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*** 3NT1_ENZIMA_NEMO ***elNémo ID: 22030921275826620Job options:ID = 22030921275826620 JOBID = 3NT1_ENZIMA_NEMO USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER 3NT1_ENZIMA_NEMO HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 02-JUL-10 3NT1 TITLE HIGH RESOLUTION STRUCTURE OF NAPROXEN:COX-2 COMPLEX. CAVEAT 3NT1 NAG A 661 HAS WRONG CHIRALITY AT ATOM C1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE 2; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: UNP RESIDUES 18-604, CATALYTIC DOMAIN; COMPND 5 EC: 1.14.99.1; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: COX-2 PGHS-B, MCG_5001, PTGS2; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS PROSTAGLANDIN H2 SYNTHASE, CYCLOOXYGENASE-2, NAPROXEN, KEYWDS 2 OXIDOREDUCTASE, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR K.C.DUGGAN,J.MUSEE,M.J.WALTERS,J.M.HARP,J.R.KIEFER,J.A.OATES, AUTHOR 2 L.J.MARNETT REVDAT 4 29-JUL-20 3NT1 1 CAVEAT COMPND REMARK HETNAM REVDAT 4 2 1 LINK SITE ATOM REVDAT 3 08-NOV-17 3NT1 1 REMARK REVDAT 2 17-NOV-10 3NT1 1 JRNL REVDAT 1 01-SEP-10 3NT1 0 JRNL AUTH K.C.DUGGAN,M.J.WALTERS,J.MUSEE,J.M.HARP,J.R.KIEFER, JRNL AUTH 2 J.A.OATES,L.J.MARNETT JRNL TITL MOLECULAR BASIS FOR CYCLOOXYGENASE INHIBITION BY THE JRNL TITL 2 NON-STEROIDAL ANTI-INFLAMMATORY DRUG NAPROXEN. JRNL REF J.BIOL.CHEM. V. 285 34950 2010 JRNL REFN ISSN 0021-9258 JRNL PMID 20810665 JRNL DOI 10.1074/JBC.M110.162982 REMARK 2 REMARK 2 RESOLUTION. 1.73 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0109 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.73 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2 REMARK 3 NUMBER OF REFLECTIONS : 142975 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) : 0.168 REMARK 3 R VALUE (WORKING SET) : 0.167 REMARK 3 FREE R VALUE : 0.186 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 7592 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.73 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.78 REMARK 3 REFLECTION IN BIN (WORKING SET) : 9768 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.72 REMARK 3 BIN R VALUE (WORKING SET) : 0.2340 REMARK 3 BIN FREE R VALUE SET COUNT : 524 REMARK 3 BIN FREE R VALUE : 0.2500 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 8948 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 314 REMARK 3 SOLVENT ATOMS : 1051 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.68 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.81000 REMARK 3 B22 (A**2) : 0.37000 REMARK 3 B33 (A**2) : -2.18000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.094 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.089 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.062 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.186 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.960 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9578 ; 0.007 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 6590 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13028 ; 1.076 ; 2.012 REMARK 3 BOND ANGLES OTHERS (DEGREES): 15828 ; 0.852 ; 3.004 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1108 ; 5.304 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 451 ;35.959 ;24.102 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1558 ;12.240 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 47 ;12.029 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1381 ; 0.065 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10404 ; 0.004 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): 1927 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5533 ; 0.340 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2213 ; 0.072 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8996 ; 0.692 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4045 ; 1.280 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4031 ; 2.178 ; 4.500 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 33 A 583 REMARK 3 ORIGIN FOR THE GROUP (A): -33.9786 -45.1901 -24.6335 REMARK 3 T TENSOR REMARK 3 T11: 0.0212 T22: 0.0346 REMARK 3 T33: 0.0335 T12: -0.0058 REMARK 3 T13: 0.0104 T23: 0.0145 REMARK 3 L TENSOR REMARK 3 L11: 0.9986 L22: 0.7678 REMARK 3 L33: 0.8118 L12: -0.4797 REMARK 3 L13: -0.1164 L23: -0.0353 REMARK 3 S TENSOR REMARK 3 S11: -0.0229 S12: -0.1532 S13: -0.0451 REMARK 3 S21: 0.0844 S22: 0.0468 S23: 0.0590 REMARK 3 S31: 0.0156 S32: -0.0406 S33: -0.0239 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 33 B 583 REMARK 3 ORIGIN FOR THE GROUP (A): -40.0680 -36.9591 -63.0668 REMARK 3 T TENSOR REMARK 3 T11: 0.0219 T22: 0.0348 REMARK 3 T33: 0.0327 T12: 0.0013 REMARK 3 T13: -0.0102 T23: 0.0057 REMARK 3 L TENSOR REMARK 3 L11: 0.7071 L22: 0.9607 REMARK 3 L33: 1.0265 L12: -0.4183 REMARK 3 L13: -0.0762 L23: 0.0170 REMARK 3 S TENSOR REMARK 3 S11: 0.0487 S12: 0.1342 S13: -0.0298 REMARK 3 S21: -0.1068 S22: -0.0191 S23: 0.0347 REMARK 3 S31: 0.0966 S32: -0.0166 S33: -0.0296 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3NT1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUL-10. REMARK 100 THE DEPOSITION ID IS D_1000060243. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-MAR-10 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 21-ID-F REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97856 REMARK 200 MONOCHROMATOR : CRYSTAL REMARK 200 OPTICS : CRYSTAL MONOCHROMATOR REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MAR CCD 300 MM REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 150576 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.730 REMARK 200 RESOLUTION RANGE LOW (A) : 35.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6 REMARK 200 DATA REDUNDANCY : 4.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.06700 REMARK 200 FOR THE DATA SET : 23.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.73 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.40900 REMARK 200 FOR SHELL : 2.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 55.13 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: MMP550, MGCL2, PH 8, VAPOR DIFFUSION, REMARK 280 HANGING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2 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,Y,-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 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 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 61.14750 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 66.61650 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 90.63450 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 61.14750 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 66.61650 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 90.63450 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 61.14750 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 66.61650 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 90.63450 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 61.14750 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 66.61650 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 90.63450 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 12820 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 41650 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 ASP A 584 REMARK 465 PRO A 585 REMARK 465 GLN A 586 REMARK 465 PRO A 587 REMARK 465 THR A 588 REMARK 465 LYS A 589 REMARK 465 THR A 590 REMARK 465 ALA A 591 REMARK 465 THR A 592 REMARK 465 ILE A 593 REMARK 465 ASN A 594 REMARK 465 ALA A 595 REMARK 465 SER A 596 REMARK 465 ALA A 597 REMARK 465 SER A 598 REMARK 465 HIS A 599 REMARK 465 SER A 600 REMARK 465 ARG A 601 REMARK 465 LEU A 602 REMARK 465 ASP A 603 REMARK 465 ASP A 604 REMARK 465 ILE A 605 REMARK 465 ASN A 606 REMARK 465 PRO A 607 REMARK 465 THR A 608 REMARK 465 VAL A 609 REMARK 465 LEU A 610 REMARK 465 ILE A 611 REMARK 465 LYS A 612 REMARK 465 ARG A 613 REMARK 465 ARG A 614 REMARK 465 SER A 615 REMARK 465 THR A 616 REMARK 465 GLU A 617 REMARK 465 LEU A 618 REMARK 465 ASP B 584 REMARK 465 PRO B 585 REMARK 465 GLN B 586 REMARK 465 PRO B 587 REMARK 465 THR B 588 REMARK 465 LYS B 589 REMARK 465 THR B 590 REMARK 465 ALA B 591 REMARK 465 THR B 592 REMARK 465 ILE B 593 REMARK 465 ASN B 594 REMARK 465 ALA B 595 REMARK 465 SER B 596 REMARK 465 ALA B 597 REMARK 465 SER B 598 REMARK 465 HIS B 599 REMARK 465 SER B 600 REMARK 465 ARG B 601 REMARK 465 LEU B 602 REMARK 465 ASP B 603 REMARK 465 ASP B 604 REMARK 465 ILE B 605 REMARK 465 ASN B 606 REMARK 465 PRO B 607 REMARK 465 THR B 608 REMARK 465 VAL B 609 REMARK 465 LEU B 610 REMARK 465 ILE B 611 REMARK 465 LYS B 612 REMARK 465 ARG B 613 REMARK 465 ARG B 614 REMARK 465 SER B 615 REMARK 465 THR B 616 REMARK 465 GLU B 617 REMARK 465 LEU B 618 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 THR A 129 -89.79 -120.78 REMARK 500 ARG A 185 -81.46 -89.43 REMARK 500 ASP A 362 89.70 -152.89 REMARK 500 TRP A 387 50.85 -91.90 REMARK 500 GLU A 398 -118.92 55.65 REMARK 500 ASN A 439 17.18 -140.32 REMARK 500 SER A 496 -51.67 72.10 REMARK 500 THR B 129 -91.23 -123.31 REMARK 500 ARG B 185 -87.19 -89.49 REMARK 500 GLU B 398 -121.29 57.97 REMARK 500 ASN B 439 17.83 -140.82 REMARK 500 SER B 496 -60.99 72.06 REMARK 500 REMARK 500 REMARK: NULL 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 HEM A 619 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 388 NE2 REMARK 620 2 HEM A 619 NA 94.5 REMARK 620 3 HEM A 619 NB 91.7 88.0 REMARK 620 4 HEM A 619 NC 87.8 177.7 91.4 REMARK 620 5 HEM A 619 ND 89.0 90.5 178.4 90.0 REMARK 620 6 HOH A 943 O 173.4 78.9 88.4 98.8 90.8 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM B 619 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS B 388 NE2 REMARK 620 2 HEM B 619 NA 92.8 REMARK 620 3 HEM B 619 NB 92.4 88.7 REMARK 620 4 HEM B 619 NC 89.1 178.1 90.8 REMARK 620 5 HEM B 619 ND 86.9 90.5 178.9 90.0 REMARK 620 6 HOH B1002 O 173.6 80.8 87.9 97.3 92.7 REMARK 620 N 1 2 3 4 5 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3PGH RELATED DB: PDB REMARK 900 COX-2:FLURBIPROFEN REMARK 900 RELATED ID: 1PXX RELATED DB: PDB REMARK 900 COX-2:DICLOFENAC REMARK 900 RELATED ID: 1CQE RELATED DB: PDB REMARK 900 COX-1:FLURBIPROFEN REMARK 900 RELATED ID: 3NTB RELATED DB: PDB DBREF 3NT1 A 33 618 UNP Q543K3 Q543K3_MOUSE 18 604 DBREF 3NT1 B 33 618 UNP Q543K3 Q543K3_MOUSE 18 604 SEQRES 1 A 587 ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY SEQRES 2 A 587 GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP SEQRES 3 A 587 CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR SEQRES 4 A 587 PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO SEQRES 5 A 587 THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS SEQRES 6 A 587 GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG SEQRES 7 A 587 SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR SEQRES 8 A 587 LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY SEQRES 9 A 587 TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR SEQRES 10 A 587 THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR SEQRES 11 A 587 PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER SEQRES 12 A 587 LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE SEQRES 13 A 587 ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE SEQRES 14 A 587 PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP SEQRES 15 A 587 HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS SEQRES 16 A 587 GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP SEQRES 17 A 587 ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU SEQRES 18 A 587 LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR SEQRES 19 A 587 VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS SEQRES 20 A 587 ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL SEQRES 21 A 587 PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE SEQRES 22 A 587 TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS SEQRES 23 A 587 GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN SEQRES 24 A 587 THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE SEQRES 25 A 587 VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS SEQRES 26 A 587 PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN SEQRES 27 A 587 GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN SEQRES 28 A 587 THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE SEQRES 29 A 587 ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU SEQRES 30 A 587 TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN SEQRES 31 A 587 PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL SEQRES 32 A 587 ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL SEQRES 33 A 587 ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR SEQRES 34 A 587 GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS SEQRES 35 A 587 PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU SEQRES 36 A 587 MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP SEQRES 37 A 587 VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO SEQRES 38 A 587 ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU SEQRES 39 A 587 GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO SEQRES 40 A 587 ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY SEQRES 41 A 587 GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE SEQRES 42 A 587 GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE SEQRES 43 A 587 THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR SEQRES 44 A 587 ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP SEQRES 45 A 587 ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR SEQRES 46 A 587 GLU LEU SEQRES 1 B 587 ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY SEQRES 2 B 587 GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP SEQRES 3 B 587 CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR SEQRES 4 B 587 PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO SEQRES 5 B 587 THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS SEQRES 6 B 587 GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG SEQRES 7 B 587 SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR SEQRES 8 B 587 LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY SEQRES 9 B 587 TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR SEQRES 10 B 587 THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR SEQRES 11 B 587 PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER SEQRES 12 B 587 LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE SEQRES 13 B 587 ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE SEQRES 14 B 587 PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP SEQRES 15 B 587 HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS SEQRES 16 B 587 GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP SEQRES 17 B 587 ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU SEQRES 18 B 587 LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR SEQRES 19 B 587 VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS SEQRES 20 B 587 ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL SEQRES 21 B 587 PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE SEQRES 22 B 587 TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS SEQRES 23 B 587 GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN SEQRES 24 B 587 THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE SEQRES 25 B 587 VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS SEQRES 26 B 587 PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN SEQRES 27 B 587 GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN SEQRES 28 B 587 THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE SEQRES 29 B 587 ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU SEQRES 30 B 587 TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN SEQRES 31 B 587 PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL SEQRES 32 B 587 ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL SEQRES 33 B 587 ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR SEQRES 34 B 587 GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS SEQRES 35 B 587 PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU SEQRES 36 B 587 MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP SEQRES 37 B 587 VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO SEQRES 38 B 587 ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU SEQRES 39 B 587 GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO SEQRES 40 B 587 ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY SEQRES 41 B 587 GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE SEQRES 42 B 587 GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE SEQRES 43 B 587 THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR SEQRES 44 B 587 ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP SEQRES 45 B 587 ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR SEQRES 46 B 587 GLU LEU MODRES 3NT1 ASN B 410 ASN GLYCOSYLATION SITE MODRES 3NT1 ASN A 144 ASN GLYCOSYLATION SITE MODRES 3NT1 ASN B 144 ASN GLYCOSYLATION SITE MODRES 3NT1 ASN A 68 ASN GLYCOSYLATION SITE MODRES 3NT1 ASN B 68 ASN GLYCOSYLATION SITE MODRES 3NT1 ASN A 410 ASN GLYCOSYLATION SITE HET NAG C 1 14 HET NAG C 2 14 HET NAG D 1 14 HET NAG D 2 14 HET NAG A 661 14 HET NAG A 681 14 HET BOG A 3 20 HET NPS A 5 17 HET HEM A 619 43 HET BOG A 6 20 HET BOG A 620 20 HET CL A 1 1 HET NAG B 681 14 HET NPS B 4 17 HET BOG B 3 20 HET HEM B 619 43 HET NAG B 9 14 HET CL B 1 1 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BOG OCTYL BETA-D-GLUCOPYRANOSIDE HETNAM NPS (2S)-2-(6-METHOXYNAPHTHALEN-2-YL)PROPANOIC ACID HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETNAM CL CHLORIDE ION HETSYN NPS NAPROXEN HETSYN HEM HEME FORMUL 3 NAG 8(C8 H15 N O6) FORMUL 7 BOG 4(C14 H28 O6) FORMUL 8 NPS 2(C14 H14 O3) FORMUL 9 HEM 2(C34 H32 FE N4 O4) FORMUL 12 CL 2(CL 1-) FORMUL 19 HOH *1051(H2 O) HELIX 1 1 GLU A 73 LYS A 83 1 11 HELIX 2 2 THR A 85 THR A 94 1 10 HELIX 3 3 PHE A 96 TYR A 122 1 28 HELIX 4 4 SER A 138 ASN A 144 1 7 HELIX 5 5 ASP A 173 LEU A 182 1 10 HELIX 6 6 ASN A 195 HIS A 207 1 13 HELIX 7 7 LEU A 230 GLY A 235 1 6 HELIX 8 8 THR A 237 ARG A 245 1 9 HELIX 9 9 THR A 265 GLN A 270 1 6 HELIX 10 10 PRO A 280 GLN A 284 1 5 HELIX 11 11 VAL A 295 HIS A 320 1 26 HELIX 12 12 GLY A 324 GLY A 354 1 31 HELIX 13 13 ASP A 362 PHE A 367 1 6 HELIX 14 14 ALA A 378 LEU A 391 1 14 HELIX 15 15 SER A 403 LEU A 408 1 6 HELIX 16 16 ASN A 411 GLN A 429 1 19 HELIX 17 17 PRO A 441 MET A 458 1 18 HELIX 18 18 SER A 462 PHE A 470 1 9 HELIX 19 19 SER A 477 GLY A 483 1 7 HELIX 20 20 LYS A 485 GLU A 510 1 26 HELIX 21 21 GLY A 519 SER A 541 1 23 HELIX 22 22 LYS A 546 THR A 561 1 16 HELIX 23 23 SER A 563 VAL A 572 1 10 SHEET 1 1 1 GLU A 46 GLY A 51 0 SHEET 2 2 1 GLN A 54 ASP A 58 0 SHEET 3 3 1 PHE A 64 TYR A 65 0 SHEET 4 4 1 THR A 71 PRO A 72 0 SHEET 5 5 1 GLN A 255 ILE A 257 0 SHEET 6 6 1 GLU A 260 TYR A 262 0 SHEET 7 7 1 PHE A 395 ILE A 397 0 SHEET 8 8 1 GLN A 400 TYR A 402 0 SSBOND 1 CYS A 36 CYS A 47 1555 1555 2.05 SSBOND 2 CYS A 37 CYS A 159 1555 1555 2.02 SSBOND 3 CYS A 41 CYS A 57 1555 1555 2.02 SSBOND 4 CYS A 59 CYS A 69 1555 1555 2.03 SSBOND 5 CYS A 569 CYS A 575 1555 1555 2.03 SSBOND 6 CYS B 36 CYS B 47 1555 1555 2.05 SSBOND 7 CYS B 37 CYS B 159 1555 1555 2.03 SSBOND 8 CYS B 41 CYS B 57 1555 1555 2.03 SSBOND 9 CYS B 59 CYS B 69 1555 1555 2.04 SSBOND 10 CYS B 569 CYS B 575 1555 1555 2.03 LINK ND2 ASN A 68 C1 NAG A 661 1555 1555 1.45 LINK ND2 ASN A 144 C1 NAG C 1 1555 1555 1.45 LINK ND2 ASN A 410 C1 NAG A 681 1555 1555 1.45 LINK C1 NAG B 9 ND2 ASN B 68 1555 1555 1.45 LINK ND2 ASN B 144 C1 NAG D 1 1555 1555 1.45 LINK ND2 ASN B 410 C1 NAG B 681 1555 1555 1.44 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44 LINK NE2 HIS A 388 FE HEM A 619 1555 1555 2.76 LINK FE HEM A 619 O HOH A 943 1555 1555 2.47 LINK NE2 HIS B 388 FE HEM B 619 1555 1555 2.77 LINK FE HEM B 619 O HOH B1002 1555 1555 2.49 CISPEP 1 SER A 126 PRO A 127 0 0.75 CISPEP 2 SER B 126 PRO B 127 0 1.42 CRYST1 122.295 133.233 181.269 90.00 90.00 90.00 I 2 2 2 16 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.008177 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007506 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005517 0.00000 ATOM 1 N ALA A 33 -54.058 -16.845 -23.914 1.00 39.61 N ANISOU 1 N ALA A 33 5169 4755 5124 1499 762 -155 N ATOM 2 CA ALA A 33 -54.196 -16.053 -25.171 1.00 39.89 C ANISOU 2 CA ALA A 33 5231 4720 5206 1548 763 -104 C ATOM 3 C ALA A 33 -54.684 -16.948 -26.308 1.00 38.92 C ANISOU 3 C ALA A 33 5021 4687 5080 1529 730 -21 C ATOM 4 O ALA A 33 -55.818 -16.811 -26.772 1.00 39.65 O ANISOU 4 O ALA A 33 5058 4841 5166 1613 740 26 O ATOM 5 CB ALA A 33 -52.874 -15.401 -25.528 1.00 40.03 C ANISOU 5 CB ALA A 33 5344 4593 5274 1491 753 -131 C ATOM 6 N ASN A 34 -53.826 -17.861 -26.754 1.00 37.65 N ANISOU 6 N ASN A 34 4847 4533 4923 1420 689 -8 N ATOM 7 CA ASN A 34 -54.220 -18.877 -27.724 1.00 36.60 C ANISOU 7 CA ASN A 34 4632 4491 4783 1389 650 56 C ATOM 8 C ASN A 34 -55.411 -19.672 -27.163 1.00 36.26 C ANISOU 8 C ASN A 34 4486 4585 4708 1413 655 68 C ATOM 9 O ASN A 34 -55.340 -20.171 -26.041 1.00 35.96 O ANISOU 9 O ASN A 34 4434 4584 4645 1378 669 30 O ATOM 10 CB ASN A 34 -53.033 -19.804 -28.025 1.00 35.64 C ANISOU 10 CB ASN A 34 4519 4357 4667 1265 609 53 C ATOM 11 CG ASN A 34 -53.248 -20.660 -29.259 1.00 35.84 C ANISOU 11 CG ASN A 34 4483 4445 4690 1238 566 113 C ATOM 12 OD1 ASN A 34 -54.300 -21.277 -29.430 1.00 36.38 O ANISOU 12 OD1 ASN A 34 4464 4618 4742 1263 553 142 O ATOM 13 ND2 ASN A 34 -52.233 -20.719 -30.120 1.00 35.80 N ANISOU 13 ND2 ASN A 34 4521 4379 4703 1184 543 129 N ATOM 14 N PRO A 35 -56.525 -19.763 -27.919 1.00 35.87 N ANISOU 14 N PRO A 35 4362 4611 4658 1476 646 121 N ATOM 15 CA PRO A 35 -57.682 -20.517 -27.414 1.00 35.62 C ANISOU 15 CA PRO A 35 4220 4708 4607 1493 654 136 C ATOM 16 C PRO A 35 -57.439 -22.022 -27.223 1.00 34.16 C ANISOU 16 C PRO A 35 3970 4595 4416 1379 621 140 C ATOM 17 O PRO A 35 -58.258 -22.696 -26.598 1.00 34.64 O ANISOU 17 O PRO A 35 3945 4751 4465 1378 636 149 O ATOM 18 CB PRO A 35 -58.755 -20.279 -28.484 1.00 36.38 C ANISOU 18 CB PRO A 35 4250 4860 4711 1576 637 192 C ATOM 19 CG PRO A 35 -58.016 -19.867 -29.695 1.00 36.21 C ANISOU 19 CG PRO A 35 4294 4760 4705 1569 606 215 C ATOM 20 CD PRO A 35 -56.812 -19.132 -29.219 1.00 36.23 C ANISOU 20 CD PRO A 35 4416 4631 4720 1542 632 171 C ATOM 21 N CYS A 36 -56.333 -22.538 -27.749 1.00 32.40 N ANISOU 21 N CYS A 36 3786 4324 4201 1288 582 137 N ATOM 22 CA CYS A 36 -55.977 -23.943 -27.567 1.00 31.08 C ANISOU 22 CA CYS A 36 3571 4208 4031 1181 552 138 C ATOM 23 C CYS A 36 -55.117 -24.186 -26.313 1.00 30.08 C ANISOU 23 C CYS A 36 3494 4050 3885 1124 574 92 C ATOM 24 O CYS A 36 -54.722 -25.316 -26.044 1.00 28.68 O ANISOU 24 O CYS A 36 3288 3906 3703 1038 555 93 O ATOM 25 CB CYS A 36 -55.282 -24.473 -28.830 1.00 30.59 C ANISOU 25 CB CYS A 36 3518 4121 3983 1118 496 160 C ATOM 26 SG CYS A 36 -56.411 -24.641 -30.249 1.00 31.09 S ANISOU 26 SG CYS A 36 3496 4262 4056 1172 453 213 S ATOM 27 N CYS A 37 -54.861 -23.136 -25.531 1.00 30.15 N ANISOU 27 N CYS A 37 3576 3998 3882 1176 613 49 N ATOM 28 CA CYS A 37 -53.989 -23.240 -24.353 1.00 29.82 C ANISOU 28 CA CYS A 37 3589 3926 3815 1131 628 -5 C ATOM 29 C CYS A 37 -54.453 -24.246 -23.298 1.00 29.44 C ANISOU 29 C CYS A 37 3478 3976 3734 1107 648 0 C ATOM 30 O CYS A 37 -53.624 -24.828 -22.607 1.00 29.17 O ANISOU 30 O CYS A 37 3469 3936 3678 1042 641 -25 O ATOM 31 CB CYS A 37 -53.803 -21.874 -23.684 1.00 30.49 C ANISOU 31 CB CYS A 37 3759 3934 3893 1203 664 -60 C ATOM 32 SG CYS A 37 -52.685 -20.782 -24.563 1.00 31.64 S ANISOU 32 SG CYS A 37 4007 3931 4084 1194 645 -80 S ATOM 33 N SER A 38 -55.763 -24.455 -23.180 1.00 29.67 N ANISOU 33 N SER A 38 3420 4094 3759 1160 675 37 N ATOM 34 CA SER A 38 -56.306 -25.389 -22.183 1.00 29.65 C ANISOU 34 CA SER A 38 3350 4185 3729 1142 705 53 C ATOM 35 C SER A 38 -56.203 -26.867 -22.592 1.00 28.95 C ANISOU 35 C SER A 38 3192 4144 3663 1041 670 95 C ATOM 36 O SER A 38 -56.604 -27.745 -21.823 1.00 29.20 O ANISOU 36 O SER A 38 3166 4247 3681 1015 697 119 O ATOM 37 CB SER A 38 -57.767 -25.052 -21.892 1.00 30.64 C ANISOU 37 CB SER A 38 3400 4390 3850 1236 753 80 C ATOM 38 OG SER A 38 -58.570 -25.295 -23.029 1.00 30.83 O ANISOU 38 OG SER A 38 3343 4456 3917 1242 725 128 O ATOM 39 N ASN A 39 -55.677 -27.138 -23.789 1.00 27.68 N ANISOU 39 N ASN A 39 3039 3942 3535 987 614 107 N ATOM 40 CA ASN A 39 -55.605 -28.500 -24.338 1.00 26.81 C ANISOU 40 CA ASN A 39 2868 3869 3452 897 574 141 C ATOM 41 C ASN A 39 -56.992 -29.158 -24.387 1.00 26.95 C ANISOU 41 C ASN A 39 2762 3985 3492 908 587 186 C ATOM 42 O ASN A 39 -57.170 -30.274 -23.886 1.00 26.30 O ANISOU 42 O ASN A 39 2623 3950 3418 848 596 210 O ATOM 43 CB ASN A 39 -54.624 -29.355 -23.522 1.00 26.46 C ANISOU 43 CB ASN A 39 2856 3810 3386 818 574 127 C ATOM 44 CG ASN A 39 -53.289 -28.658 -23.286 1.00 26.90 C ANISOU 44 CG ASN A 39 3024 3778 3420 810 565 75 C ATOM 45 OD1 ASN A 39 -52.611 -28.256 -24.229 1.00 27.73 O ANISOU 45 OD1 ASN A 39 3174 3817 3546 795 529 65 O ATOM 46 ND2 ASN A 39 -52.906 -28.521 -22.024 1.00 28.47 N ANISOU 46 ND2 ASN A 39 3264 3979 3577 820 597 44 N ATOM 47 N PRO A 40 -57.983 -28.466 -24.992 1.00 26.88 N ANISOU 47 N PRO A 40 2708 4006 3499 985 588 201 N ATOM 48 CA PRO A 40 -59.369 -28.932 -24.915 1.00 27.42 C ANISOU 48 CA PRO A 40 2653 4175 3592 1006 606 241 C ATOM 49 C PRO A 40 -59.670 -30.212 -25.691 1.00 27.19 C ANISOU 49 C PRO A 40 2533 4188 3609 921 555 269 C ATOM 50 O PRO A 40 -60.591 -30.940 -25.311 1.00 27.51 O ANISOU 50 O PRO A 40 2469 4305 3677 902 576 301 O ATOM 51 CB PRO A 40 -60.169 -27.761 -25.498 1.00 28.06 C ANISOU 51 CB PRO A 40 2721 4265 3674 1116 610 244 C ATOM 52 CG PRO A 40 -59.229 -27.083 -26.421 1.00 27.65 C ANISOU 52 CG PRO A 40 2767 4121 3617 1122 568 222 C ATOM 53 CD PRO A 40 -57.866 -27.237 -25.803 1.00 27.16 C ANISOU 53 CD PRO A 40 2803 3985 3534 1057 573 187 C ATOM 54 N CYS A 41 -58.920 -30.489 -26.762 1.00 26.12 N ANISOU 54 N CYS A 41 2435 4003 3486 871 490 257 N ATOM 55 CA CYS A 41 -59.233 -31.625 -27.626 1.00 26.14 C ANISOU 55 CA CYS A 41 2357 4042 3532 799 432 273 C ATOM 56 C CYS A 41 -58.688 -32.905 -27.009 1.00 25.39 C ANISOU 56 C CYS A 41 2256 3939 3451 696 437 279 C ATOM 57 O CYS A 41 -57.501 -32.992 -26.668 1.00 24.88 O ANISOU 57 O CYS A 41 2283 3810 3361 659 440 260 O ATOM 58 CB CYS A 41 -58.677 -31.432 -29.043 1.00 25.80 C ANISOU 58 CB CYS A 41 2359 3957 3488 797 362 259 C ATOM 59 SG CYS A 41 -59.145 -29.857 -29.812 1.00 27.23 S ANISOU 59 SG CYS A 41 2569 4132 3646 927 360 261 S ATOM 60 N GLN A 42 -59.564 -33.895 -26.859 1.00 25.71 N ANISOU 60 N GLN A 42 2186 4043 3538 650 440 307 N ATOM 61 CA GLN A 42 -59.200 -35.163 -26.229 1.00 25.46 C ANISOU 61 CA GLN A 42 2140 4006 3529 555 453 323 C ATOM 62 C GLN A 42 -58.970 -36.254 -27.261 1.00 25.15 C ANISOU 62 C GLN A 42 2071 3949 3537 469 380 316 C ATOM 63 O GLN A 42 -59.240 -36.066 -28.451 1.00 25.37 O ANISOU 63 O GLN A 42 2077 3985 3578 485 318 298 O ATOM 64 CB GLN A 42 -60.305 -35.598 -25.257 1.00 26.30 C ANISOU 64 CB GLN A 42 2143 4187 3663 556 517 367 C ATOM 65 CG GLN A 42 -60.676 -34.546 -24.220 1.00 27.15 C ANISOU 65 CG GLN A 42 2270 4324 3721 652 594 373 C ATOM 66 CD GLN A 42 -59.481 -34.090 -23.398 1.00 26.43 C ANISOU 66 CD GLN A 42 2308 4173 3563 667 622 347 C ATOM 67 OE1 GLN A 42 -58.829 -34.892 -22.727 1.00 26.25 O ANISOU 67 OE1 GLN A 42 2313 4131 3530 607 639 358 O ATOM 68 NE2 GLN A 42 -59.183 -32.796 -23.457 1.00 26.75 N ANISOU 68 NE2 GLN A 42 2425 4179 3558 748 626 312 N ATOM 69 N ASN A 43 -58.449 -37.390 -26.795 1.00 24.98 N ANISOU 69 N ASN A 43 2054 3901 3535 383 387 327 N ATOM 70 CA ASN A 43 -58.344 -38.612 -27.599 1.00 25.21 C ANISOU 70 CA ASN A 43 2046 3913 3619 295 326 321 C ATOM 71 C ASN A 43 -57.571 -38.422 -28.904 1.00 24.93 C ANISOU 71 C ASN A 43 2076 3832 3566 295 249 279 C ATOM 72 O ASN A 43 -57.920 -38.980 -29.948 1.00 24.60 O ANISOU 72 O ASN A 43 1983 3802 3561 263 183 261 O ATOM 73 CB ASN A 43 -59.739 -39.185 -27.849 1.00 26.21 C ANISOU 73 CB ASN A 43 2031 4108 3818 271 315 341 C ATOM 74 CG ASN A 43 -60.434 -39.566 -26.558 1.00 27.25 C ANISOU 74 CG ASN A 43 2095 4282 3975 258 399 392 C ATOM 75 OD1 ASN A 43 -59.906 -40.360 -25.784 1.00 28.07 O ANISOU 75 OD1 ASN A 43 2226 4354 4085 202 435 417 O ATOM 76 ND2 ASN A 43 -61.597 -38.985 -26.305 1.00 26.81 N ANISOU 76 ND2 ASN A 43 1953 4301 3931 317 434 414 N ATOM 77 N ARG A 44 -56.520 -37.612 -28.808 1.00 24.63 N ANISOU 77 N ARG A 44 2148 3742 3468 333 259 262 N ATOM 78 CA ARG A 44 -55.613 -37.307 -29.914 1.00 24.63 C ANISOU 78 CA ARG A 44 2223 3693 3442 340 204 230 C ATOM 79 C ARG A 44 -56.215 -36.439 -31.031 1.00 24.76 C ANISOU 79 C ARG A 44 2221 3739 3448 411 164 220 C ATOM 80 O ARG A 44 -55.622 -36.307 -32.107 1.00 24.60 O ANISOU 80 O ARG A 44 2248 3690 3408 418 115 200 O ATOM 81 CB ARG A 44 -54.974 -38.590 -30.452 1.00 24.69 C ANISOU 81 CB ARG A 44 2238 3666 3476 253 155 217 C ATOM 82 CG ARG A 44 -54.392 -39.433 -29.319 1.00 26.13 C ANISOU 82 CG ARG A 44 2441 3821 3668 192 198 235 C ATOM 83 CD ARG A 44 -53.193 -40.219 -29.725 1.00 28.36 C ANISOU 83 CD ARG A 44 2787 4043 3948 136 163 217 C ATOM 84 NE ARG A 44 -52.214 -39.337 -30.346 1.00 29.96 N ANISOU 84 NE ARG A 44 3077 4206 4100 177 144 192 N ATOM 85 CZ ARG A 44 -51.349 -39.701 -31.283 1.00 31.06 C ANISOU 85 CZ ARG A 44 3263 4306 4232 154 96 169 C ATOM 86 NH1 ARG A 44 -51.300 -40.955 -31.730 1.00 32.63 N ANISOU 86 NH1 ARG A 44 3436 4495 4467 91 57 160 N ATOM 87 NH2 ARG A 44 -50.529 -38.792 -31.780 1.00 31.43 N ANISOU 87 NH2 ARG A 44 3384 4322 4238 195 91 155 N ATOM 88 N GLY A 45 -57.362 -35.824 -30.762 1.00 25.10 N ANISOU 88 N GLY A 45 2197 3842 3499 472 190 237 N ATOM 89 CA GLY A 45 -57.902 -34.792 -31.640 1.00 25.66 C ANISOU 89 CA GLY A 45 2261 3939 3550 560 166 233 C ATOM 90 C GLY A 45 -56.980 -33.584 -31.633 1.00 25.23 C ANISOU 90 C GLY A 45 2323 3820 3443 620 191 227 C ATOM 91 O GLY A 45 -56.268 -33.352 -30.655 1.00 24.64 O ANISOU 91 O GLY A 45 2311 3699 3350 608 241 224 O ATOM 92 N GLU A 46 -56.988 -32.819 -32.723 1.00 25.38 N ANISOU 92 N GLU A 46 2371 3834 3440 684 158 225 N ATOM 93 CA GLU A 46 -56.055 -31.700 -32.894 1.00 25.10 C ANISOU 93 CA GLU A 46 2446 3725 3366 733 179 222 C ATOM 94 C GLU A 46 -56.779 -30.363 -32.789 1.00 25.08 C ANISOU 94 C GLU A 46 2446 3735 3350 842 215 238 C ATOM 95 O GLU A 46 -57.842 -30.177 -33.385 1.00 25.69 O ANISOU 95 O GLU A 46 2453 3877 3433 899 190 252 O ATOM 96 CB GLU A 46 -55.328 -31.823 -34.236 1.00 25.06 C ANISOU 96 CB GLU A 46 2489 3690 3342 726 124 217 C ATOM 97 CG GLU A 46 -54.453 -33.061 -34.288 1.00 26.73 C ANISOU 97 CG GLU A 46 2714 3876 3564 625 96 198 C ATOM 98 CD GLU A 46 -53.733 -33.260 -35.596 1.00 28.57 C ANISOU 98 CD GLU A 46 2992 4087 3774 621 45 190 C ATOM 99 OE1 GLU A 46 -53.708 -32.322 -36.424 1.00 30.47 O ANISOU 99 OE1 GLU A 46 3271 4320 3986 696 39 205 O ATOM 100 OE2 GLU A 46 -53.170 -34.370 -35.778 1.00 30.25 O ANISOU 100 OE2 GLU A 46 3206 4289 3997 546 14 172 O ATOM 101 N CYS A 47 -56.195 -29.445 -32.021 1.00 24.72 N ANISOU 101 N CYS A 47 2481 3625 3288 872 270 231 N ATOM 102 CA CYS A 47 -56.798 -28.142 -31.755 1.00 25.40 C ANISOU 102 CA CYS A 47 2581 3706 3362 976 312 240 C ATOM 103 C CYS A 47 -56.257 -27.097 -32.719 1.00 25.28 C ANISOU 103 C CYS A 47 2649 3626 3330 1036 304 251 C ATOM 104 O CYS A 47 -55.049 -26.986 -32.914 1.00 24.41 O ANISOU 104 O CYS A 47 2622 3438 3214 996 303 240 O ATOM 105 CB CYS A 47 -56.499 -27.696 -30.323 1.00 25.71 C ANISOU 105 CB CYS A 47 2665 3709 3394 979 377 220 C ATOM 106 SG CYS A 47 -57.508 -26.309 -29.765 1.00 27.48 S ANISOU 106 SG CYS A 47 2886 3946 3609 1108 434 225 S ATOM 107 N MET A 48 -57.165 -26.338 -33.315 1.00 25.76 N ANISOU 107 N MET A 48 2682 3720 3385 1134 301 275 N ATOM 108 CA MET A 48 -56.809 -25.234 -34.191 1.00 26.18 C ANISOU 108 CA MET A 48 2812 3713 3423 1209 304 297 C ATOM 109 C MET A 48 -57.636 -24.024 -33.770 1.00 26.95 C ANISOU 109 C MET A 48 2912 3806 3520 1322 352 309 C ATOM 110 O MET A 48 -58.843 -24.144 -33.538 1.00 27.56 O ANISOU 110 O MET A 48 2898 3972 3602 1368 352 318 O ATOM 111 CB MET A 48 -57.119 -25.619 -35.636 1.00 26.33 C ANISOU 111 CB MET A 48 2793 3786 3425 1230 239 322 C ATOM 112 CG MET A 48 -56.799 -24.564 -36.687 1.00 27.02 C ANISOU 112 CG MET A 48 2955 3822 3489 1314 241 357 C ATOM 113 SD MET A 48 -57.463 -25.003 -38.310 1.00 26.91 S ANISOU 113 SD MET A 48 2881 3904 3441 1364 160 385 S ATOM 114 CE MET A 48 -59.215 -24.746 -38.065 1.00 27.75 C ANISOU 114 CE MET A 48 2871 4119 3555 1455 153 395 C ATOM 115 N SER A 49 -56.994 -22.864 -33.658 1.00 27.00 N ANISOU 115 N SER A 49 3021 3711 3527 1367 395 310 N ATOM 116 CA SER A 49 -57.728 -21.624 -33.407 1.00 28.11 C ANISOU 116 CA SER A 49 3178 3834 3670 1485 439 322 C ATOM 117 C SER A 49 -58.559 -21.282 -34.639 1.00 29.23 C ANISOU 117 C SER A 49 3280 4030 3796 1581 407 372 C ATOM 118 O SER A 49 -58.140 -21.545 -35.763 1.00 28.59 O ANISOU 118 O SER A 49 3215 3948 3701 1567 365 396 O ATOM 119 CB SER A 49 -56.774 -20.473 -33.068 1.00 28.05 C ANISOU 119 CB SER A 49 3294 3688 3675 1503 489 308 C ATOM 120 OG SER A 49 -55.900 -20.182 -34.146 1.00 27.72 O ANISOU 120 OG SER A 49 3320 3577 3634 1494 474 337 O ATOM 121 N THR A 50 -59.743 -20.717 -34.428 1.00 30.72 N ANISOU 121 N THR A 50 3416 4272 3984 1683 427 387 N ATOM 122 CA THR A 50 -60.613 -20.315 -35.529 1.00 32.21 C ANISOU 122 CA THR A 50 3563 4520 4155 1790 396 434 C ATOM 123 C THR A 50 -60.972 -18.836 -35.399 1.00 33.76 C ANISOU 123 C THR A 50 3819 4654 4354 1922 453 458 C ATOM 124 O THR A 50 -61.943 -18.358 -35.986 1.00 35.42 O ANISOU 124 O THR A 50 3984 4923 4551 2036 442 496 O ATOM 125 CB THR A 50 -61.887 -21.177 -35.556 1.00 32.87 C ANISOU 125 CB THR A 50 3498 4752 4239 1795 354 435 C ATOM 126 OG1 THR A 50 -62.543 -21.095 -34.287 1.00 33.29 O ANISOU 126 OG1 THR A 50 3504 4835 4311 1809 404 414 O ATOM 127 CG2 THR A 50 -61.530 -22.631 -35.839 1.00 31.60 C ANISOU 127 CG2 THR A 50 3283 4642 4081 1667 293 413 C ATOM 128 N GLY A 51 -60.150 -18.116 -34.645 1.00 34.07 N ANISOU 128 N GLY A 51 3962 4570 4412 1907 511 432 N ATOM 129 CA GLY A 51 -60.405 -16.729 -34.286 1.00 35.12 C ANISOU 129 CA GLY A 51 4162 4623 4558 2020 572 439 C ATOM 130 C GLY A 51 -59.591 -16.422 -33.048 1.00 35.15 C ANISOU 130 C GLY A 51 4245 4527 4585 1962 622 379 C ATOM 131 O GLY A 51 -58.881 -17.290 -32.536 1.00 34.08 O ANISOU 131 O GLY A 51 4105 4394 4451 1842 607 340 O ATOM 132 N PHE A 52 -59.696 -15.194 -32.551 1.00 36.32 N ANISOU 132 N PHE A 52 4464 4586 4750 2050 679 368 N ATOM 133 CA PHE A 52 -58.896 -14.778 -31.399 1.00 36.80 C ANISOU 133 CA PHE A 52 4608 4543 4832 2003 722 301 C ATOM 134 C PHE A 52 -59.241 -15.520 -30.103 1.00 37.01 C ANISOU 134 C PHE A 52 4572 4650 4839 1957 732 246 C ATOM 135 O PHE A 52 -58.360 -15.746 -29.274 1.00 36.76 O ANISOU 135 O PHE A 52 4589 4568 4812 1871 740 191 O ATOM 136 CB PHE A 52 -58.999 -13.264 -31.193 1.00 37.95 C ANISOU 136 CB PHE A 52 4846 4571 5003 2115 780 296 C ATOM 137 CG PHE A 52 -58.228 -12.474 -32.207 1.00 38.31 C ANISOU 137 CG PHE A 52 4985 4490 5079 2129 786 340 C ATOM 138 CD1 PHE A 52 -58.865 -11.910 -33.300 1.00 40.02 C ANISOU 138 CD1 PHE A 52 5198 4718 5291 2242 786 416 C ATOM 139 CD2 PHE A 52 -56.853 -12.325 -32.086 1.00 38.76 C ANISOU 139 CD2 PHE A 52 5131 4425 5171 2031 793 309 C ATOM 140 CE1 PHE A 52 -58.147 -11.186 -34.246 1.00 40.26 C ANISOU 140 CE1 PHE A 52 5317 4633 5348 2258 800 467 C ATOM 141 CE2 PHE A 52 -56.129 -11.607 -33.028 1.00 38.80 C ANISOU 141 CE2 PHE A 52 5218 4314 5210 2040 807 357 C ATOM 142 CZ PHE A 52 -56.777 -11.038 -34.107 1.00 39.71 C ANISOU 142 CZ PHE A 52 5334 4436 5317 2155 813 439 C ATOM 143 N ASP A 53 -60.504 -15.915 -29.943 1.00 37.74 N ANISOU 143 N ASP A 53 4556 4871 4911 2014 730 266 N ATOM 144 CA ASP A 53 -60.965 -16.560 -28.705 1.00 38.18 C ANISOU 144 CA ASP A 53 4547 5010 4949 1986 752 227 C ATOM 145 C ASP A 53 -61.843 -17.794 -28.957 1.00 37.74 C ANISOU 145 C ASP A 53 4347 5109 4882 1952 714 261 C ATOM 146 O ASP A 53 -62.702 -18.122 -28.138 1.00 38.11 O ANISOU 146 O ASP A 53 4315 5248 4920 1976 742 254 O ATOM 147 CB ASP A 53 -61.750 -15.549 -27.858 1.00 39.67 C ANISOU 147 CB ASP A 53 4752 5190 5131 2112 815 204 C ATOM 148 CG ASP A 53 -60.896 -14.387 -27.380 1.00 41.42 C ANISOU 148 CG ASP A 53 5116 5254 5369 2137 854 153 C ATOM 149 OD1 ASP A 53 -61.316 -13.227 -27.579 1.00 45.61 O ANISOU 149 OD1 ASP A 53 5693 5723 5912 2256 887 163 O ATOM 150 OD2 ASP A 53 -59.818 -14.630 -26.792 1.00 43.29 O ANISOU 150 OD2 ASP A 53 5414 5427 5607 2039 850 101 O ATOM 151 N GLN A 54 -61.630 -18.473 -30.082 1.00 36.66 N ANISOU 151 N GLN A 54 4176 5002 4752 1895 653 296 N ATOM 152 CA GLN A 54 -62.433 -19.641 -30.450 1.00 36.27 C ANISOU 152 CA GLN A 54 3991 5089 4701 1857 607 322 C ATOM 153 C GLN A 54 -61.529 -20.726 -31.040 1.00 34.31 C ANISOU 153 C GLN A 54 3745 4833 4456 1726 549 320 C ATOM 154 O GLN A 54 -60.526 -20.414 -31.684 1.00 33.41 O ANISOU 154 O GLN A 54 3723 4629 4342 1700 533 321 O ATOM 155 CB GLN A 54 -63.525 -19.242 -31.447 1.00 37.50 C ANISOU 155 CB GLN A 54 4078 5315 4857 1967 582 371 C ATOM 156 CG GLN A 54 -64.495 -18.180 -30.910 1.00 40.84 C ANISOU 156 CG GLN A 54 4489 5751 5276 2109 641 378 C ATOM 157 CD GLN A 54 -65.587 -17.795 -31.897 1.00 44.53 C ANISOU 157 CD GLN A 54 4882 6296 5740 2226 613 430 C ATOM 158 OE1 GLN A 54 -66.068 -18.624 -32.671 1.00 47.52 O ANISOU 158 OE1 GLN A 54 5160 6776 6121 2196 549 453 O ATOM 159 NE2 GLN A 54 -65.992 -16.528 -31.863 1.00 47.09 N ANISOU 159 NE2 GLN A 54 5256 6575 6062 2364 658 444 N ATOM 160 N TYR A 55 -61.874 -21.992 -30.793 1.00 33.15 N ANISOU 160 N TYR A 55 3499 4780 4316 1643 523 317 N ATOM 161 CA TYR A 55 -61.112 -23.130 -31.326 1.00 31.75 C ANISOU 161 CA TYR A 55 3317 4604 4145 1521 467 312 C ATOM 162 C TYR A 55 -62.025 -24.161 -31.985 1.00 31.77 C ANISOU 162 C TYR A 55 3185 4724 4160 1495 409 334 C ATOM 163 O TYR A 55 -63.235 -24.173 -31.766 1.00 31.95 O ANISOU 163 O TYR A 55 3107 4839 4196 1550 419 349 O ATOM 164 CB TYR A 55 -60.283 -23.806 -30.219 1.00 30.98 C ANISOU 164 CB TYR A 55 3251 4472 4047 1417 491 276 C ATOM 165 CG TYR A 55 -61.110 -24.558 -29.188 1.00 31.23 C ANISOU 165 CG TYR A 55 3184 4596 4087 1394 520 275 C ATOM 166 CD1 TYR A 55 -61.384 -25.921 -29.334 1.00 30.73 C ANISOU 166 CD1 TYR A 55 3025 4605 4045 1303 482 286 C ATOM 167 CD2 TYR A 55 -61.625 -23.906 -28.074 1.00 32.64 C ANISOU 167 CD2 TYR A 55 3365 4785 4253 1464 588 265 C ATOM 168 CE1 TYR A 55 -62.153 -26.605 -28.394 1.00 31.44 C ANISOU 168 CE1 TYR A 55 3021 4775 4149 1280 517 295 C ATOM 169 CE2 TYR A 55 -62.390 -24.586 -27.128 1.00 33.06 C ANISOU 169 CE2 TYR A 55 3325 4926 4310 1448 623 272 C ATOM 170 CZ TYR A 55 -62.646 -25.935 -27.295 1.00 32.16 C ANISOU 170 CZ TYR A 55 3114 4881 4222 1353 589 291 C ATOM 171 OH TYR A 55 -63.406 -26.612 -26.368 1.00 31.88 O ANISOU 171 OH TYR A 55 2985 4929 4198 1335 632 308 O ATOM 172 N LYS A 56 -61.422 -25.024 -32.794 1.00 31.04 N ANISOU 172 N LYS A 56 3094 4629 4070 1411 348 331 N ATOM 173 CA LYS A 56 -62.094 -26.204 -33.325 1.00 31.16 C ANISOU 173 CA LYS A 56 2990 4742 4105 1357 287 335 C ATOM 174 C LYS A 56 -61.203 -27.414 -33.091 1.00 29.48 C ANISOU 174 C LYS A 56 2792 4503 3906 1221 266 311 C ATOM 175 O LYS A 56 -59.976 -27.318 -33.210 1.00 28.67 O ANISOU 175 O LYS A 56 2795 4313 3787 1180 267 298 O ATOM 176 CB LYS A 56 -62.367 -26.045 -34.823 1.00 31.92 C ANISOU 176 CB LYS A 56 3070 4873 4185 1410 218 353 C ATOM 177 CG LYS A 56 -63.001 -27.278 -35.465 1.00 34.09 C ANISOU 177 CG LYS A 56 3225 5245 4481 1350 141 345 C ATOM 178 CD LYS A 56 -63.476 -27.012 -36.876 1.00 37.21 C ANISOU 178 CD LYS A 56 3594 5695 4851 1427 71 360 C ATOM 179 CE LYS A 56 -64.092 -28.266 -37.483 1.00 39.05 C ANISOU 179 CE LYS A 56 3706 6022 5108 1361 -13 337 C ATOM 180 NZ LYS A 56 -65.386 -28.634 -36.831 1.00 40.91 N ANISOU 180 NZ LYS A 56 3796 6353 5393 1359 -4 339 N ATOM 181 N CYS A 57 -61.814 -28.550 -32.763 1.00 28.61 N ANISOU 181 N CYS A 57 2575 4467 3830 1151 250 308 N ATOM 182 CA CYS A 57 -61.079 -29.810 -32.695 1.00 27.33 C ANISOU 182 CA CYS A 57 2416 4283 3685 1025 222 289 C ATOM 183 C CYS A 57 -61.302 -30.619 -33.960 1.00 27.14 C ANISOU 183 C CYS A 57 2334 4303 3674 990 134 282 C ATOM 184 O CYS A 57 -62.437 -30.782 -34.415 1.00 27.75 O ANISOU 184 O CYS A 57 2303 4468 3772 1021 98 288 O ATOM 185 CB CYS A 57 -61.505 -30.644 -31.490 1.00 27.49 C ANISOU 185 CB CYS A 57 2364 4341 3740 961 264 293 C ATOM 186 SG CYS A 57 -61.162 -29.873 -29.921 1.00 26.30 S ANISOU 186 SG CYS A 57 2284 4146 3562 996 363 293 S ATOM 187 N ASP A 58 -60.209 -31.117 -34.517 1.00 26.10 N ANISOU 187 N ASP A 58 2274 4113 3528 927 98 264 N ATOM 188 CA ASP A 58 -60.239 -32.023 -35.650 1.00 26.16 C ANISOU 188 CA ASP A 58 2242 4154 3544 883 14 246 C ATOM 189 C ASP A 58 -60.153 -33.441 -35.094 1.00 25.62 C ANISOU 189 C ASP A 58 2122 4090 3524 761 5 228 C ATOM 190 O ASP A 58 -59.096 -33.873 -34.646 1.00 24.65 O ANISOU 190 O ASP A 58 2070 3898 3397 695 26 219 O ATOM 191 CB ASP A 58 -59.053 -31.727 -36.573 1.00 25.63 C ANISOU 191 CB ASP A 58 2289 4019 3430 892 -12 239 C ATOM 192 CG ASP A 58 -59.063 -32.561 -37.834 1.00 26.89 C ANISOU 192 CG ASP A 58 2419 4215 3582 864 -100 216 C ATOM 193 OD1 ASP A 58 -59.921 -33.467 -37.966 1.00 27.31 O ANISOU 193 OD1 ASP A 58 2364 4338 3675 822 -148 197 O ATOM 194 OD2 ASP A 58 -58.194 -32.304 -38.700 1.00 27.74 O ANISOU 194 OD2 ASP A 58 2612 4281 3646 885 -121 216 O ATOM 195 N CYS A 59 -61.278 -34.154 -35.114 1.00 26.67 N ANISOU 195 N CYS A 59 2125 4301 3706 734 -24 225 N ATOM 196 CA CYS A 59 -61.349 -35.493 -34.525 1.00 26.85 C ANISOU 196 CA CYS A 59 2088 4327 3788 620 -24 216 C ATOM 197 C CYS A 59 -61.125 -36.605 -35.549 1.00 26.87 C ANISOU 197 C CYS A 59 2070 4328 3811 548 -112 178 C ATOM 198 O CYS A 59 -61.386 -37.771 -35.260 1.00 27.13 O ANISOU 198 O CYS A 59 2035 4367 3906 455 -125 168 O ATOM 199 CB CYS A 59 -62.697 -35.704 -33.830 1.00 27.80 C ANISOU 199 CB CYS A 59 2072 4526 3964 619 5 238 C ATOM 200 SG CYS A 59 -63.194 -34.397 -32.682 1.00 29.22 S ANISOU 200 SG CYS A 59 2258 4725 4117 721 106 278 S ATOM 201 N THR A 60 -60.619 -36.251 -36.732 1.00 26.53 N ANISOU 201 N THR A 60 2090 4272 3717 592 -168 158 N ATOM 202 CA THR A 60 -60.378 -37.225 -37.800 1.00 26.56 C ANISOU 202 CA THR A 60 2086 4279 3727 540 -256 115 C ATOM 203 C THR A 60 -59.631 -38.465 -37.298 1.00 25.99 C ANISOU 203 C THR A 60 2036 4143 3695 422 -248 98 C ATOM 204 O THR A 60 -58.565 -38.355 -36.702 1.00 25.28 O ANISOU 204 O THR A 60 2042 3982 3583 402 -196 113 O ATOM 205 CB THR A 60 -59.575 -36.595 -38.964 1.00 26.11 C ANISOU 205 CB THR A 60 2130 4198 3591 607 -293 105 C ATOM 206 OG1 THR A 60 -60.311 -35.499 -39.511 1.00 25.83 O ANISOU 206 OG1 THR A 60 2072 4222 3519 721 -304 125 O ATOM 207 CG2 THR A 60 -59.318 -37.621 -40.062 1.00 26.70 C ANISOU 207 CG2 THR A 60 2201 4280 3664 560 -383 55 C ATOM 208 N ARG A 61 -60.227 -39.634 -37.543 1.00 26.91 N ANISOU 208 N ARG A 61 2061 4287 3876 346 -302 68 N ATOM 209 CA ARG A 61 -59.649 -40.948 -37.208 1.00 26.55 C ANISOU 209 CA ARG A 61 2026 4182 3879 234 -306 49 C ATOM 210 C ARG A 61 -59.311 -41.182 -35.725 1.00 26.26 C ANISOU 210 C ARG A 61 2008 4099 3873 183 -212 93 C ATOM 211 O ARG A 61 -58.498 -42.046 -35.404 1.00 26.28 O ANISOU 211 O ARG A 61 2057 4035 3892 110 -202 88 O ATOM 212 CB ARG A 61 -58.427 -41.248 -38.097 1.00 26.13 C ANISOU 212 CB ARG A 61 2081 4072 3776 226 -350 14 C ATOM 213 CG ARG A 61 -58.793 -41.612 -39.521 1.00 26.79 C ANISOU 213 CG ARG A 61 2131 4199 3848 241 -455 -42 C ATOM 214 CD ARG A 61 -57.554 -41.921 -40.360 1.00 26.64 C ANISOU 214 CD ARG A 61 2222 4126 3774 240 -490 -74 C ATOM 215 NE ARG A 61 -56.745 -40.728 -40.623 1.00 25.13 N ANISOU 215 NE ARG A 61 2134 3917 3495 328 -454 -42 N ATOM 216 CZ ARG A 61 -57.047 -39.777 -41.510 1.00 24.93 C ANISOU 216 CZ ARG A 61 2119 3944 3409 428 -482 -37 C ATOM 217 NH1 ARG A 61 -58.158 -39.841 -42.232 1.00 25.27 N ANISOU 217 NH1 ARG A 61 2073 4071 3459 460 -554 -65 N ATOM 218 NH2 ARG A 61 -56.231 -38.735 -41.662 1.00 23.18 N ANISOU 218 NH2 ARG A 61 1997 3690 3121 497 -438 -2 N ATOM 219 N THR A 62 -59.943 -40.435 -34.824 1.00 26.39 N ANISOU 219 N THR A 62 1985 4151 3891 227 -144 135 N ATOM 220 CA THR A 62 -59.725 -40.630 -33.388 1.00 26.14 C ANISOU 220 CA THR A 62 1965 4089 3878 190 -55 177 C ATOM 221 C THR A 62 -60.633 -41.715 -32.813 1.00 26.96 C ANISOU 221 C THR A 62 1950 4219 4074 108 -41 194 C ATOM 222 O THR A 62 -60.330 -42.283 -31.769 1.00 27.20 O ANISOU 222 O THR A 62 1992 4214 4128 55 21 226 O ATOM 223 CB THR A 62 -59.997 -39.346 -32.584 1.00 25.97 C ANISOU 223 CB THR A 62 1960 4095 3814 278 19 213 C ATOM 224 OG1 THR A 62 -61.351 -38.933 -32.786 1.00 25.97 O ANISOU 224 OG1 THR A 62 1848 4180 3840 327 9 222 O ATOM 225 CG2 THR A 62 -59.029 -38.236 -32.999 1.00 24.92 C ANISOU 225 CG2 THR A 62 1950 3919 3599 352 19 202 C ATOM 226 N GLY A 63 -61.743 -41.985 -33.490 1.00 28.11 N ANISOU 226 N GLY A 63 1979 4428 4273 100 -98 174 N ATOM 227 CA GLY A 63 -62.772 -42.882 -32.960 1.00 29.04 C ANISOU 227 CA GLY A 63 1964 4579 4492 25 -81 194 C ATOM 228 C GLY A 63 -63.832 -42.149 -32.151 1.00 29.88 C ANISOU 228 C GLY A 63 1983 4761 4608 82 -12 243 C ATOM 229 O GLY A 63 -64.779 -42.767 -31.656 1.00 30.61 O ANISOU 229 O GLY A 63 1953 4891 4785 29 15 269 O ATOM 230 N PHE A 64 -63.680 -40.830 -32.034 1.00 29.39 N ANISOU 230 N PHE A 64 1982 4719 4465 190 20 254 N ATOM 231 CA PHE A 64 -64.595 -39.985 -31.273 1.00 30.06 C ANISOU 231 CA PHE A 64 2004 4874 4546 264 89 297 C ATOM 232 C PHE A 64 -65.044 -38.816 -32.134 1.00 30.60 C ANISOU 232 C PHE A 64 2066 4996 4565 375 46 278 C ATOM 233 O PHE A 64 -64.428 -38.520 -33.160 1.00 30.27 O ANISOU 233 O PHE A 64 2100 4927 4475 403 -21 241 O ATOM 234 CB PHE A 64 -63.898 -39.430 -30.030 1.00 29.55 C ANISOU 234 CB PHE A 64 2036 4769 4422 298 188 334 C ATOM 235 CG PHE A 64 -63.445 -40.479 -29.053 1.00 29.07 C ANISOU 235 CG PHE A 64 1987 4661 4395 207 242 363 C ATOM 236 CD1 PHE A 64 -62.253 -41.163 -29.246 1.00 28.75 C ANISOU 236 CD1 PHE A 64 2044 4538 4344 143 214 342 C ATOM 237 CD2 PHE A 64 -64.196 -40.758 -27.918 1.00 30.83 C ANISOU 237 CD2 PHE A 64 2129 4927 4658 193 327 418 C ATOM 238 CE1 PHE A 64 -61.823 -42.122 -28.335 1.00 28.76 C ANISOU 238 CE1 PHE A 64 2059 4495 4372 67 265 375 C ATOM 239 CE2 PHE A 64 -63.773 -41.716 -27.002 1.00 30.15 C ANISOU 239 CE2 PHE A 64 2059 4799 4599 116 381 455 C ATOM 240 CZ PHE A 64 -62.594 -42.402 -27.214 1.00 29.60 C ANISOU 240 CZ PHE A 64 2085 4642 4518 54 349 434 C ATOM 241 N TYR A 65 -66.111 -38.150 -31.707 1.00 31.53 N ANISOU 241 N TYR A 65 2096 5192 4693 444 89 308 N ATOM 242 CA TYR A 65 -66.582 -36.927 -32.356 1.00 32.22 C ANISOU 242 CA TYR A 65 2181 5330 4730 567 64 302 C ATOM 243 C TYR A 65 -67.117 -35.953 -31.302 1.00 32.42 C ANISOU 243 C TYR A 65 2193 5393 4732 656 161 346 C ATOM 244 O TYR A 65 -66.991 -36.204 -30.104 1.00 32.35 O ANISOU 244 O TYR A 65 2192 5367 4732 625 246 377 O ATOM 245 CB TYR A 65 -67.630 -37.251 -33.428 1.00 33.39 C ANISOU 245 CB TYR A 65 2196 5562 4927 566 -29 275 C ATOM 246 CG TYR A 65 -68.862 -37.953 -32.913 1.00 35.59 C ANISOU 246 CG TYR A 65 2302 5916 5303 512 -8 297 C ATOM 247 CD1 TYR A 65 -69.999 -37.236 -32.562 1.00 37.71 C ANISOU 247 CD1 TYR A 65 2467 6276 5583 596 32 330 C ATOM 248 CD2 TYR A 65 -68.891 -39.338 -32.786 1.00 36.48 C ANISOU 248 CD2 TYR A 65 2352 6005 5502 378 -27 288 C ATOM 249 CE1 TYR A 65 -71.135 -37.879 -32.092 1.00 39.24 C ANISOU 249 CE1 TYR A 65 2493 6543 5873 545 55 355 C ATOM 250 CE2 TYR A 65 -70.020 -39.991 -32.318 1.00 38.02 C ANISOU 250 CE2 TYR A 65 2384 6264 5798 321 -3 313 C ATOM 251 CZ TYR A 65 -71.138 -39.258 -31.973 1.00 39.27 C ANISOU 251 CZ TYR A 65 2434 6519 5966 404 39 348 C ATOM 252 OH TYR A 65 -72.262 -39.905 -31.507 1.00 41.01 O ANISOU 252 OH TYR A 65 2483 6806 6292 346 67 377 O ATOM 253 N GLY A 66 -67.685 -34.836 -31.744 1.00 33.09 N ANISOU 253 N GLY A 66 2264 5527 4780 774 152 348 N ATOM 254 CA GLY A 66 -68.151 -33.796 -30.833 1.00 33.70 C ANISOU 254 CA GLY A 66 2343 5633 4827 876 241 382 C ATOM 255 C GLY A 66 -67.117 -32.698 -30.671 1.00 32.93 C ANISOU 255 C GLY A 66 2413 5453 4646 949 274 374 C ATOM 256 O GLY A 66 -65.973 -32.837 -31.122 1.00 31.85 O ANISOU 256 O GLY A 66 2388 5235 4478 908 239 349 O ATOM 257 N GLU A 67 -67.514 -31.612 -30.010 1.00 33.61 N ANISOU 257 N GLU A 67 2514 5557 4699 1056 344 394 N ATOM 258 CA GLU A 67 -66.683 -30.410 -29.915 1.00 33.34 C ANISOU 258 CA GLU A 67 2629 5444 4594 1139 373 383 C ATOM 259 C GLU A 67 -65.247 -30.689 -29.457 1.00 32.01 C ANISOU 259 C GLU A 67 2594 5171 4396 1065 390 363 C ATOM 260 O GLU A 67 -64.317 -30.091 -29.994 1.00 31.07 O ANISOU 260 O GLU A 67 2593 4976 4237 1087 366 343 O ATOM 261 CB GLU A 67 -67.327 -29.359 -28.999 1.00 34.41 C ANISOU 261 CB GLU A 67 2759 5609 4706 1253 459 403 C ATOM 262 CG GLU A 67 -66.562 -28.028 -28.983 1.00 35.66 C ANISOU 262 CG GLU A 67 3068 5680 4802 1344 484 386 C ATOM 263 CD GLU A 67 -67.180 -26.976 -28.075 1.00 38.83 C ANISOU 263 CD GLU A 67 3473 6102 5179 1461 568 397 C ATOM 264 OE1 GLU A 67 -68.206 -27.259 -27.423 1.00 41.24 O ANISOU 264 OE1 GLU A 67 3662 6497 5509 1478 612 422 O ATOM 265 OE2 GLU A 67 -66.629 -25.853 -28.013 1.00 40.78 O ANISOU 265 OE2 GLU A 67 3840 6272 5384 1538 591 380 O ATOM 266 N ASN A 68 -65.079 -31.591 -28.488 1.00 31.51 N ANISOU 266 N ASN A 68 2510 5108 4355 980 432 373 N ATOM 267 CA ASN A 68 -63.763 -31.913 -27.918 1.00 30.84 C ANISOU 267 CA ASN A 68 2541 4935 4241 914 451 357 C ATOM 268 C ASN A 68 -63.286 -33.342 -28.197 1.00 29.61 C ANISOU 268 C ASN A 68 2363 4760 4126 784 406 353 C ATOM 269 O ASN A 68 -62.366 -33.822 -27.534 1.00 27.96 O ANISOU 269 O ASN A 68 2224 4498 3903 723 430 350 O ATOM 270 CB ASN A 68 -63.781 -31.707 -26.399 1.00 31.54 C ANISOU 270 CB ASN A 68 2651 5030 4305 936 547 372 C ATOM 271 CG ASN A 68 -64.078 -30.279 -25.997 1.00 35.40 C ANISOU 271 CG ASN A 68 3185 5519 4748 1065 597 365 C ATOM 272 OD1 ASN A 68 -63.833 -29.341 -26.759 1.00 33.29 O ANISOU 272 OD1 ASN A 68 2980 5211 4459 1129 