083 52.958 1.00 44.92 C ANISOU 4692 CE2 PHE B 360 4574 6486 6008 -229 -672 -1915 C ATOM 4693 CZ PHE B 360 40.896 33.513 53.818 1.00 42.36 C ANISOU 4693 CZ PHE B 360 4164 6236 5693 -256 -778 -2043 C ATOM 4694 N LEU B 361 41.499 26.696 50.791 1.00 32.03 N ANISOU 4694 N LEU B 361 3004 4893 4272 -8 -686 -1165 N ATOM 4695 CA LEU B 361 41.553 25.234 50.776 1.00 31.76 C ANISOU 4695 CA LEU B 361 2999 4890 4179 47 -703 -1022 C ATOM 4696 C LEU B 361 42.509 24.621 49.719 1.00 34.66 C ANISOU 4696 C LEU B 361 3310 5167 4691 69 -675 -949 C ATOM 4697 O LEU B 361 42.571 23.392 49.596 1.00 34.30 O ANISOU 4697 O LEU B 361 3283 5126 4621 117 -681 -833 O ATOM 4698 CB LEU B 361 40.128 24.657 50.648 1.00 32.18 C ANISOU 4698 CB LEU B 361 3166 4935 4126 66 -633 -941 C ATOM 4699 CG LEU B 361 39.164 24.967 51.817 1.00 35.82 C ANISOU 4699 CG LEU B 361 3684 5505 4422 56 -659 -990 C ATOM 4700 CD1 LEU B 361 37.749 24.645 51.447 1.00 35.55 C ANISOU 4700 CD1 LEU B 361 3746 5433 4330 63 -569 -927 C ATOM 4701 CD2 LEU B 361 39.544 24.208 53.059 1.00 37.08 C ANISOU 4701 CD2 LEU B 361 3834 5809 4445 88 -766 -948 C ATOM 4702 N SER B 362 43.278 25.469 49.004 1.00 30.12 N ANISOU 4702 N SER B 362 2660 4511 4272 33 -641 -1017 N ATOM 4703 CA SER B 362 44.286 25.042 48.036 1.00 29.97 C ANISOU 4703 CA SER B 362 2574 4414 4397 48 -606 -967 C ATOM 4704 C SER B 362 45.540 25.879 48.216 1.00 33.68 C ANISOU 4704 C SER B 362 2918 4885 4995 12 -656 -1065 C ATOM 4705 O SER B 362 45.531 27.078 47.955 1.00 34.05 O ANISOU 4705 O SER B 362 2942 4877 5119 -43 -617 -1156 O ATOM 4706 CB SER B 362 43.765 25.144 46.606 1.00 33.81 C ANISOU 4706 CB SER B 362 3116 4777 4954 38 -470 -924 C ATOM 4707 OG SER B 362 44.819 24.999 45.667 1.00 41.32 O ANISOU 4707 OG SER B 362 3991 5655 6052 41 -423 -903 O ATOM 4708 N GLY B 363 46.606 25.231 48.656 1.00 31.26 N ANISOU 4708 N GLY B 363 2523 4633 4720 43 -744 -1041 N ATOM 4709 CA GLY B 363 47.915 25.850 48.833 1.00 30.69 C ANISOU 4709 CA GLY B 363 2312 4565 4783 14 -804 -1125 C ATOM 4710 C GLY B 363 48.511 26.330 47.528 1.00 35.49 C ANISOU 4710 C GLY B 363 2862 5043 5578 -16 -690 -1131 C ATOM 4711 O GLY B 363 49.242 27.322 47.508 1.00 37.48 O ANISOU 4711 O GLY B 363 3019 5267 5956 -68 -698 -1225 O ATOM 4712 N LYS B 364 48.168 25.648 46.425 1.00 31.42 N ANISOU 4712 N LYS B 364 2409 4451 5080 14 -580 -1032 N ATOM 4713 CA LYS B 364 48.624 25.959 45.067 1.00 30.61 C ANISOU 4713 CA LYS B 364 2273 4232 5126 -8 -453 -1017 C ATOM 4714 C LYS B 364 48.020 27.262 44.564 1.00 32.72 C ANISOU 4714 C LYS B 364 2578 4425 5426 -72 -370 -1076 C ATOM 4715 O LYS B 364 48.764 28.113 44.086 1.00 32.73 O ANISOU 4715 O LYS B 364 2496 4364 5577 -119 -325 -1125 O ATOM 4716 CB LYS B 364 48.346 24.786 44.113 1.00 33.07 C ANISOU 4716 CB LYS B 364 2649 4497 5417 46 -368 -903 C ATOM 4717 CG LYS B 364 49.268 23.592 44.341 1.00 43.98 C ANISOU 4717 CG LYS B 364 3956 5913 6841 108 -426 -847 C ATOM 4718 CD LYS B 364 49.479 22.810 43.051 1.00 62.66 C ANISOU 4718 CD LYS B 364 6336 8196 9275 142 -308 -775 C ATOM 4719 CE LYS B 364 50.148 21.473 43.274 1.00 74.19 C ANISOU 4719 CE LYS B 364 7740 9678 10771 214 -358 -711 C ATOM 4720 NZ LYS B 364 50.232 20.701 42.004 1.00 81.54 N ANISOU 4720 NZ LYS B 364 8696 10526 11760 248 -235 -657 N ATOM 4721 N PHE B 365 46.685 27.443 44.714 1.00 28.18 N ANISOU 4721 N PHE B 365 2125 3858 4725 -75 -352 -1071 N ATOM 4722 CA PHE B 365 45.999 28.686 44.341 1.00 27.11 C ANISOU 4722 CA PHE B 365 2029 3652 4618 -128 -285 -1125 C ATOM 4723 C PHE B 365 46.409 29.814 45.290 1.00 32.38 C ANISOU 4723 C PHE B 365 2618 4347 5337 -180 -364 -1258 C ATOM 4724 O PHE B 365 46.704 30.912 44.824 1.00 34.02 O ANISOU 4724 O PHE B 365 2779 4470 5677 -234 -310 -1312 O ATOM 4725 CB PHE B 365 44.461 28.507 44.305 1.00 28.21 C ANISOU 4725 CB PHE B 365 2307 3797 4615 -111 -253 -1086 C ATOM 4726 CG PHE B 365 43.900 27.923 43.021 1.00 28.55 C ANISOU 4726 CG PHE B 365 2431 3772 4646 -86 -144 -982 C ATOM 4727 CD1 PHE B 365 43.871 28.676 41.842 1.00 30.55 C ANISOU 4727 CD1 PHE B 365 2692 3924 4993 -118 -36 -969 C ATOM 4728 CD2 PHE B 365 43.366 26.636 42.998 1.00 28.50 C ANISOU 4728 CD2 PHE B 365 2493 3803 4531 -32 -151 -899 C ATOM 4729 CE1 PHE B 365 43.343 28.139 40.661 1.00 30.74 C ANISOU 4729 CE1 PHE B 365 2793 3900 4988 -95 57 -880 C ATOM 4730 CE2 PHE B 365 42.825 26.108 41.820 1.00 30.37 C ANISOU 4730 CE2 PHE B 365 2804 3980 4755 -12 -58 -820 C ATOM 4731 CZ PHE B 365 42.819 26.862 40.660 1.00 28.67 C ANISOU 4731 CZ PHE B 365 2597 3678 4618 -43 43 -814 C ATOM 4732 N ARG B 366 46.502 29.532 46.608 1.00 29.61 N ANISOU 4732 N ARG B 366 2247 4115 4888 -164 -493 -1309 N ATOM 4733 CA ARG B 366 46.904 30.511 47.627 1.00 30.22 C ANISOU 4733 CA ARG B 366 2249 4239 4995 -210 -585 -1451 C ATOM 4734 C ARG B 366 48.246 31.166 47.280 1.00 36.73 C ANISOU 4734 C ARG B 366 2930 5002 6023 -256 -584 -1509 C ATOM 4735 O ARG B 366 48.388 32.378 47.390 1.00 37.57 O ANISOU 4735 O ARG B 366 2988 5058 6230 -317 -580 -1619 O ATOM 4736 CB ARG B 366 46.972 29.846 49.006 1.00 29.99 C ANISOU 4736 CB ARG B 366 2216 4365 4814 -174 -728 -1472 C ATOM 4737 CG ARG B 366 47.137 30.817 50.172 1.00 32.20 C ANISOU 4737 CG ARG B 366 2444 4717 5072 -218 -830 -1632 C ATOM 4738 CD ARG B 366 47.034 30.185 51.556 1.00 42.83 C ANISOU 4738 CD ARG B 366 3819 6232 6221 -181 -960 -1646 C ATOM 4739 NE ARG B 366 47.469 28.786 51.660 1.00 54.13 N ANISOU 4739 NE ARG B 366 5241 7737 7590 -116 -1019 -1520 N ATOM 4740 CZ ARG B 366 46.661 27.737 51.788 1.00 68.92 C ANISOU 4740 CZ ARG B 366 7215 9648 9323 -60 -1000 -1395 C ATOM 4741 NH1 ARG B 366 45.346 27.898 51.782 1.00 55.16 N ANISOU 4741 NH1 ARG B 366 5590 7882 7486 -62 -919 -1375 N ATOM 4742 NH2 ARG B 366 47.161 26.516 51.893 1.00 58.11 N ANISOU 4742 NH2 ARG B 366 5823 8333 7923 -3 -1060 -1286 N ATOM 4743 N GLU B 367 49.214 30.352 46.846 1.00 34.28 N ANISOU 4743 N GLU B 367 2549 4691 5784 -226 -583 -1437 N ATOM 4744 CA GLU B 367 50.559 30.751 46.441 1.00 34.30 C ANISOU 4744 CA GLU B 367 2406 4640 5987 -261 -572 -1471 C ATOM 4745 C GLU B 367 50.506 31.705 45.238 1.00 37.57 C ANISOU 4745 C GLU B 367 2818 4910 6548 -316 -425 -1468 C ATOM 4746 O GLU B 367 51.254 32.681 45.192 1.00 36.89 O ANISOU 4746 O GLU B 367 2625 4766 6624 -379 -421 -1550 O ATOM 4747 CB GLU B 367 51.327 29.484 46.073 1.00 35.81 C ANISOU 4747 CB GLU B 367 2550 4854 6201 -201 -573 -1369 C ATOM 4748 CG GLU B 367 52.817 29.630 45.938 1.00 52.40 C ANISOU 4748 CG GLU B 367 4478 6946 8484 -220 -609 -1409 C ATOM 4749 CD GLU B 367 53.501 28.281 45.975 1.00 85.64 C ANISOU 4749 CD GLU B 367 8641 11207 12691 -146 -650 -1321 C ATOM 4750 OE1 GLU B 367 53.353 27.519 44.993 1.00 68.35 O ANISOU 4750 OE1 GLU B 367 6504 8962 10504 -107 -540 -1218 O ATOM 4751 OE2 GLU B 367 54.161 27.972 46.995 1.00 95.10 O ANISOU 4751 OE2 GLU B 367 9751 12501 13881 -125 -795 -1356 O ATOM 4752 N GLN B 368 49.611 31.427 44.280 1.00 34.46 N ANISOU 4752 N GLN B 368 2542 4457 6094 -293 -309 -1369 N ATOM 4753 CA GLN B 368 49.444 32.220 43.065 1.00 34.82 C ANISOU 4753 CA GLN B 368 2607 4374 6248 -335 -166 -1336 C ATOM 4754 C GLN B 368 48.771 33.566 43.355 1.00 39.96 C ANISOU 4754 C GLN B 368 3284 4970 6929 -391 -161 -1424 C ATOM 4755 O GLN B 368 49.252 34.600 42.879 1.00 40.12 O ANISOU 4755 O GLN B 368 3236 4892 7117 -452 -101 -1459 O ATOM 4756 CB GLN B 368 48.678 31.415 41.998 1.00 36.34 C ANISOU 4756 CB GLN B 368 2919 4539 6348 -287 -61 -1206 C ATOM 4757 CG GLN B 368 49.434 30.176 41.477 1.00 34.07 C ANISOU 4757 CG GLN B 368 2598 4276 6071 -235 -37 -1125 C ATOM 4758 CD GLN B 368 50.793 30.511 40.897 1.00 47.96 C ANISOU 4758 CD GLN B 368 4219 5983 8022 -268 18 -1135 C ATOM 4759 OE1 GLN B 368 50.954 31.417 40.060 1.00 42.64 O ANISOU 4759 OE1 GLN B 368 3524 5216 7461 -320 123 -1130 O ATOM 4760 NE2 GLN B 368 51.805 29.792 41.342 1.00 33.80 N ANISOU 4760 NE2 GLN B 368 2322 4245 6274 -238 -52 -1144 N ATOM 4761 N PHE B 369 47.689 33.555 44.172 1.00 35.55 N ANISOU 4761 N PHE B 369 2817 4473 6217 -372 -224 -1462 N ATOM 4762 CA PHE B 369 46.975 34.763 44.588 1.00 34.36 C ANISOU 4762 CA PHE B 369 2692 4278 6084 -417 -228 -1560 C ATOM 4763 C PHE B 369 47.906 35.652 45.412 1.00 38.02 C ANISOU 4763 C PHE B 369 3025 4746 6675 -475 -311 -1708 C ATOM 4764 O PHE B 369 47.937 36.859 45.186 1.00 36.93 O ANISOU 4764 O PHE B 369 2850 4502 6679 -534 -267 -1775 O ATOM 4765 CB PHE B 369 45.701 34.409 45.374 1.00 36.21 C ANISOU 4765 CB PHE B 369 3041 4597 6121 -378 -278 -1574 C ATOM 4766 CG PHE B 369 44.667 33.541 44.679 1.00 37.41 C ANISOU 4766 CG PHE B 369 3320 4750 6145 -324 -210 -1442 C ATOM 4767 CD1 PHE B 369 44.551 33.534 43.291 1.00 40.23 C ANISOU 4767 CD1 PHE B 369 3712 5009 6566 -323 -89 -1338 C ATOM 4768 CD2 PHE B 369 43.780 32.763 45.415 1.00 37.97 C ANISOU 4768 CD2 PHE B 369 3475 4923 6030 -278 -265 -1427 C ATOM 4769 CE1 PHE B 369 43.581 32.750 42.662 1.00 40.51 C ANISOU 4769 CE1 PHE B 369 3861 5048 6482 -277 -36 -1231 C ATOM 4770 CE2 PHE B 369 42.803 31.989 44.781 1.00 39.44 C ANISOU 4770 CE2 PHE B 369 3771 5103 6113 -235 -204 -1314 C ATOM 4771 CZ PHE B 369 42.704 31.996 43.415 1.00 37.45 C ANISOU 4771 CZ PHE B 369 3549 4753 5928 -235 -95 -1224 C ATOM 4772 N LYS B 370 48.719 35.045 46.311 1.00 36.22 N ANISOU 4772 N LYS B 370 2720 4632 6410 -459 -432 -1755 N ATOM 4773 CA LYS B 370 49.698 35.765 47.141 1.00 37.10 C ANISOU 4773 CA LYS B 370 2696 4765 6635 -512 -532 -1902 C ATOM 4774 C LYS B 370 50.729 36.471 46.243 1.00 45.03 C ANISOU 4774 C LYS B 370 3581 5640 7887 -571 -451 -1901 C ATOM 4775 O LYS B 370 51.032 37.635 46.476 1.00 44.71 O ANISOU 4775 O LYS B 370 3465 5532 7991 -641 -461 -2020 O ATOM 4776 CB LYS B 370 50.370 34.819 48.160 1.00 38.80 C ANISOU 4776 CB LYS B 370 2855 5136 6750 -471 -679 -1922 C ATOM 4777 CG LYS B 370 51.236 35.523 49.191 1.00 51.59 C ANISOU 4777 CG LYS B 370 4347 6808 8445 -522 -810 -2091 C ATOM 4778 CD LYS B 370 51.755 34.567 50.253 1.00 64.36 C ANISOU 4778 CD LYS B 370 5925 8595 9933 -473 -966 -2096 C ATOM 4779 CE LYS B 370 52.660 35.267 51.238 1.00 79.93 C ANISOU 4779 CE LYS B 370 7766 10631 11972 -522 -1109 -2268 C ATOM 4780 NZ LYS B 370 53.157 34.337 52.286 1.00 87.58 N ANISOU 4780 NZ LYS B 370 8697 11773 12808 -469 -1269 -2256 N ATOM 4781 N ALA B 371 51.207 35.782 45.188 1.00 44.67 N ANISOU 4781 N ALA B 371 3523 5558 7893 -546 -360 -1768 N ATOM 4782 CA ALA B 371 52.153 36.319 44.204 1.00 46.19 C ANISOU 4782 CA ALA B 371 3610 5633 8305 -597 -259 -1741 C ATOM 4783 C ALA B 371 51.522 37.464 43.392 1.00 50.74 C ANISOU 4783 C ALA B 371 4239 6064 8976 -647 -132 -1724 C ATOM 4784 O ALA B 371 52.196 38.441 43.098 1.00 50.28 O ANISOU 4784 O ALA B 371 4080 5903 9122 -717 -85 -1769 O ATOM 4785 CB ALA B 371 52.626 35.210 43.272 1.00 47.07 C ANISOU 4785 CB ALA B 371 3719 5753 8411 -546 -183 -1602 C ATOM 4786 N ALA B 372 50.235 37.331 43.032 1.00 48.53 N ANISOU 4786 N ALA B 372 4112 5773 8555 -611 -78 -1655 N ATOM 4787 CA ALA B 372 49.467 38.330 42.278 1.00 48.44 C ANISOU 4787 CA ALA B 372 4165 5632 8609 -644 32 -1622 C ATOM 4788 C ALA B 372 49.351 39.638 43.039 1.00 53.10 C ANISOU 4788 C ALA B 372 4706 6162 9308 -706 -18 -1773 C ATOM 4789 O ALA B 372 49.627 40.679 42.458 1.00 52.86 O ANISOU 4789 O ALA B 372 4623 5995 9464 -767 62 -1777 O ATOM 4790 CB ALA B 372 48.083 37.795 41.931 1.00 48.67 C ANISOU 4790 CB ALA B 372 4359 5686 8449 -584 69 -1530 C ATOM 4791 N PHE B 373 49.015 39.585 44.339 1.00 51.00 N ANISOU 4791 N PHE B 373 4450 5997 8932 -694 -148 -1900 N ATOM 4792 CA PHE B 373 48.875 40.778 45.175 1.00 52.10 C ANISOU 4792 CA PHE B 373 4546 6093 9158 -750 -205 -2069 C ATOM 4793 C PHE B 373 50.195 41.324 45.737 1.00 59.65 C ANISOU 4793 C PHE B 373 5333 7039 10292 -817 -280 -2203 C ATOM 4794 O PHE B 373 50.258 42.518 46.016 1.00 60.38 O ANISOU 4794 O PHE B 373 5368 7036 10535 -881 -284 -2327 O ATOM 4795 CB PHE B 373 47.865 40.552 46.308 1.00 53.84 C ANISOU 4795 CB PHE B 373 4855 6431 9173 -709 -300 -2156 C ATOM 4796 CG PHE B 373 46.458 40.228 45.859 1.00 55.76 C ANISOU 4796 CG PHE B 373 5252 6667 9268 -655 -230 -2054 C ATOM 4797 CD1 PHE B 373 45.691 41.173 45.182 1.00 58.56 C ANISOU 4797 CD1 PHE B 373 5654 6880 9717 -676 -131 -2031 C ATOM 4798 CD2 PHE B 373 45.880 38.996 46.156 1.00 57.93 C ANISOU 4798 CD2 PHE B 373 5618 7074 9317 -584 -269 -1982 C ATOM 4799 CE1 PHE B 373 44.394 40.874 44.770 1.00 59.31 C ANISOU 4799 CE1 PHE B 373 5881 6973 9682 -625 -76 -1940 C ATOM 4800 CE2 PHE B 373 44.583 38.695 45.738 1.00 60.51 C ANISOU 4800 CE2 PHE B 373 6077 7395 9521 -539 -207 -1894 C ATOM 4801 CZ PHE B 373 43.844 39.643 45.064 1.00 58.70 C ANISOU 4801 CZ PHE B 373 5887 7031 9384 -559 -115 -1878 C ATOM 4802 N SER B 374 51.231 40.475 45.915 1.00 58.15 N ANISOU 4802 N SER B 374 5057 6941 10097 -802 -342 -2185 N ATOM 4803 CA SER B 374 52.533 40.886 46.479 1.00 58.81 C ANISOU 4803 CA SER B 374 4967 7030 10347 -862 -427 -2311 C ATOM 4804 C SER B 374 53.578 41.279 45.455 1.00 64.40 C ANISOU 4804 C SER B 374 5558 7608 11304 -918 -321 -2252 C ATOM 4805 O SER B 374 54.485 42.034 45.782 1.00 64.83 O ANISOU 4805 O SER B 374 5475 7600 11558 -994 -354 -2371 O ATOM 4806 CB SER B 374 53.129 39.781 47.351 1.00 63.23 C ANISOU 4806 CB SER B 374 5480 7765 10779 -813 -567 -2328 C ATOM 4807 OG SER B 374 52.221 39.321 48.337 1.00 78.47 O ANISOU 4807 OG SER B 374 7517 9834 12465 -758 -666 -2366 O ATOM 4808 N TRP B 375 53.480 40.739 44.234 1.00 62.60 N ANISOU 4808 N TRP B 375 5379 7347 11060 -882 -195 -2073 N ATOM 4809 CA TRP B 375 54.495 40.947 43.213 1.00 63.47 C ANISOU 4809 CA TRP B 375 5385 7358 11374 -924 -80 -1994 C ATOM 4810 C TRP B 375 53.961 41.370 41.837 1.00 70.34 C ANISOU 4810 C TRP B 375 6337 8091 12297 -935 104 -1850 C ATOM 4811 O TRP B 375 54.358 42.427 41.353 1.00 69.58 O ANISOU 4811 O TRP B 375 6168 7854 12413 -1011 184 -1863 O ATOM 4812 CB TRP B 375 55.339 39.668 43.113 1.00 62.12 C ANISOU 4812 CB TRP B 375 5161 7295 11146 -868 -105 -1920 C ATOM 4813 CG TRP B 375 56.671 39.828 42.457 1.00 63.28 C ANISOU 4813 CG TRP B 375 5147 7378 11519 -915 -34 -1894 C ATOM 4814 CD1 TRP B 375 57.795 40.377 43.002 1.00 66.12 C ANISOU 4814 CD1 TRP B 375 5325 7722 12074 -982 -107 -2016 C ATOM 4815 CD2 TRP B 375 57.052 39.317 41.174 1.00 63.26 C ANISOU 4815 CD2 TRP B 375 5144 7328 11563 -898 124 -1739 C ATOM 4816 NE1 TRP B 375 58.839 40.295 42.111 1.00 65.70 N ANISOU 4816 NE1 TRP B 375 5154 7608 12202 -1009 3 -1941 N ATOM 4817 CE2 TRP B 375 58.413 39.639 40.983 1.00 67.08 C ANISOU 4817 CE2 TRP B 375 5439 7765 12282 -957 149 -1772 C ATOM 4818 CE3 TRP B 375 56.363 38.638 40.150 1.00 64.54 C ANISOU 4818 CE3 TRP B 375 5446 7486 11591 -840 247 -1583 C ATOM 4819 CZ2 TRP B 375 59.099 39.316 39.806 1.00 66.33 C ANISOU 4819 CZ2 TRP B 375 5293 7622 12289 -958 305 -1650 C ATOM 4820 CZ3 TRP B 375 57.047 38.312 38.990 1.00 65.97 C ANISOU 4820 CZ3 TRP B 375 5580 7623 11861 -840 394 -1469 C ATOM 4821 CH2 TRP B 375 58.399 38.646 38.827 1.00 66.59 C ANISOU 4821 CH2 TRP B 375 5472 7658 12171 -898 427 -1502 C ATOM 4822 N TRP B 376 53.080 40.559 41.211 1.00 70.04 N ANISOU 4822 N TRP B 376 6448 8092 12072 -862 168 -1713 N ATOM 4823 CA TRP B 376 52.544 40.808 39.868 1.00 71.55 C ANISOU 4823 CA TRP B 376 6728 8178 12278 -862 333 -1563 C ATOM 4824 C TRP B 376 51.834 42.159 39.723 1.00 75.51 C ANISOU 4824 C TRP B 376 7267 8542 12883 -914 382 -1589 C ATOM 4825 O TRP B 376 52.329 42.997 38.963 1.00 74.16 O ANISOU 4825 O TRP B 376 7033 8240 12905 -975 492 -1540 O ATOM 4826 CB TRP B 376 51.651 39.653 39.400 1.00 71.53 C ANISOU 4826 CB TRP B 376 6880 8256 12041 -774 365 -1439 C ATOM 4827 CG TRP B 376 52.383 38.361 39.192 1.00 73.60 C ANISOU 4827 CG TRP B 376 7110 8615 12239 -723 363 -1379 C ATOM 4828 CD1 TRP B 376 52.299 37.237 39.962 1.00 76.67 C ANISOU 4828 CD1 TRP B 376 7527 9138 12467 -657 253 -1401 C ATOM 4829 CD2 TRP B 376 53.319 38.062 38.142 1.00 74.01 C ANISOU 4829 CD2 TRP B 376 7094 8633 12394 -732 483 -1286 C ATOM 4830 NE1 TRP B 376 53.124 36.255 39.460 1.00 76.52 N ANISOU 4830 NE1 TRP B 376 7456 9161 12456 -622 290 -1332 N ATOM 4831 CE2 TRP B 376 53.763 36.734 38.342 1.00 78.11 C ANISOU 4831 CE2 TRP B 376 7598 9265 12815 -666 434 -1266 C ATOM 4832 CE3 TRP B 376 53.832 38.792 37.052 1.00 75.59 C ANISOU 4832 CE3 TRP B 376 7241 8717 12762 -788 633 -1214 C ATOM 4833 CZ2 TRP B 376 54.695 36.119 37.493 1.00 77.55 C ANISOU 4833 CZ2 TRP B 376 7458 9194 12813 -653 530 -1191 C ATOM 4834 CZ3 TRP B 376 54.749 38.180 36.208 1.00 77.27 C ANISOU 4834 CZ3 TRP B 376 7390 8940 13029 -779 733 -1134 C ATOM 4835 CH2 TRP B 376 55.163 36.856 36.425 1.00 77.95 C ANISOU 4835 CH2 TRP B 376 7460 9139 13017 -710 683 -1129 C ATOM 4836 N LEU B 377 50.692 42.373 40.444 1.00 72.93 N ANISOU 4836 N LEU B 377 7036 8238 12434 -889 308 -1659 N ATOM 4837 CA LEU B 377 49.915 43.627 40.424 1.00 73.11 C ANISOU 4837 CA LEU B 377 7096 8130 12552 -927 344 -1694 C ATOM 4838 C LEU B 377 50.721 44.837 40.933 1.00 79.94 C ANISOU 4838 C LEU B 377 7815 8888 13671 -1019 317 -1836 C ATOM 4839 O LEU B 377 50.734 45.837 40.211 1.00 79.48 O ANISOU 4839 O LEU B 377 7735 8669 13793 -1071 423 -1783 O ATOM 4840 CB LEU B 377 48.557 43.516 41.145 1.00 72.76 C ANISOU 4840 CB LEU B 377 7177 8145 12323 -875 272 -1748 C ATOM 4841 CG LEU B 377 47.538 42.543 40.549 1.00 76.67 C ANISOU 4841 CG LEU B 377 7823 8712 12595 -793 311 -1606 C ATOM 4842 CD1 LEU B 377 46.452 42.193 41.559 1.00 76.10 C ANISOU 4842 CD1 LEU B 377 7842 8738 12337 -744 214 -1688 C ATOM 4843 CD2 LEU B 377 46.948 43.073 39.254 1.00 79.00 C ANISOU 4843 CD2 LEU B 377 8191 8885 12941 -794 450 -1453 C ATOM 4844 N PRO B 378 51.463 44.784 42.086 1.00 79.10 N ANISOU 4844 N PRO B 378 7598 8859 13596 -1045 183 -2006 N ATOM 4845 CA PRO B 378 52.285 45.949 42.481 1.00 79.96 C ANISOU 4845 CA PRO B 378 7558 8857 13966 -1141 161 -2146 C ATOM 4846 C PRO B 378 53.317 46.367 41.423 1.00 87.31 C ANISOU 4846 C PRO B 378 8378 9664 15132 -1204 286 -2049 C ATOM 4847 O PRO B 378 53.644 47.551 41.322 1.00 87.20 O ANISOU 4847 O PRO B 378 8275 9497 15360 -1286 327 -2107 O ATOM 4848 CB PRO B 378 52.981 45.477 43.763 1.00 81.38 C ANISOU 4848 CB PRO B 378 7647 9184 14089 -1141 -11 -2315 C ATOM 4849 CG PRO B 378 52.144 44.401 44.279 1.00 85.25 C ANISOU 4849 CG PRO B 378 8270 9836 14284 -1050 -86 -2296 C ATOM 4850 CD PRO B 378 51.594 43.699 43.083 1.00 80.76 C ANISOU 4850 CD PRO B 378 7813 9259 13613 -992 41 -2080 C ATOM 4851 N GLY B 379 53.803 45.393 40.651 1.00 86.21 N ANISOU 4851 N GLY B 379 8243 9588 14922 -1166 353 -1903 N ATOM 4852 CA GLY B 379 54.762 45.606 39.573 1.00 87.30 C ANISOU 4852 CA GLY B 379 8288 9633 15249 -1215 490 -1790 C ATOM 4853 C GLY B 379 54.148 46.256 38.352 1.00 94.29 C ANISOU 4853 C GLY B 379 9262 10377 16187 -1227 656 -1629 C ATOM 4854 O GLY B 379 54.772 47.130 37.744 1.00 93.50 O ANISOU 4854 O GLY B 379 9072 10134 16321 -1303 761 -1587 O ATOM 4855 N LEU B 380 52.910 45.824 37.988 1.00 93.52 N ANISOU 4855 N LEU B 380 9340 10321 15874 -1152 678 -1532 N ATOM 4856 CA LEU B 380 52.124 46.364 36.870 1.00 94.38 C ANISOU 4856 CA LEU B 380 9556 10316 15987 -1146 815 -1372 C ATOM 4857 C LEU B 380 51.702 47.802 37.201 1.00 99.27 C ANISOU 4857 C LEU B 380 10153 10772 16793 -1206 812 -1450 C ATOM 4858 O LEU B 380 51.776 48.668 36.326 1.00 99.04 O ANISOU 4858 O LEU B 380 10109 10590 16929 -1253 937 -1342 O ATOM 4859 CB LEU B 380 50.893 45.481 36.580 1.00 94.79 C ANISOU 4859 CB LEU B 380 9788 10469 15758 -1050 806 -1282 C ATOM 4860 CG LEU B 380 49.942 45.967 35.480 1.00100.06 C ANISOU 4860 CG LEU B 380 10576 11048 16393 -1031 934 -1103 C ATOM 4861 CD1 LEU B 380 50.634 46.013 34.134 1.00100.46 C ANISOU 4861 CD1 LEU B 380 10717 11201 16254 -967 1006 -949 C ATOM 4862 CD2 LEU B 380 48.687 45.103 35.417 1.00102.61 C ANISOU 4862 CD2 LEU B 380 11007 11341 16639 -997 877 -1142 C ATOM 4863 N ALA B 381 51.302 48.051 38.475 1.00 96.55 N ANISOU 4863 N ALA B 381 9800 10459 16425 -1205 673 -1638 N ATOM 4864 CA ALA B 381 50.910 49.368 38.994 1.00 96.87 C ANISOU 4864 CA ALA B 381 9811 10354 16642 -1258 650 -1756 C ATOM 4865 C ALA B 381 52.093 50.346 38.926 1.00102.43 C ANISOU 4865 C ALA B 381 10342 10914 17662 -1365 690 -1815 C ATOM 4866 O ALA B 381 51.893 51.527 38.629 1.00102.47 O ANISOU 4866 O ALA B 381 10326 10735 17874 -1419 756 -1807 O ATOM 4867 CB ALA B 381 50.414 49.243 40.426 1.00 97.50 C ANISOU 4867 CB ALA B 381 9907 10534 16604 -1233 489 -1963 C ATOM 4868 N ALA B 382 53.323 49.838 39.173 1.00 99.49 N ANISOU 4868 N ALA B 382 9843 10620 17338 -1396 653 -1866 N ATOM 4869 CA ALA B 382 54.571 50.599 39.104 1.00 99.33 C ANISOU 4869 CA ALA B 382 9641 10484 17617 -1499 688 -1921 C ATOM 4870 C ALA B 382 54.895 50.968 37.649 1.00103.27 C ANISOU 4870 C ALA B 382 10130 10852 18256 -1534 883 -1704 C ATOM 4871 O ALA B 382 55.465 52.032 37.407 1.00103.13 O ANISOU 4871 O ALA B 382 9998 10666 18522 -1626 951 -1714 O ATOM 4872 CB ALA B 382 55.709 49.790 39.703 1.00100.08 C ANISOU 4872 CB ALA B 382 9610 10721 17694 -1506 588 -2020 C ATOM 4873 N ALA B 383 54.514 50.094 36.689 1.00 99.49 N ANISOU 4873 N ALA B 383 9772 10451 17578 -1462 974 -1508 N ATOM 4874 CA ALA B 383 54.721 50.297 35.254 1.00123.18 C ANISOU 4874 CA ALA B 383 12789 13362 20651 -1481 1162 -1287 C ATOM 4875 C ALA B 383 53.499 50.960 34.621 1.00150.59 C ANISOU 4875 C ALA B 383 16408 16730 24078 -1453 1239 -1154 C ATOM 4876 O ALA B 383 53.025 51.986 35.108 1.00111.26 O ANISOU 4876 O ALA B 383 11421 11615 19235 -1486 1208 -1231 O ATOM 4877 CB ALA B 383 54.999 48.966 34.576 1.00123.85 C ANISOU 4877 CB ALA B 383 12913 13603 20541 -1418 1213 -1168 C TER 4878 ALA B 383 HETATM 4879 C10 7MA A 401 10.897 4.691 32.774 0.88 32.66 C HETATM 4880 C13 7MA A 401 11.299 -0.066 36.691 0.88 37.18 C HETATM 4881 C15 7MA A 401 11.562 -1.735 34.703 0.88 39.54 C HETATM 4882 C20 7MA A 401 10.829 -2.970 34.641 0.88 39.85 C HETATM 4883 C22 7MA A 401 11.491 -2.586 29.847 0.88 37.77 C HETATM 4884 C26 7MA A 401 13.479 -3.464 36.734 0.88 45.90 C HETATM 4885 C28 7MA A 401 12.487 -5.119 38.223 0.88 43.65 C HETATM 4886 C32 7MA A 401 14.437 -4.179 34.453 0.88 38.89 C HETATM 4887 C31 7MA A 401 13.774 -4.447 35.786 0.88 42.47 C HETATM 4888 C30 7MA A 401 13.436 -5.794 36.085 0.88 42.74 C HETATM 4889 C29 7MA A 401 12.796 -6.109 37.315 0.88 44.83 C HETATM 4890 C27 7MA A 401 12.809 -3.769 37.937 0.88 40.48 C HETATM 4891 S23 7MA A 401 13.737 -1.616 36.488 0.88 58.15 S HETATM 4892 O24 7MA A 401 14.206 -0.963 37.928 0.88 60.96 O HETATM 4893 O25 7MA A 401 14.839 -1.295 35.345 0.88 57.38 O HETATM 4894 N14 7MA A 401 12.055 -1.079 35.982 0.88 46.73 N HETATM 4895 C16 7MA A 401 12.097 -1.153 33.536 0.88 35.21 C HETATM 4896 N17 7MA A 401 11.872 -1.689 32.367 0.88 36.50 N HETATM 4897 C19 7MA A 401 10.609 -3.529 33.380 0.88 40.69 C HETATM 4898 C18 7MA A 401 11.161 -2.832 32.229 0.88 37.10 C HETATM 4899 O21 7MA A 401 10.975 -3.319 30.936 0.88 35.68 O HETATM 4900 C11 7MA A 401 10.774 1.139 35.848 0.88 36.15 C HETATM 4901 O12 7MA A 401 9.720 0.977 35.312 0.88 37.04 O HETATM 4902 N03 7MA A 401 11.498 2.374 35.687 0.88 34.40 N HETATM 4903 C02 7MA A 401 12.857 2.592 36.288 0.88 33.69 C HETATM 4904 C01 7MA A 401 12.825 3.400 37.645 0.88 34.49 C HETATM 4905 C04 7MA A 401 10.875 3.437 34.877 0.88 33.97 C HETATM 4906 C05 7MA A 401 11.291 3.550 33.424 0.88 32.83 C HETATM 4907 C09 7MA A 401 11.262 4.871 31.422 0.88 31.87 C HETATM 4908 C08 7MA A 401 12.036 3.888 30.829 0.88 31.90 C HETATM 4909 N07 7MA A 401 12.415 2.815 31.473 0.88 31.42 N HETATM 4910 C06 7MA A 401 12.083 2.607 32.776 0.88 33.42 C HETATM 4911 H1 7MA A 401 10.377 5.327 33.208 0.50 32.67 H HETATM 4912 H2 7MA A 401 10.526 -0.506 37.079 0.50 37.80 H HETATM 4913 H3 7MA A 401 11.860 0.283 37.397 0.50 36.51 H HETATM 4914 H4 7MA A 401 10.513 -3.382 35.413 0.50 39.88 H HETATM 4915 H5 7MA A 401 11.215 -3.009 29.020 0.50 38.78 H HETATM 4916 H6 7MA A 401 11.146 -1.679 29.863 0.50 37.17 H HETATM 4917 H7 7MA A 401 12.460 -2.571 29.888 0.50 37.41 H HETATM 4918 H8 7MA A 401 12.079 -5.339 39.029 0.50 43.68 H HETATM 4919 H9 7MA A 401 13.971 -3.458 34.003 0.50 38.71 H HETATM 4920 H10 7MA A 401 15.361 -3.925 34.595 0.50 38.07 H HETATM 4921 H11 7MA A 401 14.407 -4.973 33.896 0.50 39.88 H HETATM 4922 H12 7MA A 401 13.655 -6.476 35.492 0.50 42.72 H HETATM 4923 H13 7MA A 401 12.614 -6.996 37.518 0.50 44.82 H HETATM 4924 H14 7MA A 401 12.593 -3.096 38.541 0.50 40.39 H HETATM 4925 H15 7MA A 401 12.628 -0.394 33.602 0.50 35.16 H HETATM 4926 H16 7MA A 401 10.101 -4.301 33.276 0.50 40.74 H HETATM 4927 H17 7MA A 401 13.378 3.100 35.650 0.50 33.01 H HETATM 4928 H18 7MA A 401 13.301 1.743 36.435 0.50 34.37 H HETATM 4929 H19 7MA A 401 13.541 4.054 37.648 0.50 34.18 H HETATM 4930 H20 7MA A 401 11.973 3.856 37.727 0.50 33.99 H HETATM 4931 H21 7MA A 401 12.939 2.790 38.391 0.50 35.32 H HETATM 4932 H22 7MA A 401 9.911 3.347 34.900 0.50 34.56 H HETATM 4933 H23 7MA A 401 11.109 4.278 35.301 0.50 33.40 H HETATM 4934 H24 7MA A 401 11.007 5.628 30.949 0.50 31.87 H HETATM 4935 H25 7MA A 401 12.297 3.993 29.946 0.50 31.92 H HETATM 4936 H26 7MA A 401 12.365 1.840 33.213 0.50 33.49 H HETATM 4937 S SO4 A 402 19.629 8.190 2.302 1.00 95.48 S HETATM 4938 O1 SO4 A 402 20.395 8.638 1.131 1.00 98.19 O HETATM 4939 O2 SO4 A 402 18.220 8.016 1.924 1.00 92.99 O HETATM 4940 O3 SO4 A 402 19.715 9.170 3.382 1.00 94.91 O HETATM 4941 O4 SO4 A 402 20.205 6.928 2.764 1.00 95.45 O HETATM 4942 O1 PG4 A 403 2.272 -0.598 44.338 1.00 60.23 O HETATM 4943 C1 PG4 A 403 2.220 -1.896 43.724 1.00 56.91 C HETATM 4944 C2 PG4 A 403 1.486 -1.772 42.394 1.00 54.71 C HETATM 4945 O2 PG4 A 403 2.228 -2.449 41.385 1.00 53.98 O HETATM 4946 C3 PG4 A 403 2.220 -1.786 40.124 1.00 51.17 C HETATM 4947 C4 PG4 A 403 2.831 -2.714 39.083 1.00 49.17 C HETATM 4948 O3 PG4 A 403 4.164 -2.994 39.485 1.00 50.11 O HETATM 4949 C5 PG4 A 403 4.924 -3.722 38.525 1.00 50.31 C HETATM 4950 C6 PG4 A 403 6.372 -3.840 39.008 1.00 52.79 C HETATM 4951 O4 PG4 A 403 6.438 -4.320 40.355 1.00 53.79 O HETATM 4952 C7 PG4 A 403 7.688 -4.918 40.694 1.00 54.57 C HETATM 4953 C8 PG4 A 403 7.425 -6.202 41.475 1.00 58.45 C HETATM 4954 O5 PG4 A 403 6.791 -7.187 40.640 1.00 60.07 O HETATM 4955 O1 PG4 A 404 7.446 14.770 24.856 1.00 69.91 O HETATM 4956 C1 PG4 A 404 7.140 14.283 23.533 1.00 73.17 C HETATM 4957 C2 PG4 A 404 8.183 14.719 22.492 1.00 74.16 C HETATM 4958 O2 PG4 A 404 7.774 14.394 21.152 1.00 73.25 O HETATM 4959 C3 PG4 A 404 8.881 14.094 20.300 1.00 72.97 C HETATM 4960 C4 PG4 A 404 8.461 14.143 18.831 1.00 75.06 C HETATM 4961 O3 PG4 A 404 9.590 14.434 17.992 1.00 76.98 O HETATM 4962 C5 PG4 A 404 9.237 14.744 16.641 1.00 75.50 C HETATM 4963 C6 PG4 A 404 10.017 15.961 16.154 1.00 75.13 C HETATM 4964 O4 PG4 A 404 9.116 17.053 15.908 1.00 75.40 O HETATM 4965 C7 PG4 A 404 9.492 17.857 14.782 1.00 72.95 C HETATM 4966 C8 PG4 A 404 8.324 18.724 14.318 1.00 70.33 C HETATM 4967 O5 PG4 A 404 8.281 18.785 12.885 1.00 68.67 O HETATM 4968 O1 PG4 A 405 1.509 4.527 22.807 1.00 81.73 O HETATM 4969 C1 PG4 A 405 1.143 3.272 22.264 1.00 82.64 C HETATM 4970 C2 PG4 A 405 2.276 2.591 21.554 1.00 83.17 C HETATM 4971 O2 PG4 A 405 2.597 3.271 20.345 1.00 83.33 O HETATM 4972 C3 PG4 A 405 3.753 2.744 19.705 1.00 82.95 C HETATM 4973 C4 PG4 A 405 3.869 3.307 18.323 