565 346 O ATOM 273 ND2 ASN A 68 -64.595 -30.107 -24.764 1.00 44.60 N ANISOU 273 ND2 ASN A 68 4322 6727 5897 1106 680 383 N ATOM 274 N CYS A 69 -63.903 -34.016 -29.166 1.00 29.73 N ANISOU 274 N CYS A 69 2284 4821 4192 745 337 351 N ATOM 275 CA CYS A 69 -63.582 -35.410 -29.495 1.00 29.58 C ANISOU 275 CA CYS A 69 2234 4783 4222 623 290 342 C ATOM 276 C CYS A 69 -63.754 -36.337 -28.284 1.00 29.78 C ANISOU 276 C CYS A 69 2210 4818 4286 550 356 375 C ATOM 277 O CYS A 69 -62.912 -37.203 -28.038 1.00 28.58 O ANISOU 277 O CYS A 69 2108 4610 4142 466 353 372 O ATOM 278 CB CYS A 69 -62.153 -35.531 -30.042 1.00 28.72 C ANISOU 278 CB CYS A 69 2255 4583 4075 586 247 310 C ATOM 279 SG CYS A 69 -61.716 -34.308 -31.296 1.00 29.40 S ANISOU 279 SG CYS A 69 2427 4641 4102 680 194 284 S ATOM 280 N THR A 70 -64.840 -36.146 -27.534 1.00 30.98 N ANISOU 280 N THR A 70 2266 5045 4461 589 418 412 N ATOM 281 CA THR A 70 -65.128 -36.980 -26.355 1.00 31.86 C ANISOU 281 CA THR A 70 2321 5176 4608 530 493 456 C ATOM 282 C THR A 70 -66.350 -37.899 -26.499 1.00 33.35 C ANISOU 282 C THR A 70 2340 5436 4896 470 486 484 C ATOM 283 O THR A 70 -66.604 -38.710 -25.608 1.00 33.89 O ANISOU 283 O THR A 70 2355 5516 5007 410 548 529 O ATOM 284 CB THR A 70 -65.321 -36.121 -25.084 1.00 32.07 C ANISOU 284 CB THR A 70 2376 5230 4579 619 595 484 C ATOM 285 OG1 THR A 70 -66.343 -35.145 -25.311 1.00 32.83 O ANISOU 285 OG1 THR A 70 2407 5396 4670 721 605 487 O ATOM 286 CG2 THR A 70 -64.020 -35.433 -24.701 1.00 31.56 C ANISOU 286 CG2 THR A 70 2477 5086 4429 653 609 454 C ATOM 287 N THR A 71 -67.106 -37.780 -27.591 1.00 34.05 N ANISOU 287 N THR A 71 2342 5573 5023 485 412 461 N ATOM 288 CA THR A 71 -68.231 -38.687 -27.835 1.00 35.52 C ANISOU 288 CA THR A 71 2359 5823 5313 417 390 477 C ATOM 289 C THR A 71 -67.747 -39.868 -28.665 1.00 35.46 C ANISOU 289 C THR A 71 2352 5760 5359 300 303 440 C ATOM 290 O THR A 71 -67.374 -39.694 -29.825 1.00 35.11 O ANISOU 290 O THR A 71 2352 5696 5291 312 210 388 O ATOM 291 CB THR A 71 -69.398 -37.991 -28.564 1.00 36.30 C ANISOU 291 CB THR A 71 2347 6017 5429 497 348 467 C ATOM 292 OG1 THR A 71 -69.775 -36.810 -27.850 1.00 36.72 O ANISOU 292 OG1 THR A 71 2414 6114 5425 619 427 495 O ATOM 293 CG2 THR A 71 -70.607 -38.922 -28.665 1.00 38.29 C ANISOU 293 CG2 THR A 71 2409 6342 5797 422 333 484 C ATOM 294 N PRO A 72 -67.738 -41.077 -28.076 1.00 36.24 N ANISOU 294 N PRO A 72 2408 5830 5530 191 336 470 N ATOM 295 CA PRO A 72 -67.231 -42.236 -28.806 1.00 36.31 C ANISOU 295 CA PRO A 72 2428 5775 5594 79 259 432 C ATOM 296 C PRO A 72 -68.199 -42.777 -29.852 1.00 37.83 C ANISOU 296 C PRO A 72 2480 6017 5877 32 166 394 C ATOM 297 O PRO A 72 -69.415 -42.743 -29.654 1.00 38.84 O ANISOU 297 O PRO A 72 2461 6227 6067 38 188 420 O ATOM 298 CB PRO A 72 -66.999 -43.273 -27.704 1.00 36.43 C ANISOU 298 CB PRO A 72 2438 5744 5659 -10 339 486 C ATOM 299 CG PRO A 72 -67.967 -42.921 -26.642 1.00 37.33 C ANISOU 299 CG PRO A 72 2459 5935 5789 32 441 554 C ATOM 300 CD PRO A 72 -68.185 -41.435 -26.714 1.00 36.99 C ANISOU 300 CD PRO A 72 2447 5950 5658 169 451 541 C ATOM 301 N GLU A 73 -67.647 -43.259 -30.962 1.00 38.21 N ANISOU 301 N GLU A 73 2572 6018 5928 -12 63 330 N ATOM 302 CA GLU A 73 -68.409 -44.026 -31.944 1.00 40.04 C ANISOU 302 CA GLU A 73 2681 6280 6250 -79 -35 281 C ATOM 303 C GLU A 73 -68.732 -45.391 -31.337 1.00 41.14 C ANISOU 303 C GLU A 73 2735 6383 6513 -213 -1 309 C ATOM 304 O GLU A 73 -68.094 -45.808 -30.369 1.00 40.31 O ANISOU 304 O GLU A 73 2699 6213 6406 -251 82 358 O ATOM 305 CB GLU A 73 -67.606 -44.196 -33.236 1.00 39.63 C ANISOU 305 CB GLU A 73 2721 6183 6156 -84 -149 202 C ATOM 306 CG GLU A 73 -67.408 -42.891 -34.012 1.00 40.52 C ANISOU 306 CG GLU A 73 2902 6336 6157 46 -191 177 C ATOM 307 CD GLU A 73 -66.271 -42.947 -35.019 1.00 41.68 C ANISOU 307 CD GLU A 73 3180 6420 6234 53 -268 120 C ATOM 308 OE1 GLU A 73 -65.589 -43.988 -35.115 1.00 42.58 O ANISOU 308 OE1 GLU A 73 3338 6458 6381 -40 -290 96 O ATOM 309 OE2 GLU A 73 -66.055 -41.931 -35.714 1.00 43.67 O ANISOU 309 OE2 GLU A 73 3494 6699 6398 155 -301 105 O ATOM 310 N PHE A 74 -69.719 -46.084 -31.901 1.00 43.14 N ANISOU 310 N PHE A 74 2839 6677 6878 -282 -65 279 N ATOM 311 CA PHE A 74 -70.189 -47.343 -31.318 1.00 44.67 C ANISOU 311 CA PHE A 74 2930 6836 7207 -412 -26 313 C ATOM 312 C PHE A 74 -69.064 -48.367 -31.166 1.00 44.21 C ANISOU 312 C PHE A 74 2985 6650 7162 -501 -22 306 C ATOM 313 O PHE A 74 -68.918 -48.980 -30.108 1.00 44.28 O ANISOU 313 O PHE A 74 2998 6611 7217 -558 75 376 O ATOM 314 CB PHE A 74 -71.333 -47.937 -32.141 1.00 46.52 C ANISOU 314 CB PHE A 74 2989 7123 7562 -479 -118 261 C ATOM 315 CG PHE A 74 -71.957 -49.152 -31.511 1.00 48.74 C ANISOU 315 CG PHE A 74 3146 7372 8000 -614 -69 303 C ATOM 316 CD1 PHE A 74 -72.856 -49.019 -30.460 1.00 50.80 C ANISOU 316 CD1 PHE A 74 3290 7695 8319 -613 43 392 C ATOM 317 CD2 PHE A 74 -71.635 -50.427 -31.959 1.00 50.22 C ANISOU 317 CD2 PHE A 74 3337 7464 8280 -739 -130 255 C ATOM 318 CE1 PHE A 74 -73.431 -50.139 -29.870 1.00 52.75 C ANISOU 318 CE1 PHE A 74 3419 7908 8715 -738 97 440 C ATOM 319 CE2 PHE A 74 -72.208 -51.553 -31.375 1.00 51.81 C ANISOU 319 CE2 PHE A 74 3425 7624 8636 -867 -81 298 C ATOM 320 CZ PHE A 74 -73.105 -51.409 -30.330 1.00 53.26 C ANISOU 320 CZ PHE A 74 3488 7869 8879 -869 35 394 C ATOM 321 N LEU A 75 -68.262 -48.535 -32.213 1.00 43.81 N ANISOU 321 N LEU A 75 3030 6548 7068 -504 -123 227 N ATOM 322 CA LEU A 75 -67.143 -49.476 -32.172 1.00 43.52 C ANISOU 322 CA LEU A 75 3106 6391 7037 -577 -127 214 C ATOM 323 C LEU A 75 -66.142 -49.078 -31.085 1.00 42.55 C ANISOU 323 C LEU A 75 3119 6225 6825 -531 -19 282 C ATOM 324 O LEU A 75 -65.612 -49.937 -30.375 1.00 42.41 O ANISOU 324 O LEU A 75 3143 6127 6845 -600 37 323 O ATOM 325 CB LEU A 75 -66.442 -49.556 -33.532 1.00 43.19 C ANISOU 325 CB LEU A 75 3149 6317 6944 -565 -251 115 C ATOM 326 CG LEU A 75 -65.906 -50.938 -33.912 1.00 44.00 C ANISOU 326 CG LEU A 75 3283 6313 7122 -677 -301 69 C ATOM 327 CD1 LEU A 75 -67.059 -51.825 -34.385 1.00 45.92 C ANISOU 327 CD1 LEU A 75 3362 6574 7512 -775 -367 26 C ATOM 328 CD2 LEU A 75 -64.822 -50.835 -34.987 1.00 43.96 C ANISOU 328 CD2 LEU A 75 3413 6268 7023 -637 -389 -9 C ATOM 329 N THR A 76 -65.897 -47.774 -30.956 1.00 41.98 N ANISOU 329 N THR A 76 3112 6203 6636 -413 6 294 N ATOM 330 CA THR A 76 -65.015 -47.246 -29.916 1.00 41.21 C ANISOU 330 CA THR A 76 3135 6076 6448 -360 102 350 C ATOM 331 C THR A 76 -65.525 -47.582 -28.509 1.00 42.45 C ANISOU 331 C THR A 76 3228 6245 6654 -389 223 441 C ATOM 332 O THR A 76 -64.739 -47.948 -27.635 1.00 41.75 O ANISOU 332 O THR A 76 3225 6099 6541 -407 291 486 O ATOM 333 CB THR A 76 -64.854 -45.717 -30.046 1.00 40.56 C ANISOU 333 CB THR A 76 3115 6049 6247 -228 106 341 C ATOM 334 OG1 THR A 76 -64.476 -45.390 -31.390 1.00 39.41 O ANISOU 334 OG1 THR A 76 3018 5898 6056 -196 -1 266 O ATOM 335 CG2 THR A 76 -63.804 -45.198 -29.078 1.00 39.09 C ANISOU 335 CG2 THR A 76 3064 5822 5968 -179 187 380 C ATOM 336 N ARG A 77 -66.832 -47.450 -28.295 1.00 44.35 N ANISOU 336 N ARG A 77 3320 6568 6962 -388 250 471 N ATOM 337 CA ARG A 77 -67.445 -47.832 -27.016 1.00 45.96 C ANISOU 337 CA ARG A 77 3446 6794 7222 -418 369 563 C ATOM 338 C ARG A 77 -67.138 -49.290 -26.663 1.00 46.64 C ANISOU 338 C ARG A 77 3529 6789 7404 -542 393 594 C ATOM 339 O ARG A 77 -66.765 -49.595 -25.527 1.00 46.48 O ANISOU 339 O ARG A 77 3555 6738 7369 -550 494 670 O ATOM 340 CB ARG A 77 -68.964 -47.619 -27.038 1.00 47.50 C ANISOU 340 CB ARG A 77 3459 7092 7498 -413 382 584 C ATOM 341 CG ARG A 77 -69.414 -46.215 -26.657 1.00 48.48 C ANISOU 341 CG ARG A 77 3575 7313 7531 -279 431 605 C ATOM 342 CD ARG A 77 -70.915 -46.174 -26.347 1.00 51.35 C ANISOU 342 CD ARG A 77 3749 7778 7984 -279 476 650 C ATOM 343 NE ARG A 77 -71.297 -44.951 -25.634 1.00 52.84 N ANISOU 343 NE ARG A 77 3939 8050 8086 -150 557 690 N ATOM 344 CZ ARG A 77 -71.643 -43.794 -26.206 1.00 53.95 C ANISOU 344 CZ ARG A 77 4074 8259 8165 -42 514 651 C ATOM 345 NH1 ARG A 77 -71.674 -43.656 -27.532 1.00 54.30 N ANISOU 345 NH1 ARG A 77 4108 8308 8214 -40 388 573 N ATOM 346 NH2 ARG A 77 -71.963 -42.755 -25.441 1.00 54.62 N ANISOU 346 NH2 ARG A 77 4166 8408 8177 73 599 691 N ATOM 347 N ILE A 78 -67.290 -50.175 -27.647 1.00 47.70 N ANISOU 347 N ILE A 78 3614 6878 7634 -634 297 534 N ATOM 348 CA ILE A 78 -67.041 -51.607 -27.461 1.00 48.63 C ANISOU 348 CA ILE A 78 3725 6894 7856 -757 307 553 C ATOM 349 C ILE A 78 -65.572 -51.888 -27.166 1.00 47.79 C ANISOU 349 C ILE A 78 3794 6693 7671 -751 323 558 C ATOM 350 O ILE A 78 -65.259 -52.616 -26.226 1.00 48.16 O ANISOU 350 O ILE A 78 3867 6684 7748 -795 408 631 O ATOM 351 CB ILE A 78 -67.488 -52.431 -28.694 1.00 49.46 C ANISOU 351 CB ILE A 78 3747 6968 8075 -851 186 467 C ATOM 352 CG1 ILE A 78 -69.012 -52.397 -28.825 1.00 51.12 C ANISOU 352 CG1 ILE A 78 3761 7269 8394 -881 179 473 C ATOM 353 CG2 ILE A 78 -66.996 -53.875 -28.586 1.00 49.74 C ANISOU 353 CG2 ILE A 78 3813 6878 8209 -970 189 474 C ATOM 354 CD1 ILE A 78 -69.548 -53.156 -30.025 1.00 52.50 C ANISOU 354 CD1 ILE A 78 3840 7424 8683 -971 52 379 C ATOM 355 N LYS A 79 -64.675 -51.310 -27.963 1.00 47.03 N ANISOU 355 N LYS A 79 3814 6583 7474 -692 245 485 N ATOM 356 CA LYS A 79 -63.236 -51.472 -27.739 1.00 46.23 C ANISOU 356 CA LYS A 79 3875 6401 7291 -677 255 484 C ATOM 357 C LYS A 79 -62.831 -50.974 -26.351 1.00 45.76 C ANISOU 357 C LYS A 79 3878 6359 7150 -616 374 570 C ATOM 358 O LYS A 79 -62.046 -51.627 -25.665 1.00 45.55 O ANISOU 358 O LYS A 79 3928 6265 7115 -643 424 613 O ATOM 359 CB LYS A 79 -62.420 -50.747 -28.815 1.00 45.36 C ANISOU 359 CB LYS A 79 3866 6288 7081 -612 161 398 C ATOM 360 CG LYS A 79 -62.467 -51.414 -30.189 1.00 46.67 C ANISOU 360 CG LYS A 79 4009 6417 7305 -670 39 307 C ATOM 361 CD LYS A 79 -61.335 -50.935 -31.103 1.00 46.66 C ANISOU 361 CD LYS A 79 4140 6391 7198 -612 -34 238 C ATOM 362 CE LYS A 79 -61.564 -49.518 -31.625 1.00 47.20 C ANISOU 362 CE LYS A 79 4213 6546 7173 -504 -64 212 C ATOM 363 NZ LYS A 79 -62.661 -49.453 -32.638 1.00 48.53 N ANISOU 363 NZ LYS A 79 4266 6781 7394 -509 -150 156 N ATOM 364 N LEU A 80 -63.371 -49.824 -25.948 1.00 45.74 N ANISOU 364 N LEU A 80 3845 6449 7085 -527 416 591 N ATOM 365 CA LEU A 80 -63.131 -49.275 -24.608 1.00 45.54 C ANISOU 365 CA LEU A 80 3869 6455 6979 -460 528 665 C ATOM 366 C LEU A 80 -63.553 -50.256 -23.513 1.00 46.45 C ANISOU 366 C LEU A 80 3923 6554 7171 -524 629 761 C ATOM 367 O LEU A 80 -62.827 -50.453 -22.541 1.00 45.96 O ANISOU 367 O LEU A 80 3946 6463 7054 -507 700 816 O ATOM 368 CB LEU A 80 -63.878 -47.944 -24.416 1.00 45.80 C ANISOU 368 CB LEU A 80 3857 6592 6953 -359 556 668 C ATOM 369 CG LEU A 80 -63.149 -46.638 -24.764 1.00 45.18 C ANISOU 369 CG LEU A 80 3890 6528 6748 -254 519 613 C ATOM 370 CD1 LEU A 80 -62.300 -46.760 -26.022 1.00 44.85 C ANISOU 370 CD1 LEU A 80 3926 6425 6691 -275 408 532 C ATOM 371 CD2 LEU A 80 -64.159 -45.498 -24.898 1.00 46.15 C ANISOU 371 CD2 LEU A 80 3936 6748 6849 -169 526 606 C ATOM 372 N LEU A 81 -64.727 -50.861 -23.684 1.00 47.60 N ANISOU 372 N LEU A 81 3920 6722 7445 -595 635 782 N ATOM 373 CA LEU A 81 -65.288 -51.779 -22.688 1.00 48.83 C ANISOU 373 CA LEU A 81 3998 6865 7690 -660 738 883 C ATOM 374 C LEU A 81 -64.404 -53.017 -22.503 1.00 48.30 C ANISOU 374 C LEU A 81 4008 6680 7665 -740 745 907 C ATOM 375 O LEU A 81 -64.157 -53.442 -21.376 1.00 48.83 O ANISOU 375 O LEU A 81 4107 6729 7718 -739 847 999 O ATOM 376 CB LEU A 81 -66.712 -52.204 -23.088 1.00 50.39 C ANISOU 376 CB LEU A 81 4009 7102 8034 -733 728 889 C ATOM 377 CG LEU A 81 -67.771 -52.336 -21.983 1.00 52.64 C ANISOU 377 CG LEU A 81 4171 7452 8379 -739 857 1000 C ATOM 378 CD1 LEU A 81 -67.262 -53.155 -20.796 1.00 53.66 C ANISOU 378 CD1 LEU A 81 4358 7521 8509 -768 970 1104 C ATOM 379 CD2 LEU A 81 -68.253 -50.960 -21.522 1.00 52.90 C ANISOU 379 CD2 LEU A 81 4185 7606 8307 -611 906 1013 C ATOM 380 N LEU A 82 -63.923 -53.583 -23.607 1.00 47.51 N ANISOU 380 N LEU A 82 3941 6502 7608 -800 637 825 N ATOM 381 CA LEU A 82 -63.142 -54.822 -23.563 1.00 47.21 C ANISOU 381 CA LEU A 82 3970 6345 7623 -879 634 840 C ATOM 382 C LEU A 82 -61.671 -54.618 -23.190 1.00 45.30 C ANISOU 382 C LEU A 82 3899 6061 7252 -816 642 840 C ATOM 383 O LEU A 82 -61.044 -55.526 -22.646 1.00 45.52 O ANISOU 383 O LEU A 82 3985 6010 7300 -854 685 892 O ATOM 384 CB LEU A 82 -63.221 -55.553 -24.910 1.00 47.62 C ANISOU 384 CB LEU A 82 3989 6329 7775 -966 512 745 C ATOM 385 CG LEU A 82 -64.616 -55.889 -25.456 1.00 49.55 C ANISOU 385 CG LEU A 82 4060 6605 8163 -1043 479 724 C ATOM 386 CD1 LEU A 82 -64.503 -56.876 -26.615 1.00 50.67 C ANISOU 386 CD1 LEU A 82 4191 6654 8407 -1139 366 633 C ATOM 387 CD2 LEU A 82 -65.546 -56.440 -24.379 1.00 51.02 C ANISOU 387 CD2 LEU A 82 4131 6803 8453 -1097 599 839 C ATOM 388 N LYS A 83 -61.124 -53.437 -23.476 1.00 43.49 N ANISOU 388 N LYS A 83 3747 5883 6895 -721 602 784 N ATOM 389 CA LYS A 83 -59.685 -53.199 -23.323 1.00 41.53 C ANISOU 389 CA LYS A 83 3654 5595 6532 -668 590 766 C ATOM 390 C LYS A 83 -59.221 -53.250 -21.861 1.00 40.61 C ANISOU 390 C LYS A 83 3595 5485 6348 -627 700 860 C ATOM 391 O LYS A 83 -59.691 -52.466 -21.038 1.00 40.64 O ANISOU 391 O LYS A 83 3574 5572 6294 -560 772 905 O ATOM 392 CB LYS A 83 -59.295 -51.845 -23.930 1.00 40.70 C ANISOU 392 CB LYS A 83 3606 5543 6314 -578 529 690 C ATOM 393 CG LYS A 83 -57.802 -51.555 -23.877 1.00 40.35 C ANISOU 393 CG LYS A 83 3712 5459 6162 -529 509 663 C ATOM 394 CD LYS A 83 -57.452 -50.209 -24.493 1.00 40.90 C ANISOU 394 CD LYS A 83 3833 5574 6134 -446 455 594 C ATOM 395 CE LYS A 83 -55.943 -50.022 -24.533 1.00 40.37 C ANISOU 395 CE LYS A 83 3903 5459 5977 -413 430 565 C ATOM 396 NZ LYS A 83 -55.522 -48.688 -25.050 1.00 40.27 N ANISOU 396 NZ LYS A 83 3947 5481 5874 -334 390 507 N ATOM 397 N PRO A 84 -58.289 -54.167 -21.539 1.00 39.36 N ANISOU 397 N PRO A 84 3519 5244 6193 -658 714 890 N ATOM 398 CA PRO A 84 -57.739 -54.206 -20.184 1.00 38.67 C ANISOU 398 CA PRO A 84 3497 5168 6026 -608 810 976 C ATOM 399 C PRO A 84 -56.756 -53.070 -19.925 1.00 36.44 C ANISOU 399 C PRO A 84 3325 4929 5589 -505 794 936 C ATOM 400 O PRO A 84 -56.106 -52.590 -20.855 1.00 35.58 O ANISOU 400 O PRO A 84 3272 4802 5443 -490 706 847 O ATOM 401 CB PRO A 84 -57.016 -55.555 -20.138 1.00 38.86 C ANISOU 401 CB PRO A 84 3574 5083 6108 -673 811 1007 C ATOM 402 CG PRO A 84 -56.634 -55.819 -21.537 1.00 38.77 C ANISOU 402 CG PRO A 84 3581 5007 6142 -720 694 906 C ATOM 403 CD PRO A 84 -57.736 -55.245 -22.380 1.00 39.33 C ANISOU 403 CD PRO A 84 3546 5132 6264 -736 644 848 C ATOM 404 N THR A 85 -56.646 -52.659 -18.665 1.00 35.46 N ANISOU 404 N THR A 85 3233 4862 5378 -436 881 1000 N ATOM 405 CA THR A 85 -55.728 -51.588 -18.282 1.00 33.59 C ANISOU 405 CA THR A 85 3098 4666 4998 -341 871 961 C ATOM 406 C THR A 85 -54.282 -52.072 -18.343 1.00 32.35 C ANISOU 406 C THR A 85 3054 4438 4797 -344 830 942 C ATOM 407 O THR A 85 -54.031 -53.280 -18.306 1.00 32.28 O ANISOU 407 O THR A 85 3052 4359 4854 -404 840 985 O ATOM 408 CB THR A 85 -55.998 -51.089 -16.851 1.00 34.09 C ANISOU 408 CB THR A 85 3166 4811 4976 -263 974 1032 C ATOM 409 OG1 THR A 85 -55.671 -52.123 -15.913 1.00 33.69 O ANISOU 409 OG1 THR A 85 3141 4731 4928 -279 1044 1124 O ATOM 410 CG2 THR A 85 -57.463 -50.661 -16.681 1.00 34.65 C ANISOU 410 CG2 THR A 85 3118 4957 5090 -254 1028 1063 C ATOM 411 N PRO A 86 -53.322 -51.134 -18.442 1.00 30.51 N ANISOU 411 N PRO A 86 2910 4222 4459 -280 786 878 N ATOM 412 CA PRO A 86 -51.915 -51.529 -18.400 1.00 29.57 C ANISOU 412 CA PRO A 86 2893 4049 4292 -274 753 863 C ATOM 413 C PRO A 86 -51.542 -52.324 -17.148 1.00 29.64 C ANISOU 413 C PRO A 86 2936 4054 4270 -260 829 955 C ATOM 414 O PRO A 86 -50.771 -53.280 -17.239 1.00 29.22 O ANISOU 414 O PRO A 86 2928 3932 4241 -293 813 972 O ATOM 415 CB PRO A 86 -51.171 -50.190 -18.422 1.00 28.58 C ANISOU 415 CB PRO A 86 2838 3965 4057 -198 715 792 C ATOM 416 CG PRO A 86 -52.096 -49.261 -19.126 1.00 28.97 C ANISOU 416 CG PRO A 86 2826 4053 4129 -189 691 744 C ATOM 417 CD PRO A 86 -53.487 -49.706 -18.774 1.00 30.13 C ANISOU 417 CD PRO A 86 2866 4232 4349 -218 755 810 C ATOM 418 N ASN A 87 -52.079 -51.935 -15.993 1.00 29.78 N ANISOU 418 N ASN A 87 2935 4148 4232 -205 912 1014 N ATOM 419 CA ASN A 87 -51.788 -52.651 -14.748 1.00 30.22 C ANISOU 419 CA ASN A 87 3023 4213 4248 -180 992 1111 C ATOM 420 C ASN A 87 -52.272 -54.101 -14.791 1.00 30.99 C ANISOU 420 C ASN A 87 3068 4240 4466 -262 1033 1195 C ATOM 421 O ASN A 87 -51.597 -54.992 -14.268 1.00 31.10 O ANISOU 421 O ASN A 87 3134 4211 4471 -264 1060 1254 O ATOM 422 CB ASN A 87 -52.359 -51.911 -13.530 1.00 30.83 C ANISOU 422 CB ASN A 87 3086 4392 4234 -98 1077 1157 C ATOM 423 CG ASN A 87 -51.578 -50.640 -13.190 1.00 30.66 C ANISOU 423 CG ASN A 87 3144 4428 4077 -7 1043 1081 C ATOM 424 OD1 ASN A 87 -50.449 -50.445 -13.642 1.00 29.73 O ANISOU 424 OD1 ASN A 87 3099 4273 3924 -4 967 1014 O ATOM 425 ND2 ASN A 87 -52.180 -49.775 -12.384 1.00 31.21 N ANISOU 425 ND2 ASN A 87 3199 4587 4075 66 1099 1091 N ATOM 426 N THR A 88 -53.420 -54.339 -15.428 1.00 31.38 N ANISOU 426 N THR A 88 3015 4274 4633 -331 1036 1197 N ATOM 427 CA THR A 88 -53.939 -55.705 -15.601 1.00 32.52 C ANISOU 427 CA THR A 88 3102 4340 4916 -424 1066 1264 C ATOM 428 C THR A 88 -53.066 -56.526 -16.554 1.00 31.99 C ANISOU 428 C THR A 88 3086 4163 4906 -483 983 1214 C ATOM 429 O THR A 88 -52.776 -57.687 -16.286 1.00 32.82 O ANISOU 429 O THR A 88 3212 4193 5066 -521 1014 1278 O ATOM 430 CB THR A 88 -55.392 -55.706 -16.131 1.00 33.36 C ANISOU 430 CB THR A 88 3075 4460 5140 -487 1077 1265 C ATOM 431 OG1 THR A 88 -56.259 -55.110 -15.161 1.00 34.19 O ANISOU 431 OG1 THR A 88 3124 4665 5202 -433 1170 1329 O ATOM 432 CG2 THR A 88 -55.868 -57.127 -16.414 1.00 34.47 C ANISOU 432 CG2 THR A 88 3155 4505 5438 -595 1096 1319 C ATOM 433 N VAL A 89 -52.660 -55.923 -17.667 1.00 30.86 N ANISOU 433 N VAL A 89 2967 4010 4750 -485 882 1101 N ATOM 434 CA VAL A 89 -51.794 -56.600 -18.638 1.00 30.45 C ANISOU 434 CA VAL A 89 2967 3863 4739 -529 800 1043 C ATOM 435 C VAL A 89 -50.429 -56.919 -18.021 1.00 29.59 C ANISOU 435 C VAL A 89 2968 3730 4546 -480 808 1069 C ATOM 436 O VAL A 89 -49.921 -58.036 -18.157 1.00 29.48 O ANISOU 436 O VAL A 89 2987 3628 4587 -518 803 1095 O ATOM 437 CB VAL A 89 -51.614 -55.762 -19.923 1.00 29.56 C ANISOU 437 CB VAL A 89 2860 3760 4611 -526 697 923 C ATOM 438 CG1 VAL A 89 -50.572 -56.392 -20.832 1.00 29.41 C ANISOU 438 CG1 VAL A 89 2910 3654 4612 -553 620 865 C ATOM 439 CG2 VAL A 89 -52.943 -55.628 -20.651 1.00 30.53 C ANISOU 439 CG2 VAL A 89 2871 3899 4828 -579 677 895 C ATOM 440 N HIS A 90 -49.854 -55.937 -17.329 1.00 28.87 N ANISOU 440 N HIS A 90 2931 3717 4322 -392 820 1061 N ATOM 441 CA HIS A 90 -48.595 -56.128 -16.615 1.00 28.60 C ANISOU 441 CA HIS A 90 2992 3680 4196 -335 827 1085 C ATOM 442 C HIS A 90 -48.691 -57.275 -15.602 1.00 29.65 C ANISOU 442 C HIS A 90 3128 3782 4354 -341 915 1207 C ATOM 443 O HIS A 90 -47.769 -58.093 -15.491 1.00 29.76 O ANISOU 443 O HIS A 90 3205 3738 4365 -338 906 1233 O ATOM 444 CB HIS A 90 -48.177 -54.834 -15.908 1.00 27.99 C ANISOU 444 CB HIS A 90 2956 3700 3978 -243 832 1057 C ATOM 445 CG HIS A 90 -46.910 -54.962 -15.124 1.00 27.36 C ANISOU 445 CG HIS A 90 2965 3631 3798 -181 834 1076 C ATOM 446 ND1 HIS A 90 -46.894 -55.287 -13.786 1.00 28.53 N ANISOU 446 ND1 HIS A 90 3133 3823 3884 -129 914 1169 N ATOM 447 CD2 HIS A 90 -45.616 -54.825 -15.495 1.00 26.12 C ANISOU 447 CD2 HIS A 90 2879 3452 3592 -159 766 1016 C ATOM 448 CE1 HIS A 90 -45.643 -55.348 -13.366 1.00 27.48 C ANISOU 448 CE1 HIS A 90 3080 3696 3666 -77 889 1162 C ATOM 449 NE2 HIS A 90 -44.848 -55.062 -14.381 1.00 27.17 N ANISOU 449 NE2 HIS A 90 3069 3618 3637 -97 800 1069 N ATOM 450 N TYR A 91 -49.801 -57.333 -14.866 1.00 30.51 N ANISOU 450 N TYR A 91 3170 3934 4489 -345 1002 1287 N ATOM 451 CA TYR A 91 -50.035 -58.430 -13.927 1.00 31.72 C ANISOU 451 CA TYR A 91 3317 4057 4678 -355 1097 1416 C ATOM 452 C TYR A 91 -49.949 -59.781 -14.634 1.00 31.98 C ANISOU 452 C TYR A 91 3344 3958 4848 -444 1077 1433 C ATOM 453 O TYR A 91 -49.215 -60.675 -14.195 1.00 31.99 O ANISOU 453 O TYR A 91 3407 3903 4844 -432 1101 1495 O ATOM 454 CB TYR A 91 -51.401 -58.295 -13.237 1.00 32.89 C ANISOU 454 CB TYR A 91 3374 4265 4858 -360 1195 1496 C ATOM 455 CG TYR A 91 -51.674 -59.402 -12.238 1.00 34.67 C ANISOU 455 CG TYR A 91 3591 4461 5120 -367 1305 1642 C ATOM 456 CD1 TYR A 91 -51.392 -59.231 -10.886 1.00 35.88 C ANISOU 456 CD1 TYR A 91 3792 4693 5148 -272 1385 1726 C ATOM 457 CD2 TYR A 91 -52.201 -60.627 -12.648 1.00 36.26 C ANISOU 457 CD2 TYR A 91 3741 4555 5483 -468 1329 1695 C ATOM 458 CE1 TYR A 91 -51.630 -60.245 -9.970 1.00 37.33 C ANISOU 458 CE1 TYR A 91 3972 4852 5361 -271 1492 1870 C ATOM 459 CE2 TYR A 91 -52.440 -61.647 -11.740 1.00 37.95 C ANISOU 459 CE2 TYR A 91 3949 4731 5738 -476 1436 1837 C ATOM 460 CZ TYR A 91 -52.153 -61.450 -10.403 1.00 38.53 C ANISOU 460 CZ TYR A 91 4072 4889 5680 -375 1520 1929 C ATOM 461 OH TYR A 91 -52.391 -62.460 -9.502 1.00 40.56 O ANISOU 461 OH TYR A 91 4327 5112 5974 -376 1633 2079 O ATOM 462 N ILE A 92 -50.697 -59.918 -15.726 1.00 31.97 N ANISOU 462 N ILE A 92 3271 3909 4967 -530 1030 1375 N ATOM 463 CA ILE A 92 -50.764 -61.179 -16.466 1.00 32.62 C ANISOU 463 CA ILE A 92 3339 3862 5192 -623 1006 1377 C ATOM 464 C ILE A 92 -49.393 -61.584 -17.017 1.00 31.68 C ANISOU 464 C ILE A 92 3320 3674 5044 -607 932 1321 C ATOM 465 O ILE A 92 -49.044 -62.764 -17.003 1.00 32.10 O ANISOU 465 O ILE A 92 3405 3626 5167 -640 947 1367 O ATOM 466 CB ILE A 92 -51.779 -61.113 -17.629 1.00 32.80 C ANISOU 466 CB ILE A 92 3266 3860 5336 -710 950 1301 C ATOM 467 CG1 ILE A 92 -53.203 -60.917 -17.097 1.00 34.20 C ANISOU 467 CG1 ILE A 92 3330 4096 5570 -737 1029 1367 C ATOM 468 CG2 ILE A 92 -51.730 -62.400 -18.454 1.00 34.04 C ANISOU 468 CG2 ILE A 92 3419 3878 5635 -803 910 1282 C ATOM 469 CD1 ILE A 92 -54.190 -60.457 -18.149 1.00 34.31 C ANISOU 469 CD1 ILE A 92 3245 4129 5663 -795 966 1281 C ATOM 470 N LEU A 93 -48.619 -60.604 -17.485 1.00 30.38 N ANISOU 470 N LEU A 93 3205 3562 4778 -553 856 1225 N ATOM 471 CA LEU A 93 -47.293 -60.871 -18.050 1.00 29.66 C ANISOU 471 CA LEU A 93 3201 3417 4651 -532 786 1168 C ATOM 472 C LEU A 93 -46.247 -61.232 -16.994 1.00 29.90 C ANISOU 472 C LEU A 93 3314 3455 4593 -460 829 1242 C ATOM 473 O LEU A 93 -45.211 -61.814 -17.326 1.00 29.57 O ANISOU 473 O LEU A 93 3338 3350 4547 -449 789 1222 O ATOM 474 CB LEU A 93 -46.799 -59.665 -18.866 1.00 28.34 C ANISOU 474 CB LEU A 93 3054 3306 4406 -498 699 1050 C ATOM 475 CG LEU A 93 -47.430 -59.519 -20.255 1.00 28.34 C ANISOU 475 CG LEU A 93 3000 3276 4490 -563 626 957 C ATOM 476 CD1 LEU A 93 -47.302 -58.089 -20.782 1.00 26.94 C ANISOU 476 CD1 LEU A 93 2825 3182 4230 -519 571 869 C ATOM 477 CD2 LEU A 93 -46.808 -60.513 -21.235 1.00 29.09 C ANISOU 477 CD2 LEU A 93 3134 3262 4656 -606 565 910 C ATOM 478 N THR A 94 -46.512 -60.877 -15.737 1.00 30.35 N ANISOU 478 N THR A 94 3366 3592 4574 -404 908 1324 N ATOM 479 CA THR A 94 -45.563 -61.094 -14.643 1.00 30.59 C ANISOU 479 CA THR A 94 3472 3652 4500 -322 947 1393 C ATOM 480 C THR A 94 -46.023 -62.186 -13.669 1.00 32.27 C ANISOU 480 C THR A 94 3675 3826 4759 -328 1053 1537 C ATOM 481 O THR A 94 -45.387 -62.406 -12.639 1.00 32.88 O ANISOU 481 O THR A 94 3809 3937 4746 -253 1098 1613 O ATOM 482 CB THR A 94 -45.322 -59.790 -13.859 1.00 30.08 C ANISOU 482 CB THR A 94 3425 3719 4284 -232 953 1372 C ATOM 483 OG1 THR A 94 -46.574 -59.278 -13.381 1.00 30.17 O ANISOU 483 OG1 THR A 94 3365 3795 4302 -238 1017 1409 O ATOM 484 CG2 THR A 94 -44.652 -58.757 -14.746 1.00 28.60 C ANISOU 484 CG2 THR A 94 3261 3559 4047 -219 853 1240 C ATOM 485 N HIS A 95 -47.118 -62.864 -14.001 1.00 33.40 N ANISOU 485 N HIS A 95 3746 3900 5044 -417 1091 1575 N ATOM 486 CA HIS A 95 -47.599 -64.008 -13.224 1.00 35.13 C ANISOU 486 CA HIS A 95 3950 4059 5338 -440 1194 1715 C ATOM 487 C HIS A 95 -47.835 -65.190 -14.162 1.00 36.09 C ANISOU 487 C HIS A 95 4051 4029 5632 -545 1170 1705 C ATOM 488 O HIS A 95 -47.564 -65.090 -15.357 1.00 35.15 O ANISOU 488 O HIS A 95 3936 3865 5556 -587 1072 1587 O ATOM 489 CB HIS A 95 -48.880 -63.633 -12.479 1.00 35.87 C ANISOU 489 CB HIS A 95 3959 4228 5440 -446 1288 1791 C ATOM 490 CG HIS A 95 -48.666 -62.644 -11.377 1.00 35.72 C ANISOU 490 CG HIS A 95 3970 4351 5251 -335 1328 1818 C ATOM 491 ND1 HIS A 95 -48.528 -61.292 -11.607 1.00 34.65 N ANISOU 491 ND1 HIS A 95 3836 4313 5016 -290 1266 1712 N ATOM 492 CD2 HIS A 95 -48.565 -62.810 -10.037 1.00 36.74 C ANISOU 492 CD2 HIS A 95 4131 4539 5288 -255 1422 1936 C ATOM 493 CE1 HIS A 95 -48.354 -60.668 -10.456 1.00 35.44 C ANISOU 493 CE1 HIS A 95 3967 4524 4975 -191 1317 1756 C ATOM 494 NE2 HIS A 95 -48.374 -61.565 -9.487 1.00 36.46 N ANISOU 494 NE2 HIS A 95 4115 4637 5100 -165 1411 1891 N ATOM 495 N PHE A 96 -48.322 -66.305 -13.619 1.00 38.14 N ANISOU 495 N PHE A 96 4293 4209 5990 -585 1260 1826 N ATOM 496 CA PHE A 96 -48.664 -67.491 -14.414 1.00 39.49 C ANISOU 496 CA PHE A 96 4438 4224 6341 -692 1247 1823 C ATOM 497 C PHE A 96 -47.463 -68.014 -15.206 1.00 39.30 C ANISOU 497 C PHE A 96 4502 4109 6319 -683 1159 1747 C ATOM 498 O PHE A 96 -47.583 -68.343 -16.388 1.00 39.09 O ANISOU 498 O PHE A 96 4458 3998 6397 -759 1083 1650 O ATOM 499 CB PHE A 96 -49.832 -67.192 -15.366 1.00 39.57 C ANISOU 499 CB PHE A 96 4340 4226 6469 -793 1205 1740 C ATOM 500 CG PHE A 96 -50.974 -66.458 -14.719 1.00 40.33 C ANISOU 500 CG PHE A 96 4343 4431 6548 -792 1276 1792 C ATOM 501 CD1 PHE A 96 -51.237 -65.133 -15.042 1.00 39.47 C ANISOU 501 CD1 PHE A 96 4200 4442 6356 -761 1224 1700 C ATOM 502 CD2 PHE A 96 -51.783 -67.091 -13.785 1.00 42.37 C ANISOU 502 CD2 PHE A 96 4550 4672 6875 -817 1401 1936 C ATOM 503 CE1 PHE A 96 -52.283 -64.449 -14.445 1.00 40.18 C ANISOU 503 CE1 PHE A 96 4206 4633 6428 -751 1292 1746 C ATOM 504 CE2 PHE A 96 -52.838 -66.415 -13.185 1.00 42.73 C ANISOU 504 CE2 PHE A 96 4507 4824 6903 -809 1473 1986 C ATOM 505 CZ PHE A 96 -53.088 -65.091 -13.515 1.00 41.79 C ANISOU 505 CZ PHE A 96 4355 4826 6698 -774 1416 1888 C ATOM 506 N LYS A 97 -46.311 -68.093 -14.545 1.00 39.55 N ANISOU 506 N LYS A 97 4627 4165 6234 -586 1170 1790 N ATOM 507 CA LYS A 97 -45.060 -68.493 -15.196 1.00 39.52 C ANISOU 507 CA LYS A 97 4708 4096 6211 -558 1091 1723 C ATOM 508 C LYS A 97 -45.182 -69.834 -15.933 1.00 40.43 C ANISOU 508 C LYS A 97 4829 4035 6495 -643 1081 1721 C ATOM 509 O LYS A 97 -44.632 -69.996 -17.021 1.00 39.92 O ANISOU 509 O LYS A 97 4796 3911 6462 -663 990 1611 O ATOM 510 CB LYS A 97 -43.921 -68.565 -14.173 1.00 39.73 C ANISOU 510 CB LYS A 97 4824 4172 6102 -440 1123 1799 C ATOM 511 CG LYS A 97 -42.531 -68.465 -14.779 1.00 39.95 C ANISOU 511 CG LYS A 97 4928 4192 6059 -386 1030 1709 C ATOM 512 CD LYS A 97 -41.492 -69.095 -13.869 1.00 42.85 C ANISOU 512 CD LYS A 97 5377 4552 6350 -292 1070 1805 C ATOM 513 CE LYS A 97 -40.090 -68.859 -14.387 1.00 42.68 C ANISOU 513 CE LYS A 97 5421 4547 6247 -229 979 1716 C ATOM 514 NZ LYS A 97 -39.651 -67.460 -14.176 1.00 42.84 N ANISOU 514 NZ LYS A 97 5437 4720 6119 -168 933 1647 N ATOM 515 N GLY A 98 -45.908 -70.780 -15.339 1.00 41.91 N ANISOU 515 N GLY A 98 4989 4142 6794 -691 1177 1842 N ATOM 516 CA GLY A 98 -46.104 -72.106 -15.929 1.00 42.97 C ANISOU 516 CA GLY A 98 5127 4096 7104 -778 1179 1850 C ATOM 517 C GLY A 98 -46.828 -72.071 -17.263 1.00 42.75 C ANISOU 517 C GLY A 98 5031 4012 7200 -888 1095 1717 C ATOM 518 O GLY A 98 -46.464 -72.794 -18.193 1.00 42.89 O ANISOU 518 O GLY A 98 5083 3909 7304 -929 1030 1641 O ATOM 519 N VAL A 99 -47.854 -71.229 -17.357 1.00 42.44 N ANISOU 519 N VAL A 99 4895 4065 7167 -930 1093 1686 N ATOM 520 CA VAL A 99 -48.562 -71.017 -18.619 1.00 42.15 C ANISOU 520 CA VAL A 99 4786 4004 7225 -1022 1004 1553 C ATOM 521 C VAL A 99 -47.649 -70.359 -19.661 1.00 40.46 C ANISOU 521 C VAL A 99 4627 3829 6917 -976 882 1404 C ATOM 522 O VAL A 99 -47.640 -70.764 -20.824 1.00 40.38 O ANISOU 522 O VAL A 99 4618 3736 6990 -1033 798 1296 O ATOM 523 CB VAL A 99 -49.818 -70.139 -18.434 1.00 42.25 C ANISOU 523 CB VAL A 99 4682 4126 7245 -1058 1031 1557 C ATOM 524 CG1 VAL A 99 -50.517 -69.928 -19.768 1.00 42.55 C ANISOU 524 CG1 VAL A 99 4646 4145 7375 -1145 930 1417 C ATOM 525 CG2 VAL A 99 -50.775 -70.770 -17.427 1.00 44.04 C ANISOU 525 CG2 VAL A 99 4843 4319 7569 -1106 1159 1709 C ATOM 526 N TRP A 100 -46.889 -69.347 -19.249 1.00 39.06 N ANISOU 526 N TRP A 100 4495 3778 6568 -874 871 1397 N ATOM 527 CA TRP A 100 -45.969 -68.668 -20.166 1.00 37.47 C ANISOU 527 CA TRP A 100 4345 3619 6273 -827 766 1269 C ATOM 528 C TRP A 100 -44.876 -69.604 -20.670 1.00 37.89 C ANISOU 528 C TRP A 100 4488 3560 6349 -808 726 1239 C ATOM 529 O TRP A 100 -44.462 -69.510 -21.821 1.00 37.04 O ANISOU 529 O TRP A 100 4401 3428 6243 -816 634 1119 O ATOM 530 CB TRP A 100 -45.334 -67.438 -19.511 1.00 36.15 C ANISOU 530 CB TRP A 100 4207 3600 5927 -724 771 1276 C ATOM 531 CG TRP A 100 -46.290 -66.298 -19.353 1.00 34.75 C ANISOU 531 CG TRP A 100 3950 3540 5714 -732 781 1261 C ATOM 532 CD1 TRP A 100 -46.753 -65.781 -18.185 1.00 34.57 C ANISOU 532 CD1 TRP A 100 3897 3609 5628 -694 864 1353 C ATOM 533 CD2 TRP A 100 -46.908 -65.546 -20.401 1.00 33.65 C ANISOU 533 CD2 TRP A 100 3750 3439 5597 -774 707 1149 C ATOM 534 NE1 TRP A 100 -47.620 -64.744 -18.433 1.00 34.11 N ANISOU 534 NE1 TRP A 100 3764 3641 5555 -710 847 1303 N ATOM 535 CE2 TRP A 100 -47.734 -64.579 -19.788 1.00 33.20 C ANISOU 535 CE2 TRP A 100 3627 3495 5492 -759 751 1180 C ATOM 536 CE3 TRP A 100 -46.840 -65.590 -21.800 1.00 32.51 C ANISOU 536 CE3 TRP A 100 3603 3248 5501 -816 608 1025 C ATOM 537 CZ2 TRP A 100 -48.489 -63.666 -20.524 1.00 32.62 C ANISOU 537 CZ2 TRP A 100 3486 3486 5424 -783 699 1096 C ATOM 538 CZ3 TRP A 100 -47.593 -64.684 -22.530 1.00 31.53 C ANISOU 538 CZ3 TRP A 100 3411 3193 5377 -840 556 943 C ATOM 539 CH2 TRP A 100 -48.404 -63.732 -21.890 1.00 31.88 C ANISOU 539 CH2 TRP A 100 3390 3346 5377 -823 602 980 C ATOM 540 N ASN A 101 -44.419 -70.507 -19.807 1.00 39.11 N ANISOU 540 N ASN A 101 4697 3648 6517 -778 798 1352 N ATOM 541 CA ASN A 101 -43.403 -71.484 -20.188 1.00 39.81 C ANISOU 541 CA ASN A 101 4872 3622 6633 -754 771 1338 C ATOM 542 C ASN A 101 -43.887 -72.353 -21.353 1.00 40.32 C ANISOU 542 C ASN A 101 4918 3545 6858 -852 718 1253 C ATOM 543 O ASN A 101 -43.110 -72.690 -22.250 1.00 40.07 O ANISOU 543 O ASN A 101 4943 3453 6827 -836 646 1163 O ATOM 544 CB ASN A 101 -43.019 -72.364 -18.992 1.00 41.26 C ANISOU 544 CB ASN A 101 5107 3751 6817 -708 869 1490 C ATOM 545 CG ASN A 101 -41.523 -72.488 -18.816 1.00 42.25 C ANISOU 545 CG ASN A 101 5331 3888 6834 -600 847 1494 C ATOM 546 OD1 ASN A 101 -40.964 -73.579 -18.924 1.00 46.57 O ANISOU 546 OD1 ASN A 101 5939 4312 7441 -590 855 1521 O ATOM 547 ND2 ASN A 101 -40.863 -71.365 -18.540 1.00 43.18 N ANISOU 547 ND2 ASN A 101 5462 4151 6792 -518 818 1465 N ATOM 548 N ILE A 102 -45.173 -72.702 -21.335 1.00 40.96 N ANISOU 548 N ILE A 102 4915 3576 7073 -953 752 1279 N ATOM 549 CA ILE A 102 -45.799 -73.430 -22.436 1.00 41.69 C ANISOU 549 CA ILE A 102 4973 3545 7324 -1057 694 1187 C ATOM 550 C ILE A 102 -45.892 -72.526 -23.666 1.00 40.15 C ANISOU 550 C ILE A 102 4748 3426 7082 -1066 580 1028 C ATOM 551 O ILE A 102 -45.490 -72.917 -24.764 1.00 39.76 O ANISOU 551 O ILE A 102 4736 3306 7065 -1078 497 915 O ATOM 552 CB ILE A 102 -47.218 -73.935 -22.064 1.00 43.26 C ANISOU 552 CB ILE A 102 5072 3685 7681 -1168 760 1255 C ATOM 553 CG1 ILE A 102 -47.161 -74.959 -20.922 1.00 45.26 C ANISOU 553 CG1 ILE A 102 5357 3842 7998 -1166 879 1420 C ATOM 554 CG2 ILE A 102 -47.908 -74.547 -23.278 1.00 44.32 C ANISOU 554 CG2 ILE A 102 5158 3707 7974 -1280 682 1137 C ATOM 555 CD1 ILE A 102 -46.577 -76.308 -21.313 1.00 47.13 C ANISOU 555 CD1 ILE A 102 5673 3894 8342 -1185 868 1412 C ATOM 556 N VAL A 103 -46.415 -71.316 -23.468 1.00 38.88 N ANISOU 556 N VAL A 103 4523 3410 6839 -1052 580 1021 N ATOM 557 CA VAL A 103 -46.576 -70.346 -24.550 1.00 37.60 C ANISOU 557 CA VAL A 103 4329 3333 6625 -1052 482 886 C ATOM 558 C VAL A 103 -45.252 -70.071 -25.267 1.00 36.13 C ANISOU 558 C VAL A 103 4235 3163 6330 -972 409 800 C ATOM 559 O VAL A 103 -45.202 -70.053 -26.496 1.00 35.67 O ANISOU 559 O VAL A 103 4180 3083 6289 -991 318 677 O ATOM 560 CB VAL A 103 -47.155 -69.003 -24.032 1.00 36.85 C ANISOU 560 CB VAL A 103 4167 3397 6437 -1025 507 912 C ATOM 561 CG1 VAL A 103 -47.197 -67.969 -25.149 1.00 36.09 C ANISOU 561 CG1 VAL A 103 4050 3387 6276 -1011 408 779 C ATOM 562 CG2 VAL A 103 -48.546 -69.208 -23.445 1.00 38.16 C ANISOU 562 CG2 VAL A 103 4228 3559 6713 -1105 576 987 C ATOM 563 N ASN A 104 -44.187 -69.877 -24.491 1.00 35.29 N ANISOU 563 N ASN A 104 4200 3098 6111 -881 449 867 N ATOM 564 CA ASN A 104 -42.860 -69.590 -25.042 1.00 34.25 C ANISOU 564 CA ASN A 104 4149 2990 5873 -800 391 800 C ATOM 565 C ASN A 104 -42.304 -70.699 -25.942 1.00 35.22 C ANISOU 565 C ASN A 104 4333 2978 6070 -813 342 734 C ATOM 566 O ASN A 104 -41.466 -70.431 -26.806 1.00 34.48 O ANISOU 566 O ASN A 104 4286 2903 5911 -765 275 644 O ATOM 567 CB ASN A 104 -41.859 -69.296 -23.916 1.00 33.48 C ANISOU 567 CB ASN A 104 4109 2957 5655 -704 447 893 C ATOM 568 CG ASN A 104 -42.177 -68.014 -23.162 1.00 32.45 C ANISOU 568 CG ASN A 104 3934 2973 5420 -671 478 929 C ATOM 569 OD1 ASN A 104 -42.827 -67.109 -23.689 1.00 31.20 O ANISOU 569 OD1 ASN A 104 3719 2887 5248 -696 440 863 O ATOM 570 ND2 ASN A 104 -41.711 -67.930 -21.924 1.00 31.42 N ANISOU 570 ND2 ASN A 104 3834 2891 5214 -607 545 1032 N ATOM 571 N ASN A 105 -42.758 -71.933 -25.732 1.00 37.14 N ANISOU 571 N ASN A 105 4575 3085 6451 -875 380 781 N ATOM 572 CA ASN A 105 -42.295 -73.078 -26.520 1.00 38.25 C ANISOU 572 CA ASN A 105 4777 3081 6676 -890 339 721 C ATOM 573 C ASN A 105 -43.252 -73.480 -27.647 1.00 38.95 C ANISOU 573 C ASN A 105 4814 3094 6892 -989 270 608 C ATOM 574 O ASN A 105 -43.086 -74.541 -28.249 1.00 39.94 O ANISOU 574 O ASN A 105 4981 3082 7112 -1018 240 557 O ATOM 575 CB ASN A 105 -42.030 -74.276 -25.600 1.00 39.84 C ANISOU 575 CB ASN A 105 5026 3161 6952 -886 423 842 C ATOM 576 CG ASN A 105 -40.886 -74.026 -24.637 1.00 40.32 C ANISOU 576 CG ASN A 105 5152 3289 6881 -774 474 935 C ATOM 577 OD1 ASN A 105 -39.790 -73.631 -25.038 1.00 42.09 O ANISOU 577 OD1 ASN A 105 5431 3565 6998 -693 427 881 O ATOM 578 ND2 ASN A 105 -41.136 -74.253 -23.356 1.00 43.60 N ANISOU 578 ND2 ASN A 105 5557 3706 7302 -766 570 1079 N ATOM 579 N ILE A 105A -44.249 -72.639 -27.924 1.00 38.44 N ANISOU 579 N ILE A 105A 4659 3119 6827 -1037 242 567 N ATOM 580 CA ILE A 105A -45.127 -72.818 -29.080 1.00 39.03 C ANISOU 580 CA ILE A 105A 4678 3155 6998 -1120 160 444 C ATOM 581 C ILE A 105A -44.873 -71.645 -30.030 1.00 37.75 C ANISOU 581 C ILE A 105A 4511 3120 6710 -1068 75 335 C ATOM 582 O ILE A 105A -45.434 -70.564 -29.837 1.00 36.89 O ANISOU 582 O ILE A 105A 4338 3136 6542 -1065 79 346 O ATOM 583 CB ILE A 105A -46.609 -72.852 -28.674 1.00 39.96 C ANISOU 583 CB ILE A 105A 4679 3270 7233 -1223 195 487 C ATOM 584 CG1 ILE A 105A -46.878 -74.020 -27.722 1.00 41.52 C ANISOU 584 CG1 ILE A 105A 4877 3335 7561 -1277 289 608 C ATOM 585 CG2 ILE A 105A -47.500 -72.983 -29.906 1.00 40.53 C ANISOU 585 CG2 ILE A 105A 4687 3315 7399 -1304 97 350 C ATOM 586 CD1 ILE A 105A -48.287 -74.029 -27.157 1.00 43.28 C ANISOU 586 CD1 ILE A 105A 4982 3565 7899 -1373 343 674 C ATOM 587 N PRO A 106 -44.013 -71.847 -31.047 1.00 37.62 N ANISOU 587 N PRO A 106 4569 3075 6650 -1021 4 233 N ATOM 588 CA PRO A 106 -43.569 -70.740 -31.909 1.00 36.37 C ANISOU 588 CA PRO A 106 4423 3038 6359 -956 -64 145 C ATOM 589 C PRO A 106 -44.690 -69.878 -32.496 1.00 36.43 C ANISOU 589 C PRO A 106 4336 3137 6367 -999 -116 80 C ATOM 590 O PRO A 106 -44.581 -68.651 -32.493 1.00 35.47 O ANISOU 590 O PRO A 106 4199 3147 6133 -948 -121 82 O ATOM 591 CB PRO A 106 -42.804 -71.455 -33.023 1.00 36.64 C ANISOU 591 CB PRO A 106 4535 2991 6397 -927 -132 38 C ATOM 592 CG PRO A 106 -42.267 -72.674 -32.365 1.00 37.62 C ANISOU 592 CG PRO A 106 4719 2979 6594 -928 -75 108 C ATOM 593 CD PRO A 106 -43.340 -73.111 -31.406 1.00 38.46 C ANISOU 593 CD PRO A 106 4756 3033 6823 -1017 -9 203 C ATOM 594 N PHE A 107 -45.758 -70.508 -32.980 1.00 37.57 N ANISOU 594 N PHE A 107 4419 3213 6644 -1092 -156 24 N ATOM 595 CA PHE A 107 -46.887 -69.768 -33.560 1.00 37.97 C ANISOU 595 CA PHE A 107 4372 3350 6704 -1134 -212 -39 C ATOM 596 C PHE A 107 -47.475 -68.754 -32.571 1.00 36.96 C ANISOU 596 C PHE A 107 4172 3336 6534 -1131 -144 60 C ATOM 597 O PHE A 107 -47.764 -67.612 -32.936 1.00 36.14 O ANISOU 597 O PHE A 107 4030 3354 6345 -1097 -177 27 O ATOM 598 CB PHE A 107 -47.979 -70.734 -34.040 1.00 39.81 C ANISOU 598 CB PHE A 107 4539 3481 7106 -1246 -257 -102 C ATOM 599 CG PHE A 107 -49.303 -70.071 -34.299 1.00 41.78 C ANISOU 599 CG PHE A 107 4665 3818 7391 -1301 -293 -135 C ATOM 600 CD1 PHE A 107 -49.487 -69.276 -35.424 1.00 43.19 C ANISOU 600 CD1 PHE A 107 4826 4095 7491 -1266 -389 -246 C ATOM 601 CD2 PHE A 107 -50.359 -70.227 -33.412 1.00 43.99 C ANISOU 601 CD2 PHE A 107 4847 4089 7780 -1382 -229 -48 C ATOM 602 CE1 PHE A 107 -50.710 -68.653 -35.666 1.00 44.54 C ANISOU 602 CE1 PHE A 107 4881 4352 7691 -1309 -424 -274 C ATOM 603 CE2 PHE A 107 -51.585 -69.611 -33.646 1.00 45.08 C ANISOU 603 CE2 PHE A 107 4864 4312 7950 -1428 -261 -76 C ATOM 604 CZ PHE A 107 -51.761 -68.824 -34.776 1.00 44.88 C ANISOU 604 CZ PHE A 107 4822 4385 7847 -1391 -362 -191 C ATOM 605 N LEU A 108 -47.633 -69.181 -31.320 1.00 36.86 N ANISOU 605 N LEU A 108 4146 3282 6576 -1158 -47 185 N ATOM 606 CA LEU A 108 -48.225 -68.347 -30.275 1.00 36.23 C ANISOU 606 CA LEU A 108 4001 3302 6463 -1154 28 286 C ATOM 607 C LEU A 108 -47.254 -67.261 -29.789 1.00 34.06 C ANISOU 607 C LEU A 108 3785 3138 6020 -1047 57 327 C ATOM 608 O LEU A 108 -47.660 -66.120 -29.560 1.00 33.28 O ANISOU 608 O LEU A 108 3639 3157 5850 -1020 67 341 O ATOM 609 CB LEU A 108 -48.680 -69.231 -29.109 1.00 37.57 C ANISOU 609 CB LEU A 108 4142 3389 6744 -1213 126 408 C ATOM 610 CG LEU A 108 -49.695 -68.689 -28.103 1.00 39.02 C ANISOU 610 CG LEU A 108 4230 3650 6947 -1240 205 508 C ATOM 611 CD1 LEU A 108 -50.731 -67.776 -28.754 1.00 40.01 C ANISOU 611 CD1 LEU A 108 4255 3878 7070 -1265 147 435 C ATOM 612 CD2 LEU A 108 -50.377 -69.857 -27.392 1.00 41.18 C ANISOU 612 CD2 LEU A 108 4459 3808 7380 -1329 280 598 C ATOM 613 N ARG A 109 -45.981 -67.617 -29.632 1.00 32.81 N ANISOU 613 N ARG A 109 3727 2937 5803 -986 71 345 N ATOM 614 CA ARG A 109 -44.942 -66.641 -29.295 1.00 31.17 C ANISOU 614 CA ARG A 109 3576 2826 5441 -887 86 368 C ATOM 615 C ARG A 109 -44.865 -65.541 -30.362 1.00 29.95 C ANISOU 615 C ARG A 109 3415 2766 5199 -849 9 267 C ATOM 616 O ARG A 109 -44.777 -64.353 -30.041 1.00 28.60 O ANISOU 616 O ARG A 109 3232 2704 4929 -801 24 287 O ATOM 617 CB ARG A 109 -43.579 -67.326 -29.143 1.00 30.99 C ANISOU 617 CB ARG A 109 3655 2736 5383 -832 99 387 C ATOM 618 CG ARG A 109 -42.431 -66.371 -28.821 1.00 29.95 C ANISOU 618 CG ARG A 109 3577 2701 5101 -734 109 405 C ATOM 619 CD ARG A 109 -41.195 -67.117 -28.348 1.00 30.56 C ANISOU 619 CD ARG A 109 3739 2718 5154 -681 140 454 C ATOM 620 NE ARG A 109 -40.069 -66.215 -28.097 1.00 29.14 N ANISOU 620 NE ARG A 109 3602 2631 4838 -593 142 461 N ATOM 621 CZ ARG A 109 -38.860 -66.313 -28.654 1.00 29.70 C ANISOU 621 CZ ARG A 109 3739 2693 4853 -533 108 417 C ATOM 622 NH1 ARG A 109 -38.569 -67.287 -29.516 1.00 30.67 N ANISOU 622 NH1 ARG A 109 3902 2717 5035 -543 70 359 N ATOM 623 NH2 ARG A 109 -37.921 -65.429 -28.340 1.00 29.00 N ANISOU 623 NH2 ARG A 109 3674 2694 4650 -463 113 429 N ATOM 624 N SER A 110 -44.907 -65.951 -31.627 1.00 29.94 N ANISOU 624 N SER A 110 3424 2719 5234 -869 -73 159 N ATOM 625 CA SER A 110 -44.922 -65.008 -32.743 1.00 29.24 C ANISOU 625 CA SER A 110 3328 2714 5068 -834 -148 64 C ATOM 626 C SER A 110 -46.153 -64.107 -32.708 1.00 29.01 C ANISOU 626 C SER A 110 3202 2776 5046 -862 -154 63 C ATOM 627 O SER A 110 -46.034 -62.891 -32.869 1.00 27.88 O ANISOU 627 O SER A 110 3054 2736 4802 -807 -163 54 O ATOM 628 CB SER A 110 -44.862 -65.754 -34.077 1.00 30.02 C ANISOU 628 CB SER A 110 3452 2742 5210 -851 -235 -53 C ATOM 629 OG SER A 110 -43.573 -66.300 -34.285 1.00 30.59 O ANISOU 629 OG SER A 110 3621 2758 5243 -798 -236 -65 O ATOM 630 N LEU A 111 -47.324 -64.711 -32.493 1.00 29.90 N ANISOU 630 N LEU A 111 3234 2845 5282 -948 -146 77 N ATOM 631 CA LEU A 111 -48.591 -63.969 -32.440 1.00 30.15 C ANISOU 631 CA LEU A 111 3161 2960 5336 -980 -150 79 C ATOM 632 C LEU A 111 -48.565 -62.875 -31.367 1.00 29.10 C ANISOU 632 C LEU A 111 3015 2926 5117 -929 -74 171 C ATOM 633 O LEU A 111 -48.953 -61.729 -31.617 1.00 28.17 O ANISOU 633 O LEU A 111 2861 2911 4933 -894 -93 149 O ATOM 634 CB LEU A 111 -49.756 -64.925 -32.175 1.00 31.86 C ANISOU 634 CB LEU A 111 3290 3104 5712 -1085 -136 98 C ATOM 635 CG LEU A 111 -51.171 -64.356 -32.308 1.00 33.27 C ANISOU 635 CG LEU A 111 3344 3359 5938 -1129 -154 84 C ATOM 636 CD1 LEU A 111 -51.428 -63.873 -33.730 1.00 33.98 C ANISOU 636 CD1 LEU A 111 3416 3501 5992 -1111 -267 -43 C ATOM 637 CD2 LEU A 111 -52.188 -65.409 -31.905 1.00 35.83 C ANISOU 637 CD2 LEU A 111 3583 3599 6432 -1239 -125 117 C ATOM 638 N ILE A 112 -48.095 -63.236 -30.178 1.00 28.81 N ANISOU 638 N ILE A 112 3011 2857 5077 -921 11 270 N ATOM 639 CA ILE A 112 -48.052 -62.309 -29.046 1.00 28.10 C ANISOU 639 CA ILE A 112 2915 2855 4906 -872 85 357 C ATOM 640 C ILE A 112 -46.989 -61.221 -29.235 1.00 26.59 C ANISOU 640 C ILE A 112 2794 2739 4571 -780 66 330 C ATOM 641 O ILE A 112 -47.251 -60.043 -28.966 1.00 25.85 O ANISOU 641 O ILE A 112 2673 2741 4406 -741 81 341 O ATOM 642 CB ILE A 112 -47.835 -63.063 -27.710 1.00 28.50 C ANISOU 642 CB ILE A 112 2985 2855 4989 -882 180 473 C ATOM 643 CG1 ILE A 112 -49.030 -63.982 -27.425 1.00 30.74 C ANISOU 643 CG1 ILE A 112 3185 3074 5422 -977 214 514 C ATOM 644 CG2 ILE A 112 -47.655 -62.081 -26.564 1.00 27.69 C ANISOU 644 CG2 ILE A 112 2888 2849 4783 -819 250 551 C ATOM 645 CD1 ILE A 112 -48.751 -65.058 -26.387 1.00 32.39 C ANISOU 645 CD1 ILE A 112 3425 3195 5687 -997 297 620 C ATOM 646 N MET A 113 -45.802 -61.596 -29.714 1.00 26.01 N ANISOU 646 N MET A 113 2805 2619 4459 -746 35 295 N ATOM 647 CA MET A 113 -44.763 -60.605 -29.967 1.00 24.94 C ANISOU 647 CA MET A 113 2729 2547 4199 -666 17 268 C ATOM 648 C MET A 113 -45.194 -59.653 -31.076 1.00 24.81 C ANISOU 648 C MET A 113 2683 2597 4146 -651 -48 186 C ATOM 649 O MET A 113 -44.939 -58.458 -30.992 1.00 23.52 O ANISOU 649 O MET A 113 2528 2514 3894 -597 -42 188 O ATOM 650 CB MET A 113 -43.425 -61.255 -30.332 1.00 24.44 C ANISOU 650 CB MET A 113 2755 2422 4109 -633 -3 245 C ATOM 651 CG MET A 113 -42.258 -60.259 -30.383 1.00 23.64 C ANISOU 651 CG MET A 113 2710 2387 3886 -553 -7 235 C ATOM 652 SD MET A 113 -41.875 -59.590 -28.754 1.00 23.84 S ANISOU 652 SD MET A 113 2742 2474 3841 -513 74 333 S ATOM 653 CE MET A 113 -40.985 -58.088 -29.195 1.00 21.69 C ANISOU 653 CE MET A 113 2503 2291 3449 -441 47 288 C ATOM 654 N LYS A 114 -45.855 -60.180 -32.105 1.00 25.94 N ANISOU 654 N LYS A 114 2792 2705 4358 -695 -111 115 N ATOM 655 CA LYS A 114 -46.376 -59.329 -33.177 1.00 26.25 C ANISOU 655 CA LYS A 114 2799 2813 4364 -677 -176 41 C ATOM 656 C LYS A 114 -47.308 -58.258 -32.605 1.00 26.30 C ANISOU 656 C LYS A 114 2734 2909 4352 -670 -143 81 C ATOM 657 O LYS A 114 -47.199 -57.074 -32.957 1.00 25.70 O ANISOU 657 O LYS A 114 2664 2909 4192 -614 -158 62 O ATOM 658 CB LYS A 114 -47.109 -60.161 -34.232 1.00 27.39 C ANISOU 658 CB LYS A 114 2905 2908 4594 -733 -250 -41 C ATOM 659 CG LYS A 114 -47.537 -59.351 -35.459 1.00 28.57 C ANISOU 659 CG LYS A 114 3030 3131 4695 -701 -327 -123 C ATOM 660 CD LYS A 114 -48.379 -60.151 -36.446 1.00 31.99 C ANISOU 660 CD LYS A 114 3414 3527 5213 -757 -408 -210 C ATOM 661 CE LYS A 114 -47.621 -61.321 -37.055 1.00 33.59 C ANISOU 661 CE LYS A 114 3687 3630 5445 -769 -446 -268 C ATOM 662 NZ LYS A 114 -47.805 -62.570 -36.269 1.00 36.93 N ANISOU 662 NZ LYS A 114 4098 3945 5989 -846 -406 -226 N ATOM 663 N TYR A 115 -48.211 -58.674 -31.719 1.00 27.09 N ANISOU 663 N TYR A 115 2767 2996 4530 -724 -93 141 N ATOM 664 CA TYR A 115 -49.163 -57.751 -31.101 1.00 27.51 C ANISOU 664 CA TYR A 115 2746 3133 4573 -717 -54 184 C ATOM 665 C TYR A 115 -48.468 -56.731 -30.194 1.00 26.06 C ANISOU 665 C TYR A 115 2610 3008 4283 -647 5 239 C ATOM 666 O TYR A 115 -48.879 -55.567 -30.154 1.00 25.61 O ANISOU 666 O TYR A 115 2525 3032 4173 -606 10 237 O ATOM 667 CB TYR A 115 -50.268 -58.501 -30.337 1.00 29.10 C ANISOU 667 CB TYR A 115 2862 3308 4888 -792 -6 242 C ATOM 668 CG TYR A 115 -51.172 -57.561 -29.568 1.00 31.37 C ANISOU 668 CG TYR A 115 3078 3686 5157 -774 48 296 C ATOM 669 CD1 TYR A 115 -52.183 -56.851 -30.212 1.00 34.41 C ANISOU 669 CD1 TYR A 115 3383 4140 5551 -772 5 252 C ATOM 670 CD2 TYR A 115 -50.980 -57.340 -28.206 1.00 33.57 C ANISOU 670 CD2 TYR A 115 3371 3987 5399 -748 140 389 C ATOM 671 CE1 TYR A 115 -53.001 -55.964 -29.506 1.00 36.09 C ANISOU 671 CE1 TYR A 115 3531 4438 5745 -746 58 301 C ATOM 672 CE2 TYR A 115 -51.783 -56.456 -27.499 1.00 35.57 C ANISOU 672 CE2 TYR A 115 3564 4325 5627 -722 192 434 C ATOM 673 CZ TYR A 115 -52.791 -55.774 -28.150 1.00 36.53 C ANISOU 673 CZ TYR A 115 3606 4510 5765 -722 152 390 C ATOM 674 OH TYR A 115 -53.584 -54.901 -27.433 1.00 40.11 O ANISOU 674 OH TYR A 115 4000 5048 6194 -689 207 435 O ATOM 675 N VAL A 116 -47.423 -57.156 -29.478 1.00 24.94 N ANISOU 675 N VAL A 116 2539 2825 4112 -629 46 284 N ATOM 676 CA VAL A 116 -46.620 -56.226 -28.678 1.00 23.92 C ANISOU 676 CA VAL A 116 2460 2748 3879 -562 90 321 C ATOM 677 C VAL A 116 -46.016 -55.143 -29.573 1.00 22.89 C ANISOU 677 C VAL A 116 2369 2662 3665 -506 40 257 C ATOM 678 O VAL A 116 -46.119 -53.958 -29.272 1.00 22.23 O ANISOU 678 O VAL A 116 2280 2647 3520 -462 58 265 O ATOM 679 CB VAL A 116 -45.484 -56.936 -27.906 1.00 23.79 C ANISOU 679 CB VAL A 116 2515 2681 3842 -549 128 370 C ATOM 680 CG1 VAL A 116 -44.542 -55.909 -27.273 1.00 23.13 C ANISOU 680 CG1 VAL A 116 2484 2656 3647 -478 153 386 C ATOM 681 CG2 VAL A 116 -46.058 -57.864 -26.841 1.00 24.50 C ANISOU 681 CG2 VAL A 116 2572 2735 4002 -592 194 453 C ATOM 682 N LEU A 117 -45.416 -55.548 -30.686 1.00 22.53 N ANISOU 682 N LEU A 117 2363 2577 3621 -505 -20 196 N ATOM 683 CA LEU A 117 -44.792 -54.584 -31.597 1.00 22.04 C ANISOU 683 CA LEU A 117 2340 2553 3481 -450 -61 142 C ATOM 684 C LEU A 117 -45.803 -53.614 -32.216 1.00 22.69 C ANISOU 684 C LEU A 117 2367 2701 3554 -437 -90 111 C ATOM 685 O LEU A 117 -45.572 -52.400 -32.231 1.00 22.31 O ANISOU 685 O LEU A 117 2334 2706 3436 -384 -81 111 O ATOM 686 CB LEU A 117 -44.030 -55.305 -32.712 1.00 21.72 C ANISOU 686 CB LEU A 117 2350 2460 3443 -449 -117 83 C ATOM 687 CG LEU A 117 -42.828 -56.153 -32.300 1.00 21.28 C ANISOU 687 CG LEU A 117 2359 2343 3383 -444 -96 106 C ATOM 688 CD1 LEU A 117 -42.288 -56.875 -33.528 1.00 20.71 C ANISOU 688 CD1 LEU A 117 2328 2221 3320 -441 -154 39 C ATOM 689 CD2 LEU A 117 -41.744 -55.312 -31.629 1.00 20.88 C ANISOU 689 CD2 LEU A 117 2355 2330 3248 -390 -58 140 C ATOM 690 N THR A 118 -46.914 -54.144 -32.718 1.00 23.98 N ANISOU 690 N THR A 118 2464 2858 3791 -483 -125 84 N ATOM 691 CA THR A 118 -47.892 -53.318 -33.439 1.00 24.91 C ANISOU 691 CA THR A 118 2524 3041 3901 -465 -163 49 C ATOM 692 C THR A 118 -48.674 -52.394 -32.498 1.00 25.34 C ANISOU 692 C THR A 118 2525 3158 3944 -449 -108 102 C ATOM 693 O THR A 118 -48.880 -51.212 -32.812 1.00 24.88 O ANISOU 693 O THR A 118 2462 3160 3830 -395 -116 90 O ATOM 694 CB THR A 118 -48.877 -54.166 -34.282 1.00 26.05 C ANISOU 694 CB THR A 118 2603 3166 4129 -520 -226 -4 C ATOM 695 OG1 THR A 118 -49.643 -55.036 -33.436 1.00 27.17 O ANISOU 695 OG1 THR A 118 2681 3273 4368 -591 -189 39 O ATOM 696 CG2 THR A 118 -48.132 -54.984 -35.327 1.00 26.61 C ANISOU 696 CG2 THR A 118 2732 3180 4200 -525 -287 -70 C ATOM 697 N SER A 119 -49.103 -52.921 -31.350 1.00 25.83 N ANISOU 697 N SER A 119 2551 3206 4057 -488 -49 162 N ATOM 698 CA SER A 119 -49.871 -52.115 -30.392 1.00 26.39 C ANISOU 698 CA SER A 119 2571 3340 4116 -468 10 214 C ATOM 699 C SER A 119 -49.031 -50.969 -29.806 1.00 25.72 C ANISOU 699 C SER A 119 2552 3288 3931 -398 48 233 C ATOM 700 O SER A 119 -49.535 -49.860 -29.631 1.00 25.89 O ANISOU 700 O SER A 119 2549 3371 3915 -354 65 238 O ATOM 701 CB SER A 119 -50.471 -52.987 -29.278 1.00 27.19 C ANISOU 701 CB SER A 119 2621 3419 4289 -522 73 282 C ATOM 702 OG SER A 119 -49.469 -53.551 -28.455 1.00 27.26 O ANISOU 702 OG SER A 119 2699 3381 4279 -523 117 326 O ATOM 703 N ARG A 120 -47.757 -51.232 -29.529 1.00 25.50 N ANISOU 703 N ARG A 120 2604 3220 3863 -386 59 240 N ATOM 704 CA ARG A 120 -46.845 -50.203 -29.017 1.00 25.10 C ANISOU 704 CA ARG A 120 2616 3195 3725 -327 85 249 C ATOM 705 C ARG A 120 -46.537 -49.150 -30.076 1.00 24.81 C ANISOU 705 C ARG A 120 2606 3182 3638 -281 41 197 C ATOM 706 O ARG A 120 -46.577 -47.951 -29.802 1.00 24.43 O ANISOU 706 O ARG A 120 2567 3176 3542 -234 62 200 O ATOM 707 CB ARG A 120 -45.528 -50.824 -28.540 1.00 24.72 C ANISOU 707 CB ARG A 120 2639 3101 3653 -328 99 266 C ATOM 708 CG ARG A 120 -45.629 -51.699 -27.297 1.00 26.43 C ANISOU 708 CG ARG A 120 2846 3300 3897 -355 156 331 C ATOM 709 CD ARG A 120 -46.233 -50.957 -26.159 1.00 27.03 C ANISOU 709 CD ARG A 120 2893 3435 3942 -327 215 375 C ATOM 710 NE ARG A 120 -46.077 -51.624 -24.871 1.00 26.45 N ANISOU 710 NE ARG A 120 2829 3355 3867 -333 276 444 N ATOM 711 CZ ARG A 120 -46.643 -51.179 -23.754 1.00 26.84 C ANISOU 711 CZ ARG A 120 2852 3456 3888 -308 337 491 C ATOM 712 NH1 ARG A 120 -47.406 -50.093 -23.790 1.00 27.26 N ANISOU 712 NH1 ARG A 120 2869 3567 3922 -278 344 474 N ATOM 713 NH2 ARG A 120 -46.457 -51.814 -22.606 1.00 26.66 N ANISOU 713 NH2 ARG A 120 2843 3431 3856 -305 393 557 N ATOM 714 N SER A 121 -46.221 -49.603 -31.283 1.00 24.95 N ANISOU 714 N SER A 121 2641 3170 3667 -292 -17 150 N ATOM 715 CA SER A 121 -45.802 -48.691 -32.350 1.00 24.97 C ANISOU 715 CA SER A 121 2678 3191 3618 -244 -55 109 C ATOM 716 C SER A 121 -46.930 -47.747 -32.782 1.00 25.18 C ANISOU 716 C SER A 121 2652 3275 3641 -214 -68 98 C