1.00 81.31 C HETATM 4974 O3 PG4 A 405 4.981 2.721 17.656 1.00 80.02 O HETATM 4975 C5 PG4 A 405 4.987 1.301 17.744 1.00 79.98 C HETATM 4976 C6 PG4 A 405 6.225 0.754 17.114 1.00 79.73 C HETATM 4977 O4 PG4 A 405 6.280 -0.650 17.325 1.00 79.92 O HETATM 4978 C7 PG4 A 405 7.362 -1.266 16.638 1.00 80.45 C HETATM 4979 C8 PG4 A 405 7.274 -2.753 16.756 1.00 80.10 C HETATM 4980 O5 PG4 A 405 8.279 -3.406 16.015 1.00 78.44 O HETATM 4981 C1 CIT A 406 26.410 17.163 7.542 1.00 49.02 C HETATM 4982 O1 CIT A 406 25.320 17.182 6.924 1.00 48.77 O HETATM 4983 O2 CIT A 406 26.733 18.104 8.305 1.00 48.58 O HETATM 4984 C2 CIT A 406 27.367 15.990 7.336 1.00 49.85 C HETATM 4985 C3 CIT A 406 27.252 14.815 8.337 1.00 52.78 C HETATM 4986 O7 CIT A 406 27.401 15.328 9.671 1.00 55.27 O HETATM 4987 C4 CIT A 406 25.899 14.097 8.202 1.00 50.41 C HETATM 4988 C5 CIT A 406 25.373 13.378 9.436 1.00 47.20 C HETATM 4989 O3 CIT A 406 24.162 13.064 9.444 1.00 46.48 O HETATM 4990 O4 CIT A 406 26.129 13.112 10.398 1.00 46.26 O HETATM 4991 C6 CIT A 406 28.356 13.791 8.071 1.00 56.64 C HETATM 4992 O5 CIT A 406 28.347 13.180 6.968 1.00 60.79 O HETATM 4993 O6 CIT A 406 29.256 13.570 8.935 1.00 54.24 O HETATM 4994 C1 SOG A 407 24.580 -16.286 38.884 0.85 88.55 C HETATM 4995 C2 SOG A 407 23.659 -16.487 40.099 0.85 87.17 C HETATM 4996 C3 SOG A 407 22.530 -17.480 39.816 0.85 84.73 C HETATM 4997 C4 SOG A 407 21.800 -17.133 38.519 0.85 83.42 C HETATM 4998 C5 SOG A 407 22.802 -17.164 37.357 0.85 85.31 C HETATM 4999 C6 SOG A 407 22.169 -16.738 36.033 0.85 85.27 C HETATM 5000 C1' SOG A 407 26.474 -14.716 37.683 0.85 87.95 C HETATM 5001 C2' SOG A 407 27.549 -13.639 37.819 0.85 84.96 C HETATM 5002 C3' SOG A 407 27.106 -12.328 37.176 0.85 81.01 C HETATM 5003 C4' SOG A 407 27.005 -11.214 38.211 0.85 77.55 C HETATM 5004 C5' SOG A 407 27.544 -9.915 37.634 0.85 76.07 C HETATM 5005 S1 SOG A 407 25.452 -14.764 39.128 0.85 89.64 S HETATM 5006 O2 SOG A 407 24.425 -16.944 41.223 0.85 87.90 O HETATM 5007 O3 SOG A 407 21.622 -17.496 40.919 0.85 83.80 O HETATM 5008 O4 SOG A 407 20.717 -18.041 38.324 0.85 81.06 O HETATM 5009 O5 SOG A 407 23.882 -16.242 37.615 0.85 87.35 O HETATM 5010 O6 SOG A 407 21.484 -17.830 35.417 0.85 85.01 O HETATM 5011 C1 SOG A 408 17.559 4.091 50.929 1.00122.23 C HETATM 5012 C2 SOG A 408 16.420 5.062 51.251 1.00121.24 C HETATM 5013 C3 SOG A 408 16.890 6.516 51.182 1.00122.04 C HETATM 5014 C4 SOG A 408 18.190 6.780 51.961 1.00122.72 C HETATM 5015 C5 SOG A 408 19.226 5.645 51.838 1.00123.01 C HETATM 5016 C6 SOG A 408 20.274 5.729 52.948 1.00122.80 C HETATM 5017 C1' SOG A 408 17.993 1.609 49.905 1.00121.79 C HETATM 5018 C2' SOG A 408 17.727 0.103 49.889 1.00120.84 C HETATM 5019 C3' SOG A 408 18.574 -0.647 50.912 1.00120.50 C HETATM 5020 C4' SOG A 408 19.910 -1.109 50.340 1.00120.37 C HETATM 5021 S1 SOG A 408 17.010 2.421 51.125 1.00122.44 S HETATM 5022 O2 SOG A 408 15.331 4.879 50.350 1.00119.87 O HETATM 5023 O3 SOG A 408 15.842 7.364 51.668 1.00121.95 O HETATM 5024 O4 SOG A 408 18.764 8.018 51.509 1.00122.77 O HETATM 5025 O5 SOG A 408 18.640 4.326 51.847 1.00122.91 O HETATM 5026 O6 SOG A 408 19.822 5.047 54.127 1.00122.35 O HETATM 5027 C1 SOG A 409 -1.888 18.060 37.980 1.00 88.78 C HETATM 5028 C2 SOG A 409 -2.555 18.495 39.292 1.00 89.64 C HETATM 5029 C3 SOG A 409 -4.083 18.466 39.189 1.00 89.99 C HETATM 5030 C4 SOG A 409 -4.657 18.974 37.859 1.00 90.93 C HETATM 5031 C5 SOG A 409 -3.856 18.447 36.655 1.00 89.96 C HETATM 5032 C6 SOG A 409 -4.322 18.932 35.278 1.00 90.27 C HETATM 5033 C1' SOG A 409 0.382 16.590 37.601 1.00 78.35 C HETATM 5034 C2' SOG A 409 1.799 16.620 37.038 1.00 71.67 C HETATM 5035 C3' SOG A 409 2.405 15.221 37.015 1.00 65.43 C HETATM 5036 C4' SOG A 409 3.901 15.202 36.712 1.00 59.37 C HETATM 5037 C5' SOG A 409 4.706 15.013 37.992 1.00 55.41 C HETATM 5038 C6' SOG A 409 6.009 14.239 37.780 1.00 54.13 C HETATM 5039 C7' SOG A 409 7.234 15.104 37.468 1.00 54.10 C HETATM 5040 C8' SOG A 409 7.531 16.184 38.493 1.00 53.25 C HETATM 5041 S1 SOG A 409 -0.123 18.216 38.076 1.00 85.66 S HETATM 5042 O2 SOG A 409 -2.191 17.566 40.314 1.00 90.13 O HETATM 5043 O3 SOG A 409 -4.651 19.171 40.297 1.00 89.94 O HETATM 5044 O4 SOG A 409 -6.037 18.581 37.776 1.00 92.69 O HETATM 5045 O5 SOG A 409 -2.461 18.750 36.848 1.00 89.50 O HETATM 5046 O6 SOG A 409 -5.738 18.779 35.081 1.00 91.68 O HETATM 5047 C1 SOG A 410 -0.930 16.524 44.363 1.00 96.56 C HETATM 5048 C2 SOG A 410 -2.125 15.567 44.250 1.00 98.55 C HETATM 5049 C3 SOG A 410 -2.048 14.380 45.223 1.00 98.25 C HETATM 5050 C4 SOG A 410 -0.735 13.624 45.099 1.00 97.43 C HETATM 5051 C5 SOG A 410 0.489 14.536 45.095 1.00 95.32 C HETATM 5052 C6 SOG A 410 1.414 14.176 43.940 1.00 90.70 C HETATM 5053 C1' SOG A 410 1.173 17.831 42.960 1.00 86.71 C HETATM 5054 C2' SOG A 410 2.021 17.698 41.688 1.00 79.72 C HETATM 5055 C3' SOG A 410 3.493 17.397 41.992 1.00 72.58 C HETATM 5056 C4' SOG A 410 4.482 17.910 40.946 1.00 67.25 C HETATM 5057 C5' SOG A 410 5.407 18.956 41.571 1.00 62.70 C HETATM 5058 C6' SOG A 410 6.747 19.128 40.851 1.00 58.10 C HETATM 5059 C7' SOG A 410 7.540 20.270 41.492 1.00 54.09 C HETATM 5060 C8' SOG A 410 8.769 20.686 40.712 1.00 49.58 C HETATM 5061 S1 SOG A 410 -0.450 17.133 42.765 1.00 93.86 S HETATM 5062 O2 SOG A 410 -3.340 16.299 44.465 1.00100.49 O HETATM 5063 O3 SOG A 410 -3.080 13.422 44.974 1.00 98.01 O HETATM 5064 O4 SOG A 410 -0.626 12.649 46.146 1.00 97.84 O HETATM 5065 O5 SOG A 410 0.182 15.957 45.091 1.00 97.08 O HETATM 5066 O6 SOG A 410 2.500 15.084 43.825 1.00 86.30 O HETATM 5067 C1 SOG A 411 2.876 14.753 48.342 1.00 69.39 C HETATM 5068 C2 SOG A 411 1.569 14.762 49.161 1.00 72.71 C HETATM 5069 C3 SOG A 411 1.783 15.497 50.487 1.00 73.92 C HETATM 5070 C4 SOG A 411 2.928 14.874 51.286 1.00 71.70 C HETATM 5071 C5 SOG A 411 4.203 14.697 50.434 1.00 68.64 C HETATM 5072 C6 SOG A 411 5.240 13.822 51.141 1.00 67.26 C HETATM 5073 C1' SOG A 411 4.243 13.697 46.083 1.00 65.91 C HETATM 5074 C2' SOG A 411 4.859 15.030 45.654 1.00 58.17 C HETATM 5075 C3' SOG A 411 6.362 14.944 45.407 1.00 51.18 C HETATM 5076 C4' SOG A 411 6.756 15.692 44.142 1.00 44.45 C HETATM 5077 C5' SOG A 411 8.241 15.511 43.873 1.00 41.46 C HETATM 5078 C6' SOG A 411 8.942 16.810 43.503 1.00 37.52 C HETATM 5079 C7' SOG A 411 10.396 16.543 43.129 1.00 36.14 C HETATM 5080 C8' SOG A 411 11.021 17.788 42.559 1.00 34.31 C HETATM 5081 S1 SOG A 411 2.635 13.812 46.848 1.00 69.73 S HETATM 5082 O2 SOG A 411 0.452 15.324 48.450 1.00 73.22 O HETATM 5083 O3 SOG A 411 0.583 15.475 51.273 1.00 77.42 O HETATM 5084 O4 SOG A 411 3.183 15.719 52.412 1.00 71.91 O HETATM 5085 O5 SOG A 411 3.944 14.169 49.122 1.00 67.14 O HETATM 5086 O6 SOG A 411 4.896 12.430 51.120 1.00 66.71 O HETATM 5087 C1 SOG A 412 18.457 32.972 17.026 1.00 85.00 C HETATM 5088 C2 SOG A 412 17.159 33.295 16.268 1.00 86.55 C HETATM 5089 C3 SOG A 412 15.943 32.725 17.010 1.00 86.08 C HETATM 5090 C4 SOG A 412 16.099 31.213 17.239 1.00 83.96 C HETATM 5091 C5 SOG A 412 17.449 30.891 17.909 1.00 81.74 C HETATM 5092 C6 SOG A 412 17.729 29.386 17.989 1.00 76.46 C HETATM 5093 C1' SOG A 412 20.999 34.027 17.218 1.00 84.15 C HETATM 5094 C2' SOG A 412 22.379 34.101 16.578 1.00 83.26 C HETATM 5095 C3' SOG A 412 23.432 33.372 17.403 1.00 83.35 C HETATM 5096 C4' SOG A 412 24.818 33.943 17.115 1.00 84.01 C HETATM 5097 C5' SOG A 412 25.894 32.861 17.052 1.00 84.14 C HETATM 5098 C6' SOG A 412 27.015 33.252 16.094 1.00 84.84 C HETATM 5099 C7' SOG A 412 28.163 33.947 16.827 1.00 85.06 C HETATM 5100 C8' SOG A 412 29.430 33.981 15.997 1.00 84.80 C HETATM 5101 S1 SOG A 412 19.839 33.439 16.029 1.00 85.52 S HETATM 5102 O2 SOG A 412 17.015 34.710 16.078 1.00 88.40 O HETATM 5103 O3 SOG A 412 14.730 33.017 16.300 1.00 86.47 O HETATM 5104 O4 SOG A 412 15.011 30.684 18.011 1.00 82.35 O HETATM 5105 O5 SOG A 412 18.564 31.558 17.281 1.00 83.37 O HETATM 5106 O6 SOG A 412 17.743 28.733 16.710 1.00 71.24 O HETATM 5107 C1 SOG A 413 25.759 -3.400 43.296 0.90 73.52 C HETATM 5108 C2 SOG A 413 26.688 -3.887 44.415 0.90 76.01 C HETATM 5109 C3 SOG A 413 26.124 -3.489 45.793 0.90 77.12 C HETATM 5110 C4 SOG A 413 25.414 -2.114 45.867 0.90 74.91 C HETATM 5111 C5 SOG A 413 24.948 -1.507 44.533 0.90 73.68 C HETATM 5112 C6 SOG A 413 25.033 0.014 44.607 0.90 72.38 C HETATM 5113 C1' SOG A 413 25.243 -3.020 40.592 0.90 62.54 C HETATM 5114 C2' SOG A 413 26.123 -2.214 39.644 0.90 55.52 C HETATM 5115 C3' SOG A 413 26.780 -1.054 40.383 0.90 51.29 C HETATM 5116 C4' SOG A 413 27.390 -0.058 39.410 0.90 48.64 C HETATM 5117 C5' SOG A 413 28.853 0.252 39.719 0.90 43.70 C HETATM 5118 C6' SOG A 413 29.649 0.351 38.423 0.90 39.47 C HETATM 5119 C7' SOG A 413 29.864 1.794 37.971 0.90 35.50 C HETATM 5120 C8' SOG A 413 30.624 1.817 36.664 0.90 31.08 C HETATM 5121 S1 SOG A 413 26.234 -3.990 41.690 0.90 70.17 S HETATM 5122 O2 SOG A 413 26.889 -5.308 44.347 0.90 76.81 O HETATM 5123 O3 SOG A 413 27.188 -3.533 46.755 0.90 79.01 O HETATM 5124 O4 SOG A 413 24.295 -2.151 46.768 0.90 73.27 O HETATM 5125 O5 SOG A 413 25.699 -1.970 43.395 0.90 73.81 O HETATM 5126 O6 SOG A 413 24.495 0.583 43.411 0.90 71.90 O HETATM 5127 C1 SOG A 414 32.919 15.463 25.057 0.79 66.83 C HETATM 5128 C2 SOG A 414 34.154 14.629 24.668 0.79 65.66 C HETATM 5129 C3 SOG A 414 34.980 15.355 23.591 0.79 67.02 C HETATM 5130 C4 SOG A 414 34.110 15.796 22.404 0.79 69.44 C HETATM 5131 C5 SOG A 414 32.880 16.582 22.902 0.79 68.88 C HETATM 5132 C6 SOG A 414 31.937 17.037 21.787 0.79 69.29 C HETATM 5133 C1' SOG A 414 30.415 15.570 26.244 0.79 63.68 C HETATM 5134 C2' SOG A 414 29.598 15.140 27.454 0.79 62.48 C HETATM 5135 C3' SOG A 414 28.796 13.863 27.207 0.79 60.63 C HETATM 5136 C4' SOG A 414 28.042 13.452 28.471 0.79 58.41 C HETATM 5137 C5' SOG A 414 26.539 13.731 28.405 0.79 54.96 C HETATM 5138 C6' SOG A 414 26.015 14.519 29.607 0.79 52.78 C HETATM 5139 C7' SOG A 414 25.282 15.798 29.196 0.79 49.89 C HETATM 5140 C8' SOG A 414 24.234 16.184 30.215 0.79 47.14 C HETATM 5141 S1 SOG A 414 31.897 14.616 26.225 0.79 67.49 S HETATM 5142 O2 SOG A 414 34.959 14.297 25.809 0.79 64.07 O HETATM 5143 O3 SOG A 414 36.135 14.607 23.164 0.79 65.76 O HETATM 5144 O4 SOG A 414 34.913 16.616 21.544 0.79 72.40 O HETATM 5145 O5 SOG A 414 32.158 15.821 23.888 0.79 67.58 O HETATM 5146 O6 SOG A 414 30.589 17.174 22.268 0.79 69.22 O HETATM 5147 C1 SOG A 415 15.784 -16.655 24.878 1.00104.64 C HETATM 5148 C2 SOG A 415 14.857 -15.429 25.001 1.00102.95 C HETATM 5149 C3 SOG A 415 13.665 -15.544 24.057 1.00102.09 C HETATM 5150 C4 SOG A 415 14.176 -15.805 22.642 1.00105.24 C HETATM 5151 C5 SOG A 415 15.016 -17.089 22.572 1.00105.28 C HETATM 5152 C6 SOG A 415 15.591 -17.347 21.173 1.00103.33 C HETATM 5153 C1' SOG A 415 17.963 -17.981 25.794 1.00105.72 C HETATM 5154 C2' SOG A 415 19.475 -17.948 25.616 1.00106.02 C HETATM 5155 S1 SOG A 415 17.325 -16.342 25.682 1.00105.82 S HETATM 5156 O2 SOG A 415 14.345 -15.286 26.325 1.00103.27 O HETATM 5157 O3 SOG A 415 12.886 -14.345 24.121 1.00 99.23 O HETATM 5158 O4 SOG A 415 13.120 -15.825 21.686 1.00106.91 O HETATM 5159 O5 SOG A 415 16.106 -16.962 23.505 1.00105.64 O HETATM 5160 O6 SOG A 415 14.565 -17.773 20.266 1.00101.70 O HETATM 5161 C1 SOG A 416 31.115 0.207 27.538 1.00 98.42 C HETATM 5162 C2 SOG A 416 31.728 1.606 27.409 1.00 98.98 C HETATM 5163 C3 SOG A 416 33.076 1.562 28.133 1.00100.61 C HETATM 5164 C4 SOG A 416 32.936 1.144 29.603 1.00102.03 C HETATM 5165 C5 SOG A 416 32.078 -0.133 29.731 1.00101.61 C HETATM 5166 C6 SOG A 416 31.717 -0.467 31.178 1.00102.28 C HETATM 5167 C1' SOG A 416 29.820 -1.698 26.022 1.00 91.66 C HETATM 5168 C2' SOG A 416 28.692 -2.035 25.052 1.00 87.16 C HETATM 5169 C3' SOG A 416 27.704 -3.011 25.678 1.00 84.42 C HETATM 5170 C4' SOG A 416 26.630 -3.436 24.684 1.00 83.19 C HETATM 5171 C5' SOG A 416 26.744 -4.918 24.338 1.00 82.92 C HETATM 5172 C6' SOG A 416 26.850 -5.142 22.831 1.00 82.79 C HETATM 5173 C7' SOG A 416 28.271 -5.505 22.405 1.00 82.66 C HETATM 5174 C8' SOG A 416 28.279 -6.408 21.187 1.00 82.35 C HETATM 5175 S1 SOG A 416 29.666 -0.020 26.546 1.00 96.11 S HETATM 5176 O2 SOG A 416 31.913 1.971 26.035 1.00 99.39 O HETATM 5177 O3 SOG A 416 33.802 2.787 27.999 1.00101.27 O HETATM 5178 O4 SOG A 416 34.247 0.932 30.158 1.00103.01 O HETATM 5179 O5 SOG A 416 30.876 -0.058 28.933 1.00 99.88 O HETATM 5180 O6 SOG A 416 32.824 -1.103 31.828 1.00102.36 O HETATM 5181 C1 SOG A 417 -3.400 11.905 39.338 1.00111.21 C HETATM 5182 C2 SOG A 417 -3.549 13.117 40.255 1.00111.33 C HETATM 5183 C3 SOG A 417 -3.446 12.721 41.723 1.00111.23 C HETATM 5184 C4 SOG A 417 -4.205 11.451 42.138 1.00110.92 C HETATM 5185 C5 SOG A 417 -4.354 10.393 41.024 1.00111.72 C HETATM 5186 C6 SOG A 417 -5.569 9.486 41.252 1.00111.65 C HETATM 5187 C1' SOG A 417 -1.944 12.702 37.211 1.00105.85 C HETATM 5188 C2' SOG A 417 -1.854 13.748 36.107 1.00101.15 C HETATM 5189 C3' SOG A 417 -1.309 13.113 34.834 1.00 96.82 C HETATM 5190 C4' SOG A 417 0.198 13.298 34.730 1.00 92.96 C HETATM 5191 C5' SOG A 417 0.962 12.017 35.048 1.00 89.31 C HETATM 5192 C6' SOG A 417 2.452 12.224 34.807 1.00 86.68 C HETATM 5193 C7' SOG A 417 2.923 11.514 33.551 1.00 85.92 C HETATM 5194 C8' SOG A 417 2.885 12.427 32.344 1.00 86.45 C HETATM 5195 S1 SOG A 417 -3.624 12.443 37.671 1.00110.13 S HETATM 5196 O2 SOG A 417 -2.615 14.163 39.958 1.00111.30 O HETATM 5197 O3 SOG A 417 -3.928 13.827 42.473 1.00110.99 O HETATM 5198 O4 SOG A 417 -3.550 10.881 43.283 1.00109.49 O HETATM 5199 O5 SOG A 417 -4.417 10.945 39.690 1.00111.89 O HETATM 5200 O6 SOG A 417 -6.814 10.197 41.166 1.00110.66 O HETATM 5201 C1 SOG A 418 -7.264 9.361 37.312 1.00110.88 C HETATM 5202 C2 SOG A 418 -7.719 10.794 37.637 1.00112.43 C HETATM 5203 C3 SOG A 418 -9.208 10.838 38.022 1.00112.76 C HETATM 5204 C4 SOG A 418 -10.118 10.040 37.075 1.00112.33 C HETATM 5205 C5 SOG A 418 -9.527 8.667 36.693 1.00111.96 C HETATM 5206 C6 SOG A 418 -10.300 8.024 35.542 1.00111.34 C HETATM 5207 C1' SOG A 418 -5.533 9.844 35.181 1.00104.55 C HETATM 5208 C2' SOG A 418 -4.115 10.204 34.750 1.00100.99 C HETATM 5209 C3' SOG A 418 -3.711 9.436 33.498 1.00 98.01 C HETATM 5210 C4' SOG A 418 -2.744 10.245 32.645 1.00 95.62 C HETATM 5211 C5' SOG A 418 -2.835 9.795 31.194 1.00 94.54 C HETATM 5212 C6' SOG A 418 -1.642 10.282 30.382 1.00 94.35 C HETATM 5213 C7' SOG A 418 -1.560 9.532 29.057 1.00 94.23 C HETATM 5214 C8' SOG A 418 -0.561 10.179 28.124 1.00 94.18 C HETATM 5215 S1 SOG A 418 -5.548 9.284 36.857 1.00107.84 S HETATM 5216 O2 SOG A 418 -6.930 11.341 38.701 1.00112.45 O HETATM 5217 O3 SOG A 418 -9.655 12.197 38.088 1.00112.76 O HETATM 5218 O4 SOG A 418 -11.399 9.874 37.701 1.00111.83 O HETATM 5219 O5 SOG A 418 -8.133 8.758 36.329 1.00111.71 O HETATM 5220 O6 SOG A 418 -11.454 7.340 36.050 1.00110.59 O HETATM 5221 C1' SOG A 419 6.932 27.204 19.091 1.00103.31 C HETATM 5222 C2' SOG A 419 6.414 25.844 18.633 1.00 99.60 C HETATM 5223 C3' SOG A 419 7.339 24.707 19.055 1.00 96.02 C HETATM 5224 C4' SOG A 419 6.675 23.360 18.782 1.00 92.90 C HETATM 5225 C5' SOG A 419 7.654 22.197 18.900 1.00 89.90 C HETATM 5226 C6' SOG A 419 7.214 21.016 18.041 1.00 87.46 C HETATM 5227 S1 SOG A 419 6.460 28.455 17.936 1.00106.26 S HETATM 5228 C1' SOG A 420 8.742 16.836 7.528 1.00 81.17 C HETATM 5229 C2' SOG A 420 8.637 15.370 7.938 1.00 75.38 C HETATM 5230 C3' SOG A 420 8.088 15.243 9.353 1.00 70.78 C HETATM 5231 C4' SOG A 420 8.191 13.817 9.883 1.00 67.50 C HETATM 5232 C5' SOG A 420 7.808 13.776 11.360 1.00 65.57 C HETATM 5233 C6' SOG A 420 7.378 12.384 11.799 1.00 64.08 C HETATM 5234 S1 SOG A 420 8.497 17.014 5.786 1.00 86.44 S HETATM 5235 C1' SOG A 421 -6.423 4.590 35.745 1.00 91.98 C HETATM 5236 C2' SOG A 421 -5.487 5.646 35.176 1.00 88.48 C HETATM 5237 C3' SOG A 421 -5.034 5.237 33.785 1.00 86.07 C HETATM 5238 C4' SOG A 421 -3.533 5.402 33.606 1.00 83.69 C HETATM 5239 C5' SOG A 421 -3.117 4.951 32.212 1.00 83.34 C HETATM 5240 C6' SOG A 421 -1.761 5.523 31.806 1.00 83.22 C HETATM 5241 S1 SOG A 421 -7.170 5.199 37.218 1.00 95.77 S HETATM 5242 C1' SOG A 422 -6.741 1.765 38.330 1.00 82.29 C HETATM 5243 C2' SOG A 422 -5.881 0.705 37.648 1.00 77.84 C HETATM 5244 C3' SOG A 422 -6.059 0.723 36.134 1.00 73.64 C HETATM 5245 C4' SOG A 422 -4.748 0.396 35.428 1.00 70.56 C HETATM 5246 C5' SOG A 422 -4.932 0.338 33.916 1.00 68.07 C HETATM 5247 C6' SOG A 422 -4.121 1.424 33.219 1.00 66.71 C HETATM 5248 S1 SOG A 422 -5.853 2.608 39.609 1.00 86.05 S HETATM 5249 C1' SOG A 423 15.055 -18.162 28.766 1.00 82.51 C HETATM 5250 C2' SOG A 423 15.732 -17.424 29.914 1.00 79.67 C HETATM 5251 C3' SOG A 423 17.239 -17.356 29.721 1.00 78.62 C HETATM 5252 C4' SOG A 423 17.937 -17.372 31.073 1.00 79.04 C HETATM 5253 C5' SOG A 423 19.005 -18.459 31.134 1.00 79.84 C HETATM 5254 C6' SOG A 423 19.963 -18.221 32.296 1.00 79.99 C HETATM 5255 S1 SOG A 423 13.517 -17.379 28.397 1.00 84.94 S HETATM 5256 C1' SOG A 424 14.108 -19.607 34.336 1.00 96.34 C HETATM 5257 C2' SOG A 424 15.310 -20.466 34.673 1.00 93.60 C HETATM 5258 C3' SOG A 424 16.559 -19.608 34.660 1.00 92.36 C HETATM 5259 C4' SOG A 424 17.059 -19.424 36.084 1.00 91.83 C HETATM 5260 C5' SOG A 424 18.539 -19.082 36.067 1.00 91.53 C HETATM 5261 C6' SOG A 424 19.383 -20.292 36.445 1.00 91.47 C HETATM 5262 S1 SOG A 424 12.674 -20.614 34.441 1.00 99.73 S HETATM 5263 C1' SOG A 425 19.549 -13.873 30.456 1.00 90.77 C HETATM 5264 C2' SOG A 425 20.772 -13.136 29.920 1.00 89.05 C HETATM 5265 C3' SOG A 425 21.642 -14.053 29.067 1.00 87.76 C HETATM 5266 C4' SOG A 425 22.912 -13.335 28.617 1.00 86.83 C HETATM 5267 C5' SOG A 425 24.160 -14.168 28.892 1.00 86.15 C HETATM 5268 C6' SOG A 425 25.429 -13.402 28.535 1.00 85.15 C HETATM 5269 S1 SOG A 425 18.886 -13.015 31.849 1.00 91.76 S HETATM 5270 C1' SOG A 426 1.816 21.620 22.011 1.00 97.20 C HETATM 5271 C2' SOG A 426 2.945 20.626 22.264 1.00 95.73 C HETATM 5272 C3' SOG A 426 2.496 19.193 22.002 1.00 94.53 C HETATM 5273 C4' SOG A 426 3.653 18.206 22.123 1.00 93.87 C HETATM 5274 C5' SOG A 426 4.023 17.611 20.767 1.00 93.63 C HETATM 5275 C6' SOG A 426 5.261 16.726 20.858 1.00 93.34 C HETATM 5276 S1 SOG A 426 2.147 22.566 20.556 1.00 98.78 S HETATM 5277 C1' SOG A 427 20.701 -16.994 45.689 1.00 99.37 C HETATM 5278 C2' SOG A 427 21.456 -15.671 45.710 1.00 97.51 C HETATM 5279 C3' SOG A 427 22.435 -15.543 44.546 1.00 96.21 C HETATM 5280 C4' SOG A 427 22.903 -14.097 44.396 1.00 94.85 C HETATM 5281 C5' SOG A 427 24.312 -13.873 44.938 1.00 94.07 C HETATM 5282 C6' SOG A 427 24.376 -12.635 45.827 1.00 93.05 C HETATM 5283 S1 SOG A 427 18.967 -16.711 45.494 1.00101.06 S HETATM 5284 C1' SOG A 428 30.740 4.000 16.598 1.00 75.49 C HETATM 5285 C2' SOG A 428 31.600 2.877 16.022 1.00 73.69 C HETATM 5286 C3' SOG A 428 31.636 2.907 14.494 1.00 70.71 C HETATM 5287 C4' SOG A 428 32.752 2.031 13.931 1.00 67.45 C HETATM 5288 C5' SOG A 428 33.926 2.873 13.437 1.00 65.45 C HETATM 5289 C6' SOG A 428 34.851 2.069 12.529 1.00 65.29 C HETATM 5290 S1 SOG A 428 30.391 3.709 18.306 1.00 77.82 S HETATM 5291 CAD PGW A 429 12.652 28.986 14.279 1.00 99.49 C HETATM 5292 OAE PGW A 429 12.794 29.090 12.857 1.00 99.39 O HETATM 5293 OAF PGW A 429 10.267 29.175 13.992 1.00101.57 O HETATM 5294 P PGW A 429 10.856 30.177 17.917 1.00 93.89 P HETATM 5295 C01 PGW A 429 10.161 27.518 21.436 1.00 64.82 C HETATM 5296 C1 PGW A 429 13.661 26.686 20.576 1.00 50.29 C HETATM 5297 O01 PGW A 429 12.218 26.778 20.376 1.00 57.11 O HETATM 5298 C02 PGW A 429 11.593 27.864 21.051 1.00 64.38 C HETATM 5299 C2 PGW A 429 14.322 25.609 21.397 1.00 38.64 C HETATM 5300 O02 PGW A 429 14.361 27.511 20.030 1.00 57.25 O HETATM 5301 C03 PGW A 429 11.621 29.136 20.220 1.00 74.76 C HETATM 5302 C3 PGW A 429 15.500 24.993 20.648 1.00 33.75 C HETATM 5303 O03 PGW A 429 10.029 27.850 22.820 1.00 65.00 O HETATM 5304 C04 PGW A 429 11.082 28.263 16.082 1.00 97.63 C HETATM 5305 C4 PGW A 429 16.085 23.857 21.468 1.00 31.42 C HETATM 5306 O04 PGW A 429 8.042 28.912 23.285 1.00 63.92 O HETATM 5307 C05 PGW A 429 11.295 28.366 14.579 1.00 99.65 C HETATM 5308 C5 PGW A 429 17.462 23.473 20.979 1.00 32.54 C HETATM 5309 C06 PGW A 429 19.701 18.526 24.051 1.00 39.20 C HETATM 5310 C6 PGW A 429 17.978 22.309 21.813 1.00 35.10 C HETATM 5311 C07 PGW A 429 19.300 17.978 25.402 1.00 41.51 C HETATM 5312 C7 PGW A 429 18.772 21.350 20.937 1.00 35.88 C HETATM 5313 C08 PGW A 429 20.566 17.498 26.108 1.00 44.65 C HETATM 5314 C8 PGW A 429 19.412 20.218 21.723 1.00 36.10 C HETATM 5315 C09 PGW A 429 20.371 17.520 27.618 1.00 46.37 C HETATM 5316 C9 PGW A 429 18.460 19.074 21.994 1.00 38.50 C HETATM 5317 C10 PGW A 429 18.590 18.283 23.063 1.00 38.49 C HETATM 5318 C11 PGW A 429 19.523 16.353 28.100 1.00 47.09 C HETATM 5319 O11 PGW A 429 11.215 28.917 18.874 1.00 85.33 O HETATM 5320 C12 PGW A 429 19.611 16.244 29.610 1.00 47.16 C HETATM 5321 O12 PGW A 429 10.402 29.423 16.565 1.00 96.37 O HETATM 5322 C13 PGW A 429 18.330 16.691 30.290 1.00 43.98 C HETATM 5323 O13 PGW A 429 9.650 30.894 18.500 1.00 94.82 O HETATM 5324 C14 PGW A 429 18.357 16.124 31.689 1.00 44.74 C HETATM 5325 O14 PGW A 429 12.105 30.976 17.609 1.00 93.71 O HETATM 5326 C15 PGW A 429 10.821 20.627 27.927 1.00 39.26 C HETATM 5327 C16 PGW A 429 11.454 21.609 28.909 1.00 35.53 C HETATM 5328 C17 PGW A 429 12.950 21.409 29.067 1.00 34.93 C HETATM 5329 C18 PGW A 429 13.573 22.725 29.514 1.00 34.20 C HETATM 5330 C19 PGW A 429 8.736 27.925 23.474 1.00 61.40 C HETATM 5331 C20 PGW A 429 8.258 26.779 24.337 1.00 54.94 C HETATM 5332 C21 PGW A 429 8.823 26.799 25.755 1.00 48.56 C HETATM 5333 C22 PGW A 429 8.905 25.385 26.349 1.00 46.57 C HETATM 5334 C23 PGW A 429 7.546 24.717 26.577 1.00 47.18 C HETATM 5335 C24 PGW A 429 7.455 23.971 27.906 1.00 48.79 C HETATM 5336 C25 PGW A 429 7.562 22.461 27.712 1.00 50.83 C HETATM 5337 C26 PGW A 429 8.641 21.839 28.606 1.00 48.93 C HETATM 5338 C27 PGW A 429 9.287 20.567 28.028 1.00 44.10 C HETATM 5339 C28 PGW A 429 14.978 22.527 30.068 1.00 34.53 C HETATM 5340 C29 PGW A 429 16.754 23.852 31.233 1.00 25.18 C HETATM 5341 C30 PGW A 429 15.273 23.600 31.113 1.00 31.89 C HETATM 5342 NA NA A 430 15.247 1.798 22.856 1.00 52.69 NA1+ HETATM 5343 C10 7MA B 401 16.860 29.177 39.141 0.91 33.82 C HETATM 5344 C13 7MA B 401 14.674 34.285 36.460 0.91 38.02 C HETATM 5345 C15 7MA B 401 16.760 35.708 37.160 0.91 42.22 C HETATM 5346 C20 7MA B 401 16.665 37.033 37.730 0.91 40.46 C HETATM 5347 C22 7MA B 401 20.997 36.008 39.627 0.91 38.15 C HETATM 5348 C26 7MA B 401 16.276 37.366 34.255 0.91 48.09 C HETATM 5349 C28 7MA B 401 14.812 39.295 33.952 0.91 43.97 C HETATM 5350 C32 7MA B 401 18.763 37.699 34.772 0.91 39.54 C HETATM 5351 C31 7MA B 401 17.370 38.208 34.466 0.91 44.49 C HETATM 5352 C30 7MA B 401 17.172 39.622 34.418 0.91 42.98 C HETATM 5353 C29 7MA B 401 15.875 40.143 34.161 0.91 44.84 C HETATM 5354 C27 7MA B 401 14.993 37.890 34.002 0.91 41.21 C HETATM 5355 S23 7MA B 401 16.333 35.479 34.405 0.91 60.70 S HETATM 5356 O24 7MA B 401 15.256 34.847 33.322 0.91 62.57 O HETATM 5357 O25 7MA B 401 17.836 34.935 34.130 0.91 59.03 O HETATM 5358 N14 7MA B 401 15.807 35.124 36.131 0.91 48.49 N HETATM 5359 C16 7MA B 401 17.931 34.934 37.310 0.91 36.50 C HETATM 5360 N17 7MA B 401 18.909 35.378 38.044 0.91 36.50 N HETATM 5361 C19 7MA B 401 17.745 37.494 38.485 0.91 41.07 C HETATM 5362 C18 7MA B 401 18.890 36.609 38.610 0.91 36.56 C HETATM 5363 O21 7MA B 401 20.002 36.972 39.363 0.91 34.36 O HETATM 5364 C11 7MA B 401 14.890 33.086 37.445 0.91 35.31 C HETATM 5365 O12 7MA B 401 14.808 33.345 38.616 0.91 34.17 O HETATM 5366 N03 7MA B 401 15.131 31.730 37.001 0.91 34.73 N HETATM 5367 C02 7MA B 401 15.296 31.359 35.553 0.91 35.16 C HETATM 5368 C01 7MA B 401 13.960 30.891 34.847 0.91 35.62 C HETATM 5369 C04 7MA B 401 15.294 30.681 38.019 0.91 35.01 C HETATM 5370 C05 7MA B 401 16.713 30.318 38.403 0.91 33.98 C HETATM 5371 C09 7MA B 401 18.166 28.785 39.526 0.91 33.22 C HETATM 5372 C08 7MA B 401 19.232 29.592 39.153 0.91 33.10 C HETATM 5373 N07 7MA B 401 19.067 30.678 38.438 0.91 32.83 N HETATM 5374 C06 7MA B 401 17.832 31.073 38.026 0.91 34.70 C HETATM 5375 H1 7MA B 401 16.121 28.666 39.383 0.50 33.88 H HETATM 5376 H2 7MA B 401 14.005 34.862 36.860 0.50 38.48 H HETATM 5377 H3 7MA B 401 14.333 33.923 35.632 0.50 37.53 H HETATM 5378 H4 7MA B 401 15.922 37.571 37.575 0.50 40.48 H HETATM 5379 H5 7MA B 401 21.658 36.384 40.224 0.50 38.89 H HETATM 5380 H6 7MA B 401 20.597 35.231 40.048 0.50 37.93 H HETATM 5381 H7 7MA B 401 21.434 35.746 38.801 0.50 37.72 H HETATM 5382 H8 7MA B 401 13.971 39.639 33.762 0.50 43.93 H HETATM 5383 H9 7MA B 401 18.724 37.054 35.494 0.50 39.44 H HETATM 5384 H10 7MA B 401 19.128 37.279 33.978 0.50 38.85 H HETATM 5385 H11 7MA B 401 19.337 38.435 35.036 0.50 40.29 H HETATM 5386 H12 7MA B 401 17.891 40.202 34.531 0.50 42.90 H HETATM 5387 H13 7MA B 401 15.755 41.062 34.082 0.50 44.84 H HETATM 5388 H14 7MA B 401 14.266 37.320 33.893 0.50 41.11 H HETATM 5389 H15 7MA B 401 18.003 34.109 36.888 0.50 36.48 H HETATM 5390 H16 7MA B 401 17.726 38.322 38.906 0.50 41.13 H HETATM 5391 H17 7MA B 401 15.929 30.627 35.507 0.50 34.57 H HETATM 5392 H18 7MA B 401 15.661 32.112 35.065 0.50 35.76 H HETATM 5393 H19 7MA B 401 14.133 30.086 34.334 0.50 35.49 H HETATM 5394 H20 7MA B 401 13.293 30.705 35.524 0.50 35.09 H HETATM 5395 H21 7MA B 401 13.639 31.592 34.258 0.50 36.30 H HETATM 5396 H22 7MA B 401 14.825 30.932 38.828 0.50 35.50 H HETATM 5397 H23 7MA B 401 14.882 29.879 37.661 0.50 34.59 H HETATM 5398 H24 7MA B 401 18.306 28.017 40.027 0.50 33.17 H HETATM 5399 H25 7MA B 401 20.093 29.335 39.387 0.50 33.14 H HETATM 5400 H26 7MA B 401 17.735 31.855 37.535 0.50 34.75 H HETATM 5401 S SO4 B 402 46.816 21.665 47.866 1.00106.10 S HETATM 5402 O1 SO4 B 402 45.601 20.863 47.684 1.00106.05 O HETATM 5403 O2 SO4 B 402 47.012 22.534 46.700 1.00103.80 O HETATM 5404 O3 SO4 B 402 47.976 20.775 48.005 1.00107.41 O HETATM 5405 O4 SO4 B 402 46.678 22.460 49.093 1.00105.48 O HETATM 5406 S SO4 B 403 44.477 12.267 40.357 1.00 85.72 S HETATM 5407 O1 SO4 B 403 43.269 11.626 39.843 1.00 84.62 O HETATM 5408 O2 SO4 B 403 44.652 13.592 39.732 1.00 86.31 O HETATM 5409 O3 SO4 B 403 45.621 11.422 40.039 1.00 89.00 O HETATM 5410 O4 SO4 B 403 44.399 12.422 41.801 1.00 84.55 O HETATM 5411 O1 PG4 B 404 9.446 39.494 38.538 1.00 59.03 O HETATM 5412 C1 PG4 B 404 10.301 38.915 39.538 1.00 56.70 C HETATM 5413 C2 PG4 B 404 9.869 39.320 40.948 1.00 52.24 C HETATM 5414 O2 PG4 B 404 9.242 38.206 41.582 1.00 49.81 O HETATM 5415 C3 PG4 B 404 8.437 38.601 42.678 1.00 48.05 C HETATM 5416 C4 PG4 B 404 7.313 37.596 42.819 1.00 49.31 C HETATM 5417 O3 PG4 B 404 6.283 37.891 41.885 1.00 51.04 O HETATM 5418 C5 PG4 B 404 5.015 37.614 42.462 1.00 50.90 C HETATM 5419 C6 PG4 B 404 3.945 37.635 41.387 1.00 52.49 C HETATM 5420 O4 PG4 B 404 3.851 36.386 40.705 1.00 54.65 O HETATM 5421 C7 PG4 B 404 3.588 36.654 39.332 1.00 57.41 C HETATM 5422 C8 PG4 B 404 3.561 35.388 38.491 1.00 60.34 C HETATM 5423 O5 PG4 B 404 3.800 35.794 37.137 1.00 63.14 O HETATM 5424 O1 PG4 B 405 23.622 18.867 49.660 1.00 70.05 O HETATM 5425 C1 PG4 B 405 23.461 19.123 48.260 1.00 69.03 C HETATM 5426 C2 PG4 B 405 24.835 19.174 47.607 1.00 69.39 C HETATM 5427 O2 PG4 B 405 25.854 