ATOM 717 O SER A 121 -46.669 -46.609 -33.181 1.00 25.16 O ANISOU 717 O SER A 121 2677 3297 3585 -160 -70 88 O ATOM 718 CB SER A 121 -45.262 -49.487 -33.536 1.00 24.95 C ANISOU 718 CB SER A 121 2706 3151 3624 -256 -112 62 C ATOM 719 OG SER A 121 -44.079 -50.176 -33.152 1.00 26.37 O ANISOU 719 OG SER A 121 2941 3281 3796 -267 -96 74 O ATOM 720 N TYR A 122 -48.173 -48.215 -32.665 1.00 26.07 N ANISOU 720 N TYR A 122 2685 3407 3814 -249 -74 104 N ATOM 721 CA TYR A 122 -49.365 -47.416 -32.979 1.00 26.76 C ANISOU 721 CA TYR A 122 2707 3556 3905 -221 -85 98 C ATOM 722 C TYR A 122 -49.443 -46.083 -32.221 1.00 25.56 C ANISOU 722 C TYR A 122 2566 3443 3704 -164 -32 129 C ATOM 723 O TYR A 122 -50.091 -45.139 -32.686 1.00 25.18 O ANISOU 723 O TYR A 122 2491 3440 3635 -116 -44 119 O ATOM 724 CB TYR A 122 -50.624 -48.237 -32.684 1.00 28.47 C ANISOU 724 CB TYR A 122 2827 3785 4206 -277 -86 110 C ATOM 725 CG TYR A 122 -51.908 -47.615 -33.170 1.00 31.90 C ANISOU 725 CG TYR A 122 3180 4286 4656 -253 -111 96 C ATOM 726 CD1 TYR A 122 -52.328 -47.782 -34.486 1.00 36.31 C ANISOU 726 CD1 TYR A 122 3710 4860 5225 -250 -190 41 C ATOM 727 CD2 TYR A 122 -52.712 -46.863 -32.311 1.00 35.38 C ANISOU 727 CD2 TYR A 122 3570 4777 5095 -226 -57 138 C ATOM 728 CE1 TYR A 122 -53.525 -47.213 -34.940 1.00 38.16 C ANISOU 728 CE1 TYR A 122 3863 5163 5471 -223 -219 28 C ATOM 729 CE2 TYR A 122 -53.903 -46.286 -32.755 1.00 37.70 C ANISOU 729 CE2 TYR A 122 3783 5136 5404 -197 -80 128 C ATOM 730 CZ TYR A 122 -54.303 -46.465 -34.068 1.00 39.28 C ANISOU 730 CZ TYR A 122 3953 5355 5617 -196 -162 74 C ATOM 731 OH TYR A 122 -55.484 -45.900 -34.505 1.00 41.97 O ANISOU 731 OH TYR A 122 4210 5768 5971 -162 -189 64 O ATOM 732 N LEU A 123 -48.787 -46.009 -31.066 1.00 23.90 N ANISOU 732 N LEU A 123 2395 3216 3472 -164 24 163 N ATOM 733 CA LEU A 123 -48.791 -44.802 -30.238 1.00 23.34 C ANISOU 733 CA LEU A 123 2340 3175 3352 -112 74 184 C ATOM 734 C LEU A 123 -47.819 -43.719 -30.718 1.00 22.35 C ANISOU 734 C LEU A 123 2289 3037 3167 -61 65 161 C ATOM 735 O LEU A 123 -47.832 -42.605 -30.192 1.00 22.09 O ANISOU 735 O LEU A 123 2273 3021 3097 -14 98 168 O ATOM 736 CB LEU A 123 -48.479 -45.159 -28.777 1.00 23.33 C ANISOU 736 CB LEU A 123 2351 3166 3345 -128 135 226 C ATOM 737 CG LEU A 123 -49.660 -45.601 -27.908 1.00 24.62 C ANISOU 737 CG LEU A 123 2437 3364 3553 -150 179 269 C ATOM 738 CD1 LEU A 123 -50.600 -44.428 -27.637 1.00 25.71 C ANISOU 738 CD1 LEU A 123 2536 3562 3671 -94 206 274 C ATOM 739 CD2 LEU A 123 -50.421 -46.754 -28.536 1.00 26.11 C ANISOU 739 CD2 LEU A 123 2557 3540 3822 -212 145 267 C ATOM 740 N ILE A 124 -46.982 -44.037 -31.703 1.00 21.56 N ANISOU 740 N ILE A 124 2232 2904 3057 -68 22 133 N ATOM 741 CA ILE A 124 -45.973 -43.098 -32.194 1.00 20.94 C ANISOU 741 CA ILE A 124 2221 2808 2928 -26 18 118 C ATOM 742 C ILE A 124 -46.387 -42.554 -33.565 1.00 21.16 C ANISOU 742 C ILE A 124 2242 2855 2943 12 -24 95 C ATOM 743 O ILE A 124 -46.723 -43.322 -34.470 1.00 20.77 O ANISOU 743 O ILE A 124 2168 2811 2914 -6 -72 74 O ATOM 744 CB ILE A 124 -44.593 -43.782 -32.325 1.00 20.47 C ANISOU 744 CB ILE A 124 2219 2701 2857 -52 9 109 C ATOM 745 CG1 ILE A 124 -44.139 -44.381 -30.983 1.00 20.64 C ANISOU 745 CG1 ILE A 124 2249 2708 2885 -83 46 134 C ATOM 746 CG2 ILE A 124 -43.545 -42.799 -32.853 1.00 20.58 C ANISOU 746 CG2 ILE A 124 2293 2698 2827 -13 10 97 C ATOM 747 CD1 ILE A 124 -44.106 -43.387 -29.830 1.00 19.92 C ANISOU 747 CD1 ILE A 124 2170 2636 2763 -54 94 150 C ATOM 748 N ASP A 125 -46.362 -41.229 -33.708 1.00 21.09 N ANISOU 748 N ASP A 125 2257 2856 2901 68 -6 99 N ATOM 749 CA ASP A 125 -46.615 -40.584 -34.995 1.00 21.65 C ANISOU 749 CA ASP A 125 2333 2943 2949 118 -38 88 C ATOM 750 C ASP A 125 -45.438 -40.823 -35.926 1.00 20.68 C ANISOU 750 C ASP A 125 2270 2789 2801 118 -61 74 C ATOM 751 O ASP A 125 -44.297 -40.494 -35.588 1.00 20.29 O ANISOU 751 O ASP A 125 2274 2701 2734 115 -32 80 O ATOM 752 CB ASP A 125 -46.782 -39.070 -34.834 1.00 22.04 C ANISOU 752 CB ASP A 125 2403 2999 2973 180 -4 104 C ATOM 753 CG ASP A 125 -48.007 -38.690 -34.032 1.00 25.41 C ANISOU 753 CG ASP A 125 2771 3465 3417 198 21 117 C ATOM 754 OD1 ASP A 125 -49.005 -39.447 -34.023 1.00 27.43 O ANISOU 754 OD1 ASP A 125 2956 3760 3706 174 -1 116 O ATOM 755 OD2 ASP A 125 -47.970 -37.604 -33.413 1.00 29.51 O ANISOU 755 OD2 ASP A 125 3316 3976 3922 236 63 127 O ATOM 756 N SER A 126 -45.714 -41.388 -37.098 1.00 20.31 N ANISOU 756 N SER A 126 2209 2759 2749 124 -114 51 N ATOM 757 CA SER A 126 -44.663 -41.699 -38.058 1.00 19.90 C ANISOU 757 CA SER A 126 2211 2684 2667 131 -135 36 C ATOM 758 C SER A 126 -45.264 -41.715 -39.464 1.00 20.01 C ANISOU 758 C SER A 126 2211 2737 2654 174 -190 14 C ATOM 759 O SER A 126 -46.105 -42.565 -39.746 1.00 20.62 O ANISOU 759 O SER A 126 2237 2840 2757 151 -237 -15 O ATOM 760 CB SER A 126 -44.047 -43.059 -37.729 1.00 19.72 C ANISOU 760 CB SER A 126 2194 2627 2670 70 -146 20 C ATOM 761 OG SER A 126 -42.953 -43.357 -38.583 1.00 19.74 O ANISOU 761 OG SER A 126 2250 2608 2643 81 -160 6 O ATOM 762 N PRO A 127 -44.862 -40.769 -40.346 1.00 20.03 N ANISOU 762 N PRO A 127 2257 2746 2607 239 -183 29 N ATOM 763 CA PRO A 127 -43.886 -39.682 -40.178 1.00 19.07 C ANISOU 763 CA PRO A 127 2194 2590 2463 267 -128 63 C ATOM 764 C PRO A 127 -44.154 -38.740 -38.997 1.00 18.63 C ANISOU 764 C PRO A 127 2129 2519 2430 266 -78 88 C ATOM 765 O PRO A 127 -45.303 -38.562 -38.584 1.00 18.24 O ANISOU 765 O PRO A 127 2030 2503 2399 274 -82 89 O ATOM 766 CB PRO A 127 -43.994 -38.911 -41.499 1.00 19.81 C ANISOU 766 CB PRO A 127 2312 2710 2504 345 -141 76 C ATOM 767 CG PRO A 127 -44.418 -39.922 -42.476 1.00 20.84 C ANISOU 767 CG PRO A 127 2421 2880 2616 348 -208 37 C ATOM 768 CD PRO A 127 -45.374 -40.811 -41.727 1.00 20.51 C ANISOU 768 CD PRO A 127 2310 2853 2628 290 -237 9 C ATOM 769 N PRO A 128 -43.092 -38.116 -38.467 1.00 17.68 N ANISOU 769 N PRO A 128 2056 2352 2310 259 -30 105 N ATOM 770 CA PRO A 128 -43.205 -37.321 -37.252 1.00 17.48 C ANISOU 770 CA PRO A 128 2029 2307 2304 254 14 116 C ATOM 771 C PRO A 128 -43.850 -35.969 -37.497 1.00 17.67 C ANISOU 771 C PRO A 128 2059 2337 2318 319 35 137 C ATOM 772 O PRO A 128 -43.932 -35.522 -38.641 1.00 17.99 O ANISOU 772 O PRO A 128 2116 2387 2331 371 23 152 O ATOM 773 CB PRO A 128 -41.752 -37.142 -36.828 1.00 17.30 C ANISOU 773 CB PRO A 128 2056 2233 2284 226 46 118 C ATOM 774 CG PRO A 128 -41.012 -37.138 -38.098 1.00 17.19 C ANISOU 774 CG PRO A 128 2076 2211 2244 249 36 127 C ATOM 775 CD PRO A 128 -41.726 -38.072 -39.018 1.00 17.70 C ANISOU 775 CD PRO A 128 2114 2320 2293 259 -16 112 C ATOM 776 N THR A 129 -44.271 -35.327 -36.415 1.00 17.80 N ANISOU 776 N THR A 129 2065 2346 2352 323 68 139 N ATOM 777 CA THR A 129 -45.072 -34.108 -36.481 1.00 18.06 C ANISOU 777 CA THR A 129 2096 2384 2381 388 89 156 C ATOM 778 C THR A 129 -44.379 -32.929 -35.778 1.00 18.11 C ANISOU 778 C THR A 129 2154 2330 2399 398 140 161 C ATOM 779 O THR A 129 -43.602 -32.209 -36.399 1.00 18.35 O ANISOU 779 O THR A 129 2234 2315 2424 418 158 177 O ATOM 780 CB THR A 129 -46.467 -34.373 -35.890 1.00 18.34 C ANISOU 780 CB THR A 129 2064 2475 2431 395 79 151 C ATOM 781 OG1 THR A 129 -46.331 -34.986 -34.599 1.00 17.90 O ANISOU 781 OG1 THR A 129 1991 2415 2394 339 96 137 O ATOM 782 CG2 THR A 129 -47.250 -35.313 -36.801 1.00 18.67 C ANISOU 782 CG2 THR A 129 2051 2573 2468 394 23 144 C ATOM 783 N TYR A 130 -44.632 -32.759 -34.484 1.00 18.33 N ANISOU 783 N TYR A 130 2171 2354 2441 383 164 145 N ATOM 784 CA TYR A 130 -44.279 -31.526 -33.768 1.00 18.42 C ANISOU 784 CA TYR A 130 2225 2313 2463 404 208 138 C ATOM 785 C TYR A 130 -42.822 -31.462 -33.307 1.00 18.03 C ANISOU 785 C TYR A 130 2221 2207 2425 354 222 120 C ATOM 786 O TYR A 130 -42.104 -32.458 -33.313 1.00 17.94 O ANISOU 786 O TYR A 130 2203 2202 2410 302 202 113 O ATOM 787 CB TYR A 130 -45.197 -31.357 -32.554 1.00 18.84 C ANISOU 787 CB TYR A 130 2246 2393 2518 418 227 123 C ATOM 788 CG TYR A 130 -46.665 -31.466 -32.902 1.00 19.28 C ANISOU 788 CG TYR A 130 2244 2513 2570 464 214 140 C ATOM 789 CD1 TYR A 130 -47.453 -32.495 -32.386 1.00 20.05 C ANISOU 789 CD1 TYR A 130 2275 2671 2670 435 200 138 C ATOM 790 CD2 TYR A 130 -47.256 -30.564 -33.785 1.00 20.17 C ANISOU 790 CD2 TYR A 130 2362 2625 2677 535 216 163 C ATOM 791 CE1 TYR A 130 -48.807 -32.601 -32.719 1.00 21.77 C ANISOU 791 CE1 TYR A 130 2428 2951 2893 473 186 152 C ATOM 792 CE2 TYR A 130 -48.598 -30.665 -34.120 1.00 22.14 C ANISOU 792 CE2 TYR A 130 2549 2940 2922 580 199 177 C ATOM 793 CZ TYR A 130 -49.366 -31.686 -33.584 1.00 22.41 C ANISOU 793 CZ TYR A 130 2512 3037 2966 546 182 169 C ATOM 794 OH TYR A 130 -50.697 -31.780 -33.920 1.00 24.50 O ANISOU 794 OH TYR A 130 2705 3370 3234 586 164 181 O ATOM 795 N ASN A 131 -42.387 -30.271 -32.905 1.00 17.86 N ANISOU 795 N ASN A 131 2241 2126 2420 371 255 111 N ATOM 796 CA ASN A 131 -41.110 -30.128 -32.205 1.00 17.37 C ANISOU 796 CA ASN A 131 2211 2014 2374 321 266 82 C ATOM 797 C ASN A 131 -41.158 -28.933 -31.258 1.00 17.49 C ANISOU 797 C ASN A 131 2257 1984 2406 343 297 52 C ATOM 798 O ASN A 131 -42.223 -28.349 -31.068 1.00 17.45 O ANISOU 798 O ASN A 131 2246 1990 2396 397 312 54 O ATOM 799 CB ASN A 131 -39.909 -30.104 -33.178 1.00 17.27 C ANISOU 799 CB ASN A 131 2227 1961 2375 297 266 101 C ATOM 800 CG ASN A 131 -39.850 -28.852 -34.052 1.00 17.96 C ANISOU 800 CG ASN A 131 2351 1990 2482 343 297 131 C ATOM 801 OD1 ASN A 131 -40.278 -27.766 -33.665 1.00 18.29 O ANISOU 801 OD1 ASN A 131 2414 1994 2541 379 323 124 O ATOM 802 ND2 ASN A 131 -39.280 -29.010 -35.240 1.00 18.33 N ANISOU 802 ND2 ASN A 131 2410 2031 2526 344 297 168 N ATOM 803 N VAL A 132 -40.032 -28.582 -30.643 1.00 17.67 N ANISOU 803 N VAL A 132 2309 1957 2449 303 304 18 N ATOM 804 CA VAL A 132 -40.031 -27.511 -29.634 1.00 18.13 C ANISOU 804 CA VAL A 132 2398 1970 2522 319 325 -26 C ATOM 805 C VAL A 132 -40.536 -26.162 -30.176 1.00 18.85 C ANISOU 805 C VAL A 132 2522 2001 2640 378 358 -10 C ATOM 806 O VAL A 132 -41.122 -25.361 -29.437 1.00 19.29 O ANISOU 806 O VAL A 132 2595 2037 2698 419 377 -40 O ATOM 807 CB VAL A 132 -38.634 -27.349 -28.978 1.00 18.20 C ANISOU 807 CB VAL A 132 2429 1932 2554 261 319 -71 C ATOM 808 CG1 VAL A 132 -37.604 -26.865 -29.984 1.00 17.78 C ANISOU 808 CG1 VAL A 132 2398 1811 2546 236 330 -47 C ATOM 809 CG2 VAL A 132 -38.705 -26.397 -27.779 1.00 19.00 C ANISOU 809 CG2 VAL A 132 2559 1999 2661 278 331 -132 C ATOM 810 N HIS A 133 -40.334 -25.917 -31.468 1.00 18.97 N ANISOU 810 N HIS A 133 2549 1987 2673 391 366 39 N ATOM 811 CA HIS A 133 -40.723 -24.652 -32.074 1.00 20.00 C ANISOU 811 CA HIS A 133 2715 2055 2830 451 401 66 C ATOM 812 C HIS A 133 -42.044 -24.664 -32.834 1.00 19.85 C ANISOU 812 C HIS A 133 2674 2087 2781 526 400 112 C ATOM 813 O HIS A 133 -42.526 -23.600 -33.227 1.00 20.16 O ANISOU 813 O HIS A 133 2743 2081 2837 589 430 136 O ATOM 814 CB HIS A 133 -39.615 -24.146 -32.987 1.00 20.34 C ANISOU 814 CB HIS A 133 2792 2023 2914 427 421 98 C ATOM 815 CG HIS A 133 -38.413 -23.657 -32.248 1.00 22.43 C ANISOU 815 CG HIS A 133 3080 2214 3228 365 430 49 C ATOM 816 ND1 HIS A 133 -37.149 -23.669 -32.794 1.00 24.01 N ANISOU 816 ND1 HIS A 133 3287 2370 3464 312 438 66 N ATOM 817 CD2 HIS A 133 -38.280 -23.154 -30.996 1.00 24.60 C ANISOU 817 CD2 HIS A 133 3371 2456 3521 349 429 -19 C ATOM 818 CE1 HIS A 133 -36.290 -23.181 -31.916 1.00 25.21 C ANISOU 818 CE1 HIS A 133 3454 2464 3662 261 439 9 C ATOM 819 NE2 HIS A 133 -36.949 -22.868 -30.815 1.00 25.15 N ANISOU 819 NE2 HIS A 133 3453 2462 3640 284 430 -46 N ATOM 820 N TYR A 134 -42.625 -25.844 -33.031 1.00 19.02 N ANISOU 820 N TYR A 134 2518 2074 2636 520 367 124 N ATOM 821 CA TYR A 134 -43.843 -25.983 -33.829 1.00 19.03 C ANISOU 821 CA TYR A 134 2487 2134 2610 584 355 163 C ATOM 822 C TYR A 134 -44.910 -26.819 -33.125 1.00 19.21 C ANISOU 822 C TYR A 134 2448 2244 2606 586 333 145 C ATOM 823 O TYR A 134 -44.762 -28.040 -32.972 1.00 18.86 O ANISOU 823 O TYR A 134 2367 2251 2548 533 303 136 O ATOM 824 CB TYR A 134 -43.512 -26.558 -35.213 1.00 18.49 C ANISOU 824 CB TYR A 134 2413 2088 2524 581 333 206 C ATOM 825 CG TYR A 134 -42.731 -25.574 -36.045 1.00 18.84 C ANISOU 825 CG TYR A 134 2515 2054 2592 602 367 243 C ATOM 826 CD1 TYR A 134 -41.342 -25.601 -36.061 1.00 18.92 C ANISOU 826 CD1 TYR A 134 2553 2008 2629 540 380 237 C ATOM 827 CD2 TYR A 134 -43.377 -24.581 -36.770 1.00 19.34 C ANISOU 827 CD2 TYR A 134 2601 2095 2654 685 391 287 C ATOM 828 CE1 TYR A 134 -40.619 -24.683 -36.792 1.00 19.20 C ANISOU 828 CE1 TYR A 134 2635 1966 2694 554 419 276 C ATOM 829 CE2 TYR A 134 -42.657 -23.652 -37.513 1.00 19.47 C ANISOU 829 CE2 TYR A 134 2671 2031 2696 705 431 330 C ATOM 830 CZ TYR A 134 -41.273 -23.718 -37.518 1.00 19.76 C ANISOU 830 CZ TYR A 134 2732 2011 2764 635 447 325 C ATOM 831 OH TYR A 134 -40.536 -22.805 -38.242 1.00 21.41 O ANISOU 831 OH TYR A 134 2989 2137 3007 649 494 373 O ATOM 832 N GLY A 135 -45.970 -26.137 -32.691 1.00 19.53 N ANISOU 832 N GLY A 135 2478 2297 2646 650 353 142 N ATOM 833 CA GLY A 135 -47.151 -26.777 -32.099 1.00 19.83 C ANISOU 833 CA GLY A 135 2450 2420 2663 665 342 136 C ATOM 834 C GLY A 135 -48.246 -27.067 -33.117 1.00 20.15 C ANISOU 834 C GLY A 135 2437 2529 2689 714 316 174 C ATOM 835 O GLY A 135 -49.375 -27.415 -32.746 1.00 20.52 O ANISOU 835 O GLY A 135 2422 2647 2729 738 310 175 O ATOM 836 N TYR A 136 -47.912 -26.886 -34.394 1.00 20.05 N ANISOU 836 N TYR A 136 2447 2498 2671 734 301 207 N ATOM 837 CA TYR A 136 -48.755 -27.264 -35.531 1.00 20.05 C ANISOU 837 CA TYR A 136 2402 2566 2649 777 264 239 C ATOM 838 C TYR A 136 -47.825 -27.946 -36.531 1.00 19.81 C ANISOU 838 C TYR A 136 2392 2530 2606 734 234 250 C ATOM 839 O TYR A 136 -46.616 -27.734 -36.490 1.00 19.56 O ANISOU 839 O TYR A 136 2415 2430 2586 695 255 247 O ATOM 840 CB TYR A 136 -49.411 -26.024 -36.154 1.00 20.75 C ANISOU 840 CB TYR A 136 2511 2639 2733 880 285 275 C ATOM 841 CG TYR A 136 -48.428 -24.920 -36.513 1.00 20.13 C ANISOU 841 CG TYR A 136 2520 2457 2670 899 326 296 C ATOM 842 CD1 TYR A 136 -47.811 -24.887 -37.757 1.00 20.09 C ANISOU 842 CD1 TYR A 136 2549 2435 2650 910 317 335 C ATOM 843 CD2 TYR A 136 -48.118 -23.910 -35.603 1.00 20.72 C ANISOU 843 CD2 TYR A 136 2645 2451 2778 907 374 276 C ATOM 844 CE1 TYR A 136 -46.901 -23.884 -38.085 1.00 20.32 C ANISOU 844 CE1 TYR A 136 2653 2366 2702 922 362 362 C ATOM 845 CE2 TYR A 136 -47.202 -22.902 -35.921 1.00 21.01 C ANISOU 845 CE2 TYR A 136 2758 2383 2843 915 413 294 C ATOM 846 CZ TYR A 136 -46.603 -22.898 -37.165 1.00 21.00 C ANISOU 846 CZ TYR A 136 2784 2365 2832 921 409 342 C ATOM 847 OH TYR A 136 -45.705 -21.907 -37.500 1.00 21.99 O ANISOU 847 OH TYR A 136 2979 2384 2992 926 455 368 O ATOM 848 N LYS A 137 -48.373 -28.774 -37.412 1.00 19.38 N ANISOU 848 N LYS A 137 2289 2546 2527 741 185 258 N ATOM 849 CA LYS A 137 -47.556 -29.471 -38.396 1.00 19.19 C ANISOU 849 CA LYS A 137 2285 2524 2483 710 155 264 C ATOM 850 C LYS A 137 -46.986 -28.488 -39.430 1.00 19.02 C ANISOU 850 C LYS A 137 2328 2454 2444 769 179 308 C ATOM 851 O LYS A 137 -47.671 -27.558 -39.861 1.00 19.18 O ANISOU 851 O LYS A 137 2356 2478 2453 853 193 340 O ATOM 852 CB LYS A 137 -48.361 -30.574 -39.079 1.00 19.55 C ANISOU 852 CB LYS A 137 2265 2658 2507 708 91 253 C ATOM 853 CG LYS A 137 -48.479 -31.841 -38.237 1.00 21.02 C ANISOU 853 CG LYS A 137 2398 2872 2717 624 68 215 C ATOM 854 CD LYS A 137 -49.641 -32.721 -38.670 1.00 23.22 C ANISOU 854 CD LYS A 137 2594 3235 2993 626 10 201 C ATOM 855 CE LYS A 137 -50.912 -32.352 -37.920 1.00 25.73 C ANISOU 855 CE LYS A 137 2848 3595 3332 657 24 204 C ATOM 856 NZ LYS A 137 -52.150 -32.957 -38.486 1.00 27.08 N ANISOU 856 NZ LYS A 137 2931 3853 3506 674 -33 195 N ATOM 857 N SER A 138 -45.729 -28.689 -39.811 1.00 18.65 N ANISOU 857 N SER A 138 2328 2364 2396 728 190 314 N ATOM 858 CA SER A 138 -45.096 -27.817 -40.805 1.00 19.39 C ANISOU 858 CA SER A 138 2481 2410 2476 778 222 364 C ATOM 859 C SER A 138 -43.985 -28.538 -41.541 1.00 18.86 C ANISOU 859 C SER A 138 2437 2341 2389 738 212 369 C ATOM 860 O SER A 138 -43.411 -29.502 -41.023 1.00 18.04 O ANISOU 860 O SER A 138 2316 2241 2297 661 194 331 O ATOM 861 CB SER A 138 -44.533 -26.562 -40.130 1.00 19.64 C ANISOU 861 CB SER A 138 2566 2343 2555 779 287 376 C ATOM 862 OG SER A 138 -43.404 -26.879 -39.338 1.00 21.08 O ANISOU 862 OG SER A 138 2763 2476 2771 691 301 343 O ATOM 863 N TRP A 139 -43.664 -28.061 -42.743 1.00 19.23 N ANISOU 863 N TRP A 139 2523 2381 2404 797 228 420 N ATOM 864 CA TRP A 139 -42.563 -28.646 -43.485 1.00 18.95 C ANISOU 864 CA TRP A 139 2512 2342 2346 770 229 431 C ATOM 865 C TRP A 139 -41.246 -28.471 -42.729 1.00 18.19 C ANISOU 865 C TRP A 139 2443 2164 2303 693 274 422 C ATOM 866 O TRP A 139 -40.391 -29.362 -42.761 1.00 17.79 O ANISOU 866 O TRP A 139 2389 2122 2250 637 262 402 O ATOM 867 CB TRP A 139 -42.439 -28.104 -44.920 1.00 19.67 C ANISOU 867 CB TRP A 139 2643 2444 2385 857 247 495 C ATOM 868 CG TRP A 139 -41.585 -29.034 -45.684 1.00 19.90 C ANISOU 868 CG TRP A 139 2682 2502 2377 834 230 492 C ATOM 869 CD1 TRP A 139 -40.256 -28.903 -45.945 1.00 19.93 C ANISOU 869 CD1 TRP A 139 2725 2455 2394 806 279 520 C ATOM 870 CD2 TRP A 139 -41.971 -30.316 -46.179 1.00 20.09 C ANISOU 870 CD2 TRP A 139 2671 2610 2351 831 159 449 C ATOM 871 NE1 TRP A 139 -39.793 -30.016 -46.613 1.00 20.73 N ANISOU 871 NE1 TRP A 139 2820 2608 2449 795 246 501 N ATOM 872 CE2 TRP A 139 -40.830 -30.899 -46.765 1.00 20.56 C ANISOU 872 CE2 TRP A 139 2757 2665 2388 809 170 454 C ATOM 873 CE3 TRP A 139 -43.184 -31.019 -46.208 1.00 21.20 C ANISOU 873 CE3 TRP A 139 2758 2828 2468 845 87 405 C ATOM 874 CZ2 TRP A 139 -40.862 -32.156 -47.371 1.00 21.14 C ANISOU 874 CZ2 TRP A 139 2814 2805 2414 805 110 412 C ATOM 875 CZ3 TRP A 139 -43.215 -32.265 -46.817 1.00 21.44 C ANISOU 875 CZ3 TRP A 139 2767 2921 2457 833 26 363 C ATOM 876 CH2 TRP A 139 -42.065 -32.818 -47.391 1.00 21.02 C ANISOU 876 CH2 TRP A 139 2750 2858 2379 815 37 365 C ATOM 877 N GLU A 140 -41.086 -27.348 -42.027 1.00 18.51 N ANISOU 877 N GLU A 140 2510 2129 2396 690 324 432 N ATOM 878 CA GLU A 140 -39.881 -27.147 -41.209 1.00 18.75 C ANISOU 878 CA GLU A 140 2558 2083 2482 612 358 413 C ATOM 879 C GLU A 140 -39.755 -28.235 -40.139 1.00 18.05 C ANISOU 879 C GLU A 140 2430 2026 2404 535 320 348 C ATOM 880 O GLU A 140 -38.684 -28.828 -39.983 1.00 18.24 O ANISOU 880 O GLU A 140 2453 2038 2439 474 319 333 O ATOM 881 CB GLU A 140 -39.862 -25.747 -40.579 1.00 19.38 C ANISOU 881 CB GLU A 140 2671 2074 2618 624 410 422 C ATOM 882 CG GLU A 140 -38.640 -25.437 -39.696 1.00 19.59 C ANISOU 882 CG GLU A 140 2713 2021 2710 543 440 393 C ATOM 883 CD GLU A 140 -37.313 -25.417 -40.443 1.00 21.23 C ANISOU 883 CD GLU A 140 2941 2192 2934 514 473 431 C ATOM 884 OE1 GLU A 140 -36.264 -25.541 -39.767 1.00 20.69 O ANISOU 884 OE1 GLU A 140 2868 2085 2910 438 481 399 O ATOM 885 OE2 GLU A 140 -37.307 -25.275 -41.690 1.00 22.74 O ANISOU 885 OE2 GLU A 140 3152 2397 3092 570 492 494 O ATOM 886 N ALA A 141 -40.843 -28.504 -39.415 1.00 18.36 N ANISOU 886 N ALA A 141 2433 2107 2437 541 290 315 N ATOM 887 CA ALA A 141 -40.822 -29.518 -38.350 1.00 17.71 C ANISOU 887 CA ALA A 141 2313 2054 2362 474 259 262 C ATOM 888 C ALA A 141 -40.600 -30.916 -38.922 1.00 17.71 C ANISOU 888 C ALA A 141 2288 2110 2330 445 216 253 C ATOM 889 O ALA A 141 -39.852 -31.714 -38.364 1.00 17.43 O ANISOU 889 O ALA A 141 2245 2071 2306 383 206 226 O ATOM 890 CB ALA A 141 -42.110 -29.467 -37.522 1.00 17.69 C ANISOU 890 CB ALA A 141 2275 2087 2360 494 246 239 C ATOM 891 N PHE A 142 -41.242 -31.215 -40.045 1.00 18.03 N ANISOU 891 N PHE A 142 2319 2202 2331 496 188 273 N ATOM 892 CA PHE A 142 -41.016 -32.498 -40.681 1.00 17.68 C ANISOU 892 CA PHE A 142 2258 2205 2256 475 145 258 C ATOM 893 C PHE A 142 -39.568 -32.658 -41.149 1.00 17.65 C ANISOU 893 C PHE A 142 2291 2166 2250 450 168 272 C ATOM 894 O PHE A 142 -38.927 -33.670 -40.856 1.00 17.78 O ANISOU 894 O PHE A 142 2296 2188 2271 396 150 244 O ATOM 895 CB PHE A 142 -41.934 -32.738 -41.879 1.00 18.21 C ANISOU 895 CB PHE A 142 2309 2335 2273 540 104 269 C ATOM 896 CG PHE A 142 -41.491 -33.905 -42.693 1.00 17.55 C ANISOU 896 CG PHE A 142 2225 2288 2157 526 65 252 C ATOM 897 CD1 PHE A 142 -41.625 -35.185 -42.189 1.00 18.14 C ANISOU 897 CD1 PHE A 142 2263 2385 2245 466 24 205 C ATOM 898 CD2 PHE A 142 -40.840 -33.726 -43.910 1.00 18.53 C ANISOU 898 CD2 PHE A 142 2390 2415 2238 572 77 283 C ATOM 899 CE1 PHE A 142 -41.160 -36.281 -42.900 1.00 18.52 C ANISOU 899 CE1 PHE A 142 2316 2456 2267 453 -11 183 C ATOM 900 CE2 PHE A 142 -40.375 -34.814 -44.623 1.00 18.79 C ANISOU 900 CE2 PHE A 142 2426 2478 2236 563 44 261 C ATOM 901 CZ PHE A 142 -40.537 -36.094 -44.120 1.00 18.99 C ANISOU 901 CZ PHE A 142 2416 2522 2278 503 -3 208 C ATOM 902 N SER A 143 -39.056 -31.660 -41.865 1.00 17.67 N ANISOU 902 N SER A 143 2334 2131 2249 491 212 319 N ATOM 903 CA SER A 143 -37.828 -31.823 -42.644 1.00 17.69 C ANISOU 903 CA SER A 143 2365 2117 2239 486 236 344 C ATOM 904 C SER A 143 -36.528 -31.582 -41.884 1.00 17.64 C ANISOU 904 C SER A 143 2368 2047 2285 421 276 340 C ATOM 905 O SER A 143 -35.490 -32.113 -42.277 1.00 17.41 O ANISOU 905 O SER A 143 2346 2019 2252 399 284 345 O ATOM 906 CB SER A 143 -37.853 -30.923 -43.882 1.00 18.50 C ANISOU 906 CB SER A 143 2504 2215 2309 566 270 407 C ATOM 907 OG SER A 143 -37.777 -29.550 -43.536 1.00 18.01 O ANISOU 907 OG SER A 143 2468 2084 2292 579 325 442 O ATOM 908 N ASN A 144 -36.576 -30.784 -40.821 1.00 17.26 N ANISOU 908 N ASN A 144 2321 1949 2288 394 298 326 N ATOM 909 CA ASN A 144 -35.352 -30.388 -40.121 1.00 17.30 C ANISOU 909 CA ASN A 144 2335 1893 2348 335 332 318 C ATOM 910 C ASN A 144 -34.924 -31.449 -39.110 1.00 16.67 C ANISOU 910 C ASN A 144 2225 1834 2276 268 298 265 C ATOM 911 O ASN A 144 -35.480 -31.539 -38.018 1.00 16.37 O ANISOU 911 O ASN A 144 2170 1802 2249 247 279 227 O ATOM 912 CB ASN A 144 -35.538 -29.033 -39.443 1.00 17.41 C ANISOU 912 CB ASN A 144 2367 1837 2411 337 368 319 C ATOM 913 CG ASN A 144 -34.228 -28.436 -38.980 1.00 18.63 C ANISOU 913 CG ASN A 144 2530 1920 2627 281 406 315 C ATOM 914 OD1 ASN A 144 -33.324 -29.158 -38.542 1.00 16.47 O ANISOU 914 OD1 ASN A 144 2237 1658 2364 225 391 287 O ATOM 915 ND2 ASN A 144 -34.109 -27.101 -39.121 1.00 21.49 N ANISOU 915 ND2 ASN A 144 2924 2206 3035 299 455 344 N ATOM 916 N LEU A 145 -33.922 -32.242 -39.480 1.00 16.96 N ANISOU 916 N LEU A 145 2256 1884 2305 242 295 267 N ATOM 917 CA LEU A 145 -33.497 -33.384 -38.678 1.00 16.84 C ANISOU 917 CA LEU A 145 2214 1894 2290 190 261 225 C ATOM 918 C LEU A 145 -32.701 -32.993 -37.428 1.00 16.71 C ANISOU 918 C LEU A 145 2189 1838 2322 134 273 196 C ATOM 919 O LEU A 145 -32.433 -33.840 -36.581 1.00 15.90 O ANISOU 919 O LEU A 145 2067 1757 2218 97 245 162 O ATOM 920 CB LEU A 145 -32.678 -34.351 -39.532 1.00 16.76 C ANISOU 920 CB LEU A 145 2203 1910 2254 190 255 237 C ATOM 921 CG LEU A 145 -33.378 -34.909 -40.775 1.00 17.76 C ANISOU 921 CG LEU A 145 2339 2085 2325 245 233 252 C ATOM 922 CD1 LEU A 145 -32.399 -35.750 -41.583 1.00 18.48 C ANISOU 922 CD1 LEU A 145 2435 2195 2391 250 234 261 C ATOM 923 CD2 LEU A 145 -34.614 -35.728 -40.404 1.00 18.82 C ANISOU 923 CD2 LEU A 145 2451 2261 2439 246 180 217 C ATOM 924 N SER A 146 -32.351 -31.713 -37.299 1.00 17.23 N ANISOU 924 N SER A 146 2272 1844 2431 131 312 207 N ATOM 925 CA SER A 146 -31.611 -31.254 -36.125 1.00 17.93 C ANISOU 925 CA SER A 146 2352 1894 2567 78 316 169 C ATOM 926 C SER A 146 -32.476 -31.142 -34.861 1.00 17.71 C ANISOU 926 C SER A 146 2320 1875 2535 74 293 123 C ATOM 927 O SER A 146 -31.936 -31.013 -33.768 1.00 18.12 O ANISOU 927 O SER A 146 2363 1912 2608 35 283 80 O ATOM 928 CB SER A 146 -30.900 -29.930 -36.410 1.00 18.80 C ANISOU 928 CB SER A 146 2480 1929 2736 69 365 190 C ATOM 929 OG SER A 146 -29.816 -30.133 -37.301 1.00 20.70 O ANISOU 929 OG SER A 146 2714 2165 2987 59 391 228 O ATOM 930 N TYR A 147 -33.801 -31.173 -35.010 1.00 17.18 N ANISOU 930 N TYR A 147 2256 1835 2436 119 283 131 N ATOM 931 CA TYR A 147 -34.709 -31.188 -33.864 1.00 17.31 C ANISOU 931 CA TYR A 147 2264 1872 2441 122 266 94 C ATOM 932 C TYR A 147 -35.020 -32.606 -33.376 1.00 16.54 C ANISOU 932 C TYR A 147 2137 1840 2309 104 229 79 C ATOM 933 O TYR A 147 -35.190 -33.526 -34.178 1.00 16.26 O ANISOU 933 O TYR A 147 2090 1839 2249 112 211 100 O ATOM 934 CB TYR A 147 -36.062 -30.597 -34.247 1.00 17.76 C ANISOU 934 CB TYR A 147 2329 1934 2484 181 275 114 C ATOM 935 CG TYR A 147 -36.155 -29.109 -34.473 1.00 17.78 C ANISOU 935 CG TYR A 147 2365 1870 2520 212 314 127 C ATOM 936 CD1 TYR A 147 -36.003 -28.568 -35.746 1.00 18.44 C ANISOU 936 CD1 TYR A 147 2470 1926 2611 246 341 179 C ATOM 937 CD2 TYR A 147 -36.514 -28.251 -33.433 1.00 18.86 C ANISOU 937 CD2 TYR A 147 2514 1973 2678 218 326 91 C ATOM 938 CE1 TYR A 147 -36.158 -27.203 -35.969 1.00 18.96 C ANISOU 938 CE1 TYR A 147 2569 1923 2710 280 382 200 C ATOM 939 CE2 TYR A 147 -36.672 -26.884 -33.647 1.00 19.91 C ANISOU 939 CE2 TYR A 147 2682 2036 2846 251 363 103 C ATOM 940 CZ TYR A 147 -36.486 -26.365 -34.915 1.00 20.12 C ANISOU 940 CZ TYR A 147 2730 2029 2887 281 392 160 C ATOM 941 OH TYR A 147 -36.636 -25.008 -35.140 1.00 21.10 O ANISOU 941 OH TYR A 147 2892 2074 3050 316 433 179 O ATOM 942 N TYR A 148 -35.162 -32.768 -32.063 1.00 16.29 N ANISOU 942 N TYR A 148 2096 1822 2273 85 218 42 N ATOM 943 CA TYR A 148 -35.928 -33.895 -31.535 1.00 16.26 C ANISOU 943 CA TYR A 148 2065 1876 2237 83 194 38 C ATOM 944 C TYR A 148 -37.385 -33.640 -31.900 1.00 16.45 C ANISOU 944 C TYR A 148 2079 1921 2250 128 198 55 C ATOM 945 O TYR A 148 -37.823 -32.496 -31.919 1.00 16.82 O ANISOU 945 O TYR A 148 2142 1940 2308 161 220 55 O ATOM 946 CB TYR A 148 -35.828 -33.981 -30.015 1.00 16.46 C ANISOU 946 CB TYR A 148 2085 1916 2254 65 189 2 C ATOM 947 CG TYR A 148 -34.473 -34.365 -29.461 1.00 16.58 C ANISOU 947 CG TYR A 148 2101 1925 2273 24 176 -19 C ATOM 948 CD1 TYR A 148 -33.962 -35.651 -29.637 1.00 17.21 C ANISOU 948 CD1 TYR A 148 2165 2034 2341 2 156 -4 C ATOM 949 CD2 TYR A 148 -33.720 -33.453 -28.724 1.00 17.55 C ANISOU 949 CD2 TYR A 148 2239 2015 2414 10 181 -58 C ATOM 950 CE1 TYR A 148 -32.725 -36.018 -29.103 1.00 18.06 C ANISOU 950 CE1 TYR A 148 2269 2142 2450 -28 143 -22 C ATOM 951 CE2 TYR A 148 -32.476 -33.811 -28.187 1.00 18.34 C ANISOU 951 CE2 TYR A 148 2330 2119 2518 -25 163 -81 C ATOM 952 CZ TYR A 148 -31.988 -35.093 -28.377 1.00 18.82 C ANISOU 952 CZ TYR A 148 2373 2214 2562 -42 145 -60 C ATOM 953 OH TYR A 148 -30.762 -35.457 -27.852 1.00 20.43 O ANISOU 953 OH TYR A 148 2565 2427 2769 -69 125 -80 O ATOM 954 N THR A 149 -38.139 -34.693 -32.182 1.00 16.31 N ANISOU 954 N THR A 149 2032 1951 2215 129 175 69 N ATOM 955 CA THR A 149 -39.574 -34.549 -32.387 1.00 16.45 C ANISOU 955 CA THR A 149 2027 2000 2225 168 174 81 C ATOM 956 C THR A 149 -40.281 -34.502 -31.026 1.00 16.86 C ANISOU 956 C THR A 149 2060 2076 2271 169 186 64 C ATOM 957 O THR A 149 -39.647 -34.656 -29.967 1.00 16.75 O ANISOU 957 O THR A 149 2055 2057 2253 142 192 43 O ATOM 958 CB THR A 149 -40.159 -35.654 -33.321 1.00 16.70 C ANISOU 958 CB THR A 149 2028 2071 2246 167 141 96 C ATOM 959 OG1 THR A 149 -41.466 -35.262 -33.771 1.00 15.79 O ANISOU 959 OG1 THR A 149 1889 1985 2127 211 137 108 O ATOM 960 CG2 THR A 149 -40.253 -37.000 -32.621 1.00 15.51 C ANISOU 960 CG2 THR A 149 1848 1950 2096 124 123 89 C ATOM 961 N ARG A 150 -41.584 -34.260 -31.055 1.00 17.11 N ANISOU 961 N ARG A 150 2064 2137 2299 206 191 74 N ATOM 962 CA ARG A 150 -42.376 -34.151 -29.840 1.00 17.18 C ANISOU 962 CA ARG A 150 2052 2175 2300 219 211 64 C ATOM 963 C ARG A 150 -43.641 -35.001 -29.932 1.00 17.26 C ANISOU 963 C ARG A 150 2003 2244 2312 222 200 84 C ATOM 964 O ARG A 150 -44.416 -34.876 -30.881 1.00 17.76 O ANISOU 964 O ARG A 150 2042 2324 2381 250 186 99 O ATOM 965 CB ARG A 150 -42.719 -32.690 -29.562 1.00 17.66 C ANISOU 965 CB ARG A 150 2138 2209 2363 270 241 51 C ATOM 966 CG ARG A 150 -41.557 -31.892 -28.983 1.00 17.50 C ANISOU 966 CG ARG A 150 2169 2132 2348 257 254 18 C ATOM 967 CD ARG A 150 -41.374 -32.175 -27.498 1.00 18.04 C ANISOU 967 CD ARG A 150 2237 2223 2395 240 261 -12 C ATOM 968 NE ARG A 150 -42.331 -31.433 -26.684 1.00 18.66 N ANISOU 968 NE ARG A 150 2314 2318 2459 290 289 -27 N ATOM 969 CZ ARG A 150 -42.143 -30.202 -26.212 1.00 18.48 C ANISOU 969 CZ ARG A 150 2331 2250 2440 320 308 -64 C ATOM 970 NH1 ARG A 150 -41.016 -29.534 -26.458 1.00 18.82 N ANISOU 970 NH1 ARG A 150 2416 2225 2508 298 302 -89 N ATOM 971 NH2 ARG A 150 -43.095 -29.628 -25.485 1.00 18.69 N ANISOU 971 NH2 ARG A 150 2355 2298 2450 373 335 -77 N ATOM 972 N ALA A 151 -43.815 -35.876 -28.942 1.00 16.98 N ANISOU 972 N ALA A 151 1942 2239 2271 192 206 86 N ATOM 973 CA ALA A 151 -45.025 -36.683 -28.790 1.00 17.24 C ANISOU 973 CA ALA A 151 1912 2324 2316 187 205 108 C ATOM 974 C ALA A 151 -46.244 -35.823 -28.491 1.00 17.82 C ANISOU 974 C ALA A 151 1956 2429 2387 242 232 113 C ATOM 975 O ALA A 151 -47.345 -36.154 -28.903 1.00 17.65 O ANISOU 975 O ALA A 151 1875 2447 2383 251 223 131 O ATOM 976 CB ALA A 151 -44.837 -37.716 -27.699 1.00 17.06 C ANISOU 976 CB ALA A 151 1875 2319 2288 147 218 118 C ATOM 977 N LEU A 152 -46.049 -34.741 -27.743 1.00 17.96 N ANISOU 977 N LEU A 152 2011 2429 2385 279 264 94 N ATOM 978 CA LEU A 152 -47.077 -33.722 -27.577 1.00 18.37 C ANISOU 978 CA LEU A 152 2048 2499 2433 344 291 95 C ATOM 979 C LEU A 152 -46.479 -32.378 -27.942 1.00 18.66 C ANISOU 979 C LEU A 152 2147 2475 2467 381 297 73 C ATOM 980 O LEU A 152 -45.325 -32.106 -27.596 1.00 18.16 O ANISOU 980 O LEU A 152 2137 2365 2398 358 298 47 O ATOM 981 CB LEU A 152 -47.590 -33.653 -26.138 1.00 18.79 C ANISOU 981 CB LEU A 152 2087 2590 2465 364 333 91 C ATOM 982 CG LEU A 152 -48.596 -34.705 -25.664 1.00 19.47 C ANISOU 982 CG LEU A 152 2097 2741 2558 347 347 125 C ATOM 983 CD1 LEU A 152 -48.940 -34.442 -24.201 1.00 19.51 C ANISOU 983 CD1 LEU A 152 2104 2781 2529 380 397 122 C ATOM 984 CD2 LEU A 152 -49.868 -34.716 -26.518 1.00 19.64 C ANISOU 984 CD2 LEU A 152 2050 2802 2611 371 336 149 C ATOM 985 N PRO A 153 -47.274 -31.518 -28.603 1.00 19.10 N ANISOU 985 N PRO A 153 2195 2532 2531 440 303 84 N ATOM 986 CA PRO A 153 -46.777 -30.197 -28.951 1.00 19.18 C ANISOU 986 CA PRO A 153 2267 2476 2547 480 316 70 C ATOM 987 C PRO A 153 -46.474 -29.362 -27.713 1.00 19.49 C ANISOU 987 C PRO A 153 2348 2483 2574 499 350 31 C ATOM 988 O PRO A 153 -47.039 -29.607 -26.636 1.00 19.87 O ANISOU 988 O PRO A 153 2371 2576 2601 510 371 21 O ATOM 989 CB PRO A 153 -47.940 -29.580 -29.727 1.00 19.53 C ANISOU 989 CB PRO A 153 2282 2542 2596 550 320 96 C ATOM 990 CG PRO A 153 -49.150 -30.251 -29.182 1.00 20.29 C ANISOU 990 CG PRO A 153 2302 2719 2687 559 325 108 C ATOM 991 CD PRO A 153 -48.711 -31.658 -28.908 1.00 19.48 C ANISOU 991 CD PRO A 153 2174 2641 2586 479 303 109 C ATOM 992 N PRO A 154 -45.602 -28.363 -27.863 1.00 19.62 N ANISOU 992 N PRO A 154 2429 2421 2606 504 358 7 N ATOM 993 CA PRO A 154 -45.316 -27.486 -26.740 1.00 19.94 C ANISOU 993 CA PRO A 154 2513 2424 2639 524 384 -42 C ATOM 994 C PRO A 154 -46.497 -26.609 -26.349 1.00 20.60 C ANISOU 994 C PRO A 154 2591 2520 2714 607 418 -46 C ATOM 995 O PRO A 154 -47.359 -26.292 -27.181 1.00 21.21 O ANISOU 995 O PRO A 154 2646 2610 2803 657 423 -10 O ATOM 996 CB PRO A 154 -44.157 -26.628 -27.260 1.00 19.69 C ANISOU 996 CB PRO A 154 2543 2297 2642 506 381 -59 C ATOM 997 CG PRO A 154 -44.347 -26.600 -28.710 1.00 20.21 C ANISOU 997 CG PRO A 154 2599 2353 2727 519 373 -8 C ATOM 998 CD PRO A 154 -44.849 -27.968 -29.065 1.00 19.40 C ANISOU 998 CD PRO A 154 2435 2334 2604 494 346 25 C ATOM 999 N VAL A 155 -46.530 -26.225 -25.077 1.00 21.10 N ANISOU 999 N VAL A 155 2676 2586 2754 628 440 -92 N ATOM 1000 CA VAL A 155 -47.462 -25.216 -24.604 1.00 21.89 C ANISOU 1000 CA VAL A 155 2787 2684 2846 713 477 -109 C ATOM 1001 C VAL A 155 -47.077 -23.904 -25.282 1.00 23.02 C ANISOU 1001 C VAL A 155 2991 2724 3030 743 485 -121 C ATOM 1002 O VAL A 155 -45.910 -23.506 -25.253 1.00 22.46 O ANISOU 1002 O VAL A 155 2973 2577 2983 700 474 -155 O ATOM 1003 CB VAL A 155 -47.409 -25.073 -23.074 1.00 22.37 C ANISOU 1003 CB VAL A 155 2869 2766 2865 730 497 -165 C ATOM 1004 CG1 VAL A 155 -48.322 -23.945 -22.603 1.00 22.29 C ANISOU 1004 CG1 VAL A 155 2878 2745 2846 826 538 -189 C ATOM 1005 CG2 VAL A 155 -47.790 -26.399 -22.404 1.00 21.25 C ANISOU 1005 CG2 VAL A 155 2668 2724 2684 702 498 -139 C ATOM 1006 N ALA A 156 -48.054 -23.258 -25.913 1.00 24.18 N ANISOU 1006 N ALA A 156 3128 2871 3190 817 505 -88 N ATOM 1007 CA ALA A 156 -47.815 -22.028 -26.662 1.00 25.57 C ANISOU 1007 CA ALA A 156 3361 2948 3407 856 519 -83 C ATOM 1008 C ALA A 156 -47.219 -20.947 -25.761 1.00 27.11 C ANISOU 1008 C ALA A 156 3629 3053 3617 868 540 -155 C ATOM 1009 O ALA A 156 -47.498 -20.905 -24.563 1.00 27.20 O ANISOU 1009 O ALA A 156 3643 3095 3596 890 552 -205 O ATOM 1010 CB ALA A 156 -49.112 -21.534 -27.301 1.00 26.08 C ANISOU 1010 CB ALA A 156 3398 3041 3472 950 538 -37 C ATOM 1011 N ASP A 157 -46.400 -20.079 -26.348 1.00 28.99 N ANISOU 1011 N ASP A 157 3926 3180 3907 854 544 -160 N ATOM 1012 CA ASP A 157 -45.693 -19.041 -25.587 1.00 30.87 C ANISOU 1012 CA ASP A 157 4236 3317 4177 850 557 -234 C ATOM 1013 C ASP A 157 -46.628 -18.060 -24.884 1.00 32.34 C ANISOU 1013 C ASP A 157 4451 3485 4353 948 593 -271 C ATOM 1014 O ASP A 157 -46.329 -17.605 -23.778 1.00 33.40 O ANISOU 1014 O ASP A 157 4624 3587 4479 951 596 -353 O ATOM 1015 CB ASP A 157 -44.729 -18.264 -26.494 1.00 31.46 C ANISOU 1015 CB ASP A 157 4362 3270 4323 817 563 -219 C ATOM 1016 CG ASP A 157 -43.563 -19.111 -26.988 1.00 32.58 C ANISOU 1016 CG ASP A 157 4484 3417 4477 718 530 -200 C ATOM 1017 OD1 ASP A 157 -43.291 -20.181 -26.405 1.00 34.49 O ANISOU 1017 OD1 ASP A 157 4688 3738 4677 667 500 -220 O ATOM 1018 OD2 ASP A 157 -42.906 -18.692 -27.965 1.00 36.23 O ANISOU 1018 OD2 ASP A 157 4970 3804 4990 694 540 -162 O ATOM 1019 N ASP A 158 -47.759 -17.737 -25.505 1.00 33.15 N ANISOU 1019 N ASP A 158 4533 3611 4453 1032 618 -216 N ATOM 1020 CA ASP A 158 -48.662 -16.729 -24.940 1.00 34.44 C ANISOU 1020 CA ASP A 158 4724 3749 4611 1136 656 -246 C ATOM 1021 C ASP A 158 -49.726 -17.286 -23.982 1.00 34.11 C ANISOU 1021 C ASP A 158 4628 3829 4502 1187 668 -260 C ATOM 1022 O ASP A 158 -50.626 -16.556 -23.569 1.00 35.08 O ANISOU 1022 O ASP A 158 4762 3953 4614 1284 704 -275 O ATOM 1023 CB ASP A 158 -49.299 -15.879 -26.052 1.00 35.47 C ANISOU 1023 CB ASP A 158 4870 3829 4779 1217 683 -182 C ATOM 1024 CG ASP A 158 -50.207 -16.673 -26.968 1.00 36.85 C ANISOU 1024 CG ASP A 158 4965 4113 4925 1243 671 -96 C ATOM 1025 OD1 ASP A 158 -50.881 -16.035 -27.803 1.00 40.46 O ANISOU 1025 OD1 ASP A 158 5426 4551 5398 1324 690 -43 O ATOM 1026 OD2 ASP A 158 -50.244 -17.920 -26.870 1.00 39.99 O ANISOU 1026 OD2 ASP A 158 5295 4612 5285 1186 641 -83 O ATOM 1027 N CYS A 159 -49.614 -18.560 -23.607 1.00 32.79 N ANISOU 1027 N CYS A 159 4402 3762 4293 1124 643 -252 N ATOM 1028 CA CYS A 159 -50.538 -19.141 -22.634 1.00 32.57 C ANISOU 1028 CA CYS A 159 4321 3848 4205 1163 661 -259 C ATOM 1029 C CYS A 159 -50.301 -18.541 -21.242 1.00 33.06 C ANISOU 1029 C CYS A 159 4442 3885 4236 1194 680 -351 C ATOM 1030 O CYS A 159 -49.156 -18.251 -20.876 1.00 33.47 O ANISOU 1030 O CYS A 159 4553 3862 4303 1139 658 -413 O ATOM 1031 CB CYS A 159 -50.391 -20.665 -22.586 1.00 31.63 C ANISOU 1031 CB CYS A 159 4133 3829 4056 1083 633 -224 C ATOM 1032 SG CYS A 159 -50.850 -21.512 -24.121 1.00 30.30 S ANISOU 1032 SG CYS A 159 3888 3711 3913 1055 606 -128 S ATOM 1033 N PRO A 160 -51.377 -18.363 -20.460 1.00 33.09 N ANISOU 1033 N PRO A 160 4423 3956 4194 1283 720 -361 N ATOM 1034 CA PRO A 160 -51.265 -17.682 -19.168 1.00 33.65 C ANISOU 1034 CA PRO A 160 4555 4004 4227 1333 740 -453 C ATOM 1035 C PRO A 160 -50.457 -18.422 -18.093 1.00 32.95 C ANISOU 1035 C PRO A 160 4475 3961 4085 1269 716 -505 C ATOM 1036 O PRO A 160 -49.935 -17.778 -17.183 1.00 33.82 O ANISOU 1036 O PRO A 160 4653 4024 4174 1287 714 -597 O ATOM 1037 CB PRO A 160 -52.725 -17.511 -18.729 1.00 34.41 C ANISOU 1037 CB PRO A 160 4607 4185 4282 1447 793 -431 C ATOM 1038 CG PRO A 160 -53.488 -18.511 -19.494 1.00 33.87 C ANISOU 1038 CG PRO A 160 4437 4215 4218 1428 791 -332 C ATOM 1039 CD PRO A 160 -52.781 -18.664 -20.798 1.00 33.24 C ANISOU 1039 CD PRO A 160 4362 4070 4199 1352 748 -291 C ATOM 1040 N THR A 161 -50.366 -19.749 -18.186 1.00 31.58 N ANISOU 1040 N THR A 161 4234 3877 3888 1201 698 -450 N ATOM 1041 CA THR A 161 -49.597 -20.541 -17.216 1.00 30.77 C ANISOU 1041 CA THR A 161 4136 3822 3732 1144 675 -487 C ATOM 1042 C THR A 161 -48.650 -21.507 -17.928 1.00 29.69 C ANISOU 1042 C THR A 161 3975 3680 3627 1031 628 -447 C ATOM 1043 O THR A 161 -48.838 -21.804 -19.112 1.00 28.87 O ANISOU 1043 O THR A 161 3833 3567 3571 1001 618 -379 O ATOM 1044 CB THR A 161 -50.519 -21.330 -16.245 1.00 30.98 C ANISOU 1044 CB THR A 161 4107 3983 3680 1191 715 -460 C ATOM 1045 OG1 THR A 161 -51.142 -22.421 -16.933 1.00 29.12 O ANISOU 1045 OG1 THR A 161 3781 3824 3461 1155 719 -361 O ATOM 1046 CG2 THR A 161 -51.589 -20.425 -15.637 1.00 31.87 C ANISOU 1046 CG2 THR A 161 4233 4114 3761 1314 770 -487 C ATOM 1047 N PRO A 162 -47.620 -22.005 -17.214 1.00 29.33 N ANISOU 1047 N PRO A 162 3951 3644 3549 972 595 -491 N ATOM 1048 CA PRO A 162 -46.663 -22.915 -17.853 1.00 28.32 C ANISOU 1048 CA PRO A 162 3802 3509 3450 869 551 -457 C ATOM 1049 C PRO A 162 -47.311 -24.147 -18.489 1.00 27.59 C ANISOU 1049 C PRO A 162 3627 3498 3359 841 557 -360 C ATOM 1050 O PRO A 162 -46.907 -24.550 -19.580 1.00 26.61 O ANISOU 1050 O PRO A 162 3484 3344 3283 782 530 -317 O ATOM 1051 CB PRO A 162 -45.737 -23.313 -16.700 1.00 28.54 C ANISOU 1051 CB PRO A 162 3857 3566 3422 838 525 -518 C ATOM 1052 CG PRO A 162 -45.798 -22.158 -15.765 1.00 29.58 C ANISOU 1052 CG PRO A 162 4052 3663 3525 908 537 -612 C ATOM 1053 CD PRO A 162 -47.219 -21.682 -15.830 1.00 30.03 C ANISOU 1053 CD PRO A 162 4090 3745 3573 1002 593 -581 C ATOM 1054 N MET A 163 -48.318 -24.718 -17.830 1.00 27.64 N ANISOU 1054 N MET A 163 3584 3602 3315 885 594 -327 N ATOM 1055 CA MET A 163 -49.006 -25.906 -18.355 1.00 27.28 C ANISOU 1055 CA MET A 163 3455 3631 3279 856 600 -239 C ATOM 1056 C MET A 163 -50.188 -25.592 -19.273 1.00 27.16 C ANISOU 1056 C MET A 163 3391 3626 3303 902 621 -189 C ATOM 1057 O MET A 163 -50.814 -26.510 -19.804 1.00 26.97 O ANISOU 1057 O MET A 163 3292 3659 3295 876 621 -122 O ATOM 1058 CB MET A 163 -49.470 -26.808 -17.206 1.00 27.69 C ANISOU 1058 CB MET A 163 3469 3787 3266 869 632 -217 C ATOM 1059 CG MET A 163 -48.333 -27.414 -16.421 1.00 28.17 C ANISOU 1059 CG MET A 163 3563 3855 3284 819 605 -248 C ATOM 1060 SD MET A 163 -47.190 -28.258 -17.517 1.00 28.14 S ANISOU 1060 SD MET A 163 3552 3802 3337 707 544 -220 S ATOM 1061 CE MET A 163 -46.020 -28.933 -16.334 1.00 29.01 C ANISOU 1061 CE MET A 163 3697 3943 3383 673 521 -255 C ATOM 1062 N GLY A 164 -50.481 -24.310 -19.471 1.00 27.41 N ANISOU 1062 N GLY A 164 3463 3599 3352 970 637 -221 N ATOM 1063 CA GLY A 164 -51.561 -23.898 -20.357 1.00 27.73 C ANISOU 1063 CA GLY A 164 3462 3647 3427 1025 655 -175 C ATOM 1064 C GLY A 164 -52.411 -22.853 -19.677 1.00 28.64 C ANISOU 1064 C GLY A 164 3597 3768 3517 1135 704 -207 C ATOM 1065 O GLY A 164 -52.133 -21.664 -19.788 1.00 28.88 O ANISOU 1065 O GLY A 164 3697 3709 3567 1178 707 -253 O ATOM 1066 N VAL A 165 -53.435 -23.310 -18.962 1.00 29.25 N ANISOU 1066 N VAL A 165 3611 3946 3554 1181 745 -180 N ATOM 1067 CA VAL A 165 -54.309 -22.431 -18.177 1.00 30.71 C ANISOU 1067 CA VAL A 165 3808 4155 3706 1294 800 -209 C ATOM 1068 C VAL A 165 -54.388 -22.816 -16.694 1.00 31.65 C ANISOU 1068 C VAL A 165 3930 4349 3748 1317 836 -236 C ATOM 1069 O VAL A 165 -54.759 -21.984 -15.868 1.00 32.29 O ANISOU 1069 O VAL A 165 4050 4432 3787 1409 876 -285 O ATOM 1070 CB VAL A 165 -55.748 -22.387 -18.751 1.00 31.25 C ANISOU 1070 CB VAL A 165 3790 4288 3797 1360 830 -144 C ATOM 1071 CG1 VAL A 165 -55.739 -21.868 -20.180 1.00 30.86 C ANISOU 1071 CG1 VAL A 165 3745 4170 3810 1360 797 -119 C ATOM 1072 CG2 VAL A 165 -56.415 -23.755 -18.664 1.00 30.99 C ANISOU 1072 CG2 VAL A 165 3647 4370 3758 1316 841 -73 C ATOM 1073 N LYS A 166 -54.049 -24.062 -16.359 1.00 31.61 N ANISOU 1073 N LYS A 166 3887 4404 3721 1242 825 -203 N ATOM 1074 CA LYS A 166 -54.119 -24.537 -14.973 1.00 32.78 C ANISOU 1074 CA LYS A 166 4034 4631 3789 1266 863 -214 C ATOM 1075 C LYS A 166 -52.871 -24.158 -14.179 1.00 33.06 C ANISOU 1075 C LYS A 166 4168 4614 3778 1252 834 -303 C ATOM 1076 O LYS A 166 -51.814 -23.895 -14.748 1.00 32.35 O ANISOU 1076 O LYS A 166 4129 4433 3727 1191 779 -340 O ATOM 1077 CB LYS A 166 -54.285 -26.057 -14.925 1.00 32.45 C ANISOU 1077 CB LYS A 166 3911 4671 3746 1194 868 -134 C ATOM 1078 CG LYS A 166 -55.578 -26.589 -15.518 1.00 33.55 C ANISOU 1078 CG LYS A 166 3939 4880 3930 1202 898 -50 C ATOM 1079 CD LYS A 166 -55.562 -28.120 -15.525 1.00 34.42 C ANISOU 1079 CD LYS A 166 3979 5047 4053 1113 894 22 C ATOM 1080 CE LYS A 166 -56.819 -28.718 -16.145 1.00 35.13 C ANISOU 1080 CE LYS A 166 3948 5202 4199 1107 917 101 C ATOM 1081 NZ LYS A 166 -58.046 -28.350 -15.403 1.00 36.19 N ANISOU 1081 NZ LYS A 166 4030 5419 4302 1204 993 122 N ATOM 1082 N GLY A 167 -53.005 -24.150 -12.856 1.00 34.48 N ANISOU 1082 N GLY A 167 4370 4857 3872 1311 871 -336 N ATOM 1083 CA GLY A 167 -51.868 -23.949 -11.963 1.00 35.11 C ANISOU 1083 CA GLY A 167 4534 4911 3895 1301 839 -421 C ATOM 1084 C GLY A 167 -51.529 -22.493 -11.712 1.00 36.52 C ANISOU 1084 C GLY A 167 4804 5002 4070 1362 827 -530 C ATOM 1085 O GLY A 167 -52.232 -21.584 -12.160 1.00 36.88 O ANISOU 1085 O GLY A 167 4854 5005 4152 1424 852 -537 O ATOM 1086 N ASN A 168 -50.444 -22.285 -10.973 1.00 37.44 N ANISOU 1086 N ASN A 168 4992 5090 4143 1344 787 -617 N ATOM 1087 CA ASN A 168 -49.949 -20.952 -10.659 1.00 38.73 C ANISOU 1087 CA ASN A 168 5248 5160 4308 1387 764 -736 C ATOM 1088 C ASN A 168 -49.178 -20.365 -11.833 1.00 38.44 C ANISOU 1088 C ASN A 168 5239 4987 4379 1313 714 -754 C ATOM 1089 O ASN A 168 -48.862 -21.070 -12.794 1.00 37.22 O ANISOU 1089 O ASN A 168 5039 4821 4282 1227 689 -683 O ATOM 1090 CB ASN A 168 -49.048 -21.002 -9.418 1.00 39.51 C ANISOU 1090 CB ASN A 168 5406 5287 4321 1391 732 -827 C ATOM 1091 CG ASN A 168 -49.784 -21.481 -8.174 1.00 41.00 C ANISOU 1091 CG ASN A 168 5578 5610 4389 1479 788 -812 C ATOM 1092 OD1 ASN A 168 -49.299 -22.351 -7.449 1.00 42.73 O ANISOU 1092 OD1 ASN A 168 5792 5907 4537 1457 775 -801 O ATOM 1093 ND2 ASN A 168 -50.958 -20.918 -7.925 1.00 42.14 N ANISOU 1093 ND2 ASN A 168 5715 5787 4510 1585 855 -805 N ATOM 1094 N LYS A 169 -48.874 -19.072 -11.743 1.00 39.49 N ANISOU 1094 N LYS A 169 5450 5017 4540 1349 702 -850 N ATOM 1095 CA LYS A 169 -48.154 -18.349 -12.799 1.00 39.42 C ANISOU 1095 CA LYS A 169 5475 4866 4637 1289 664 -869 C ATOM 1096 C LYS A 169 -46.767 -18.930 -13.074 1.00 38.50 C ANISOU 1096 C LYS A 169 5360 4719 4551 1168 599 -879 C ATOM 1097 O LYS A 169 -46.289 -18.892 -14.207 1.00 37.73 O ANISOU 1097 O LYS A 169 5252 4545 4539 1098 577 -840 O ATOM 1098 CB LYS A 169 -48.022 -16.867 -12.425 1.00 41.00 C ANISOU 1098 CB LYS A 169 5764 4957 4857 1350 664 -982 C ATOM 1099 CG LYS A 169 -47.448 -15.975 -13.529 1.00 41.99 C ANISOU 1099 CG LYS A 169 5927 4926 5101 1302 643 -992 C ATOM 1100 CD LYS A 169 -47.282 -14.534 -13.051 1.00 45.04 C ANISOU 1100 CD LYS A 169 6406 5196 5513 1359 643 -1111 C ATOM 1101 CE LYS A 169 -48.616 -13.804 -12.971 1.00 46.65 C ANISOU 1101 CE LYS A 169 6621 5403 5700 1490 708 -1100 C ATOM 1102 NZ LYS A 169 -48.486 -12.481 -12.311 1.00 49.13 N ANISOU 1102 NZ LYS A 169 7031 5612 6025 1556 710 -1228 N ATOM 1103 N GLU A 170 -46.119 -19.442 -12.032 1.00 38.34 N ANISOU 1103 N GLU A 170 5352 4759 4456 1151 569 -931 N ATOM 1104 CA GLU A 170 -44.823 -20.099 -12.174 1.00 37.60 C ANISOU 1104 CA GLU A 170 5251 4655 4380 1045 508 -938 C ATOM 1105 C GLU A 170 -44.875 -21.471 -11.527 1.00 36.15 C ANISOU 1105 C GLU A 170 5019 4606 4110 1035 511 -884 C ATOM 1106 O GLU A 170 -45.584 -21.676 -10.538 1.00 36.82 O ANISOU 1106 O GLU A 170 5101 4785 4102 1114 548 -888 O ATOM 1107 CB GLU A 170 -43.717 -19.265 -11.518 1.00 38.84 C ANISOU 1107 CB GLU A 170 5480 4738 4541 1028 454 -1073 C ATOM 1108 CG GLU A 170 -43.535 -17.864 -12.113 1.00 41.45 C ANISOU 1108 CG GLU A 170 5865 4915 4970 1028 451 -1133 C ATOM 1109 CD GLU A 170 -43.055 -17.874 -13.562 1.00 42.41 C ANISOU 1109 CD GLU A 170 5962 4947 5205 941 441 -1063 C ATOM 1110 OE1 GLU A 170 -42.408 -18.854 -13.992 1.00 44.59 O ANISOU 1110 OE1 GLU A 170 6192 5260 5490 860 412 -1006 O ATOM 1111 OE2 GLU A 170 -43.326 -16.887 -14.279 1.00 45.23 O ANISOU 1111 OE2 GLU A 170 6348 5196 5641 960 464 -1062 O ATOM 1112 N LEU A 171 -44.124 -22.411 -12.092 1.00 34.10 N ANISOU 1112 N LEU A 171 4722 4355 3881 942 476 -830 N ATOM 1113 CA LEU A 171 -43.987 -23.736 -11.501 1.00 32.90 C ANISOU 1113 CA LEU A 171 4530 4315 3656 924 472 -780 C ATOM 1114 C LEU A 171 -43.139 -23.640 -10.233 1.00 33.04 C ANISOU 1114 C LEU A 171 4595 4367 3592 940 432 -877 C ATOM 1115 O LEU A 171 -42.399 -22.667 -10.052 1.00 33.10 O ANISOU 1115 O LEU A 171 4657 4295 3624 932 390 -983 O ATOM 1116 CB LEU A 171 -43.363 -24.711 -12.505 1.00 31.64 C ANISOU 1116 CB LEU A 171 4323 4143 3556 823 443 -703 C ATOM 1117 CG LEU A 171 -44.319 -25.156 -13.613 1.00 30.75 C ANISOU 1117 CG LEU A 171 4152 4035 3498 814 482 -596 C ATOM 1118 CD1 LEU A 171 -43.566 -25.734 -14.814 1.00 29.86 C ANISOU 1118 CD1 LEU A 171 4011 3874 3460 718 445 -547 C ATOM 1119 CD2 LEU A 171 -45.342 -26.153 -13.075 1.00 30.33 C ANISOU 1119 CD2 LEU A 171 4045 4098 3382 853 531 -520 C ATOM 1120 N PRO A 172 -43.252 -24.639 -9.339 1.00 32.58 N ANISOU 1120 N PRO A 172 4516 4425 3438 965 444 -842 N ATOM 1121 CA PRO A 172 -42.445 -24.600 -8.120 1.00 32.76 C ANISOU 1121 CA PRO A 172 4582 4493 3370 990 402 -932 C ATOM 1122 C PRO A 172 -40.943 -24.622 -8.397 1.00 31.91 C ANISOU 1122 C PRO A 172 4486 4328 3310 899 319 -986 C ATOM 1123 O PRO A 172 -40.504 -25.134 -9.432 1.00 30.14 O ANISOU 1123 O PRO A 172 4223 4061 3166 815 303 -923 O ATOM 1124 CB PRO A 172 -42.871 -25.867 -7.362 1.00 32.83 C ANISOU 1124 CB PRO A 172 4556 4638 3281 1024 439 -847 C ATOM 1125 CG PRO A 172 -43.579 -26.713 -8.352 1.00 32.40 C ANISOU 1125 CG PRO A 172 4433 4589 3290 981 482 -716 C ATOM 1126 CD PRO A 172 -44.183 -25.781 -9.346 1.00 32.24 C ANISOU 1126 CD PRO A 172 4410 4477 3362 981 501 -721 C ATOM 1127 N ASP A 173 -40.181 -24.045 -7.471 1.00 32.28 N ANISOU 1127 N ASP A 173 4584 4376 3305 921 267 -1106 N ATOM 1128 CA ASP A 173 -38.718 -24.048 -7.513 1.00 32.27 C ANISOU 1128 CA ASP A 173 4588 4336 3337 844 184 -1172 C ATOM 1129 C ASP A 173 -38.201 -25.461 -7.799 1.00 30.79 C ANISOU 1129 C ASP A 173 4347 4211 3143 785 171 -1073 C ATOM 1130 O ASP A 173 -38.482 -26.388 -7.042 1.00 30.24 O ANISOU 1130 O ASP A 173 4264 4253 2974 830 191 -1022 O ATOM 1131 CB ASP A 173 -38.184 -23.542 -6.165 1.00 34.03 C ANISOU 1131 CB ASP A 173 4863 4602 3464 899 133 -1305 C ATOM 1132 CG ASP A 173 -36.691 -23.266 -6.175 1.00 35.91 C ANISOU 1132 CG ASP A 173 5106 4788 3749 821 40 -1398 C ATOM 1133 OD1 ASP A 173 -36.246 -22.509 -5.287 1.00 41.37 O ANISOU 1133 OD1 ASP A 173 5845 5478 4396 855 -10 -1533 O ATOM 1134 OD2 ASP A 173 -35.965 -23.792 -7.038 1.00 39.15 O ANISOU 1134 OD2 ASP A 173 5473 5164 4239 730 17 -1343 O ATOM 1135 N SER A 174 -37.452 -25.623 -8.892 1.00 29.61 N ANISOU 1135 N SER A 174 4167 3987 3098 690 142 -1043 N ATOM 1136 CA SER A 174 -36.969 -26.945 -9.299 1.00 28.51 C ANISOU 1136 CA SER A 174 3977 3893 2963 634 131 -949 C ATOM 1137 C SER A 174 -35.986 -27.545 -8.285 1.00 28.97 C ANISOU 1137 C SER A 174 4039 4033 2936 640 74 -990 C ATOM 1138 O SER A 174 -35.954 -28.761 -8.108 1.00 28.13 O ANISOU 1138 O SER A 174 3903 4004 2781 641 85 -906 O ATOM 1139 CB SER A 174 -36.352 -26.913 -10.710 1.00 27.68 C ANISOU 1139 CB SER A 174 3843 3690 2985 538 114 -915 C ATOM 1140 OG SER A 174 -35.248 -26.028 -10.788 1.00 28.06 O ANISOU 1140 OG SER A 174 3910 3660 3090 491 55 -1015 O ATOM 1141 N LYS A 175 -35.203 -26.694 -7.620 1.00 30.08 N ANISOU 1141 N LYS A 175 4216 4155 3060 646 13 -1119 N ATOM 1142 CA LYS A 175 -34.306 -27.143 -6.546 1.00 30.92 C ANISOU 1142 CA LYS A 175 4328 4350 3072 667 -49 -1173 C ATOM 1143 C LYS A 175 -35.108 -27.735 -5.389 1.00 31.24 C ANISOU 1143 C LYS A 175 4387 4517 2967 770 -8 -1139 C ATOM 1144 O LYS A 175 -34.708 -28.737 -4.797 1.00 31.18 O ANISOU 1144 O LYS A 175 4365 4604 2879 788 -24 -1097 O ATOM 1145 CB LYS A 175 -33.429 -25.988 -6.038 1.00 32.32 C ANISOU 1145 CB LYS A 175 4540 4480 3262 657 -125 -1334 C ATOM 1146 CG LYS A 175 -32.428 -26.382 -4.936 1.00 34.22 C ANISOU 1146 CG LYS A 175 4782 4816 3404 679 -203 -1404 C ATOM 1147 CD LYS A 175 -31.689 -25.173 -4.372 1.00 37.07 C ANISOU 1147 CD LYS A 175 5177 5131 3777 674 -282 -1576 C ATOM 1148 CE LYS A 175 -30.892 -25.547 -3.118 1.00 38.93 C ANISOU 1148 CE LYS A 175 5419 5484 3887 721 -359 -1652 C ATOM 1149 NZ LYS A 175 -30.117 -24.408 -2.537 1.00 40.77 N ANISOU 1149 NZ LYS A 175 5680 5677 4133 712 -448 -1833 N ATOM 1150 N GLU A 176 -36.240 -27.116 -5.072 1.00 31.64 N ANISOU 1150 N GLU A 176 4469 4569 2983 842 49 -1152 N ATOM 1151 CA GLU A 176 -37.094 -27.598 -3.991 1.00 32.35 C ANISOU 1151 CA GLU A 176 4576 4780 2937 946 101 -1115 C ATOM 1152 C GLU A 176 -37.717 -28.951 -4.336 1.00 30.75 C ANISOU 1152 C GLU A 176 4323 4633 2729 937 167 -952 C ATOM 1153 O GLU A 176 -37.747 -29.850 -3.501 1.00 30.93 O ANISOU 1153 O GLU A 176 4343 4763 2647 987 182 -900 O ATOM 1154 CB GLU A 176 -38.177 -26.571 -3.657 1.00 33.52 C ANISOU 1154 CB GLU A 176 4763 4911 3060 1025 152 -1166 C ATOM 1155 CG GLU A 176 -38.826 -26.793 -2.300 1.00 36.82 C ANISOU 1155 CG GLU A 176 5212 5458 3320 1146 191 -1169 C ATOM 1156 CD GLU A 176 -39.408 -25.532 -1.694 1.00 39.99 C ANISOU 1156 CD GLU A 176 5673 5844 3679 1232 204 -1282 C ATOM 1157 OE1 GLU A 176 -39.801 -25.577 -0.513 1.00 43.69 O ANISOU 1157 OE1 GLU A 176 6175 6418 4008 1338 227 -1307 O ATOM 1158 OE2 GLU A 176 -39.479 -24.495 -2.389 1.00 42.91 O ANISOU 1158 OE2 GLU A 176 6058 6094 4151 