19.208 48.610 1.00 70.08 O HETATM 5428 C3 PG4 B 405 26.748 18.101 48.473 1.00 70.17 C HETATM 5429 C4 PG4 B 405 28.121 18.374 49.086 1.00 68.18 C HETATM 5430 O3 PG4 B 405 28.814 17.131 49.193 1.00 66.87 O HETATM 5431 C5 PG4 B 405 29.052 16.745 50.547 1.00 66.86 C HETATM 5432 C6 PG4 B 405 28.740 15.268 50.784 1.00 66.53 C HETATM 5433 O4 PG4 B 405 29.846 14.631 51.433 1.00 66.03 O HETATM 5434 C7 PG4 B 405 29.570 14.241 52.780 1.00 65.10 C HETATM 5435 C8 PG4 B 405 30.850 13.753 53.451 1.00 64.43 C HETATM 5436 O5 PG4 B 405 30.789 13.993 54.865 1.00 64.34 O HETATM 5437 C1 SOG B 406 -1.787 24.094 41.339 1.00 47.81 C HETATM 5438 C2 SOG B 406 -1.936 24.216 42.864 1.00 47.32 C HETATM 5439 C3 SOG B 406 -2.569 25.573 43.189 1.00 47.08 C HETATM 5440 C4 SOG B 406 -1.909 26.766 42.475 1.00 46.67 C HETATM 5441 C5 SOG B 406 -1.674 26.471 40.987 1.00 48.78 C HETATM 5442 C6 SOG B 406 -0.787 27.507 40.306 1.00 52.56 C HETATM 5443 C1' SOG B 406 0.640 22.764 40.674 1.00 47.21 C HETATM 5444 C2' SOG B 406 1.258 21.446 40.212 1.00 42.42 C HETATM 5445 C3' SOG B 406 1.852 21.552 38.810 1.00 39.04 C HETATM 5446 C4' SOG B 406 2.958 20.517 38.643 1.00 36.51 C HETATM 5447 C5' SOG B 406 3.264 20.246 37.173 1.00 34.60 C HETATM 5448 C6' SOG B 406 4.539 19.426 37.076 1.00 31.70 C HETATM 5449 C7' SOG B 406 4.881 19.108 35.640 1.00 31.55 C HETATM 5450 C8' SOG B 406 6.195 18.352 35.565 1.00 30.00 C HETATM 5451 S1 SOG B 406 -1.107 22.558 40.792 1.00 50.54 S HETATM 5452 O2 SOG B 406 -2.784 23.204 43.434 1.00 47.18 O HETATM 5453 O3 SOG B 406 -2.529 25.735 44.607 1.00 47.88 O HETATM 5454 O4 SOG B 406 -2.684 27.971 42.621 1.00 46.27 O HETATM 5455 O5 SOG B 406 -1.035 25.200 40.831 1.00 47.24 O HETATM 5456 O6 SOG B 406 -1.558 28.539 39.667 1.00 55.18 O HETATM 5457 C1 SOG B 407 13.838 46.090 46.671 1.00 47.03 C HETATM 5458 C2 SOG B 407 13.160 45.347 45.520 1.00 47.41 C HETATM 5459 C3 SOG B 407 12.332 46.296 44.639 1.00 47.18 C HETATM 5460 C4 SOG B 407 11.366 47.148 45.477 1.00 47.01 C HETATM 5461 C5 SOG B 407 12.081 47.808 46.662 1.00 46.19 C HETATM 5462 C6 SOG B 407 11.084 48.488 47.591 1.00 43.52 C HETATM 5463 C1' SOG B 407 15.282 45.885 48.980 1.00 46.30 C HETATM 5464 C2' SOG B 407 16.281 45.086 49.803 1.00 50.48 C HETATM 5465 C3' SOG B 407 17.473 45.964 50.185 1.00 55.99 C HETATM 5466 C4' SOG B 407 17.955 45.650 51.601 1.00 59.99 C HETATM 5467 C5' SOG B 407 19.447 45.930 51.799 1.00 63.52 C HETATM 5468 C6' SOG B 407 20.113 44.940 52.762 1.00 65.93 C HETATM 5469 C7' SOG B 407 19.803 45.237 54.234 1.00 67.39 C HETATM 5470 C8' SOG B 407 20.924 44.789 55.146 1.00 68.36 C HETATM 5471 S1 SOG B 407 14.613 44.881 47.695 1.00 43.49 S HETATM 5472 O2 SOG B 407 14.162 44.680 44.753 1.00 46.05 O HETATM 5473 O3 SOG B 407 11.597 45.508 43.691 1.00 47.07 O HETATM 5474 O4 SOG B 407 10.773 48.154 44.657 1.00 47.44 O HETATM 5475 O5 SOG B 407 12.861 46.853 47.416 1.00 47.84 O HETATM 5476 O6 SOG B 407 10.439 47.515 48.425 1.00 42.25 O HETATM 5477 C1 SOG B 408 10.465 52.413 44.592 1.00 76.21 C HETATM 5478 C2 SOG B 408 9.597 52.483 45.856 1.00 73.78 C HETATM 5479 C3 SOG B 408 8.903 51.134 46.054 1.00 74.16 C HETATM 5480 C4 SOG B 408 8.132 50.689 44.802 1.00 75.77 C HETATM 5481 C5 SOG B 408 8.983 50.807 43.522 1.00 75.81 C HETATM 5482 C6 SOG B 408 8.164 50.569 42.251 1.00 74.34 C HETATM 5483 C1' SOG B 408 11.950 53.769 42.689 1.00 76.46 C HETATM 5484 C2' SOG B 408 13.402 53.303 42.712 1.00 74.15 C HETATM 5485 C3' SOG B 408 14.354 54.488 42.732 1.00 71.10 C HETATM 5486 C4' SOG B 408 15.482 54.268 43.731 1.00 68.65 C HETATM 5487 C5' SOG B 408 16.448 55.441 43.656 1.00 67.84 C HETATM 5488 C6' SOG B 408 17.850 54.995 43.262 1.00 68.25 C HETATM 5489 C7' SOG B 408 18.919 55.787 44.004 1.00 67.88 C HETATM 5490 C8' SOG B 408 19.428 54.993 45.182 1.00 67.02 C HETATM 5491 S1 SOG B 408 11.338 53.928 44.339 1.00 77.47 S HETATM 5492 O2 SOG B 408 10.397 52.785 47.003 1.00 73.18 O HETATM 5493 O3 SOG B 408 8.066 51.143 47.218 1.00 74.11 O HETATM 5494 O4 SOG B 408 7.630 49.355 44.978 1.00 76.54 O HETATM 5495 O5 SOG B 408 9.640 52.089 43.459 1.00 76.79 O HETATM 5496 O6 SOG B 408 8.833 51.119 41.107 1.00 72.51 O HETATM 5497 C1 SOG B 409 3.080 18.891 47.652 1.00 99.47 C HETATM 5498 C2 SOG B 409 2.562 19.420 48.995 1.00101.13 C HETATM 5499 C3 SOG B 409 1.124 18.986 49.270 1.00102.45 C HETATM 5500 C4 SOG B 409 0.184 18.945 48.052 1.00102.13 C HETATM 5501 C5 SOG B 409 0.832 18.943 46.657 1.00100.40 C HETATM 5502 C6 SOG B 409 0.015 19.814 45.698 1.00100.05 C HETATM 5503 C1' SOG B 409 5.446 18.509 46.217 1.00 93.02 C HETATM 5504 C2' SOG B 409 6.343 19.318 45.290 1.00 88.63 C HETATM 5505 C3' SOG B 409 7.734 19.554 45.866 1.00 84.43 C HETATM 5506 C4' SOG B 409 8.404 20.692 45.108 1.00 80.98 C HETATM 5507 C5' SOG B 409 9.885 20.814 45.441 1.00 77.86 C HETATM 5508 C6' SOG B 409 10.416 22.168 44.974 1.00 73.84 C HETATM 5509 C7' SOG B 409 10.866 23.068 46.118 1.00 70.40 C HETATM 5510 C8' SOG B 409 9.739 23.974 46.557 1.00 70.49 C HETATM 5511 S1 SOG B 409 4.688 19.581 47.383 1.00 98.87 S HETATM 5512 O2 SOG B 409 3.381 18.987 50.090 1.00102.14 O HETATM 5513 O3 SOG B 409 0.588 19.813 50.314 1.00103.23 O HETATM 5514 O4 SOG B 409 -0.668 17.795 48.142 1.00102.78 O HETATM 5515 O5 SOG B 409 2.206 19.367 46.620 1.00 99.27 O HETATM 5516 O6 SOG B 409 0.187 21.214 45.947 1.00 99.72 O HETATM 5517 C1 SOG B 410 20.971 49.441 25.565 1.00109.88 C HETATM 5518 C2 SOG B 410 19.962 50.515 25.119 1.00108.88 C HETATM 5519 C3 SOG B 410 19.183 50.000 23.902 1.00109.85 C HETATM 5520 C4 SOG B 410 20.117 49.547 22.770 1.00111.83 C HETATM 5521 C5 SOG B 410 21.111 48.517 23.337 1.00111.88 C HETATM 5522 C6 SOG B 410 22.074 47.910 22.320 1.00112.64 C HETATM 5523 C1' SOG B 410 23.243 48.798 27.019 1.00107.07 C HETATM 5524 C2' SOG B 410 24.513 49.504 27.482 1.00105.92 C HETATM 5525 C3' SOG B 410 25.239 50.190 26.325 1.00104.80 C HETATM 5526 C4' SOG B 410 25.186 51.711 26.449 1.00102.82 C HETATM 5527 C5' SOG B 410 26.063 52.376 25.395 1.00101.80 C HETATM 5528 C6' SOG B 410 27.082 53.305 26.047 1.00101.63 C HETATM 5529 C7' SOG B 410 28.361 53.409 25.221 1.00101.27 C HETATM 5530 C8' SOG B 410 29.584 53.469 26.110 1.00100.77 C HETATM 5531 S1 SOG B 410 21.897 49.944 26.991 1.00109.35 S HETATM 5532 O2 SOG B 410 19.051 50.864 26.169 1.00107.51 O HETATM 5533 O3 SOG B 410 18.226 50.960 23.444 1.00109.55 O HETATM 5534 O4 SOG B 410 19.337 49.001 21.694 1.00113.19 O HETATM 5535 O5 SOG B 410 21.824 49.077 24.457 1.00110.83 O HETATM 5536 O6 SOG B 410 21.886 46.487 22.300 1.00112.98 O HETATM 5537 C1 SOG B 411 16.610 35.643 20.292 1.00 77.98 C HETATM 5538 C2 SOG B 411 15.898 36.082 19.007 1.00 81.03 C HETATM 5539 C3 SOG B 411 14.388 35.849 19.186 1.00 81.05 C HETATM 5540 C4 SOG B 411 14.000 34.494 19.819 1.00 79.33 C HETATM 5541 C5 SOG B 411 15.031 33.916 20.821 1.00 77.36 C HETATM 5542 C6 SOG B 411 14.995 32.407 21.083 1.00 73.96 C HETATM 5543 C1' SOG B 411 18.653 35.481 22.045 1.00 64.55 C HETATM 5544 C2' SOG B 411 19.843 34.530 22.066 1.00 58.18 C HETATM 5545 C3' SOG B 411 19.448 33.089 21.746 1.00 54.33 C HETATM 5546 C4' SOG B 411 20.043 32.676 20.403 1.00 50.52 C HETATM 5547 C5' SOG B 411 20.448 31.207 20.306 1.00 45.68 C HETATM 5548 C6' SOG B 411 21.936 31.038 20.007 1.00 40.88 C HETATM 5549 C7' SOG B 411 22.324 29.569 19.936 1.00 36.16 C HETATM 5550 C8' SOG B 411 23.815 29.387 20.094 1.00 33.71 C HETATM 5551 S1 SOG B 411 18.332 36.047 20.400 1.00 73.05 S HETATM 5552 O2 SOG B 411 16.146 37.466 18.719 1.00 83.74 O HETATM 5553 O3 SOG B 411 13.709 36.034 17.937 1.00 82.36 O HETATM 5554 O4 SOG B 411 12.725 34.638 20.456 1.00 78.55 O HETATM 5555 O5 SOG B 411 16.384 34.237 20.460 1.00 78.66 O HETATM 5556 O6 SOG B 411 14.041 31.694 20.292 1.00 72.22 O HETATM 5557 C1 SOG B 412 37.947 14.915 57.526 1.00 91.02 C HETATM 5558 C2 SOG B 412 39.152 15.501 58.287 1.00 92.60 C HETATM 5559 C3 SOG B 412 39.822 14.434 59.167 1.00 93.20 C HETATM 5560 C4 SOG B 412 38.835 13.576 59.973 1.00 93.38 C HETATM 5561 C5 SOG B 412 37.663 13.099 59.093 1.00 91.82 C HETATM 5562 C6 SOG B 412 36.606 12.293 59.848 1.00 90.50 C HETATM 5563 C1' SOG B 412 35.951 15.199 55.694 1.00 82.75 C HETATM 5564 C2' SOG B 412 35.504 15.970 54.459 1.00 78.32 C HETATM 5565 C3' SOG B 412 34.375 16.928 54.804 1.00 74.93 C HETATM 5566 C4' SOG B 412 34.303 18.046 53.774 1.00 72.70 C HETATM 5567 C5' SOG B 412 33.457 19.218 54.260 1.00 69.91 C HETATM 5568 C6' SOG B 412 31.979 18.989 53.977 1.00 66.89 C HETATM 5569 C7' SOG B 412 31.479 19.895 52.865 1.00 64.77 C HETATM 5570 C8' SOG B 412 30.062 19.505 52.520 1.00 63.80 C HETATM 5571 S1 SOG B 412 37.093 16.174 56.622 1.00 87.94 S HETATM 5572 O2 SOG B 412 40.124 16.032 57.370 1.00 92.59 O HETATM 5573 O3 SOG B 412 40.787 15.034 60.039 1.00 93.05 O HETATM 5574 O4 SOG B 412 39.559 12.457 60.498 1.00 95.11 O HETATM 5575 O5 SOG B 412 37.055 14.221 58.425 1.00 91.55 O HETATM 5576 O6 SOG B 412 36.647 10.926 59.414 1.00 89.54 O HETATM 5577 C1 SOG B 413 58.080 45.315 41.383 1.00114.58 C HETATM 5578 C2 SOG B 413 57.938 45.570 42.892 1.00115.96 C HETATM 5579 C3 SOG B 413 58.634 46.858 43.368 1.00116.99 C HETATM 5580 C4 SOG B 413 59.995 47.142 42.701 1.00117.08 C HETATM 5581 C5 SOG B 413 59.935 46.877 41.186 1.00116.81 C HETATM 5582 C6 SOG B 413 61.267 47.117 40.463 1.00115.74 C HETATM 5583 C1' SOG B 413 57.874 43.563 39.272 1.00108.43 C HETATM 5584 C2' SOG B 413 57.330 42.253 38.707 1.00107.21 C HETATM 5585 C3' SOG B 413 55.873 42.336 38.261 1.00106.97 C HETATM 5586 C4' SOG B 413 55.733 43.022 36.906 1.00107.78 C HETATM 5587 S1 SOG B 413 57.576 43.657 41.006 1.00110.58 S HETATM 5588 O2 SOG B 413 56.547 45.633 43.225 1.00116.29 O HETATM 5589 O3 SOG B 413 58.782 46.825 44.796 1.00117.11 O HETATM 5590 O4 SOG B 413 60.408 48.491 42.978 1.00116.60 O HETATM 5591 O5 SOG B 413 59.435 45.547 40.950 1.00116.83 O HETATM 5592 O6 SOG B 413 61.798 45.910 39.894 1.00114.76 O HETATM 5593 C1 SOG B 414 4.501 29.335 22.082 1.00101.82 C HETATM 5594 C2 SOG B 414 3.859 30.635 21.571 1.00104.14 C HETATM 5595 C3 SOG B 414 4.379 31.864 22.344 1.00104.87 C HETATM 5596 C4 SOG B 414 4.522 31.673 23.869 1.00102.82 C HETATM 5597 C5 SOG B 414 4.928 30.251 24.302 1.00100.93 C HETATM 5598 C6 SOG B 414 4.562 30.007 25.759 1.00 99.25 C HETATM 5599 C1' SOG B 414 3.908 26.630 22.406 1.00 93.95 C HETATM 5600 C2' SOG B 414 5.230 25.892 22.245 1.00 88.52 C HETATM 5601 C3' SOG B 414 5.297 24.656 23.130 1.00 83.68 C HETATM 5602 C4' SOG B 414 6.380 23.723 22.606 1.00 80.29 C HETATM 5603 C5' SOG B 414 6.642 22.574 23.567 1.00 77.36 C HETATM 5604 C6' SOG B 414 7.382 21.447 22.864 1.00 75.22 C HETATM 5605 C7' SOG B 414 7.667 20.319 23.844 1.00 74.63 C HETATM 5606 C8' SOG B 414 7.160 19.002 23.300 1.00 75.00 C HETATM 5607 S1 SOG B 414 3.825 27.940 21.222 1.00 99.14 S HETATM 5608 O2 SOG B 414 4.107 30.791 20.164 1.00104.45 O HETATM 5609 O3 SOG B 414 3.536 32.997 22.082 1.00105.50 O HETATM 5610 O4 SOG B 414 5.474 32.621 24.376 1.00101.90 O HETATM 5611 O5 SOG B 414 4.315 29.224 23.504 1.00101.34 O HETATM 5612 O6 SOG B 414 3.295 29.348 25.890 1.00 98.57 O HETATM 5613 C3' SOG B 415 24.927 40.407 53.179 1.00 74.20 C HETATM 5614 C4' SOG B 415 23.674 41.236 52.916 1.00 71.26 C HETATM 5615 C5' SOG B 415 23.673 41.805 51.502 1.00 68.85 C HETATM 5616 C6' SOG B 415 22.413 41.386 50.755 1.00 67.73 C HETATM 5617 C7' SOG B 415 21.974 42.441 49.743 1.00 66.46 C HETATM 5618 C8' SOG B 415 20.827 41.938 48.893 1.00 65.54 C HETATM 5619 C1 SOG B 416 31.961 40.349 48.211 1.00 94.39 C HETATM 5620 C1' SOG B 416 31.020 37.774 48.602 1.00 90.27 C HETATM 5621 C2' SOG B 416 31.144 36.475 49.394 1.00 86.95 C HETATM 5622 C3' SOG B 416 29.772 35.942 49.798 1.00 85.70 C HETATM 5623 C4' SOG B 416 29.866 34.538 50.392 1.00 84.55 C HETATM 5624 C5' SOG B 416 28.514 33.828 50.477 1.00 82.38 C HETATM 5625 C6' SOG B 416 28.711 32.350 50.812 1.00 81.61 C HETATM 5626 C7' SOG B 416 27.428 31.684 51.315 1.00 81.33 C HETATM 5627 C8' SOG B 416 27.699 30.367 52.022 1.00 79.27 C HETATM 5628 S1 SOG B 416 31.905 39.065 49.418 1.00 94.72 S HETATM 5629 C1' SOG B 417 29.245 41.124 50.847 1.00103.42 C HETATM 5630 C2' SOG B 417 29.015 40.640 52.275 1.00102.22 C HETATM 5631 C3' SOG B 417 29.787 39.354 52.547 1.00101.23 C HETATM 5632 C4' SOG B 417 29.176 38.573 53.707 1.00100.42 C HETATM 5633 C5' SOG B 417 29.454 37.080 53.572 1.00 99.15 C HETATM 5634 C6' SOG B 417 29.892 36.473 54.901 1.00 98.03 C HETATM 5635 C7' SOG B 417 30.454 35.068 54.705 1.00 96.78 C HETATM 5636 C8' SOG B 417 29.896 34.105 55.728 1.00 96.07 C HETATM 5637 S1 SOG B 417 28.816 42.828 50.692 1.00104.71 S HETATM 5638 C1' SOG B 418 32.450 34.572 28.972 1.00 79.67 C HETATM 5639 C2' SOG B 418 33.525 35.520 29.488 1.00 78.23 C HETATM 5640 C3' SOG B 418 33.379 36.882 28.811 1.00 77.83 C HETATM 5641 C4' SOG B 418 32.928 37.976 29.777 1.00 76.51 C HETATM 5642 C5' SOG B 418 33.088 39.354 29.145 1.00 75.67 C HETATM 5643 C6' SOG B 418 34.211 40.140 29.815 1.00 75.07 C HETATM 5644 C7' SOG B 418 34.579 41.378 29.008 1.00 74.79 C HETATM 5645 S1 SOG B 418 33.163 33.064 28.398 1.00 81.75 S HETATM 5646 C1' SOG B 419 40.952 26.705 29.745 1.00 68.33 C HETATM 5647 C2' SOG B 419 41.996 26.130 30.703 1.00 66.05 C HETATM 5648 C3' SOG B 419 43.365 26.774 30.466 1.00 64.31 C HETATM 5649 C4' SOG B 419 44.251 25.875 29.612 1.00 64.36 C HETATM 5650 C5' SOG B 419 45.320 26.646 28.851 1.00 65.79 C HETATM 5651 C6' SOG B 419 46.573 25.790 28.649 1.00 66.73 C HETATM 5652 C7' SOG B 419 47.823 26.657 28.506 1.00 66.22 C HETATM 5653 C8' SOG B 419 48.678 26.224 27.333 1.00 65.95 C HETATM 5654 S1 SOG B 419 39.348 26.012 30.000 1.00 70.06 S HETATM 5655 C1' SOG B 420 49.479 35.193 38.167 1.00 77.45 C HETATM 5656 C2' SOG B 420 50.206 34.043 37.483 1.00 77.11 C HETATM 5657 C3' SOG B 420 50.759 34.499 36.138 1.00 77.39 C HETATM 5658 C4' SOG B 420 52.218 34.098 35.950 1.00 76.88 C HETATM 5659 S1 SOG B 420 48.035 34.586 38.969 1.00 79.28 S HETATM 5660 C1 SOG B 421 37.055 -1.032 41.637 1.00125.12 C HETATM 5661 C2 SOG B 421 35.528 -1.006 41.411 1.00125.11 C HETATM 5662 C3 SOG B 421 35.135 -1.425 39.982 1.00125.24 C HETATM 5663 C4 SOG B 421 35.971 -0.710 38.922 1.00125.00 C HETATM 5664 C5 SOG B 421 37.451 -0.966 39.231 1.00125.13 C HETATM 5665 C6 SOG B 421 38.391 -0.369 38.200 1.00125.60 C HETATM 5666 C1' SOG B 421 39.211 -0.395 43.234 1.00123.62 C HETATM 5667 C2' SOG B 421 39.842 0.870 43.806 1.00122.37 C HETATM 5668 C3' SOG B 421 41.276 0.657 44.280 1.00121.77 C HETATM 5669 C4' SOG B 421 41.609 1.626 45.410 1.00121.25 C HETATM 5670 S1 SOG B 421 37.460 -0.181 43.138 1.00124.74 S HETATM 5671 O2 SOG B 421 34.857 -1.840 42.365 1.00124.78 O HETATM 5672 O3 SOG B 421 33.750 -1.175 39.722 1.00125.32 O HETATM 5673 O4 SOG B 421 35.593 -1.184 37.622 1.00124.68 O HETATM 5674 O5 SOG B 421 37.771 -0.440 40.531 1.00124.97 O HETATM 5675 O6 SOG B 421 38.517 -1.268 37.091 1.00126.36 O HETATM 5676 C1' SOG B 422 30.773 -2.948 41.405 1.00 95.39 C HETATM 5677 C2' SOG B 422 31.364 -1.683 42.012 1.00 93.08 C HETATM 5678 C3' SOG B 422 30.818 -1.423 43.409 1.00 92.45 C HETATM 5679 C4' SOG B 422 29.776 -0.307 43.412 1.00 92.14 C HETATM 5680 C5' SOG B 422 28.915 -0.394 44.669 1.00 92.51 C HETATM 5681 C6' SOG B 422 28.492 0.986 45.159 1.00 91.99 C HETATM 5682 C7' SOG B 422 28.046 0.934 46.614 1.00 91.86 C HETATM 5683 S1 SOG B 422 31.341 -3.122 39.746 1.00 98.25 S HETATM 5684 C1' SOG B 423 4.884 47.528 56.191 1.00 85.39 C HETATM 5685 C2' SOG B 423 5.994 47.210 55.193 1.00 81.11 C HETATM 5686 C3' SOG B 423 7.312 47.832 55.635 1.00 78.20 C HETATM 5687 C4' SOG B 423 8.417 47.551 54.626 1.00 77.89 C HETATM 5688 C5' SOG B 423 9.470 46.585 55.165 1.00 77.32 C HETATM 5689 C6' SOG B 423 10.266 45.952 54.023 1.00 76.33 C HETATM 5690 C7' SOG B 423 11.342 44.986 54.509 1.00 74.87 C HETATM 5691 C8' SOG B 423 11.547 43.877 53.505 1.00 73.17 C HETATM 5692 S1 SOG B 423 4.074 46.050 56.724 1.00 89.06 S HETATM 5693 C1' SOG B 424 45.465 33.247 54.250 1.00 81.29 C HETATM 5694 C2' SOG B 424 45.325 33.853 52.857 1.00 77.53 C HETATM 5695 C3' SOG B 424 46.672 33.972 52.149 1.00 76.22 C HETATM 5696 C4' SOG B 424 46.630 35.047 51.067 1.00 74.64 C HETATM 5697 C5' SOG B 424 47.051 34.506 49.707 1.00 72.29 C HETATM 5698 S1 SOG B 424 45.235 31.492 54.229 1.00 84.58 S HETATM 5699 C1' SOG B 425 42.289 37.270 50.823 1.00 85.03 C HETATM 5700 C2' SOG B 425 41.563 36.304 49.893 1.00 81.37 C HETATM 5701 C3' SOG B 425 42.322 36.111 48.587 1.00 76.51 C HETATM 5702 C4' SOG B 425 41.385 35.543 47.535 1.00 72.93 C HETATM 5703 C5' SOG B 425 41.476 36.384 46.275 1.00 71.71 C HETATM 5704 C6' SOG B 425 41.008 35.592 45.066 1.00 71.59 C HETATM 5705 S1 SOG B 425 41.960 36.813 52.493 1.00 87.30 S HETATM 5706 C1' SOG B 426 43.537 41.509 48.330 1.00 90.49 C HETATM 5707 C2' SOG B 426 42.180 40.834 48.499 1.00 86.94 C HETATM 5708 C3' SOG B 426 41.243 41.228 47.364 1.00 83.83 C HETATM 5709 C4' SOG B 426 40.468 40.025 46.842 1.00 80.81 C HETATM 5710 C5' SOG B 426 39.846 40.308 45.481 1.00 77.92 C HETATM 5711 C6' SOG B 426 39.288 39.023 44.882 1.00 76.22 C HETATM 5712 S1 SOG B 426 44.442 41.452 49.846 1.00 93.75 S HETATM 5713 C1' SOG B 427 -3.419 18.760 29.130 1.00101.57 C HETATM 5714 C2' SOG B 427 -2.169 18.869 28.258 1.00 99.26 C HETATM 5715 C3' SOG B 427 -1.089 17.896 28.725 1.00 97.43 C HETATM 5716 C4' SOG B 427 0.143 17.945 27.826 1.00 95.54 C HETATM 5717 C5' SOG B 427 1.418 17.720 28.630 1.00 94.06 C HETATM 5718 C6' SOG B 427 2.649 17.643 27.732 1.00 93.43 C HETATM 5719 S1 SOG B 427 -4.787 19.587 28.375 1.00103.01 S HETATM 5720 C1' SOG B 428 -1.878 23.210 28.034 1.00 96.32 C HETATM 5721 C2' SOG B 428 -0.854 22.693 27.026 1.00 93.00 C HETATM 5722 C3' SOG B 428 0.542 23.189 27.389 1.00 89.78 C HETATM 5723 C4' SOG B 428 1.639 22.445 26.640 1.00 86.69 C HETATM 5724 C5' SOG B 428 2.846 22.224 27.543 1.00 84.74 C HETATM 5725 C6' SOG B 428 3.913 21.389 26.843 1.00 84.02 C HETATM 5726 S1 SOG B 428 -3.531 22.959 27.464 1.00 99.01 S HETATM 5727 C1' SOG B 429 -1.725 16.441 33.011 1.00 86.51 C HETATM 5728 C2' SOG B 429 -0.556 17.384 32.753 1.00 79.19 C HETATM 5729 C3' SOG B 429 0.708 16.906 33.458 1.00 71.49 C HETATM 5730 C4' SOG B 429 1.853 16.796 32.461 1.00 64.66 C HETATM 5731 C5' SOG B 429 3.195 16.616 33.153 1.00 58.64 C HETATM 5732 C6' SOG B 429 4.185 16.006 32.180 1.00 54.75 C HETATM 5733 S1 SOG B 429 -2.077 15.522 31.547 1.00 92.49 S HETATM 5734 C1' SOG B 430 0.311 24.220 47.509 1.00 77.81 C HETATM 5735 C2' SOG B 430 1.460 24.616 48.430 1.00 71.68 C HETATM 5736 C3' SOG B 430 2.515 23.524 48.472 1.00 68.07 C HETATM 5737 C4' SOG B 430 3.847 24.050 47.955 1.00 68.07 C HETATM 5738 C5' SOG B 430 5.028 23.261 48.517 1.00 67.74 C HETATM 5739 C6' SOG B 430 6.128 23.072 47.477 1.00 67.56 C HETATM 5740 S1 SOG B 430 -0.651 25.643 47.089 1.00 83.93 S HETATM 5741 CAD PGW B 431 22.623 1.942 50.336 1.00101.00 C HETATM 5742 OAE PGW B 431 21.284 2.382 50.075 1.00100.00 O HETATM 5743 OAF PGW B 431 23.314 -0.363 49.947 1.00103.43 O HETATM 5744 P PGW B 431 26.098 2.994 49.553 1.00101.13 P HETATM 5745 C01 PGW B 431 24.780 5.068 46.117 1.00 60.85 C HETATM 5746 C1 PGW B 431 21.659 5.806 47.950 1.00 62.71 C HETATM 5747 O01 PGW B 431 22.778 5.018 47.415 1.00 66.38 O HETATM 5748 C02 PGW B 431 24.077 5.622 47.350 1.00 68.47 C HETATM 5749 C2 PGW B 431 20.248 5.281 47.811 1.00 55.54 C HETATM 5750 O02 PGW B 431 21.837 6.873 48.525 1.00 65.04 O HETATM 5751 C03 PGW B 431 24.880 5.223 48.587 1.00 80.30 C HETATM 5752 C3 PGW B 431 19.520 6.025 46.694 1.00 48.82 C HETATM 5753 O03 PGW B 431 24.627 5.967 45.033 1.00 55.82 O HETATM 5754 C04 PGW B 431 24.266 1.335 48.480 1.00102.20 C HETATM 5755 C4 PGW B 431 18.689 7.161 47.263 1.00 42.60 C HETATM 5756 O04 PGW B 431 26.639 7.061 45.258 1.00 57.19 O HETATM 5757 C05 PGW B 431 23.057 0.893 49.311 1.00102.23 C HETATM 5758 C5 PGW B 431 18.139 8.061 46.170 1.00 40.14 C HETATM 5759 C06 PGW B 431 17.376 13.030 43.517 1.00 41.95 C HETATM 5760 C6 PGW B 431 17.717 9.416 46.733 1.00 40.27 C HETATM 5761 C07 PGW B 431 18.627 12.770 42.701 1.00 37.33 C HETATM 5762 C7 PGW B 431 16.944 10.174 45.665 1.00 43.09 C HETATM 5763 C08 PGW B 431 18.219 12.642 41.239 1.00 36.44 C HETATM 5764 C8 PGW B 431 16.304 11.494 46.106 1.00 44.81 C HETATM 5765 C09 PGW B 431 18.717 11.357 40.598 1.00 35.41 C HETATM 5766 C9 PGW B 431 17.274 12.669 46.028 1.00 47.39 C HETATM 5767 C10 PGW B 431 17.739 13.331 44.950 1.00 45.43 C HETATM 5768 C11 PGW B 431 17.774 10.905 39.494 1.00 35.62 C HETATM 5769 O11 PGW B 431 25.473 3.932 48.389 1.00 91.48 O HETATM 5770 C12 PGW B 431 18.479 10.894 38.148 1.00 36.19 C HETATM 5771 O12 PGW B 431 25.461 1.529 49.250 1.00102.23 O HETATM 5772 C13 PGW B 431 18.504 9.493 37.551 1.00 37.11 C HETATM 5773 O13 PGW B 431 27.592 2.926 49.310 1.00101.64 O HETATM 5774 C14 PGW B 431 18.020 9.518 36.117 1.00 36.99 C HETATM 5775 O14 PGW B 431 25.594 3.443 50.915 1.00102.68 O HETATM 5776 C15 PGW B 431 26.888 13.579 37.337 1.00 37.30 C HETATM 5777 C16 PGW B 431 25.564 14.282 37.027 1.00 41.17 C HETATM 5778 C17 PGW B 431 25.258 14.345 35.529 1.00 43.27 C HETATM 5779 C18 PGW B 431 24.508 15.634 35.201 1.00 43.10 C HETATM 5780 C19 PGW B 431 25.739 6.731 44.509 1.00 52.31 C HETATM 5781 C20 PGW B 431 25.738 7.132 43.054 1.00 44.36 C HETATM 5782 C21 PGW B 431 26.946 7.968 42.661 1.00 36.84 C HETATM 5783 C22 PGW B 431 26.616 8.622 41.337 1.00 33.36 C HETATM 5784 C23 PGW B 431 27.834 9.233 40.671 1.00 31.01 C HETATM 5785 C24 PGW B 431 27.411 10.593 40.142 1.00 33.10 C HETATM 5786 C25 PGW B 431 28.485 11.265 39.291 1.00 33.55 C HETATM 5787 C26 PGW B 431 28.359 12.790 39.270 1.00 33.39 C HETATM 5788 C27 PGW B 431 27.011 13.359 38.841 1.00 33.77 C HETATM 5789 C28 PGW B 431 23.098 15.365 34.691 1.00 42.87 C HETATM 5790 C29 PGW B 431 20.745 16.217 34.685 1.00 42.32 C HETATM 5791 C30 PGW B 431 22.058 16.187 35.439 1.00 42.32 C HETATM 5792 NA NA B 432 28.128 30.176 39.985 1.00 45.25 NA1+ HETATM 5793 O HOH A 501 5.782 -7.962 28.797 1.00 41.92 O HETATM 5794 O HOH A 502 20.101 2.191 16.301 1.00 33.30 O HETATM 5795 O HOH A 503 28.377 22.367 13.862 1.00 33.93 O HETATM 5796 O HOH A 504 18.411 0.616 17.760 1.00 28.95 O HETATM 5797 O HOH A 505 19.533 6.078 39.426 1.00 25.62 O HETATM 5798 O HOH A 506 24.680 1.731 1.277 1.00 46.92 O HETATM 5799 O HOH A 507 6.060 -2.221 43.746 1.00 51.30 O HETATM 5800 O HOH A 508 12.280 -0.570 39.732 1.00 49.16 O HETATM 5801 O HOH A 509 17.680 12.674 17.785 1.00 27.75 O HETATM 5802 O HOH A 510 11.747 -6.654 47.197 1.00 52.49 O HETATM 5803 O HOH A 511 28.140 24.904 14.840 1.00 34.66 O HETATM 5804 O HOH A 512 12.665 4.973 18.227 1.00 34.38 O HETATM 5805 O HOH A 513 14.697 -1.128 24.314 1.00 34.88 O HETATM 5806 O HOH A 514 10.465 -17.971 47.007 1.00 47.99 O HETATM 5807 O HOH A 515 7.572 -1.187 35.613 1.00 35.02 O HETATM 5808 O HOH A 516 6.306 1.687 27.576 1.00 22.00 O HETATM 5809 O HOH A 517 15.024 27.676 12.298 1.00 38.38 O HETATM 5810 O HOH A 518 20.977 11.556 3.407 1.00 36.31 O HETATM 5811 O HOH A 519 -4.808 18.248 42.829 1.00 95.25 O HETATM 5812 O HOH A 520 5.611 7.011 48.605 1.00 42.71 O HETATM 5813 O HOH A 521 14.188 9.759 4.704 1.00 33.80 O HETATM 5814 O HOH A 522 22.054 8.740 8.956 1.00 35.28 O HETATM 5815 O HOH A 523 7.670 -5.395 46.511 1.00 50.72 O HETATM 5816 O HOH A 524 1.797 2.760 44.216 1.00 35.70 O HETATM 5817 O HOH A 525 15.622 -15.189 42.785 1.00 47.34 O HETATM 5818 O HOH A 526 15.509 8.045 1.711 1.00 66.28 O HETATM 5819 O HOH A 527 28.238 18.106 21.256 1.00 74.65 O HETATM 5820 O HOH A 528 -5.536 0.472 42.402 1.00 44.59 O HETATM 5821 O HOH A 529 22.105 -13.368 41.262 1.00 53.23 O HETATM 5822 O HOH A 530 12.192 -14.027 36.744 1.00 48.38 O HETATM 5823 O HOH A 531 27.114 23.046 8.935 1.00 36.98 O HETATM 5824 O HOH A 532 6.572 5.939 46.365 1.00 30.42 O HETATM 5825 O HOH A 533 14.467 -27.037 46.520 1.00 69.51 O HETATM 5826 O HOH A 534 24.043 13.946 14.267 1.00 38.97 O HETATM 5827 O HOH A 535 24.090 10.497 8.131 1.00 39.94 O HETATM 5828 O HOH A 536 22.293 25.573 7.346 1.00 52.83 O HETATM 5829 O HOH A 537 13.354 0.244 30.672 1.00 31.51 O HETATM 5830 O HOH A 538 25.178 15.417 4.790 1.00 61.22 O HETATM 5831 O HOH A 539 23.661 22.460 3.164 1.00 45.16 O HETATM 5832 O HOH A 540 28.387 17.447 3.753 1.00 55.86 O HETATM 5833 O HOH A 541 37.753 2.076 5.888 1.00 64.13 O HETATM 5834 O HOH A 542 24.018 31.403 14.609 1.00 52.37 O HETATM 5835 O HOH A 543 9.714 1.779 39.679 1.00 37.28 O HETATM 5836 O HOH A 544 7.250 -18.573 39.661 1.00 44.87 O HETATM 5837 O HOH A 545 10.054 -9.442 40.837 1.00 40.73 O HETATM 5838 O HOH A 546 21.742 15.388 8.491 1.00 56.72 O HETATM 5839 O HOH A 547 8.822 -0.749 45.959 1.00 35.94 O HETATM 5840 O HOH A 548 21.685 7.657 5.024 1.00 58.85 O HETATM 5841 O HOH A 549 7.477 3.221 46.119 1.00 41.98 O HETATM 5842 O HOH A 550 21.521 22.560 5.049 1.00 37.71 O HETATM 5843 O HOH A 551 10.709 8.074 32.449 1.00 23.26 O HETATM 5844 O HOH A 552 18.818 29.583 11.577 1.00 53.69 O HETATM 5845 O HOH A 553 10.767 -2.575 40.662 1.00 61.05 O HETATM 5846 O HOH A 554 -1.681 2.107 50.437 1.00 45.41 O HETATM 5847 O HOH A 555 -4.600 18.587 45.513 1.00 75.51 O HETATM 5848 O HOH A 556 13.377 6.420 1.719 1.00 66.75 O HETATM 5849 O HOH A 557 7.115 1.601 37.863 1.00 45.99 O HETATM 5850 O HOH A 558 26.412 16.550 19.592 1.00 56.73 O HETATM 5851 O HOH A 559 18.634 -8.191 47.430 1.00 67.84 O HETATM 5852 O HOH A 560 -6.627 -9.779 42.679 1.00 68.25 O HETATM 5853 O HOH A 561 27.901 23.281 5.012 1.00 59.65 O HETATM 5854 O HOH A 562 7.812 -0.611 39.443 1.00 42.98 O HETATM 5855 O HOH A 563 27.329 20.132 14.989 1.00 37.34 O HETATM 5856 O HOH A 564 24.773 24.423 7.425 1.00 47.70 O HETATM 5857 O HOH A 565 16.047 0.009 26.498 1.00 43.64 O HETATM 5858 O HOH A 566 17.926 9.109 5.853 1.00 40.15 O HETATM 5859 O HOH A 567 7.197 -10.307 40.734 1.00 56.68 O HETATM 5860 O HOH A 568 9.896 0.348 49.968 1.00 42.56 O HETATM 5861 O HOH A 569 40.571 17.970 18.401 1.00 78.99 O HETATM 5862 O HOH A 570 20.342 9.036 6.880 1.00 43.84 O HETATM 5863 O HOH A 571 9.229 7.456 34.893 1.00 26.41 O HETATM 5864 O HOH A 572 12.616 7.117 28.679 1.00 41.22 O HETATM 5865 O HOH A 573 35.686 8.176 10.503 1.00 54.82 O HETATM 5866 O HOH A 574 24.220 7.244 5.794 1.00 58.36 O HETATM 5867 O HOH A 575 36.653 5.928 1.292 1.00 71.31 O HETATM 5868 O HOH A 576 31.943 12.136 8.885 1.00 57.19 O HETATM 5869 O HOH A 577 32.938 8.282 1.462 1.00 74.37 O HETATM 5870 O HOH A 578 30.465 15.753 16.468 1.00 53.92 O HETATM 5871 O HOH A 579 36.757 6.179 8.466 1.00 57.78 O HETATM 5872 O HOH A 580 17.112 28.657 13.697 1.00 49.86 O HETATM 5873 O HOH A 581 4.261 -6.681 34.884 1.00 60.50 O HETATM 5874 O HOH A 582 32.375 15.505 9.517 1.00 73.40 O HETATM 5875 O HOH A 583 15.241 -14.364 48.200 1.00 59.29 O HETATM 5876 O HOH A 584 -9.641 -3.075 46.035 1.00 67.11 O HETATM 5877 O HOH A 585 4.549 -9.255 41.405 1.00 62.59 O HETATM 5878 O HOH A 586 30.494 19.882 20.627 1.00 79.40 O HETATM 5879 O HOH A 587 30.675 9.619 5.057 1.00 69.04 O HETATM 5880 O HOH A 588 10.550 -7.581 38.959 1.00 54.78 O HETATM 5881 O HOH A 589 38.568 15.585 14.012 1.00 77.42 O HETATM 5882 O HOH A 590 33.601 5.347 0.811 1.00 63.39 O HETATM 5883 O HOH A 591 22.956 14.171 5.906 1.00 30.00 O HETATM 5884 O HOH A 592 25.789 30.292 12.850 1.00 43.88 O HETATM 5885 O HOH A 593 16.034 -15.380 45.473 1.00 62.60 O HETATM 5886 O HOH A 594 22.671 28.883 7.642 1.00 58.78 O HETATM 5887 O HOH A 595 21.468 32.227 13.720 1.00 68.29 O HETATM 5888 O HOH A 596 4.728 1.712 45.222 1.00 51.37 O HETATM 5889 O HOH A 597 26.112 -5.591 5.463 1.00 64.54 O HETATM 5890 O HOH A 598 29.513 24.881 -7.383 1.00 57.40 O HETATM 5891 O HOH A 599 36.913 13.268 12.145 1.00 56.50 O HETATM 5892 O HOH A 600 14.741 29.255 9.808 1.00 65.01 O HETATM 5893 O HOH A 601 7.886 4.003 53.479 1.00 62.93 O HETATM 5894 O HOH A 602 2.671 7.079 49.209 1.00 54.18 O HETATM 5895 O HOH A 603 10.769 -6.993 34.676 1.00 50.13 O HETATM 5896 O HOH A 604 36.994 8.236 13.989 1.00 66.48 O HETATM 5897 O HOH A 605 6.997 4.074 50.210 1.00 46.38 O HETATM 5898 O HOH A 606 26.383 15.808 1.464 1.00 46.33 O HETATM 5899 O HOH A 607 18.523 6.625 -2.085 1.00 74.35 O HETATM 5900 O HOH A 608 12.930 15.165 1.824 1.00 64.18 O HETATM 5901 O HOH A 609 27.654 19.756 19.162 1.00 64.94 O HETATM 5902 O HOH A 610 35.025 16.159 8.999 1.00 76.22 O HETATM 5903 O HOH B 501 33.921 30.938 40.261 1.00 29.94 O HETATM 5904 O HOH B 502 37.958 16.491 38.618 1.00 33.09 O HETATM 5905 O HOH B 503 31.916 18.882 41.854 1.00 22.34 O HETATM 5906 O HOH B 504 35.915 28.798 39.524 1.00 36.91 O HETATM 5907 O HOH B 505 42.306 21.576 42.321 1.00 30.17 O HETATM 5908 O HOH B 506 2.738 33.153 41.201 1.00 41.17 O HETATM 5909 O HOH B 507 19.571 32.307 45.629 1.00 26.57 O HETATM 5910 O HOH B 508 30.331 27.410 45.343 1.00 30.18 O HETATM 5911 O HOH B 509 36.471 36.180 43.947 1.00 36.89 O HETATM 5912 O HOH B 510 0.817 29.381 35.294 1.00 37.11 O HETATM 5913 O HOH B 511 26.903 33.601 39.655 1.00 43.79 O HETATM 5914 O HOH B 512 39.162 7.580 35.621 1.00 32.94 O HETATM 5915 O HOH B 513 3.328 30.049 36.161 1.00 30.64 O HETATM 5916 O HOH B 514 11.041 32.707 36.365 1.00 35.32 O HETATM 5917 O HOH B 515 30.268 3.110 43.484 1.00 40.03 O HETATM 5918 O HOH B 516 3.576 57.936 43.858 1.00 70.83 O HETATM 5919 O HOH B 517 43.301 7.628 46.278 1.00 41.36 O HETATM 5920 O HOH B 518 6.817 41.842 30.335 1.00 56.68 O HETATM 5921 O HOH B 519 6.089 50.435 50.696 1.00 45.15 O HETATM 5922 O HOH B 520 15.307 27.173 28.372 1.00 25.66 O HETATM 5923 O HOH B 521 12.466 34.759 34.141 1.00 56.24 O HETATM 5924 O HOH B 522 20.469 33.028 37.665 1.00 25.06 O HETATM 5925 O HOH B 523 -2.777 28.087 36.759 1.00 36.29 O HETATM 5926 O HOH B 524 12.544 44.332 41.432 1.00 48.38 O HETATM 5927 O HOH B 525 18.293 45.947 23.543 1.00 41.24 O HETATM 5928 O HOH B 526 41.713 21.380 51.211 1.00 34.83 O HETATM 5929 O HOH B 527 -3.297 35.850 47.292 1.00 75.07 O HETATM 5930 O HOH B 528 7.250 35.072 24.047 1.00 71.51 O HETATM 5931 O HOH B 529 50.253 21.961 48.918 1.00 59.20 O HETATM 5932 O HOH B 530 11.577 37.699 18.267 1.00 66.32 O HETATM 5933 O HOH B 531 38.349 10.108 36.016 1.00 30.23 O HETATM 5934 O HOH B 532 -2.779 30.528 41.079 1.00 56.58 O HETATM 5935 O HOH B 533 11.632 45.315 49.511 1.00 32.81 O HETATM 5936 O HOH B 534 13.677 41.776 42.229 1.00 42.22 O HETATM 5937 O HOH B 535 53.790 33.079 46.125 1.00 47.36 O HETATM 5938 O HOH B 536 43.819 19.556 41.139 1.00 33.52 O HETATM 5939 O HOH B 537 46.321 15.731 39.400 1.00 59.79 O HETATM 5940 O HOH B 538 16.384 51.199 25.450 1.00 61.64 O HETATM 5941 O HOH B 539 54.466 2.589 44.738 1.00 31.00 O HETATM 5942 O HOH B 540 -2.512 31.722 43.554 1.00 53.75 O HETATM 5943 O HOH B 541 -1.153 30.230 37.553 1.00 58.52 O HETATM 5944 O HOH B 542 20.962 25.967 39.893 1.00 31.55 O HETATM 5945 O HOH B 543 37.715 5.209 35.424 1.00 22.60 O HETATM 5946 O HOH B 544 4.385 32.198 34.874 1.00 44.82 O HETATM 5947 O HOH B 545 45.983 18.365 46.503 1.00 41.29 O HETATM 5948 O HOH B 546 13.761 35.566 39.981 1.00 39.47 O HETATM 5949 O HOH B 547 11.941 44.122 34.132 1.00 33.92 O HETATM 5950 O HOH B 548 3.599 39.998 45.833 1.00 52.00 O HETATM 5951 O HOH B 549 14.079 48.957 28.008 1.00 46.81 O HETATM 5952 O HOH B 550 42.926 21.575 47.490 1.00 36.21 O HETATM 5953 O HOH B 551 61.160 41.327 43.260 1.00 61.51 O HETATM 5954 O HOH B 552 43.032 8.197 33.675 1.00 55.74 O HETATM 5955 O HOH B 553 5.494 36.037 33.651 1.00 27.81 O HETATM 5956 O HOH B 554 2.662 35.057 30.793 1.00 51.43 O HETATM 5957 O HOH B 555 45.020 24.731 52.230 1.00 39.12 O HETATM 5958 O HOH B 556 51.255 27.311 43.008 1.00 29.87 O HETATM 5959 O HOH B 557 1.877 28.592 39.044 1.00 47.58 O HETATM 5960 O HOH B 558 2.038 33.383 48.541 1.00 45.57 O HETATM 5961 O HOH B 559 34.631 1.344 44.805 1.00 57.75 O HETATM 5962 O HOH B 560 54.071 24.931 30.425 1.00 55.55 O HETATM 5963 O HOH B 561 25.656 32.501 37.790 1.00 38.05 O HETATM 5964 O HOH B 562 5.182 40.812 33.559 1.00 54.45 O HETATM 5965 O HOH B 563 16.944 47.427 33.995 1.00 44.53 O HETATM 5966 O HOH B 564 33.106 4.281 48.416 1.00 41.60 O HETATM 5967 O HOH B 565 10.212 41.960 23.629 1.00 58.59 O HETATM 5968 O HOH B 566 48.502 22.067 51.274 1.00 73.19 O HETATM 5969 O HOH B 567 16.671 25.754 39.688 1.00 28.12 O HETATM 5970 O HOH B 568 17.502 39.370 20.387 1.00 55.56 O HETATM 5971 O HOH B 569 5.099 50.124 46.115 1.00 82.54 O HETATM 5972 O HOH B 570 13.848 26.793 39.896 1.00 22.10 O HETATM 5973 O HOH B 571 11.375 33.334 39.569 1.00 40.62 O HETATM 5974 O HOH B 572 31.813 0.127 50.910 1.00 77.76 O HETATM 5975 O HOH B 573 -0.561 29.005 46.052 1.00 56.61 O HETATM 5976 O HOH B 574 49.387 18.390 40.441 1.00 84.54 O HETATM 5977 O HOH B 575 45.526 22.169 51.765 1.00 62.00 O HETATM 5978 O HOH B 576 44.350 28.438 54.501 1.00 55.42 O HETATM 5979 O HOH B 577 42.326 5.195 42.972 1.00 49.63 O HETATM 5980 O HOH B 578 16.784 40.805 38.669 1.00 30.32 O HETATM 5981 O HOH B 579 42.648 16.691 39.458 1.00 45.82 O HETATM 5982 O HOH B 580 1.846 46.621 48.432 1.00 69.87 O HETATM 5983 O HOH B 581 -3.000 41.001 50.070 1.00 59.70 O HETATM 5984 O HOH B 582 45.460 22.638 43.893 1.00 61.20 O HETATM 5985 O HOH B 583 43.170 21.296 44.879 1.00 44.73 O HETATM 5986 O HOH B 584 13.288 41.884 34.855 1.00 57.91 O HETATM 5987 O HOH B 585 40.500 14.633 44.705 1.00 39.03 O HETATM 5988 O HOH B 586 42.404 6.859 38.508 1.00 37.99 O HETATM 5989 O HOH B 587 -0.380 33.537 46.208 1.00 48.90 O HETATM 5990 O HOH B 588 10.816 35.569 38.147 1.00 56.63 O HETATM 5991 O HOH B 589 11.795 37.213 35.022 1.00 52.22 O HETATM 5992 O HOH B 590 44.922 15.700 36.495 1.00 37.33 O HETATM 5993 O HOH B 591 42.728 15.717 42.662 1.00 62.05 O HETATM 5994 O HOH B 592 5.957 43.263 53.477 1.00 42.16 O HETATM 5995 O HOH B 593 37.871 9.350 22.160 1.00 61.70 O HETATM 5996 O HOH B 594 43.640 24.294 54.840 1.00 58.92 O HETATM 5997 O HOH B 595 -5.674 23.042 45.610 1.00 61.66 O HETATM 5998 O HOH B 596 55.019 32.056 35.248 1.00 45.70 O HETATM 5999 O HOH B 597 10.736 43.131 39.139 1.00 50.28 O HETATM 6000 O HOH B 598 32.711 3.156 45.961 1.00 43.56 O HETATM 6001 O HOH B 599 34.504 2.058 50.104 1.00 50.08 O HETATM 6002 O HOH B 600 3.365 33.318 50.903 1.00 64.16 O HETATM 6003 O HOH B 601 14.549 40.035 37.339 1.00 47.81 O CONECT 381 5342 CONECT 581 1211 CONECT 1211 581 CONECT 1835 5342 CONECT 2154 5342 CONECT 2929 5792 CONECT 3129 3683 CONECT 3683 3129 CONECT 4295 5792 CONECT 4614 5792 CONECT 4879 4906 4907 4911 CONECT 4880 4894 4900 4912 4913 CONECT 4881 4882 4894 4895 CONECT 4882 4881 4897 4914 CONECT 4883 4899 4915 4916 4917 CONECT 4884 4887 4890 4891 CONECT 4885 4889 4890 4918 CONECT 4886 4887 4919 4920 4921 CONECT 4887 4884 4886 4888 CONECT 4888 4887 4889 4922 CONECT 4889 4885 4888 4923 CONECT 4890 4884 4885 4924 CONECT 4891 4884 4892 4893 4894 CONECT 4892 4891 CONECT 4893 4891 CONECT 4894 4880 4881 4891 CONECT 4895 4881 4896 4925 CONECT 4896 4895 4898 CONECT 4897 4882 4898 4926 CONECT 4898 4896 4897 4899 CONECT 4899 4883 4898 CONECT 4900 4880 4901 4902 CONECT 4901 4900 CONECT 4902 4900 4903 4905 CONECT 4903 4902 4904 4927 4928 CONECT 4904 4903 4929 4930 4931 CONECT 4905 4902 4906 4932 4933 CONECT 4906 4879 4905 4910 CONECT 4907 4879 4908 4934 CONECT 4908 4907 4909 4935 CONECT 4909 4908 4910 CONECT 4910 4906 4909 4936 CONECT 4911 4879 CONECT 4912 4880 CONECT 4913 4880 CONECT 4914 4882 CONECT 4915 4883 CONECT 4916 4883 CONECT 4917 4883 CONECT 4918 4885 CONECT 4919 4886 CONECT 4920 4886 CONECT 4921 4886 CONECT 4922 4888 CONECT 4923 4889 CONECT 4924 4890 CONECT 4925 4895 CONECT 4926 4897 CONECT 4927 4903 CONECT 4928 4903 CONECT 4929 4904 CONECT 4930 4904 CONECT 4931 4904 CONECT 4932 4905 CONECT 4933 4905 CONECT 4934 4907 CONECT 4935 4908 CONECT 4936 4910 CONECT 4937 4938 4939 4940 4941 CONECT 4938 4937 CONECT 4939 4937 CONECT 4940 4937 CONECT 4941 4937 CONECT 4942 4943 CONECT 4943 4942 4944 CONECT 4944 4943 4945 CONECT 4945 4944 4946 CONECT 4946 4945 4947 CONECT 4947 4946 4948 CONECT 4948 4947 4949 CONECT 4949 4948 4950 CONECT 4950 4949 4951 CONECT 4951 4950 4952 CONECT 4952 4951 4953 CONECT 4953 4952 4954 CONECT 4954 4953 CONECT 4955 4956 CONECT 4956 4955 4957 CONECT 4957 4956 4958 CONECT 4958 4957 4959 CONECT 4959 4958 4960 CONECT 4960 4959 4961 CONECT 4961 4960 4962 CONECT 4962 4961 4963 CONECT 4963 4962 4964 CONECT 4964 4963 4965 CONECT 4965 4964 4966 CONECT 4966 4965 4967 CONECT 4967 4966 CONECT 4968 4969 CONECT 4969 4968 4970 CONECT 4970 4969 4971 CONECT 4971 4970 4972 CONECT 4972 4971 4973 CONECT 4973 4972 4974 CONECT 4974 4973 4975 CONECT 4975 4974 4976 CONECT 4976 4975 4977 CONECT 4977 4976 4978 CONECT 4978 4977 4979 CONECT 4979 4978 4980 CONECT 4980 4979 CONECT 4981 4982 4983 4984 CONECT 4982 4981 CONECT 4983 4981 CONECT 4984 4981 4985 CONECT 4985 4984 4986 4987 4991 CONECT 4986 4985 CONECT 4987 4985 4988 CONECT 4988 4987 4989 4990 CONECT 4989 4988 CONECT 4990 4988 CONECT 4991 4985 4992 4993 CONECT 4992 4991 CONECT 4993 4991 CONECT 4994 4995 5005 5009 CONECT 4995 4994 4996 5006 CONECT 4996 4995 4997 5007 CONECT 4997 4996 4998 5008 CONECT 4998 4997 4999 5009 CONECT 4999 4998 5010 CONECT 5000 5001 5005 CONECT 5001 5000 5002 CONECT 5002 5001 5003 CONECT 5003 5002 5004 CONECT 5004 5003 CONECT 5005 4994 5000 CONECT 5006 4995 CONECT 5007 4996 CONECT 5008 4997 CONECT 5009 4994 4998 CONECT 5010 4999 CONECT 5011 5012 5021 5025 CONECT 5012 5011 5013 5022 CONECT 5013 5012 5014 5023 CONECT 5014 5013 5015 5024 CONECT 5015 5014 5016 5025 CONECT 5016 5015 5026 CONECT 5017 5018 5021 CONECT 5018 5017 5019 CONECT 5019 5018 5020 CONECT 5020 5019 CONECT 5021 5011 5017 CONECT 5022 5012 CONECT 5023 5013 CONECT 5024 5014 CONECT 5025 5011 5015 CONECT 5026 5016 CONECT 5027 5028 5041 5045 CONECT 5028 5027 5029 5042 CONECT 5029 5028 5030 5043 CONECT 5030 5029 5031 5044 CONECT 5031 5030 5032 5045 CONECT 5032 5031 5046 CONECT 5033 5034 5041 CONECT 5034 5033 5035 CONECT 5035 5034 5036 CONECT 5036 5035 5037 CONECT 5037 5036 5038 CONECT 5038 5037 5039 CONECT 5039 5038 5040 CONECT 5040 5039 CONECT 5041 5027 5033 CONECT 5042 5028 CONECT 5043 5029 CONECT 5044 5030 CONECT 5045 5027 5031 CONECT 5046 5032 CONECT 5047 5048 5061 5065 CONECT 5048 5047 5049 5062 CONECT 5049 5048 5050 5063 CONECT 5050 5049 5051 5064 CONECT 5051 5050 5052 5065 CONECT 5052 5051 5066 CONECT 5053 5054 5061 CONECT 5054 5053 5055 CONECT 5055 5054 5056 CONECT 5056 5055 5057 CONECT 5057 5056 5058 CONECT 5058 5057 5059 CONECT 5059 5058 5060 CONECT 5060 5059 CONECT 5061 5047 5053 CONECT 5062 5048 CONECT 5063 5049 CONECT 5064 5050 CONECT 5065 5047 5051 CONECT 5066 5052 CONECT 5067 5068 5081 5085 CONECT 5068 5067 5069 5082 CONECT 5069 5068 5070 5083 CONECT 5070 5069 5071 5084 CONECT 5071 5070 5072 5085 CONECT 5072 5071 5086 CONECT 5073 5074 5081 CONECT 5074 5073 5075 CONECT 5075 5074 5076 CONECT 5076 5075 5077 CONECT 5077 5076 5078 CONECT 5078 5077 5079 CONECT 5079 5078 5080 CONECT 5080 5079 CONECT 5081 5067 5073 CONECT 5082 5068 CONECT 5083 5069 CONECT 5084 5070 CONECT 5085 5067 5071 CONECT 5086 5072 CONECT 5087 5088 5101 5105 CONECT 5088 5087 5089 5102 CONECT 5089 5088 5090 5103 CONECT 5090 5089 5091 5104 CONECT 5091 5090 5092 5105 CONECT 5092 5091 5106 CONECT 5093 5094 5101 CONECT 5094 5093 5095 CONECT 5095 5094 5096 CONECT 5096 5095 5097 CONECT 5097 5096 5098 CONECT 5098 5097 5099 CONECT 5099 5098 5100 CONECT 5100 5099 CONECT 5101 5087 5093 CONECT 5102 5088 CONECT 5103 5089 CONECT 5104 5090 CONECT 5105 5087 5091 CONECT 5106 5092 CONECT 5107 5108 5121 5125 CONECT 5108 5107 5109 5122 CONECT 5109 5108 5110 5123 CONECT 5110 5109 5111 5124 CONECT 5111 5110 5112 5125 CONECT 5112 5111 5126 CONECT 5113 5114 5121 CONECT 5114 5113 5115 CONECT 5115 5114 5116 CONECT 5116 5115 5117 CONECT 5117 5116 5118 CONECT 5118 5117 5119 CONECT 5119 5118 5120 CONECT 5120 5119 CONECT 5121 5107 5113 CONECT 5122 5108 CONECT 5123 5109 CONECT 5124 5110 CONECT 5125 5107 5111 CONECT 5126 5112 CONECT 5127 5128 5141 5145 CONECT 5128 5127 5129 5142 CONECT 5129 5128 5130 5143 CONECT 5130 5129 5131 5144 CONECT 5131 5130 5132 5145 CONECT 5132 5131 5146 CONECT 5133 5134 5141 CONECT 5134 5133 5135 CONECT 5135 5134 5136 CONECT 5136 5135 5137 CONECT 5137 5136 5138 CONECT 5138 5137 5139 CONECT 5139 5138 5140 CONECT 5140 5139 CONECT 5141 5127 5133 CONECT 5142 5128 CONECT 5143 5129 CONECT 5144 5130 CONECT 5145 5127 5131 CONECT 5146 5132 CONECT 5147 5148 5155 5159 CONECT 5148 5147 5149 5156 CONECT 5149 5148 5150 5157 CONECT 5150 5149 5151 5158 CONECT 5151 5150 5152 5159 CONECT 5152 5151 5160 CONECT 5153 5154 5155 CONECT 5154 5153 CONECT 5155 5147 5153 CONECT 5156 5148 CONECT 5157 5149 CONECT 5158 5150 CONECT 5159 5147 5151 CONECT 5160 5152 CONECT 5161 5162 5175 5179 CONECT 5162 5161 5163 5176 CONECT 5163 5162 5164 5177 CONECT 5164 5163 5165 5178 CONECT 5165 5164 5166 5179 CONECT 5166 5165 5180 CONECT 5167 5168 5175 CONECT 5168 5167 5169 CONECT 5169 5168 5170 CONECT 5170 5169 5171 CONECT 5171 5170 5172 CONECT 5172 5171 5173 CONECT 5173 5172 5174 CONECT 5174 5173 CONECT 5175 5161 5167 CONECT 5176 5162 CONECT 5177 5163 CONECT 5178 5164 CONECT 5179 5161 5165 CONECT 5180 5166 CONECT 5181 5182 5195 5199 CONECT 5182 5181 5183 5196 CONECT 5183 5182 5184 5197 CONECT 5184 5183 5185 5198 CONECT 5185 5184 5186 5199 CONECT 5186 5185 5200 CONECT 5187 5188 5195 CONECT 5188 5187 5189 CONECT 5189 5188 5190 CONECT 5190 5189 5191 CONECT 5191 5190 5192 CONECT 5192 5191 5193 CONECT 5193 5192 5194 CONECT 5194 5193 CONECT 5195 5181 5187 CONECT 5196 5182 CONECT 5197 5183 CONECT 5198 5184 CONECT 5199 5181 5185 CONECT 5200 5186 CONECT 5201 5202 5215 5219 CONECT 5202 5201 5203 5216 CONECT 5203 5202 5204 5217 CONECT 5204 5203 5205 5218 CONECT 5205 5204 5206 5219 CONECT 5206 5205 5220 CONECT 5207 5208 5215 CONECT 5208 5207 5209 CONECT 5209 5208 5210 CONECT 5210 5209 5211 CONECT 5211 5210 5212 CONECT 5212 5211 5213 CONECT 5213 5212 5214 CONECT 5214 5213 CONECT 5215 5201 5207 CONECT 5216 5202 CONECT 5217 5203 CONECT 5218 5204 CONECT 5219 5201 5205 CONECT 5220 5206 CONECT 5221 5222 5227 CONECT 5222 5221 5223 CONECT 5223 5222 5224 CONECT 5224 5223 5225 CONECT 5225 5224 5226 CONECT 5226 5225 CONECT 5227 5221 CONECT 5228 5229 5234 CONECT 5229 5228 5230 CONECT 5230 5229 5231 CONECT 5231 5230 5232 CONECT 5232 5231 5233 CONECT 5233 5232 CONECT 5234 5228 CONECT 5235 5236 5241 CONECT 5236 5235 5237 CONECT 5237 5236 5238 CONECT 5238 5237 5239 CONECT 5239 5238 5240 CONECT 5240 5239 CONECT 5241 5235 CONECT 5242 5243 5248 CONECT 5243 5242 5244 CONECT 5244 5243 5245 CONECT 5245 5244 5246 CONECT 5246 5245 5247 CONECT 5247 5246 CONECT 5248 5242 CONECT 5249 5250 5255 CONECT 5250 5249 5251 CONECT 5251 5250 5252 CONECT 5252 5251 5253 CONECT 5253 5252 5254 CONECT 5254 5253 CONECT 5255 5249 CONECT 5256 5257 5262 CONECT 5257 5256 5258 CONECT 5258 5257 5259 CONECT 5259 5258 5260 CONECT 5260 5259 5261 CONECT 5261 5260 CONECT 5262 5256 CONECT 5263 5264 5269 CONECT 5264 5263 5265 CONECT 5265 5264 5266 CONECT 5266 5265 5267 CONECT 5267 5266 5268 CONECT 5268 5267 CONECT 5269 5263 CONECT 5270 5271 5276 CONECT 5271 5270 5272 CONECT 5272 5271 5273 CONECT 5273 5272 5274 CONECT 5274 5273 5275 CONECT 5275 5274 CONECT 5276 5270 CONECT 5277 5278 5283 CONECT 5278 5277 5279 CONECT 5279 5278 5280 CONECT 5280 5279 5281 CONECT 5281 5280 5282 CONECT 5282 5281 CONECT 5283 5277 CONECT 5284 5285 5290 CONECT 5285 5284 5286 CONECT 5286 5285 5287 CONECT 5287 5286 5288 CONECT 5288 5287 5289 CONECT 5289 5288 CONECT 5290 5284 CONECT 5291 5292 5307 CONECT 5292 5291 CONECT 5293 5307 CONECT 5294 5319 5321 5323 5325 CONECT 5295 5298 5303 CONECT 5296 5297 5299 5300 CONECT 5297 5296 5298 CONECT 5298 5295 5297 5301 CONECT 5299 5296 5302 CONECT 5300 5296 CONECT 5301 5298 5319 CONECT 5302 5299 5305 CONECT 5303 5295 5330 CONECT 5304 5307 5321 CONECT 5305 5302 5308 CONECT 5306 5330 CONECT 5307 5291 5293 5304 CONECT 5308 5305 5310 CONECT 5309 5311 5317 CONECT 5310 5308 5312 CONECT 5311 5309 5313 CONECT 5312 5310 5314 CONECT 5313 5311 5315 CONECT 5314 5312 5316 CONECT 5315 5313 5318 CONECT 5316 5314 5317 CONECT 5317 5309 5316 CONECT 5318 5315 5320 CONECT 5319 5294 5301 CONECT 5320 5318 5322 CONECT 5321 5294 5304 CONECT 5322 5320 5324 CONECT 5323 5294 CONECT 5324 5322 CONECT 5325 5294 CONECT 5326 5327 5338 CONECT 5327 5326 5328 CONECT 5328 5327 5329 CONECT 5329 5328 5339 CONECT 5330 5303 5306 5331 CONECT 5331 5330 5332 CONECT 5332 5331 5333 CONECT 5333 5332 5334 CONECT 5334 5333 5335 CONECT 5335 5334 5336 CONECT 5336 5335 5337 CONECT 5337 5336 5338 CONECT 5338 5326 5337 CONECT 5339 5329 5341 CONECT 5340 5341 CONECT 5341 5339 5340 CONECT 5342 381 1835 2154 CONECT 5343 5370 5371 5375 CONECT 5344 5358 5364 5376 5377 CONECT 5345 5346 5358 5359 CONECT 5346 5345 5361 5378 CONECT 5347 5363 5379 5380 5381 CONECT 5348 5351 5354 5355 CONECT 5349 5353 5354 5382 CONECT 5350 5351 5383 5384 5385 CONECT 5351 5348 5350 5352 CONECT 5352 5351 5353 5386 CONECT 5353 5349 5352 5387 CONECT 5354 5348 5349 5388 CONECT 5355 5348 5356 5357 5358 CONECT 5356 5355 CONECT 5357 5355 CONECT 5358 5344 5345 5355 CONECT 5359 5345 5360 5389 CONECT 5360 5359 5362 CONECT 5361 5346 5362 5390 CONECT 5362 5360 5361 5363 CONECT 5363 5347 5362 CONECT 5364 5344 5365 5366 CONECT 5365 5364 CONECT 5366 5364 5367 5369 CONECT 5367 5366 5368 5391 5392 CONECT 5368 5367 5393 5394 5395 CONECT 5369 5366 5370 5396 5397 CONECT 5370 5343 5369 5374 CONECT 5371 5343 5372 5398 CONECT 5372 5371 5373 5399 CONECT 5373 5372 5374 CONECT 5374 5370 5373 5400 CONECT 5375 5343 CONECT 5376 5344 CONECT 5377 5344 CONECT 5378 5346 CONECT 5379 5347 CONECT 5380 5347 CONECT 5381 5347 CONECT 5382 5349 CONECT 5383 5350 CONECT 5384 5350 CONECT 5385 5350 CONECT 5386 5352 CONECT 5387 5353 CONECT 5388 5354 CONECT 5389 5359 CONECT 5390 5361 CONECT 5391 5367 CONECT 5392 5367 CONECT 5393 5368 CONECT 5394 5368 CONECT 5395 5368 CONECT 5396 5369 CONECT 5397 5369 CONECT 5398 5371 CONECT 5399 5372 CONECT 5400 5374 CONECT 5401 5402 5403 5404 5405 CONECT 5402 5401 CONECT 5403 5401 CONECT 5404 5401 CONECT 5405 5401 CONECT 5406 5407 5408 5409 5410 CONECT 5407 5406 CONECT 5408 5406 CONECT 5409 5406 CONECT 5410 5406 CONECT 5411 5412 CONECT 5412 5411 5413 CONECT 5413 5412 5414 CONECT 5414 5413 5415 CONECT 5415 5414 5416 CONECT 5416 5415 5417 CONECT 5417 5416 5418 CONECT 5418 5417 5419 CONECT 5419 5418 5420 CONECT 5420 5419 5421 CONECT 5421 5420 5422 CONECT 5422 5421 5423 CONECT 5423 5422 CONECT 5424 5425 CONECT 5425 5424 5426 CONECT 5426 5425 5427 CONECT 5427 5426 5428 CONECT 5428 5427 5429 CONECT 5429 5428 5430 CONECT 5430 5429 5431 CONECT 5431 5430 5432 CONECT 5432 5431 5433 CONECT 5433 5432 5434 CONECT 5434 5433 5435 CONECT 5435 5434 5436 CONECT 5436 5435 CONECT 5437 5438 5451 5455 CONECT 5438 5437 5439 5452 CONECT 5439 5438 5440 5453 CONECT 5440 5439 5441 5454 CONECT 5441 5440 5442 5455 CONECT 5442 5441 5456 CONECT 5443 5444 5451 CONECT 5444 5443 5445 CONECT 5445 5444 5446 CONECT 5446 5445 5447 CONECT 5447 5446 5448 CONECT 5448 5447 5449 CONECT 5449 5448 5450 CONECT 5450 5449 CONECT 5451 5437 5443 CONECT 5452 5438 CONECT 5453 5439 CONECT 5454 5440 CONECT 5455 5437 5441 CONECT 5456 5442 CONECT 5457 5458 5471 5475 CONECT 5458 5457 5459 5472 CONECT 5459 5458 5460 5473 CONECT 5460 5459 5461 5474 CONECT 5461 5460 5462 5475 CONECT 5462 5461 5476 CONECT 5463 5464 5471 CONECT 5464 5463 5465 CONECT 5465 5464 5466 CONECT 5466 5465 5467 CONECT 5467 5466 5468 CONECT 5468 5467 5469 CONECT 5469 5468 5470 CONECT 5470 5469 CONECT 5471 5457 5463 CONECT 5472 5458 CONECT 5473 5459 CONECT 5474 5460 CONECT 5475 5457 5461 CONECT 5476 5462 CONECT 5477 5478 5491 5495 CONECT 5478 5477 5479 5492 CONECT 5479 5478 5480 5493 CONECT 5480 5479 5481 5494 CONECT 5481 5480 5482 5495 CONECT 5482 5481 5496 CONECT 5483 5484 5491 CONECT 5484 5483 5485 CONECT 5485 5484 5486 CONECT 5486 5485 5487 CONECT 5487 5486 5488 CONECT 5488 5487 5489 CONECT 5489 5488 5490 CONECT 5490 5489 CONECT 5491 5477 5483 CONECT 5492 5478 CONECT 5493 5479 CONECT 5494 5480 CONECT 5495 5477 5481 CONECT 5496 5482 CONECT 5497 5498 5511 5515 CONECT 5498 5497 5499 5512 CONECT 5499 5498 5500 5513 CONECT 5500 5499 5501 5514 CONECT 5501 5500 5502 5515 CONECT 5502 5501 5516 CONECT 5503 5504 5511 CONECT 5504 5503 5505 CONECT 5505 5504 5506 CONECT 5506 5505 5507 CONECT 5507 5506 5508 CONECT 5508 5507 5509 CONECT 5509 5508 5510 CONECT 5510 5509 CONECT 5511 5497 5503 CONECT 5512 5498 CONECT 5513 5499 CONECT 5514 5500 CONECT 5515 5497 5501 CONECT 5516 5502 CONECT 5517 5518 5531 5535 CONECT 5518 5517 5519 5532 CONECT 5519 5518 5520 5533 CONECT 5520 5519 5521 5534 CONECT 5521 5520 5522 5535 CONECT 5522 5521 5536 CONECT 5523 5524 5531 CONECT 5524 5523 5525 CONECT 5525 5524 5526 CONECT 5526 5525 5527 CONECT 5527 5526 5528 CONECT 5528 5527 5529 CONECT 5529 5528 5530 CONECT 5530 5529 CONECT 5531 5517 5523 CONECT 5532 5518 CONECT 5533 5519 CONECT 5534 5520 CONECT 5535 5517 5521 CONECT 5536 5522 CONECT 5537 5538 5551 5555 CONECT 5538 5537 5539 5552 CONECT 5539 5538 5540 5553 CONECT 5540 5539 5541 5554 CONECT 5541 5540 5542 5555 CONECT 5542 5541 5556 CONECT 5543 5544 5551 CONECT 5544 5543 5545 CONECT 5545 5544 5546 CONECT 5546 5545 5547 CONECT 5547 5546 5548 CONECT 5548 5547 5549 CONECT 5549 5548 5550 CONECT 5550 5549 CONECT 5551 5537 5543 CONECT 5552 5538 CONECT 5553 5539 CONECT 5554 5540 CONECT 5555 5537 5541 CONECT 5556 5542 CONECT 5557 5558 5571 5575 CONECT 5558 5557 5559 5572 CONECT 5559 5558 5560 5573 CONECT 5560 5559 5561 5574 CONECT 5561 5560 5562 5575 CONECT 5562 5561 5576 CONECT 5563 5564 5571 CONECT 5564 5563 5565 CONECT 5565 5564 5566 CONECT 5566 5565 5567 CONECT 5567 5566 5568 CONECT 5568 5567 5569 CONECT 5569 5568 5570 CONECT 5570 5569 CONECT 5571 5557 5563 CONECT 5572 5558 CONECT 5573 5559 CONECT 5574 5560 CONECT 5575 5557 5561 CONECT 5576 5562 CONECT 5577 5578 5587 5591 CONECT 5578 5577 5579 5588 CONECT 5579 5578 5580 5589 CONECT 5580 5579 5581 5590 CONECT 5581 5580 5582 5591 CONECT 5582 5581 5592 CONECT 5583 5584 5587 CONECT 5584 5583 5585 CONECT 5585 5584 5586 CONECT 5586 5585 CONECT 5587 5577 5583 CONECT 5588 5578 CONECT 5589 5579 CONECT 5590 5580 CONECT 5591 5577 5581 CONECT 5592 5582 CONECT 5593 5594 5607 5611 CONECT 5594 5593 5595 5608 CONECT 5595 5594 5596 5609 CONECT 5596 5595 5597 5610 CONECT 5597 5596 5598 5611 CONECT 5598 5597 5612 CONECT 5599 5600 5607 CONECT 5600 5599 5601 CONECT 5601 5600 5602 CONECT 5602 5601 5603 CONECT 5603 5602 5604 CONECT 5604 5603 5605 CONECT 5605 5604 5606 CONECT 5606 5605 CONECT 5607 5593 5599 CONECT 5608 5594 CONECT 5609 5595 CONECT 5610 5596 CONECT 5611 5593 5597 CONECT 5612 5598 CONECT 5613 5614 CONECT 5614 5613 5615 CONECT 5615 5614 5616 CONECT 5616 5615 5617 CONECT 5617 5616 5618 CONECT 5618 5617 CONECT 5619 5628 CONECT 5620 5621 5628 CONECT 5621 5620 5622 CONECT 5622 5621 5623 CONECT 5623 5622 5624 CONECT 5624 5623 5625 CONECT 5625 5624 5626 CONECT 5626 5625 5627 CONECT 5627 5626 CONECT 5628 5619 5620 CONECT 5629 5630 5637 CONECT 5630 5629 5631 CONECT 5631 5630 5632 CONECT 5632 5631 5633 CONECT 5633 5632 5634 CONECT 5634 5633 5635 CONECT 5635 5634 5636 CONECT 5636 5635 CONECT 5637 5629 CONECT 5638 5639 5645 CONECT 5639 5638 5640 CONECT 5640 5639 5641 CONECT 5641 5640 5642 CONECT 5642 5641 5643 CONECT 5643 5642 5644 CONECT 5644 5643 CONECT 5645 5638 CONECT 5646 5647 5654 CONECT 5647 5646 5648 CONECT 5648 5647 5649 CONECT 5649 5648 5650 CONECT 5650 5649 5651 CONECT 5651 5650 5652 CONECT 5652 5651 5653 CONECT 5653 5652 CONECT 5654 5646 CONECT 5655 5656 5659 CONECT 5656 5655 5657 CONECT 5657 5656 5658 CONECT 5658 5657 CONECT 5659 5655 CONECT 5660 5661 5670 5674 CONECT 5661 5660 5662 5671 CONECT 5662 5661 5663 5672 CONECT 5663 5662 5664 5673 CONECT 5664 5663 5665 5674 CONECT 5665 5664 5675 CONECT 5666 5667 5670 CONECT 5667 5666 5668 CONECT 5668 5667 5669 CONECT 5669 5668 CONECT 5670 5660 5666 CONECT 5671 5661 CONECT 5672 5662 CONECT 5673 5663 CONECT 5674 5660 5664 CONECT 5675 5665 CONECT 5676 5677 5683 CONECT 5677 5676 5678 CONECT 5678 5677 5679 CONECT 5679 5678 5680 CONECT 5680 5679 5681 CONECT 5681 5680 5682 CONECT 5682 5681 CONECT 5683 5676 CONECT 5684 5685 5692 CONECT 5685 5684 5686 CONECT 5686 5685 5687 CONECT 5687 5686 5688 CONECT 5688 5687 5689 CONECT 5689 5688 5690 CONECT 5690 5689 5691 CONECT 5691 5690 CONECT 5692 5684 CONECT 5693 5694 5698 CONECT 5694 5693 5695 CONECT 5695 5694 5696 CONECT 5696 5695 5697 CONECT 5697 5696 CONECT 5698 5693 CONECT 5699 5700 5705 CONECT 5700 5699 5701 CONECT 5701 5700 5702 CONECT 5702 5701 5703 CONECT 5703 5702 5704 CONECT 5704 5703 CONECT 5705 5699 CONECT 5706 5707 5712 CONECT 5707 5706 5708 CONECT 5708 5707 5709 CONECT 5709 5708 5710 CONECT 5710 5709 5711 CONECT 5711 5710 CONECT 5712 5706 CONECT 5713 5714 5719 CONECT 5714 5713 5715 CONECT 5715 5714 5716 CONECT 5716 5715 5717 CONECT 5717 5716 5718 CONECT 5718 5717 CONECT 5719 5713 CONECT 5720 5721 5726 CONECT 5721 5720 5722 CONECT 5722 5721 5723 CONECT 5723 5722 5724 CONECT 5724 5723 5725 CONECT 5725 5724 CONECT 5726 5720 CONECT 5727 5728 5733 CONECT 5728 5727 5729 CONECT 5729 5728 5730 CONECT 5730 5729 5731 CONECT 5731 5730 5732 CONECT 5732 5731 CONECT 5733 5727 CONECT 5734 5735 5740 CONECT 5735 5734 5736 CONECT 5736 5735 5737 CONECT 5737 5736 5738 CONECT 5738 5737 5739 CONECT 5739 5738 CONECT 5740 5734 CONECT 5741 5742 5757 CONECT 5742 5741 CONECT 5743 5757 CONECT 5744 5769 5771 5773 5775 CONECT 5745 5748 5753 CONECT 5746 5747 5749 5750 CONECT 5747 5746 5748 CONECT 5748 5745 5747 5751 CONECT 5749 5746 5752 CONECT 5750 5746 CONECT 5751 5748 5769 CONECT 5752 5749 5755 CONECT 5753 5745 5780 CONECT 5754 5757 5771 CONECT 5755 5752 5758 CONECT 5756 5780 CONECT 5757 5741 5743 5754 CONECT 5758 5755 5760 CONECT 5759 5761 5767 CONECT 5760 5758 5762 CONECT 5761 5759 5763 CONECT 5762 5760 5764 CONECT 5763 5761 5765 CONECT 5764 5762 5766 CONECT 5765 5763 5768 CONECT 5766 5764 5767 CONECT 5767 5759 5766 CONECT 5768 5765 5770 CONECT 5769 5744 5751 CONECT 5770 5768 5772 CONECT 5771 5744 5754 CONECT 5772 5770 5774 CONECT 5773 5744 CONECT 5774 5772 CONECT 5775 5744 CONECT 5776 5777 5788 CONECT 5777 5776 5778 CONECT 5778 5777 5779 CONECT 5779 5778 5789 CONECT 5780 5753 5756 5781 CONECT 5781 5780 5782 CONECT 5782 5781 5783 CONECT 5783 5782 5784 CONECT 5784 5783 5785 CONECT 5785 5784 5786 CONECT 5786 5785 5787 CONECT 5787 5786 5788 CONECT 5788 5776 5787 CONECT 5789 5779 5791 CONECT 5790 5791 CONECT 5791 5789 5790 CONECT 5792 2929 4295 4614 MASTER 402 0 62 29 4 0 0 6 5949 2 924 52 END