1199 195 -1343 O ATOM 1159 N VAL A 177 -38.209 -29.096 -5.563 1.00 29.17 N ANISOU 1159 N VAL A 177 4084 4359 2640 876 205 -873 N ATOM 1160 CA VAL A 177 -38.739 -30.384 -6.025 1.00 28.09 C ANISOU 1160 CA VAL A 177 3896 4260 2519 852 258 -727 C ATOM 1161 C VAL A 177 -37.651 -31.458 -5.933 1.00 27.70 C ANISOU 1161 C VAL A 177 3827 4246 2452 809 211 -691 C ATOM 1162 O VAL A 177 -37.872 -32.543 -5.387 1.00 27.73 O ANISOU 1162 O VAL A 177 3817 4334 2386 840 243 -605 O ATOM 1163 CB VAL A 177 -39.253 -30.301 -7.474 1.00 27.30 C ANISOU 1163 CB VAL A 177 3757 4068 2548 785 286 -667 C ATOM 1164 CG1 VAL A 177 -39.710 -31.676 -7.962 1.00 26.11 C ANISOU 1164 CG1 VAL A 177 3552 3950 2418 753 330 -529 C ATOM 1165 CG2 VAL A 177 -40.381 -29.276 -7.582 1.00 27.73 C ANISOU 1165 CG2 VAL A 177 3826 4091 2619 837 336 -693 C ATOM 1166 N LEU A 178 -36.475 -31.126 -6.457 1.00 27.09 N ANISOU 1166 N LEU A 178 3749 4103 2440 740 137 -755 N ATOM 1167 CA LEU A 178 -35.301 -31.999 -6.420 1.00 26.85 C ANISOU 1167 CA LEU A 178 3700 4101 2403 699 82 -737 C ATOM 1168 C LEU A 178 -34.995 -32.472 -4.997 1.00 27.68 C ANISOU 1168 C LEU A 178 3828 4323 2364 777 64 -754 C ATOM 1169 O LEU A 178 -34.959 -33.672 -4.727 1.00 27.22 O ANISOU 1169 O LEU A 178 3752 4331 2259 791 84 -659 O ATOM 1170 CB LEU A 178 -34.093 -31.248 -6.993 1.00 26.96 C ANISOU 1170 CB LEU A 178 3712 4031 2499 627 4 -832 C ATOM 1171 CG LEU A 178 -32.724 -31.937 -6.984 1.00 27.64 C ANISOU 1171 CG LEU A 178 3774 4140 2588 583 -64 -836 C ATOM 1172 CD1 LEU A 178 -32.667 -33.040 -8.022 1.00 26.23 C ANISOU 1172 CD1 LEU A 178 3551 3937 2478 524 -37 -717 C ATOM 1173 CD2 LEU A 178 -31.610 -30.914 -7.216 1.00 29.80 C ANISOU 1173 CD2 LEU A 178 4050 4345 2929 529 -140 -957 C ATOM 1174 N GLU A 179 -34.792 -31.525 -4.089 1.00 28.68 N ANISOU 1174 N GLU A 179 3999 4476 2420 833 26 -874 N ATOM 1175 CA GLU A 179 -34.378 -31.858 -2.725 1.00 29.85 C ANISOU 1175 CA GLU A 179 4175 4743 2424 914 -5 -908 C ATOM 1176 C GLU A 179 -35.457 -32.589 -1.928 1.00 30.31 C ANISOU 1176 C GLU A 179 4243 4902 2371 1005 81 -809 C ATOM 1177 O GLU A 179 -35.145 -33.510 -1.179 1.00 30.71 O ANISOU 1177 O GLU A 179 4295 5047 2327 1050 78 -757 O ATOM 1178 CB GLU A 179 -33.920 -30.601 -1.979 1.00 31.16 C ANISOU 1178 CB GLU A 179 4387 4908 2544 952 -72 -1075 C ATOM 1179 CG GLU A 179 -32.600 -30.052 -2.504 1.00 31.84 C ANISOU 1179 CG GLU A 179 4458 4918 2723 864 -168 -1173 C ATOM 1180 CD GLU A 179 -31.975 -29.023 -1.587 1.00 34.92 C ANISOU 1180 CD GLU A 179 4888 5325 3055 901 -249 -1343 C ATOM 1181 OE1 GLU A 179 -32.717 -28.306 -0.880 1.00 35.05 O ANISOU 1181 OE1 GLU A 179 4955 5364 3000 980 -224 -1406 O ATOM 1182 OE2 GLU A 179 -30.728 -28.940 -1.573 1.00 37.19 O ANISOU 1182 OE2 GLU A 179 5155 5605 3369 852 -339 -1415 O ATOM 1183 N LYS A 180 -36.715 -32.191 -2.098 1.00 30.22 N ANISOU 1183 N LYS A 180 4236 4871 2376 1034 159 -779 N ATOM 1184 CA LYS A 180 -37.805 -32.758 -1.301 1.00 31.05 C ANISOU 1184 CA LYS A 180 4345 5073 2379 1123 248 -690 C ATOM 1185 C LYS A 180 -38.189 -34.189 -1.700 1.00 30.12 C ANISOU 1185 C LYS A 180 4179 4975 2291 1091 309 -525 C ATOM 1186 O LYS A 180 -38.462 -35.010 -0.821 1.00 30.86 O ANISOU 1186 O LYS A 180 4277 5166 2280 1159 354 -447 O ATOM 1187 CB LYS A 180 -39.040 -31.848 -1.329 1.00 31.47 C ANISOU 1187 CB LYS A 180 4412 5104 2442 1169 313 -713 C ATOM 1188 CG LYS A 180 -38.865 -30.559 -0.525 1.00 33.83 C ANISOU 1188 CG LYS A 180 4773 5414 2669 1239 270 -869 C ATOM 1189 CD LYS A 180 -40.150 -29.754 -0.465 1.00 35.62 C ANISOU 1189 CD LYS A 180 5013 5629 2892 1301 345 -880 C ATOM 1190 CE LYS A 180 -40.043 -28.577 0.501 1.00 37.82 C ANISOU 1190 CE LYS A 180 5361 5930 3079 1390 310 -1034 C ATOM 1191 NZ LYS A 180 -40.164 -28.986 1.918 1.00 40.79 N ANISOU 1191 NZ LYS A 180 5771 6451 3277 1506 331 -1032 N ATOM 1192 N VAL A 181 -38.205 -34.500 -2.997 1.00 29.06 N ANISOU 1192 N VAL A 181 4000 4748 2293 993 312 -470 N ATOM 1193 CA VAL A 181 -38.706 -35.810 -3.443 1.00 28.37 C ANISOU 1193 CA VAL A 181 3866 4667 2246 959 373 -321 C ATOM 1194 C VAL A 181 -37.816 -36.635 -4.389 1.00 27.51 C ANISOU 1194 C VAL A 181 3726 4498 2228 865 329 -277 C ATOM 1195 O VAL A 181 -38.141 -37.788 -4.660 1.00 26.96 O ANISOU 1195 O VAL A 181 3625 4435 2186 842 373 -160 O ATOM 1196 CB VAL A 181 -40.118 -35.675 -4.076 1.00 28.04 C ANISOU 1196 CB VAL A 181 3790 4591 2274 949 456 -258 C ATOM 1197 CG1 VAL A 181 -41.070 -35.001 -3.095 1.00 29.17 C ANISOU 1197 CG1 VAL A 181 3958 4804 2321 1052 513 -284 C ATOM 1198 CG2 VAL A 181 -40.057 -34.910 -5.395 1.00 27.22 C ANISOU 1198 CG2 VAL A 181 3669 4372 2301 870 422 -308 C ATOM 1199 N LEU A 182 -36.709 -36.075 -4.881 1.00 27.23 N ANISOU 1199 N LEU A 182 3698 4405 2242 813 244 -369 N ATOM 1200 CA LEU A 182 -35.854 -36.791 -5.833 1.00 26.42 C ANISOU 1200 CA LEU A 182 3565 4247 2228 728 205 -331 C ATOM 1201 C LEU A 182 -34.522 -37.258 -5.254 1.00 26.95 C ANISOU 1201 C LEU A 182 3642 4361 2236 739 136 -358 C ATOM 1202 O LEU A 182 -34.066 -38.356 -5.577 1.00 26.41 O ANISOU 1202 O LEU A 182 3552 4292 2192 708 133 -280 O ATOM 1203 CB LEU A 182 -35.581 -35.941 -7.079 1.00 25.55 C ANISOU 1203 CB LEU A 182 3441 4026 2240 649 170 -392 C ATOM 1204 CG LEU A 182 -36.797 -35.472 -7.879 1.00 25.61 C ANISOU 1204 CG LEU A 182 3433 3977 2321 632 229 -364 C ATOM 1205 CD1 LEU A 182 -36.326 -34.828 -9.174 1.00 24.88 C ANISOU 1205 CD1 LEU A 182 3328 3779 2347 554 191 -406 C ATOM 1206 CD2 LEU A 182 -37.752 -36.621 -8.169 1.00 26.10 C ANISOU 1206 CD2 LEU A 182 3458 4058 2402 625 299 -233 C ATOM 1207 N LEU A 183 -33.902 -36.434 -4.413 1.00 27.79 N ANISOU 1207 N LEU A 183 3782 4509 2268 783 77 -472 N ATOM 1208 CA LEU A 183 -32.555 -36.721 -3.931 1.00 28.38 C ANISOU 1208 CA LEU A 183 3859 4628 2296 789 -3 -517 C ATOM 1209 C LEU A 183 -32.506 -37.913 -2.978 1.00 28.71 C ANISOU 1209 C LEU A 183 3908 4774 2224 860 19 -427 C ATOM 1210 O LEU A 183 -33.373 -38.090 -2.121 1.00 29.20 O ANISOU 1210 O LEU A 183 3995 4907 2191 940 80 -383 O ATOM 1211 CB LEU A 183 -31.921 -35.491 -3.271 1.00 29.55 C ANISOU 1211 CB LEU A 183 4037 4793 2398 816 -79 -673 C ATOM 1212 CG LEU A 183 -31.477 -34.367 -4.220 1.00 29.77 C ANISOU 1212 CG LEU A 183 4053 4709 2550 732 -124 -770 C ATOM 1213 CD1 LEU A 183 -30.670 -33.328 -3.433 1.00 32.60 C ANISOU 1213 CD1 LEU A 183 4438 5089 2861 756 -210 -926 C ATOM 1214 CD2 LEU A 183 -30.671 -34.882 -5.407 1.00 30.39 C ANISOU 1214 CD2 LEU A 183 4085 4716 2745 637 -149 -727 C ATOM 1215 N ARG A 184 -31.468 -38.723 -3.155 1.00 28.69 N ANISOU 1215 N ARG A 184 3886 4780 2235 835 -27 -396 N ATOM 1216 CA ARG A 184 -31.263 -39.929 -2.366 1.00 29.14 C ANISOU 1216 CA ARG A 184 3949 4924 2196 899 -10 -303 C ATOM 1217 C ARG A 184 -30.921 -39.592 -0.920 1.00 30.69 C ANISOU 1217 C ARG A 184 4186 5240 2236 1003 -50 -371 C ATOM 1218 O ARG A 184 -30.022 -38.795 -0.654 1.00 31.03 O ANISOU 1218 O ARG A 184 4233 5298 2258 1003 -140 -498 O ATOM 1219 CB ARG A 184 -30.142 -40.760 -2.995 1.00 28.63 C ANISOU 1219 CB ARG A 184 3853 4831 2193 846 -58 -268 C ATOM 1220 CG ARG A 184 -29.732 -42.006 -2.224 1.00 28.82 C ANISOU 1220 CG ARG A 184 3885 4939 2125 914 -52 -175 C ATOM 1221 CD ARG A 184 -28.701 -42.778 -3.030 1.00 27.87 C ANISOU 1221 CD ARG A 184 3729 4773 2085 856 -93 -141 C ATOM 1222 NE ARG A 184 -29.276 -43.337 -4.251 1.00 25.57 N ANISOU 1222 NE ARG A 184 3414 4379 1920 778 -34 -58 N ATOM 1223 CZ ARG A 184 -28.570 -43.817 -5.275 1.00 23.96 C ANISOU 1223 CZ ARG A 184 3179 4108 1815 711 -60 -39 C ATOM 1224 NH1 ARG A 184 -27.243 -43.804 -5.255 1.00 24.63 N ANISOU 1224 NH1 ARG A 184 3246 4216 1896 708 -140 -94 N ATOM 1225 NH2 ARG A 184 -29.198 -44.307 -6.336 1.00 23.00 N ANISOU 1225 NH2 ARG A 184 3042 3901 1798 648 -6 30 N ATOM 1226 N ARG A 185 -31.658 -40.191 0.010 1.00 31.56 N ANISOU 1226 N ARG A 185 4322 5435 2233 1092 18 -285 N ATOM 1227 CA ARG A 185 -31.266 -40.190 1.409 1.00 33.31 C ANISOU 1227 CA ARG A 185 4582 5786 2288 1205 -15 -321 C ATOM 1228 C ARG A 185 -30.397 -41.437 1.561 1.00 34.02 C ANISOU 1228 C ARG A 185 4659 5917 2350 1221 -38 -233 C ATOM 1229 O ARG A 185 -29.168 -41.355 1.474 1.00 35.23 O ANISOU 1229 O ARG A 185 4796 6077 2512 1201 -134 -304 O ATOM 1230 CB ARG A 185 -32.489 -40.222 2.333 1.00 33.83 C ANISOU 1230 CB ARG A 185 4684 5927 2242 1302 79 -263 C ATOM 1231 CG ARG A 185 -33.139 -38.860 2.592 1.00 34.01 C ANISOU 1231 CG ARG A 185 4734 5947 2242 1327 81 -380 C ATOM 1232 CD ARG A 185 -33.771 -38.234 1.352 1.00 32.59 C ANISOU 1232 CD ARG A 185 4525 5638 2221 1226 110 -397 C ATOM 1233 NE ARG A 185 -34.526 -37.023 1.697 1.00 32.33 N ANISOU 1233 NE ARG A 185 4522 5608 2155 1268 128 -491 N ATOM 1234 CZ ARG A 185 -34.958 -36.107 0.829 1.00 31.75 C ANISOU 1234 CZ ARG A 185 4437 5433 2194 1204 133 -549 C ATOM 1235 NH1 ARG A 185 -34.729 -36.228 -0.475 1.00 30.89 N ANISOU 1235 NH1 ARG A 185 4286 5213 2236 1092 121 -525 N ATOM 1236 NH2 ARG A 185 -35.619 -35.045 1.275 1.00 32.41 N ANISOU 1236 NH2 ARG A 185 4554 5526 2233 1258 150 -633 N ATOM 1237 N GLU A 186 -31.040 -42.591 1.717 1.00 34.08 N ANISOU 1237 N GLU A 186 4670 5942 2337 1252 53 -77 N ATOM 1238 CA GLU A 186 -30.353 -43.873 1.739 1.00 34.24 C ANISOU 1238 CA GLU A 186 4680 5980 2349 1264 48 27 C ATOM 1239 C GLU A 186 -30.530 -44.564 0.388 1.00 32.31 C ANISOU 1239 C GLU A 186 4395 5611 2270 1155 86 109 C ATOM 1240 O GLU A 186 -31.599 -44.472 -0.221 1.00 31.12 O ANISOU 1240 O GLU A 186 4232 5392 2201 1105 159 150 O ATOM 1241 CB GLU A 186 -30.940 -44.741 2.845 1.00 35.83 C ANISOU 1241 CB GLU A 186 4916 6279 2419 1374 129 153 C ATOM 1242 CG GLU A 186 -30.026 -45.841 3.328 1.00 38.91 C ANISOU 1242 CG GLU A 186 5313 6729 2742 1432 102 230 C ATOM 1243 CD GLU A 186 -30.550 -46.501 4.586 1.00 43.02 C ANISOU 1243 CD GLU A 186 5877 7361 3109 1559 177 341 C ATOM 1244 OE1 GLU A 186 -31.787 -46.555 4.752 1.00 45.90 O ANISOU 1244 OE1 GLU A 186 6251 7720 3469 1572 283 415 O ATOM 1245 OE2 GLU A 186 -29.734 -46.957 5.414 1.00 47.16 O ANISOU 1245 OE2 GLU A 186 6423 7982 3513 1650 132 356 O ATOM 1246 N PHE A 187 -29.487 -45.252 -0.073 1.00 31.27 N ANISOU 1246 N PHE A 187 4242 5455 2186 1123 35 130 N ATOM 1247 CA PHE A 187 -29.542 -45.984 -1.339 1.00 29.94 C ANISOU 1247 CA PHE A 187 4040 5172 2164 1029 64 203 C ATOM 1248 C PHE A 187 -30.688 -46.989 -1.324 1.00 29.83 C ANISOU 1248 C PHE A 187 4032 5134 2168 1037 179 355 C ATOM 1249 O PHE A 187 -30.810 -47.777 -0.387 1.00 30.43 O ANISOU 1249 O PHE A 187 4135 5282 2147 1121 222 448 O ATOM 1250 CB PHE A 187 -28.215 -46.703 -1.600 1.00 29.86 C ANISOU 1250 CB PHE A 187 4012 5161 2174 1022 -2 214 C ATOM 1251 CG PHE A 187 -28.221 -47.590 -2.824 1.00 28.47 C ANISOU 1251 CG PHE A 187 3808 4874 2134 940 30 294 C ATOM 1252 CD1 PHE A 187 -28.180 -48.977 -2.697 1.00 29.09 C ANISOU 1252 CD1 PHE A 187 3896 4949 2208 971 75 426 C ATOM 1253 CD2 PHE A 187 -28.247 -47.041 -4.097 1.00 26.92 C ANISOU 1253 CD2 PHE A 187 3581 4577 2069 838 13 236 C ATOM 1254 CE1 PHE A 187 -28.170 -49.798 -3.824 1.00 27.92 C ANISOU 1254 CE1 PHE A 187 3728 4696 2186 898 100 489 C ATOM 1255 CE2 PHE A 187 -28.235 -47.852 -5.226 1.00 26.81 C ANISOU 1255 CE2 PHE A 187 3545 4468 2172 769 38 301 C ATOM 1256 CZ PHE A 187 -28.198 -49.237 -5.087 1.00 26.61 C ANISOU 1256 CZ PHE A 187 3530 4438 2143 799 79 423 C ATOM 1257 N ILE A 188 -31.529 -46.934 -2.356 1.00 28.77 N ANISOU 1257 N ILE A 188 3873 4901 2158 951 228 377 N ATOM 1258 CA ILE A 188 -32.644 -47.862 -2.515 1.00 28.76 C ANISOU 1258 CA ILE A 188 3865 4861 2203 937 332 512 C ATOM 1259 C ILE A 188 -32.335 -48.792 -3.686 1.00 27.86 C ANISOU 1259 C ILE A 188 3724 4641 2219 855 330 568 C ATOM 1260 O ILE A 188 -32.368 -48.364 -4.837 1.00 26.51 O ANISOU 1260 O ILE A 188 3526 4389 2159 769 305 512 O ATOM 1261 CB ILE A 188 -33.976 -47.118 -2.785 1.00 28.65 C ANISOU 1261 CB ILE A 188 3836 4819 2229 907 391 497 C ATOM 1262 CG1 ILE A 188 -34.298 -46.149 -1.639 1.00 30.05 C ANISOU 1262 CG1 ILE A 188 4044 5099 2276 995 395 433 C ATOM 1263 CG2 ILE A 188 -35.115 -48.115 -2.979 1.00 28.95 C ANISOU 1263 CG2 ILE A 188 3855 4817 2328 884 496 635 C ATOM 1264 CD1 ILE A 188 -35.568 -45.320 -1.863 1.00 30.15 C ANISOU 1264 CD1 ILE A 188 4042 5091 2323 976 451 409 C ATOM 1265 N PRO A 189 -32.031 -50.073 -3.403 1.00 28.20 N ANISOU 1265 N PRO A 189 3779 4687 2249 885 357 677 N ATOM 1266 CA PRO A 189 -31.660 -50.975 -4.494 1.00 27.60 C ANISOU 1266 CA PRO A 189 3683 4511 2294 814 351 721 C ATOM 1267 C PRO A 189 -32.857 -51.351 -5.366 1.00 27.03 C ANISOU 1267 C PRO A 189 3585 4343 2342 735 422 780 C ATOM 1268 O PRO A 189 -33.989 -51.344 -4.890 1.00 27.61 O ANISOU 1268 O PRO A 189 3656 4437 2397 751 498 835 O ATOM 1269 CB PRO A 189 -31.133 -52.208 -3.758 1.00 28.49 C ANISOU 1269 CB PRO A 189 3823 4658 2345 886 371 829 C ATOM 1270 CG PRO A 189 -31.890 -52.226 -2.484 1.00 29.80 C ANISOU 1270 CG PRO A 189 4015 4913 2396 971 439 894 C ATOM 1271 CD PRO A 189 -32.197 -50.794 -2.127 1.00 29.67 C ANISOU 1271 CD PRO A 189 3998 4958 2317 986 411 779 C ATOM 1272 N ASP A 190 -32.601 -51.686 -6.629 1.00 26.42 N ANISOU 1272 N ASP A 190 3486 4168 2386 653 397 766 N ATOM 1273 CA ASP A 190 -33.663 -52.128 -7.527 1.00 26.09 C ANISOU 1273 CA ASP A 190 3416 4035 2463 576 452 815 C ATOM 1274 C ASP A 190 -34.151 -53.525 -7.117 1.00 26.96 C ANISOU 1274 C ASP A 190 3535 4120 2589 592 530 956 C ATOM 1275 O ASP A 190 -33.358 -54.466 -7.092 1.00 26.83 O ANISOU 1275 O ASP A 190 3537 4080 2575 612 517 1005 O ATOM 1276 CB ASP A 190 -33.171 -52.162 -8.974 1.00 25.06 C ANISOU 1276 CB ASP A 190 3265 3812 2444 495 400 760 C ATOM 1277 CG ASP A 190 -34.160 -52.831 -9.909 1.00 25.16 C ANISOU 1277 CG ASP A 190 3251 3730 2577 420 448 813 C ATOM 1278 OD1 ASP A 190 -35.383 -52.718 -9.671 1.00 25.03 O ANISOU 1278 OD1 ASP A 190 3217 3720 2574 410 510 851 O ATOM 1279 OD2 ASP A 190 -33.720 -53.481 -10.873 1.00 25.04 O ANISOU 1279 OD2 ASP A 190 3232 3638 2644 373 423 814 O ATOM 1280 N PRO A 191 -35.457 -53.668 -6.814 1.00 27.52 N ANISOU 1280 N PRO A 191 3589 4190 2677 584 614 1024 N ATOM 1281 CA PRO A 191 -35.971 -54.998 -6.482 1.00 28.45 C ANISOU 1281 CA PRO A 191 3709 4270 2828 588 695 1163 C ATOM 1282 C PRO A 191 -35.978 -55.984 -7.660 1.00 27.90 C ANISOU 1282 C PRO A 191 3624 4074 2903 503 692 1192 C ATOM 1283 O PRO A 191 -36.037 -57.193 -7.428 1.00 28.31 O ANISOU 1283 O PRO A 191 3688 4081 2986 509 742 1298 O ATOM 1284 CB PRO A 191 -37.404 -54.713 -6.012 1.00 29.09 C ANISOU 1284 CB PRO A 191 3763 4382 2907 587 782 1211 C ATOM 1285 CG PRO A 191 -37.778 -53.469 -6.707 1.00 28.58 C ANISOU 1285 CG PRO A 191 3669 4318 2873 543 740 1096 C ATOM 1286 CD PRO A 191 -36.521 -52.648 -6.745 1.00 27.85 C ANISOU 1286 CD PRO A 191 3605 4264 2713 573 643 983 C ATOM 1287 N GLN A 192 -35.934 -55.483 -8.896 1.00 26.63 N ANISOU 1287 N GLN A 192 3437 3855 2826 428 637 1099 N ATOM 1288 CA GLN A 192 -35.785 -56.350 -10.080 1.00 26.31 C ANISOU 1288 CA GLN A 192 3386 3700 2910 355 619 1106 C ATOM 1289 C GLN A 192 -34.360 -56.876 -10.269 1.00 25.84 C ANISOU 1289 C GLN A 192 3361 3622 2834 383 562 1092 C ATOM 1290 O GLN A 192 -34.115 -57.687 -11.160 1.00 26.07 O ANISOU 1290 O GLN A 192 3392 3560 2955 338 548 1101 O ATOM 1291 CB GLN A 192 -36.257 -55.650 -11.368 1.00 25.67 C ANISOU 1291 CB GLN A 192 3268 3570 2917 274 582 1016 C ATOM 1292 CG GLN A 192 -37.741 -55.817 -11.629 1.00 26.33 C ANISOU 1292 CG GLN A 192 3306 3617 3081 217 644 1057 C ATOM 1293 CD GLN A 192 -38.219 -55.080 -12.867 1.00 25.00 C ANISOU 1293 CD GLN A 192 3100 3412 2987 149 603 968 C ATOM 1294 OE1 GLN A 192 -38.894 -54.059 -12.766 1.00 24.76 O ANISOU 1294 OE1 GLN A 192 3045 3431 2933 152 610 929 O ATOM 1295 NE2 GLN A 192 -37.876 -55.597 -14.043 1.00 25.33 N ANISOU 1295 NE2 GLN A 192 3140 3370 3116 94 560 938 N ATOM 1296 N GLY A 193 -33.424 -56.414 -9.445 1.00 25.41 N ANISOU 1296 N GLY A 193 3333 3657 2664 461 525 1066 N ATOM 1297 CA GLY A 193 -32.057 -56.926 -9.473 1.00 25.05 C ANISOU 1297 CA GLY A 193 3314 3610 2593 500 473 1061 C ATOM 1298 C GLY A 193 -31.169 -56.405 -10.590 1.00 23.79 C ANISOU 1298 C GLY A 193 3141 3421 2479 459 391 954 C ATOM 1299 O GLY A 193 -30.138 -57.006 -10.875 1.00 23.54 O ANISOU 1299 O GLY A 193 3123 3365 2457 477 355 957 O ATOM 1300 N SER A 194 -31.543 -55.290 -11.219 1.00 22.64 N ANISOU 1300 N SER A 194 2968 3276 2358 409 365 864 N ATOM 1301 CA SER A 194 -30.694 -54.678 -12.248 1.00 21.66 C ANISOU 1301 CA SER A 194 2830 3129 2270 373 293 766 C ATOM 1302 C SER A 194 -29.311 -54.388 -11.677 1.00 21.93 C ANISOU 1302 C SER A 194 2875 3235 2222 434 234 727 C ATOM 1303 O SER A 194 -29.191 -53.963 -10.529 1.00 22.49 O ANISOU 1303 O SER A 194 2957 3395 2192 496 232 727 O ATOM 1304 CB SER A 194 -31.296 -53.377 -12.777 1.00 21.41 C ANISOU 1304 CB SER A 194 2773 3103 2258 326 279 681 C ATOM 1305 OG SER A 194 -32.597 -53.582 -13.294 1.00 20.64 O ANISOU 1305 OG SER A 194 2657 2951 2234 273 328 712 O ATOM 1306 N ASN A 195 -28.281 -54.614 -12.487 1.00 21.10 N ANISOU 1306 N ASN A 195 2763 3095 2157 420 186 692 N ATOM 1307 CA ASN A 195 -26.898 -54.462 -12.042 1.00 21.55 C ANISOU 1307 CA ASN A 195 2820 3217 2151 475 127 658 C ATOM 1308 C ASN A 195 -26.187 -53.364 -12.830 1.00 21.01 C ANISOU 1308 C ASN A 195 2721 3152 2109 434 66 549 C ATOM 1309 O ASN A 195 -26.815 -52.674 -13.633 1.00 20.60 O ANISOU 1309 O ASN A 195 2655 3058 2113 372 72 503 O ATOM 1310 CB ASN A 195 -26.159 -55.806 -12.127 1.00 21.79 C ANISOU 1310 CB ASN A 195 2868 3214 2198 511 130 728 C ATOM 1311 CG ASN A 195 -26.048 -56.339 -13.549 1.00 21.51 C ANISOU 1311 CG ASN A 195 2825 3076 2272 452 128 718 C ATOM 1312 OD1 ASN A 195 -26.202 -55.604 -14.523 1.00 21.66 O ANISOU 1312 OD1 ASN A 195 2822 3063 2344 391 109 648 O ATOM 1313 ND2 ASN A 195 -25.793 -57.637 -13.667 1.00 22.48 N ANISOU 1313 ND2 ASN A 195 2970 3144 2425 476 150 791 N ATOM 1314 N MET A 196 -24.888 -53.189 -12.595 1.00 21.45 N ANISOU 1314 N MET A 196 2764 3261 2126 470 8 509 N ATOM 1315 CA MET A 196 -24.146 -52.116 -13.265 1.00 21.23 C ANISOU 1315 CA MET A 196 2701 3238 2127 431 -47 409 C ATOM 1316 C MET A 196 -23.848 -52.421 -14.730 1.00 20.53 C ANISOU 1316 C MET A 196 2597 3066 2136 378 -48 400 C ATOM 1317 O MET A 196 -23.662 -51.492 -15.524 1.00 19.71 O ANISOU 1317 O MET A 196 2469 2944 2076 329 -70 330 O ATOM 1318 CB MET A 196 -22.871 -51.760 -12.489 1.00 21.91 C ANISOU 1318 CB MET A 196 2768 3415 2144 483 -111 364 C ATOM 1319 CG MET A 196 -23.135 -51.087 -11.140 1.00 24.34 C ANISOU 1319 CG MET A 196 3087 3813 2349 531 -125 339 C ATOM 1320 SD MET A 196 -24.207 -49.633 -11.242 1.00 28.63 S ANISOU 1320 SD MET A 196 3631 4343 2905 476 -110 264 S ATOM 1321 CE MET A 196 -23.187 -48.525 -12.188 1.00 28.13 C ANISOU 1321 CE MET A 196 3521 4256 2909 415 -173 154 C ATOM 1322 N MET A 197 -23.832 -53.700 -15.112 1.00 20.48 N ANISOU 1322 N MET A 197 2610 3007 2166 389 -21 469 N ATOM 1323 CA MET A 197 -23.788 -54.041 -16.536 1.00 20.15 C ANISOU 1323 CA MET A 197 2562 2881 2213 341 -15 460 C ATOM 1324 C MET A 197 -25.019 -53.468 -17.237 1.00 19.53 C ANISOU 1324 C MET A 197 2484 2751 2185 276 13 438 C ATOM 1325 O MET A 197 -24.918 -52.920 -18.325 1.00 18.59 O ANISOU 1325 O MET A 197 2348 2598 2117 231 0 388 O ATOM 1326 CB MET A 197 -23.709 -55.557 -16.759 1.00 20.74 C ANISOU 1326 CB MET A 197 2663 2898 2318 366 12 537 C ATOM 1327 CG MET A 197 -22.406 -56.187 -16.300 1.00 22.25 C ANISOU 1327 CG MET A 197 2851 3131 2471 435 -18 559 C ATOM 1328 SD MET A 197 -20.962 -55.581 -17.203 1.00 23.90 S ANISOU 1328 SD MET A 197 3014 3361 2707 426 -74 480 S ATOM 1329 CE MET A 197 -21.210 -56.338 -18.812 1.00 21.58 C ANISOU 1329 CE MET A 197 2736 2954 2510 385 -46 488 C ATOM 1330 N PHE A 198 -26.176 -53.584 -16.588 1.00 19.47 N ANISOU 1330 N PHE A 198 2493 2745 2159 275 54 480 N ATOM 1331 CA PHE A 198 -27.416 -53.031 -17.117 1.00 19.07 C ANISOU 1331 CA PHE A 198 2437 2658 2150 221 81 463 C ATOM 1332 C PHE A 198 -27.381 -51.506 -17.185 1.00 18.89 C ANISOU 1332 C PHE A 198 2394 2672 2110 201 55 382 C ATOM 1333 O PHE A 198 -27.709 -50.916 -18.221 1.00 18.92 O ANISOU 1333 O PHE A 198 2386 2635 2167 154 52 341 O ATOM 1334 CB PHE A 198 -28.611 -53.493 -16.275 1.00 19.52 C ANISOU 1334 CB PHE A 198 2509 2719 2189 232 135 531 C ATOM 1335 CG PHE A 198 -29.913 -52.857 -16.674 1.00 19.53 C ANISOU 1335 CG PHE A 198 2496 2698 2226 183 162 514 C ATOM 1336 CD1 PHE A 198 -30.673 -53.391 -17.709 1.00 20.41 C ANISOU 1336 CD1 PHE A 198 2601 2733 2421 132 181 528 C ATOM 1337 CD2 PHE A 198 -30.372 -51.715 -16.027 1.00 20.70 C ANISOU 1337 CD2 PHE A 198 2637 2904 2324 193 165 478 C ATOM 1338 CE1 PHE A 198 -31.868 -52.802 -18.093 1.00 20.50 C ANISOU 1338 CE1 PHE A 198 2592 2730 2465 92 202 511 C ATOM 1339 CE2 PHE A 198 -31.569 -51.115 -16.406 1.00 20.22 C ANISOU 1339 CE2 PHE A 198 2560 2825 2296 156 191 463 C ATOM 1340 CZ PHE A 198 -32.321 -51.658 -17.437 1.00 20.67 C ANISOU 1340 CZ PHE A 198 2605 2812 2436 106 209 482 C ATOM 1341 N ALA A 199 -26.986 -50.876 -16.084 1.00 19.24 N ANISOU 1341 N ALA A 199 2437 2792 2079 241 35 358 N ATOM 1342 CA ALA A 199 -26.938 -49.417 -15.995 1.00 19.60 C ANISOU 1342 CA ALA A 199 2468 2869 2108 225 9 277 C ATOM 1343 C ALA A 199 -26.046 -48.807 -17.073 1.00 19.23 C ANISOU 1343 C ALA A 199 2398 2793 2115 188 -28 216 C ATOM 1344 O ALA A 199 -26.457 -47.876 -17.786 1.00 18.61 O ANISOU 1344 O ALA A 199 2311 2684 2077 146 -26 172 O ATOM 1345 CB ALA A 199 -26.467 -48.987 -14.606 1.00 20.25 C ANISOU 1345 CB ALA A 199 2556 3040 2098 280 -16 255 C ATOM 1346 N PHE A 200 -24.829 -49.335 -17.203 1.00 19.73 N ANISOU 1346 N PHE A 200 2449 2867 2179 206 -59 218 N ATOM 1347 CA PHE A 200 -23.891 -48.816 -18.199 1.00 19.48 C ANISOU 1347 CA PHE A 200 2388 2814 2198 174 -88 168 C ATOM 1348 C PHE A 200 -24.265 -49.196 -19.629 1.00 18.74 C ANISOU 1348 C PHE A 200 2299 2644 2178 136 -63 186 C ATOM 1349 O PHE A 200 -23.917 -48.479 -20.558 1.00 18.33 O ANISOU 1349 O PHE A 200 2229 2567 2169 102 -72 144 O ATOM 1350 CB PHE A 200 -22.445 -49.196 -17.858 1.00 20.08 C ANISOU 1350 CB PHE A 200 2441 2936 2252 210 -129 162 C ATOM 1351 CG PHE A 200 -21.880 -48.402 -16.710 1.00 21.51 C ANISOU 1351 CG PHE A 200 2606 3195 2372 235 -172 111 C ATOM 1352 CD1 PHE A 200 -21.827 -47.016 -16.776 1.00 23.07 C ANISOU 1352 CD1 PHE A 200 2784 3396 2585 198 -193 34 C ATOM 1353 CD2 PHE A 200 -21.422 -49.029 -15.563 1.00 24.08 C ANISOU 1353 CD2 PHE A 200 2937 3589 2625 299 -193 138 C ATOM 1354 CE1 PHE A 200 -21.327 -46.268 -15.721 1.00 24.33 C ANISOU 1354 CE1 PHE A 200 2929 3623 2691 218 -239 -26 C ATOM 1355 CE2 PHE A 200 -20.908 -48.283 -14.507 1.00 24.73 C ANISOU 1355 CE2 PHE A 200 3003 3749 2644 326 -241 81 C ATOM 1356 CZ PHE A 200 -20.870 -46.901 -14.588 1.00 24.27 C ANISOU 1356 CZ PHE A 200 2925 3691 2605 283 -265 -6 C ATOM 1357 N PHE A 201 -24.990 -50.301 -19.810 1.00 18.50 N ANISOU 1357 N PHE A 201 2293 2575 2162 141 -31 245 N ATOM 1358 CA PHE A 201 -25.500 -50.650 -21.135 1.00 17.99 C ANISOU 1358 CA PHE A 201 2234 2440 2161 105 -12 253 C ATOM 1359 C PHE A 201 -26.545 -49.631 -21.572 1.00 17.60 C ANISOU 1359 C PHE A 201 2181 2373 2132 66 2 222 C ATOM 1360 O PHE A 201 -26.499 -49.144 -22.702 1.00 17.12 O ANISOU 1360 O PHE A 201 2113 2280 2112 38 -1 192 O ATOM 1361 CB PHE A 201 -26.096 -52.059 -21.175 1.00 17.76 C ANISOU 1361 CB PHE A 201 2230 2368 2150 114 16 317 C ATOM 1362 CG PHE A 201 -26.476 -52.510 -22.557 1.00 18.23 C ANISOU 1362 CG PHE A 201 2296 2358 2274 82 24 313 C ATOM 1363 CD1 PHE A 201 -25.582 -53.224 -23.340 1.00 17.80 C ANISOU 1363 CD1 PHE A 201 2246 2274 2243 95 12 314 C ATOM 1364 CD2 PHE A 201 -27.730 -52.214 -23.081 1.00 18.21 C ANISOU 1364 CD2 PHE A 201 2293 2323 2302 43 42 307 C ATOM 1365 CE1 PHE A 201 -25.930 -53.640 -24.623 1.00 18.37 C ANISOU 1365 CE1 PHE A 201 2328 2286 2366 72 17 303 C ATOM 1366 CE2 PHE A 201 -28.080 -52.621 -24.363 1.00 18.74 C ANISOU 1366 CE2 PHE A 201 2366 2334 2421 18 42 296 C ATOM 1367 CZ PHE A 201 -27.183 -53.335 -25.130 1.00 18.11 C ANISOU 1367 CZ PHE A 201 2296 2224 2360 33 29 292 C ATOM 1368 N ALA A 202 -27.477 -49.308 -20.674 1.00 17.90 N ANISOU 1368 N ALA A 202 2226 2436 2138 71 21 232 N ATOM 1369 CA ALA A 202 -28.492 -48.289 -20.952 1.00 17.93 C ANISOU 1369 CA ALA A 202 2226 2430 2156 43 35 204 C ATOM 1370 C ALA A 202 -27.831 -46.978 -21.372 1.00 17.82 C ANISOU 1370 C ALA A 202 2198 2422 2152 28 11 139 C ATOM 1371 O ALA A 202 -28.217 -46.369 -22.376 1.00 17.72 O ANISOU 1371 O ALA A 202 2182 2374 2179 1 17 118 O ATOM 1372 CB ALA A 202 -29.377 -48.059 -19.722 1.00 17.87 C ANISOU 1372 CB ALA A 202 2226 2465 2101 64 58 220 C ATOM 1373 N GLN A 203 -26.829 -46.554 -20.608 1.00 18.28 N ANISOU 1373 N GLN A 203 2247 2524 2174 47 -18 109 N ATOM 1374 CA GLN A 203 -26.158 -45.282 -20.866 1.00 18.54 C ANISOU 1374 CA GLN A 203 2263 2558 2222 28 -41 45 C ATOM 1375 C GLN A 203 -25.451 -45.322 -22.221 1.00 18.07 C ANISOU 1375 C GLN A 203 2188 2457 2219 3 -44 41 C ATOM 1376 O GLN A 203 -25.622 -44.423 -23.051 1.00 17.85 O ANISOU 1376 O GLN A 203 2157 2397 2229 -25 -36 16 O ATOM 1377 CB GLN A 203 -25.156 -44.961 -19.755 1.00 19.35 C ANISOU 1377 CB GLN A 203 2352 2719 2279 52 -78 10 C ATOM 1378 CG GLN A 203 -24.691 -43.510 -19.757 1.00 20.27 C ANISOU 1378 CG GLN A 203 2453 2835 2415 27 -101 -64 C ATOM 1379 CD GLN A 203 -23.568 -43.228 -18.775 1.00 22.10 C ANISOU 1379 CD GLN A 203 2662 3124 2611 45 -149 -109 C ATOM 1380 OE1 GLN A 203 -23.018 -44.139 -18.154 1.00 22.47 O ANISOU 1380 OE1 GLN A 203 2705 3217 2616 81 -167 -83 O ATOM 1381 NE2 GLN A 203 -23.214 -41.950 -18.638 1.00 23.78 N ANISOU 1381 NE2 GLN A 203 2861 3332 2843 20 -172 -181 N ATOM 1382 N HIS A 204 -24.681 -46.383 -22.442 1.00 17.91 N ANISOU 1382 N HIS A 204 2163 2440 2202 19 -53 71 N ATOM 1383 CA HIS A 204 -23.926 -46.548 -23.682 1.00 17.43 C ANISOU 1383 CA HIS A 204 2088 2348 2185 6 -53 70 C ATOM 1384 C HIS A 204 -24.856 -46.616 -24.900 1.00 17.27 C ANISOU 1384 C HIS A 204 2085 2275 2200 -14 -26 84 C ATOM 1385 O HIS A 204 -24.713 -45.839 -25.850 1.00 16.94 O ANISOU 1385 O HIS A 204 2036 2210 2191 -34 -19 64 O ATOM 1386 CB HIS A 204 -23.047 -47.809 -23.597 1.00 17.75 C ANISOU 1386 CB HIS A 204 2125 2402 2217 38 -64 103 C ATOM 1387 CG HIS A 204 -22.167 -48.004 -24.785 1.00 17.14 C ANISOU 1387 CG HIS A 204 2031 2303 2178 35 -62 101 C ATOM 1388 ND1 HIS A 204 -22.492 -48.856 -25.820 1.00 16.57 N ANISOU 1388 ND1 HIS A 204 1981 2187 2129 39 -43 128 N ATOM 1389 CD2 HIS A 204 -20.986 -47.432 -25.122 1.00 16.51 C ANISOU 1389 CD2 HIS A 204 1914 2240 2118 28 -75 75 C ATOM 1390 CE1 HIS A 204 -21.542 -48.805 -26.737 1.00 17.82 C ANISOU 1390 CE1 HIS A 204 2119 2339 2311 42 -42 119 C ATOM 1391 NE2 HIS A 204 -20.622 -47.943 -26.343 1.00 16.98 N ANISOU 1391 NE2 HIS A 204 1974 2270 2207 34 -58 92 N ATOM 1392 N PHE A 205 -25.829 -47.519 -24.848 1.00 17.02 N ANISOU 1392 N PHE A 205 2076 2226 2164 -8 -11 120 N ATOM 1393 CA PHE A 205 -26.763 -47.720 -25.954 1.00 17.15 C ANISOU 1393 CA PHE A 205 2106 2199 2213 -25 5 129 C ATOM 1394 C PHE A 205 -27.558 -46.458 -26.300 1.00 17.12 C ANISOU 1394 C PHE A 205 2100 2187 2219 -45 15 103 C ATOM 1395 O PHE A 205 -27.616 -46.059 -27.470 1.00 16.41 O ANISOU 1395 O PHE A 205 2010 2071 2154 -55 20 93 O ATOM 1396 CB PHE A 205 -27.707 -48.892 -25.646 1.00 17.40 C ANISOU 1396 CB PHE A 205 2153 2213 2244 -21 17 169 C ATOM 1397 CG PHE A 205 -28.860 -49.003 -26.588 1.00 17.34 C ANISOU 1397 CG PHE A 205 2152 2168 2268 -43 28 170 C ATOM 1398 CD1 PHE A 205 -28.662 -49.391 -27.909 1.00 16.75 C ANISOU 1398 CD1 PHE A 205 2085 2060 2221 -45 21 160 C ATOM 1399 CD2 PHE A 205 -30.157 -48.729 -26.158 1.00 18.41 C ANISOU 1399 CD2 PHE A 205 2283 2309 2404 -56 43 179 C ATOM 1400 CE1 PHE A 205 -29.733 -49.489 -28.787 1.00 16.56 C ANISOU 1400 CE1 PHE A 205 2063 2009 2221 -62 22 155 C ATOM 1401 CE2 PHE A 205 -31.232 -48.837 -27.032 1.00 17.05 C ANISOU 1401 CE2 PHE A 205 2108 2109 2263 -75 47 177 C ATOM 1402 CZ PHE A 205 -31.014 -49.210 -28.351 1.00 16.58 C ANISOU 1402 CZ PHE A 205 2055 2017 2228 -78 32 162 C ATOM 1403 N THR A 206 -28.171 -45.825 -25.301 1.00 17.49 N ANISOU 1403 N THR A 206 2146 2258 2243 -45 20 94 N ATOM 1404 CA THR A 206 -29.027 -44.665 -25.567 1.00 17.43 C ANISOU 1404 CA THR A 206 2138 2240 2245 -57 33 72 C ATOM 1405 C THR A 206 -28.266 -43.439 -26.063 1.00 17.48 C ANISOU 1405 C THR A 206 2138 2235 2270 -67 28 36 C ATOM 1406 O THR A 206 -28.829 -42.613 -26.783 1.00 17.02 O ANISOU 1406 O THR A 206 2083 2152 2232 -75 41 27 O ATOM 1407 CB THR A 206 -29.867 -44.250 -24.343 1.00 17.72 C ANISOU 1407 CB THR A 206 2177 2305 2248 -46 43 69 C ATOM 1408 OG1 THR A 206 -29.006 -43.890 -23.260 1.00 18.57 O ANISOU 1408 OG1 THR A 206 2283 2450 2323 -33 26 45 O ATOM 1409 CG2 THR A 206 -30.816 -45.373 -23.931 1.00 17.80 C ANISOU 1409 CG2 THR A 206 2190 2322 2250 -40 60 115 C ATOM 1410 N HIS A 207 -26.985 -43.329 -25.712 1.00 17.88 N ANISOU 1410 N HIS A 207 2174 2302 2318 -68 11 18 N ATOM 1411 CA HIS A 207 -26.200 -42.147 -26.081 1.00 18.15 C ANISOU 1411 CA HIS A 207 2195 2321 2381 -86 9 -16 C ATOM 1412 C HIS A 207 -25.771 -42.116 -27.551 1.00 17.78 C ANISOU 1412 C HIS A 207 2143 2241 2370 -94 23 -1 C ATOM 1413 O HIS A 207 -25.082 -41.187 -27.968 1.00 17.62 O ANISOU 1413 O HIS A 207 2109 2204 2381 -110 30 -18 O ATOM 1414 CB HIS A 207 -25.007 -41.956 -25.131 1.00 18.89 C ANISOU 1414 CB HIS A 207 2265 2448 2464 -87 -19 -46 C ATOM 1415 CG HIS A 207 -25.390 -41.345 -23.817 1.00 21.30 C ANISOU 1415 CG HIS A 207 2577 2780 2734 -80 -33 -81 C ATOM 1416 ND1 HIS A 207 -26.555 -41.682 -23.159 1.00 23.83 N ANISOU 1416 ND1 HIS A 207 2920 3117 3016 -59 -21 -64 N ATOM 1417 CD2 HIS A 207 -24.778 -40.416 -23.046 1.00 24.48 C ANISOU 1417 CD2 HIS A 207 2966 3198 3136 -89 -56 -135 C ATOM 1418 CE1 HIS A 207 -26.638 -40.992 -22.035 1.00 25.10 C ANISOU 1418 CE1 HIS A 207 3086 3307 3146 -49 -34 -104 C ATOM 1419 NE2 HIS A 207 -25.572 -40.218 -21.941 1.00 25.29 N ANISOU 1419 NE2 HIS A 207 3090 3328 3191 -67 -59 -152 N ATOM 1420 N GLN A 208 -26.181 -43.112 -28.338 1.00 17.04 N ANISOU 1420 N GLN A 208 2062 2138 2273 -81 30 30 N ATOM 1421 CA GLN A 208 -26.075 -42.983 -29.791 1.00 17.09 C ANISOU 1421 CA GLN A 208 2073 2118 2302 -79 47 43 C ATOM 1422 C GLN A 208 -27.206 -42.135 -30.352 1.00 17.06 C ANISOU 1422 C GLN A 208 2085 2091 2305 -80 63 42 C ATOM 1423 O GLN A 208 -27.026 -41.484 -31.385 1.00 17.89 O ANISOU 1423 O GLN A 208 2193 2176 2428 -78 81 48 O ATOM 1424 CB GLN A 208 -26.014 -44.334 -30.488 1.00 16.69 C ANISOU 1424 CB GLN A 208 2032 2064 2244 -61 42 66 C ATOM 1425 CG GLN A 208 -27.306 -45.079 -30.596 1.00 16.16 C ANISOU 1425 CG GLN A 208 1984 1988 2168 -57 38 77 C ATOM 1426 CD GLN A 208 -27.071 -46.516 -30.980 1.00 16.01 C ANISOU 1426 CD GLN A 208 1975 1961 2147 -43 29 92 C ATOM 1427 OE1 GLN A 208 -26.770 -46.809 -32.141 1.00 16.76 O ANISOU 1427 OE1 GLN A 208 2080 2043 2246 -28 31 92 O ATOM 1428 NE2 GLN A 208 -27.176 -47.424 -30.007 1.00 14.78 N ANISOU 1428 NE2 GLN A 208 1821 1812 1982 -41 19 106 N ATOM 1429 N PHE A 209 -28.361 -42.122 -29.686 1.00 16.77 N ANISOU 1429 N PHE A 209 2056 2062 2254 -79 60 40 N ATOM 1430 CA PHE A 209 -29.486 -41.342 -30.204 1.00 16.91 C ANISOU 1430 CA PHE A 209 2084 2064 2278 -73 74 41 C ATOM 1431 C PHE A 209 -29.949 -40.193 -29.310 1.00 17.40 C ANISOU 1431 C PHE A 209 2147 2124 2338 -76 82 18 C ATOM 1432 O PHE A 209 -30.718 -39.351 -29.769 1.00 18.14 O ANISOU 1432 O PHE A 209 2249 2201 2441 -66 97 18 O ATOM 1433 CB PHE A 209 -30.652 -42.233 -30.679 1.00 16.77 C ANISOU 1433 CB PHE A 209 2071 2050 2252 -64 68 59 C ATOM 1434 CG PHE A 209 -31.069 -43.310 -29.709 1.00 16.88 C ANISOU 1434 CG PHE A 209 2080 2083 2253 -69 58 68 C ATOM 1435 CD1 PHE A 209 -31.833 -43.008 -28.593 1.00 17.17 C ANISOU 1435 CD1 PHE A 209 2111 2138 2276 -70 66 67 C ATOM 1436 CD2 PHE A 209 -30.772 -44.639 -29.969 1.00 15.90 C ANISOU 1436 CD2 PHE A 209 1957 1954 2129 -70 46 83 C ATOM 1437 CE1 PHE A 209 -32.244 -44.012 -27.716 1.00 17.12 C ANISOU 1437 CE1 PHE A 209 2099 2148 2257 -72 65 86 C ATOM 1438 CE2 PHE A 209 -31.180 -45.643 -29.106 1.00 17.49 C ANISOU 1438 CE2 PHE A 209 2156 2164 2325 -75 43 101 C ATOM 1439 CZ PHE A 209 -31.918 -45.327 -27.974 1.00 17.74 C ANISOU 1439 CZ PHE A 209 2180 2217 2343 -76 55 106 C ATOM 1440 N PHE A 210 -29.457 -40.123 -28.072 1.00 17.66 N ANISOU 1440 N PHE A 210 2174 2177 2359 -83 71 -4 N ATOM 1441 CA PHE A 210 -29.610 -38.921 -27.256 1.00 17.93 C ANISOU 1441 CA PHE A 210 2213 2206 2393 -84 76 -38 C ATOM 1442 C PHE A 210 -28.261 -38.202 -27.248 1.00 18.61 C ANISOU 1442 C PHE A 210 2288 2274 2507 -105 69 -66 C ATOM 1443 O PHE A 210 -27.335 -38.583 -26.517 1.00 19.21 O ANISOU 1443 O PHE A 210 2349 2377 2574 -114 46 -83 O ATOM 1444 CB PHE A 210 -30.069 -39.236 -25.824 1.00 17.87 C ANISOU 1444 CB PHE A 210 2206 2238 2344 -72 67 -50 C ATOM 1445 CG PHE A 210 -31.350 -40.035 -25.737 1.00 17.75 C ANISOU 1445 CG PHE A 210 2192 2242 2310 -57 78 -16 C ATOM 1446 CD1 PHE A 210 -32.436 -39.770 -26.572 1.00 16.73 C ANISOU 1446 CD1 PHE A 210 2064 2095 2197 -50 94 -1 C ATOM 1447 CD2 PHE A 210 -31.473 -41.039 -24.789 1.00 17.19 C ANISOU 1447 CD2 PHE A 210 2118 2208 2206 -49 73 1 C ATOM 1448 CE1 PHE A 210 -33.612 -40.514 -26.478 1.00 17.62 C ANISOU 1448 CE1 PHE A 210 2167 2227 2300 -42 102 28 C ATOM 1449 CE2 PHE A 210 -32.642 -41.782 -24.682 1.00 17.70 C ANISOU 1449 CE2 PHE A 210 2177 2286 2263 -42 88 36 C ATOM 1450 CZ PHE A 210 -33.718 -41.516 -25.530 1.00 17.71 C ANISOU 1450 CZ PHE A 210 2172 2269 2288 -42 102 47 C ATOM 1451 N LYS A 211 -28.153 -37.186 -28.101 1.00 18.96 N ANISOU 1451 N LYS A 211 2338 2275 2591 -113 89 -67 N ATOM 1452 CA LYS A 211 -26.937 -36.394 -28.258 1.00 20.02 C ANISOU 1452 CA LYS A 211 2457 2382 2769 -141 92 -88 C ATOM 1453 C LYS A 211 -27.340 -34.939 -28.415 1.00 20.89 C ANISOU 1453 C LYS A 211 2584 2439 2913 -144 114 -106 C ATOM 1454 O LYS A 211 -27.308 -34.381 -29.506 1.00 20.93 O ANISOU 1454 O LYS A 211 2597 2404 2952 -144 144 -78 O ATOM 1455 CB LYS A 211 -26.146 -36.863 -29.479 1.00 20.02 C ANISOU 1455 CB LYS A 211 2443 2373 2789 -145 105 -51 C ATOM 1456 CG LYS A 211 -25.740 -38.322 -29.427 1.00 20.79 C ANISOU 1456 CG LYS A 211 2528 2514 2856 -136 86 -33 C ATOM 1457 CD LYS A 211 -24.589 -38.630 -30.379 1.00 21.77 C ANISOU 1457 CD LYS A 211 2632 2635 3005 -141 98 -10 C ATOM 1458 CE LYS A 211 -24.936 -38.367 -31.828 1.00 22.51 C ANISOU 1458 CE LYS A 211 2743 2701 3109 -125 132 26 C ATOM 1459 NZ LYS A 211 -23.775 -38.653 -32.727 1.00 22.73 N ANISOU 1459 NZ LYS A 211 2750 2731 3155 -124 150 50 N ATOM 1460 N THR A 212 -27.737 -34.328 -27.311 1.00 21.86 N ANISOU 1460 N THR A 212 2718 2562 3025 -142 103 -150 N ATOM 1461 CA THR A 212 -28.310 -32.990 -27.359 1.00 22.97 C ANISOU 1461 CA THR A 212 2883 2650 3196 -136 125 -170 C ATOM 1462 C THR A 212 -27.282 -31.964 -27.835 1.00 24.19 C ANISOU 1462 C THR A 212 3029 2742 3420 -172 139 -183 C ATOM 1463 O THR A 212 -26.135 -31.957 -27.376 1.00 24.53 O ANISOU 1463 O THR A 212 3044 2790 3487 -207 117 -216 O ATOM 1464 CB THR A 212 -28.893 -32.606 -26.003 1.00 23.13 C ANISOU 1464 CB THR A 212 2917 2687 3183 -120 108 -222 C ATOM 1465 OG1 THR A 212 -29.958 -33.512 -25.702 1.00 23.59 O ANISOU 1465 OG1 THR A 212 2981 2799 3185 -87 107 -196 O ATOM 1466 CG2 THR A 212 -29.427 -31.173 -26.014 1.00 23.99 C ANISOU 1466 CG2 THR A 212 3055 2734 3327 -111 131 -249 C ATOM 1467 N ASP A 213 -27.701 -31.126 -28.783 1.00 25.12 N ANISOU 1467 N ASP A 213 3167 2803 3573 -161 178 -153 N ATOM 1468 CA ASP A 213 -26.846 -30.091 -29.342 1.00 26.82 C ANISOU 1468 CA ASP A 213 3378 2949 3864 -194 205 -151 C ATOM 1469 C ASP A 213 -27.005 -28.856 -28.476 1.00 28.20 C ANISOU 1469 C ASP A 213 3572 3069 4074 -205 201 -213 C ATOM 1470 O ASP A 213 -27.835 -27.983 -28.745 1.00 28.23 O ANISOU 1470 O ASP A 213 3611 3023 4093 -178 230 -205 O ATOM 1471 CB ASP A 213 -27.236 -29.801 -30.794 1.00 27.01 C ANISOU 1471 CB ASP A 213 3420 2939 3903 -169 252 -81 C ATOM 1472 CG ASP A 213 -26.253 -28.880 -31.494 1.00 28.49 C ANISOU 1472 CG ASP A 213 3598 3056 4169 -202 291 -61 C ATOM 1473 OD1 ASP A 213 -25.383 -28.298 -30.818 1.00 29.00 O ANISOU 1473 OD1 ASP A 213 3642 3087 4289 -251 279 -109 O ATOM 1474 OD2 ASP A 213 -26.357 -28.743 -32.727 1.00 30.18 O ANISOU 1474 OD2 ASP A 213 3825 3252 4391 -180 332 4 O ATOM 1475 N HIS A 214 -26.196 -28.786 -27.427 1.00 29.72 N ANISOU 1475 N HIS A 214 3742 3273 4278 -240 163 -279 N ATOM 1476 CA HIS A 214 -26.358 -27.750 -26.414 1.00 31.27 C ANISOU 1476 CA HIS A 214 3958 3427 4494 -247 147 -356 C ATOM 1477 C HIS A 214 -26.096 -26.345 -26.959 1.00 32.14 C ANISOU 1477 C HIS A 214 4085 3430 4698 -273 184 -360 C ATOM 1478 O HIS A 214 -26.610 -25.371 -26.409 1.00 33.25 O ANISOU 1478 O HIS A 214 4259 3517 4856 -262 186 -410 O ATOM 1479 CB HIS A 214 -25.477 -28.055 -25.201 1.00 32.04 C ANISOU 1479 CB HIS A 214 4026 3571 4577 -276 90 -430 C ATOM 1480 CG HIS A 214 -25.787 -29.371 -24.559 1.00 32.73 C ANISOU 1480 CG HIS A 214 4105 3758 4572 -244 59 -422 C ATOM 1481 ND1 HIS A 214 -26.898 -29.570 -23.768 1.00 33.14 N ANISOU 1481 ND1 HIS A 214 4188 3850 4553 -195 52 -437 N ATOM 1482 CD2 HIS A 214 -25.141 -30.560 -24.607 1.00 33.58 C ANISOU 1482 CD2 HIS A 214 4178 3931 4650 -250 38 -394 C ATOM 1483 CE1 HIS A 214 -26.919 -30.823 -23.351 1.00 32.90 C ANISOU 1483 CE1 HIS A 214 4142 3902 4457 -177 30 -416 C ATOM 1484 NE2 HIS A 214 -25.864 -31.445 -23.846 1.00 33.42 N ANISOU 1484 NE2 HIS A 214 4171 3982 4546 -208 19 -391 N ATOM 1485 N LYS A 215 -25.334 -26.250 -28.049 1.00 32.37 N ANISOU 1485 N LYS A 215 4091 3423 4786 -304 218 -305 N ATOM 1486 CA LYS A 215 -25.106 -24.973 -28.749 1.00 33.38 C ANISOU 1486 CA LYS A 215 4234 3441 5006 -326 267 -286 C ATOM 1487 C LYS A 215 -26.416 -24.368 -29.266 1.00 32.52 C ANISOU 1487 C LYS A 215 4182 3291 4882 -266 308 -247 C ATOM 1488 O LYS A 215 -26.585 -23.144 -29.269 1.00 33.37 O ANISOU 1488 O LYS A 215 4320 3304 5053 -270 336 -263 O ATOM 1489 CB LYS A 215 -24.155 -25.166 -29.936 1.00 33.85 C ANISOU 1489 CB LYS A 215 4259 3488 5115 -356 306 -214 C ATOM 1490 CG LYS A 215 -22.753 -25.663 -29.566 1.00 36.19 C ANISOU 1490 CG LYS A 215 4490 3820 5442 -415 273 -245 C ATOM 1491 CD LYS A 215 -22.214 -26.677 -30.584 1.00 38.37 C ANISOU 1491 CD LYS A 215 4733 4152 5695 -407 295 -167 C ATOM 1492 CE LYS A 215 -21.637 -26.008 -31.820 1.00 40.10 C ANISOU 1492 CE LYS A 215 4942 4303 5991 -427 365 -95 C ATOM 1493 NZ LYS A 215 -20.275 -25.459 -31.560 1.00 42.84 N ANISOU 1493 NZ LYS A 215 5229 4608 6439 -505 365 -127 N ATOM 1494 N ARG A 216 -27.329 -25.229 -29.712 1.00 30.48 N ANISOU 1494 N ARG A 216 3935 3101 4544 -211 311 -195 N ATOM 1495 CA ARG A 216 -28.619 -24.792 -30.249 1.00 29.75 C ANISOU 1495 CA ARG A 216 3886 2988 4428 -148 344 -154 C ATOM 1496 C ARG A 216 -29.696 -24.741 -29.167 1.00 28.42 C ANISOU 1496 C ARG A 216 3741 2849 4207 -108 318 -209 C ATOM 1497 O ARG A 216 -30.486 -23.798 -29.119 1.00 28.69 O ANISOU 1497 O ARG A 216 3814 2829 4258 -71 341 -216 O ATOM 1498 CB ARG A 216 -29.066 -25.712 -31.390 1.00 29.36 C ANISOU 1498 CB ARG A 216 3831 2998 4325 -108 360 -72 C ATOM 1499 CG ARG A 216 -28.126 -25.719 -32.595 1.00 31.32 C ANISOU 1499 CG ARG A 216 4064 3221 4614 -130 397 -8 C ATOM 1500 CD ARG A 216 -28.707 -26.556 -33.729 1.00 33.24 C ANISOU 1500 CD ARG A 216 4311 3524 4794 -79 408 64 C ATOM 1501 NE ARG A 216 -27.863 -26.564 -34.926 1.00 36.04 N ANISOU 1501 NE ARG A 216 4656 3863 5176 -87 449 129 N ATOM 1502 CZ ARG A 216 -27.829 -25.605 -35.853 1.00 37.95 C ANISOU 1502 CZ ARG A 216 4922 4038 5459 -68 507 188 C ATOM 1503 NH1 ARG A 216 -28.586 -24.518 -35.747 1.00 39.66 N ANISOU 1503 NH1 ARG A 216 5178 4190 5702 -39 529 188 N ATOM 1504 NH2 ARG A 216 -27.019 -25.728 -36.900 1.00 39.22 N ANISOU 1504 NH2 ARG A 216 5070 4197 5635 -72 547 250 N ATOM 1505 N GLY A 217 -29.727 -25.760 -28.308 1.00 26.68 N ANISOU 1505 N GLY A 217 3499 2715 3924 -111 273 -243 N ATOM 1506 CA GLY A 217 -30.701 -25.841 -27.219 1.00 25.62 C ANISOU 1506 CA GLY A 217 3380 2621 3731 -72 251 -290 C ATOM 1507 C GLY A 217 -31.123 -27.265 -26.931 1.00 24.05 C ANISOU 1507 C GLY A 217 3157 2527 3453 -55 225 -270 C ATOM 1508 O GLY A 217 -30.817 -28.171 -27.710 1.00 22.86 O ANISOU 1508 O GLY A 217 2984 2411 3291 -66 225 -218 O ATOM 1509 N PRO A 218 -31.851 -27.477 -25.818 1.00 23.07 N ANISOU 1509 N PRO A 218 3041 2452 3273 -25 207 -310 N ATOM 1510 CA PRO A 218 -32.233 -28.829 -25.392 1.00 22.33 C ANISOU 1510 CA PRO A 218 2924 2452 3110 -12 186 -290 C ATOM 1511 C PRO A 218 -33.155 -29.571 -26.366 1.00 21.37 C ANISOU 1511 C PRO A 218 2792 2363 2965 16 205 -217 C ATOM 1512 O PRO A 218 -33.223 -30.801 -26.329 1.00 21.28 O ANISOU 1512 O PRO A 218 2757 2413 2915 11 189 -190 O ATOM 1513 CB PRO A 218 -32.942 -28.588 -24.050 1.00 22.78 C ANISOU 1513 CB PRO A 218 2998 2541 3118 24 178 -343 C ATOM 1514 CG PRO A 218 -33.377 -27.183 -24.085 1.00 23.34 C ANISOU 1514 CG PRO A 218 3103 2537 3226 48 203 -374 C ATOM 1515 CD PRO A 218 -32.363 -26.447 -24.895 1.00 23.86 C ANISOU 1515 CD PRO A 218 3174 2519 3374 3 210 -373 C ATOM 1516 N GLY A 219 -33.856 -28.831 -27.223 1.00 21.16 N ANISOU 1516 N GLY A 219 2783 2294 2963 47 236 -186 N ATOM 1517 CA GLY A 219 -34.748 -29.431 -28.216 1.00 20.26 C ANISOU 1517 CA GLY A 219 2658 2213 2829 76 247 -123 C ATOM 1518 C GLY A 219 -34.064 -29.877 -29.502 1.00 19.78 C ANISOU 1518 C GLY A 219 2587 2141 2787 55 249 -75 C ATOM 1519 O GLY A 219 -34.736 -30.329 -30.438 1.00 19.14 O ANISOU 1519 O GLY A 219 2498 2085 2688 82 253 -29 O ATOM 1520 N PHE A 220 -32.736 -29.765 -29.546 1.00 19.13 N ANISOU 1520 N PHE A 220 2501 2028 2740 10 245 -89 N ATOM 1521 CA PHE A 220 -31.955 -30.079 -30.742 1.00 18.98 C ANISOU 1521 CA PHE A 220 2474 1998 2741 -7 255 -44 C ATOM 1522 C PHE A 220 -31.006 -31.239 -30.511 1.00 18.54 C ANISOU 1522 C PHE A 220 2389 1986 2670 -44 227 -50 C ATOM 1523 O PHE A 220 -30.474 -31.407 -29.412 1.00 18.85 O ANISOU 1523 O PHE A 220 2416 2040 2705 -70 203 -95 O ATOM 1524 CB PHE A 220 -31.159 -28.855 -31.170 1.00 19.55 C ANISOU 1524 CB PHE A 220 2562 1988 2879 -26 287 -42 C ATOM 1525 CG PHE A 220 -32.016 -27.737 -31.679 1.00 20.31 C ANISOU 1525 CG PHE A 220 2691 2031 2995 18 322 -19 C ATOM 1526 CD1 PHE A 220 -32.504 -26.768 -30.813 1.00 22.33 C ANISOU 1526 CD1 PHE A 220 2970 2246 3268 31 327 -64 C ATOM 1527 CD2 PHE A 220 -32.354 -27.663 -33.024 1.00 20.81 C ANISOU 1527 CD2 PHE A 220 2766 2089 3053 55 349 48 C ATOM 1528 CE1 PHE A 220 -33.302 -25.742 -31.281 1.00 22.65 C ANISOU 1528 CE1 PHE A 220 3044 2236 3328 79 361 -40 C ATOM 1529 CE2 PHE A 220 -33.153 -26.636 -33.502 1.00 22.18 C ANISOU 1529 CE2 PHE A 220 2971 2217 3241 104 382 75 C ATOM 1530 CZ PHE A 220 -33.631 -25.677 -32.634 1.00 23.00 C ANISOU 1530 CZ PHE A 220 3096 2275 3367 116 389 33 C ATOM 1531 N THR A 221 -30.779 -32.020 -31.561 1.00 18.22 N ANISOU 1531 N THR A 221 2339 1967 2617 -40 230 -5 N ATOM 1532 CA THR A 221 -29.927 -33.200 -31.479 1.00 18.02 C ANISOU 1532 CA THR A 221 2288 1982 2576 -65 206 -5 C ATOM 1533 C THR A 221 -28.811 -33.165 -32.520 1.00 18.47 C ANISOU 1533 C THR A 221 2337 2018 2663 -79 227 26 C ATOM 1534 O THR A 221 -28.968 -32.582 -33.596 1.00 18.62 O ANISOU 1534 O THR A 221 2372 2007 2697 -58 260 65 O ATOM 1535 CB THR A 221 -30.747 -34.494 -31.659 1.00 17.59 C ANISOU 1535 CB THR A 221 2227 1983 2472 -43 186 14 C ATOM 1536 OG1 THR A 221 -29.894 -35.635 -31.499 1.00 17.06 O ANISOU 1536 OG1 THR A 221 2141 1947 2393 -64 164 14 O ATOM 1537 CG2 THR A 221 -31.424 -34.548 -33.042 1.00 17.34 C ANISOU 1537 CG2 THR A 221 2208 1952 2430 -8 200 57 C ATOM 1538 N ARG A 222 -27.688 -33.794 -32.179 1.00 19.03 N ANISOU 1538 N ARG A 222 2381 2108 2741 -110 211 13 N ATOM 1539 CA ARG A 222 -26.599 -34.024 -33.126 1.00 19.95 C ANISOU 1539 CA ARG A 222 2482 2221 2879 -120 230 45 C ATOM 1540 C ARG A 222 -26.680 -35.416 -33.750 1.00 19.40 C ANISOU 1540 C ARG A 222 2409 2200 2762 -96 216 71 C ATOM 1541 O ARG A 222 -25.876 -35.744 -34.621 1.00 19.68 O ANISOU 1541 O ARG A 222 2434 2240 2802 -92 234 99 O ATOM 1542 CB ARG A 222 -25.242 -33.868 -32.433 1.00 21.30 C ANISOU 1542 CB ARG A 222 2617 2386 3090 -166 220 14 C ATOM 1543 CG ARG A 222 -25.010 -32.495 -31.808 1.00 24.76 C ANISOU 1543 CG ARG A 222 3054 2768 3585 -198 229 -22 C ATOM 1544 CD ARG A 222 -23.536 -32.234 -31.452 1.00 30.07 C ANISOU 1544 CD ARG A 222 3681 3430 4313 -248 223 -47 C ATOM 1545 NE ARG A 222 -22.785 -33.453 -31.150 1.00 34.62 N ANISOU 1545 NE ARG A 222 4224 4070 4860 -252 191 -52 N ATOM 1546 CZ ARG A 222 -22.862 -34.141 -30.008 1.00 36.87 C ANISOU 1546 CZ ARG A 222 4502 4404 5103 -249 143 -92 C ATOM 1547 NH1 ARG A 222 -22.131 -35.244 -29.850 1.00 38.27 N ANISOU 1547 NH1 ARG A 222 4650 4634 5257 -245 120 -87 N ATOM 1548 NH2 ARG A 222 -23.664 -33.740 -29.025 1.00 38.40 N ANISOU 1548 NH2 ARG A 222 4719 4595 5275 -243 122 -134 N ATOM 1549 N GLY A 223 -27.629 -36.232 -33.292 1.00 18.75 N ANISOU 1549 N GLY A 223 2335 2151 2637 -80 187 59 N ATOM 1550 CA GLY A 223 -27.782 -37.606 -33.773 1.00 18.29 C ANISOU 1550 CA GLY A 223 2276 2130 2542 -62 169 75 C ATOM 1551 C GLY A 223 -28.738 -37.658 -34.947 1.00 18.05 C ANISOU 1551 C GLY A 223 2267 2101 2488 -25 178 102 C ATOM 1552 O GLY A 223 -29.888 -38.058 -34.792 1.00 17.66 O ANISOU 1552 O GLY A 223 2224 2069 2416 -11 158 96 O ATOM 1553 N LEU A 224 -28.252 -37.277 -36.127 1.00 18.05 N ANISOU 1553 N LEU A 224 2276 2088 2493 -6 207 133 N ATOM 1554 CA LEU A 224 -29.130 -37.101 -37.293 1.00 18.26 C ANISOU 1554 CA LEU A 224 2326 2119 2493 39 216 159 C ATOM 1555 C LEU A 224 -29.646 -38.407 -37.886 1.00 17.89 C ANISOU 1555 C LEU A 224 2285 2111 2403 63 184 155 C ATOM 1556 O LEU A 224 -30.553 -38.383 -38.720 1.00 18.38 O ANISOU 1556 O LEU A 224 2361 2185 2437 100 177 165 O ATOM 1557 CB LEU A 224 -28.452 -36.245 -38.375 1.00 18.85 C ANISOU 1557 CB LEU A 224 2412 2169 2580 59 263 200 C ATOM 1558 CG LEU A 224 -27.936 -34.870 -37.923 1.00 20.25 C ANISOU 1558 CG LEU A 224 2586 2295 2814 31 299 206 C ATOM 1559 CD1 LEU A 224 -27.459 -34.053 -39.116 1.00 21.41 C ANISOU 1559 CD1 LEU A 224 2747 2415 2974 57 353 260 C ATOM 1560 CD2 LEU A 224 -29.001 -34.096 -37.136 1.00 20.88 C ANISOU 1560 CD2 LEU A 224 2677 2353 2905 30 290 184 C ATOM 1561 N GLY A 225 -29.073 -39.534 -37.466 1.00 17.27 N ANISOU 1561 N GLY A 225 2193 2048 2321 44 162 138 N ATOM 1562 CA GLY A 225 -29.599 -40.849 -37.817 1.00 17.05 C ANISOU 1562 CA GLY A 225 2171 2044 2264 58 128 125 C ATOM 1563 C GLY A 225 -30.867 -41.212 -37.057 1.00 16.60 C ANISOU 1563 C GLY A 225 2105 1994 2206 44 98 106 C ATOM 1564 O GLY A 225 -31.596 -42.118 -37.464 1.00 16.55 O ANISOU 1564 O GLY A 225 2100 2003 2184 54 69 95 O ATOM 1565 N HIS A 226 -31.121 -40.523 -35.943 1.00 16.18 N ANISOU 1565 N HIS A 226 2042 1934 2174 21 105 100 N ATOM 1566 CA HIS A 226 -32.344 -40.700 -35.154 1.00 15.83 C ANISOU 1566 CA HIS A 226 1985 1900 2128 12 88 88 C ATOM 1567 C HIS A 226 -32.663 -42.163 -34.796 1.00 16.03 C ANISOU 1567 C HIS A 226 2000 1939 2150 -3 60 80 C ATOM 1568 O HIS A 226 -33.813 -42.604 -34.860 1.00 15.79 O ANISOU 1568 O HIS A 226 1959 1921 2120 -2 42 76 O ATOM 1569 CB HIS A 226 -33.532 -40.034 -35.867 1.00 16.22 C ANISOU 1569 CB HIS A 226 2038 1956 2169 43 88 96 C ATOM 1570 CG HIS A 226 -33.549 -38.549 -35.719 1.00 15.68 C ANISOU 1570 CG HIS A 226 1978 1866 2112 55 119 105 C ATOM 1571 ND1 HIS A 226 -34.206 -37.917 -34.688 1.00 16.09 N ANISOU 1571 ND1 HIS A 226 2022 1915 2176 48 126 94 N ATOM 1572 CD2 HIS A 226 -32.993 -37.567 -36.469 1.00 14.97 C ANISOU 1572 CD2 HIS A 226 1906 1752 2028 74 148 125 C ATOM 1573 CE1 HIS A 226 -34.053 -36.611 -34.806 1.00 15.13 C ANISOU 1573 CE1 HIS A 226 1916 1764 2069 62 154 101 C ATOM 1574 NE2 HIS A 226 -33.320 -36.371 -35.877 1.00 15.07 N ANISOU 1574 NE2 HIS A 226 1924 1741 2062 76 169 123 N ATOM 1575 N GLY A 227 -31.645 -42.906 -34.386 1.00 15.89 N ANISOU 1575 N GLY A 227 1983 1918 2135 -18 57 78 N ATOM 1576 CA GLY A 227 -31.856 -44.305 -34.055 1.00 16.00 C ANISOU 1576 CA GLY A 227 1993 1935 2151 -30 35 75 C ATOM 1577 C GLY A 227 -30.587 -45.105 -33.895 1.00 16.09 C ANISOU 1577 C GLY A 227 2010 1940 2162 -33 33 77 C ATOM 1578 O GLY A 227 -29.529 -44.567 -33.555 1.00 15.66 O ANISOU 1578 O GLY A 227 1952 1889 2109 -34 48 79 O ATOM 1579 N VAL A 228 -30.721 -46.404 -34.134 1.00 16.08 N ANISOU 1579 N VAL A 228 2015 1930 2164 -32 14 75 N ATOM 1580 CA VAL A 228 -29.650 -47.354 -33.860 1.00 16.35 C ANISOU 1580 CA VAL A 228 2055 1957 2199 -29 12 80 C ATOM 1581 C VAL A 228 -28.763 -47.498 -35.098 1.00 16.50 C ANISOU 1581 C VAL A 228 2089 1973 2207 0 15 73 C ATOM 1582 O VAL A 228 -28.875 -48.467 -35.871 1.00 17.15 O ANISOU 1582 O VAL A 228 2189 2041 2287 15 -2 62 O ATOM 1583 CB VAL A 228 -30.220 -48.708 -33.395 1.00 16.58 C ANISOU 1583 CB VAL A 228 2088 1968 2244 -42 -4 84 C ATOM 1584 CG1 VAL A 228 -29.095 -49.637 -32.949 1.00 16.87 C ANISOU 1584 CG1 VAL A 228 2134 1996 2281 -31 -4 95 C ATOM 1585 CG2 VAL A 228 -31.229 -48.501 -32.249 1.00 16.48 C ANISOU 1585 CG2 VAL A 228 2058 1965 2239 -66 1 98 C ATOM 1586 N ASP A 229 -27.881 -46.513 -35.283 1.00 16.31 N ANISOU 1586 N ASP A 229 2058 1960 2178 7 37 80 N ATOM 1587 CA ASP A 229 -26.925 -46.511 -36.395 1.00 16.07 C ANISOU 1587 CA ASP A 229 2035 1933 2136 37 52 83 C ATOM 1588 C ASP A 229 -25.496 -46.824 -35.937 1.00 15.98 C ANISOU 1588 C ASP A 229 2008 1931 2133 41 62 92 C ATOM 1589 O ASP A 229 -24.588 -46.936 -36.760 1.00 16.28 O ANISOU 1589 O ASP A 229 2047 1975 2163 68 79 98 O ATOM 1590 CB ASP A 229 -26.982 -45.180 -37.186 1.00 16.35 C ANISOU 1590 CB ASP A 229 2071 1974 2166 48 77 94 C ATOM 1591 CG ASP A 229 -26.653 -43.949 -36.347 1.00 17.21 C ANISOU 1591 CG ASP A 229 2159 2082 2298 21 97 101 C ATOM 1592 OD1 ASP A 229 -26.237 -44.074 -35.177 1.00 16.24 O ANISOU 1592 OD1 ASP A 229 2018 1963 2189 -3 89 95 O ATOM 1593 OD2 ASP A 229 -26.829 -42.822 -36.879 1.00 19.43 O ANISOU 1593 OD2 ASP A 229 2443 2357 2583 26 120 113 O ATOM 1594 N LEU A 230 -25.317 -46.981 -34.626 1.00 15.26 N ANISOU 1594 N LEU A 230 1900 1844 2052 19 52 93 N ATOM 1595 CA LEU A 230 -24.018 -47.244 -34.005 1.00 15.43 C ANISOU 1595 CA LEU A 230 1900 1883 2080 23 54 99 C ATOM 1596 C LEU A 230 -22.973 -46.137 -34.255 1.00 15.44 C ANISOU 1596 C LEU A 230 1872 1899 2096 17 78 103 C ATOM 1597 O LEU A 230 -21.770 -46.394 -34.251 1.00 15.47 O ANISOU 1597 O LEU A 230 1852 1920 2107 30 85 108 O ATOM 1598 CB LEU A 230 -23.490 -48.640 -34.393 1.00 15.59 C ANISOU 1598 CB LEU A 230 1934 1896 2092 55 47 103 C ATOM 1599 CG LEU A 230 -23.961 -49.798 -33.504 1.00 16.51 C ANISOU 1599 CG LEU A 230 2065 1998 2210 53 25 107 C ATOM 1600 CD1 LEU A 230 -25.499 -49.858 -33.355 1.00 16.14 C ANISOU 1600 CD1 LEU A 230 2035 1930 2166 28 14 103 C ATOM 1601 CD2 LEU A 230 -23.436 -51.117 -34.041 1.00 16.97 C ANISOU 1601 CD2 LEU A 230 2144 2038 2266 89 20 109 C ATOM 1602 N ASN A 231 -23.433 -44.894 -34.397 1.00 15.56 N ANISOU 1602 N ASN A 231 1884 1905 2122 -2 93 100 N ATOM 1603 CA ASN A 231 -22.521 -43.748 -34.519 1.00 15.75 C ANISOU 1603 CA ASN A 231 1879 1932 2173 -18 118 104 C ATOM 1604 C ASN A 231 -21.647 -43.570 -33.279 1.00 15.91 C ANISOU 1604 C ASN A 231 1862 1972 2213 -42 102 89 C ATOM 1605 O ASN A 231 -20.591 -42.931 -33.345 1.00 15.99 O ANISOU 1605 O ASN A 231 1835 1988 2253 -56 118 90 O ATOM 1606 CB ASN A 231 -23.290 -42.448 -34.794 1.00 16.11 C ANISOU 1606 CB ASN A 231 1935 1954 2231 -33 137 105 C ATOM 1607 CG ASN A 231 -23.978 -41.898 -33.553 1.00 16.29 C ANISOU 1607 CG ASN A 231 1957 1972 2259 -61 117 82 C ATOM 1608 OD1 ASN A 231 -23.341 -41.267 -32.706 1.00 18.29 O ANISOU 1608 OD1 ASN A 231 2184 2229 2536 -87 113 64 O ATOM 1609 ND2 ASN A 231 -25.278 -42.135 -33.438 1.00 15.75 N ANISOU 1609 ND2 ASN A 231 1914 1900 2170 -54 105 79 N ATOM 1610 N HIS A 232 -22.088 -44.128 -32.151 1.00 15.73 N ANISOU 1610 N HIS A 232 1844 1960 2171 -46 71 76 N ATOM 1611 CA HIS A 232 -21.318 -44.056 -30.914 1.00 15.66 C ANISOU 1611 CA HIS A 232 1804 1980 2167 -59 48 59 C ATOM 1612 C HIS A 232 -20.096 -44.970 -30.942 1.00 16.01 C ANISOU 1612 C HIS A 232 1823 2052 2210 -35 41 70 C ATOM 1613 O HIS A 232 -19.208 -44.850 -30.090 1.00 16.36 O ANISOU 1613 O HIS A 232 1829 2128 2261 -41 21 56 O ATOM 1614 CB HIS A 232 -22.206 -44.308 -29.683 1.00 15.69 C ANISOU 1614 CB HIS A 232 1825 1993 2142 -62 23 48 C ATOM 1615 CG HIS A 232 -22.794 -45.684 -29.604 1.00 15.12 C ANISOU 1615 CG HIS A 232 1781 1921 2044 -37 15 70 C ATOM 1616 ND1 HIS A 232 -23.143 -46.423 -30.716 1.00 15.48 N ANISOU 1616 ND1 HIS A 232 1850 1942 2090 -20 27 87 N ATOM 1617 CD2 HIS A 232 -23.156 -46.427 -28.530 1.00 15.73 C ANISOU 1617 CD2 HIS A 232 1868 2014 2095 -27 -2 78 C ATOM 1618 CE1 HIS A 232 -23.654 -47.578 -30.327 1.00 16.76 C ANISOU 1618 CE1 HIS A 232 2032 2098 2237 -6 15 101 C ATOM 1619 NE2 HIS A 232 -23.681 -47.602 -29.006 1.00 15.46 N ANISOU 1619 NE2 HIS A 232 1860 1957 2056 -10 1 102 N ATOM 1620 N ILE A 233 -20.053 -45.856 -31.939 1.00 15.99 N ANISOU 1620 N ILE A 233 1838 2039 2198 -4 56 91 N ATOM 1621 CA ILE A 233 -18.882 -46.671 -32.244 1.00 16.31 C ANISOU 1621 CA ILE A 233 1857 2101 2239 28 58 104 C ATOM 1622 C ILE A 233 -18.122 -46.135 -33.471 1.00 16.43 C ANISOU 1622 C ILE A 233 1851 2116 2278 34 97 117 C ATOM 1623 O ILE A 233 -16.898 -46.028 -33.451 1.00 16.62 O ANISOU 1623 O ILE A 233 1825 2167 2322 38 105 121 O ATOM 1624 CB ILE A 233 -19.307 -48.138 -32.503 1.00 16.45 C ANISOU 1624 CB ILE A 233 1915 2104 2231 67 50 117 C ATOM 1625 CG1 ILE A 233 -19.878 -48.750 -31.222 1.00 17.04 C ANISOU 1625 CG1 ILE A 233 2005 2182 2288 64 21 118 C ATOM 1626 CG2 ILE A 233 -18.119 -48.958 -33.049 1.00 16.52 C ANISOU 1626 CG2 ILE A 233 1907 2129 2239 110 60 131 C ATOM 1627 CD1 ILE A 233 -20.761 -49.977 -31.438 1.00 17.91 C ANISOU 1627 CD1 ILE A 233 2163 2257 2385 84 16 130 C ATOM 1628 N TYR A 234 -18.853 -45.775 -34.524 1.00 16.52 N ANISOU 1628 N TYR A 234 1895 2100 2283 38 122 125 N ATOM 1629 CA TYR A 234 -18.243 -45.463 -35.821 1.00 16.94 C ANISOU 1629 CA TYR A 234 1939 2155 2344 58 165 146 C ATOM 1630 C TYR A 234 -18.085 -43.971 -36.126 1.00 17.81 C ANISOU 1630 C TYR A 234 2025 2252 2490 24 198 156 C ATOM 1631 O TYR A 234 -17.436 -43.607 -37.107 1.00 18.20 O ANISOU 1631 O TYR A 234 2058 2305 2550 38 242 182 O ATOM 1632 CB TYR A 234 -19.072 -46.117 -36.923 1.00 16.86 C ANISOU 1632 CB TYR A 234 1983 2127 2295 97 171 151 C ATOM 1633 CG TYR A 234 -19.150 -47.619 -36.800 1.00 16.67 C ANISOU 1633 CG TYR A 234 1986 2103 2246 131 145 141 C ATOM 1634 CD1 TYR A 234 -18.020 -48.414 -37.011 1.00 16.89 C ANISOU 1634 CD1 TYR A 234 1995 2151 2272 170 154 150 C ATOM 1635 CD2 TYR A 234 -20.345 -48.253 -36.480 1.00 16.47 C ANISOU 1635 CD2 TYR A 234 2001 2053 2205 126 113 126 C ATOM 1636 CE1 TYR A 234 -18.081 -49.796 -36.904 1.00 17.33 C ANISOU 1636 CE1 TYR A 234 2079 2196 2309 205 132 142 C ATOM 1637 CE2 TYR A 234 -20.416 -49.637 -36.368 1.00 16.93 C ANISOU 1637 CE2 TYR A 234 2084 2098 2251 154 92 119 C ATOM 1638 CZ TYR A 234 -19.284 -50.403 -36.581 1.00 17.48 C ANISOU 1638 CZ TYR A 234 2142 2181 2317 195 101 126 C ATOM 1639 OH TYR A 234 -19.366 -51.769 -36.479 1.00 17.98 O ANISOU 1639 OH TYR A 234 2235 2222 2372 225 82 120 O ATOM 1640 N GLY A 235 -18.691 -43.114 -35.307 1.00 18.23 N ANISOU 1640 N GLY A 235 2079 2287 2560 -18 181 137 N ATOM 1641 CA GLY A 235 -18.699 -41.678 -35.554 1.00 18.99 C ANISOU 1641 CA GLY A 235 2162 2357 2695 -51 212 143 C ATOM 1642 C GLY A 235 -19.946 -41.231 -36.297 1.00 19.56 C ANISOU 1642 C GLY A 235 2286 2400 2747 -38 228 155 C ATOM 1643 O GLY A 235 -20.475 -41.954 -37.142 1.00 19.57 O ANISOU 1643 O GLY A 235 2323 2407 2706 3 230 167 O ATOM 1644 N GLU A 236 -20.413 -40.028 -35.977 1.00 20.27 N ANISOU 1644 N GLU A 236 2379 2459 2865 -70 236 148 N ATOM 1645 CA GLU A 236 -21.589 -39.441 -36.620 1.00 20.95 C ANISOU 1645 CA GLU A 236 2508 2518 2934 -55 251 162 C ATOM 1646 C GLU A 236 -21.299 -39.073 -38.080 1.00 21.81 C ANISOU 1646 C GLU A 236 2626 2619 3040 -24 304 208 C ATOM 1647 O GLU A 236 -22.155 -39.262 -38.951 1.00 22.45 O ANISOU 1647 O GLU A 236 2748 2704 3079 17 308 224 O ATOM 1648 CB GLU A 236 -22.042 -38.211 -35.820 1.00 21.35 C ANISOU 1648 CB GLU A 236 2557 2533 3021 -93 249 141 C ATOM 1649 CG GLU A 236 -23.246 -37.450 -36.367 1.00 22.37 C ANISOU 1649 CG GLU A 236 2727 2633 3139 -75 266 156 C ATOM 1650 CD GLU A 236 -24.568 -38.208 -36.285 1.00 22.70 C ANISOU 1650 CD GLU A 236 2802 2695 3129 -48 232 144 C ATOM 1651 OE1 GLU A 236 -25.414 -37.984 -37.180 1.00 23.60 O ANISOU 1651 OE1 GLU A 236 2945 2802 3220 -15 245 166 O ATOM 1652 OE2 GLU A 236 -24.782 -38.990 -35.331 1.00 21.35 O ANISOU 1652 OE2 GLU A 236 2626 2545 2943 -59 194 116 O ATOM 1653 N THR A 237 -20.089 -38.575 -38.342 1.00 21.97 N ANISOU 1653 N THR A 237 2607 2636 3104 -40 343 231 N ATOM 1654 CA THR A 237 -19.697 -38.090 -39.663 1.00 22.72 C ANISOU 1654 CA THR A 237 2706 2725 3201 -11 405 285 C ATOM 1655 C THR A 237 -18.660 -38.998 -40.329 1.00 22.55 C ANISOU 1655 C THR A 237 2662 2745 3161 22 426 305 C ATOM 1656 O THR A 237 -17.917 -39.722 -39.657 1.00 21.48 O ANISOU 1656 O THR A 237 2491 2635 3036 9 399 281 O ATOM 1657 CB THR A 237 -19.083 -36.671 -39.576 1.00 23.47 C ANISOU 1657 CB THR A 237 2769 2776 3374 -57 451 307 C ATOM 1658 OG1 THR A 237 -17.854 -36.725 -38.839 1.00 25.56 O ANISOU 1658 OG1 THR A 237 2968 3050 3692 -102 444 288 O ATOM 1659 CG2 THR A 237 -20.037 -35.693 -38.888 1.00 24.38 C ANISOU 1659 CG2 THR A 237 2908 2843 3513 -87 434 283 C ATOM 1660 N LEU A 238 -18.599 -38.927 -41.655 1.00 22.66 N ANISOU 1660 N LEU A 238 2698 2768 3143 72 475 352 N ATOM 1661 CA LEU A 238 -17.637 -39.711 -42.432 1.00 23.07 C ANISOU 1661 CA LEU A 238 2733 2861 3171 116 505 375 C ATOM 1662 C LEU A 238 -16.180 -39.375 -42.066 1.00 23.36 C ANISOU 1662 C LEU A 238 2694 2904 3278 77 538 392 C ATOM 1663 O LEU A 238 -15.330 -40.263 -41.995 1.00 23.36 O ANISOU 1663 O LEU A 238 2662 2942 3271 95 532 385 O ATOM 1664 CB LEU A 238 -17.882 -39.494 -43.932 1.00 23.67 C ANISOU 1664 CB LEU A 238 2849 2948 3195 181 558 426 C ATOM 1665 CG LEU A 238 -17.279 -40.513 -44.898 1.00 24.38 C ANISOU 1665 CG LEU A 238 2947 3088 3228 251 579 439 C ATOM 1666 CD1 LEU A 238 -17.735 -41.931 -44.563 1.00 23.03 C ANISOU 1666 CD1 LEU A 238 2804 2937 3009 274 510 381 C ATOM 1667 CD2 LEU A 238 -17.656 -40.152 -46.339 1.00 25.89 C ANISOU 1667 CD2 LEU A 238 3185 3293 3359 320 630 488 C ATOM 1668 N ASP A 239 -15.899 -38.093 -41.830 1.00 23.87 N ANISOU 1668 N ASP A 239 2728 2928 3415 24 571 412 N ATOM 1669 CA ASP A 239 -14.553 -37.648 -41.450 1.00 24.78 C ANISOU 1669 CA ASP A 239 2760 3043 3610 -25 600 423 C ATOM 1670 C ASP A 239 -14.082 -38.336 -40.159 1.00 23.44 C ANISOU 1670 C ASP A 239 2548 2900 3458 -58 532 363 C ATOM 1671 O ASP A 239 -12.956 -38.826 -40.088 1.00 23.69 O ANISOU 1671 O ASP A 239 2520 2971 3510 -56 540 368 O ATOM 1672 CB ASP A 239 -14.521 -36.123 -41.294 1.00 26.06 C ANISOU 1672 CB ASP A 239 2905 3143 3855 -86 637 443 C ATOM 1673 CG ASP A 239 -13.229 -35.615 -40.671 1.00 30.48 C ANISOU 1673 CG ASP A 239 3373 3696 4514 -154 649 436 C ATOM 1674 OD1 ASP A 239 -13.315 -34.913 -39.637 1.00 36.62 O ANISOU 1674 OD1 ASP A 239 4130 4433 5350 -220 612 390 O ATOM 1675 OD2 ASP A 239 -12.134 -35.906 -41.210 1.00 35.46 O ANISOU 1675 OD2 ASP A 239 3948 4362 5162 -141 694 473 O ATOM 1676 N ARG A 240 -14.954 -38.385 -39.156 1.00 21.87 N ANISOU 1676 N ARG A 240 2378 2685 3246 -82 468 311 N ATOM 1677 CA ARG A 240 -14.643 -39.051 -37.888 1.00 20.92 C ANISOU 1677 CA ARG A 240 2228 2593 3129 -104 403 258 C ATOM 1678 C ARG A 240 -14.477 -40.568 -38.080 1.00 20.09 C ANISOU 1678 C ARG A 240 2135 2537 2961 -44 381 256 C ATOM 1679 O ARG A 240 -13.535 -41.172 -37.565 1.00 20.36 O ANISOU 1679 O ARG A 240 2119 2609 3007 -43 362 244 O ATOM 1680 CB ARG A 240 -15.755 -38.773 -36.867 1.00 20.58 C ANISOU 1680 CB ARG A 240 2222 2523 3073 -130 349 211 C ATOM 1681 CG ARG A 240 -15.388 -39.111 -35.437 1.00 20.72 C ANISOU 1681 CG ARG A 240 2204 2566 3101 -160 287 158 C ATOM 1682 CD ARG A 240 -16.509 -38.716 -34.481 1.00 20.86 C ANISOU 1682 CD ARG A 240 2263 2559 3104 -181 245 117 C ATOM 1683 NE ARG A 240 -16.196 -39.096 -33.106 1.00 20.88 N ANISOU 1683 NE ARG A 240 2237 2594 3101 -198 185 69 N ATOM 1684 CZ ARG A 240 -15.504 -38.357 -32.245 1.00 20.77 C ANISOU 1684 CZ ARG A 240 2172 2580 3138 -246 163 30 C ATOM 1685 NH1 ARG A 240 -15.037 -37.162 -32.589 1.00 22.46 N ANISOU 1685 NH1 ARG A 240 2355 2753 3426 -291 197 33 N ATOM 1686 NH2 ARG A 240 -15.278 -38.819 -31.022 1.00 20.05 N ANISOU 1686 NH2 ARG A 240 2062 2529 3025 -247 104 -13 N ATOM 1687 N GLN A 241 -15.400 -41.179 -38.818 1.00 19.11 N ANISOU 1687 N GLN A 241 2079 2411 2772 7 382 266 N ATOM 1688 CA GLN A 241 -15.321 -42.613 -39.121 1.00 18.84 C ANISOU 1688 CA GLN A 241 2066 2410 2681 65 364 261 C ATOM 1689 C GLN A 241 -13.990 -42.979 -39.759 1.00 19.57 C ANISOU 1689 C GLN A 241 2112 2541 2784 97 407 291 C ATOM 1690 O GLN A 241 -13.363 -43.969 -39.387 1.00 18.96 O ANISOU 1690 O GLN A 241 2012 2495 2696 122 384 278 O ATOM 1691 CB GLN A 241 -16.457 -43.025 -40.061 1.00 18.69 C ANISOU 1691 CB GLN A 241 2123 2380 2599 112 366 266 C ATOM 1692 CG GLN A 241 -16.499 -44.525 -40.391 1.00 18.53 C ANISOU 1692 CG GLN A 241 2134 2381 2524 170 343 251 C ATOM 1693 CD GLN A 241 -17.184 -44.802 -41.715 1.00 18.67 C ANISOU 1693 CD GLN A 241 2211 2399 2485 226 361 260 C ATOM 1694 OE1 GLN A 241 -16.542 -45.196 -42.697 1.00 19.71 O ANISOU 1694 OE1 GLN A 241 2345 2556 2589 281 398 280 O ATOM 1695 NE2 GLN A 241 -18.487 -44.564 -41.760 1.00 18.19 N ANISOU 1695 NE2 GLN A 241 2195 2314 2403 217 335 245 N ATOM 1696 N HIS A 242 -13.562 -42.179 -40.725 1.00 20.47 N ANISOU 1696 N HIS A 242 2209 2651 2919 102 474 336 N ATOM 1697 CA HIS A 242 -12.340 -42.479 -41.452 1.00 21.60 C ANISOU 1697 CA HIS A 242 2304 2833 3068 139 527 373 C ATOM 1698 C HIS A 242 -11.092 -42.339 -40.577 1.00 22.18 C ANISOU 1698 C HIS A 242 2285 2932 3212 96 519 366 C ATOM 1699 O HIS A 242 -10.126 -43.072 -40.773 1.00 23.34 O ANISOU 1699 O HIS A 242 2390 3123 3354 135 533 377 O ATOM 1700 CB HIS A 242 -12.276 -41.652 -42.739 1.00 22.21 C ANISOU 1700 CB HIS A 242 2392 2903 3146 160 607 433 C ATOM 1701 CG HIS A 242 -13.176 -42.176 -43.817 1.00 23.92 C ANISOU 1701 CG HIS A 242 2692 3123 3273 233 615 440 C ATOM 1702 ND1 HIS A 242 -13.170 -41.683 -45.104 1.00 26.54 N ANISOU 1702 ND1 HIS A 242 3047 3462 3577 278 685 495 N ATOM 1703 CD2 HIS A 242 -14.085 -43.181 -43.803 1.00 24.02 C ANISOU 1703 CD2 HIS A 242 2770 3137 3220 270 559 398 C ATOM 1704 CE1 HIS A 242 -14.055 -42.344 -45.829 1.00 26.63 C ANISOU 1704 CE1 HIS A 242 3134 3483 3503 342 665 479 C ATOM 1705 NE2 HIS A 242 -14.613 -43.270 -45.068 1.00 25.08 N ANISOU 1705 NE2 HIS A 242 2962 3281 3288 334 589 419 N ATOM 1706 N LYS A 243 -11.129 -41.447 -39.588 1.00 21.86 N ANISOU 1706 N LYS A 243 2209 2864 3232 21 491 341 N ATOM 1707 CA LYS A 243 -10.033 -41.325 -38.616 1.00 22.28 C ANISOU 1707 CA LYS A 243 2173 2945 3349 -24 465 319 C ATOM 1708 C LYS A 243 -9.981 -42.510 -37.642 1.00 21.44 C ANISOU 1708 C LYS A 243 2068 2876 3203 2 394 276 C ATOM 1709 O LYS A 243 -8.924 -42.814 -37.089 1.00 21.38 O ANISOU 1709 O LYS A 243 1987 2912 3225 -1 376 267 O ATOM 1710 CB LYS A 243 -10.167 -40.033 -37.800 1.00 22.77 C ANISOU 1710 CB LYS A 243 2206 2965 3482 -109 447 292 C ATOM 1711 CG LYS A 243 -9.869 -38.747 -38.552 1.00 25.30 C ANISOU 1711 CG LYS A 243 2498 3244 3872 -149 521 336 C ATOM 1712 CD LYS A 243 -10.317 -37.560 -37.699 1.00 27.24 C ANISOU 1712 CD LYS A 243 2742 3431 4176 -227 492 297 C ATOM 1713 CE LYS A 243 -9.701 -36.250 -38.122 1.00 30.48 C ANISOU 1713 CE LYS A 243 3099 3795 4686 -286 556 332 C ATOM 1714 NZ LYS A 243 -10.161 -35.188 -37.175 1.00 31.12 N ANISOU 1714 NZ LYS A 243 3185 3816 4823 -358 518 280 N ATOM 1715 N LEU A 244 -11.127 -43.148 -37.417 1.00 20.37 N ANISOU 1715 N LEU A 244 2013 2722 3005 27 354 254 N ATOM 1716 CA LEU A 244 -11.224 -44.293 -36.510 1.00 19.87 C ANISOU 1716 CA LEU A 244 1964 2683 2902 54 292 222 C ATOM 1717 C LEU A 244 -10.900 -45.625 -37.194 1.00 19.93 C ANISOU 1717 C LEU A 244 1993 2717 2862 134 306 241 C ATOM 1718 O LEU A 244 -10.666 -46.624 -36.515 1.00 19.60 O ANISOU 1718 O LEU A 244 1950 2699 2799 163 265 225 O ATOM 1719 CB LEU A 244 -12.623 -44.359 -35.893 1.00 19.28 C ANISOU 1719 CB LEU A 244 1960 2572 2791 40 248 193 C ATOM 1720 CG LEU A 244 -12.949 -43.249 -34.891 1.00 18.93 C ANISOU 1720 CG LEU A 244 1899 2509 2785 -29 219 162 C ATOM 1721 CD1 LEU A 244 -14.429 -43.239 -34.560 1.00 18.51 C ANISOU 1721 CD1 LEU A 244 1919 2420 2693 -34 194 144 C ATOM 1722 CD2 LEU A 244 -12.111 -43.416 -33.626 1.00 19.91 C ANISOU 1722 CD2 LEU A 244 1961 2674 2928 -46 170 130 C ATOM 1723 N ARG A 245 -10.882 -45.636 -38.525 1.00 19.91 N ANISOU 1723 N ARG A 245 2014 2710 2840 172 363 274 N ATOM 1724 CA ARG A 245 -10.704 -46.877 -39.287 1.00 20.11 C ANISOU 1724 CA ARG A 245 2075 2754 2814 254 377 283 C ATOM 1725 C ARG A 245 -9.239 -47.191 -39.595 1.00 20.91 C ANISOU 1725 C ARG A 245 2101 2907 2935 292 414 309 C ATOM 1726 O ARG A 245 -8.410 -46.291 -39.785 1.00 21.38 O ANISOU 1726 O ARG A 245 2088 2987 3049 260 456 335 O ATOM 1727 CB ARG A 245 -11.536 -46.846 -40.580 1.00 20.09 C ANISOU 1727 CB ARG A 245 2144 2726 2762 290 412 297 C ATOM 1728 CG ARG A 245 -13.010 -47.180 -40.363 1.00 18.36 C ANISOU 1728 CG ARG A 245 2006 2465 2504 283 364 264 C ATOM 1729 CD ARG A 245 -13.833 -47.020 -41.626 1.00 18.11 C ANISOU 1729 CD ARG A 245 2038 2417 2427 316 392 274 C ATOM 1730 NE ARG A 245 -13.395 -47.896 -42.707 1.00 18.56 N ANISOU 1730 NE ARG A 245 2118 2497 2435 397 421 281 N ATOM 1731 CZ ARG A 245 -13.853 -47.845 -43.956 1.00 19.13 C ANISOU 1731 CZ ARG A 245 2241 2571 2457 444 451 290 C ATOM 1732 NH1 ARG A 245 -14.779 -46.961 -44.302 1.00 18.97 N ANISOU 1732 NH1 ARG A 245 2250 2531 2428 420 455 298 N ATOM 1733 NH2 ARG A 245 -13.371 -48.682 -44.874 1.00 20.93 N ANISOU 1733 NH2 ARG A 245 2490 2824 2637 524 476 290 N ATOM 1734 N LEU A 246 -8.934 -48.485 -39.645 1.00 21.33 N ANISOU 1734 N LEU A 246 2173 2979 2951 360 400 302 N ATOM 1735 CA LEU A 246 -7.587 -48.977 -39.968 1.00 22.37 C ANISOU 1735 CA LEU A 246 2241 3164 3093 414 434 325 C ATOM 1736 C LEU A 246 -7.347 -49.019 -41.478 1.00 23.00 C ANISOU 1736 C LEU A 246 2340 3256 3142 475 509 358 C ATOM 1737 O LEU A 246 -6.207 -48.926 -41.935 1.00 23.44 O ANISOU 1737 O LEU A 246 2327 3360 3220 503 562 391 O ATOM 1738 CB LEU A 246 -7.403 -50.385 -39.387 1.00 22.69 C ANISOU 1738 CB LEU A 246 2302 3215 3103 473 389 305 C ATOM 1739 CG LEU A 246 -6.043 -51.079 -39.495 1.00 24.42 C ANISOU 1739 CG LEU A 246 2456 3492 3331 539 412 323 C ATOM 1740 CD1 LEU A 246 -4.956 -50.285 -38.781 1.00 26.16 C ANISOU 1740 CD1 LEU A 246 2555 3763 3619 490 410 335 C ATOM 1741 CD2 LEU A 246 -6.137 -52.499 -38.933 1.00 25.78 C ANISOU 1741 CD2 LEU A 246 2673 3653 3468 600 365 304 C ATOM 1742 N PHE A 247 -8.429 -49.170 -42.239 1.00 22.80 N ANISOU 1742 N PHE A 247 2407 3193 3062 497 512 348 N ATOM 1743 CA PHE A 247 -8.385 -49.351 -43.696 1.00 23.54 C ANISOU 1743 CA PHE A 247 2540 3300 3104 569 573 370 C ATOM 1744 C PHE A 247 -7.653 -50.622 -44.159 1.00 24.23 C ANISOU 1744 C PHE A 247 2635 3419 3152 666 587 365 C ATOM 1745 O PHE A 247 -7.202 -50.720 -45.304 1.00 24.70 O ANISOU 1745 O PHE A 247 2701 3510 3176 734 650 390 O ATOM 1746 CB PHE A 247 -7.869 -48.090 -44.392 1.00 24.07 C ANISOU 1746 CB PHE A 247 2554 3389 3203 545 649 425 C ATOM 1747 CG PHE A 247 -8.833 -46.953 -44.307 1.00 24.26 C ANISOU 1747 CG PHE A 247 2604 3369 3245 475 643 428 C ATOM 1748 CD1 PHE A 247 -8.604 -45.892 -43.445 1.00 24.77 C ANISOU 1748 CD1 PHE A 247 2603 3421 3389 385 636 435 C ATOM 1749 CD2 PHE A 247 -10.009 -46.978 -45.042 1.00 24.64 C ANISOU 1749 CD2 PHE A 247 2743 3389 3231 501 637 417 C ATOM 1750 CE1 PHE A 247 -9.516 -44.862 -43.347 1.00 25.01 C ANISOU 1750 CE1 PHE A 247 2663 3405 3435 327 630 436 C ATOM 1751 CE2 PHE A 247 -10.923 -45.949 -44.948 1.00 25.40 C ANISOU 1751 CE2 PHE A 247 2864 3447 3342 443 630 422 C ATOM 1752 CZ PHE A 247 -10.673 -44.887 -44.097 1.00 24.98 C ANISOU 1752 CZ PHE A 247 2748 3375 3368 358 629 433 C ATOM 1753 N LYS A 248 -7.575 -51.597 -43.262 1.00 24.39 N ANISOU 1753 N LYS A 248 2661 3430 3177 678 531 334 N ATOM 1754 CA LYS A 248 -7.179 -52.948 -43.608 1.00 25.26 C ANISOU 1754 CA LYS A 248 2804 3548 3246 772 530 319 C ATOM 1755 C LYS A 248 -8.207 -53.902 -43.003 1.00 24.17 C ANISOU 1755 C LYS A 248 2747 3349 3087 769 458 271 C ATOM 1756 O LYS A 248 -8.578 -53.755 -41.834 1.00 23.75 O ANISOU 1756 O LYS A 248 2681 3276 3067 706 407 262 O ATOM 1757 CB LYS A 248 -5.783 -53.251 -43.066 1.00 26.27 C ANISOU 1757 CB LYS A 248 2839 3731 3413 799 543 341 C ATOM 1758 CG LYS A 248 -5.314 -54.663 -43.349 1.00 29.22 C ANISOU 1758 CG LYS A 248 3245 4109 3748 903 544 327 C ATOM 1759 CD LYS A 248 -3.801 -54.787 -43.294 1.00 33.08 C ANISOU 1759 CD LYS A 248 3633 4671 4267 951 585 361 C ATOM 1760 CE LYS A 248 -3.340 -56.139 -43.819 1.00 35.09 C ANISOU 1760 CE LYS A 248 3928 4929 4476 1071 600 349 C ATOM 1761 NZ LYS A 248 -3.824 -57.260 -42.972 1.00 37.01 N ANISOU 1761 NZ LYS A 248 4232 5118 4711 1088 530 313 N ATOM 1762 N ASP A 249 -8.684 -54.846 -43.817 1.00 23.95 N ANISOU 1762 N ASP A 249 2804 3292 3006 837 456 241 N ATOM 1763 CA ASP A 249 -9.576 -55.928 -43.377 1.00 23.30 C ANISOU 1763 CA ASP A 249 2799 3145 2909 843 394 197 C ATOM 1764 C ASP A 249 -10.888 -55.455 -42.735 1.00 21.71 C ANISOU 1764 C ASP A 249 2629 2897 2723 756 345 179 C ATOM 1765 O ASP A 249 -11.516 -56.197 -41.983 1.00 20.73 O ANISOU 1765 O ASP A 249 2543 2725 2609 740 295 156 O ATOM 1766 CB ASP A 249 -8.824 -56.881 -42.435 1.00 23.86 C ANISOU 1766 CB ASP A 249 2843 3217 3005 876 371 201 C ATOM 1767 CG ASP A 249 -7.670 -57.601 -43.128 1.00 26.15 C ANISOU 1767 CG ASP A 249 3118 3544 3275 979 416 210 C ATOM 1768 OD1 ASP A 249 -6.755 -58.075 -42.428 1.00 28.12 O ANISOU 1768 OD1 ASP A 249 3317 3819 3549 1009 412 228 O ATOM 1769 OD2 ASP A 249 -7.675 -57.691 -44.370 1.00 27.42 O ANISOU 1769 OD2 ASP A 249 3316 3713 3390 1036 456 198 O ATOM 1770 N GLY A 250 -11.298 -54.228 -43.055 1.00 20.95 N ANISOU 1770 N GLY A 250 2517 2814 2630 704 364 194 N ATOM 1771 CA GLY A 250 -12.539 -53.652 -42.545 1.00 19.78 C ANISOU 1771 CA GLY A 250 2394 2628 2493 628 324 180 C ATOM 1772 C GLY A 250 -12.478 -53.129 -41.123 1.00 19.20 C ANISOU 1772 C GLY A 250 2268 2556 2469 555 295 192 C ATOM 1773 O GLY A 250 -13.483 -52.659 -40.583 1.00 18.19 O ANISOU 1773 O GLY A 250 2159 2401 2353 494 263 181 O ATOM 1774 N LYS A 251 -11.294 -53.162 -40.521 1.00 19.47 N ANISOU 1774 N LYS A 251 2234 2631 2533 564 305 214 N ATOM 1775 CA LYS A 251 -11.187 -53.021 -39.073 1.00 19.25 C ANISOU 1775 CA LYS A 251 2165 2608 2541 514 264 216 C ATOM 1776 C LYS A 251 -11.142 -51.577 -38.591 1.00 19.22 C ANISOU 1776 C LYS A 251 2103 2624 2575 437 268 227 C ATOM 1777 O LYS A 251 -10.893 -50.645 -39.363 1.00 19.41 O ANISOU 1777 O LYS A 251 2102 2664 2610 424 313 244 O ATOM 1778 CB LYS A 251 -9.973 -53.806 -38.554 1.00 19.81 C ANISOU 1778 CB LYS A 251 2188 2716 2622 565 260 228 C ATOM 1779 CG LYS A 251 -10.190 -55.317 -38.617 1.00 20.54 C ANISOU 1779 CG LYS A 251 2347 2770 2686 632 241 214 C ATOM 1780 CD LYS A 251 -9.009 -56.097 -38.071 1.00 20.87 C ANISOU 1780 CD LYS A 251 2345 2848 2738 691 238 231 C ATOM 1781 CE LYS A 251 -9.273 -57.590 -38.106 1.00 21.59 C ANISOU 1781 CE LYS A 251 2509 2887 2807 757 221 218 C ATOM 1782 NZ LYS A 251 -8.154 -58.389 -37.521 1.00 23.00 N ANISOU 1782 NZ LYS A 251 2648 3098 2993 823 217 239 N ATOM 1783 N LEU A 252 -11.425 -51.416 -37.301 1.00 19.02 N ANISOU 1783 N LEU A 252 2063 2595 2568 390 222 216 N ATOM 1784 CA LEU A 252 -11.218 -50.165 -36.579 1.00 18.68 C ANISOU 1784 CA LEU A 252 1960 2572 2566 320 215 216 C ATOM 1785 C LEU A 252 -9.831 -50.172 -35.952 1.00 19.12 C ANISOU 1785 C LEU A 252 1928 2685 2653 329 209 224 C ATOM 1786 O LEU A 252 -9.338 -51.220 -35.535 1.00 19.15 O ANISOU 1786 O LEU A 252 1927 2707 2640 380 189 227 O ATOM 1787 CB LEU A 252 -12.275 -50.023 -35.482 1.00 18.37 C ANISOU 1787 CB LEU A 252 1954 2505 2521 273 165 193 C ATOM 1788 CG LEU A 252 -13.710 -49.736 -35.916 1.00 17.53 C ANISOU 1788 CG LEU A 252 1916 2348 2395 248 166 183 C ATOM 1789 CD1 LEU A 252 -14.679 -49.990 -34.769 1.00 17.53 C ANISOU 1789 CD1 LEU A 252 1948 2326 2385 220 119 166 C ATOM 1790 CD2 LEU A 252 -13.828 -48.294 -36.423 1.00 18.26 C ANISOU 1790 CD2 LEU A 252 1987 2437 2514 202 198 188 C ATOM 1791 N LYS A 253 -9.203 -49.001 -35.880 1.00 19.21 N ANISOU 1791 N LYS A 253 1866 2722 2712 279 227 229 N ATOM 1792 CA LYS A 253 -7.920 -48.855 -35.200 1.00 20.18 C ANISOU 1792 CA LYS A 253 1891 2903 2874 274 213 230 C ATOM 1793 C LYS A 253 -8.034 -49.188 -33.719 1.00 19.77 C ANISOU 1793 C LYS A 253 1834 2868 2811 263 143 203 C ATOM 1794 O LYS A 253 -9.096 -49.054 -33.109 1.00 19.23 O ANISOU 1794 O LYS A 253 1820 2765 2721 233 111 184 O ATOM 1795 CB LYS A 253 -7.376 -47.430 -35.337 1.00 20.87 C ANISOU 1795 CB LYS A 253 1902 3000 3026 205 241 233 C ATOM 1796 CG LYS A 253 -6.884 -47.073 -36.722 1.00 23.52 C ANISOU 1796 CG LYS A 253 2218 3339 3381 222 320 272 C ATOM 1797 CD LYS A 253 -6.695 -45.572 -36.889 1.00 25.69 C ANISOU 1797 CD LYS A 253 2440 3599 3724 144 352 280 C ATOM 1798 CE LYS A 253 -5.557 -45.022 -36.041 1.00 28.54 C ANISOU 1798 CE LYS A 253 2685 4003 4157 96 328 265 C ATOM 1799 NZ LYS A 253 -4.223 -45.522 -36.458 1.00 31.36 N ANISOU 1799 NZ LYS A 253 2958 4422 4534 142 362 295 N ATOM 1800 N TYR A 254 -6.911 -49.596 -33.146 1.00 20.11 N ANISOU 1800 N TYR A 254 1805 2971 2866 293 121 205 N ATOM 1801 CA TYR A 254 -6.834 -49.940 -31.735 1.00 20.19 C ANISOU 1801 CA TYR A 254 1802 3012 2858 297 54 185 C ATOM 1802 C TYR A 254 -5.393 -49.811 -31.268 1.00 20.88 C ANISOU 1802 C TYR A 254 1776 3178 2981 307 34 182 C ATOM 1803 O TYR A 254 -4.482 -49.638 -32.086 1.00 21.38 O ANISOU 1803 O TYR A 254 1776 3267 3082 318 79 202 O ATOM 1804 CB TYR A 254 -7.341 -51.372 -31.509 1.00 20.21 C ANISOU 1804 CB TYR A 254 1882 2994 2803 368 37 200 C ATOM 1805 CG TYR A 254 -6.564 -52.422 -32.273 1.00 21.34 C ANISOU 1805 CG TYR A 254 2019 3151 2937 451 69 229 C ATOM 1806 CD1 TYR A 254 -5.510 -53.105 -31.673 1.00 24.10 C ANISOU 1806 CD1 TYR A 254 2313 3561 3283 509 45 240 C ATOM 1807 CD2 TYR A 254 -6.866 -52.721 -33.601 1.00 21.83 C ANISOU 1807 CD2 TYR A 254 2131 3172 2990 478 123 243 C ATOM 1808 CE1 TYR A 254 -4.779 -54.059 -32.372 1.00 25.96 C ANISOU 1808 CE1 TYR A 254 2542 3809 3511 592 77 266 C ATOM 1809 CE2 TYR A 254 -6.143 -53.681 -34.308 1.00 24.24 C ANISOU 1809 CE2 TYR A 254 2435 3491 3283 561 154 263 C ATOM 1810 CZ TYR A 254 -5.103 -54.344 -33.686 1.00 25.78 C ANISOU 1810 CZ TYR A 254 2575 3742 3480 618 132 275 C ATOM 1811 OH TYR A 254 -4.377 -55.293 -34.370 1.00 28.04 O ANISOU 1811 OH TYR A 254 2859 4040 3754 707 165 295 O ATOM 1812 N GLN A 255 -5.194 -49.874 -29.958 1.00 20.80 N ANISOU 1812 N GLN A 255 1737 3210 2956 305 -31 158 N ATOM 1813 CA GLN A 255 -3.860 -50.010 -29.389 1.00 21.75 C ANISOU 1813 CA GLN A 255 1752 3414 3097 331 -64 153 C ATOM 1814 C GLN A 255 -3.846 -51.241 -28.498 1.00 21.84 C ANISOU 1814 C GLN A 255 1797 3455 3047 411 -110 166 C ATOM 1815 O GLN A 255 -4.899 -51.769 -28.131 1.00 20.93 O ANISOU 1815 O GLN A 255 1777 3295 2882 426 -121 172 O ATOM 1816 CB GLN A 255 -3.448 -48.755 -28.609 1.00 22.58 C ANISOU 1816 CB GLN A 255 1774 3556 3251 252 -108 105 C ATOM 1817 CG GLN A 255 -4.337 -48.412 -27.428 1.00 22.28 C ANISOU 1817 CG GLN A 255 1785 3506 3175 219 -167 65 C ATOM 1818 CD GLN A 255 -3.885 -47.166 -26.684 1.00 23.04 C ANISOU 1818 CD GLN A 255 1800 3636 3320 143 -215 7 C ATOM 1819 OE1 GLN A 255 -2.695 -46.880 -26.586 1.00 25.06 O ANISOU 1819 OE1 GLN A 255 1945 3951 3625 133 -232 -8 O ATOM 1820 NE2 GLN A 255 -4.837 -46.431 -26.139 1.00 23.15 N ANISOU 1820 NE2 GLN A 255 1866 3610 3322 91 -237 -31 N ATOM 1821 N VAL A 256 -2.649 -51.711 -28.178 1.00 22.53 N ANISOU 1821 N VAL A 256 1802 3619 3140 465 -132 175 N ATOM 1822 CA VAL A 256 -2.495 -52.877 -27.317 1.00 22.97 C ANISOU 1822 CA VAL A 256 1881 3708 3137 551 -174 194 C ATOM 1823 C VAL A 256 -1.666 -52.468 -26.114 1.00 23.56 C ANISOU 1823 C VAL A 256 1860 3877 3213 546 -248 162 C ATOM 1824 O VAL A 256 -0.504 -52.077 -26.256 1.00 23.77 O ANISOU 1824 O VAL A 256 1771 3969 3289 540 -255 151 O ATOM 1825 CB VAL A 256 -1.856 -54.044 -28.066 1.00 23.45 C ANISOU 1825 CB VAL A 256 1945 3774 3191 647 -134 239 C ATOM 1826 CG1 VAL A 256 -1.844 -55.305 -27.195 1.00 24.35 C ANISOU 1826 CG1 VAL A 256 2102 3905 3245 740 -172 267 C ATOM 1827 CG2 VAL A 256 -2.609 -54.299 -29.369 1.00 22.90 C ANISOU 1827 CG2 VAL A 256 1961 3616 3123 645 -64 257 C ATOM 1828 N ILE A 257 -2.291 -52.520 -24.939 1.00 23.29 N ANISOU 1828 N ILE A 257 1871 3852 3125 547 -304 145 N ATOM 1829 CA ILE A 257 -1.655 -52.120 -23.686 1.00 24.36 C ANISOU 1829 CA ILE A 257 1930 4079 3246 547 -385 106 C ATOM 1830 C ILE A 257 -1.691 -53.313 -22.743 1.00 24.95 C ANISOU 1830 C ILE A 257 2049 4191 3240 648 -422 141 C ATOM 1831 O ILE A 257 -2.767 -53.838 -22.442 1.00 24.24 O ANISOU 1831 O ILE A 257 2067 4044 3097 666 -411 167 O ATOM 1832 CB ILE A 257 -2.372 -50.919 -23.039 1.00 24.04 C ANISOU 1832 CB ILE A 257 1901 4023 3208 456 -420 46 C ATOM 1833 CG1 ILE A 257 -2.526 -49.772 -24.048 1.00 23.90 C ANISOU 1833 CG1 ILE A 257 1862 3947 3271 358 -370 23 C ATOM 1834 CG2 ILE A 257 -1.600 -50.440 -21.814 1.00 25.50 C ANISOU 1834 CG2 ILE A 257 1998 4310 3381 455 -509 -7 C ATOM 1835 CD1 ILE A 257 -3.273 -48.554 -23.495 1.00 23.37 C ANISOU 1835 CD1 ILE A 257 1814 3852 3213 271 -398 -36 C ATOM 1836 N GLY A 258 -0.517 -53.755 -22.306 1.00 26.38 N ANISOU 1836 N GLY A 258 2146 4466 3414 716 -463 148 N ATOM 1837 CA GLY A 258 -0.398 -54.964 -21.488 1.00 27.49 C ANISOU 1837 CA GLY A 258 2323 4644 3478 828 -493 194 C ATOM 1838 C GLY A 258 -0.983 -56.187 -22.177 1.00 27.50 C ANISOU 1838 C GLY A 258 2431 4557 3462 891 -427 261 C ATOM 1839 O GLY A 258 -1.568 -57.049 -21.526 1.00 27.89 O ANISOU 1839 O GLY A 258 2563 4584 3448 951 -434 301 O ATOM 1840 N GLY A 259 -0.835 -56.251 -23.499 1.00 27.51 N ANISOU 1840 N GLY A 259 2430 4505 3518 877 -361 272 N ATOM 1841 CA GLY A 259 -1.367 -57.354 -24.296 1.00 27.18 C ANISOU 1841 CA GLY A 259 2487 4374 3467 930 -300 322 C ATOM 1842 C GLY A 259 -2.864 -57.321 -24.560 1.00 26.31 C ANISOU 1842 C GLY A 259 2496 4156 3346 875 -267 323 C ATOM 1843 O GLY A 259 -3.393 -58.244 -25.179 1.00 26.68 O ANISOU 1843 O GLY A 259 2627 4122 3387 913 -222 357 O ATOM 1844 N GLU A 260 -3.540 -56.257 -24.127 1.00 25.42 N ANISOU 1844 N GLU A 260 2385 4040 3233 786 -289 283 N ATOM 1845 CA GLU A 260 -4.997 -56.143 -24.239 1.00 24.78 C ANISOU 1845 CA GLU A 260 2407 3870 3140 734 -265 283 C ATOM 1846 C GLU A 260 -5.383 -55.048 -25.226 1.00 23.54 C ANISOU 1846 C GLU A 260 2240 3669 3035 640 -229 246 C ATOM 1847 O GLU A 260 -4.763 -53.982 -25.248 1.00 23.18 O ANISOU 1847 O GLU A 260 2109 3673 3027 588 -245 207 O ATOM 1848 CB GLU A 260 -5.602 -55.815 -22.876 1.00 25.13 C ANISOU 1848 CB GLU A 260 2473 3943 3133 717 -315 270 C ATOM 1849 CG GLU A 260 -5.592 -56.970 -21.892 1.00 27.97 C ANISOU 1849 CG GLU A 260 2874 4324 3429 810 -338 321 C ATOM 1850 CD GLU A 260 -6.738 -57.933 -22.115 1.00 30.10 C ANISOU 1850 CD GLU A 260 3260 4493 3685 828 -292 370 C ATOM 1851 OE1 GLU A 260 -7.908 -57.480 -22.189 1.00 31.83 O ANISOU 1851 OE1 GLU A 260 3533 4653 3906 760 -274 356 O ATOM 1852 OE2 GLU A 260 -6.473 -59.144 -22.216 1.00 32.50 O ANISOU 1852 OE2 GLU A 260 3598 4772 3979 910 -275 421 O ATOM 1853 N VAL A 261 -6.417 -55.312 -26.021 1.00 22.36 N ANISOU 1853 N VAL A 261 2177 3428 2889 620 -183 258 N ATOM 1854 CA VAL A 261 -6.908 -54.357 -27.023 1.00 21.46 C ANISOU 1854 CA VAL A 261 2068 3269 2816 543 -145 232 C ATOM 1855 C VAL A 261 -7.799 -53.272 -26.413 1.00 20.86 C ANISOU 1855 C VAL A 261 2007 3183 2738 462 -168 197 C ATOM 1856 O VAL A 261 -8.778 -53.560 -25.717 1.00 20.11 O ANISOU 1856 O VAL A 261 1978 3060 2604 461 -182 205 O ATOM 1857 CB VAL A 261 -7.671 -55.070 -28.167 1.00 20.83 C ANISOU 1857 CB VAL A 261 2074 3102 2739 559 -93 253 C ATOM 1858 CG1 VAL A 261 -8.278 -54.058 -29.146 1.00 20.67 C ANISOU 1858 CG1 VAL A 261 2064 3039 2749 486 -57 229 C ATOM 1859 CG2 VAL A 261 -6.747 -56.008 -28.904 1.00 21.45 C ANISOU 1859 CG2 VAL A 261 2137 3189 2824 639 -65 278 C ATOM 1860 N TYR A 262 -7.443 -52.022 -26.692 1.00 20.72 N ANISOU 1860 N TYR A 262 1925 3184 2764 396 -166 161 N ATOM 1861 CA TYR A 262 -8.210 -50.859 -26.277 1.00 20.07 C ANISOU 1861 CA TYR A 262 1853 3084 2688 318 -181 122 C ATOM 1862 C TYR A 262 -8.375 -49.916 -27.463 1.00 19.66 C ANISOU 1862 C TYR A 262 1793 2988 2691 258 -132 112 C ATOM 1863 O TYR A 262 -7.669 -50.046 -28.464 1.00 19.17 O ANISOU 1863 O TYR A 262 1696 2927 2661 274 -93 130 O ATOM 1864 CB TYR A 262 -7.501 -50.143 -25.126 1.00 21.08 C ANISOU 1864 CB TYR A 262 1905 3288 2817 298 -242 80 C ATOM 1865 CG TYR A 262 -7.538 -50.926 -23.839 1.00 22.47 C ANISOU 1865 CG TYR A 262 2101 3512 2926 358 -293 90 C ATOM 1866 CD1 TYR A 262 -6.431 -51.636 -23.403 1.00 23.89 C ANISOU 1866 CD1 TYR A 262 2224 3763 3088 427 -324 106 C ATOM 1867 CD2 TYR A 262 -8.705 -50.991 -23.082 1.00 24.15 C ANISOU 1867 CD2 TYR A 262 2390 3699 3087 354 -304 91 C ATOM 1868 CE1 TYR A 262 -6.471 -52.372 -22.219 1.00 26.02 C ANISOU 1868 CE1 TYR A 262 2518 4079 3289 491 -368 124 C ATOM 1869 CE2 TYR A 262 -8.756 -51.722 -21.902 1.00 25.36 C ANISOU 1869 CE2 TYR A 262 2565 3897 3172 415 -343 110 C ATOM 1870 CZ TYR A 262 -7.637 -52.407 -21.479 1.00 26.00 C ANISOU 1870 CZ TYR A 262 2594 4049 3234 485 -375 128 C ATOM 1871 OH TYR A 262 -7.692 -53.133 -20.312 1.00 29.27 O ANISOU 1871 OH TYR A 262 3034 4510 3576 553 -411 154 O ATOM 1872 N PRO A 263 -9.316 -48.961 -27.362 1.00 19.19 N ANISOU 1872 N PRO A 263 1765 2887 2638 194 -131 85 N ATOM 1873 CA PRO A 263 -9.435 -47.971 -28.424 1.00 18.88 C ANISOU 1873 CA PRO A 263 1716 2808 2651 139 -85 80 C ATOM 1874 C PRO A 263 -8.140 -47.186 -28.601 1.00 19.31 C ANISOU 1874 C PRO A 263 1665 2905 2768 109 -83 64 C ATOM 1875 O PRO A 263 -7.364 -47.064 -27.658 1.00 19.72 O ANISOU 1875 O PRO A 263 1651 3016 2825 108 -133 37 O ATOM 1876 CB PRO A 263 -10.570 -47.055 -27.932 1.00 18.77 C ANISOU 1876 CB PRO A 263 1745 2756 2631 82 -98 49 C ATOM 1877 CG PRO A 263 -11.304 -47.862 -26.905 1.00 18.48 C ANISOU 1877 CG PRO A 263 1764 2727 2530 118 -133 52 C ATOM 1878 CD PRO A 263 -10.263 -48.706 -26.265 1.00 19.10 C ANISOU 1878 CD PRO A 263 1798 2871 2588 174 -167 63 C ATOM 1879 N PRO A 264 -7.905 -46.650 -29.808 1.00 19.35 N ANISOU 1879 N PRO A 264 1651 2880 2820 85 -24 82 N ATOM 1880 CA PRO A 264 -6.696 -45.883 -30.057 1.00 19.89 C ANISOU 1880 CA PRO A 264 1615 2983 2959 50 -11 76 C ATOM 1881 C PRO A 264 -6.754 -44.528 -29.354 1.00 20.00 C ANISOU 1881 C PRO A 264 1591 2986 3021 -34 -42 25 C ATOM 1882 O PRO A 264 -7.790 -44.158 -28.798 1.00 19.57 O ANISOU 1882 O PRO A 264 1599 2897 2939 -58 -66 -2 O ATOM 1883 CB PRO A 264 -6.713 -45.710 -31.574 1.00 19.71 C ANISOU 1883 CB PRO A 264 1606 2921 2962 53 70 118 C ATOM 1884 CG PRO A 264 -8.159 -45.639 -31.904 1.00 19.30 C ANISOU 1884 CG PRO A 264 1660 2803 2871 46 84 121 C ATOM 1885 CD PRO A 264 -8.877 -46.505 -30.907 1.00 18.85 C ANISOU 1885 CD PRO A 264 1661 2750 2750 78 30 106 C ATOM 1886 N THR A 265 -5.649 -43.794 -29.384 1.00 20.97 N ANISOU 1886 N THR A 265 1611 3139 3219 -77 -41 10 N ATOM 1887 CA THR A 265 -5.577 -42.509 -28.692 1.00 21.35 C ANISOU 1887 CA THR A 265 1616 3174 3323 -159 -76 -48 C ATOM 1888 C THR A 265 -6.051 -41.358 -29.565 1.00 21.32 C ANISOU 1888 C THR A 265 1633 3090 3379 -222 -14 -36 C ATOM 1889 O THR A 265 -6.110 -41.465 -30.802 1.00 21.20 O ANISOU 1889 O THR A 265 1637 3044 3373 -205 60 21 O ATOM 1890 CB THR A 265 -4.149 -42.191 -28.231 1.00 22.47 C ANISOU 1890 CB THR A 265 1627 3381 3530 -186 -112 -78 C ATOM 1891 OG1 THR A 265 -3.309 -41.975 -29.375 1.00 24.01 O ANISOU 1891 OG1 THR A 265 1753 3573 3796 -199 -41 -32 O ATOM 1892 CG2 THR A 265 -3.593 -43.325 -27.382 1.00 22.53 C ANISOU 1892 CG2 THR A 265 1608 3477 3477 -114 -174 -85 C ATOM 1893 N VAL A 266 -6.385 -40.255 -28.900 1.00 21.40 N ANISOU 1893 N VAL A 266 1641 3065 3425 -290 -45 -91 N ATOM 1894 CA VAL A 266 -6.681 -38.994 -29.568 1.00 21.50 C ANISOU 1894 CA VAL A 266 1660 2998 3511 -357 7 -86 C ATOM 1895 C VAL A 266 -5.485 -38.521 -30.399 1.00 22.64 C ANISOU 1895 C VAL A 266 1705 3146 3753 -393 62 -53 C ATOM 1896 O VAL A 266 -5.645 -38.040 -31.519 1.00 21.85 O ANISOU 1896 O VAL A 266 1622 2992 3689 -407 142 -1 O ATOM 1897 CB VAL A 266 -7.073 -37.917 -28.532 1.00 21.85 C ANISOU 1897 CB VAL A 266 1708 3009 3583 -421 -47 -164 C ATOM 1898 CG1 VAL A 266 -7.053 -36.517 -29.148 1.00 22.37 C ANISOU 1898 CG1 VAL A 266 1757 2991 3750 -499 5 -163 C ATOM 1899 CG2 VAL A 266 -8.459 -38.244 -27.956 1.00 20.95 C ANISOU 1899 CG2 VAL A 266 1705 2879 3376 -385 -75 -181 C ATOM 1900 N LYS A 267 -4.285 -38.665 -29.854 1.00 23.93 N ANISOU 1900 N LYS A 267 1761 3376 3956 -405 21 -81 N ATOM 1901 CA LYS A 267 -3.090 -38.210 -30.557 1.00 25.93 C ANISOU 1901 CA LYS A 267 1904 3639 4310 -444 72 -50 C ATOM 1902 C LYS A 267 -2.858 -38.988 -31.854 1.00 26.18 C ANISOU 1902 C LYS A 267 1946 3686 4316 -378 156 39 C ATOM 1903 O LYS A 267 -2.481 -38.410 -32.873 1.00 26.42 O ANISOU 1903 O LYS A 267 1942 3684 4413 -406 238 90 O ATOM 1904 CB LYS A 267 -1.865 -38.322 -29.655 1.00 27.16 C ANISOU 1904 CB LYS A 267 1936 3876 4507 -462 1 -101 C ATOM 1905 CG LYS A 267 -0.553 -37.980 -30.363 1.00 30.00 C ANISOU 1905 CG LYS A 267 2166 4258 4974 -498 55 -65 C ATOM 1906 CD LYS A 267 0.323 -37.053 -29.566 1.00 33.33 C ANISOU 1906 CD LYS A 267 2467 4693 5502 -589 -3 -138 C ATOM 1907 CE LYS A 267 -0.174 -35.621 -29.607 1.00 34.66 C ANISOU 1907 CE LYS A 267 2658 4754 5756 -687 17 -169 C ATOM 1908 NZ LYS A 267 0.985 -34.684 -29.693 1.00 36.33 N ANISOU 1908 NZ LYS A 267 2728 4957 6119 -783 30 -186 N ATOM 1909 N ASP A 268 -3.065 -40.299 -31.797 1.00 26.10 N ANISOU 1909 N ASP A 268 1984 3725 4209 -289 137 56 N ATOM 1910 CA ASP A 268 -2.849 -41.184 -32.941 1.00 26.85 C ANISOU 1910 CA ASP A 268 2095 3839 4266 -214 206 127 C ATOM 1911 C ASP A 268 -3.888 -40.944 -34.047 1.00 26.11 C ANISOU 1911 C ASP A 268 2104 3673 4144 -202 278 174 C ATOM 1912 O ASP A 268 -3.536 -40.870 -35.228 1.00 26.94 O ANISOU 1912 O ASP A 268 2195 3773 4269 -184 361 234 O ATOM 1913 CB ASP A 268 -2.859 -42.640 -32.445 1.00 26.93 C ANISOU 1913 CB ASP A 268 2138 3910 4186 -124 157 123 C ATOM 1914 CG ASP A 268 -2.803 -43.663 -33.562 1.00 29.45 C ANISOU 1914 CG ASP A 268 2496 4241 4454 -37 220 185 C ATOM 1915 OD1 ASP A 268 -3.454 -44.716 -33.411 1.00 34.35 O ANISOU 1915 OD1 ASP A 268 3199 4861 4990 29 195 186 O ATOM 1916 OD2 ASP A 268 -2.103 -43.453 -34.569 1.00 34.58 O ANISOU 1916 OD2 ASP A 268 3093 4900 5147 -32 293 232 O ATOM 1917 N THR A 269 -5.152 -40.793 -33.655 1.00 24.79 N ANISOU 1917 N THR A 269 2035 3456 3928 -211 247 146 N ATOM 1918 CA THR A 269 -6.273 -40.688 -34.594 1.00 23.85 C ANISOU 1918 CA THR A 269 2018 3277 3767 -190 299 182 C ATOM 1919 C THR A 269 -6.638 -39.259 -35.013 1.00 24.36 C ANISOU 1919 C THR A 269 2089 3268 3897 -259 344 192 C ATOM 1920 O THR A 269 -7.218 -39.065 -36.074 1.00 23.34 O ANISOU 1920 O THR A 269 2019 3100 3749 -237 407 240 O ATOM 1921 CB THR A 269 -7.551 -41.325 -34.006 1.00 22.80 C ANISOU 1921 CB THR A 269 1988 3128 3546 -157 245 153 C ATOM 1922 OG1 THR A 269 -7.920 -40.644 -32.798 1.00 21.47 O ANISOU 1922 OG1 THR A 269 1818 2943 3396 -214 183 92 O ATOM 1923 CG2 THR A 269 -7.345 -42.814 -33.717 1.00 22.47 C ANISOU 1923 CG2 THR A 269 1960 3143 3437 -81 211 154 C ATOM 1924 N GLN A 270 -6.309 -38.269 -34.186 1.00 25.66 N ANISOU 1924 N GLN A 270 2198 3414 4139 -338 310 145 N ATOM 1925 CA GLN A 270 -6.804 -36.895 -34.372 1.00 27.15 C ANISOU 1925 CA GLN A 270 2406 3519 4392 -405 342 143 C ATOM 1926 C GLN A 270 -8.319 -36.745 -34.218 1.00 26.58 C ANISOU 1926 C GLN A 270 2449 3394 4255 -391 324 127 C ATOM 1927 O GLN A 270 -8.867 -35.747 -34.683 1.00 26.55 O ANISOU 1927 O GLN A 270 2480 3320 4288 -423 367 145 O ATOM 1928 CB GLN A 270 -6.412 -36.313 -35.747 1.00 28.19 C ANISOU 1928 CB GLN A 270 2516 3616 4577 -412 447 223 C ATOM 1929 CG GLN A 270 -5.245 -35.378 -35.729 1.00 32.40 C ANISOU 1929 CG GLN A 270 2936 4137 5238 -490 477 227 C ATOM 1930 CD GLN A 270 -3.956 -36.085 -35.985 1.00 35.75 C ANISOU 1930 CD GLN A 270 3261 4641 5681 -464 495 254 C ATOM 1931 OE1 GLN A 270 -3.040 -35.528 -36.596 1.00 39.88 O ANISOU 1931 OE1 GLN A 270 3699 5159 6293 -500 562 300 O ATOM 1932 NE2 GLN A 270 -3.867 -37.328 -35.529 1.00 37.27 N ANISOU 1932 NE2 GLN A 270 3461 4908 5792 -399 439 231 N ATOM 1933 N VAL A 271 -9.001 -37.698 -33.583 1.00 26.41 N ANISOU 1933 N VAL A 271 2484 3406 4144 -344 266 97 N ATOM 1934 CA VAL A 271 -10.450 -37.536 -33.360 1.00 26.43 C ANISOU 1934 CA VAL A 271 2585 3364 4093 -334 248 80 C ATOM 1935 C VAL A 271 -10.680 -36.747 -32.066 1.00 27.00 C ANISOU 1935 C VAL A 271 2649 3416 4194 -390 187 6 C ATOM 1936 O VAL A 271 -10.011 -36.977 -31.051 1.00 27.60 O ANISOU 1936 O VAL A 271 2671 3540 4277 -404 126 -44 O ATOM 1937 CB VAL A 271 -11.270 -38.868 -33.371 1.00 26.09 C ANISOU 1937 CB VAL A 271 2615 3353 3944 -260 224 89 C ATOM 1938 CG1 VAL A 271 -10.691 -39.870 -34.360 1.00 25.91 C ANISOU 1938 CG1 VAL A 271 2582 3369 3893 -201 264 142 C ATOM 1939 CG2 VAL A 271 -11.416 -39.467 -31.991 1.00 27.10 C ANISOU 1939 CG2 VAL A 271 2745 3521 4030 -253 144 35 C ATOM 1940 N GLU A 272 -11.598 -35.790 -32.131 1.00 26.59 N ANISOU 1940 N GLU A 272 2651 3295 4157 -417 203 -3 N ATOM 1941 CA GLU A 272 -11.943 -34.961 -30.981 1.00 27.18 C ANISOU 1941 CA GLU A 272 2731 3341 4256 -463 151 -76 C ATOM 1942 C GLU A 272 -12.642 -35.819 -29.917 1.00 25.25 C ANISOU 1942 C GLU A 272 2530 3145 3917 -422 83 -117 C ATOM 1943 O GLU A 272 -13.544 -36.595 -30.234 1.00 24.81 O ANISOU 1943 O GLU A 272 2541 3099 3788 -369 92 -85 O ATOM 1944 CB GLU A 272 -12.866 -33.812 -31.410 1.00 27.73 C ANISOU 1944 CB GLU A 272 2858 3321 4356 -487 193 -67 C ATOM 1945 CG GLU A 272 -12.241 -32.803 -32.375 1.00 31.75 C ANISOU 1945 CG GLU A 272 3330 3770 4965 -531 265 -22 C ATOM 1946 CD GLU A 272 -13.236 -31.740 -32.848 1.00 35.19 C ANISOU 1946 CD GLU A 272 3833 4116 5423 -540 310 -3 C ATOM 1947 OE1 GLU A 272 -12.795 -30.716 -33.407 1.00 38.60 O ANISOU 1947 OE1 GLU A 272 4239 4482 5947 -585 366 25 O ATOM 1948 OE2 GLU A 272 -14.460 -31.929 -32.667 1.00 38.37 O ANISOU 1948 OE2 GLU A 272 4312 4513 5753 -500 293 -11 O ATOM 1949 N MET A 273 -12.194 -35.695 -28.668 1.00 24.90 N ANISOU 1949 N MET A 273 2447 3135 3879 -445 14 -187 N ATOM 1950 CA MET A 273 -12.873 -36.289 -27.506 1.00 23.62 C ANISOU 1950 CA MET A 273 2328 3016 3631 -409 -48 -228 C ATOM 1951 C MET A 273 -12.937 -35.248 -26.392 1.00 24.31 C ANISOU 1951 C MET A 273 2407 3085 3746 -454 -98 -314 C ATOM 1952 O MET A 273 -12.112 -34.346 -26.343 1.00 24.74 O ANISOU 1952 O MET A 273 2400 3113 3887 -514 -103 -350 O ATOM 1953 CB MET A 273 -12.111 -37.504 -26.975 1.00 23.40 C ANISOU 1953 CB MET A 273 2259 3076 3555 -368 -92 -227 C ATOM 1954 CG MET A 273 -12.047 -38.695 -27.913 1.00 21.57 C ANISOU 1954 CG MET A 273 2041 2867 3287 -313 -53 -154 C ATOM 1955 SD MET A 273 -13.620 -39.545 -28.131 1.00 20.21 S ANISOU 1955 SD MET A 273 1977 2678 3025 -257 -37 -117 S ATOM 1956 CE MET A 273 -14.000 -40.048 -26.456 1.00 19.71 C ANISOU 1956 CE MET A 273 1933 2668 2888 -231 -111 -165 C ATOM 1957 N ILE A 274 -13.911 -35.384 -25.495 1.00 24.07 N ANISOU 1957 N ILE A 274 2437 3067 3643 -425 -133 -347 N ATOM 1958 CA ILE A 274 -13.982 -34.515 -24.321 1.00 24.85 C ANISOU 1958 CA ILE A 274 2533 3160 3748 -454 -188 -437 C ATOM 1959 C ILE A 274 -13.175 -35.139 -23.180 1.00 25.36 C ANISOU 1959 C ILE A 274 2549 3318 3770 -435 -264 -485 C ATOM 1960 O ILE A 274 -13.538 -36.193 -22.659 1.00 24.91 O ANISOU 1960 O ILE A 274 2522 3323 3621 -374 -287 -466 O ATOM 1961 CB ILE A 274 -15.433 -34.278 -23.855 1.00 24.57 C ANISOU 1961 CB ILE A 274 2584 3099 3651 -425 -185 -451 C ATOM 1962 CG1 ILE A 274 -16.279 -33.686 -24.985 1.00 24.50 C ANISOU 1962 CG1 ILE A 274 2625 3006 3679 -434 -113 -401 C ATOM 1963 CG2 ILE A 274 -15.446 -33.340 -22.648 1.00 25.33 C ANISOU 1963 CG2 ILE A 274 2681 3191 3753 -449 -241 -551 C ATOM 1964 CD1 ILE A 274 -17.765 -33.654 -24.675 1.00 25.56 C ANISOU 1964 CD1 ILE A 274 2839 3126 3748 -395 -104 -399 C ATOM 1965 N TYR A 275 -12.067 -34.494 -22.824 1.00 26.58 N ANISOU 1965 N TYR A 275 2624 3480 3994 -486 -304 -545 N ATOM 1966 CA TYR A 275 -11.242 -34.900 -21.688 1.00 27.50 C ANISOU 1966 CA TYR A 275 2686 3688 4074 -471 -387 -605 C ATOM 1967 C TYR A 275 -10.663 -33.657 -21.025 1.00 29.20 C ANISOU 1967 C TYR A 275 2852 3880 4363 -539 -440 -709 C ATOM 1968 O TYR A 275 -10.274 -32.720 -21.720 1.00 29.33 O ANISOU 1968 O TYR A 275 2832 3820 4491 -609 -404 -714 O ATOM 1969 CB TYR A 275 -10.063 -35.757 -22.141 1.00 27.54 C ANISOU 1969 CB TYR A 275 2612 3754 4100 -459 -387 -560 C ATOM 1970 CG TYR A 275 -10.387 -37.177 -22.525 1.00 25.78 C ANISOU 1970 CG TYR A 275 2427 3573 3796 -384 -359 -475 C ATOM 1971 CD1 TYR A 275 -10.315 -37.591 -23.850 1.00 25.06 C ANISOU 1971 CD1 TYR A 275 2337 3450 3736 -378 -286 -393 C ATOM 1972 CD2 TYR A 275 -10.724 -38.118 -21.561 1.00 25.23 C ANISOU 1972 CD2 TYR A 275 2391 3574 3619 -315 -404 -478 C ATOM 1973 CE1 TYR A 275 -10.601 -38.901 -24.208 1.00 24.42 C ANISOU 1973 CE1 TYR A 275 2293 3400 3586 -310 -264 -324 C ATOM 1974 CE2 TYR A 275 -11.010 -39.428 -21.907 1.00 24.47 C ANISOU 1974 CE2 TYR A 275 2332 3506 3461 -250 -377 -401 C ATOM 1975 CZ TYR A 275 -10.947 -39.814 -23.235 1.00 23.75 C ANISOU 1975 CZ TYR A 275 2242 3375 3407 -250 -309 -329 C ATOM 1976 OH TYR A 275 -11.224 -41.115 -23.586 1.00 23.20 O ANISOU 1976 OH TYR A 275 2211 3326 3280 -186 -286 -262 O ATOM 1977 N PRO A 276 -10.572 -33.657 -19.682 1.00 30.68 N ANISOU 1977 N PRO A 276 3035 4132 4488 -517 -524 -793 N ATOM 1978 CA PRO A 276 -9.749 -32.649 -19.005 1.00 32.64 C ANISOU 1978 CA PRO A 276 3217 4378 4807 -580 -592 -904 C ATOM 1979 C PRO A 276 -8.325 -32.658 -19.563 1.00 34.04 C ANISOU 1979 C PRO A 276 3276 4572 5086 -632 -595 -893 C ATOM 1980 O PRO A 276 -7.836 -33.717 -19.940 1.00 33.69 O ANISOU 1980 O PRO A 276 3197 4591 5012 -590 -582 -823 O ATOM 1981 CB PRO A 276 -9.745 -33.119 -17.547 1.00 33.02 C ANISOU 1981 CB PRO A 276 3274 4531 4740 -519 -684 -973 C ATOM 1982 CG PRO A 276 -10.979 -33.924 -17.396 1.00 31.84 C ANISOU 1982 CG PRO A 276 3225 4400 4472 -439 -650 -909 C ATOM 1983 CD PRO A 276 -11.240 -34.562 -18.731 1.00 30.19 C ANISOU 1983 CD PRO A 276 3033 4150 4289 -432 -560 -790 C ATOM 1984 N PRO A 277 -7.653 -31.492 -19.602 1.00 36.19 N ANISOU 1984 N PRO A 277 3483 4786 5482 -721 -612 -963 N ATOM 1985 CA PRO A 277 -6.338 -31.407 -20.251 1.00 37.30 C ANISOU 1985 CA PRO A 277 3504 4933 5737 -780 -601 -944 C ATOM 1986 C PRO A 277 -5.218 -32.250 -19.615 1.00 38.36 C ANISOU 1986 C PRO A 277 3542 5197 5837 -749 -679 -968 C ATOM 1987 O PRO A 277 -4.201 -32.500 -20.269 1.00 39.11 O ANISOU 1987 O PRO A 277 3540 5314 6004 -774 -656 -924 O ATOM 1988 CB PRO A 277 -5.994 -29.912 -20.147 1.00 38.63 C ANISOU 1988 CB PRO A 277 3631 5007 6040 -885 -616 -1033 C ATOM 1989 CG PRO A 277 -6.803 -29.410 -19.001 1.00 38.86 C ANISOU 1989 CG PRO A 277 3737 5029 6001 -866 -681 -1135 C ATOM 1990 CD PRO A 277 -8.080 -30.192 -19.055 1.00 36.91 C ANISOU 1990 CD PRO A 277 3606 4798 5618 -774 -640 -1063 C ATOM 1991 N HIS A 278 -5.397 -32.679 -18.366 1.00 38.59 N ANISOU 1991 N HIS A 278 3595 5314 5752 -689 -767 -1032 N ATOM 1992 CA HIS A 278 -4.350 -33.408 -17.641 1.00 39.52 C ANISOU 1992 CA HIS A 278 3624 5562 5830 -652 -852 -1063 C ATOM 1993 C HIS A 278 -4.369 -34.932 -17.848 1.00 37.91 C ANISOU 1993 C HIS A 278 3440 5441 5523 -552 -827 -960 C ATOM 1994 O HIS A 278 -3.476 -35.624 -17.356 1.00 38.68 O ANISOU 1994 O HIS A 278 3464 5646 5588 -511 -889 -969 O ATOM 1995 CB HIS A 278 -4.435 -33.097 -16.138 1.00 40.87 C ANISOU 1995 CB HIS A 278 3807 5796 5925 -630 -965 -1188 C ATOM 1996 CG HIS A 278 -5.682 -33.611 -15.487 1.00 41.33 C ANISOU 1996 CG HIS A 278 3993 5877 5832 -541 -964 -1172 C ATOM 1997 ND1 HIS A 278 -6.868 -32.906 -15.488 1.00 42.87 N ANISOU 1997 ND1 HIS A 278 4290 5981 6017 -554 -925 -1189 N ATOM 1998 CD2 HIS A 278 -5.930 -34.764 -14.822 1.00 42.41 C ANISOU 1998 CD2 HIS A 278 4170 6116 5828 -437 -992 -1135 C ATOM 1999 CE1 HIS A 278 -7.793 -33.604 -14.852 1.00 42.40 C ANISOU 1999 CE1 HIS A 278 4322 5971 5816 -464 -929 -1164 C ATOM 2000 NE2 HIS A 278 -7.250 -34.735 -14.438 1.00 42.36 N ANISOU 2000 NE2 HIS A 278 4283 6080 5732 -393 -967 -1129 N ATOM 2001 N ILE A 279 -5.367 -35.459 -18.557 1.00 35.51 N ANISOU 2001 N ILE A 279 3233 5088 5171 -511 -743 -865 N ATOM 2002 CA ILE A 279 -5.440 -36.909 -18.787 1.00 34.01 C ANISOU 2002 CA ILE A 279 3070 4962 4892 -420 -717 -770 C ATOM 2003 C ILE A 279 -4.226 -37.359 -19.611 1.00 33.70 C ANISOU 2003 C ILE A 279 2925 4953 4925 -430 -691 -717 C ATOM 2004 O ILE A 279 -3.931 -36.762 -20.645 1.00 33.99 O ANISOU 2004 O ILE A 279 2924 4920 5072 -496 -628 -690 O ATOM 2005 CB ILE A 279 -6.745 -37.333 -19.510 1.00 32.53 C ANISOU 2005 CB ILE A 279 3000 4704 4655 -386 -629 -683 C ATOM 2006 CG1 ILE A 279 -7.978 -36.935 -18.691 1.00 32.28 C ANISOU 2006 CG1 ILE A 279 3067 4647 4549 -370 -648 -728 C ATOM 2007 CG2 ILE A 279 -6.761 -38.843 -19.752 1.00 31.58 C ANISOU 2007 CG2 ILE A 279 2904 4640 4455 -297 -606 -592 C ATOM 2008 CD1 ILE A 279 -7.999 -37.510 -17.285 1.00 33.10 C ANISOU 2008 CD1 ILE A 279 3186 4855 4535 -298 -731 -772 C ATOM 2009 N PRO A 280 -3.501 -38.394 -19.141 1.00 33.03 N ANISOU 2009 N PRO A 280 2792 4977 4781 -359 -739 -701 N ATOM 2010 CA PRO A 280 -2.349 -38.909 -19.887 1.00 32.79 C ANISOU 2010 CA PRO A 280 2660 4987 4811 -355 -714 -649 C ATOM 2011 C PRO A 280 -2.671 -39.290 -21.333 1.00 30.91 C ANISOU 2011 C PRO A 280 2462 4679 4605 -350 -600 -543 C ATOM 2012 O PRO A 280 -3.764 -39.781 -21.621 1.00 29.19 O ANISOU 2012 O PRO A 280 2357 4417 4318 -307 -553 -491 O ATOM 2013 CB PRO A 280 -1.950 -40.156 -19.093 1.00 33.19 C ANISOU 2013 CB PRO A 280 2700 5156 4755 -251 -774 -632 C ATOM 2014 CG PRO A 280 -2.383 -39.864 -17.703 1.00 34.01 C ANISOU 2014 CG PRO A 280 2842 5303 4778 -233 -863 -717 C ATOM 2015 CD PRO A 280 -3.641 -39.057 -17.831 1.00 33.35 C ANISOU 2015 CD PRO A 280 2861 5115 4697 -279 -822 -735 C ATOM 2016 N GLU A 281 -1.707 -39.078 -22.224 1.00 30.39 N ANISOU 2016 N GLU A 281 2299 4606 4640 -390 -557 -514 N ATOM 2017 CA GLU A 281 -1.908 -39.292 -23.655 1.00 29.23 C ANISOU 2017 CA GLU A 281 2182 4396 4529 -389 -447 -421 C ATOM 2018 C GLU A 281 -2.537 -40.646 -23.977 1.00 28.20 C ANISOU 2018 C GLU A 281 2143 4279 4292 -288 -412 -343 C ATOM 2019 O GLU A 281 -3.524 -40.710 -24.707 1.00 26.32 O ANISOU 2019 O GLU A 281 2001 3968 4032 -281 -346 -296 O ATOM 2020 CB GLU A 281 -0.573 -39.153 -24.395 1.00 30.01 C ANISOU 2020 CB GLU A 281 2147 4521 4733 -421 -414 -394 C ATOM 2021 CG GLU A 281 -0.672 -39.326 -25.898 1.00 29.07 C ANISOU 2021 CG GLU A 281 2051 4346 4648 -415 -298 -299 C ATOM 2022 CD GLU A 281 0.672 -39.171 -26.581 1.00 29.27 C ANISOU 2022 CD GLU A 281 1939 4405 4776 -443 -260 -269 C ATOM 2023 OE1 GLU A 281 1.012 -40.009 -27.432 1.00 27.93 O ANISOU 2023 OE1 GLU A 281 1762 4262 4587 -381 -199 -193 O ATOM 2024 OE2 GLU A 281 1.392 -38.212 -26.260 1.00 31.85 O ANISOU 2024 OE2 GLU A 281 2164 4732 5206 -528 -291 -325 O ATOM 2025 N ASN A 282 -1.966 -41.725 -23.440 1.00 28.68 N ANISOU 2025 N ASN A 282 2173 4433 4290 -210 -458 -331 N ATOM 2026 CA ASN A 282 -2.459 -43.073 -23.766 1.00 28.42 C ANISOU 2026 CA ASN A 282 2223 4408 4168 -114 -423 -256 C ATOM 2027 C ASN A 282 -3.827 -43.392 -23.167 1.00 27.09 C ANISOU 2027 C ASN A 282 2183 4207 3904 -82 -437 -258 C ATOM 2028 O ASN A 282 -4.498 -44.320 -23.632 1.00 26.91 O ANISOU 2028 O ASN A 282 2242 4156 3825 -25 -393 -196 O ATOM 2029 CB ASN A 282 -1.435 -44.162 -23.385 1.00 29.62 C ANISOU 2029 CB ASN A 282 2308 4662 4285 -32 -462 -235 C ATOM 2030 CG ASN A 282 -0.520 -44.560 -24.550 1.00 31.54 C ANISOU 2030 CG ASN A 282 2482 4916 4587 -14 -397 -175 C ATOM 2031 OD1 ASN A 282 0.275 -45.493 -24.430 1.00 35.72 O ANISOU 2031 OD1 ASN A 282 2962 5520 5090 61 -414 -148 O ATOM 2032 ND2 ASN A 282 -0.629 -43.856 -25.674 1.00 32.82 N ANISOU 2032 ND2 ASN A 282 2640 5006 4823 -75 -319 -152 N ATOM 2033 N LEU A 283 -4.255 -42.622 -22.166 1.00 27.11 N ANISOU 2033 N LEU A 283 2201 4211 3890 -119 -495 -330 N ATOM 2034 CA LEU A 283 -5.598 -42.793 -21.588 1.00 26.10 C ANISOU 2034 CA LEU A 283 2189 4051 3676 -93 -500 -331 C ATOM 2035 C LEU A 283 -6.663 -41.901 -22.226 1.00 25.42 C ANISOU 2035 C LEU A 283 2171 3861 3626 -155 -444 -333 C ATOM 2036 O LEU A 283 -7.831 -41.976 -21.848 1.00 24.83 O ANISOU 2036 O LEU A 283 2189 3757 3489 -138 -441 -332 O ATOM 2037 CB LEU A 283 -5.570 -42.576 -20.072 1.00 26.74 C ANISOU 2037 CB LEU A 283 2263 4201 3697 -78 -593 -405 C ATOM 2038 CG LEU A 283 -4.773 -43.629 -19.293 1.00 27.22 C ANISOU 2038 CG LEU A 283 2282 4371 3691 7 -652 -393 C ATOM 2039 CD1 LEU A 283 -4.654 -43.249 -17.831 1.00 28.67 C ANISOU 2039 CD1 LEU A 283 2449 4629 3816 19 -748 -475 C ATOM 2040 CD2 LEU A 283 -5.412 -44.998 -19.442 1.00 27.80 C ANISOU 2040 CD2 LEU A 283 2441 4438 3682 94 -612 -306 C ATOM 2041 N GLN A 284 -6.284 -41.064 -23.192 1.00 25.28 N ANISOU 2041 N GLN A 284 2108 3789 3707 -222 -397 -330 N ATOM 2042 CA GLN A 284 -7.287 -40.346 -23.981 1.00 24.49 C ANISOU 2042 CA GLN A 284 2077 3590 3637 -265 -333 -313 C ATOM 2043 C GLN A 284 -7.778 -41.249 -25.108 1.00 23.80 C ANISOU 2043 C GLN A 284 2049 3473 3522 -218 -260 -226 C ATOM 2044 O GLN A 284 -7.403 -41.066 -26.268 1.00 23.67 O ANISOU 2044 O GLN A 284 2006 3423 3564 -236 -198 -185 O ATOM 2045 CB GLN A 284 -6.736 -39.035 -24.544 1.00 24.87 C ANISOU 2045 CB GLN A 284 2059 3586 3803 -354 -306 -340 C ATOM 2046 CG GLN A 284 -6.424 -38.002 -23.477 1.00 26.75 C ANISOU 2046 CG GLN A 284 2252 3834 4079 -412 -378 -439 C ATOM 2047 CD GLN A 284 -5.908 -36.696 -24.057 1.00 29.38 C ANISOU 2047 CD GLN A 284 2522 4099 4542 -507 -347 -462 C ATOM 2048 OE1 GLN A 284 -6.291 -36.294 -25.158 1.00 30.56 O ANISOU 2048 OE1 GLN A 284 2703 4171 4738 -531 -265 -408 O ATOM 2049 NE2 GLN A 284 -5.043 -36.021 -23.312 1.00 31.35 N ANISOU 2049 NE2 GLN A 284 2683 4377 4851 -560 -413 -544 N ATOM 2050 N PHE A 285 -8.622 -42.222 -24.758 1.00 23.22 N ANISOU 2050 N PHE A 285 2055 3409 3358 -155 -267 -200 N ATOM 2051 CA PHE A 285 -9.155 -43.162 -25.733 1.00 22.80 C ANISOU 2051 CA PHE A 285 2063 3326 3275 -108 -209 -129 C ATOM 2052 C PHE A 285 -10.087 -42.433 -26.683 1.00 22.06 C ANISOU 2052 C PHE A 285 2025 3148 3211 -148 -150 -113 C ATOM 2053 O PHE A 285 -10.871 -41.581 -26.258 1.00 22.09 O ANISOU 2053 O PHE A 285 2062 3114 3215 -186 -160 -149 O ATOM 2054 CB PHE A 285 -9.928 -44.306 -25.055 1.00 22.63 C ANISOU 2054 CB PHE A 285 2115 3324 3161 -42 -232 -108 C ATOM 2055 CG PHE A 285 -9.087 -45.213 -24.190 1.00 25.74 C ANISOU 2055 CG PHE A 285 2467 3799 3512 16 -284 -107 C ATOM 2056 CD1 PHE A 285 -9.668 -45.869 -23.119 1.00 28.55 C ANISOU 2056 CD1 PHE A 285 2874 4185 3788 62 -321 -106 C ATOM 2057 CD2 PHE A 285 -7.740 -45.432 -24.440 1.00 27.80 C ANISOU 2057 CD2 PHE A 285 2640 4111 3811 29 -292 -102 C ATOM 2058 CE1 PHE A 285 -8.926 -46.722 -22.303 1.00 29.46 C ANISOU 2058 CE1 PHE A 285 2959 4378 3858 126 -368 -98 C ATOM 2059 CE2 PHE A 285 -6.994 -46.282 -23.626 1.00 29.94 C ANISOU 2059 CE2 PHE A 285 2874 4462 4039 92 -342 -98 C ATOM 2060 CZ PHE A 285 -7.593 -46.923 -22.557 1.00 30.01 C ANISOU 2060 CZ PHE A 285 2940 4497 3963 142 -381 -96 C ATOM 2061 N ALA A 286 -9.996 -42.772 -27.965 1.00 21.24 N ANISOU 2061 N ALA A 286 1929 3017 3125 -132 -89 -59 N ATOM 2062 CA ALA A 286 -10.826 -42.166 -28.999 1.00 20.39 C ANISOU 2062 CA ALA A 286 1873 2838 3038 -156 -30 -35 C ATOM 2063 C ALA A 286 -11.819 -43.198 -29.524 1.00 19.38 C ANISOU 2063 C ALA A 286 1829 2689 2845 -102 -8 5 C ATOM 2064 O ALA A 286 -11.420 -44.261 -30.004 1.00 18.74 O ANISOU 2064 O ALA A 286 1749 2631 2741 -50 5 39 O ATOM 2065 CB ALA A 286 -9.947 -41.648 -30.123 1.00 20.77 C ANISOU 2065 CB ALA A 286 1862 2872 3156 -180 26 -6 C ATOM 2066 N VAL A 287 -13.106 -42.875 -29.417 1.00 18.73 N ANISOU 2066 N VAL A 287 1815 2563 2737 -114 -6 -3 N ATOM 2067 CA VAL A 287 -14.193 -43.737 -29.872 1.00 18.30 C ANISOU 2067 CA VAL A 287 1837 2483 2631 -75 10 27 C ATOM 2068 C VAL A 287 -15.247 -42.889 -30.593 1.00 18.13 C ANISOU 2068 C VAL A 287 1862 2404 2621 -101 45 33 C ATOM 2069 O VAL A 287 -15.129 -41.662 -30.655 1.00 18.36 O ANISOU 2069 O VAL A 287 1869 2408 2697 -147 59 16 O ATOM 2070 CB VAL A 287 -14.824 -44.508 -28.691 1.00 18.05 C ANISOU 2070 CB VAL A 287 1843 2475 2542 -49 -35 15 C ATOM 2071 CG1 VAL A 287 -13.807 -45.478 -28.094 1.00 17.91 C ANISOU 2071 CG1 VAL A 287 1787 2515 2506 -8 -66 21 C ATOM 2072 CG2 VAL A 287 -15.335 -43.538 -27.627 1.00 18.22 C ANISOU 2072 CG2 VAL A 287 1866 2494 2561 -87 -66 -30 C ATOM 2073 N GLY A 288 -16.265 -43.544 -31.147 1.00 17.94 N ANISOU 2073 N GLY A 288 1902 2357 2559 -71 60 56 N ATOM 2074 CA GLY A 288 -17.258 -42.874 -31.976 1.00 17.72 C ANISOU 2074 CA GLY A 288 1916 2282 2535 -83 92 66 C ATOM 2075 C GLY A 288 -17.942 -41.708 -31.291 1.00 18.05 C ANISOU 2075 C GLY A 288 1967 2299 2593 -124 82 36 C ATOM 2076 O GLY A 288 -18.121 -40.652 -31.899 1.00 18.10 O ANISOU 2076 O GLY A 288 1976 2269 2633 -148 114 41 O ATOM 2077 N GLN A 289 -18.291 -41.901 -30.022 1.00 18.12 N ANISOU 2077 N GLN A 289 1982 2328 2575 -127 40 7 N ATOM 2078 CA GLN A 289 -19.011 -40.903 -29.234 1.00 18.53 C ANISOU 2078 CA GLN A 289 2049 2362 2631 -156 26 -29 C ATOM 2079 C GLN A 289 -18.023 -40.081 -28.404 1.00 19.50 C ANISOU 2079 C GLN A 289 2118 2500 2791 -192 0 -73 C ATOM 2080 O GLN A 289 -17.348 -40.617 -27.520 1.00 19.29 O ANISOU 2080 O GLN A 289 2061 2522 2744 -181 -39 -92 O ATOM 2081 CB GLN A 289 -20.041 -41.599 -28.325 1.00 18.52 C ANISOU 2081 CB GLN A 289 2086 2378 2573 -133 0 -33 C ATOM 2082 CG GLN A 289 -21.472 -41.043 -28.429 1.00 18.66 C ANISOU 2082 CG GLN A 289 2149 2361 2580 -137 16 -34 C ATOM 2083 CD GLN A 289 -21.660 -39.708 -27.736 1.00 19.58 C ANISOU 2083 CD GLN A 289 2262 2461 2717 -166 9 -78 C ATOM 2084 OE1 GLN A 289 -20.708 -38.942 -27.562 1.00 20.67 O ANISOU 2084 OE1 GLN A 289 2364 2595 2896 -195 2 -107 O ATOM 2085 NE2 GLN A 289 -22.900 -39.412 -27.342 1.00 19.93 N ANISOU 2085 NE2 GLN A 289 2343 2494 2737 -159 12 -86 N ATOM 2086 N GLU A 290 -17.973 -38.773 -28.669 1.00 20.38 N ANISOU 2086 N GLU A 290 2220 2568 2957 -232 20 -92 N ATOM 2087 CA GLU A 290 -17.004 -37.870 -28.035 1.00 21.99 C ANISOU 2087 CA GLU A 290 2369 2773 3213 -277 -3 -140 C ATOM 2088 C GLU A 290 -17.113 -37.745 -26.513 1.00 22.16 C ANISOU 2088 C GLU A 290 2389 2828 3202 -279 -62 -202 C ATOM 2089 O GLU A 290 -16.169 -37.290 -25.872 1.00 22.16 O ANISOU 2089 O GLU A 290 2336 2849 3235 -308 -97 -250 O ATOM 2090 CB GLU A 290 -17.075 -36.470 -28.665 1.00 22.95 C ANISOU 2090 CB GLU A 290 2490 2824 3405 -320 37 -143 C ATOM 2091 CG GLU A 290 -18.331 -35.663 -28.333 1.00 26.01 C ANISOU 2091 CG GLU A 290 2934 3167 3782 -323 40 -167 C ATOM 2092 CD GLU A 290 -18.350 -34.306 -29.030 1.00 31.33 C ANISOU 2092 CD GLU A 290 3611 3763 4531 -360 85 -162 C ATOM 2093 OE1 GLU A 290 -18.009 -34.244 -30.233 1.00 35.03 O ANISOU 2093 OE1 GLU A 290 4070 4209 5032 -360 135 -106 O ATOM 2094 OE2 GLU A 290 -18.703 -33.298 -28.377 1.00 35.93 O ANISOU 2094 OE2 GLU A 290 4208 4307 5138 -384 72 -211 O ATOM 2095 N VAL A 291 -18.257 -38.130 -25.941 1.00 21.59 N ANISOU 2095 N VAL A 291 2372 2766 3065 -248 -73 -203 N ATOM 2096 CA VAL A 291 -18.463 -38.018 -24.496 1.00 22.45 C ANISOU 2096 CA VAL A 291 2487 2913 3129 -239 -122 -257 C ATOM 2097 C VAL A 291 -18.076 -39.276 -23.700 1.00 22.28 C ANISOU 2097 C VAL A 291 2454 2966 3044 -196 -160 -247 C ATOM 2098 O VAL A 291 -18.124 -39.261 -22.476 1.00 23.22 O ANISOU 2098 O VAL A 291 2577 3130 3118 -180 -203 -287 O ATOM 2099 CB VAL A 291 -19.943 -37.641 -24.152 1.00 22.42 C ANISOU 2099 CB VAL A 291 2546 2884 3090 -224 -109 -264 C ATOM 2100 CG1 VAL A 291 -20.406 -36.438 -24.981 1.00 23.40 C ANISOU 2100 CG1 VAL A 291 2687 2932 3273 -255 -68 -265 C ATOM 2101 CG2 VAL A 291 -20.888 -38.815 -24.344 1.00 21.90 C ANISOU 2101 CG2 VAL A 291 2520 2836 2966 -181 -91 -207 C ATOM 2102 N PHE A 292 -17.681 -40.355 -24.375 1.00 21.80 N ANISOU 2102 N PHE A 292 2384 2922 2979 -172 -144 -193 N ATOM 2103 CA PHE A 292 -17.565 -41.668 -23.713 1.00 21.63 C ANISOU 2103 CA PHE A 292 2368 2957 2893 -122 -170 -168 C ATOM 2104 C PHE A 292 -16.346 -41.843 -22.793 1.00 22.70 C ANISOU 2104 C PHE A 292 2448 3160 3016 -111 -223 -201 C ATOM 2105 O PHE A 292 -16.229 -42.857 -22.101 1.00 23.06 O ANISOU 2105 O PHE A 292 2501 3258 3005 -62 -247 -181 O ATOM 2106 CB PHE A 292 -17.666 -42.800 -24.750 1.00 21.11 C ANISOU 2106 CB PHE A 292 2320 2875 2825 -94 -134 -103 C ATOM 2107 CG PHE A 292 -19.091 -43.146 -25.152 1.00 19.39 C ANISOU 2107 CG PHE A 292 2164 2619 2584 -83 -102 -70 C ATOM 2108 CD1 PHE A 292 -20.181 -42.404 -24.698 1.00 19.47 C ANISOU 2108 CD1 PHE A 292 2206 2609 2580 -96 -98 -92 C ATOM 2109 CD2 PHE A 292 -19.334 -44.205 -26.014 1.00 18.57 C ANISOU 2109 CD2 PHE A 292 2084 2498 2476 -58 -78 -21 C ATOM 2110 CE1 PHE A 292 -21.478 -42.736 -25.075 1.00 17.99 C ANISOU 2110 CE1 PHE A 292 2065 2393 2377 -87 -71 -61 C ATOM 2111 CE2 PHE A 292 -20.622 -44.532 -26.400 1.00 17.67 C ANISOU 2111 CE2 PHE A 292 2017 2349 2347 -53 -55 3 C ATOM 2112 CZ PHE A 292 -21.697 -43.798 -25.928 1.00 17.60 C ANISOU 2112 CZ PHE A 292 2033 2328 2327 -68 -51 -15 C ATOM 2113 N GLY A 293 -15.464 -40.848 -22.762 1.00 23.48 N ANISOU 2113 N GLY A 293 2492 3259 3172 -154 -244 -252 N ATOM 2114 CA GLY A 293 -14.418 -40.782 -21.741 1.00 24.67 C ANISOU 2114 CA GLY A 293 2585 3477 3310 -150 -307 -302 C ATOM 2115 C GLY A 293 -14.930 -40.362 -20.371 1.00 25.21 C ANISOU 2115 C GLY A 293 2680 3579 3320 -137 -353 -360 C ATOM 2116 O GLY A 293 -14.189 -40.437 -19.390 1.00 26.67 O ANISOU 2116 O GLY A 293 2827 3832 3473 -119 -414 -404 O ATOM 2117 N LEU A 294 -16.192 -39.928 -20.304 1.00 25.17 N ANISOU 2117 N LEU A 294 2740 3531 3295 -140 -326 -362 N ATOM 2118 CA LEU A 294 -16.845 -39.483 -19.061 1.00 25.70 C ANISOU 2118 CA LEU A 294 2841 3625 3299 -121 -359 -415 C ATOM 2119 C LEU A 294 -16.696 -40.482 -17.913 1.00 25.64 C ANISOU 2119 C LEU A 294 2839 3706 3196 -55 -399 -404 C ATOM 2120 O LEU A 294 -16.332 -40.100 -16.802 1.00 26.14 O ANISOU 2120 O LEU A 294 2888 3826 3218 -40 -456 -469 O ATOM 2121 CB LEU A 294 -18.340 -39.229 -19.313 1.00 25.41 C ANISOU 2121 CB LEU A 294 2873 3535 3248 -118 -309 -390 C ATOM 2122 CG LEU A 294 -19.244 -38.849 -18.126 1.00 26.55 C ANISOU 2122 CG LEU A 294 3063 3705 3321 -88 -325 -431 C ATOM 2123 CD1 LEU A 294 -18.889 -37.483 -17.569 1.00 28.18 C ANISOU 2123 CD1 LEU A 294 3252 3899 3555 -122 -365 -530 C ATOM 2124 CD2 LEU A 294 -20.709 -38.892 -18.550 1.00 26.54 C ANISOU 2124 CD2 LEU A 294 3118 3657 3308 -78 -267 -384 C ATOM 2125 N VAL A 295 -17.006 -41.750 -18.178 1.00 24.95 N ANISOU 2125 N VAL A 295 2777 3630 3074 -12 -370 -323 N ATOM 2126 CA VAL A 295 -16.881 -42.790 -17.160 1.00 24.97 C ANISOU 2126 CA VAL A 295 2791 3709 2989 57 -398 -296 C ATOM 2127 C VAL A 295 -16.344 -44.092 -17.751 1.00 23.94 C ANISOU 2127 C VAL A 295 2647 3586 2865 87 -381 -222 C ATOM 2128 O VAL A 295 -16.661 -44.439 -18.892 1.00 22.71 O ANISOU 2128 O VAL A 295 2504 3368 2756 68 -332 -174 O ATOM 2129 CB VAL A 295 -18.227 -43.093 -16.442 1.00 25.23 C ANISOU 2129 CB VAL A 295 2892 3748 2946 96 -372 -267 C ATOM 2130 CG1 VAL A 295 -18.504 -42.058 -15.356 1.00 26.75 C ANISOU 2130 CG1 VAL A 295 3095 3974 3094 99 -408 -346 C ATOM 2131 CG2 VAL A 295 -19.353 -43.172 -17.436 1.00 24.82 C ANISOU 2131 CG2 VAL A 295 2880 3618 2934 70 -306 -218 C ATOM 2132 N PRO A 296 -15.525 -44.816 -16.969 1.00 23.95 N ANISOU 2132 N PRO A 296 2622 3663 2814 141 -425 -214 N ATOM 2133 CA PRO A 296 -14.955 -46.096 -17.379 1.00 23.58 C ANISOU 2133 CA PRO A 296 2564 3627 2766 183 -413 -145 C ATOM 2134 C PRO A 296 -15.995 -47.137 -17.774 1.00 22.66 C ANISOU 2134 C PRO A 296 2514 3462 2634 207 -355 -63 C ATOM 2135 O PRO A 296 -15.693 -48.015 -18.572 1.00 22.16 O ANISOU 2135 O PRO A 296 2450 3370 2600 221 -329 -13 O ATOM 2136 CB PRO A 296 -14.213 -46.559 -16.125 1.00 24.56 C ANISOU 2136 CB PRO A 296 2667 3852 2815 248 -473 -154 C ATOM 2137 CG PRO A 296 -13.851 -45.339 -15.448 1.00 24.97 C ANISOU 2137 CG PRO A 296 2682 3943 2863 219 -528 -248 C ATOM 2138 CD PRO A 296 -14.911 -44.341 -15.716 1.00 24.87 C ANISOU 2138 CD PRO A 296 2709 3863 2878 164 -495 -281 C ATOM 2139 N GLY A 297 -17.195 -47.049 -17.204 1.00 22.36 N ANISOU 2139 N GLY A 297 2531 3414 2552 214 -334 -53 N ATOM 2140 CA GLY A 297 -18.291 -47.937 -17.588 1.00 21.77 C ANISOU 2140 CA GLY A 297 2512 3285 2474 225 -278 19 C ATOM 2141 C GLY A 297 -18.677 -47.814 -19.050 1.00 21.02 C ANISOU 2141 C GLY A 297 2423 3108 2458 174 -236 29 C ATOM 2142 O GLY A 297 -18.986 -48.809 -19.696 1.00 20.77 O ANISOU 2142 O GLY A 297 2416 3033 2443 185 -203 85 O ATOM 2143 N LEU A 298 -18.670 -46.588 -19.569 1.00 20.49 N ANISOU 2143 N LEU A 298 2334 3015 2436 120 -238 -26 N ATOM 2144 CA LEU A 298 -18.911 -46.343 -20.993 1.00 19.79 C ANISOU 2144 CA LEU A 298 2247 2856 2415 77 -200 -18 C ATOM 2145 C LEU A 298 -17.746 -46.855 -21.839 1.00 19.75 C ANISOU 2145 C LEU A 298 2204 2850 2450 83 -202 -3 C ATOM 2146 O LEU A 298 -17.946 -47.476 -22.880 1.00 19.21 O ANISOU 2146 O LEU A 298 2153 2735 2409 84 -169 34 O ATOM 2147 CB LEU A 298 -19.120 -44.851 -21.258 1.00 19.64 C ANISOU 2147 CB LEU A 298 2216 2812 2435 24 -200 -76 C ATOM 2148 CG LEU A 298 -20.425 -44.266 -20.732 1.00 19.97 C ANISOU 2148 CG LEU A 298 2299 2840 2449 17 -185 -89 C ATOM 2149 CD1 LEU A 298 -20.444 -42.754 -20.926 1.00 19.28 C ANISOU 2149 CD1 LEU A 298 2198 2724 2402 -29 -189 -151 C ATOM 2150 CD2 LEU A 298 -21.629 -44.909 -21.409 1.00 21.06 C ANISOU 2150 CD2 LEU A 298 2479 2930 2593 19 -139 -35 C ATOM 2151 N MET A 299 -16.527 -46.610 -21.377 1.00 20.42 N ANISOU 2151 N MET A 299 2235 2989 2535 91 -243 -34 N ATOM 2152 CA MET A 299 -15.346 -47.069 -22.109 1.00 21.08 C ANISOU 2152 CA MET A 299 2272 3081 2654 103 -243 -19 C ATOM 2153 C MET A 299 -15.239 -48.603 -22.102 1.00 20.43 C ANISOU 2153 C MET A 299 2215 3005 2541 165 -234 42 C ATOM 2154 O MET A 299 -14.686 -49.197 -23.033 1.00 20.15 O ANISOU 2154 O MET A 299 2168 2951 2537 179 -213 68 O ATOM 2155 CB MET A 299 -14.091 -46.420 -21.539 1.00 22.31 C ANISOU 2155 CB MET A 299 2354 3299 2822 94 -293 -70 C ATOM 2156 CG MET A 299 -12.973 -46.250 -22.527 1.00 25.79 C ANISOU 2156 CG MET A 299 2733 3738 3330 75 -281 -72 C ATOM 2157 SD MET A 299 -13.461 -45.466 -24.086 1.00 27.90 S ANISOU 2157 SD MET A 299 3014 3918 3669 16 -218 -65 S ATOM 2158 CE MET A 299 -13.568 -43.742 -23.671 1.00 29.53 C ANISOU 2158 CE MET A 299 3195 4110 3914 -55 -237 -137 C ATOM 2159 N MET A 300 -15.775 -49.241 -21.066 1.00 20.27 N ANISOU 2159 N MET A 300 2233 3009 2460 205 -245 68 N ATOM 2160 CA MET A 300 -15.862 -50.706 -21.028 1.00 20.12 C ANISOU 2160 CA MET A 300 2249 2979 2417 262 -229 133 C ATOM 2161 C MET A 300 -16.651 -51.216 -22.230 1.00 19.16 C ANISOU 2161 C MET A 300 2171 2774 2336 243 -180 164 C ATOM 2162 O MET A 300 -16.163 -52.055 -22.979 1.00 19.18 O ANISOU 2162 O MET A 300 2175 2753 2361 269 -165 191 O ATOM 2163 CB MET A 300 -16.522 -51.194 -19.728 1.00 20.61 C ANISOU 2163 CB MET A 300 2351 3071 2409 302 -237 163 C ATOM 2164 CG MET A 300 -16.651 -52.714 -19.637 1.00 21.21 C ANISOU 2164 CG MET A 300 2467 3124 2467 360 -215 238 C ATOM 2165 SD MET A 300 -17.768 -53.297 -18.348 1.00 23.57 S ANISOU 2165 SD MET A 300 2824 3434 2698 395 -198 292 S ATOM 2166 CE MET A 300 -19.337 -52.622 -18.902 1.00 23.30 C ANISOU 2166 CE MET A 300 2823 3332 2699 322 -157 277 C ATOM 2167 N TYR A 301 -17.866 -50.707 -22.416 1.00 18.81 N ANISOU 2167 N TYR A 301 2161 2688 2299 201 -157 156 N ATOM 2168 CA TYR A 301 -18.692 -51.127 -23.553 1.00 17.93 C ANISOU 2168 CA TYR A 301 2086 2501 2223 181 -118 176 C ATOM 2169 C TYR A 301 -18.114 -50.670 -24.894 1.00 17.38 C ANISOU 2169 C TYR A 301 1991 2409 2202 158 -106 153 C ATOM 2170 O TYR A 301 -18.218 -51.387 -25.882 1.00 17.35 O ANISOU 2170 O TYR A 301 2010 2362 2221 169 -83 173 O ATOM 2171 CB TYR A 301 -20.139 -50.660 -23.407 1.00 17.69 C ANISOU 2171 CB TYR A 301 2090 2442 2190 146 -99 173 C ATOM 2172 CG TYR A 301 -20.977 -51.570 -22.531 1.00 17.38 C ANISOU 2172 CG TYR A 301 2090 2398 2117 171 -88 220 C ATOM 2173 CD1 TYR A 301 -21.276 -52.867 -22.936 1.00 18.20 C ANISOU 2173 CD1 TYR A 301 2225 2452 2238 190 -67 267 C ATOM 2174 CD2 TYR A 301 -21.465 -51.141 -21.307 1.00 18.36 C ANISOU 2174 CD2 TYR A 301 2218 2564 2194 177 -95 219 C ATOM 2175 CE1 TYR A 301 -22.034 -53.717 -22.141 1.00 18.55 C ANISOU 2175 CE1 TYR A 301 2302 2484 2261 210 -50 318 C ATOM 2176 CE2 TYR A 301 -22.236 -51.984 -20.500 1.00 17.97 C ANISOU 2176 CE2 TYR A 301 2202 2511 2113 203 -75 272 C ATOM 2177 CZ TYR A 301 -22.523 -53.267 -20.929 1.00 17.83 C ANISOU 2177 CZ TYR A 301 2214 2440 2123 216 -50 325 C ATOM 2178 OH TYR A 301 -23.281 -54.111 -20.142 1.00 18.57 O ANISOU 2178 OH TYR A 301 2338 2523 2196 237 -24 385 O ATOM 2179 N ALA A 302 -17.493 -49.491 -24.931 1.00 17.10 N ANISOU 2179 N ALA A 302 1910 2403 2185 128 -119 112 N ATOM 2180 CA ALA A 302 -16.872 -49.023 -26.174 1.00 16.80 C ANISOU 2180 CA ALA A 302 1843 2346 2193 109 -99 100 C ATOM 2181 C ALA A 302 -15.774 -49.988 -26.604 1.00 16.76 C ANISOU 2181 C ALA A 302 1817 2358 2195 156 -98 123 C ATOM 2182 O ALA A 302 -15.631 -50.283 -27.789 1.00 17.32 O ANISOU 2182 O ALA A 302 1896 2397 2288 164 -68 135 O ATOM 2183 CB ALA A 302 -16.313 -47.619 -26.020 1.00 16.69 C ANISOU 2183 CB ALA A 302 1778 2356 2206 66 -112 55 C ATOM 2184 N THR A 303 -15.012 -50.483 -25.633 1.00 17.30 N ANISOU 2184 N THR A 303 1860 2478 2236 194 -129 131 N ATOM 2185 CA THR A 303 -13.924 -51.417 -25.905 1.00 17.43 C ANISOU 2185 CA THR A 303 1851 2517 2255 248 -130 155 C ATOM 2186 C THR A 303 -14.466 -52.768 -26.359 1.00 17.49 C ANISOU 2186 C THR A 303 1921 2471 2252 289 -107 196 C ATOM 2187 O THR A 303 -13.943 -53.370 -27.306 1.00 17.54 O ANISOU 2187 O THR A 303 1928 2458 2277 320 -85 208 O ATOM 2188 CB THR A 303 -13.018 -51.589 -24.666 1.00 18.27 C ANISOU 2188 CB THR A 303 1913 2699 2330 285 -176 152 C ATOM 2189 OG1 THR A 303 -12.422 -50.330 -24.327 1.00 18.25 O ANISOU 2189 OG1 THR A 303 1845 2742 2347 242 -203 103 O ATOM 2190 CG2 THR A 303 -11.910 -52.592 -24.924 1.00 17.43 C ANISOU 2190 CG2 THR A 303 1779 2617 2225 350 -177 181 C ATOM 2191 N ILE A 304 -15.517 -53.242 -25.691 1.00 17.54 N ANISOU 2191 N ILE A 304 1980 2451 2232 291 -108 216 N ATOM 2192 CA ILE A 304 -16.133 -54.516 -26.052 1.00 17.54 C ANISOU 2192 CA ILE A 304 2041 2390 2234 320 -87 253 C ATOM 2193 C ILE A 304 -16.653 -54.488 -27.490 1.00 17.08 C ANISOU 2193 C ILE A 304 2008 2270 2210 295 -57 238 C ATOM 2194 O ILE A 304 -16.394 -55.416 -28.252 1.00 16.83 O ANISOU 2194 O ILE A 304 2000 2204 2191 331 -43 250 O ATOM 2195 CB ILE A 304 -17.260 -54.917 -25.061 1.00 17.70 C ANISOU 2195 CB ILE A 304 2106 2391 2229 315 -87 281 C ATOM 2196 CG1 ILE A 304 -16.654 -55.302 -23.712 1.00 18.96 C ANISOU 2196 CG1 ILE A 304 2252 2611 2343 365 -112 308 C ATOM 2197 CG2 ILE A 304 -18.082 -56.089 -25.610 1.00 17.90 C ANISOU 2197 CG2 ILE A 304 2191 2336 2275 324 -61 311 C ATOM 2198 CD1 ILE A 304 -17.672 -55.437 -22.590 1.00 19.62 C ANISOU 2198 CD1 ILE A 304 2370 2695 2390 362 -109 337 C ATOM 2199 N TRP A 305 -17.372 -53.424 -27.858 1.00 16.53 N ANISOU 2199 N TRP A 305 1938 2192 2152 239 -50 210 N ATOM 2200 CA TRP A 305 -17.932 -53.298 -29.201 1.00 16.35 C ANISOU 2200 CA TRP A 305 1939 2121 2152 220 -26 196 C ATOM 2201 C TRP A 305 -16.862 -53.122 -30.283 1.00 16.73 C ANISOU 2201 C TRP A 305 1957 2183 2216 241 -10 186 C ATOM 2202 O TRP A 305 -17.011 -53.652 -31.386 1.00 16.50 O ANISOU 2202 O TRP A 305 1959 2117 2194 260 8 184 O ATOM 2203 CB TRP A 305 -18.973 -52.168 -29.264 1.00 16.08 C ANISOU 2203 CB TRP A 305 1910 2077 2123 163 -22 175 C ATOM 2204 CG TRP A 305 -20.302 -52.543 -28.657 1.00 16.12 C ANISOU 2204 CG TRP A 305 1954 2052 2120 146 -25 187 C ATOM 2205 CD1 TRP A 305 -20.834 -52.084 -27.488 1.00 16.35 C ANISOU 2205 CD1 TRP A 305 1978 2104 2128 127 -35 190 C ATOM 2206 CD2 TRP A 305 -21.260 -53.466 -29.196 1.00 16.25 C ANISOU 2206 CD2 TRP A 305 2016 2011 2149 146 -16 198 C ATOM 2207 NE1 TRP A 305 -22.071 -52.653 -27.273 1.00 16.34 N ANISOU 2207 NE1 TRP A 305 2014 2066 2129 116 -26 210 N ATOM 2208 CE2 TRP A 305 -22.354 -53.503 -28.309 1.00 17.43 C ANISOU 2208 CE2 TRP A 305 2179 2151 2292 122 -16 213 C ATOM 2209 CE3 TRP A 305 -21.301 -54.256 -30.349 1.00 17.68 C ANISOU 2209 CE3 TRP A 305 2224 2146 2347 164 -8 192 C ATOM 2210 CZ2 TRP A 305 -23.479 -54.306 -28.536 1.00 17.84 C ANISOU 2210 CZ2 TRP A 305 2266 2149 2364 109 -9 226 C ATOM 2211 CZ3 TRP A 305 -22.414 -55.044 -30.577 1.00 18.32 C ANISOU 2211 CZ3 TRP A 305 2343 2171 2445 151 -7 196 C ATOM 2212 CH2 TRP A 305 -23.487 -55.067 -29.672 1.00 17.86 C ANISOU 2212 CH2 TRP A 305 2293 2104 2390 121 -8 214 C ATOM 2213 N LEU A 306 -15.799 -52.379 -29.969 1.00 17.02 N ANISOU 2213 N LEU A 306 1933 2274 2258 237 -17 178 N ATOM 2214 CA LEU A 306 -14.640 -52.249 -30.858 1.00 17.75 C ANISOU 2214 CA LEU A 306 1985 2391 2370 260 3 177 C ATOM 2215 C LEU A 306 -14.054 -53.629 -31.169 1.00 17.85 C ANISOU 2215 C LEU A 306 2015 2395 2373 330 9 198 C ATOM 2216 O LEU A 306 -13.830 -53.975 -32.334 1.00 17.90 O ANISOU 2216 O LEU A 306 2036 2382 2384 358 37 198 O ATOM 2217 CB LEU A 306 -13.577 -51.337 -30.223 1.00 18.30 C ANISOU 2217 CB LEU A 306 1976 2523 2455 242 -12 165 C ATOM 2218 CG LEU A 306 -12.265 -51.086 -30.983 1.00 20.73 C ANISOU 2218 CG LEU A 306 2221 2865 2791 259 12 168 C ATOM 2219 CD1 LEU A 306 -12.504 -50.905 -32.437 1.00 24.11 C ANISOU 2219 CD1 LEU A 306 2673 3258 3229 260 58 174 C ATOM 2220 CD2 LEU A 306 -11.544 -49.862 -30.428 1.00 23.39 C ANISOU 2220 CD2 LEU A 306 2480 3247 3158 212 -3 146 C ATOM 2221 N ARG A 307 -13.833 -54.421 -30.125 1.00 18.11 N ANISOU 2221 N ARG A 307 2050 2442 2388 362 -16 217 N ATOM 2222 CA ARG A 307 -13.331 -55.779 -30.293 1.00 18.71 C ANISOU 2222 CA ARG A 307 2150 2501 2458 433 -11 241 C ATOM 2223 C ARG A 307 -14.294 -56.607 -31.130 1.00 18.53 C ANISOU 2223 C ARG A 307 2203 2399 2439 441 6 239 C ATOM 2224 O ARG A 307 -13.863 -57.360 -32.002 1.00 19.03 O ANISOU 2224 O ARG A 307 2286 2440 2506 490 24 238 O ATOM 2225 CB ARG A 307 -13.093 -56.454 -28.941 1.00 19.01 C ANISOU 2225 CB ARG A 307 2186 2563 2473 468 -40 269 C ATOM 2226 CG ARG A 307 -11.942 -55.859 -28.155 1.00 19.73 C ANISOU 2226 CG ARG A 307 2197 2741 2556 478 -66 265 C ATOM 2227 CD ARG A 307 -11.816 -56.511 -26.794 1.00 20.10 C ANISOU 2227 CD ARG A 307 2250 2819 2569 520 -98 295 C ATOM 2228 NE ARG A 307 -10.755 -55.910 -25.987 1.00 19.84 N ANISOU 2228 NE ARG A 307 2137 2876 2524 529 -134 282 N ATOM 2229 CZ ARG A 307 -10.317 -56.412 -24.837 1.00 22.76 C ANISOU 2229 CZ ARG A 307 2494 3296 2856 581 -167 306 C ATOM 2230 NH1 ARG A 307 -10.844 -57.532 -24.342 1.00 23.54 N ANISOU 2230 NH1 ARG A 307 2659 3357 2928 628 -162 352 N ATOM 2231 NH2 ARG A 307 -9.350 -55.797 -24.170 1.00 22.87 N ANISOU 2231 NH2 ARG A 307 2429 3399 2860 586 -207 284 N ATOM 2232 N GLU A 308 -15.593 -56.461 -30.868 1.00 18.32 N ANISOU 2232 N GLU A 308 2217 2332 2412 393 0 234 N ATOM 2233 CA GLU A 308 -16.619 -57.207 -31.606 1.00 18.19 C ANISOU 2233 CA GLU A 308 2266 2239 2406 390 9 226 C ATOM 2234 C GLU A 308 -16.611 -56.872 -33.096 1.00 18.14 C ANISOU 2234 C GLU A 308 2267 2222 2404 391 28 195 C ATOM 2235 O GLU A 308 -16.733 -57.767 -33.937 1.00 18.10 O ANISOU 2235 O GLU A 308 2306 2170 2401 425 36 183 O ATOM 2236 CB GLU A 308 -18.008 -56.942 -31.012 1.00 18.27 C ANISOU 2236 CB GLU A 308 2301 2221 2420 333 -1 227 C ATOM 2237 CG GLU A 308 -19.173 -57.611 -31.745 1.00 18.22 C ANISOU 2237 CG GLU A 308 2351 2139 2432 316 2 212 C ATOM 2238 CD GLU A 308 -19.089 -59.132 -31.800 1.00 20.11 C ANISOU 2238 CD GLU A 308 2636 2317 2687 361 3 227 C ATOM 2239 OE1 GLU A 308 -19.829 -59.732 -32.620 1.00 20.09 O ANISOU 2239 OE1 GLU A 308 2677 2251 2707 353 2 203 O ATOM 2240 OE2 GLU A 308 -18.289 -59.745 -31.049 1.00 21.03 O ANISOU 2240 OE2 GLU A 308 2746 2447 2797 406 3 261 O ATOM 2241 N HIS A 309 -16.461 -55.592 -33.426 1.00 17.61 N ANISOU 2241 N HIS A 309 2161 2196 2336 357 38 182 N ATOM 2242 CA HIS A 309 -16.381 -55.194 -34.825 1.00 17.56 C ANISOU 2242 CA HIS A 309 2159 2187 2325 365 63 163 C ATOM 2243 C HIS A 309 -15.230 -55.915 -35.508 1.00 17.79 C ANISOU 2243 C HIS A 309 2183 2230 2349 435 83 167 C ATOM 2244 O HIS A 309 -15.392 -56.476 -36.589 1.00 17.97 O ANISOU 2244 O HIS A 309 2246 2221 2359 471 95 149 O ATOM 2245 CB HIS A 309 -16.187 -53.688 -34.987 1.00 17.13 C ANISOU 2245 CB HIS A 309 2058 2175 2277 323 78 160 C ATOM 2246 CG HIS A 309 -15.985 -53.267 -36.409 1.00 17.36 C ANISOU 2246 CG HIS A 309 2089 2208 2297 342 112 153 C ATOM 2247 ND1 HIS A 309 -17.034 -52.936 -37.243 1.00 16.45 N ANISOU 2247 ND1 HIS A 309 2016 2066 2170 325 116 136 N ATOM 2248 CD2 HIS A 309 -14.861 -53.168 -37.160 1.00 18.33 C ANISOU 2248 CD2 HIS A 309 2181 2366 2419 382 145 163 C ATOM 2249 CE1 HIS A 309 -16.560 -52.626 -38.438 1.00 16.51 C ANISOU 2249 CE1 HIS A 309 2021 2091 2163 357 150 138 C ATOM 2250 NE2 HIS A 309 -15.245 -52.758 -38.415 1.00 17.25 N ANISOU 2250 NE2 HIS A 309 2070 2221 2264 391 172 156 N ATOM 2251 N ASN A 310 -14.061 -55.884 -34.880 1.00 18.49 N ANISOU 2251 N ASN A 310 2216 2367 2442 459 84 188 N ATOM 2252 CA ASN A 310 -12.877 -56.488 -35.481 1.00 18.91 C ANISOU 2252 CA ASN A 310 2251 2443 2491 530 107 195 C ATOM 2253 C ASN A 310 -12.965 -58.015 -35.523 1.00 19.32 C ANISOU 2253 C ASN A 310 2362 2443 2537 591 99 195 C ATOM 2254 O ASN A 310 -12.422 -58.645 -36.437 1.00 19.83 O ANISOU 2254 O ASN A 310 2444 2500 2591 654 121 187 O ATOM 2255 CB ASN A 310 -11.612 -56.026 -34.765 1.00 19.31 C ANISOU 2255 CB ASN A 310 2217 2567 2555 538 106 216 C ATOM 2256 CG ASN A 310 -11.242 -54.586 -35.100 1.00 19.22 C ANISOU 2256 CG ASN A 310 2143 2599 2560 489 127 213 C ATOM 2257 OD1 ASN A 310 -11.872 -53.949 -35.938 1.00 18.08 O ANISOU 2257 OD1 ASN A 310 2022 2434 2414 460 148 203 O ATOM 2258 ND2 ASN A 310 -10.205 -54.078 -34.450 1.00 18.71 N ANISOU 2258 ND2 ASN A 310 1996 2595 2516 482 120 223 N ATOM 2259 N ARG A 311 -13.660 -58.600 -34.549 1.00 19.14 N ANISOU 2259 N ARG A 311 2372 2381 2520 574 70 206 N ATOM 2260 CA ARG A 311 -13.923 -60.038 -34.544 1.00 19.82 C ANISOU 2260 CA ARG A 311 2521 2398 2610 620 64 208 C ATOM 2261 C ARG A 311 -14.807 -60.430 -35.729 1.00 19.45 C ANISOU 2261 C ARG A 311 2540 2287 2565 617 69 168 C ATOM 2262 O ARG A 311 -14.560 -61.442 -36.387 1.00 20.05 O ANISOU 2262 O ARG A 311 2659 2320 2641 676 76 152 O ATOM 2263 CB ARG A 311 -14.601 -60.459 -33.238 1.00 19.86 C ANISOU 2263 CB ARG A 311 2546 2373 2625 593 40 236 C ATOM 2264 CG ARG A 311 -14.739 -61.970 -33.051 1.00 20.50 C ANISOU 2264 CG ARG A 311 2688 2379 2722 642 38 251 C ATOM 2265 CD ARG A 311 -15.614 -62.297 -31.862 1.00 21.43 C ANISOU 2265 CD ARG A 311 2829 2462 2851 607 23 284 C ATOM 2266 NE ARG A 311 -17.022 -62.035 -32.152 1.00 21.37 N ANISOU 2266 NE ARG A 311 2853 2406 2862 535 18 260 N ATOM 2267 CZ ARG A 311 -17.864 -62.908 -32.709 1.00 23.18 C ANISOU 2267 CZ ARG A 311 3141 2545 3121 527 18 240 C ATOM 2268 NH1 ARG A 311 -17.464 -64.132 -33.031 1.00 24.27 N ANISOU 2268 NH1 ARG A 311 3322 2622 3276 586 24 241 N ATOM 2269 NH2 ARG A 311 -19.124 -62.555 -32.948 1.00 22.89 N ANISOU 2269 NH2 ARG A 311 3119 2478 3101 459 9 217 N ATOM 2270 N VAL A 312 -15.845 -59.638 -35.981 1.00 18.91 N ANISOU 2270 N VAL A 312 2478 2210 2497 551 61 148 N ATOM 2271 CA VAL A 312 -16.729 -59.878 -37.117 1.00 18.91 C ANISOU 2271 CA VAL A 312 2531 2160 2492 545 58 105 C ATOM 2272 C VAL A 312 -15.969 -59.704 -38.439 1.00 19.29 C ANISOU 2272 C VAL A 312 2577 2241 2511 601 86 84 C ATOM 2273 O VAL A 312 -16.159 -60.486 -39.372 1.00 20.20 O ANISOU 2273 O VAL A 312 2745 2314 2616 643 84 47 O ATOM 2274 CB VAL A 312 -18.004 -59.000 -37.037 1.00 18.33 C ANISOU 2274 CB VAL A 312 2458 2083 2424 468 43 94 C ATOM 2275 CG1 VAL A 312 -18.783 -59.042 -38.338 1.00 18.61 C ANISOU 2275 CG1 VAL A 312 2535 2090 2446 469 37 46 C ATOM 2276 CG2 VAL A 312 -18.879 -59.464 -35.858 1.00 17.89 C ANISOU 2276 CG2 VAL A 312 2417 1984 2397 424 21 113 C ATOM 2277 N CYS A 313 -15.077 -58.717 -38.502 1.00 19.23 N ANISOU 2277 N CYS A 313 2508 2307 2492 604 112 106 N ATOM 2278 CA CYS A 313 -14.225 -58.532 -39.681 1.00 20.00 C ANISOU 2278 CA CYS A 313 2593 2443 2561 662 149 99 C ATOM 2279 C CYS A 313 -13.423 -59.803 -39.980 1.00 20.77 C ANISOU 2279 C CYS A 313 2717 2522 2652 749 159 92 C ATOM 2280 O CYS A 313 -13.336 -60.220 -41.134 1.00 21.46 O ANISOU 2280 O CYS A 313 2844 2599 2711 805 175 61 O ATOM 2281 CB CYS A 313 -13.264 -57.355 -39.498 1.00 19.62 C ANISOU 2281 CB CYS A 313 2463 2473 2518 646 179 133 C ATOM 2282 SG CYS A 313 -14.029 -55.739 -39.681 1.00 19.80 S ANISOU 2282 SG CYS A 313 2463 2517 2543 566 186 136 S ATOM 2283 N ASP A 314 -12.855 -60.418 -38.943 1.00 21.27 N ANISOU 2283 N ASP A 314 2762 2583 2738 767 148 120 N ATOM 2284 CA ASP A 314 -12.087 -61.657 -39.118 1.00 22.62 C ANISOU 2284 CA ASP A 314 2958 2730 2906 856 158 118 C ATOM 2285 C ASP A 314 -12.971 -62.772 -39.686 1.00 22.98 C ANISOU 2285 C ASP A 314 3096 2680 2953 876 139 73 C ATOM 2286 O ASP A 314 -12.548 -63.508 -40.582 1.00 24.03 O ANISOU 2286 O ASP A 314 3267 2794 3067 952 155 44 O ATOM 2287 CB ASP A 314 -11.462 -62.129 -37.796 1.00 22.85 C ANISOU 2287 CB ASP A 314 2955 2769 2958 872 144 161 C ATOM 2288 CG ASP A 314 -10.279 -61.283 -37.353 1.00 23.80 C ANISOU 2288 CG ASP A 314 2977 2987 3077 877 160 196 C ATOM 2289 OD1 ASP A 314 -9.626 -60.640 -38.200 1.00 25.27 O ANISOU 2289 OD1 ASP A 314 3123 3228 3251 894 194 193 O ATOM 2290 OD2 ASP A 314 -9.993 -61.286 -36.134 1.00 26.08 O ANISOU 2290 OD2 ASP A 314 3230 3300 3380 865 137 228 O ATOM 2291 N ILE A 315 -14.193 -62.886 -39.164 1.00 22.67 N ANISOU 2291 N ILE A 315 3092 2583 2939 808 105 64 N ATOM 2292 CA ILE A 315 -15.134 -63.910 -39.619 1.00 23.03 C ANISOU 2292 CA ILE A 315 3218 2532 3001 810 82 18 C ATOM 2293 C ILE A 315 -15.500 -63.712 -41.088 1.00 23.07 C ANISOU 2293 C ILE A 315 3257 2539 2970 828 83 -42 C ATOM 2294 O ILE A 315 -15.480 -64.663 -41.874 1.00 23.67 O ANISOU 2294 O ILE A 315 3392 2563 3039 885 79 -89 O ATOM 2295 CB ILE A 315 -16.419 -63.935 -38.753 1.00 22.68 C ANISOU 2295 CB ILE A 315 3189 2434 2995 723 50 25 C ATOM 2296 CG1 ILE A 315 -16.097 -64.448 -37.345 1.00 24.15 C ANISOU 2296 CG1 ILE A 315 3361 2605 3210 725 49 83 C ATOM 2297 CG2 ILE A 315 -17.486 -64.821 -39.387 1.00 23.35 C ANISOU 2297 CG2 ILE A 315 3345 2422 3103 710 23 -31 C ATOM 2298 CD1 ILE A 315 -17.279 -64.404 -36.392 1.00 23.85 C ANISOU 2298 CD1 ILE A 315 3330 2526 3206 645 28 104 C ATOM 2299 N LEU A 316 -15.814 -62.475 -41.462 1.00 22.45 N ANISOU 2299 N LEU A 316 3145 2520 2867 784 90 -41 N ATOM 2300 CA LEU A 316 -16.199 -62.168 -42.836 1.00 22.86 C ANISOU 2300 CA LEU A 316 3226 2584 2874 805 92 -90 C ATOM 2301 C LEU A 316 -15.032 -62.338 -43.809 1.00 23.77 C ANISOU 2301 C LEU A 316 3342 2745 2943 902 133 -97 C ATOM 2302 O LEU A 316 -15.232 -62.751 -44.953 1.00 24.17 O ANISOU 2302 O LEU A 316 3447 2781 2956 953 130 -151 O ATOM 2303 CB LEU A 316 -16.779 -60.755 -42.937 1.00 22.01 C ANISOU 2303 CB LEU A 316 3081 2530 2752 740 94 -75 C ATOM 2304 CG LEU A 316 -18.142 -60.549 -42.272 1.00 21.76 C ANISOU 2304 CG LEU A 316 3056 2458 2755 652 54 -81 C ATOM 2305 CD1 LEU A 316 -18.541 -59.082 -42.350 1.00 20.48 C ANISOU 2305 CD1 LEU A 316 2852 2352 2576 601 63 -61 C ATOM 2306 CD2 LEU A 316 -19.210 -61.429 -42.910 1.00 22.62 C ANISOU 2306 CD2 LEU A 316 3231 2495 2870 650 12 -147 C ATOM 2307 N LYS A 317 -13.816 -62.034 -43.355 1.00 24.28 N ANISOU 2307 N LYS A 317 3346 2868 3011 931 170 -44 N ATOM 2308 CA LYS A 317 -12.635 -62.212 -44.193 1.00 25.52 C ANISOU 2308 CA LYS A 317 3493 3074 3131 1026 217 -42 C ATOM 2309 C LYS A 317 -12.401 -63.691 -44.518 1.00 26.45 C ANISOU 2309 C LYS A 317 3677 3127 3245 1108 208 -84 C ATOM 2310 O LYS A 317 -12.013 -64.029 -45.636 1.00 26.75 O ANISOU 2310 O LYS A 317 3750 3179 3237 1190 232 -118 O ATOM 2311 CB LYS A 317 -11.393 -61.618 -43.526 1.00 25.90 C ANISOU 2311 CB LYS A 317 3450 3197 3195 1032 254 23 C ATOM 2312 CG LYS A 317 -10.139 -61.762 -44.382 1.00 28.44 C ANISOU 2312 CG LYS A 317 3748 3576 3481 1131 309 32 C ATOM 2313 CD LYS A 317 -9.088 -60.712 -44.064 1.00 30.35 C ANISOU 2313 CD LYS A 317 3886 3910 3737 1116 352 93 C ATOM 2314 CE LYS A 317 -8.118 -60.576 -45.225 1.00 32.62 C ANISOU 2314 CE LYS A 317 4151 4261 3983 1201 418 103 C ATOM 2315 NZ LYS A 317 -8.726 -59.837 -46.380 1.00 33.02 N ANISOU 2315 NZ LYS A 317 4232 4327 3985 1194 440 87 N ATOM 2316 N GLN A 318 -12.624 -64.556 -43.529 1.00 26.50 N ANISOU 2316 N GLN A 318 3704 3063 3301 1091 178 -77 N ATOM 2317 CA GLN A 318 -12.552 -66.004 -43.723 1.00 27.77 C ANISOU 2317 CA GLN A 318 3936 3140 3474 1159 166 -117 C ATOM 2318 C GLN A 318 -13.602 -66.471 -44.738 1.00 27.54 C ANISOU 2318 C GLN A 318 3990 3045 3429 1157 133 -200 C ATOM 2319 O GLN A 318 -13.301 -67.295 -45.609 1.00 28.30 O ANISOU 2319 O GLN A 318 4142 3110 3499 1242 139 -253 O ATOM 2320 CB GLN A 318 -12.728 -66.732 -42.382 1.00 28.08 C ANISOU 2320 CB GLN A 318 3982 3112 3575 1129 142 -82 C ATOM 2321 CG GLN A 318 -12.726 -68.269 -42.454 1.00 31.96 C ANISOU 2321 CG GLN A 318 4552 3497 4095 1191 130 -116 C ATOM 2322 CD GLN A 318 -11.333 -68.883 -42.492 1.00 36.63 C ANISOU 2322 CD GLN A 318 5132 4113 4672 1305 167 -92 C ATOM 2323 OE1 GLN A 318 -10.349 -68.222 -42.838 1.00 39.80 O ANISOU 2323 OE1 GLN A 318 5472 4616 5034 1349 204 -68 O ATOM 2324 NE2 GLN A 318 -11.247 -70.165 -42.136 1.00 39.39 N ANISOU 2324 NE2 GLN A 318 5538 4368 5059 1353 159 -97 N ATOM 2325 N BGLU A 319 -14.815 -65.938 -44.623 0.38 26.39 N ANISOU 2325 N BGLU A 319 3848 2881 3297 1065 98 -215 N ATOM 2326 N CGLU A 319 -14.824 -65.955 -44.616 0.62 26.88 N ANISOU 2326 N CGLU A 319 3912 2942 3361 1065 97 -216 N ATOM 2327 CA BGLU A 319 -15.908 -66.289 -45.527 0.38 26.26 C ANISOU 2327 CA BGLU A 319 3899 2811 3269 1053 57 -297 C ATOM 2328 CA CGLU A 319 -15.903 -66.305 -45.551 0.62 27.24 C ANISOU 2328 CA CGLU A 319 4024 2934 3392 1054 57 -299 C ATOM 2329 C BGLU A 319 -15.749 -65.661 -46.914 0.38 26.45 C ANISOU 2329 C BGLU A 319 3931 2908 3211 1106 75 -334 C ATOM 2330 C CGLU A 319 -15.700 -65.686 -46.933 0.62 27.03 C ANISOU 2330 C CGLU A 319 4005 2982 3283 1110 76 -334 C ATOM 2331 O BGLU A 319 -16.204 -66.230 -47.910 0.38 27.06 O ANISOU 2331 O BGLU A 319 4074 2951 3258 1145 48 -414 O ATOM 2332 O CGLU A 319 -16.074 -66.288 -47.945 0.62 27.65 O ANISOU 2332 O CGLU A 319 4149 3027 3330 1156 52 -413 O ATOM 2333 CB BGLU A 319 -17.248 -65.871 -44.916 0.38 25.45 C ANISOU 2333 CB BGLU A 319 3785 2675 3208 939 15 -295 C ATOM 2334 CB CGLU A 319 -17.287 -65.901 -45.011 0.62 26.89 C ANISOU 2334 CB CGLU A 319 3972 2856 3389 941 13 -302 C ATOM 2335 CG BGLU A 319 -17.596 -66.629 -43.649 0.38 24.59 C ANISOU 2335 CG BGLU A 319 3683 2484 3179 889 -3 -265 C ATOM 2336 CG CGLU A 319 -18.166 -67.079 -44.576 0.62 29.02 C ANISOU 2336 CG CGLU A 319 4296 3003 3728 904 -31 -339 C ATOM 2337 CD BGLU A 319 -17.550 -68.134 -43.849 0.38 24.25 C ANISOU 2337 CD BGLU A 319 3712 2333 3170 940 -19 -313 C ATOM 2338 CD CGLU A 319 -19.563 -67.022 -45.171 0.62 30.09 C ANISOU 2338 CD CGLU A 319 4460 3103 3870 844 -84 -408 C ATOM 2339 OE1BGLU A 319 -18.206 -68.623 -44.790 0.38 23.00 O ANISOU 2339 OE1BGLU A 319 3609 2124 3005 948 -52 -396 O ATOM 2340 OE1CGLU A 319 -20.224 -65.964 -45.066 0.62 32.38 O ANISOU 2340 OE1CGLU A 319 4708 3447 4149 780 -92 -389 O ATOM 2341 OE2BGLU A 319 -16.861 -68.824 -43.067 0.38 24.23 O ANISOU 2341 OE2BGLU A 319 3711 2296 3201 973 1 -269 O ATOM 2342 OE2CGLU A 319 -20.004 -68.038 -45.745 0.62 30.43 O ANISOU 2342 OE2CGLU A 319 4565 3062 3932 863 -119 -485 O ATOM 2343 N HIS A 320 -15.110 -64.495 -46.971 1.00 25.82 N ANISOU 2343 N HIS A 320 3786 2929 3097 1107 120 -276 N ATOM 2344 CA HIS A 320 -14.950 -63.745 -48.215 1.00 25.84 C ANISOU 2344 CA HIS A 320 3788 3008 3021 1154 148 -290 C ATOM 2345 C HIS A 320 -13.515 -63.249 -48.407 1.00 25.95 C ANISOU 2345 C HIS A 320 3746 3109 3004 1220 220 -231 C ATOM 2346 O HIS A 320 -13.234 -62.057 -48.242 1.00 25.25 O ANISOU 2346 O HIS A 320 3591 3091 2912 1183 254 -171 O ATOM 2347 CB HIS A 320 -15.908 -62.549 -48.235 1.00 24.99 C ANISOU 2347 CB HIS A 320 3655 2935 2907 1071 131 -276 C ATOM 2348 CG HIS A 320 -17.356 -62.921 -48.143 1.00 24.54 C ANISOU 2348 CG HIS A 320 3640 2805 2877 1006 62 -334 C ATOM 2349 ND1 HIS A 320 -18.077 -63.391 -49.220 1.00 25.20 N ANISOU 2349 ND1 HIS A 320 3789 2866 2920 1040 22 -418 N ATOM 2350 CD2 HIS A 320 -18.225 -62.868 -47.105 1.00 23.59 C ANISOU 2350 CD2 HIS A 320 3503 2637 2823 910 26 -319 C ATOM 2351 CE1 HIS A 320 -19.324 -63.623 -48.844 1.00 24.55 C ANISOU 2351 CE1 HIS A 320 3721 2721 2885 961 -37 -454 C ATOM 2352 NE2 HIS A 320 -19.437 -63.319 -47.565 1.00 23.13 N ANISOU 2352 NE2 HIS A 320 3492 2525 2770 883 -32 -391 N ATOM 2353 N PRO A 321 -12.600 -64.156 -48.795 1.00 26.73 N ANISOU 2353 N PRO A 321 3869 3203 3084 1321 247 -248 N ATOM 2354 CA PRO A 321 -11.232 -63.707 -49.077 1.00 27.09 C ANISOU 2354 CA PRO A 321 3854 3338 3099 1389 320 -192 C ATOM 2355 C PRO A 321 -11.155 -62.715 -50.241 1.00 27.04 C ANISOU 2355 C PRO A 321 3837 3416 3019 1419 364 -183 C ATOM 2356 O PRO A 321 -10.174 -61.977 -50.354 1.00 27.30 O ANISOU 2356 O PRO A 321 3800 3530 3041 1443 430 -118 O ATOM 2357 CB PRO A 321 -10.494 -65.010 -49.425 1.00 28.14 C ANISOU 2357 CB PRO A 321 4034 3438 3218 1501 332 -230 C ATOM 2358 CG PRO A 321 -11.566 -65.969 -49.809 1.00 28.79 C ANISOU 2358 CG PRO A 321 4217 3423 3298 1503 269 -322 C ATOM 2359 CD PRO A 321 -12.749 -65.611 -48.972 1.00 27.40 C ANISOU 2359 CD PRO A 321 4033 3197 3178 1376 214 -317 C ATOM 2360 N GLU A 322 -12.190 -62.708 -51.083 1.00 27.03 N ANISOU 2360 N GLU A 322 3904 3397 2971 1419 328 -245 N ATOM 2361 CA GLU A 322 -12.284 -61.824 -52.248 1.00 27.06 C ANISOU 2361 CA GLU A 322 3911 3476 2893 1455 364 -239 C ATOM 2362 C GLU A 322 -12.737 -60.386 -51.928 1.00 26.36 C ANISOU 2362 C GLU A 322 3765 3428 2823 1362 374 -177 C ATOM 2363 O GLU A 322 -12.604 -59.490 -52.763 1.00 26.57 O ANISOU 2363 O GLU A 322 3778 3524 2792 1391 421 -145 O ATOM 2364 CB GLU A 322 -13.215 -62.456 -53.302 1.00 27.83 C ANISOU 2364 CB GLU A 322 4107 3542 2926 1503 313 -338 C ATOM 2365 CG GLU A 322 -14.729 -62.364 -53.039 1.00 27.17 C ANISOU 2365 CG GLU A 322 4053 3400 2870 1410 231 -385 C ATOM 2366 CD GLU A 322 -15.261 -63.294 -51.943 1.00 27.29 C ANISOU 2366 CD GLU A 322 4083 3309 2977 1340 170 -416 C ATOM 2367 OE1 GLU A 322 -16.487 -63.237 -51.674 1.00 26.45 O ANISOU 2367 OE1 GLU A 322 3992 3155 2901 1260 107 -450 O ATOM 2368 OE2 GLU A 322 -14.481 -64.077 -51.357 1.00 27.24 O ANISOU 2368 OE2 GLU A 322 4072 3267 3012 1367 186 -403 O ATOM 2369 N TRP A 323 -13.262 -60.171 -50.726 1.00 25.18 N ANISOU 2369 N TRP A 323 3584 3234 2751 1257 334 -158 N ATOM 2370 CA TRP A 323 -13.772 -58.857 -50.333 1.00 24.27 C ANISOU 2370 CA TRP A 323 3420 3144 2659 1167 337 -109 C ATOM 2371 C TRP A 323 -12.663 -57.876 -49.952 1.00 23.99 C ANISOU 2371 C TRP A 323 3294 3173 2650 1152 406 -22 C ATOM 2372 O TRP A 323 -11.610 -58.273 -49.451 1.00 24.62 O ANISOU 2372 O TRP A 323 3330 3263 2760 1177 433 5 O ATOM 2373 CB TRP A 323 -14.720 -59.014 -49.150 1.00 23.44 C ANISOU 2373 CB TRP A 323 3313 2970 2624 1065 271 -123 C ATOM 2374 CG TRP A 323 -16.129 -59.374 -49.506 1.00 22.97 C ANISOU 2374 CG TRP A 323 3318 2859 2549 1040 204 -192 C ATOM 2375 CD1 TRP A 323 -16.609 -59.802 -50.714 1.00 23.17 C ANISOU 2375 CD1 TRP A 323 3411 2886 2508 1104 183 -259 C ATOM 2376 CD2 TRP A 323 -17.239 -59.367 -48.612 1.00 21.56 C ANISOU 2376 CD2 TRP A 323 3139 2625 2428 945 147 -204 C ATOM 2377 NE1 TRP A 323 -17.959 -60.038 -50.627 1.00 23.34 N ANISOU 2377 NE1 TRP A 323 3467 2855 2546 1048 111 -314 N ATOM 2378 CE2 TRP A 323 -18.372 -59.779 -49.347 1.00 22.38 C ANISOU 2378 CE2 TRP A 323 3303 2697 2502 950 92 -278 C ATOM 2379 CE3 TRP A 323 -17.390 -59.040 -47.261 1.00 21.16 C ANISOU 2379 CE3 TRP A 323 3041 2553 2448 859 137 -161 C ATOM 2380 CZ2 TRP A 323 -19.640 -59.868 -48.772 1.00 22.33 C ANISOU 2380 CZ2 TRP A 323 3303 2638 2542 867 32 -305 C ATOM 2381 CZ3 TRP A 323 -18.650 -59.132 -46.691 1.00 20.61 C ANISOU 2381 CZ3 TRP A 323 2983 2431 2415 783 82 -185 C ATOM 2382 CH2 TRP A 323 -19.756 -59.540 -47.444 1.00 21.33 C ANISOU 2382 CH2 TRP A 323 3128 2491 2485 785 33 -254 C ATOM 2383 N GLY A 324 -12.920 -56.591 -50.183 1.00 23.58 N ANISOU 2383 N GLY A 324 3210 3160 2590 1110 433 22 N ATOM 2384 CA GLY A 324 -12.003 -55.521 -49.790 1.00 23.25 C ANISOU 2384 CA GLY A 324 3079 3168 2587 1076 495 102 C ATOM 2385 C GLY A 324 -12.356 -54.905 -48.447 1.00 22.02 C ANISOU 2385 C GLY A 324 2874 2983 2510 964 461 124 C ATOM 2386 O GLY A 324 -13.394 -55.214 -47.854 1.00 21.16 O ANISOU 2386 O GLY A 324 2800 2819 2420 912 396 85 O ATOM 2387 N ASP A 325 -11.489 -54.015 -47.975 1.00 21.67 N ANISOU 2387 N ASP A 325 2745 2977 2512 927 507 185 N ATOM 2388 CA ASP A 325 -11.677 -53.337 -46.690 1.00 20.97 C ANISOU 2388 CA ASP A 325 2604 2868 2495 826 478 204 C ATOM 2389 C ASP A 325 -13.040 -52.636 -46.562 1.00 19.99 C ANISOU 2389 C ASP A 325 2514 2709 2370 759 440 190 C ATOM 2390 O ASP A 325 -13.703 -52.761 -45.532 1.00 19.31 O ANISOU 2390 O ASP A 325 2432 2583 2321 697 385 169 O ATOM 2391 CB ASP A 325 -10.537 -52.334 -46.476 1.00 21.40 C ANISOU 2391 CB ASP A 325 2562 2972 2595 800 538 267 C ATOM 2392 CG ASP A 325 -10.772 -51.416 -45.305 1.00 21.20 C ANISOU 2392 CG ASP A 325 2487 2931 2638 697 511 281 C ATOM 2393 OD1 ASP A 325 -10.578 -51.859 -44.149 1.00 21.13 O ANISOU 2393 OD1 ASP A 325 2451 2909 2667 666 468 267 O ATOM 2394 OD2 ASP A 325 -11.133 -50.242 -45.554 1.00 21.78 O ANISOU 2394 OD2 ASP A 325 2550 3004 2723 653 536 307 O ATOM 2395 N GLU A 326 -13.470 -51.917 -47.596 1.00 20.24 N ANISOU 2395 N GLU A 326 2573 2760 2359 778 471 203 N ATOM 2396 CA GLU A 326 -14.725 -51.163 -47.490 1.00 19.42 C ANISOU 2396 CA GLU A 326 2495 2629 2256 721 439 196 C ATOM 2397 C GLU A 326 -15.916 -52.089 -47.240 1.00 19.04 C ANISOU 2397 C GLU A 326 2508 2531 2193 711 361 130 C ATOM 2398 O GLU A 326 -16.712 -51.825 -46.338 1.00 18.01 O ANISOU 2398 O GLU A 326 2373 2367 2103 639 319 121 O ATOM 2399 CB GLU A 326 -14.976 -50.272 -48.718 1.00 20.25 C ANISOU 2399 CB GLU A 326 2621 2766 2308 757 486 226 C ATOM 2400 CG GLU A 326 -16.207 -49.350 -48.600 1.00 20.13 C ANISOU 2400 CG GLU A 326 2624 2727 2298 702 459 228 C ATOM 2401 CD GLU A 326 -16.046 -48.206 -47.598 1.00 21.17 C ANISOU 2401 CD GLU A 326 2695 2843 2507 614 474 268 C ATOM 2402 OE1 GLU A 326 -14.919 -47.949 -47.122 1.00 21.02 O ANISOU 2402 OE1 GLU A 326 2612 2839 2538 594 511 302 O ATOM 2403 OE2 GLU A 326 -17.066 -47.552 -47.283 1.00 21.41 O ANISOU 2403 OE2 GLU A 326 2738 2847 2549 566 445 263 O ATOM 2404 N GLN A 327 -16.044 -53.162 -48.024 1.00 19.27 N ANISOU 2404 N GLN A 327 2596 2556 2172 782 344 84 N ATOM 2405 CA GLN A 327 -17.190 -54.073 -47.862 1.00 18.96 C ANISOU 2405 CA GLN A 327 2613 2463 2128 768 271 18 C ATOM 2406 C GLN A 327 -17.126 -54.814 -46.528 1.00 18.73 C ANISOU 2406 C GLN A 327 2566 2387 2163 720 234 8 C ATOM 2407 O GLN A 327 -18.154 -55.042 -45.893 1.00 17.99 O ANISOU 2407 O GLN A 327 2490 2249 2098 665 182 -17 O ATOM 2408 CB GLN A 327 -17.312 -55.066 -49.022 1.00 19.78 C ANISOU 2408 CB GLN A 327 2784 2566 2165 855 257 -39 C ATOM 2409 CG GLN A 327 -18.644 -55.840 -49.005 1.00 19.87 C ANISOU 2409 CG GLN A 327 2850 2522 2178 832 178 -112 C ATOM 2410 CD GLN A 327 -18.989 -56.522 -50.323 1.00 21.51 C ANISOU 2410 CD GLN A 327 3126 2736 2310 913 156 -178 C ATOM 2411 OE1 GLN A 327 -20.128 -56.966 -50.521 1.00 23.86 O ANISOU 2411 OE1 GLN A 327 3464 2999 2603 894 91 -240 O ATOM 2412 NE2 GLN A 327 -18.028 -56.602 -51.225 1.00 19.36 N ANISOU 2412 NE2 GLN A 327 2865 2511 1979 1002 208 -167 N ATOM 2413 N LEU A 328 -15.921 -55.185 -46.107 1.00 18.79 N ANISOU 2413 N LEU A 328 2538 2408 2192 745 263 33 N ATOM 2414 CA LEU A 328 -15.728 -55.785 -44.789 1.00 18.96 C ANISOU 2414 CA LEU A 328 2538 2396 2270 707 235 37 C ATOM 2415 C LEU A 328 -16.197 -54.838 -43.691 1.00 18.21 C ANISOU 2415 C LEU A 328 2400 2299 2220 616 219 64 C ATOM 2416 O LEU A 328 -16.922 -55.243 -42.785 1.00 18.21 O ANISOU 2416 O LEU A 328 2413 2257 2250 570 176 50 O ATOM 2417 CB LEU A 328 -14.261 -56.159 -44.573 1.00 19.29 C ANISOU 2417 CB LEU A 328 2537 2470 2323 756 272 66 C ATOM 2418 CG LEU A 328 -13.789 -57.366 -45.379 1.00 21.09 C ANISOU 2418 CG LEU A 328 2812 2688 2514 851 280 33 C ATOM 2419 CD1 LEU A 328 -12.264 -57.437 -45.408 1.00 20.98 C ANISOU 2419 CD1 LEU A 328 2742 2726 2503 908 333 71 C ATOM 2420 CD2 LEU A 328 -14.383 -58.645 -44.812 1.00 20.85 C ANISOU 2420 CD2 LEU A 328 2834 2581 2506 848 226 -9 C ATOM 2421 N PHE A 329 -15.792 -53.574 -43.778 1.00 18.09 N ANISOU 2421 N PHE A 329 2336 2327 2211 592 259 104 N ATOM 2422 CA PHE A 329 -16.193 -52.590 -42.785 1.00 17.42 C ANISOU 2422 CA PHE A 329 2213 2239 2167 511 246 124 C ATOM 2423 C PHE A 329 -17.705 -52.411 -42.750 1.00 17.12 C ANISOU 2423 C PHE A 329 2217 2165 2122 470 206 98 C ATOM 2424 O PHE A 329 -18.320 -52.471 -41.680 1.00 17.18 O ANISOU 2424 O PHE A 329 2219 2146 2161 417 171 92 O ATOM 2425 CB PHE A 329 -15.546 -51.225 -43.043 1.00 17.59 C ANISOU 2425 CB PHE A 329 2180 2301 2201 493 298 168 C ATOM 2426 CG PHE A 329 -16.101 -50.147 -42.170 1.00 16.86 C ANISOU 2426 CG PHE A 329 2061 2198 2148 414 284 178 C ATOM 2427 CD1 PHE A 329 -15.702 -50.042 -40.846 1.00 17.47 C ANISOU 2427 CD1 PHE A 329 2092 2277 2270 367 263 183 C ATOM 2428 CD2 PHE A 329 -17.072 -49.279 -42.645 1.00 16.91 C ANISOU 2428 CD2 PHE A 329 2091 2193 2140 392 287 180 C ATOM 2429 CE1 PHE A 329 -16.247 -49.072 -40.015 1.00 16.49 C ANISOU 2429 CE1 PHE A 329 1949 2141 2176 300 247 184 C ATOM 2430 CE2 PHE A 329 -17.616 -48.312 -41.822 1.00 16.32 C ANISOU 2430 CE2 PHE A 329 1997 2104 2101 325 274 186 C ATOM 2431 CZ PHE A 329 -17.197 -48.207 -40.505 1.00 16.22 C ANISOU 2431 CZ PHE A 329 1941 2091 2133 278 254 185 C ATOM 2432 N GLN A 330 -18.294 -52.173 -43.920 1.00 17.39 N ANISOU 2432 N GLN A 330 2290 2206 2114 500 213 84 N ATOM 2433 CA GLN A 330 -19.717 -51.843 -43.999 1.00 16.80 C ANISOU 2433 CA GLN A 330 2243 2108 2031 465 177 62 C ATOM 2434 C GLN A 330 -20.591 -53.012 -43.565 1.00 16.78 C ANISOU 2434 C GLN A 330 2277 2057 2041 450 120 16 C ATOM 2435 O GLN A 330 -21.589 -52.822 -42.870 1.00 16.20 O ANISOU 2435 O GLN A 330 2202 1960 1994 395 88 9 O ATOM 2436 CB GLN A 330 -20.115 -51.415 -45.412 1.00 17.49 C ANISOU 2436 CB GLN A 330 2364 2220 2060 512 192 56 C ATOM 2437 CG GLN A 330 -19.447 -50.123 -45.921 1.00 17.63 C ANISOU 2437 CG GLN A 330 2351 2280 2069 523 256 111 C ATOM 2438 CD GLN A 330 -19.868 -48.857 -45.184 1.00 17.56 C ANISOU 2438 CD GLN A 330 2308 2262 2101 454 262 141 C ATOM 2439 OE1 GLN A 330 -20.893 -48.819 -44.505 1.00 19.42 O ANISOU 2439 OE1 GLN A 330 2551 2471 2357 407 219 120 O ATOM 2440 NE2 GLN A 330 -19.064 -47.797 -45.328 1.00 17.07 N ANISOU 2440 NE2 GLN A 330 2207 2222 2057 448 320 192 N ATOM 2441 N THR A 331 -20.220 -54.213 -43.988 1.00 17.28 N ANISOU 2441 N THR A 331 2374 2103 2089 501 110 -14 N ATOM 2442 CA THR A 331 -20.991 -55.404 -43.656 1.00 17.91 C ANISOU 2442 CA THR A 331 2491 2125 2190 488 60 -57 C ATOM 2443 C THR A 331 -20.896 -55.717 -42.158 1.00 17.68 C ANISOU 2443 C THR A 331 2434 2067 2215 438 50 -32 C ATOM 2444 O THR A 331 -21.890 -56.091 -41.528 1.00 17.45 O ANISOU 2444 O THR A 331 2416 1997 2217 392 15 -45 O ATOM 2445 CB THR A 331 -20.541 -56.615 -44.495 1.00 18.64 C ANISOU 2445 CB THR A 331 2630 2197 2255 560 55 -98 C ATOM 2446 OG1 THR A 331 -20.521 -56.257 -45.884 1.00 19.30 O ANISOU 2446 OG1 THR A 331 2738 2320 2275 617 70 -118 O ATOM 2447 CG2 THR A 331 -21.494 -57.778 -44.296 1.00 18.87 C ANISOU 2447 CG2 THR A 331 2701 2155 2314 540 1 -149 C ATOM 2448 N SER A 332 -19.713 -55.528 -41.577 1.00 17.50 N ANISOU 2448 N SER A 332 2373 2073 2204 450 81 7 N ATOM 2449 CA SER A 332 -19.560 -55.694 -40.133 1.00 17.54 C ANISOU 2449 CA SER A 332 2349 2066 2249 410 70 33 C ATOM 2450 C SER A 332 -20.435 -54.699 -39.365 1.00 16.94 C ANISOU 2450 C SER A 332 2249 1996 2191 340 59 47 C ATOM 2451 O SER A 332 -21.074 -55.072 -38.390 1.00 16.76 O ANISOU 2451 O SER A 332 2229 1944 2194 303 35 51 O ATOM 2452 CB SER A 332 -18.095 -55.572 -39.711 1.00 17.61 C ANISOU 2452 CB SER A 332 2312 2116 2263 438 100 67 C ATOM 2453 OG SER A 332 -17.312 -56.601 -40.296 1.00 19.21 O ANISOU 2453 OG SER A 332 2536 2310 2451 509 111 56 O ATOM 2454 N ARG A 333 -20.479 -53.445 -39.817 1.00 16.60 N ANISOU 2454 N ARG A 333 2184 1989 2135 326 80 57 N ATOM 2455 CA ARG A 333 -21.355 -52.449 -39.202 1.00 16.41 C ANISOU 2455 CA ARG A 333 2142 1968 2125 267 71 65 C ATOM 2456 C ARG A 333 -22.817 -52.900 -39.219 1.00 16.31 C ANISOU 2456 C ARG A 333 2162 1917 2116 242 35 38 C ATOM 2457 O ARG A 333 -23.500 -52.809 -38.202 1.00 16.51 O ANISOU 2457 O ARG A 333 2178 1930 2167 197 19 46 O ATOM 2458 CB ARG A 333 -21.216 -51.088 -39.888 1.00 16.57 C ANISOU 2458 CB ARG A 333 2144 2022 2131 265 102 80 C ATOM 2459 CG ARG A 333 -22.190 -50.037 -39.371 1.00 15.99 C ANISOU 2459 CG ARG A 333 2059 1945 2071 212 94 85 C ATOM 2460 CD ARG A 333 -21.785 -48.641 -39.797 1.00 16.67 C ANISOU 2460 CD ARG A 333 2120 2056 2157 208 132 109 C ATOM 2461 NE ARG A 333 -22.481 -47.610 -39.028 1.00 16.10 N ANISOU 2461 NE ARG A 333 2033 1978 2107 158 127 114 N ATOM 2462 CZ ARG A 333 -22.190 -46.314 -39.074 1.00 16.12 C ANISOU 2462 CZ ARG A 333 2012 1989 2125 140 158 135 C ATOM 2463 NH1 ARG A 333 -21.231 -45.869 -39.877 1.00 16.22 N ANISOU 2463 NH1 ARG A 333 2009 2017 2135 165 200 159 N ATOM 2464 NH2 ARG A 333 -22.853 -45.458 -38.302 1.00 17.02 N ANISOU 2464 NH2 ARG A 333 2117 2092 2259 100 150 133 N ATOM 2465 N LEU A 334 -23.295 -53.395 -40.356 1.00 16.55 N ANISOU 2465 N LEU A 334 2230 1933 2124 272 21 5 N ATOM 2466 CA LEU A 334 -24.686 -53.855 -40.443 1.00 16.43 C ANISOU 2466 CA LEU A 334 2238 1884 2120 245 -18 -27 C ATOM 2467 C LEU A 334 -24.958 -55.026 -39.489 1.00 16.47 C ANISOU 2467 C LEU A 334 2252 1839 2167 221 -40 -29 C ATOM 2468 O LEU A 334 -26.016 -55.087 -38.858 1.00 16.09 O ANISOU 2468 O LEU A 334 2197 1769 2147 173 -59 -29 O ATOM 2469 CB LEU A 334 -25.061 -54.242 -41.875 1.00 17.08 C ANISOU 2469 CB LEU A 334 2359 1964 2168 288 -37 -72 C ATOM 2470 CG LEU A 334 -25.162 -53.120 -42.914 1.00 16.70 C ANISOU 2470 CG LEU A 334 2310 1963 2072 315 -21 -68 C ATOM 2471 CD1 LEU A 334 -25.675 -53.690 -44.234 1.00 18.29 C ANISOU 2471 CD1 LEU A 334 2553 2163 2232 360 -51 -121 C ATOM 2472 CD2 LEU A 334 -26.066 -51.993 -42.416 1.00 17.26 C ANISOU 2472 CD2 LEU A 334 2353 2048 2157 266 -22 -47 C ATOM 2473 N ILE A 335 -23.998 -55.941 -39.385 1.00 16.59 N ANISOU 2473 N ILE A 335 2281 1836 2186 256 -32 -25 N ATOM 2474 CA ILE A 335 -24.084 -57.063 -38.443 1.00 17.05 C ANISOU 2474 CA ILE A 335 2351 1844 2284 243 -43 -15 C ATOM 2475 C ILE A 335 -24.141 -56.567 -36.993 1.00 16.65 C ANISOU 2475 C ILE A 335 2264 1810 2251 201 -33 31 C ATOM 2476 O ILE A 335 -24.998 -57.004 -36.231 1.00 16.41 O ANISOU 2476 O ILE A 335 2237 1747 2253 163 -45 40 O ATOM 2477 CB ILE A 335 -22.919 -58.076 -38.651 1.00 17.27 C ANISOU 2477 CB ILE A 335 2401 1852 2307 302 -33 -16 C ATOM 2478 CG1 ILE A 335 -23.105 -58.805 -39.986 1.00 18.18 C ANISOU 2478 CG1 ILE A 335 2563 1936 2407 343 -50 -73 C ATOM 2479 CG2 ILE A 335 -22.838 -59.080 -37.478 1.00 17.49 C ANISOU 2479 CG2 ILE A 335 2437 1835 2375 294 -36 12 C ATOM 2480 CD1 ILE A 335 -21.876 -59.563 -40.466 1.00 18.60 C ANISOU 2480 CD1 ILE A 335 2639 1986 2444 417 -32 -79 C ATOM 2481 N LEU A 336 -23.258 -55.640 -36.617 1.00 16.83 N ANISOU 2481 N LEU A 336 2252 1887 2256 208 -11 57 N ATOM 2482 CA LEU A 336 -23.278 -55.084 -35.257 1.00 16.61 C ANISOU 2482 CA LEU A 336 2191 1882 2236 173 -6 90 C ATOM 2483 C LEU A 336 -24.574 -54.321 -34.945 1.00 16.39 C ANISOU 2483 C LEU A 336 2154 1856 2216 122 -14 87 C ATOM 2484 O LEU A 336 -25.052 -54.364 -33.814 1.00 16.30 O ANISOU 2484 O LEU A 336 2134 1843 2217 94 -16 109 O ATOM 2485 CB LEU A 336 -22.046 -54.212 -34.961 1.00 16.81 C ANISOU 2485 CB LEU A 336 2177 1963 2246 187 13 108 C ATOM 2486 CG LEU A 336 -20.858 -54.982 -34.380 1.00 16.70 C ANISOU 2486 CG LEU A 336 2154 1959 2234 226 16 129 C ATOM 2487 CD1 LEU A 336 -20.284 -55.992 -35.400 1.00 17.27 C ANISOU 2487 CD1 LEU A 336 2256 2005 2302 282 22 114 C ATOM 2488 CD2 LEU A 336 -19.754 -54.048 -33.870 1.00 17.43 C ANISOU 2488 CD2 LEU A 336 2193 2111 2319 227 27 143 C ATOM 2489 N ILE A 337 -25.145 -53.641 -35.934 1.00 16.61 N ANISOU 2489 N ILE A 337 2186 1893 2233 117 -17 63 N ATOM 2490 CA ILE A 337 -26.461 -53.023 -35.742 1.00 16.44 C ANISOU 2490 CA ILE A 337 2156 1871 2220 76 -26 59 C ATOM 2491 C ILE A 337 -27.482 -54.106 -35.389 1.00 16.87 C ANISOU 2491 C ILE A 337 2225 1879 2306 51 -46 54 C ATOM 2492 O ILE A 337 -28.250 -53.957 -34.431 1.00 16.45 O ANISOU 2492 O ILE A 337 2156 1826 2270 16 -44 74 O ATOM 2493 CB ILE A 337 -26.916 -52.225 -36.980 1.00 16.48 C ANISOU 2493 CB ILE A 337 2166 1893 2204 85 -28 35 C ATOM 2494 CG1 ILE A 337 -26.067 -50.962 -37.121 1.00 16.29 C ANISOU 2494 CG1 ILE A 337 2121 1908 2160 97 0 51 C ATOM 2495 CG2 ILE A 337 -28.387 -51.831 -36.863 1.00 16.67 C ANISOU 2495 CG2 ILE A 337 2180 1913 2239 50 -45 27 C ATOM 2496 CD1 ILE A 337 -26.263 -50.237 -38.457 1.00 16.71 C ANISOU 2496 CD1 ILE A 337 2185 1978 2186 121 8 40 C ATOM 2497 N GLY A 338 -27.461 -55.204 -36.136 1.00 17.24 N ANISOU 2497 N GLY A 338 2302 1885 2364 71 -63 29 N ATOM 2498 CA GLY A 338 -28.373 -56.319 -35.880 1.00 17.79 C ANISOU 2498 CA GLY A 338 2385 1898 2478 43 -81 22 C ATOM 2499 C GLY A 338 -28.156 -56.951 -34.514 1.00 17.88 C ANISOU 2499 C GLY A 338 2393 1887 2513 31 -64 68 C ATOM 2500 O GLY A 338 -29.119 -57.244 -33.801 1.00 18.12 O ANISOU 2500 O GLY A 338 2413 1896 2577 -8 -64 87 O ATOM 2501 N GLU A 339 -26.893 -57.181 -34.155 1.00 17.83 N ANISOU 2501 N GLU A 339 2394 1893 2489 70 -49 90 N ATOM 2502 CA GLU A 339 -26.545 -57.697 -32.827 1.00 18.03 C ANISOU 2502 CA GLU A 339 2416 1911 2523 72 -34 139 C ATOM 2503 C GLU A 339 -27.081 -56.808 -31.717 1.00 17.70 C ANISOU 2503 C GLU A 339 2343 1912 2471 40 -22 169 C ATOM 2504 O GLU A 339 -27.579 -57.304 -30.711 1.00 17.88 O ANISOU 2504 O GLU A 339 2365 1917 2511 23 -11 207 O ATOM 2505 CB GLU A 339 -25.031 -57.792 -32.651 1.00 18.09 C ANISOU 2505 CB GLU A 339 2423 1947 2504 124 -24 155 C ATOM 2506 CG GLU A 339 -24.341 -58.857 -33.479 1.00 20.00 C ANISOU 2506 CG GLU A 339 2699 2146 2755 170 -28 135 C ATOM 2507 CD GLU A 339 -22.940 -59.127 -32.966 1.00 22.57 C ANISOU 2507 CD GLU A 339 3018 2499 3061 223 -16 165 C ATOM 2508 OE1 GLU A 339 -21.965 -58.862 -33.702 1.00 21.89 O ANISOU 2508 OE1 GLU A 339 2923 2443 2952 262 -11 147 O ATOM 2509 OE2 GLU A 339 -22.823 -59.597 -31.815 1.00 25.82 O ANISOU 2509 OE2 GLU A 339 3428 2904 3477 228 -10 209 O ATOM 2510 N THR A 340 -26.941 -55.495 -31.893 1.00 16.92 N ANISOU 2510 N THR A 340 2219 1868 2342 35 -21 155 N ATOM 2511 CA THR A 340 -27.405 -54.531 -30.906 1.00 16.64 C ANISOU 2511 CA THR A 340 2156 1873 2292 10 -11 173 C ATOM 2512 C THR A 340 -28.920 -54.627 -30.708 1.00 16.46 C ANISOU 2512 C THR A 340 2130 1829 2297 -30 -10 177 C ATOM 2513 O THR A 340 -29.391 -54.691 -29.582 1.00 16.82 O ANISOU 2513 O THR A 340 2165 1883 2343 -44 5 211 O ATOM 2514 CB THR A 340 -27.012 -53.092 -31.299 1.00 16.45 C ANISOU 2514 CB THR A 340 2112 1896 2242 11 -9 150 C ATOM 2515 OG1 THR A 340 -25.589 -53.026 -31.500 1.00 16.90 O ANISOU 2515 OG1 THR A 340 2164 1974 2283 44 -7 148 O ATOM 2516 CG2 THR A 340 -27.419 -52.104 -30.209 1.00 16.49 C ANISOU 2516 CG2 THR A 340 2094 1940 2232 -9 0 162 C ATOM 2517 N ILE A 341 -29.675 -54.647 -31.799 1.00 16.41 N ANISOU 2517 N ILE A 341 2126 1799 2309 -46 -26 144 N ATOM 2518 CA ILE A 341 -31.136 -54.724 -31.711 1.00 16.81 C ANISOU 2518 CA ILE A 341 2161 1834 2392 -85 -29 144 C ATOM 2519 C ILE A 341 -31.573 -56.042 -31.056 1.00 17.13 C ANISOU 2519 C ILE A 341 2210 1822 2477 -105 -21 175 C ATOM 2520 O ILE A 341 -32.477 -56.057 -30.204 1.00 17.08 O ANISOU 2520 O ILE A 341 2182 1818 2489 -134 -3 207 O ATOM 2521 CB ILE A 341 -31.793 -54.552 -33.098 1.00 16.67 C ANISOU 2521 CB ILE A 341 2144 1808 2384 -92 -56 95 C ATOM 2522 CG1 ILE A 341 -31.509 -53.146 -33.639 1.00 16.91 C ANISOU 2522 CG1 ILE A 341 2165 1889 2372 -73 -55 79 C ATOM 2523 CG2 ILE A 341 -33.300 -54.804 -33.019 1.00 18.13 C ANISOU 2523 CG2 ILE A 341 2303 1975 2611 -135 -65 93 C ATOM 2524 CD1 ILE A 341 -32.015 -52.911 -35.053 1.00 17.08 C ANISOU 2524 CD1 ILE A 341 2191 1911 2387 -64 -81 36 C ATOM 2525 N LYS A 342 -30.923 -57.136 -31.453 1.00 17.27 N ANISOU 2525 N LYS A 342 2259 1791 2513 -86 -29 170 N ATOM 2526 CA LYS A 342 -31.178 -58.458 -30.869 1.00 18.11 C ANISOU 2526 CA LYS A 342 2380 1833 2667 -99 -17 204 C ATOM 2527 C LYS A 342 -30.978 -58.448 -29.352 1.00 18.08 C ANISOU 2527 C LYS A 342 2369 1855 2645 -91 17 271 C ATOM 2528 O LYS A 342 -31.831 -58.923 -28.607 1.00 18.17 O ANISOU 2528 O LYS A 342 2370 1842 2691 -120 39 312 O ATOM 2529 CB LYS A 342 -30.257 -59.500 -31.512 1.00 18.49 C ANISOU 2529 CB LYS A 342 2469 1829 2727 -64 -30 186 C ATOM 2530 CG LYS A 342 -30.239 -60.879 -30.853 1.00 19.44 C ANISOU 2530 CG LYS A 342 2615 1877 2896 -65 -12 229 C ATOM 2531 CD LYS A 342 -31.512 -61.668 -31.130 1.00 20.30 C ANISOU 2531 CD LYS A 342 2720 1912 3081 -121 -20 217 C ATOM 2532 CE LYS A 342 -31.367 -63.133 -30.727 1.00 21.70 C ANISOU 2532 CE LYS A 342 2931 1996 3317 -119 -4 253 C ATOM 2533 NZ LYS A 342 -32.463 -63.969 -31.313 1.00 23.01 N ANISOU 2533 NZ LYS A 342 3097 2077 3570 -176 -22 219 N ATOM 2534 N ILE A 343 -29.836 -57.928 -28.911 1.00 17.78 N ANISOU 2534 N ILE A 343 2335 1868 2553 -49 22 282 N ATOM 2535 CA ILE A 343 -29.496 -57.900 -27.488 1.00 18.15 C ANISOU 2535 CA ILE A 343 2378 1949 2569 -29 47 338 C ATOM 2536 C ILE A 343 -30.429 -56.958 -26.735 1.00 18.06 C ANISOU 2536 C ILE A 343 2337 1987 2540 -56 63 351 C ATOM 2537 O ILE A 343 -30.880 -57.271 -25.626 1.00 18.69 O ANISOU 2537 O ILE A 343 2413 2072 2617 -57 91 404 O ATOM 2538 CB ILE A 343 -28.017 -57.487 -27.267 1.00 17.81 C ANISOU 2538 CB ILE A 343 2337 1957 2474 21 38 334 C ATOM 2539 CG1 ILE A 343 -27.080 -58.587 -27.770 1.00 18.76 C ANISOU 2539 CG1 ILE A 343 2487 2031 2610 58 31 335 C ATOM 2540 CG2 ILE A 343 -27.741 -57.217 -25.791 1.00 18.02 C ANISOU 2540 CG2 ILE A 343 2354 2037 2454 43 54 379 C ATOM 2541 CD1 ILE A 343 -25.615 -58.173 -27.832 1.00 18.21 C ANISOU 2541 CD1 ILE A 343 2409 2012 2497 105 19 323 C ATOM 2542 N VAL A 344 -30.737 -55.813 -27.342 1.00 17.56 N ANISOU 2542 N VAL A 344 2253 1958 2463 -71 49 306 N ATOM 2543 CA VAL A 344 -31.614 -54.841 -26.699 1.00 17.17 C ANISOU 2543 CA VAL A 344 2176 1953 2395 -89 64 313 C ATOM 2544 C VAL A 344 -32.993 -55.446 -26.431 1.00 17.68 C ANISOU 2544 C VAL A 344 2225 1986 2508 -126 85 343 C ATOM 2545 O VAL A 344 -33.539 -55.276 -25.351 1.00 18.08 O ANISOU 2545 O VAL A 344 2262 2065 2543 -128 115 384 O ATOM 2546 CB VAL A 344 -31.724 -53.524 -27.509 1.00 16.60 C ANISOU 2546 CB VAL A 344 2088 1912 2307 -95 47 261 C ATOM 2547 CG1 VAL A 344 -32.838 -52.638 -26.958 1.00 16.05 C ANISOU 2547 CG1 VAL A 344 1992 1877 2230 -113 63 266 C ATOM 2548 CG2 VAL A 344 -30.378 -52.772 -27.468 1.00 16.11 C ANISOU 2548 CG2 VAL A 344 2031 1889 2201 -64 36 242 C ATOM 2549 N ILE A 345 -33.548 -56.178 -27.389 1.00 18.10 N ANISOU 2549 N ILE A 345 2279 1981 2619 -156 69 323 N ATOM 2550 CA ILE A 345 -34.881 -56.754 -27.199 1.00 18.56 C ANISOU 2550 CA ILE A 345 2312 2006 2735 -201 86 348 C ATOM 2551 C ILE A 345 -34.847 -57.978 -26.265 1.00 19.18 C ANISOU 2551 C ILE A 345 2405 2039 2843 -202 121 415 C ATOM 2552 O ILE A 345 -35.551 -58.021 -25.250 1.00 19.31 O ANISOU 2552 O ILE A 345 2402 2072 2864 -213 161 470 O ATOM 2553 CB ILE A 345 -35.525 -57.141 -28.550 1.00 18.70 C ANISOU 2553 CB ILE A 345 2321 1976 2810 -235 50 295 C ATOM 2554 CG1 ILE A 345 -35.822 -55.877 -29.371 1.00 18.43 C ANISOU 2554 CG1 ILE A 345 2266 1991 2744 -231 24 243 C ATOM 2555 CG2 ILE A 345 -36.799 -57.972 -28.317 1.00 19.79 C ANISOU 2555 CG2 ILE A 345 2429 2067 3025 -288 66 322 C ATOM 2556 CD1 ILE A 345 -36.310 -56.144 -30.790 1.00 19.21 C ANISOU 2556 CD1 ILE A 345 2361 2059 2878 -250 -19 184 C ATOM 2557 N GLU A 346 -34.005 -58.949 -26.594 1.00 19.38 N ANISOU 2557 N GLU A 346 2469 2010 2886 -184 109 416 N ATOM 2558 CA GLU A 346 -34.056 -60.259 -25.952 1.00 20.41 C ANISOU 2558 CA GLU A 346 2618 2075 3061 -188 140 477 C ATOM 2559 C GLU A 346 -33.298 -60.387 -24.621 1.00 20.61 C ANISOU 2559 C GLU A 346 2663 2135 3031 -138 175 547 C ATOM 2560 O GLU A 346 -33.550 -61.330 -23.863 1.00 21.33 O ANISOU 2560 O GLU A 346 2766 2185 3154 -139 213 617 O ATOM 2561 CB GLU A 346 -33.608 -61.338 -26.947 1.00 20.79 C ANISOU 2561 CB GLU A 346 2701 2037 3161 -190 112 444 C ATOM 2562 CG GLU A 346 -34.547 -61.446 -28.156 1.00 21.47 C ANISOU 2562 CG GLU A 346 2767 2081 3310 -243 78 379 C ATOM 2563 CD GLU A 346 -34.372 -62.717 -28.970 1.00 23.71 C ANISOU 2563 CD GLU A 346 3086 2264 3660 -253 55 348 C ATOM 2564 OE1 GLU A 346 -33.824 -63.715 -28.447 1.00 24.47 O ANISOU 2564 OE1 GLU A 346 3217 2303 3778 -232 79 395 O ATOM 2565 OE2 GLU A 346 -34.816 -62.728 -30.141 1.00 23.81 O ANISOU 2565 OE2 GLU A 346 3091 2254 3702 -278 12 275 O ATOM 2566 N ASP A 347 -32.393 -59.453 -24.330 1.00 20.28 N ANISOU 2566 N ASP A 347 2625 2170 2909 -94 161 530 N ATOM 2567 CA ASP A 347 -31.703 -59.423 -23.035 1.00 20.41 C ANISOU 2567 CA ASP A 347 2655 2239 2862 -42 185 586 C ATOM 2568 C ASP A 347 -32.070 -58.200 -22.202 1.00 20.05 C ANISOU 2568 C ASP A 347 2582 2282 2754 -35 197 587 C ATOM 2569 O ASP A 347 -32.484 -58.330 -21.053 1.00 20.37 O ANISOU 2569 O ASP A 347 2620 2349 2769 -20 236 649 O ATOM 2570 CB ASP A 347 -30.188 -59.486 -23.229 1.00 20.28 C ANISOU 2570 CB ASP A 347 2662 2238 2804 12 155 566 C ATOM 2571 CG ASP A 347 -29.732 -60.801 -23.818 1.00 21.98 C ANISOU 2571 CG ASP A 347 2912 2368 3073 22 151 576 C ATOM 2572 OD1 ASP A 347 -30.179 -61.863 -23.328 1.00 24.94 O ANISOU 2572 OD1 ASP A 347 3304 2682 3489 16 184 637 O ATOM 2573 OD2 ASP A 347 -28.923 -60.769 -24.765 1.00 23.02 O ANISOU 2573 OD2 ASP A 347 3053 2490 3203 38 119 524 O ATOM 2574 N TYR A 348 -31.930 -57.017 -22.790 1.00 19.56 N ANISOU 2574 N TYR A 348 2504 2263 2667 -42 166 520 N ATOM 2575 CA TYR A 348 -32.043 -55.754 -22.055 1.00 19.26 C ANISOU 2575 CA TYR A 348 2447 2306 2566 -27 170 507 C ATOM 2576 C TYR A 348 -33.503 -55.426 -21.736 1.00 19.67 C ANISOU 2576 C TYR A 348 2471 2367 2637 -59 203 526 C ATOM 2577 O TYR A 348 -33.879 -55.313 -20.565 1.00 20.31 O ANISOU 2577 O TYR A 348 2547 2490 2678 -39 238 572 O ATOM 2578 CB TYR A 348 -31.365 -54.653 -22.872 1.00 18.45 C ANISOU 2578 CB TYR A 348 2338 2230 2443 -25 130 433 C ATOM 2579 CG TYR A 348 -31.541 -53.229 -22.403 1.00 18.61 C ANISOU 2579 CG TYR A 348 2339 2315 2415 -20 128 402 C ATOM 2580 CD1 TYR A 348 -30.761 -52.712 -21.376 1.00 19.03 C ANISOU 2580 CD1 TYR A 348 2398 2430 2402 20 123 401 C ATOM 2581 CD2 TYR A 348 -32.448 -52.380 -23.030 1.00 18.48 C ANISOU 2581 CD2 TYR A 348 2303 2299 2420 -50 127 367 C ATOM 2582 CE1 TYR A 348 -30.903 -51.398 -20.962 1.00 19.98 C ANISOU 2582 CE1 TYR A 348 2506 2601 2483 25 118 363 C ATOM 2583 CE2 TYR A 348 -32.594 -51.060 -22.632 1.00 18.60 C ANISOU 2583 CE2 TYR A 348 2307 2365 2397 -42 127 335 C ATOM 2584 CZ TYR A 348 -31.823 -50.575 -21.597 1.00 19.27 C ANISOU 2584 CZ TYR A 348 2400 2502 2420 -6 123 331 C ATOM 2585 OH TYR A 348 -31.956 -49.265 -21.205 1.00 21.18 O ANISOU 2585 OH TYR A 348 2635 2786 2628 2 120 292 O ATOM 2586 N VAL A 349 -34.327 -55.300 -22.772 1.00 19.55 N ANISOU 2586 N VAL A 349 2434 2316 2678 -105 191 491 N ATOM 2587 CA VAL A 349 -35.772 -55.086 -22.590 1.00 19.61 C ANISOU 2587 CA VAL A 349 2405 2330 2716 -138 221 509 C ATOM 2588 C VAL A 349 -36.421 -56.265 -21.858 1.00 20.51 C ANISOU 2588 C VAL A 349 2514 2408 2871 -153 268 588 C ATOM 2589 O VAL A 349 -37.271 -56.071 -20.981 1.00 20.99 O ANISOU 2589 O VAL A 349 2551 2504 2921 -153 313 632 O ATOM 2590 CB VAL A 349 -36.485 -54.838 -23.939 1.00 19.31 C ANISOU 2590 CB VAL A 349 2341 2261 2733 -181 191 454 C ATOM 2591 CG1 VAL A 349 -38.015 -54.883 -23.766 1.00 19.56 C ANISOU 2591 CG1 VAL A 349 2326 2293 2812 -219 220 479 C ATOM 2592 CG2 VAL A 349 -36.054 -53.503 -24.528 1.00 19.29 C ANISOU 2592 CG2 VAL A 349 2340 2300 2688 -164 159 391 C ATOM 2593 N GLN A 350 -36.025 -57.486 -22.212 1.00 20.89 N ANISOU 2593 N GLN A 350 2586 2383 2968 -164 263 607 N ATOM 2594 CA GLN A 350 -36.522 -58.672 -21.521 1.00 21.73 C ANISOU 2594 CA GLN A 350 2693 2441 3121 -178 312 689 C ATOM 2595 C GLN A 350 -36.345 -58.511 -20.011 1.00 22.20 C ANISOU 2595 C GLN A 350 2764 2566 3107 -126 359 759 C ATOM 2596 O GLN A 350 -37.292 -58.702 -19.251 1.00 22.49 O ANISOU 2596 O GLN A 350 2777 2612 3157 -138 414 822 O ATOM 2597 CB GLN A 350 -35.803 -59.938 -22.001 1.00 22.01 C ANISOU 2597 CB GLN A 350 2767 2390 3204 -178 298 699 C ATOM 2598 CG GLN A 350 -36.324 -61.239 -21.391 1.00 23.36 C ANISOU 2598 CG GLN A 350 2944 2491 3441 -197 350 785 C ATOM 2599 CD GLN A 350 -37.680 -61.637 -21.937 1.00 24.25 C ANISOU 2599 CD GLN A 350 3012 2546 3657 -275 361 781 C ATOM 2600 OE1 GLN A 350 -37.854 -61.769 -23.151 1.00 24.94 O ANISOU 2600 OE1 GLN A 350 3091 2586 3800 -314 313 710 O ATOM 2601 NE2 GLN A 350 -38.647 -61.837 -21.043 1.00 23.48 N ANISOU 2601 NE2 GLN A 350 2882 2456 3585 -295 423 857 N ATOM 2602 N HIS A 351 -35.140 -58.136 -19.586 1.00 21.96 N ANISOU 2602 N HIS A 351 2766 2584 2994 -68 338 747 N ATOM 2603 CA HIS A 351 -34.874 -57.949 -18.161 1.00 22.23 C ANISOU 2603 CA HIS A 351 2814 2689 2944 -9 372 804 C ATOM 2604 C HIS A 351 -35.742 -56.854 -17.545 1.00 22.41 C ANISOU 2604 C HIS A 351 2806 2788 2922 -6 397 797 C ATOM 2605 O HIS A 351 -36.431 -57.082 -16.556 1.00 22.53 O ANISOU 2605 O HIS A 351 2813 2828 2918 9 455 868 O ATOM 2606 CB HIS A 351 -33.415 -57.597 -17.890 1.00 22.01 C ANISOU 2606 CB HIS A 351 2817 2710 2837 51 332 774 C ATOM 2607 CG HIS A 351 -33.190 -57.093 -16.500 1.00 22.04 C ANISOU 2607 CG HIS A 351 2830 2806 2740 112 352 806 C ATOM 2608 ND1 HIS A 351 -33.238 -57.917 -15.396 1.00 22.51 N ANISOU 2608 ND1 HIS A 351 2909 2876 2767 155 400 900 N ATOM 2609 CD2 HIS A 351 -32.977 -55.841 -16.028 1.00 21.86 C ANISOU 2609 CD2 HIS A 351 2799 2867 2640 140 331 755 C ATOM 2610 CE1 HIS A 351 -33.049 -57.196 -14.305 1.00 22.64 C ANISOU 2610 CE1 HIS A 351 2932 2989 2683 212 406 903 C ATOM 2611 NE2 HIS A 351 -32.895 -55.932 -14.660 1.00 21.90 N ANISOU 2611 NE2 HIS A 351 2820 2938 2562 201 362 812 N ATOM 2612 N LEU A 352 -35.680 -55.653 -18.110 1.00 21.76 N ANISOU 2612 N LEU A 352 2709 2740 2819 -14 357 715 N ATOM 2613 CA LEU A 352 -36.352 -54.520 -17.475 1.00 22.11 C ANISOU 2613 CA LEU A 352 2732 2858 2811 2 377 701 C ATOM 2614 C LEU A 352 -37.881 -54.667 -17.499 1.00 22.29 C ANISOU 2614 C LEU A 352 2712 2867 2893 -39 425 738 C ATOM 2615 O LEU A 352 -38.565 -54.113 -16.636 1.00 22.43 O ANISOU 2615 O LEU A 352 2712 2944 2865 -15 466 762 O ATOM 2616 CB LEU A 352 -35.891 -53.190 -18.076 1.00 21.90 C ANISOU 2616 CB LEU A 352 2704 2862 2756 5 325 607 C ATOM 2617 CG LEU A 352 -36.250 -52.850 -19.514 1.00 21.59 C ANISOU 2617 CG LEU A 352 2643 2777 2784 -46 292 549 C ATOM 2618 CD1 LEU A 352 -37.692 -52.345 -19.633 1.00 23.84 C ANISOU 2618 CD1 LEU A 352 2886 3073 3100 -72 320 550 C ATOM 2619 CD2 LEU A 352 -35.266 -51.803 -20.055 1.00 22.67 C ANISOU 2619 CD2 LEU A 352 2793 2932 2887 -32 242 472 C ATOM 2620 N SER A 353 -38.409 -55.423 -18.465 1.00 21.97 N ANISOU 2620 N SER A 353 2649 2749 2950 -99 419 740 N ATOM 2621 CA SER A 353 -39.855 -55.663 -18.550 1.00 22.08 C ANISOU 2621 CA SER A 353 2611 2746 3034 -146 460 773 C ATOM 2622 C SER A 353 -40.363 -56.465 -17.362 1.00 22.99 C ANISOU 2622 C SER A 353 2720 2866 3149 -134 537 879 C ATOM 2623 O SER A 353 -41.485 -56.247 -16.884 1.00 23.35 O ANISOU 2623 O SER A 353 2721 2943 3206 -143 588 917 O ATOM 2624 CB SER A 353 -40.226 -56.409 -19.839 1.00 22.01 C ANISOU 2624 CB SER A 353 2581 2650 3133 -214 429 747 C ATOM 2625 OG SER A 353 -39.852 -57.777 -19.778 1.00 22.30 O ANISOU 2625 OG SER A 353 2643 2611 3219 -228 443 797 O ATOM 2626 N GLY A 354 -39.546 -57.419 -16.921 1.00 23.18 N ANISOU 2626 N GLY A 354 2788 2858 3162 -109 547 930 N ATOM 2627 CA GLY A 354 -39.933 -58.362 -15.884 1.00 24.26 C ANISOU 2627 CA GLY A 354 2927 2984 3307 -97 623 1042 C ATOM 2628 C GLY A 354 -40.906 -59.433 -16.338 1.00 24.96 C ANISOU 2628 C GLY A 354 2977 2981 3526 -172 657 1090 C ATOM 2629 O GLY A 354 -41.426 -60.168 -15.508 1.00 25.67 O ANISOU 2629 O GLY A 354 3058 3057 3638 -172 731 1191 O ATOM 2630 N TYR A 355 -41.143 -59.546 -17.646 1.00 24.68 N ANISOU 2630 N TYR A 355 2918 2881 3576 -236 605 1020 N ATOM 2631 CA TYR A 355 -42.163 -60.467 -18.150 1.00 25.65 C ANISOU 2631 CA TYR A 355 2996 2920 3832 -317 627 1047 C ATOM 2632 C TYR A 355 -41.646 -61.894 -18.188 1.00 26.55 C ANISOU 2632 C TYR A 355 3150 2929 4010 -331 638 1098 C ATOM 2633 O TYR A 355 -40.462 -62.126 -18.428 1.00 26.17 O ANISOU 2633 O TYR A 355 3161 2860 3924 -294 598 1071 O ATOM 2634 CB TYR A 355 -42.637 -60.083 -19.559 1.00 25.12 C ANISOU 2634 CB TYR A 355 2889 2827 3829 -375 559 946 C ATOM 2635 CG TYR A 355 -43.185 -58.679 -19.712 1.00 24.07 C ANISOU 2635 CG TYR A 355 2716 2784 3645 -362 542 891 C ATOM 2636 CD1 TYR A 355 -43.669 -57.958 -18.619 1.00 24.71 C ANISOU 2636 CD1 TYR A 355 2777 2952 3659 -321 599 938 C ATOM 2637 CD2 TYR A 355 -43.245 -58.084 -20.963 1.00 23.21 C ANISOU 2637 CD2 TYR A 355 2592 2672 3554 -385 471 794 C ATOM 2638 CE1 TYR A 355 -44.167 -56.678 -18.771 1.00 23.86 C ANISOU 2638 CE1 TYR A 355 2637 2920 3509 -305 585 886 C ATOM 2639 CE2 TYR A 355 -43.745 -56.812 -21.125 1.00 23.82 C ANISOU 2639 CE2 TYR A 355 2636 2825 3588 -369 457 748 C ATOM 2640 CZ TYR A 355 -44.204 -56.108 -20.028 1.00 24.03 C ANISOU 2640 CZ TYR A 355 2644 2930 3554 -329 514 793 C ATOM 2641 OH TYR A 355 -44.694 -54.831 -20.194 1.00 23.86 O ANISOU 2641 OH TYR A 355 2595 2978 3493 -308 502 745 O ATOM 2642 N HIS A 356 -42.550 -62.839 -17.951 1.00 28.04 N ANISOU 2642 N HIS A 356 3303 3051 4300 -386 696 1172 N ATOM 2643 CA HIS A 356 -42.247 -64.259 -18.111 1.00 29.15 C ANISOU 2643 CA HIS A 356 3477 3070 4530 -414 709 1217 C ATOM 2644 C HIS A 356 -42.336 -64.673 -19.579 1.00 28.83 C ANISOU 2644 C HIS A 356 3426 2937 4590 -483 636 1120 C ATOM 2645 O HIS A 356 -41.785 -65.707 -19.973 1.00 29.08 O ANISOU 2645 O HIS A 356 3503 2868 4681 -494 620 1120 O ATOM 2646 CB HIS A 356 -43.200 -65.110 -17.274 1.00 30.63 C ANISOU 2646 CB HIS A 356 3629 3212 4796 -451 806 1338 C ATOM 2647 CG HIS A 356 -43.083 -64.871 -15.802 1.00 32.30 C ANISOU 2647 CG HIS A 356 3859 3510 4905 -374 886 1445 C ATOM 2648 ND1 HIS A 356 -41.869 -64.811 -15.152 1.00 33.74 N ANISOU 2648 ND1 HIS A 356 4115 3734 4971 -281 881 1469 N ATOM 2649 CD2 HIS A 356 -44.028 -64.688 -14.851 1.00 34.08 C ANISOU 2649 CD2 HIS A 356 4037 3790 5122 -371 972 1533 C ATOM 2650 CE1 HIS A 356 -42.072 -64.601 -13.864 1.00 34.90 C ANISOU 2650 CE1 HIS A 356 4264 3961 5037 -222 957 1563 C ATOM 2651 NE2 HIS A 356 -43.374 -64.522 -13.655 1.00 35.32 N ANISOU 2651 NE2 HIS A 356 4246 4022 5151 -274 1016 1606 N ATOM 2652 N PHE A 357 -43.050 -63.880 -20.375 1.00 28.08 N ANISOU 2652 N PHE A 357 3275 2880 4513 -524 590 1037 N ATOM 2653 CA PHE A 357 -43.094 -64.068 -21.823 1.00 27.61 C ANISOU 2653 CA PHE A 357 3209 2759 4524 -575 509 931 C ATOM 2654 C PHE A 357 -41.720 -63.774 -22.425 1.00 26.71 C ANISOU 2654 C PHE A 357 3165 2655 4328 -516 444 860 C ATOM 2655 O PHE A 357 -41.069 -62.786 -22.061 1.00 25.86 O ANISOU 2655 O PHE A 357 3079 2639 4106 -452 437 849 O ATOM 2656 CB PHE A 357 -44.148 -63.153 -22.461 1.00 27.32 C ANISOU 2656 CB PHE A 357 3094 2781 4505 -615 477 865 C ATOM 2657 CG PHE A 357 -44.143 -63.180 -23.965 1.00 26.59 C ANISOU 2657 CG PHE A 357 2998 2647 4457 -652 386 749 C ATOM 2658 CD1 PHE A 357 -44.462 -64.347 -24.648 1.00 28.75 C ANISOU 2658 CD1 PHE A 357 3264 2806 4853 -719 363 726 C ATOM 2659 CD2 PHE A 357 -43.814 -62.043 -24.700 1.00 26.36 C ANISOU 2659 CD2 PHE A 357 2975 2692 4348 -615 325 664 C ATOM 2660 CE1 PHE A 357 -44.461 -64.383 -26.030 1.00 28.60 C ANISOU 2660 CE1 PHE A 357 3245 2756 4866 -745 276 614 C ATOM 2661 CE2 PHE A 357 -43.808 -62.075 -26.087 1.00 25.33 C ANISOU 2661 CE2 PHE A 357 2844 2531 4250 -640 245 562 C ATOM 2662 CZ PHE A 357 -44.133 -63.246 -26.752 1.00 27.30 C ANISOU 2662 CZ PHE A 357 3087 2674 4611 -702 218 535 C ATOM 2663 N LYS A 358 -41.296 -64.631 -23.349 1.00 26.72 N ANISOU 2663 N LYS A 358 3200 2560 4394 -540 399 810 N ATOM 2664 CA LYS A 358 -39.970 -64.531 -23.949 1.00 26.47 C ANISOU 2664 CA LYS A 358 3234 2528 4297 -484 345 751 C ATOM 2665 C LYS A 358 -40.046 -63.688 -25.221 1.00 25.22 C ANISOU 2665 C LYS A 358 3057 2408 4119 -494 269 636 C ATOM 2666 O LYS A 358 -40.500 -64.152 -26.274 1.00 25.72 O ANISOU 2666 O LYS A 358 3106 2408 4259 -544 224 570 O ATOM 2667 CB LYS A 358 -39.414 -65.926 -24.248 1.00 27.49 C ANISOU 2667 CB LYS A 358 3416 2533 4497 -490 341 760 C ATOM 2668 CG LYS A 358 -37.966 -65.943 -24.722 1.00 28.89 C ANISOU 2668 CG LYS A 358 3661 2711 4606 -422 299 715 C ATOM 2669 CD LYS A 358 -37.485 -67.367 -24.954 1.00 32.62 C ANISOU 2669 CD LYS A 358 4186 3055 5153 -423 301 729 C ATOM 2670 CE LYS A 358 -36.151 -67.401 -25.679 1.00 33.55 C ANISOU 2670 CE LYS A 358 4363 3171 5215 -360 252 667 C ATOM 2671 NZ LYS A 358 -35.099 -66.660 -24.934 1.00 35.60 N ANISOU 2671 NZ LYS A 358 4643 3531 5353 -279 264 702 N ATOM 2672 N LEU A 359 -39.609 -62.442 -25.105 1.00 24.03 N ANISOU 2672 N LEU A 359 2907 2359 3863 -444 256 612 N ATOM 2673 CA LEU A 359 -39.619 -61.505 -26.226 1.00 23.06 C ANISOU 2673 CA LEU A 359 2772 2281 3709 -442 193 517 C ATOM 2674 C LEU A 359 -38.738 -62.025 -27.361 1.00 22.98 C ANISOU 2674 C LEU A 359 2811 2215 3707 -428 138 448 C ATOM 2675 O LEU A 359 -37.850 -62.853 -27.142 1.00 22.89 O ANISOU 2675 O LEU A 359 2850 2150 3697 -401 148 474 O ATOM 2676 CB LEU A 359 -39.132 -60.133 -25.772 1.00 22.06 C ANISOU 2676 CB LEU A 359 2648 2261 3472 -387 198 514 C ATOM 2677 CG LEU A 359 -39.891 -59.475 -24.614 1.00 21.81 C ANISOU 2677 CG LEU A 359 2576 2298 3412 -384 253 575 C ATOM 2678 CD1 LEU A 359 -39.156 -58.237 -24.149 1.00 20.51 C ANISOU 2678 CD1 LEU A 359 2431 2224 3139 -323 251 563 C ATOM 2679 CD2 LEU A 359 -41.321 -59.136 -25.019 1.00 21.42 C ANISOU 2679 CD2 LEU A 359 2456 2262 3420 -437 249 554 C ATOM 2680 N LYS A 360 -38.973 -61.522 -28.569 1.00 22.75 N ANISOU 2680 N LYS A 360 2767 2201 3675 -439 80 362 N ATOM 2681 CA LYS A 360 -38.288 -62.022 -29.756 1.00 23.09 C ANISOU 2681 CA LYS A 360 2853 2195 3726 -425 27 290 C ATOM 2682 C LYS A 360 -37.924 -60.875 -30.679 1.00 22.10 C ANISOU 2682 C LYS A 360 2730 2141 3525 -389 -17 222 C ATOM 2683 O LYS A 360 -38.745 -59.996 -30.926 1.00 21.90 O ANISOU 2683 O LYS A 360 2659 2172 3490 -405 -29 200 O ATOM 2684 CB LYS A 360 -39.205 -63.013 -30.483 1.00 24.35 C ANISOU 2684 CB LYS A 360 2992 2267 3993 -490 -4 248 C ATOM 2685 CG LYS A 360 -38.568 -63.788 -31.620 1.00 25.55 C ANISOU 2685 CG LYS A 360 3195 2350 4163 -477 -55 174 C ATOM 2686 CD LYS A 360 -39.612 -64.633 -32.331 1.00 28.35 C ANISOU 2686 CD LYS A 360 3519 2626 4624 -547 -94 120 C ATOM 2687 CE LYS A 360 -38.995 -65.547 -33.377 1.00 29.44 C ANISOU 2687 CE LYS A 360 3716 2684 4786 -531 -142 43 C ATOM 2688 NZ LYS A 360 -40.052 -66.317 -34.103 1.00 32.52 N ANISOU 2688 NZ LYS A 360 4074 3000 5281 -603 -190 -24 N ATOM 2689 N PHE A 361 -36.688 -60.876 -31.171 1.00 21.69 N ANISOU 2689 N PHE A 361 2730 2090 3422 -337 -35 194 N ATOM 2690 CA PHE A 361 -36.312 -60.011 -32.283 1.00 21.08 C ANISOU 2690 CA PHE A 361 2660 2062 3287 -305 -76 127 C ATOM 2691 C PHE A 361 -36.500 -60.809 -33.573 1.00 21.82 C ANISOU 2691 C PHE A 361 2771 2096 3422 -317 -128 52 C ATOM 2692 O PHE A 361 -35.749 -61.754 -33.860 1.00 22.10 O ANISOU 2692 O PHE A 361 2855 2070 3474 -297 -135 38 O ATOM 2693 CB PHE A 361 -34.881 -59.512 -32.153 1.00 20.39 C ANISOU 2693 CB PHE A 361 2611 2015 3122 -242 -65 138 C ATOM 2694 CG PHE A 361 -34.405 -58.741 -33.345 1.00 20.12 C ANISOU 2694 CG PHE A 361 2588 2022 3035 -207 -98 77 C ATOM 2695 CD1 PHE A 361 -35.187 -57.727 -33.893 1.00 19.76 C ANISOU 2695 CD1 PHE A 361 2509 2027 2970 -217 -117 48 C ATOM 2696 CD2 PHE A 361 -33.179 -59.024 -33.925 1.00 20.34 C ANISOU 2696 CD2 PHE A 361 2659 2040 3030 -158 -107 56 C ATOM 2697 CE1 PHE A 361 -34.749 -57.014 -34.998 1.00 19.11 C ANISOU 2697 CE1 PHE A 361 2441 1983 2837 -180 -143 1 C ATOM 2698 CE2 PHE A 361 -32.739 -58.308 -35.023 1.00 19.94 C ANISOU 2698 CE2 PHE A 361 2619 2030 2929 -123 -130 9 C ATOM 2699 CZ PHE A 361 -33.524 -57.311 -35.560 1.00 18.34 C ANISOU 2699 CZ PHE A 361 2386 1875 2707 -134 -147 -16 C ATOM 2700 N ASP A 362 -37.533 -60.441 -34.322 1.00 21.94 N ANISOU 2700 N ASP A 362 2749 2132 3456 -347 -166 3 N ATOM 2701 CA ASP A 362 -37.883 -61.134 -35.551 1.00 22.66 C ANISOU 2701 CA ASP A 362 2850 2176 3585 -360 -224 -79 C ATOM 2702 C ASP A 362 -38.596 -60.176 -36.491 1.00 22.09 C ANISOU 2702 C ASP A 362 2742 2172 3477 -356 -268 -133 C ATOM 2703 O ASP A 362 -39.822 -60.058 -36.456 1.00 21.32 O ANISOU 2703 O ASP A 362 2587 2087 3427 -403 -284 -141 O ATOM 2704 CB ASP A 362 -38.758 -62.351 -35.260 1.00 24.31 C ANISOU 2704 CB ASP A 362 3036 2294 3905 -430 -228 -76 C ATOM 2705 CG ASP A 362 -39.076 -63.148 -36.511 1.00 26.06 C ANISOU 2705 CG ASP A 362 3272 2459 4171 -446 -295 -172 C ATOM 2706 OD1 ASP A 362 -38.558 -62.791 -37.595 1.00 27.38 O ANISOU 2706 OD1 ASP A 362 3472 2661 4271 -394 -336 -237 O ATOM 2707 OD2 ASP A 362 -39.838 -64.132 -36.410 1.00 30.57 O ANISOU 2707 OD2 ASP A 362 3822 2949 4844 -510 -306 -184 O ATOM 2708 N PRO A 363 -37.821 -59.478 -37.336 1.00 21.19 N ANISOU 2708 N PRO A 363 2662 2108 3280 -294 -286 -167 N ATOM 2709 CA PRO A 363 -38.397 -58.561 -38.317 1.00 21.29 C ANISOU 2709 CA PRO A 363 2651 2188 3249 -275 -326 -214 C ATOM 2710 C PRO A 363 -39.543 -59.151 -39.141 1.00 22.40 C ANISOU 2710 C PRO A 363 2760 2305 3444 -314 -390 -286 C ATOM 2711 O PRO A 363 -40.454 -58.420 -39.521 1.00 22.43 O ANISOU 2711 O PRO A 363 2719 2367 3437 -319 -417 -304 O ATOM 2712 CB PRO A 363 -37.202 -58.233 -39.208 1.00 20.58 C ANISOU 2712 CB PRO A 363 2618 2123 3077 -203 -333 -242 C ATOM 2713 CG PRO A 363 -36.060 -58.240 -38.254 1.00 20.22 C ANISOU 2713 CG PRO A 363 2600 2067 3016 -184 -276 -179 C ATOM 2714 CD PRO A 363 -36.348 -59.417 -37.344 1.00 21.11 C ANISOU 2714 CD PRO A 363 2708 2102 3211 -235 -261 -151 C ATOM 2715 N GLU A 364 -39.509 -60.457 -39.400 1.00 23.62 N ANISOU 2715 N GLU A 364 2939 2376 3661 -340 -416 -327 N ATOM 2716 CA GLU A 364 -40.547 -61.102 -40.220 1.00 25.23 C ANISOU 2716 CA GLU A 364 3114 2550 3924 -381 -486 -408 C ATOM 2717 C GLU A 364 -41.959 -60.955 -39.643 1.00 25.23 C ANISOU 2717 C GLU A 364 3026 2562 3998 -453 -487 -386 C ATOM 2718 O GLU A 364 -42.938 -61.003 -40.391 1.00 25.72 O ANISOU 2718 O GLU A 364 3043 2641 4088 -477 -550 -452 O ATOM 2719 CB GLU A 364 -40.206 -62.575 -40.481 1.00 26.69 C ANISOU 2719 CB GLU A 364 3343 2625 4172 -400 -508 -455 C ATOM 2720 CG GLU A 364 -38.909 -62.730 -41.279 1.00 30.01 C ANISOU 2720 CG GLU A 364 3845 3043 4514 -320 -517 -492 C ATOM 2721 CD GLU A 364 -38.630 -64.137 -41.765 1.00 35.31 C ANISOU 2721 CD GLU A 364 4566 3610 5241 -326 -550 -559 C ATOM 2722 OE1 GLU A 364 -37.441 -64.435 -42.018 1.00 39.28 O ANISOU 2722 OE1 GLU A 364 5135 4093 5695 -264 -533 -563 O ATOM 2723 OE2 GLU A 364 -39.580 -64.937 -41.909 1.00 38.89 O ANISOU 2723 OE2 GLU A 364 4990 3999 5788 -392 -593 -609 O ATOM 2724 N LEU A 365 -42.060 -60.747 -38.330 1.00 24.62 N ANISOU 2724 N LEU A 365 2922 2484 3948 -481 -419 -295 N ATOM 2725 CA LEU A 365 -43.356 -60.547 -37.667 1.00 25.17 C ANISOU 2725 CA LEU A 365 2906 2573 4085 -543 -405 -260 C ATOM 2726 C LEU A 365 -44.138 -59.358 -38.219 1.00 24.99 C ANISOU 2726 C LEU A 365 2832 2651 4013 -521 -437 -285 C ATOM 2727 O LEU A 365 -45.366 -59.339 -38.149 1.00 25.76 O ANISOU 2727 O LEU A 365 2850 2766 4171 -570 -456 -292 O ATOM 2728 CB LEU A 365 -43.160 -60.339 -36.164 1.00 24.70 C ANISOU 2728 CB LEU A 365 2838 2514 4031 -554 -319 -154 C ATOM 2729 CG LEU A 365 -42.583 -61.501 -35.355 1.00 25.56 C ANISOU 2729 CG LEU A 365 2986 2529 4198 -578 -275 -106 C ATOM 2730 CD1 LEU A 365 -42.331 -61.043 -33.916 1.00 25.76 C ANISOU 2730 CD1 LEU A 365 3006 2584 4198 -568 -193 -1 C ATOM 2731 CD2 LEU A 365 -43.500 -62.714 -35.399 1.00 27.36 C ANISOU 2731 CD2 LEU A 365 3174 2667 4553 -660 -294 -127 C ATOM 2732 N LEU A 366 -43.430 -58.364 -38.749 1.00 24.34 N ANISOU 2732 N LEU A 366 2790 2634 3825 -446 -440 -292 N ATOM 2733 CA LEU A 366 -44.067 -57.144 -39.242 1.00 24.23 C ANISOU 2733 CA LEU A 366 2737 2713 3756 -412 -462 -304 C ATOM 2734 C LEU A 366 -44.336 -57.141 -40.752 1.00 24.90 C ANISOU 2734 C LEU A 366 2827 2827 3806 -380 -546 -397 C ATOM 2735 O LEU A 366 -44.989 -56.220 -41.255 1.00 24.72 O ANISOU 2735 O LEU A 366 2767 2882 3742 -350 -573 -410 O ATOM 2736 CB LEU A 366 -43.226 -55.925 -38.860 1.00 23.28 C ANISOU 2736 CB LEU A 366 2652 2647 3545 -350 -409 -249 C ATOM 2737 CG LEU A 366 -43.138 -55.634 -37.357 1.00 23.05 C ANISOU 2737 CG LEU A 366 2609 2616 3533 -371 -332 -162 C ATOM 2738 CD1 LEU A 366 -42.179 -54.491 -37.084 1.00 21.97 C ANISOU 2738 CD1 LEU A 366 2514 2523 3310 -312 -291 -124 C ATOM 2739 CD2 LEU A 366 -44.516 -55.335 -36.756 1.00 23.76 C ANISOU 2739 CD2 LEU A 366 2613 2738 3675 -413 -321 -136 C ATOM 2740 N PHE A 367 -43.873 -58.165 -41.470 1.00 25.40 N ANISOU 2740 N PHE A 367 2937 2832 3883 -380 -589 -461 N ATOM 2741 CA PHE A 367 -43.954 -58.153 -42.936 1.00 26.01 C ANISOU 2741 CA PHE A 367 3034 2943 3907 -334 -668 -553 C ATOM 2742 C PHE A 367 -45.384 -58.189 -43.484 1.00 27.45 C ANISOU 2742 C PHE A 367 3135 3161 4132 -368 -741 -613 C ATOM 2743 O PHE A 367 -45.615 -57.728 -44.599 1.00 27.89 O ANISOU 2743 O PHE A 367 3193 3282 4120 -313 -801 -671 O ATOM 2744 CB PHE A 367 -43.122 -59.279 -43.571 1.00 26.23 C ANISOU 2744 CB PHE A 367 3133 2898 3936 -321 -697 -616 C ATOM 2745 CG PHE A 367 -41.625 -59.133 -43.403 1.00 25.37 C ANISOU 2745 CG PHE A 367 3103 2776 3759 -263 -640 -573 C ATOM 2746 CD1 PHE A 367 -40.786 -60.172 -43.791 1.00 26.42 C ANISOU 2746 CD1 PHE A 367 3302 2839 3898 -247 -651 -616 C ATOM 2747 CD2 PHE A 367 -41.047 -57.985 -42.864 1.00 24.34 C ANISOU 2747 CD2 PHE A 367 2982 2702 3566 -224 -576 -494 C ATOM 2748 CE1 PHE A 367 -39.407 -60.065 -43.651 1.00 25.53 C ANISOU 2748 CE1 PHE A 367 3254 2719 3726 -192 -600 -577 C ATOM 2749 CE2 PHE A 367 -39.672 -57.883 -42.718 1.00 23.47 C ANISOU 2749 CE2 PHE A 367 2934 2581 3402 -177 -527 -459 C ATOM 2750 CZ PHE A 367 -38.854 -58.926 -43.111 1.00 23.90 C ANISOU 2750 CZ PHE A 367 3047 2573 3462 -160 -539 -498 C ATOM 2751 N ASN A 368 -46.334 -58.735 -42.723 1.00 28.51 N ANISOU 2751 N ASN A 368 3197 3257 4379 -454 -736 -598 N ATOM 2752 CA ASN A 368 -47.743 -58.693 -43.130 1.00 29.92 C ANISOU 2752 CA ASN A 368 3282 3478 4609 -492 -802 -647 C ATOM 2753 C ASN A 368 -48.552 -57.640 -42.366 1.00 29.53 C ANISOU 2753 C ASN A 368 3156 3502 4562 -497 -758 -573 C ATOM 2754 O ASN A 368 -49.776 -57.695 -42.354 1.00 30.52 O ANISOU 2754 O ASN A 368 3188 3654 4755 -544 -792 -592 O ATOM 2755 CB ASN A 368 -48.405 -60.084 -43.034 1.00 31.43 C ANISOU 2755 CB ASN A 368 3429 3578 4935 -589 -841 -699 C ATOM 2756 CG ASN A 368 -48.564 -60.586 -41.599 1.00 32.31 C ANISOU 2756 CG ASN A 368 3508 3619 5149 -667 -759 -610 C ATOM 2757 OD1 ASN A 368 -48.171 -59.931 -40.633 1.00 33.89 O ANISOU 2757 OD1 ASN A 368 3721 3842 5316 -647 -675 -513 O ATOM 2758 ND2 ASN A 368 -49.137 -61.774 -41.465 1.00 35.57 N ANISOU 2758 ND2 ASN A 368 3882 3944 5689 -756 -783 -643 N ATOM 2759 N GLN A 369 -47.860 -56.684 -41.746 1.00 28.26 N ANISOU 2759 N GLN A 369 3034 3373 4331 -447 -683 -492 N ATOM 2760 CA GLN A 369 -48.498 -55.621 -40.972 1.00 27.91 C ANISOU 2760 CA GLN A 369 2931 3393 4279 -441 -634 -422 C ATOM 2761 C GLN A 369 -48.189 -54.257 -41.571 1.00 27.34 C ANISOU 2761 C GLN A 369 2891 3406 4091 -347 -635 -413 C ATOM 2762 O GLN A 369 -47.180 -54.084 -42.266 1.00 26.83 O ANISOU 2762 O GLN A 369 2906 3341 3947 -288 -643 -433 O ATOM 2763 CB GLN A 369 -47.993 -55.640 -39.528 1.00 27.30 C ANISOU 2763 CB GLN A 369 2871 3276 4227 -467 -537 -329 C ATOM 2764 CG GLN A 369 -48.261 -56.938 -38.780 1.00 28.72 C ANISOU 2764 CG GLN A 369 3023 3367 4520 -555 -518 -314 C ATOM 2765 CD GLN A 369 -49.739 -57.197 -38.581 1.00 30.63 C ANISOU 2765 CD GLN A 369 3153 3625 4860 -622 -538 -320 C ATOM 2766 OE1 GLN A 369 -50.266 -58.232 -39.001 1.00 34.26 O ANISOU 2766 OE1 GLN A 369 3577 4032 5408 -685 -590 -377 O ATOM 2767 NE2 GLN A 369 -50.422 -56.250 -37.955 1.00 31.20 N ANISOU 2767 NE2 GLN A 369 3166 3767 4921 -609 -497 -265 N ATOM 2768 N GLN A 370 -49.050 -53.288 -41.282 1.00 27.34 N ANISOU 2768 N GLN A 370 2829 3476 4084 -331 -621 -379 N ATOM 2769 CA GLN A 370 -48.757 -51.893 -41.604 1.00 26.88 C ANISOU 2769 CA GLN A 370 2802 3486 3926 -244 -602 -351 C ATOM 2770 C GLN A 370 -47.757 -51.364 -40.588 1.00 25.59 C ANISOU 2770 C GLN A 370 2694 3295 3732 -230 -512 -276 C ATOM 2771 O GLN A 370 -48.007 -51.397 -39.381 1.00 25.74 O ANISOU 2771 O GLN A 370 2682 3298 3800 -272 -456 -222 O ATOM 2772 CB GLN A 370 -50.026 -51.046 -41.579 1.00 27.64 C ANISOU 2772 CB GLN A 370 2812 3660 4029 -227 -614 -339 C ATOM 2773 CG GLN A 370 -51.017 -51.364 -42.676 1.00 29.84 C ANISOU 2773 CG GLN A 370 3030 3986 4322 -225 -711 -416 C ATOM 2774 CD GLN A 370 -52.284 -50.537 -42.544 1.00 32.78 C ANISOU 2774 CD GLN A 370 3310 4439 4708 -206 -719 -396 C ATOM 2775 OE1 GLN A 370 -53.041 -50.691 -41.584 1.00 34.65 O ANISOU 2775 OE1 GLN A 370 3471 4673 5024 -262 -683 -360 O ATOM 2776 NE2 GLN A 370 -52.516 -49.648 -43.502 1.00 33.57 N ANISOU 2776 NE2 GLN A 370 3415 4615 4727 -121 -761 -415 N ATOM 2777 N PHE A 371 -46.612 -50.896 -41.074 1.00 24.37 N ANISOU 2777 N PHE A 371 2622 3140 3498 -172 -499 -273 N ATOM 2778 CA PHE A 371 -45.542 -50.430 -40.212 1.00 23.02 C ANISOU 2778 CA PHE A 371 2504 2943 3298 -160 -424 -213 C ATOM 2779 C PHE A 371 -44.598 -49.557 -41.028 1.00 22.30 C ANISOU 2779 C PHE A 371 2481 2876 3116 -83 -419 -213 C ATOM 2780 O PHE A 371 -44.254 -49.908 -42.161 1.00 22.85 O ANISOU 2780 O PHE A 371 2585 2950 3149 -52 -465 -261 O ATOM 2781 CB PHE A 371 -44.780 -51.619 -39.616 1.00 23.03 C ANISOU 2781 CB PHE A 371 2538 2869 3345 -210 -404 -209 C ATOM 2782 CG PHE A 371 -43.726 -51.227 -38.634 1.00 22.41 C ANISOU 2782 CG PHE A 371 2504 2768 3241 -201 -334 -151 C ATOM 2783 CD1 PHE A 371 -44.061 -50.927 -37.322 1.00 23.50 C ANISOU 2783 CD1 PHE A 371 2611 2911 3408 -228 -279 -95 C ATOM 2784 CD2 PHE A 371 -42.397 -51.140 -39.018 1.00 21.28 C ANISOU 2784 CD2 PHE A 371 2433 2609 3044 -163 -322 -153 C ATOM 2785 CE1 PHE A 371 -43.087 -50.562 -36.411 1.00 23.78 C ANISOU 2785 CE1 PHE A 371 2687 2932 3416 -216 -222 -49 C ATOM 2786 CE2 PHE A 371 -41.428 -50.775 -38.115 1.00 21.92 C ANISOU 2786 CE2 PHE A 371 2547 2675 3106 -157 -264 -104 C ATOM 2787 CZ PHE A 371 -41.773 -50.476 -36.808 1.00 22.17 C ANISOU 2787 CZ PHE A 371 2548 2710 3163 -183 -218 -56 C ATOM 2788 N GLN A 372 -44.193 -48.429 -40.452 1.00 20.96 N ANISOU 2788 N GLN A 372 2330 2723 2913 -53 -362 -159 N ATOM 2789 CA GLN A 372 -43.287 -47.493 -41.117 1.00 20.16 C ANISOU 2789 CA GLN A 372 2287 2637 2735 14 -344 -146 C ATOM 2790 C GLN A 372 -41.852 -47.713 -40.663 1.00 19.13 C ANISOU 2790 C GLN A 372 2214 2460 2594 6 -300 -124 C ATOM 2791 O GLN A 372 -41.527 -47.530 -39.483 1.00 18.71 O ANISOU 2791 O GLN A 372 2159 2385 2564 -22 -251 -86 O ATOM 2792 CB GLN A 372 -43.704 -46.047 -40.815 1.00 19.82 C ANISOU 2792 CB GLN A 372 2229 2632 2668 53 -308 -104 C ATOM 2793 CG GLN A 372 -45.109 -45.705 -41.247 1.00 20.89 C ANISOU 2793 CG GLN A 372 2304 2823 2810 72 -349 -120 C ATOM 2794 CD GLN A 372 -45.295 -45.778 -42.751 1.00 21.36 C ANISOU 2794 CD GLN A 372 2375 2921 2820 124 -412 -163 C ATOM 2795 OE1 GLN A 372 -44.502 -45.213 -43.516 1.00 20.28 O ANISOU 2795 OE1 GLN A 372 2296 2791 2618 182 -401 -153 O ATOM 2796 NE2 GLN A 372 -46.340 -46.483 -43.188 1.00 19.73 N ANISOU 2796 NE2 GLN A 372 2112 2742 2644 104 -478 -211 N ATOM 2797 N TYR A 373 -40.986 -48.094 -41.602 1.00 18.79 N ANISOU 2797 N TYR A 373 2220 2407 2512 36 -317 -150 N ATOM 2798 CA TYR A 373 -39.573 -48.291 -41.312 1.00 18.49 C ANISOU 2798 CA TYR A 373 2232 2332 2461 37 -278 -131 C ATOM 2799 C TYR A 373 -38.838 -46.955 -41.325 1.00 18.27 C ANISOU 2799 C TYR A 373 2232 2322 2389 80 -229 -88 C ATOM 2800 O TYR A 373 -38.057 -46.656 -42.228 1.00 18.13 O ANISOU 2800 O TYR A 373 2254 2314 2322 127 -223 -88 O ATOM 2801 CB TYR A 373 -38.944 -49.279 -42.297 1.00 18.85 C ANISOU 2801 CB TYR A 373 2317 2360 2486 55 -312 -176 C ATOM 2802 CG TYR A 373 -39.529 -50.658 -42.154 1.00 18.39 C ANISOU 2802 CG TYR A 373 2236 2265 2485 4 -356 -219 C ATOM 2803 CD1 TYR A 373 -40.447 -51.146 -43.075 1.00 19.18 C ANISOU 2803 CD1 TYR A 373 2316 2383 2589 8 -423 -279 C ATOM 2804 CD2 TYR A 373 -39.192 -51.460 -41.069 1.00 18.71 C ANISOU 2804 CD2 TYR A 373 2275 2252 2581 -48 -330 -200 C ATOM 2805 CE1 TYR A 373 -41.004 -52.413 -42.933 1.00 20.58 C ANISOU 2805 CE1 TYR A 373 2470 2516 2833 -48 -463 -322 C ATOM 2806 CE2 TYR A 373 -39.740 -52.725 -40.917 1.00 19.05 C ANISOU 2806 CE2 TYR A 373 2299 2251 2688 -99 -363 -233 C ATOM 2807 CZ TYR A 373 -40.647 -53.194 -41.846 1.00 19.94 C ANISOU 2807 CZ TYR A 373 2390 2373 2814 -103 -429 -295 C ATOM 2808 OH TYR A 373 -41.198 -54.452 -41.699 1.00 21.49 O ANISOU 2808 OH TYR A 373 2564 2515 3085 -160 -463 -332 O ATOM 2809 N GLN A 374 -39.123 -46.158 -40.306 1.00 18.33 N ANISOU 2809 N GLN A 374 2216 2331 2416 63 -193 -52 N ATOM 2810 CA GLN A 374 -38.442 -44.893 -40.070 1.00 18.51 C ANISOU 2810 CA GLN A 374 2261 2356 2414 90 -143 -13 C ATOM 2811 C GLN A 374 -38.684 -44.521 -38.615 1.00 18.58 C ANISOU 2811 C GLN A 374 2246 2355 2459 54 -110 11 C ATOM 2812 O GLN A 374 -39.586 -45.066 -37.980 1.00 19.08 O ANISOU 2812 O GLN A 374 2271 2421 2557 20 -123 5 O ATOM 2813 CB GLN A 374 -38.970 -43.801 -41.004 1.00 19.22 C ANISOU 2813 CB GLN A 374 2355 2482 2466 147 -147 -5 C ATOM 2814 CG GLN A 374 -40.475 -43.558 -40.891 1.00 19.43 C ANISOU 2814 CG GLN A 374 2333 2542 2509 149 -174 -12 C ATOM 2815 CD GLN A 374 -40.968 -42.404 -41.750 1.00 22.54 C ANISOU 2815 CD GLN A 374 2731 2971 2860 215 -174 4 C ATOM 2816 OE1 GLN A 374 -40.838 -41.230 -41.379 1.00 22.19 O ANISOU 2816 OE1 GLN A 374 2699 2920 2814 236 -130 41 O ATOM 2817 NE2 GLN A 374 -41.558 -42.731 -42.893 1.00 21.96 N ANISOU 2817 NE2 GLN A 374 2651 2936 2756 251 -226 -24 N ATOM 2818 N ASN A 375 -37.879 -43.604 -38.092 1.00 18.43 N ANISOU 2818 N ASN A 375 2248 2324 2432 61 -67 37 N ATOM 2819 CA ASN A 375 -38.024 -43.141 -36.715 1.00 18.40 C ANISOU 2819 CA ASN A 375 2228 2313 2449 36 -36 54 C ATOM 2820 C ASN A 375 -37.418 -41.757 -36.562 1.00 17.68 C ANISOU 2820 C ASN A 375 2159 2212 2345 59 2 72 C ATOM 2821 O ASN A 375 -36.430 -41.432 -37.216 1.00 17.56 O ANISOU 2821 O ASN A 375 2174 2184 2314 76 14 78 O ATOM 2822 CB ASN A 375 -37.352 -44.114 -35.730 1.00 18.72 C ANISOU 2822 CB ASN A 375 2270 2332 2509 -5 -30 55 C ATOM 2823 CG ASN A 375 -37.693 -43.808 -34.271 1.00 19.40 C ANISOU 2823 CG ASN A 375 2337 2423 2610 -26 -3 70 C ATOM 2824 OD1 ASN A 375 -38.857 -43.727 -33.903 1.00 21.53 O ANISOU 2824 OD1 ASN A 375 2575 2712 2894 -31 -4 73 O ATOM 2825 ND2 ASN A 375 -36.668 -43.630 -33.445 1.00 22.73 N ANISOU 2825 ND2 ASN A 375 2777 2832 3026 -35 19 77 N ATOM 2826 N ARG A 376 -38.038 -40.941 -35.717 1.00 17.15 N ANISOU 2826 N ARG A 376 2078 2151 2288 60 22 80 N ATOM 2827 CA ARG A 376 -37.474 -39.650 -35.307 1.00 16.24 C ANISOU 2827 CA ARG A 376 1984 2015 2172 73 59 90 C ATOM 2828 C ARG A 376 -37.478 -39.662 -33.779 1.00 15.94 C ANISOU 2828 C ARG A 376 1935 1976 2147 45 74 84 C ATOM 2829 O ARG A 376 -38.492 -40.003 -33.166 1.00 16.17 O ANISOU 2829 O ARG A 376 1934 2027 2182 39 70 84 O ATOM 2830 CB ARG A 376 -38.322 -38.497 -35.861 1.00 16.28 C ANISOU 2830 CB ARG A 376 1990 2027 2170 119 68 101 C ATOM 2831 CG ARG A 376 -37.655 -37.124 -35.848 1.00 15.91 C ANISOU 2831 CG ARG A 376 1974 1945 2128 137 106 113 C ATOM 2832 CD ARG A 376 -36.612 -36.959 -36.962 1.00 16.04 C ANISOU 2832 CD ARG A 376 2020 1941 2133 151 116 130 C ATOM 2833 NE ARG A 376 -37.170 -37.046 -38.315 1.00 15.62 N ANISOU 2833 NE ARG A 376 1971 1914 2051 197 99 144 N ATOM 2834 CZ ARG A 376 -37.825 -36.070 -38.952 1.00 15.35 C ANISOU 2834 CZ ARG A 376 1945 1882 2003 249 110 167 C ATOM 2835 NH1 ARG A 376 -38.054 -34.893 -38.372 1.00 14.63 N ANISOU 2835 NH1 ARG A 376 1863 1763 1934 260 142 177 N ATOM 2836 NH2 ARG A 376 -38.276 -36.281 -40.184 1.00 16.03 N ANISOU 2836 NH2 ARG A 376 2036 2002 2054 294 87 177 N ATOM 2837 N ILE A 377 -36.344 -39.329 -33.168 1.00 15.99 N ANISOU 2837 N ILE A 377 1960 1960 2156 30 92 78 N ATOM 2838 CA ILE A 377 -36.180 -39.415 -31.721 1.00 15.82 C ANISOU 2838 CA ILE A 377 1932 1943 2134 8 101 69 C ATOM 2839 C ILE A 377 -36.961 -38.296 -31.029 1.00 16.11 C ANISOU 2839 C ILE A 377 1967 1983 2170 29 122 62 C ATOM 2840 O ILE A 377 -36.819 -37.113 -31.369 1.00 16.37 O ANISOU 2840 O ILE A 377 2019 1991 2210 50 138 58 O ATOM 2841 CB ILE A 377 -34.693 -39.355 -31.304 1.00 15.75 C ANISOU 2841 CB ILE A 377 1941 1916 2127 -11 105 58 C ATOM 2842 CG1 ILE A 377 -33.927 -40.548 -31.898 1.00 14.71 C ANISOU 2842 CG1 ILE A 377 1810 1785 1995 -25 87 66 C ATOM 2843 CG2 ILE A 377 -34.551 -39.324 -29.776 1.00 15.62 C ANISOU 2843 CG2 ILE A 377 1921 1914 2102 -23 110 43 C ATOM 2844 CD1 ILE A 377 -34.277 -41.911 -31.295 1.00 15.70 C ANISOU 2844 CD1 ILE A 377 1921 1928 2117 -42 72 72 C ATOM 2845 N ALA A 378 -37.789 -38.684 -30.062 1.00 16.11 N ANISOU 2845 N ALA A 378 1946 2013 2164 26 126 63 N ATOM 2846 CA ALA A 378 -38.623 -37.730 -29.338 1.00 16.41 C ANISOU 2846 CA ALA A 378 1979 2061 2196 53 149 55 C ATOM 2847 C ALA A 378 -37.915 -37.157 -28.114 1.00 16.30 C ANISOU 2847 C ALA A 378 1987 2039 2169 50 163 29 C ATOM 2848 O ALA A 378 -37.249 -37.882 -27.369 1.00 16.43 O ANISOU 2848 O ALA A 378 2004 2068 2172 28 155 26 O ATOM 2849 CB ALA A 378 -39.929 -38.378 -28.924 1.00 16.83 C ANISOU 2849 CB ALA A 378 1992 2155 2248 57 152 72 C ATOM 2850 N SER A 379 -38.098 -35.855 -27.896 1.00 16.48 N ANISOU 2850 N SER A 379 2026 2041 2193 77 181 9 N ATOM 2851 CA SER A 379 -37.556 -35.172 -26.731 1.00 17.05 C ANISOU 2851 CA SER A 379 2120 2105 2252 79 189 -28 C ATOM 2852 C SER A 379 -37.999 -35.844 -25.429 1.00 17.10 C ANISOU 2852 C SER A 379 2111 2163 2222 84 195 -29 C ATOM 2853 O SER A 379 -37.215 -35.990 -24.496 1.00 17.23 O ANISOU 2853 O SER A 379 2140 2189 2216 73 187 -51 O ATOM 2854 CB SER A 379 -38.009 -33.711 -26.734 1.00 17.40 C ANISOU 2854 CB SER A 379 2185 2117 2308 115 211 -50 C ATOM 2855 OG SER A 379 -37.526 -33.027 -25.602 1.00 19.58 O ANISOU 2855 OG SER A 379 2485 2383 2572 119 215 -97 O ATOM 2856 N GLU A 380 -39.260 -36.251 -25.374 1.00 17.31 N ANISOU 2856 N GLU A 380 2110 2225 2244 101 210 -1 N ATOM 2857 CA GLU A 380 -39.811 -36.851 -24.160 1.00 17.76 C ANISOU 2857 CA GLU A 380 2149 2331 2267 110 227 11 C ATOM 2858 C GLU A 380 -39.201 -38.233 -23.876 1.00 17.47 C ANISOU 2858 C GLU A 380 2103 2311 2222 76 213 35 C ATOM 2859 O GLU A 380 -39.116 -38.655 -22.719 1.00 17.52 O ANISOU 2859 O GLU A 380 2111 2352 2193 83 224 40 O ATOM 2860 CB GLU A 380 -41.332 -36.945 -24.256 1.00 18.05 C ANISOU 2860 CB GLU A 380 2146 2401 2311 134 250 40 C ATOM 2861 CG GLU A 380 -42.015 -35.596 -24.468 1.00 18.45 C ANISOU 2861 CG GLU A 380 2204 2439 2366 180 267 20 C ATOM 2862 CD GLU A 380 -42.425 -35.337 -25.915 1.00 18.40 C ANISOU 2862 CD GLU A 380 2186 2410 2397 185 253 35 C ATOM 2863 OE1 GLU A 380 -41.771 -35.887 -26.836 1.00 18.52 O ANISOU 2863 OE1 GLU A 380 2205 2403 2430 152 226 45 O ATOM 2864 OE2 GLU A 380 -43.401 -34.572 -26.125 1.00 17.71 O ANISOU 2864 OE2 GLU A 380 2085 2331 2315 228 270 38 O ATOM 2865 N PHE A 381 -38.798 -38.931 -24.935 1.00 17.08 N ANISOU 2865 N PHE A 381 2048 2239 2203 45 189 52 N ATOM 2866 CA PHE A 381 -38.080 -40.202 -24.808 1.00 17.33 C ANISOU 2866 CA PHE A 381 2078 2273 2233 15 174 72 C ATOM 2867 C PHE A 381 -36.711 -39.952 -24.179 1.00 17.68 C ANISOU 2867 C PHE A 381 2152 2313 2254 12 161 43 C ATOM 2868 O PHE A 381 -36.302 -40.664 -23.266 1.00 17.68 O ANISOU 2868 O PHE A 381 2153 2338 2225 11 160 54 O ATOM 2869 CB PHE A 381 -37.968 -40.875 -26.179 1.00 17.09 C ANISOU 2869 CB PHE A 381 2038 2216 2238 -9 151 86 C ATOM 2870 CG PHE A 381 -37.419 -42.283 -26.152 1.00 18.13 C ANISOU 2870 CG PHE A 381 2168 2345 2375 -36 138 108 C ATOM 2871 CD1 PHE A 381 -37.785 -43.191 -25.167 1.00 18.68 C ANISOU 2871 CD1 PHE A 381 2225 2439 2435 -41 154 139 C ATOM 2872 CD2 PHE A 381 -36.554 -42.710 -27.152 1.00 18.72 C ANISOU 2872 CD2 PHE A 381 2255 2391 2467 -51 113 103 C ATOM 2873 CE1 PHE A 381 -37.290 -44.488 -25.177 1.00 18.56 C ANISOU 2873 CE1 PHE A 381 2212 2411 2430 -63 144 163 C ATOM 2874 CE2 PHE A 381 -36.053 -44.015 -27.162 1.00 18.58 C ANISOU 2874 CE2 PHE A 381 2239 2364 2456 -70 102 122 C ATOM 2875 CZ PHE A 381 -36.427 -44.897 -26.178 1.00 18.16 C ANISOU 2875 CZ PHE A 381 2175 2328 2398 -76 116 152 C ATOM 2876 N ASN A 382 -36.022 -38.913 -24.645 1.00 17.57 N ANISOU 2876 N ASN A 382 2157 2267 2252 13 150 7 N ATOM 2877 CA ASN A 382 -34.793 -38.466 -24.005 1.00 18.42 C ANISOU 2877 CA ASN A 382 2283 2369 2345 8 135 -30 C ATOM 2878 C ASN A 382 -35.025 -38.188 -22.518 1.00 18.53 C ANISOU 2878 C ASN A 382 2306 2424 2312 34 144 -52 C ATOM 2879 O ASN A 382 -34.354 -38.752 -21.664 1.00 18.82 O ANISOU 2879 O ASN A 382 2346 2491 2315 35 131 -55 O ATOM 2880 CB ASN A 382 -34.246 -37.217 -24.706 1.00 18.95 C ANISOU 2880 CB ASN A 382 2366 2389 2445 2 132 -63 C ATOM 2881 CG ASN A 382 -32.810 -36.903 -24.322 1.00 21.61 C ANISOU 2881 CG ASN A 382 2711 2715 2785 -17 110 -100 C ATOM 2882 OD1 ASN A 382 -32.313 -37.345 -23.289 1.00 26.43 O ANISOU 2882 OD1 ASN A 382 3320 3360 3361 -15 94 -114 O ATOM 2883 ND2 ASN A 382 -32.131 -36.143 -25.168 1.00 25.16 N ANISOU 2883 ND2 ASN A 382 3166 3117 3277 -34 109 -113 N ATOM 2884 N THR A 383 -36.014 -37.357 -22.216 1.00 18.86 N ANISOU 2884 N THR A 383 2352 2470 2345 63 168 -65 N ATOM 2885 CA THR A 383 -36.293 -36.964 -20.838 1.00 19.48 C ANISOU 2885 CA THR A 383 2442 2588 2371 98 180 -91 C ATOM 2886 C THR A 383 -36.580 -38.156 -19.928 1.00 19.60 C ANISOU 2886 C THR A 383 2444 2660 2341 109 192 -50 C ATOM 2887 O THR A 383 -35.985 -38.274 -18.852 1.00 20.06 O ANISOU 2887 O THR A 383 2518 2755 2350 126 181 -69 O ATOM 2888 CB THR A 383 -37.459 -35.969 -20.779 1.00 19.87 C ANISOU 2888 CB THR A 383 2495 2634 2422 135 210 -104 C ATOM 2889 OG1 THR A 383 -37.083 -34.775 -21.475 1.00 20.63 O ANISOU 2889 OG1 THR A 383 2611 2671 2557 130 201 -144 O ATOM 2890 CG2 THR A 383 -37.809 -35.624 -19.333 1.00 20.71 C ANISOU 2890 CG2 THR A 383 2615 2787 2465 180 226 -132 C ATOM 2891 N LEU A 384 -37.462 -39.052 -20.368 1.00 19.34 N ANISOU 2891 N LEU A 384 2383 2636 2328 100 212 8 N ATOM 2892 CA LEU A 384 -37.859 -40.184 -19.528 1.00 19.55 C ANISOU 2892 CA LEU A 384 2396 2709 2323 108 235 59 C ATOM 2893 C LEU A 384 -36.711 -41.153 -19.270 1.00 19.19 C ANISOU 2893 C LEU A 384 2361 2668 2264 92 210 73 C ATOM 2894 O LEU A 384 -36.717 -41.852 -18.258 1.00 19.46 O ANISOU 2894 O LEU A 384 2397 2744 2252 112 225 105 O ATOM 2895 CB LEU A 384 -39.074 -40.918 -20.109 1.00 19.65 C ANISOU 2895 CB LEU A 384 2370 2721 2376 93 261 115 C ATOM 2896 CG LEU A 384 -38.925 -41.785 -21.360 1.00 19.69 C ANISOU 2896 CG LEU A 384 2359 2685 2439 48 239 139 C ATOM 2897 CD1 LEU A 384 -38.324 -43.175 -21.033 1.00 19.95 C ANISOU 2897 CD1 LEU A 384 2393 2719 2468 28 234 179 C ATOM 2898 CD2 LEU A 384 -40.282 -41.944 -22.044 1.00 20.80 C ANISOU 2898 CD2 LEU A 384 2457 2824 2622 39 256 166 C ATOM 2899 N TYR A 385 -35.715 -41.164 -20.163 1.00 18.61 N ANISOU 2899 N TYR A 385 2293 2553 2224 61 175 53 N ATOM 2900 CA TYR A 385 -34.564 -42.069 -20.051 1.00 18.37 C ANISOU 2900 CA TYR A 385 2269 2525 2186 49 149 66 C ATOM 2901 C TYR A 385 -33.428 -41.528 -19.155 1.00 18.95 C ANISOU 2901 C TYR A 385 2361 2625 2213 68 121 17 C ATOM 2902 O TYR A 385 -32.346 -42.125 -19.095 1.00 18.59 O ANISOU 2902 O TYR A 385 2316 2585 2162 61 94 20 O ATOM 2903 CB TYR A 385 -34.004 -42.372 -21.446 1.00 17.93 C ANISOU 2903 CB TYR A 385 2208 2420 2187 13 128 68 C ATOM 2904 CG TYR A 385 -33.893 -43.842 -21.796 1.00 17.28 C ANISOU 2904 CG TYR A 385 2117 2326 2123 -4 127 118 C ATOM 2905 CD1 TYR A 385 -34.505 -44.345 -22.935 1.00 16.85 C ANISOU 2905 CD1 TYR A 385 2050 2236 2117 -28 130 139 C ATOM 2906 CD2 TYR A 385 -33.172 -44.730 -20.999 1.00 17.32 C ANISOU 2906 CD2 TYR A 385 2130 2355 2096 9 120 142 C ATOM 2907 CE1 TYR A 385 -34.401 -45.688 -23.279 1.00 17.35 C ANISOU 2907 CE1 TYR A 385 2110 2280 2204 -44 126 177 C ATOM 2908 CE2 TYR A 385 -33.060 -46.073 -21.343 1.00 17.40 C ANISOU 2908 CE2 TYR A 385 2138 2343 2129 -3 122 188 C ATOM 2909 CZ TYR A 385 -33.685 -46.544 -22.483 1.00 17.40 C ANISOU 2909 CZ TYR A 385 2126 2300 2184 -32 125 203 C ATOM 2910 OH TYR A 385 -33.586 -47.873 -22.842 1.00 18.64 O ANISOU 2910 OH TYR A 385 2284 2428 2369 -45 124 240 O ATOM 2911 N HIS A 386 -33.654 -40.409 -18.463 1.00 19.58 N ANISOU 2911 N HIS A 386 2454 2723 2261 93 124 -31 N ATOM 2912 CA HIS A 386 -32.673 -39.915 -17.484 1.00 20.48 C ANISOU 2912 CA HIS A 386 2584 2870 2327 113 91 -87 C ATOM 2913 C HIS A 386 -32.771 -40.744 -16.198 1.00 20.93 C ANISOU 2913 C HIS A 386 2648 2996 2308 156 102 -53 C ATOM 2914 O HIS A 386 -33.309 -40.290 -15.185 1.00 21.30 O ANISOU 2914 O HIS A 386 2710 3087 2296 199 118 -71 O ATOM 2915 CB HIS A 386 -32.869 -38.422 -17.203 1.00 21.21 C ANISOU 2915 CB HIS A 386 2693 2950 2415 127 88 -159 C ATOM 2916 CG HIS A 386 -32.473 -37.543 -18.346 1.00 23.04 C ANISOU 2916 CG HIS A 386 2922 3112 2719 88 75 -192 C ATOM 2917 ND1 HIS A 386 -31.687 -36.420 -18.194 1.00 27.94 N ANISOU 2917 ND1 HIS A 386 3554 3708 3355 78 46 -267 N ATOM 2918 CD2 HIS A 386 -32.732 -37.643 -19.668 1.00 24.55 C ANISOU 2918 CD2 HIS A 386 3101 3254 2972 58 88 -159 C ATOM 2919 CE1 HIS A 386 -31.494 -35.858 -19.377 1.00 26.53 C ANISOU 2919 CE1 HIS A 386 3370 3464 3248 43 49 -270 C ATOM 2920 NE2 HIS A 386 -32.120 -36.581 -20.288 1.00 25.65 N ANISOU 2920 NE2 HIS A 386 3247 3342 3159 35 74 -205 N ATOM 2921 N TRP A 387 -32.232 -41.962 -16.253 1.00 20.72 N ANISOU 2921 N TRP A 387 2614 2978 2281 149 94 -2 N ATOM 2922 CA TRP A 387 -32.407 -42.946 -15.187 1.00 21.48 C ANISOU 2922 CA TRP A 387 2718 3131 2312 190 114 53 C ATOM 2923 C TRP A 387 -31.282 -42.872 -14.155 1.00 22.67 C ANISOU 2923 C TRP A 387 2882 3339 2393 227 72 16 C ATOM 2924 O TRP A 387 -30.698 -43.887 -13.776 1.00 22.70 O ANISOU 2924 O TRP A 387 2886 3369 2368 245 64 60 O ATOM 2925 CB TRP A 387 -32.485 -44.357 -15.779 1.00 21.26 C ANISOU 2925 CB TRP A 387 2678 3074 2325 167 132 132 C ATOM 2926 CG TRP A 387 -33.707 -44.631 -16.614 1.00 19.64 C ANISOU 2926 CG TRP A 387 2455 2826 2180 136 171 173 C ATOM 2927 CD1 TRP A 387 -34.825 -43.850 -16.730 1.00 20.06 C ANISOU 2927 CD1 TRP A 387 2500 2878 2245 136 199 160 C ATOM 2928 CD2 TRP A 387 -33.949 -45.796 -17.409 1.00 19.88 C ANISOU 2928 CD2 TRP A 387 2473 2813 2268 104 184 231 C ATOM 2929 NE1 TRP A 387 -35.736 -44.452 -17.566 1.00 19.42 N ANISOU 2929 NE1 TRP A 387 2395 2759 2224 104 225 206 N ATOM 2930 CE2 TRP A 387 -35.227 -45.648 -17.994 1.00 19.53 C ANISOU 2930 CE2 TRP A 387 2408 2746 2269 81 215 246 C ATOM 2931 CE3 TRP A 387 -33.209 -46.949 -17.688 1.00 19.60 C ANISOU 2931 CE3 TRP A 387 2441 2756 2251 94 170 267 C ATOM 2932 CZ2 TRP A 387 -35.778 -46.610 -18.848 1.00 19.71 C ANISOU 2932 CZ2 TRP A 387 2411 2722 2355 44 227 290 C ATOM 2933 CZ3 TRP A 387 -33.760 -47.912 -18.539 1.00 19.49 C ANISOU 2933 CZ3 TRP A 387 2414 2689 2300 59 187 312 C ATOM 2934 CH2 TRP A 387 -35.029 -47.733 -19.106 1.00 19.35 C ANISOU 2934 CH2 TRP A 387 2374 2649 2328 32 212 320 C ATOM 2935 N HIS A 388 -31.019 -41.669 -13.659 1.00 23.61 N ANISOU 2935 N HIS A 388 3011 3477 2482 242 45 -67 N ATOM 2936 CA HIS A 388 -29.886 -41.458 -12.760 1.00 24.78 C ANISOU 2936 CA HIS A 388 3167 3680 2570 271 -8 -121 C ATOM 2937 C HIS A 388 -29.986 -42.181 -11.405 1.00 24.92 C ANISOU 2937 C HIS A 388 3203 3783 2482 341 2 -81 C ATOM 2938 O HIS A 388 -28.951 -42.448 -10.787 1.00 25.49 O ANISOU 2938 O HIS A 388 3275 3905 2505 369 -44 -101 O ATOM 2939 CB HIS A 388 -29.615 -39.959 -12.590 1.00 25.82 C ANISOU 2939 CB HIS A 388 3306 3801 2704 265 -43 -228 C ATOM 2940 CG HIS A 388 -29.144 -39.305 -13.851 1.00 28.28 C ANISOU 2940 CG HIS A 388 3598 4032 3115 199 -61 -264 C ATOM 2941 ND1 HIS A 388 -29.848 -38.301 -14.480 1.00 32.00 N ANISOU 2941 ND1 HIS A 388 4075 4444 3637 177 -38 -293 N ATOM 2942 CD2 HIS A 388 -28.065 -39.554 -14.633 1.00 30.26 C ANISOU 2942 CD2 HIS A 388 3822 4252 3422 157 -92 -266 C ATOM 2943 CE1 HIS A 388 -29.213 -37.946 -15.584 1.00 31.99 C ANISOU 2943 CE1 HIS A 388 4056 4380 3718 123 -54 -308 C ATOM 2944 NE2 HIS A 388 -28.127 -38.690 -15.700 1.00 31.37 N ANISOU 2944 NE2 HIS A 388 3957 4318 3645 109 -85 -294 N ATOM 2945 N PRO A 389 -31.208 -42.536 -10.953 1.00 24.52 N ANISOU 2945 N PRO A 389 3165 3755 2398 373 65 -20 N ATOM 2946 CA PRO A 389 -31.263 -43.347 -9.737 1.00 25.05 C ANISOU 2946 CA PRO A 389 3249 3901 2367 441 84 36 C ATOM 2947 C PRO A 389 -30.602 -44.722 -9.837 1.00 24.49 C ANISOU 2947 C PRO A 389 3172 3832 2303 443 80 114 C ATOM 2948 O PRO A 389 -30.282 -45.303 -8.807 1.00 25.14 O ANISOU 2948 O PRO A 389 3271 3983 2298 505 78 149 O ATOM 2949 CB PRO A 389 -32.766 -43.496 -9.483 1.00 25.01 C ANISOU 2949 CB PRO A 389 3248 3903 2351 461 163 99 C ATOM 2950 CG PRO A 389 -33.369 -42.291 -10.097 1.00 25.29 C ANISOU 2950 CG PRO A 389 3278 3894 2437 430 166 33 C ATOM 2951 CD PRO A 389 -32.549 -42.048 -11.332 1.00 24.32 C ANISOU 2951 CD PRO A 389 3136 3696 2406 361 118 -8 C ATOM 2952 N LEU A 390 -30.409 -45.244 -11.051 1.00 23.35 N ANISOU 2952 N LEU A 390 3007 3612 2255 382 79 142 N ATOM 2953 CA LEU A 390 -29.663 -46.498 -11.232 1.00 22.99 C ANISOU 2953 CA LEU A 390 2957 3557 2222 384 70 205 C ATOM 2954 C LEU A 390 -28.281 -46.438 -10.583 1.00 23.40 C ANISOU 2954 C LEU A 390 3010 3669 2212 423 4 161 C ATOM 2955 O LEU A 390 -27.772 -47.450 -10.106 1.00 23.48 O ANISOU 2955 O LEU A 390 3027 3712 2183 465 2 220 O ATOM 2956 CB LEU A 390 -29.476 -46.816 -12.718 1.00 21.96 C ANISOU 2956 CB LEU A 390 2805 3338 2200 314 65 212 C ATOM 2957 CG LEU A 390 -30.683 -47.266 -13.536 1.00 21.55 C ANISOU 2957 CG LEU A 390 2746 3222 2221 272 120 267 C ATOM 2958 CD1 LEU A 390 -30.285 -47.346 -15.005 1.00 20.77 C ANISOU 2958 CD1 LEU A 390 2630 3048 2214 213 98 248 C ATOM 2959 CD2 LEU A 390 -31.210 -48.615 -13.064 1.00 20.77 C ANISOU 2959 CD2 LEU A 390 2657 3126 2109 296 170 371 C ATOM 2960 N LEU A 391 -27.682 -45.248 -10.579 1.00 23.43 N ANISOU 2960 N LEU A 391 3003 3685 2213 410 -50 57 N ATOM 2961 CA LEU A 391 -26.298 -45.077 -10.153 1.00 24.07 C ANISOU 2961 CA LEU A 391 3072 3817 2258 432 -123 0 C ATOM 2962 C LEU A 391 -26.122 -45.364 -8.668 1.00 25.03 C ANISOU 2962 C LEU A 391 3215 4042 2253 520 -137 11 C ATOM 2963 O LEU A 391 -26.928 -44.914 -7.845 1.00 25.39 O ANISOU 2963 O LEU A 391 3287 4129 2229 560 -111 0 O ATOM 2964 CB LEU A 391 -25.819 -43.658 -10.464 1.00 24.13 C ANISOU 2964 CB LEU A 391 3060 3805 2302 390 -173 -117 C ATOM 2965 CG LEU A 391 -25.806 -43.287 -11.948 1.00 23.90 C ANISOU 2965 CG LEU A 391 3009 3680 2392 309 -164 -130 C ATOM 2966 CD1 LEU A 391 -25.429 -41.826 -12.116 1.00 24.70 C ANISOU 2966 CD1 LEU A 391 3098 3759 2527 273 -203 -239 C ATOM 2967 CD2 LEU A 391 -24.856 -44.198 -12.725 1.00 24.42 C ANISOU 2967 CD2 LEU A 391 3047 3721 2509 288 -180 -89 C ATOM 2968 N PRO A 392 -25.067 -46.120 -8.318 1.00 25.43 N ANISOU 2968 N PRO A 392 3256 4138 2267 557 -176 33 N ATOM 2969 CA PRO A 392 -24.782 -46.443 -6.927 1.00 26.67 C ANISOU 2969 CA PRO A 392 3435 4403 2296 651 -196 47 C ATOM 2970 C PRO A 392 -24.120 -45.271 -6.207 1.00 27.67 C ANISOU 2970 C PRO A 392 3553 4597 2362 672 -274 -80 C ATOM 2971 O PRO A 392 -23.787 -44.267 -6.842 1.00 27.01 O ANISOU 2971 O PRO A 392 3444 4468 2350 607 -312 -172 O ATOM 2972 CB PRO A 392 -23.803 -47.609 -7.050 1.00 26.80 C ANISOU 2972 CB PRO A 392 3436 4430 2316 675 -217 110 C ATOM 2973 CG PRO A 392 -23.036 -47.301 -8.290 1.00 26.00 C ANISOU 2973 CG PRO A 392 3293 4260 2328 596 -253 60 C ATOM 2974 CD PRO A 392 -24.011 -46.626 -9.218 1.00 25.06 C ANISOU 2974 CD PRO A 392 3175 4052 2295 520 -209 40 C ATOM 2975 N ASP A 393 -23.934 -45.407 -4.896 1.00 29.14 N ANISOU 2975 N ASP A 393 3762 4891 2418 763 -298 -83 N ATOM 2976 CA ASP A 393 -23.201 -44.418 -4.096 1.00 30.56 C ANISOU 2976 CA ASP A 393 3935 5149 2529 793 -385 -209 C ATOM 2977 C ASP A 393 -21.709 -44.455 -4.424 1.00 30.38 C ANISOU 2977 C ASP A 393 3858 5138 2546 769 -471 -262 C ATOM 2978 O ASP A 393 -21.050 -43.415 -4.450 1.00 30.59 O ANISOU 2978 O ASP A 393 3855 5169 2598 733 -542 -384 O ATOM 2979 CB ASP A 393 -23.389 -44.677 -2.598 1.00 32.13 C ANISOU 2979 CB ASP A 393 4173 5470 2564 910 -388 -191 C ATOM 2980 CG ASP A 393 -24.794 -44.364 -2.112 1.00 33.76 C ANISOU 2980 CG ASP A 393 4426 5682 2718 940 -311 -166 C ATOM 2981 OD1 ASP A 393 -25.151 -44.853 -1.016 1.00 37.94 O ANISOU 2981 OD1 ASP A 393 4994 6302 3120 1038 -282 -109 O ATOM 2982 OD2 ASP A 393 -25.525 -43.625 -2.806 1.00 35.23 O ANISOU 2982 OD2 ASP A 393 4611 5787 2986 873 -278 -200 O ATOM 2983 N THR A 394 -21.188 -45.663 -4.642 1.00 30.26 N ANISOU 2983 N THR A 394 3830 5129 2538 791 -462 -168 N ATOM 2984 CA THR A 394 -19.802 -45.880 -5.064 1.00 30.13 C ANISOU 2984 CA THR A 394 3758 5122 2569 773 -531 -197 C ATOM 2985 C THR A 394 -19.760 -46.948 -6.146 1.00 29.38 C ANISOU 2985 C THR A 394 3652 4945 2565 738 -479 -93 C ATOM 2986 O THR A 394 -20.693 -47.746 -6.274 1.00 28.97 O ANISOU 2986 O THR A 394 3640 4853 2513 750 -399 11 O ATOM 2987 CB THR A 394 -18.903 -46.346 -3.896 1.00 31.61 C ANISOU 2987 CB THR A 394 3938 5438 2632 874 -599 -200 C ATOM 2988 OG1 THR A 394 -19.379 -47.601 -3.383 1.00 32.15 O ANISOU 2988 OG1 THR A 394 4051 5537 2626 955 -538 -66 O ATOM 2989 CG2 THR A 394 -18.876 -45.309 -2.780 1.00 31.99 C ANISOU 2989 CG2 THR A 394 3998 5577 2579 916 -661 -315 C ATOM 2990 N PHE A 395 -18.680 -46.955 -6.924 1.00 28.92 N ANISOU 2990 N PHE A 395 3538 4862 2586 694 -523 -123 N ATOM 2991 CA PHE A 395 -18.488 -47.942 -7.987 1.00 28.31 C ANISOU 2991 CA PHE A 395 3450 4712 2595 666 -482 -38 C ATOM 2992 C PHE A 395 -17.491 -48.993 -7.522 1.00 29.35 C ANISOU 2992 C PHE A 395 3565 4912 2673 744 -516 15 C ATOM 2993 O PHE A 395 -16.314 -48.702 -7.304 1.00 29.51 O ANISOU 2993 O PHE A 395 3532 4995 2683 757 -594 -49 O ATOM 2994 CB PHE A 395 -18.037 -47.254 -9.273 1.00 27.33 C ANISOU 2994 CB PHE A 395 3278 4508 2597 569 -494 -98 C ATOM 2995 CG PHE A 395 -19.027 -46.251 -9.783 1.00 26.45 C ANISOU 2995 CG PHE A 395 3186 4324 2539 499 -458 -141 C ATOM 2996 CD1 PHE A 395 -18.981 -44.929 -9.354 1.00 26.43 C ANISOU 2996 CD1 PHE A 395 3173 4345 2525 476 -502 -251 C ATOM 2997 CD2 PHE A 395 -20.031 -46.633 -10.664 1.00 24.54 C ANISOU 2997 CD2 PHE A 395 2973 3993 2358 461 -381 -74 C ATOM 2998 CE1 PHE A 395 -19.903 -44.004 -9.814 1.00 25.80 C ANISOU 2998 CE1 PHE A 395 3113 4195 2493 420 -465 -287 C ATOM 2999 CE2 PHE A 395 -20.952 -45.718 -11.124 1.00 24.74 C ANISOU 2999 CE2 PHE A 395 3013 3958 2427 405 -349 -110 C ATOM 3000 CZ PHE A 395 -20.887 -44.396 -10.696 1.00 25.02 C ANISOU 3000 CZ PHE A 395 3041 4014 2450 387 -389 -214 C ATOM 3001 N ASN A 396 -17.985 -50.217 -7.356 1.00 29.93 N ANISOU 3001 N ASN A 396 3683 4972 2717 796 -456 134 N ATOM 3002 CA ASN A 396 -17.255 -51.259 -6.643 1.00 31.16 C ANISOU 3002 CA ASN A 396 3841 5202 2797 894 -478 201 C ATOM 3003 C ASN A 396 -16.582 -52.232 -7.599 1.00 31.10 C ANISOU 3003 C ASN A 396 3811 5135 2872 884 -465 261 C ATOM 3004 O ASN A 396 -17.237 -53.099 -8.169 1.00 30.91 O ANISOU 3004 O ASN A 396 3824 5025 2896 872 -392 350 O ATOM 3005 CB ASN A 396 -18.205 -52.012 -5.709 1.00 31.85 C ANISOU 3005 CB ASN A 396 3996 5315 2791 970 -416 303 C ATOM 3006 CG ASN A 396 -18.927 -51.092 -4.743 1.00 33.56 C ANISOU 3006 CG ASN A 396 4239 5595 2917 990 -421 249 C ATOM 3007 OD1 ASN A 396 -18.512 -49.952 -4.516 1.00 35.07 O ANISOU 3007 OD1 ASN A 396 4400 5833 3092 969 -489 128 O ATOM 3008 ND2 ASN A 396 -20.015 -51.585 -4.163 1.00 35.17 N ANISOU 3008 ND2 ASN A 396 4499 5799 3064 1033 -345 338 N ATOM 3009 N ILE A 397 -15.274 -52.078 -7.777 1.00 31.74 N ANISOU 3009 N ILE A 397 3828 5261 2970 890 -536 207 N ATOM 3010 CA ILE A 397 -14.521 -52.911 -8.710 1.00 31.75 C ANISOU 3010 CA ILE A 397 3802 5214 3048 886 -528 252 C ATOM 3011 C ILE A 397 -13.462 -53.677 -7.944 1.00 33.40 C ANISOU 3011 C ILE A 397 3990 5519 3181 992 -577 288 C ATOM 3012 O ILE A 397 -12.619 -53.076 -7.267 1.00 33.52 O ANISOU 3012 O ILE A 397 3955 5639 3141 1021 -660 212 O ATOM 3013 CB ILE A 397 -13.874 -52.075 -9.830 1.00 31.21 C ANISOU 3013 CB ILE A 397 3667 5103 3088 795 -556 165 C ATOM 3014 CG1 ILE A 397 -14.950 -51.280 -10.574 1.00 30.59 C ANISOU 3014 CG1 ILE A 397 3613 4932 3078 699 -508 133 C ATOM 3015 CG2 ILE A 397 -13.122 -52.981 -10.803 1.00 30.44 C ANISOU 3015 CG2 ILE A 397 3544 4960 3063 800 -540 215 C ATOM 3016 CD1 ILE A 397 -14.411 -50.299 -11.586 1.00 31.21 C ANISOU 3016 CD1 ILE A 397 3632 4972 3255 610 -530 49 C ATOM 3017 N GLU A 398 -13.518 -55.005 -8.048 1.00 34.23 N ANISOU 3017 N GLU A 398 4132 5587 3285 1050 -528 401 N ATOM 3018 CA GLU A 398 -12.633 -55.882 -7.294 1.00 36.34 C ANISOU 3018 CA GLU A 398 4392 5939 3475 1165 -563 457 C ATOM 3019 C GLU A 398 -12.793 -55.543 -5.799 1.00 37.70 C ANISOU 3019 C GLU A 398 4585 6234 3506 1242 -603 445 C ATOM 3020 O GLU A 398 -13.903 -55.642 -5.272 1.00 38.09 O ANISOU 3020 O GLU A 398 4700 6267 3505 1255 -546 494 O ATOM 3021 CB GLU A 398 -11.196 -55.755 -7.834 1.00 36.68 C ANISOU 3021 CB GLU A 398 4349 6021 3568 1163 -631 400 C ATOM 3022 CG GLU A 398 -10.285 -56.944 -7.553 1.00 39.27 C ANISOU 3022 CG GLU A 398 4668 6394 3859 1274 -645 480 C ATOM 3023 CD GLU A 398 -8.989 -56.908 -8.362 1.00 40.86 C ANISOU 3023 CD GLU A 398 4781 6608 4135 1260 -691 435 C ATOM 3024 OE1 GLU A 398 -7.986 -57.486 -7.897 1.00 44.14 O ANISOU 3024 OE1 GLU A 398 5160 7107 4502 1355 -737 461 O ATOM 3025 OE2 GLU A 398 -8.966 -56.301 -9.458 1.00 41.88 O ANISOU 3025 OE2 GLU A 398 4875 6667 4369 1159 -678 377 O ATOM 3026 N ASP A 399 -11.725 -55.110 -5.134 1.00 39.14 N ANISOU 3026 N ASP A 399 4709 6540 3623 1293 -698 375 N ATOM 3027 CA ASP A 399 -11.774 -54.758 -3.713 1.00 40.75 C ANISOU 3027 CA ASP A 399 4929 6872 3681 1375 -748 350 C ATOM 3028 C ASP A 399 -11.816 -53.241 -3.467 1.00 40.58 C ANISOU 3028 C ASP A 399 4873 6896 3652 1309 -812 202 C ATOM 3029 O ASP A 399 -11.685 -52.791 -2.322 1.00 41.59 O ANISOU 3029 O ASP A 399 5002 7140 3659 1373 -873 151 O ATOM 3030 CB ASP A 399 -10.577 -55.379 -2.979 1.00 42.40 C ANISOU 3030 CB ASP A 399 5103 7204 3805 1496 -820 373 C ATOM 3031 CG ASP A 399 -9.235 -55.037 -3.625 1.00 43.78 C ANISOU 3031 CG ASP A 399 5173 7405 4056 1460 -899 290 C ATOM 3032 OD1 ASP A 399 -8.191 -55.298 -2.990 1.00 47.45 O ANISOU 3032 OD1 ASP A 399 5590 7987 4452 1551 -976 281 O ATOM 3033 OD2 ASP A 399 -9.222 -54.518 -4.767 1.00 45.65 O ANISOU 3033 OD2 ASP A 399 5374 7550 4422 1346 -882 238 O ATOM 3034 N GLN A 400 -12.002 -52.463 -4.532 1.00 39.14 N ANISOU 3034 N GLN A 400 4661 6619 3593 1185 -798 134 N ATOM 3035 CA GLN A 400 -12.042 -51.002 -4.440 1.00 38.99 C ANISOU 3035 CA GLN A 400 4609 6618 3589 1111 -851 -5 C ATOM 3036 C GLN A 400 -13.471 -50.481 -4.520 1.00 37.86 C ANISOU 3036 C GLN A 400 4531 6399 3453 1058 -780 -4 C ATOM 3037 O GLN A 400 -14.325 -51.094 -5.156 1.00 36.86 O ANISOU 3037 O GLN A 400 4452 6175 3379 1032 -688 87 O ATOM 3038 CB GLN A 400 -11.212 -50.377 -5.566 1.00 38.64 C ANISOU 3038 CB GLN A 400 4480 6521 3679 1011 -884 -83 C ATOM 3039 CG GLN A 400 -9.738 -50.742 -5.526 1.00 40.49 C ANISOU 3039 CG GLN A 400 4632 6836 3917 1055 -960 -98 C ATOM 3040 CD GLN A 400 -9.058 -50.310 -4.240 1.00 43.02 C ANISOU 3040 CD GLN A 400 4917 7306 4123 1127 -1067 -178 C ATOM 3041 OE1 GLN A 400 -9.413 -49.292 -3.644 1.00 44.34 O ANISOU 3041 OE1 GLN A 400 5093 7505 4248 1103 -1106 -274 O ATOM 3042 NE2 GLN A 400 -8.077 -51.086 -3.804 1.00 44.57 N ANISOU 3042 NE2 GLN A 400 5074 7596 4265 1221 -1118 -142 N ATOM 3043 N GLU A 401 -13.715 -49.349 -3.863 1.00 37.75 N ANISOU 3043 N GLU A 401 4519 6435 3389 1045 -824 -109 N ATOM 3044 CA GLU A 401 -15.005 -48.666 -3.906 1.00 37.18 C ANISOU 3044 CA GLU A 401 4500 6301 3324 995 -766 -126 C ATOM 3045 C GLU A 401 -14.754 -47.216 -4.286 1.00 36.55 C ANISOU 3045 C GLU A 401 4375 6195 3316 901 -819 -271 C ATOM 3046 O GLU A 401 -14.403 -46.391 -3.435 1.00 37.91 O ANISOU 3046 O GLU A 401 4532 6450 3422 924 -897 -377 O ATOM 3047 CB GLU A 401 -15.716 -48.743 -2.553 1.00 38.10 C ANISOU 3047 CB GLU A 401 4681 6506 3288 1092 -755 -103 C ATOM 3048 CG GLU A 401 -16.092 -50.154 -2.140 1.00 39.43 C ANISOU 3048 CG GLU A 401 4902 6691 3389 1184 -688 52 C ATOM 3049 CD GLU A 401 -16.785 -50.216 -0.792 1.00 42.68 C ANISOU 3049 CD GLU A 401 5377 7197 3644 1286 -670 83 C ATOM 3050 OE1 GLU A 401 -16.831 -51.318 -0.207 1.00 44.84 O ANISOU 3050 OE1 GLU A 401 5686 7513 3838 1382 -634 202 O ATOM 3051 OE2 GLU A 401 -17.278 -49.171 -0.310 1.00 43.96 O ANISOU 3051 OE2 GLU A 401 5553 7388 3760 1275 -688 -9 O ATOM 3052 N TYR A 402 -14.921 -46.920 -5.569 1.00 34.49 N ANISOU 3052 N TYR A 402 4094 5818 3193 799 -778 -274 N ATOM 3053 CA TYR A 402 -14.608 -45.604 -6.111 1.00 33.84 C ANISOU 3053 CA TYR A 402 3965 5692 3201 702 -818 -395 C ATOM 3054 C TYR A 402 -15.760 -44.625 -5.944 1.00 33.16 C ANISOU 3054 C TYR A 402 3929 5561 3108 668 -785 -445 C ATOM 3055 O TYR A 402 -16.906 -44.945 -6.260 1.00 32.35 O ANISOU 3055 O TYR A 402 3882 5396 3013 661 -699 -370 O ATOM 3056 CB TYR A 402 -14.254 -45.722 -7.594 1.00 32.64 C ANISOU 3056 CB TYR A 402 3771 5437 3193 617 -783 -368 C ATOM 3057 CG TYR A 402 -13.014 -46.550 -7.850 1.00 32.89 C ANISOU 3057 CG TYR A 402 3742 5509 3245 646 -818 -333 C ATOM 3058 CD1 TYR A 402 -11.744 -46.022 -7.633 1.00 34.04 C ANISOU 3058 CD1 TYR A 402 3805 5722 3407 636 -910 -423 C ATOM 3059 CD2 TYR A 402 -13.110 -47.861 -8.308 1.00 32.78 C ANISOU 3059 CD2 TYR A 402 3752 5465 3237 685 -760 -211 C ATOM 3060 CE1 TYR A 402 -10.604 -46.775 -7.867 1.00 34.34 C ANISOU 3060 CE1 TYR A 402 3780 5803 3463 668 -941 -389 C ATOM 3061 CE2 TYR A 402 -11.977 -48.622 -8.547 1.00 33.10 C ANISOU 3061 CE2 TYR A 402 3740 5542 3296 720 -790 -179 C ATOM 3062 CZ TYR A 402 -10.726 -48.075 -8.324 1.00 33.97 C ANISOU 3062 CZ TYR A 402 3764 5727 3418 714 -879 -266 C ATOM 3063 OH TYR A 402 -9.601 -48.827 -8.559 1.00 34.37 O ANISOU 3063 OH TYR A 402 3755 5819 3487 754 -907 -231 O ATOM 3064 N SER A 403 -15.444 -43.423 -5.468 1.00 33.55 N ANISOU 3064 N SER A 403 3956 5642 3149 644 -854 -577 N ATOM 3065 CA SER A 403 -16.411 -42.329 -5.438 1.00 33.41 C ANISOU 3065 CA SER A 403 3979 5569 3145 602 -828 -642 C ATOM 3066 C SER A 403 -16.652 -41.823 -6.855 1.00 32.34 C ANISOU 3066 C SER A 403 3825 5301 3160 493 -778 -640 C ATOM 3067 O SER A 403 -15.885 -42.132 -7.767 1.00 31.42 O ANISOU 3067 O SER A 403 3656 5147 3135 446 -780 -615 O ATOM 3068 CB SER A 403 -15.888 -41.179 -4.577 1.00 34.63 C ANISOU 3068 CB SER A 403 4113 5787 3260 604 -924 -793 C ATOM 3069 OG SER A 403 -14.755 -40.575 -5.183 1.00 34.74 O ANISOU 3069 OG SER A 403 4045 5771 3383 525 -986 -874 O ATOM 3070 N PHE A 404 -17.712 -41.040 -7.034 1.00 32.11 N ANISOU 3070 N PHE A 404 3841 5207 3154 459 -731 -664 N ATOM 3071 CA PHE A 404 -17.967 -40.374 -8.315 1.00 31.58 C ANISOU 3071 CA PHE A 404 3760 5017 3221 361 -689 -674 C ATOM 3072 C PHE A 404 -16.772 -39.529 -8.754 1.00 32.34 C ANISOU 3072 C PHE A 404 3784 5091 3413 288 -754 -769 C ATOM 3073 O PHE A 404 -16.383 -39.561 -9.920 1.00 31.63 O ANISOU 3073 O PHE A 404 3655 4929 3432 223 -729 -739 O ATOM 3074 CB PHE A 404 -19.209 -39.485 -8.235 1.00 31.46 C ANISOU 3074 CB PHE A 404 3800 4949 3203 347 -644 -706 C ATOM 3075 CG PHE A 404 -20.494 -40.223 -8.435 1.00 30.98 C ANISOU 3075 CG PHE A 404 3793 4863 3114 377 -554 -595 C ATOM 3076 CD1 PHE A 404 -21.084 -40.902 -7.381 1.00 32.17 C ANISOU 3076 CD1 PHE A 404 3987 5093 3141 465 -535 -545 C ATOM 3077 CD2 PHE A 404 -21.119 -40.235 -9.675 1.00 30.31 C ANISOU 3077 CD2 PHE A 404 3713 4677 3127 317 -487 -540 C ATOM 3078 CE1 PHE A 404 -22.277 -41.585 -7.556 1.00 31.91 C ANISOU 3078 CE1 PHE A 404 3997 5034 3094 486 -449 -441 C ATOM 3079 CE2 PHE A 404 -22.320 -40.917 -9.862 1.00 30.07 C ANISOU 3079 CE2 PHE A 404 3723 4623 3077 338 -409 -444 C ATOM 3080 CZ PHE A 404 -22.898 -41.594 -8.796 1.00 30.44 C ANISOU 3080 CZ PHE A 404 3809 4746 3012 419 -389 -394 C ATOM 3081 N LYS A 405 -16.202 -38.782 -7.812 1.00 33.82 N ANISOU 3081 N LYS A 405 3952 5340 3557 302 -838 -885 N ATOM 3082 CA LYS A 405 -15.028 -37.948 -8.074 1.00 34.95 C ANISOU 3082 CA LYS A 405 4018 5469 3792 231 -909 -986 C ATOM 3083 C LYS A 405 -13.854 -38.768 -8.627 1.00 34.62 C ANISOU 3083 C LYS A 405 3901 5455 3799 221 -929 -935 C ATOM 3084 O LYS A 405 -13.169 -38.326 -9.550 1.00 34.77 O ANISOU 3084 O LYS A 405 3858 5412 3940 140 -930 -954 O ATOM 3085 CB LYS A 405 -14.606 -37.211 -6.798 1.00 36.58 C ANISOU 3085 CB LYS A 405 4217 5757 3925 263 -1006 -1119 C ATOM 3086 CG LYS A 405 -13.586 -36.097 -7.008 1.00 39.02 C ANISOU 3086 CG LYS A 405 4451 6032 4342 176 -1079 -1245 C ATOM 3087 CD LYS A 405 -13.110 -35.533 -5.677 1.00 41.98 C ANISOU 3087 CD LYS A 405 4816 6502 4632 217 -1188 -1381 C ATOM 3088 CE LYS A 405 -11.919 -34.597 -5.851 1.00 43.83 C ANISOU 3088 CE LYS A 405 4959 6714 4982 128 -1271 -1504 C ATOM 3089 NZ LYS A 405 -11.229 -34.321 -4.561 1.00 45.94 N ANISOU 3089 NZ LYS A 405 5197 7098 5159 176 -1394 -1631 N ATOM 3090 N GLN A 406 -13.634 -39.955 -8.067 1.00 34.38 N ANISOU 3090 N GLN A 406 3875 5516 3671 307 -941 -865 N ATOM 3091 CA GLN A 406 -12.541 -40.832 -8.504 1.00 34.32 C ANISOU 3091 CA GLN A 406 3800 5544 3696 314 -960 -812 C ATOM 3092 C GLN A 406 -12.842 -41.565 -9.813 1.00 32.97 C ANISOU 3092 C GLN A 406 3639 5286 3603 284 -869 -696 C ATOM 3093 O GLN A 406 -11.926 -41.937 -10.548 1.00 32.85 O ANISOU 3093 O GLN A 406 3559 5263 3658 259 -873 -670 O ATOM 3094 CB GLN A 406 -12.213 -41.855 -7.413 1.00 34.92 C ANISOU 3094 CB GLN A 406 3884 5747 3638 428 -1003 -774 C ATOM 3095 CG GLN A 406 -11.651 -41.234 -6.141 1.00 36.69 C ANISOU 3095 CG GLN A 406 4083 6078 3778 467 -1110 -894 C ATOM 3096 CD GLN A 406 -11.570 -42.214 -4.983 1.00 37.54 C ANISOU 3096 CD GLN A 406 4219 6314 3729 594 -1143 -847 C ATOM 3097 OE1 GLN A 406 -12.385 -43.132 -4.864 1.00 36.19 O ANISOU 3097 OE1 GLN A 406 4117 6142 3491 657 -1071 -734 O ATOM 3098 NE2 GLN A 406 -10.585 -42.013 -4.114 1.00 40.03 N ANISOU 3098 NE2 GLN A 406 4479 6742 3987 635 -1251 -934 N ATOM 3099 N PHE A 407 -14.123 -41.776 -10.096 1.00 32.05 N ANISOU 3099 N PHE A 407 3599 5108 3471 290 -789 -631 N ATOM 3100 CA PHE A 407 -14.539 -42.575 -11.244 1.00 30.98 C ANISOU 3100 CA PHE A 407 3482 4897 3392 272 -707 -524 C ATOM 3101 C PHE A 407 -14.561 -41.743 -12.524 1.00 30.79 C ANISOU 3101 C PHE A 407 3434 4766 3497 175 -671 -545 C ATOM 3102 O PHE A 407 -14.212 -42.242 -13.591 1.00 30.41 O ANISOU 3102 O PHE A 407 3362 4675 3519 150 -634 -487 O ATOM 3103 CB PHE A 407 -15.926 -43.168 -10.974 1.00 30.53 C ANISOU 3103 CB PHE A 407 3510 4823 3267 318 -640 -447 C ATOM 3104 CG PHE A 407 -16.221 -44.433 -11.734 1.00 28.91 C ANISOU 3104 CG PHE A 407 3326 4578 3082 334 -576 -328 C ATOM 3105 CD1 PHE A 407 -15.469 -45.582 -11.517 1.00 29.47 C ANISOU 3105 CD1 PHE A 407 3378 4704 3117 394 -593 -269 C ATOM 3106 CD2 PHE A 407 -17.283 -44.490 -12.624 1.00 28.60 C ANISOU 3106 CD2 PHE A 407 3328 4447 3093 296 -500 -278 C ATOM 3107 CE1 PHE A 407 -15.757 -46.758 -12.201 1.00 29.27 C ANISOU 3107 CE1 PHE A 407 3377 4631 3112 411 -534 -166 C ATOM 3108 CE2 PHE A 407 -17.572 -45.662 -13.308 1.00 27.73 C ANISOU 3108 CE2 PHE A 407 3238 4297 3002 310 -447 -179 C ATOM 3109 CZ PHE A 407 -16.811 -46.794 -13.091 1.00 27.87 C ANISOU 3109 CZ PHE A 407 3241 4360 2989 366 -463 -125 C ATOM 3110 N LEU A 408 -14.977 -40.481 -12.415 1.00 31.26 N ANISOU 3110 N LEU A 408 3506 4785 3586 127 -678 -626 N ATOM 3111 CA LEU A 408 -15.186 -39.619 -13.589 1.00 31.28 C ANISOU 3111 CA LEU A 408 3500 4680 3705 42 -634 -639 C ATOM 3112 C LEU A 408 -13.895 -39.302 -14.350 1.00 31.37 C ANISOU 3112 C LEU A 408 3425 4673 3819 -18 -657 -664 C ATOM 3113 O LEU A 408 -12.885 -38.923 -13.753 1.00 32.20 O ANISOU 3113 O LEU A 408 3470 4834 3931 -27 -730 -739 O ATOM 3114 CB LEU A 408 -15.906 -38.317 -13.190 1.00 31.77 C ANISOU 3114 CB LEU A 408 3599 4702 3772 13 -638 -722 C ATOM 3115 CG LEU A 408 -17.444 -38.350 -13.245 1.00 32.66 C ANISOU 3115 CG LEU A 408 3792 4771 3845 36 -571 -675 C ATOM 3116 CD1 LEU A 408 -18.026 -39.684 -12.779 1.00 33.87 C ANISOU 3116 CD1 LEU A 408 3986 4982 3901 113 -544 -584 C ATOM 3117 CD2 LEU A 408 -18.037 -37.201 -12.432 1.00 34.93 C ANISOU 3117 CD2 LEU A 408 4116 5053 4103 38 -592 -768 C ATOM 3118 N TYR A 409 -13.953 -39.462 -15.672 1.00 30.52 N ANISOU 3118 N TYR A 409 3312 4492 3793 -58 -593 -601 N ATOM 3119 CA TYR A 409 -12.820 -39.220 -16.575 1.00 30.69 C ANISOU 3119 CA TYR A 409 3255 4490 3917 -113 -594 -604 C ATOM 3120 C TYR A 409 -11.555 -39.966 -16.157 1.00 31.18 C ANISOU 3120 C TYR A 409 3244 4644 3958 -78 -650 -605 C ATOM 3121 O TYR A 409 -10.450 -39.433 -16.264 1.00 31.96 O ANISOU 3121 O TYR A 409 3259 4758 4127 -122 -689 -656 O ATOM 3122 CB TYR A 409 -12.545 -37.713 -16.712 1.00 31.50 C ANISOU 3122 CB TYR A 409 3324 4535 4110 -194 -610 -693 C ATOM 3123 CG TYR A 409 -13.630 -36.979 -17.457 1.00 31.69 C ANISOU 3123 CG TYR A 409 3408 4455 4178 -232 -542 -677 C ATOM 3124 CD1 TYR A 409 -13.799 -37.156 -18.828 1.00 31.95 C ANISOU 3124 CD1 TYR A 409 3445 4420 4273 -256 -469 -600 C ATOM 3125 CD2 TYR A 409 -14.498 -36.117 -16.793 1.00 33.58 C ANISOU 3125 CD2 TYR A 409 3701 4668 4390 -234 -552 -738 C ATOM 3126 CE1 TYR A 409 -14.805 -36.488 -19.523 1.00 31.94 C ANISOU 3126 CE1 TYR A 409 3499 4331 4307 -283 -410 -582 C ATOM 3127 CE2 TYR A 409 -15.505 -35.446 -17.476 1.00 33.59 C ANISOU 3127 CE2 TYR A 409 3755 4576 4430 -261 -490 -720 C ATOM 3128 CZ TYR A 409 -15.653 -35.636 -18.838 1.00 33.22 C ANISOU 3128 CZ TYR A 409 3709 4467 4444 -285 -420 -641 C ATOM 3129 OH TYR A 409 -16.652 -34.973 -19.517 1.00 35.13 O ANISOU 3129 OH TYR A 409 4003 4624 4719 -304 -363 -621 O ATOM 3130 N ASN A 410 -11.719 -41.203 -15.694 1.00 30.59 N ANISOU 3130 N ASN A 410 3200 4631 3793 3 -653 -543 N ATOM 3131 CA ASN A 410 -10.602 -41.958 -15.141 1.00 31.42 C ANISOU 3131 CA ASN A 410 3245 4833 3861 54 -710 -541 C ATOM 3132 C ASN A 410 -10.471 -43.340 -15.767 1.00 30.28 C ANISOU 3132 C ASN A 410 3110 4691 3702 106 -666 -435 C ATOM 3133 O ASN A 410 -10.799 -44.361 -15.148 1.00 30.08 O ANISOU 3133 O ASN A 410 3130 4712 3589 184 -667 -383 O ATOM 3134 CB ASN A 410 -10.742 -42.055 -13.621 1.00 32.46 C ANISOU 3134 CB ASN A 410 3399 5056 3877 119 -778 -586 C ATOM 3135 CG ASN A 410 -9.443 -42.418 -12.935 1.00 35.32 C ANISOU 3135 CG ASN A 410 3683 5528 4211 160 -860 -617 C ATOM 3136 OD1 ASN A 410 -8.460 -42.785 -13.587 1.00 35.26 O ANISOU 3136 OD1 ASN A 410 3603 5530 4265 150 -860 -592 O ATOM 3137 ND2 ASN A 410 -9.437 -42.310 -11.595 1.00 40.22 N ANISOU 3137 ND2 ASN A 410 4314 6236 4732 214 -931 -674 N ATOM 3138 N ASN A 411 -9.965 -43.358 -16.995 1.00 29.19 N ANISOU 3138 N ASN A 411 2932 4505 3656 65 -624 -404 N ATOM 3139 CA ASN A 411 -9.730 -44.604 -17.721 1.00 28.39 C ANISOU 3139 CA ASN A 411 2835 4399 3553 111 -581 -315 C ATOM 3140 C ASN A 411 -8.611 -45.459 -17.121 1.00 28.68 C ANISOU 3140 C ASN A 411 2813 4533 3549 180 -634 -302 C ATOM 3141 O ASN A 411 -8.502 -46.640 -17.447 1.00 28.18 O ANISOU 3141 O ASN A 411 2769 4475 3463 239 -606 -227 O ATOM 3142 CB ASN A 411 -9.436 -44.318 -19.200 1.00 27.97 C ANISOU 3142 CB ASN A 411 2751 4274 3601 55 -522 -290 C ATOM 3143 CG ASN A 411 -10.639 -43.767 -19.943 1.00 27.80 C ANISOU 3143 CG ASN A 411 2799 4156 3608 9 -460 -278 C ATOM 3144 OD1 ASN A 411 -11.787 -44.069 -19.607 1.00 27.58 O ANISOU 3144 OD1 ASN A 411 2850 4107 3522 33 -442 -255 O ATOM 3145 ND2 ASN A 411 -10.381 -42.967 -20.979 1.00 27.35 N ANISOU 3145 ND2 ASN A 411 2708 4042 3640 -56 -423 -286 N ATOM 3146 N SER A 412 -7.786 -44.880 -16.246 1.00 29.38 N ANISOU 3146 N SER A 412 2833 4700 3629 176 -714 -379 N ATOM 3147 CA SER A 412 -6.753 -45.653 -15.558 1.00 30.08 C ANISOU 3147 CA SER A 412 2865 4895 3670 250 -774 -371 C ATOM 3148 C SER A 412 -7.365 -46.796 -14.737 1.00 29.60 C ANISOU 3148 C SER A 412 2883 4873 3491 350 -774 -308 C ATOM 3149 O SER A 412 -6.741 -47.842 -14.582 1.00 29.38 O ANISOU 3149 O SER A 412 2836 4899 3427 426 -785 -255 O ATOM 3150 CB SER A 412 -5.857 -44.760 -14.683 1.00 31.57 C ANISOU 3150 CB SER A 412 2966 5165 3865 226 -870 -476 C ATOM 3151 OG SER A 412 -6.538 -44.311 -13.525 1.00 33.09 O ANISOU 3151 OG SER A 412 3211 5388 3974 242 -915 -532 O ATOM 3152 N ILE A 413 -8.589 -46.596 -14.240 1.00 28.82 N ANISOU 3152 N ILE A 413 2871 4743 3335 351 -755 -308 N ATOM 3153 CA ILE A 413 -9.324 -47.636 -13.508 1.00 28.57 C ANISOU 3153 CA ILE A 413 2921 4735 3199 437 -738 -238 C ATOM 3154 C ILE A 413 -9.570 -48.851 -14.406 1.00 27.93 C ANISOU 3154 C ILE A 413 2880 4593 3140 467 -666 -133 C ATOM 3155 O ILE A 413 -9.374 -49.993 -13.985 1.00 27.84 O ANISOU 3155 O ILE A 413 2888 4620 3070 552 -667 -67 O ATOM 3156 CB ILE A 413 -10.684 -47.105 -12.960 1.00 28.07 C ANISOU 3156 CB ILE A 413 2940 4640 3086 422 -717 -255 C ATOM 3157 CG1 ILE A 413 -10.451 -46.009 -11.913 1.00 29.43 C ANISOU 3157 CG1 ILE A 413 3083 4880 3218 411 -794 -363 C ATOM 3158 CG2 ILE A 413 -11.508 -48.236 -12.342 1.00 27.83 C ANISOU 3158 CG2 ILE A 413 2992 4622 2962 505 -682 -165 C ATOM 3159 CD1 ILE A 413 -11.731 -45.381 -11.363 1.00 28.52 C ANISOU 3159 CD1 ILE A 413 3044 4738 3054 400 -773 -389 C ATOM 3160 N LEU A 414 -9.982 -48.596 -15.647 1.00 27.21 N ANISOU 3160 N LEU A 414 2801 4404 3132 400 -604 -120 N ATOM 3161 CA LEU A 414 -10.216 -49.667 -16.617 1.00 27.04 C ANISOU 3161 CA LEU A 414 2818 4318 3140 422 -539 -36 C ATOM 3162 C LEU A 414 -8.928 -50.433 -16.915 1.00 27.91 C ANISOU 3162 C LEU A 414 2865 4473 3268 472 -556 -9 C ATOM 3163 O LEU A 414 -8.916 -51.664 -16.895 1.00 27.40 O ANISOU 3163 O LEU A 414 2836 4405 3171 544 -535 64 O ATOM 3164 CB LEU A 414 -10.830 -49.108 -17.909 1.00 26.31 C ANISOU 3164 CB LEU A 414 2743 4124 3128 342 -479 -40 C ATOM 3165 CG LEU A 414 -11.322 -50.130 -18.941 1.00 26.26 C ANISOU 3165 CG LEU A 414 2790 4042 3147 358 -412 34 C ATOM 3166 CD1 LEU A 414 -12.367 -51.056 -18.327 1.00 25.99 C ANISOU 3166 CD1 LEU A 414 2839 3989 3048 406 -389 93 C ATOM 3167 CD2 LEU A 414 -11.882 -49.445 -20.180 1.00 26.03 C ANISOU 3167 CD2 LEU A 414 2774 3929 3189 284 -362 21 C ATOM 3168 N LEU A 415 -7.844 -49.704 -17.171 1.00 28.82 N ANISOU 3168 N LEU A 415 2885 4627 3438 436 -592 -65 N ATOM 3169 CA LEU A 415 -6.536 -50.329 -17.401 1.00 30.24 C ANISOU 3169 CA LEU A 415 2990 4863 3637 485 -612 -45 C ATOM 3170 C LEU A 415 -6.020 -51.098 -16.186 1.00 31.21 C ANISOU 3170 C LEU A 415 3103 5086 3671 584 -671 -26 C ATOM 3171 O LEU A 415 -5.422 -52.166 -16.333 1.00 31.74 O ANISOU 3171 O LEU A 415 3160 5176 3726 660 -663 33 O ATOM 3172 CB LEU A 415 -5.494 -49.283 -17.821 1.00 30.98 C ANISOU 3172 CB LEU A 415 2973 4986 3814 419 -641 -114 C ATOM 3173 CG LEU A 415 -5.333 -49.076 -19.327 1.00 32.24 C ANISOU 3173 CG LEU A 415 3111 5069 4069 364 -572 -94 C ATOM 3174 CD1 LEU A 415 -4.404 -47.912 -19.607 1.00 33.94 C ANISOU 3174 CD1 LEU A 415 3217 5308 4369 289 -597 -161 C ATOM 3175 CD2 LEU A 415 -4.791 -50.339 -19.970 1.00 33.44 C ANISOU 3175 CD2 LEU A 415 3261 5224 4221 439 -537 -22 C ATOM 3176 N GLU A 416 -6.250 -50.553 -14.993 1.00 31.56 N ANISOU 3176 N GLU A 416 3152 5192 3649 590 -730 -76 N ATOM 3177 CA GLU A 416 -5.760 -51.153 -13.748 1.00 32.62 C ANISOU 3177 CA GLU A 416 3275 5434 3685 688 -794 -64 C ATOM 3178 C GLU A 416 -6.395 -52.516 -13.469 1.00 31.82 C ANISOU 3178 C GLU A 416 3266 5310 3513 779 -749 41 C ATOM 3179 O GLU A 416 -5.697 -53.475 -13.150 1.00 31.88 O ANISOU 3179 O GLU A 416 3258 5374 3483 871 -767 92 O ATOM 3180 CB GLU A 416 -6.027 -50.203 -12.573 1.00 33.42 C ANISOU 3180 CB GLU A 416 3375 5600 3724 674 -861 -146 C ATOM 3181 CG GLU A 416 -5.591 -50.706 -11.198 1.00 36.44 C ANISOU 3181 CG GLU A 416 3751 6106 3989 780 -933 -142 C ATOM 3182 CD GLU A 416 -4.086 -50.813 -11.049 1.00 39.81 C ANISOU 3182 CD GLU A 416 4063 6635 4430 818 -1006 -172 C ATOM 3183 OE1 GLU A 416 -3.352 -50.260 -11.899 1.00 42.00 O ANISOU 3183 OE1 GLU A 416 4253 6892 4812 746 -1009 -215 O ATOM 3184 OE2 GLU A 416 -3.636 -51.448 -10.070 1.00 43.00 O ANISOU 3184 OE2 GLU A 416 4459 7141 4737 922 -1060 -150 O ATOM 3185 N HIS A 417 -7.718 -52.590 -13.584 1.00 30.38 N ANISOU 3185 N HIS A 417 3179 5045 3320 752 -689 74 N ATOM 3186 CA HIS A 417 -8.462 -53.808 -13.253 1.00 29.94 C ANISOU 3186 CA HIS A 417 3214 4957 3206 825 -642 172 C ATOM 3187 C HIS A 417 -8.650 -54.750 -14.445 1.00 29.04 C ANISOU 3187 C HIS A 417 3136 4741 3159 824 -569 242 C ATOM 3188 O HIS A 417 -8.654 -55.969 -14.271 1.00 29.32 O ANISOU 3188 O HIS A 417 3214 4764 3163 904 -544 324 O ATOM 3189 CB HIS A 417 -9.828 -53.448 -12.659 1.00 29.56 C ANISOU 3189 CB HIS A 417 3244 4879 3108 802 -616 174 C ATOM 3190 CG HIS A 417 -9.742 -52.716 -11.356 1.00 30.10 C ANISOU 3190 CG HIS A 417 3296 5051 3089 826 -685 113 C ATOM 3191 ND1 HIS A 417 -9.458 -53.349 -10.165 1.00 31.55 N ANISOU 3191 ND1 HIS A 417 3494 5330 3165 931 -722 151 N ATOM 3192 CD2 HIS A 417 -9.905 -51.406 -11.055 1.00 30.65 C ANISOU 3192 CD2 HIS A 417 3342 5144 3160 763 -723 15 C ATOM 3193 CE1 HIS A 417 -9.446 -52.461 -9.187 1.00 32.29 C ANISOU 3193 CE1 HIS A 417 3571 5507 3191 934 -784 74 C ATOM 3194 NE2 HIS A 417 -9.719 -51.274 -9.699 1.00 31.52 N ANISOU 3194 NE2 HIS A 417 3451 5364 3161 831 -786 -12 N ATOM 3195 N GLY A 418 -8.816 -54.187 -15.641 1.00 27.93 N ANISOU 3195 N GLY A 418 2980 4525 3106 738 -534 210 N ATOM 3196 CA GLY A 418 -9.067 -54.973 -16.853 1.00 27.12 C ANISOU 3196 CA GLY A 418 2916 4325 3066 732 -467 262 C ATOM 3197 C GLY A 418 -10.547 -55.241 -17.076 1.00 26.25 C ANISOU 3197 C GLY A 418 2899 4118 2957 700 -407 299 C ATOM 3198 O GLY A 418 -11.351 -55.136 -16.151 1.00 25.77 O ANISOU 3198 O GLY A 418 2883 4072 2838 707 -410 310 O ATOM 3199 N LEU A 419 -10.901 -55.599 -18.307 1.00 25.61 N ANISOU 3199 N LEU A 419 2847 3944 2941 668 -354 318 N ATOM 3200 CA LEU A 419 -12.299 -55.817 -18.680 1.00 25.23 C ANISOU 3200 CA LEU A 419 2877 3802 2909 628 -301 345 C ATOM 3201 C LEU A 419 -12.932 -56.992 -17.951 1.00 25.21 C ANISOU 3201 C LEU A 419 2944 3775 2860 689 -277 424 C ATOM 3202 O LEU A 419 -14.108 -56.935 -17.576 1.00 24.83 O ANISOU 3202 O LEU A 419 2946 3692 2794 663 -251 442 O ATOM 3203 CB LEU A 419 -12.427 -56.058 -20.187 1.00 24.98 C ANISOU 3203 CB LEU A 419 2858 3683 2951 593 -256 345 C ATOM 3204 CG LEU A 419 -12.491 -54.843 -21.101 1.00 26.18 C ANISOU 3204 CG LEU A 419 2974 3817 3155 510 -250 282 C ATOM 3205 CD1 LEU A 419 -12.550 -55.321 -22.549 1.00 27.29 C ANISOU 3205 CD1 LEU A 419 3135 3881 3352 500 -206 293 C ATOM 3206 CD2 LEU A 419 -13.685 -53.987 -20.793 1.00 27.13 C ANISOU 3206 CD2 LEU A 419 3126 3917 3267 448 -243 256 C ATOM 3207 N THR A 420 -12.161 -58.062 -17.775 1.00 25.53 N ANISOU 3207 N THR A 420 2985 3830 2885 772 -281 475 N ATOM 3208 CA THR A 420 -12.657 -59.257 -17.104 1.00 25.75 C ANISOU 3208 CA THR A 420 3080 3828 2877 837 -253 560 C ATOM 3209 C THR A 420 -13.160 -58.891 -15.704 1.00 26.08 C ANISOU 3209 C THR A 420 3137 3938 2836 855 -272 573 C ATOM 3210 O THR A 420 -14.282 -59.231 -15.342 1.00 25.73 O ANISOU 3210 O THR A 420 3152 3844 2778 846 -231 620 O ATOM 3211 CB THR A 420 -11.581 -60.365 -17.015 1.00 26.57 C ANISOU 3211 CB THR A 420 3175 3950 2969 936 -262 611 C ATOM 3212 OG1 THR A 420 -11.005 -60.592 -18.311 1.00 26.45 O ANISOU 3212 OG1 THR A 420 3140 3887 3025 925 -247 589 O ATOM 3213 CG2 THR A 420 -12.186 -61.662 -16.492 1.00 27.31 C ANISOU 3213 CG2 THR A 420 3349 3984 3042 997 -220 708 C ATOM 3214 N GLN A 421 -12.340 -58.172 -14.940 1.00 26.49 N ANISOU 3214 N GLN A 421 3129 4102 2832 881 -334 528 N ATOM 3215 CA GLN A 421 -12.724 -57.741 -13.591 1.00 27.03 C ANISOU 3215 CA GLN A 421 3210 4249 2810 907 -359 527 C ATOM 3216 C GLN A 421 -13.878 -56.733 -13.598 1.00 25.76 C ANISOU 3216 C GLN A 421 3069 4060 2657 822 -341 482 C ATOM 3217 O GLN A 421 -14.738 -56.770 -12.718 1.00 25.57 O ANISOU 3217 O GLN A 421 3090 4051 2574 840 -322 515 O ATOM 3218 CB GLN A 421 -11.526 -57.141 -12.852 1.00 28.12 C ANISOU 3218 CB GLN A 421 3274 4517 2892 950 -441 471 C ATOM 3219 CG GLN A 421 -11.799 -56.832 -11.392 1.00 30.90 C ANISOU 3219 CG GLN A 421 3642 4962 3134 999 -474 471 C ATOM 3220 CD GLN A 421 -12.212 -58.063 -10.608 1.00 33.56 C ANISOU 3220 CD GLN A 421 4049 5297 3406 1092 -436 584 C ATOM 3221 OE1 GLN A 421 -13.317 -58.126 -10.066 1.00 36.36 O ANISOU 3221 OE1 GLN A 421 4464 5629 3722 1089 -393 625 O ATOM 3222 NE2 GLN A 421 -11.336 -59.056 -10.565 1.00 35.48 N ANISOU 3222 NE2 GLN A 421 4283 5558 3638 1177 -445 641 N ATOM 3223 N PHE A 422 -13.883 -55.821 -14.568 1.00 24.80 N ANISOU 3223 N PHE A 422 2914 3904 2607 736 -344 410 N ATOM 3224 CA PHE A 422 -15.006 -54.888 -14.731 1.00 23.94 C ANISOU 3224 CA PHE A 422 2825 3756 2515 658 -321 370 C ATOM 3225 C PHE A 422 -16.314 -55.655 -14.891 1.00 23.53 C ANISOU 3225 C PHE A 422 2846 3618 2477 648 -253 441 C ATOM 3226 O PHE A 422 -17.290 -55.390 -14.189 1.00 23.46 O ANISOU 3226 O PHE A 422 2870 3617 2427 642 -233 454 O ATOM 3227 CB PHE A 422 -14.793 -53.956 -15.932 1.00 23.41 C ANISOU 3227 CB PHE A 422 2716 3647 2530 574 -324 298 C ATOM 3228 CG PHE A 422 -14.326 -52.581 -15.554 1.00 23.33 C ANISOU 3228 CG PHE A 422 2651 3703 2509 538 -378 208 C ATOM 3229 CD1 PHE A 422 -13.141 -52.408 -14.859 1.00 24.57 C ANISOU 3229 CD1 PHE A 422 2751 3957 2628 581 -442 175 C ATOM 3230 CD2 PHE A 422 -15.067 -51.459 -15.897 1.00 24.51 C ANISOU 3230 CD2 PHE A 422 2805 3817 2692 462 -365 154 C ATOM 3231 CE1 PHE A 422 -12.706 -51.143 -14.502 1.00 25.32 C ANISOU 3231 CE1 PHE A 422 2793 4106 2722 542 -496 84 C ATOM 3232 CE2 PHE A 422 -14.632 -50.185 -15.541 1.00 24.31 C ANISOU 3232 CE2 PHE A 422 2732 3839 2664 427 -414 67 C ATOM 3233 CZ PHE A 422 -13.444 -50.034 -14.847 1.00 25.52 C ANISOU 3233 CZ PHE A 422 2827 4084 2784 464 -480 29 C ATOM 3234 N VAL A 423 -16.322 -56.618 -15.809 1.00 23.39 N ANISOU 3234 N VAL A 423 2849 3517 2519 648 -216 486 N ATOM 3235 CA VAL A 423 -17.512 -57.424 -16.056 1.00 23.35 C ANISOU 3235 CA VAL A 423 2906 3421 2545 632 -155 550 C ATOM 3236 C VAL A 423 -17.926 -58.198 -14.798 1.00 24.30 C ANISOU 3236 C VAL A 423 3069 3567 2596 699 -133 632 C ATOM 3237 O VAL A 423 -19.086 -58.150 -14.393 1.00 24.32 O ANISOU 3237 O VAL A 423 3106 3548 2588 676 -95 662 O ATOM 3238 CB VAL A 423 -17.314 -58.398 -17.234 1.00 23.01 C ANISOU 3238 CB VAL A 423 2881 3287 2577 629 -128 576 C ATOM 3239 CG1 VAL A 423 -18.520 -59.331 -17.361 1.00 23.56 C ANISOU 3239 CG1 VAL A 423 3012 3260 2680 615 -70 641 C ATOM 3240 CG2 VAL A 423 -17.100 -57.627 -18.535 1.00 22.54 C ANISOU 3240 CG2 VAL A 423 2787 3198 2581 563 -137 503 C ATOM 3241 N GLU A 424 -16.979 -58.892 -14.172 1.00 25.34 N ANISOU 3241 N GLU A 424 3197 3751 2679 786 -156 674 N ATOM 3242 CA GLU A 424 -17.281 -59.665 -12.961 1.00 26.74 C ANISOU 3242 CA GLU A 424 3417 3958 2784 863 -133 763 C ATOM 3243 C GLU A 424 -17.852 -58.776 -11.849 1.00 26.75 C ANISOU 3243 C GLU A 424 3419 4043 2702 865 -144 743 C ATOM 3244 O GLU A 424 -18.844 -59.134 -11.210 1.00 27.10 O ANISOU 3244 O GLU A 424 3508 4071 2716 877 -93 809 O ATOM 3245 CB GLU A 424 -16.044 -60.427 -12.474 1.00 28.06 C ANISOU 3245 CB GLU A 424 3574 4182 2906 965 -165 803 C ATOM 3246 CG GLU A 424 -15.642 -61.571 -13.414 1.00 30.18 C ANISOU 3246 CG GLU A 424 3860 4356 3250 982 -139 846 C ATOM 3247 CD GLU A 424 -14.364 -62.287 -13.004 1.00 35.05 C ANISOU 3247 CD GLU A 424 4461 5031 3826 1089 -171 883 C ATOM 3248 OE1 GLU A 424 -14.098 -63.379 -13.557 1.00 37.39 O ANISOU 3248 OE1 GLU A 424 4786 5250 4172 1123 -142 935 O ATOM 3249 OE2 GLU A 424 -13.625 -61.773 -12.136 1.00 38.33 O ANISOU 3249 OE2 GLU A 424 4835 5570 4160 1141 -228 859 O ATOM 3250 N SER A 425 -17.248 -57.606 -11.654 1.00 26.49 N ANISOU 3250 N SER A 425 3335 4094 2635 851 -206 649 N ATOM 3251 CA SER A 425 -17.663 -56.679 -10.597 1.00 26.71 C ANISOU 3251 CA SER A 425 3363 4208 2579 860 -227 612 C ATOM 3252 C SER A 425 -19.007 -56.021 -10.888 1.00 26.08 C ANISOU 3252 C SER A 425 3305 4073 2533 781 -182 592 C ATOM 3253 O SER A 425 -19.880 -55.952 -10.022 1.00 26.17 O ANISOU 3253 O SER A 425 3349 4111 2484 803 -150 626 O ATOM 3254 CB SER A 425 -16.604 -55.591 -10.398 1.00 26.79 C ANISOU 3254 CB SER A 425 3309 4311 2559 858 -312 506 C ATOM 3255 OG SER A 425 -15.405 -56.129 -9.861 1.00 27.33 O ANISOU 3255 OG SER A 425 3352 4457 2575 944 -361 524 O ATOM 3256 N PHE A 426 -19.176 -55.524 -12.105 1.00 25.46 N ANISOU 3256 N PHE A 426 3205 3921 2547 695 -177 538 N ATOM 3257 CA PHE A 426 -20.411 -54.837 -12.439 1.00 25.18 C ANISOU 3257 CA PHE A 426 3184 3838 2546 624 -140 514 C ATOM 3258 C PHE A 426 -21.590 -55.792 -12.604 1.00 24.92 C ANISOU 3258 C PHE A 426 3198 3724 2548 612 -65 604 C ATOM 3259 O PHE A 426 -22.739 -55.383 -12.426 1.00 24.45 O ANISOU 3259 O PHE A 426 3152 3649 2487 579 -28 607 O ATOM 3260 CB PHE A 426 -20.216 -53.893 -13.633 1.00 24.93 C ANISOU 3260 CB PHE A 426 3114 3764 2593 542 -161 427 C ATOM 3261 CG PHE A 426 -19.446 -52.629 -13.281 1.00 27.23 C ANISOU 3261 CG PHE A 426 3362 4133 2854 535 -226 331 C ATOM 3262 CD1 PHE A 426 -19.526 -52.070 -12.002 1.00 30.50 C ANISOU 3262 CD1 PHE A 426 3779 4634 3174 576 -253 305 C ATOM 3263 CD2 PHE A 426 -18.661 -51.996 -14.224 1.00 29.97 C ANISOU 3263 CD2 PHE A 426 3662 4462 3265 486 -257 265 C ATOM 3264 CE1 PHE A 426 -18.828 -50.914 -11.677 1.00 31.85 C ANISOU 3264 CE1 PHE A 426 3909 4868 3323 565 -317 207 C ATOM 3265 CE2 PHE A 426 -17.966 -50.836 -13.907 1.00 30.72 C ANISOU 3265 CE2 PHE A 426 3712 4617 3345 471 -315 176 C ATOM 3266 CZ PHE A 426 -18.048 -50.299 -12.634 1.00 31.30 C ANISOU 3266 CZ PHE A 426 3791 4772 3332 508 -348 143 C ATOM 3267 N THR A 427 -21.311 -57.065 -12.884 1.00 24.86 N ANISOU 3267 N THR A 427 3211 3664 2572 642 -42 676 N ATOM 3268 CA THR A 427 -22.371 -58.069 -12.913 1.00 25.12 C ANISOU 3268 CA THR A 427 3287 3616 2642 634 29 766 C ATOM 3269 C THR A 427 -22.922 -58.302 -11.501 1.00 26.04 C ANISOU 3269 C THR A 427 3432 3792 2670 695 63 839 C ATOM 3270 O THR A 427 -24.119 -58.559 -11.336 1.00 26.08 O ANISOU 3270 O THR A 427 3459 3754 2694 669 124 892 O ATOM 3271 CB THR A 427 -21.896 -59.397 -13.552 1.00 25.21 C ANISOU 3271 CB THR A 427 3319 3547 2714 654 45 823 C ATOM 3272 OG1 THR A 427 -21.450 -59.149 -14.896 1.00 24.76 O ANISOU 3272 OG1 THR A 427 3236 3439 2733 602 18 754 O ATOM 3273 CG2 THR A 427 -23.035 -60.423 -13.577 1.00 25.68 C ANISOU 3273 CG2 THR A 427 3420 3512 2824 636 117 912 C ATOM 3274 N ARG A 428 -22.049 -58.169 -10.498 1.00 26.88 N ANISOU 3274 N ARG A 428 3535 4003 2677 776 22 838 N ATOM 3275 CA ARG A 428 -22.402 -58.382 -9.088 1.00 28.35 C ANISOU 3275 CA ARG A 428 3750 4264 2758 853 48 907 C ATOM 3276 C ARG A 428 -22.989 -57.159 -8.383 1.00 28.00 C ANISOU 3276 C ARG A 428 3697 4299 2642 846 39 848 C ATOM 3277 O ARG A 428 -23.673 -57.313 -7.367 1.00 28.81 O ANISOU 3277 O ARG A 428 3829 4445 2670 894 83 910 O ATOM 3278 CB ARG A 428 -21.165 -58.820 -8.289 1.00 29.51 C ANISOU 3278 CB ARG A 428 3896 4498 2817 958 2 931 C ATOM 3279 CG ARG A 428 -20.707 -60.229 -8.544 1.00 32.63 C ANISOU 3279 CG ARG A 428 4317 4830 3252 1002 27 1024 C ATOM 3280 CD ARG A 428 -19.671 -60.664 -7.504 1.00 36.78 C ANISOU 3280 CD ARG A 428 4848 5457 3670 1124 -10 1066 C ATOM 3281 NE ARG A 428 -18.503 -59.777 -7.482 1.00 39.28 N ANISOU 3281 NE ARG A 428 5108 5870 3945 1138 -105 958 N ATOM 3282 CZ ARG A 428 -17.334 -60.007 -8.091 1.00 41.36 C ANISOU 3282 CZ ARG A 428 5336 6133 4246 1151 -155 926 C ATOM 3283 NH1 ARG A 428 -17.116 -61.120 -8.794 1.00 42.12 N ANISOU 3283 NH1 ARG A 428 5451 6136 4416 1159 -121 991 N ATOM 3284 NH2 ARG A 428 -16.360 -59.109 -7.988 1.00 42.35 N ANISOU 3284 NH2 ARG A 428 5403 6352 4337 1156 -239 827 N ATOM 3285 N GLN A 429 -22.709 -55.952 -8.874 1.00 26.90 N ANISOU 3285 N GLN A 429 3520 4179 2521 792 -15 731 N ATOM 3286 CA GLN A 429 -23.146 -54.750 -8.159 1.00 26.71 C ANISOU 3286 CA GLN A 429 3491 4231 2427 794 -31 664 C ATOM 3287 C GLN A 429 -24.555 -54.331 -8.550 1.00 25.99 C ANISOU 3287 C GLN A 429 3408 4079 2387 725 28 666 C ATOM 3288 O GLN A 429 -24.836 -54.075 -9.724 1.00 24.58 O ANISOU 3288 O GLN A 429 3211 3818 2310 643 33 629 O ATOM 3289 CB GLN A 429 -22.192 -53.571 -8.358 1.00 26.63 C ANISOU 3289 CB GLN A 429 3438 4271 2411 772 -117 536 C ATOM 3290 CG GLN A 429 -22.577 -52.370 -7.470 1.00 27.52 C ANISOU 3290 CG GLN A 429 3552 4464 2440 787 -139 463 C ATOM 3291 CD GLN A 429 -21.565 -51.239 -7.482 1.00 27.84 C ANISOU 3291 CD GLN A 429 3549 4557 2470 771 -229 336 C ATOM 3292 OE1 GLN A 429 -20.565 -51.282 -8.199 1.00 27.92 O ANISOU 3292 OE1 GLN A 429 3521 4547 2539 744 -273 302 O ATOM 3293 NE2 GLN A 429 -21.825 -50.213 -6.680 1.00 27.05 N ANISOU 3293 NE2 GLN A 429 3455 4524 2297 788 -254 264 N ATOM 3294 N ILE A 430 -25.422 -54.224 -7.549 1.00 26.24 N ANISOU 3294 N ILE A 430 3465 4160 2344 766 73 707 N ATOM 3295 CA ILE A 430 -26.816 -53.864 -7.780 1.00 25.72 C ANISOU 3295 CA ILE A 430 3402 4050 2319 713 135 717 C ATOM 3296 C ILE A 430 -26.974 -52.368 -8.067 1.00 25.22 C ANISOU 3296 C ILE A 430 3317 4005 2262 667 96 596 C ATOM 3297 O ILE A 430 -26.254 -51.533 -7.506 1.00 25.67 O ANISOU 3297 O ILE A 430 3366 4139 2247 701 34 515 O ATOM 3298 CB ILE A 430 -27.709 -54.286 -6.587 1.00 26.82 C ANISOU 3298 CB ILE A 430 3575 4241 2376 777 207 811 C ATOM 3299 CG1 ILE A 430 -29.178 -54.388 -7.017 1.00 26.49 C ANISOU 3299 CG1 ILE A 430 3528 4128 2410 715 287 858 C ATOM 3300 CG2 ILE A 430 -27.527 -53.340 -5.399 1.00 27.61 C ANISOU 3300 CG2 ILE A 430 3684 4465 2342 849 174 753 C ATOM 3301 CD1 ILE A 430 -30.006 -55.258 -6.097 1.00 29.72 C ANISOU 3301 CD1 ILE A 430 3962 4553 2775 766 375 987 C ATOM 3302 N ALA A 431 -27.909 -52.061 -8.961 1.00 24.10 N ANISOU 3302 N ALA A 431 3161 3786 2208 590 131 584 N ATOM 3303 CA ALA A 431 -28.252 -50.690 -9.333 1.00 23.63 C ANISOU 3303 CA ALA A 431 3084 3725 2167 545 108 484 C ATOM 3304 C ALA A 431 -29.436 -50.219 -8.500 1.00 23.96 C ANISOU 3304 C ALA A 431 3140 3811 2151 573 161 500 C ATOM 3305 O ALA A 431 -30.112 -51.022 -7.856 1.00 25.04 O ANISOU 3305 O ALA A 431 3295 3963 2255 610 225 598 O ATOM 3306 CB ALA A 431 -28.588 -50.619 -10.823 1.00 22.66 C ANISOU 3306 CB ALA A 431 2940 3501 2170 456 115 465 C ATOM 3307 N GLY A 432 -29.671 -48.911 -8.500 1.00 23.87 N ANISOU 3307 N GLY A 432 3122 3819 2128 557 138 407 N ATOM 3308 CA GLY A 432 -30.768 -48.323 -7.741 1.00 24.18 C ANISOU 3308 CA GLY A 432 3174 3903 2110 589 185 409 C ATOM 3309 C GLY A 432 -32.119 -48.368 -8.430 1.00 23.83 C ANISOU 3309 C GLY A 432 3114 3794 2148 535 252 450 C ATOM 3310 O GLY A 432 -32.208 -48.474 -9.657 1.00 23.40 O ANISOU 3310 O GLY A 432 3037 3656 2198 462 246 442 O ATOM 3311 N ARG A 433 -33.174 -48.295 -7.618 1.00 24.65 N ANISOU 3311 N ARG A 433 3226 3943 2197 576 316 494 N ATOM 3312 CA AARG A 433 -34.548 -48.245 -8.120 0.50 24.39 C ANISOU 3312 CA AARG A 433 3169 3864 2233 533 381 530 C ATOM 3313 CA BARG A 433 -34.547 -48.242 -8.111 0.50 24.28 C ANISOU 3313 CA BARG A 433 3156 3852 2218 533 381 530 C ATOM 3314 C ARG A 433 -34.829 -46.867 -8.716 1.00 24.00 C ANISOU 3314 C ARG A 433 3108 3796 2217 499 352 426 C ATOM 3315 O ARG A 433 -34.442 -45.842 -8.146 1.00 24.52 O ANISOU 3315 O ARG A 433 3191 3912 2213 538 314 342 O ATOM 3316 CB AARG A 433 -35.548 -48.554 -7.000 0.50 25.41 C ANISOU 3316 CB AARG A 433 3307 4058 2291 594 463 612 C ATOM 3317 CB BARG A 433 -35.517 -48.522 -6.964 0.50 25.24 C ANISOU 3317 CB BARG A 433 3287 4040 2264 596 461 609 C ATOM 3318 CG AARG A 433 -36.978 -48.785 -7.486 0.50 25.48 C ANISOU 3318 CG AARG A 433 3278 4021 2380 547 538 673 C ATOM 3319 CG BARG A 433 -36.904 -48.931 -7.404 0.50 24.86 C ANISOU 3319 CG BARG A 433 3203 3945 2296 552 540 683 C ATOM 3320 CD AARG A 433 -37.940 -49.111 -6.347 0.50 26.26 C ANISOU 3320 CD AARG A 433 3380 4188 2411 609 628 763 C ATOM 3321 CD BARG A 433 -37.793 -49.202 -6.210 0.50 25.09 C ANISOU 3321 CD BARG A 433 3238 4048 2248 619 626 768 C ATOM 3322 NE AARG A 433 -38.003 -48.056 -5.337 0.50 26.62 N ANISOU 3322 NE AARG A 433 3451 4328 2335 689 626 703 N ATOM 3323 NE BARG A 433 -38.913 -50.067 -6.556 0.50 23.99 N ANISOU 3323 NE BARG A 433 3060 3858 2197 573 705 871 N ATOM 3324 CZ AARG A 433 -38.765 -48.107 -4.247 0.50 26.76 C ANISOU 3324 CZ AARG A 433 3477 4424 2268 761 701 764 C ATOM 3325 CZ BARG A 433 -39.711 -50.652 -5.670 0.50 23.77 C ANISOU 3325 CZ BARG A 433 3027 3873 2132 615 796 977 C ATOM 3326 NH1AARG A 433 -39.542 -49.161 -4.028 0.50 27.43 N ANISOU 3326 NH1AARG A 433 3541 4499 2383 757 788 894 N ATOM 3327 NH1BARG A 433 -39.521 -50.467 -4.369 0.50 25.50 N ANISOU 3327 NH1BARG A 433 3283 4192 2213 714 819 996 N ATOM 3328 NH2AARG A 433 -38.759 -47.105 -3.378 0.50 25.53 N ANISOU 3328 NH2AARG A 433 3349 4353 1999 837 690 694 N ATOM 3329 NH2BARG A 433 -40.699 -51.426 -6.087 0.50 21.82 N ANISOU 3329 NH2BARG A 433 2736 3570 1986 559 863 1065 N ATOM 3330 N VAL A 434 -35.507 -46.845 -9.861 1.00 23.04 N ANISOU 3330 N VAL A 434 2955 3598 2201 430 368 431 N ATOM 3331 CA VAL A 434 -35.763 -45.598 -10.588 1.00 22.76 C ANISOU 3331 CA VAL A 434 2909 3533 2208 396 342 343 C ATOM 3332 C VAL A 434 -37.056 -44.912 -10.152 1.00 23.08 C ANISOU 3332 C VAL A 434 2940 3605 2225 424 397 344 C ATOM 3333 O VAL A 434 -37.056 -43.713 -9.880 1.00 23.56 O ANISOU 3333 O VAL A 434 3014 3689 2247 450 377 262 O ATOM 3334 CB VAL A 434 -35.766 -45.825 -12.111 1.00 21.78 C ANISOU 3334 CB VAL A 434 2758 3317 2201 317 323 339 C ATOM 3335 CG1 VAL A 434 -36.119 -44.532 -12.849 1.00 21.23 C ANISOU 3335 CG1 VAL A 434 2678 3217 2171 291 305 261 C ATOM 3336 CG2 VAL A 434 -34.405 -46.340 -12.555 1.00 22.08 C ANISOU 3336 CG2 VAL A 434 2805 3328 2257 297 267 326 C ATOM 3337 N ALA A 435 -38.151 -45.663 -10.094 1.00 23.24 N ANISOU 3337 N ALA A 435 2934 3623 2273 417 467 434 N ATOM 3338 CA ALA A 435 -39.408 -45.147 -9.544 1.00 23.77 C ANISOU 3338 CA ALA A 435 2986 3734 2312 453 530 451 C ATOM 3339 C ALA A 435 -39.362 -45.202 -8.018 1.00 24.66 C ANISOU 3339 C ALA A 435 3130 3942 2297 542 564 477 C ATOM 3340 O ALA A 435 -38.388 -45.692 -7.437 1.00 24.81 O ANISOU 3340 O ALA A 435 3181 3991 2256 573 536 487 O ATOM 3341 CB ALA A 435 -40.593 -45.950 -10.061 1.00 24.02 C ANISOU 3341 CB ALA A 435 2967 3731 2428 408 593 539 C ATOM 3342 N GLY A 436 -40.403 -44.686 -7.369 1.00 25.02 N ANISOU 3342 N GLY A 436 3168 4041 2298 590 624 488 N ATOM 3343 CA GLY A 436 -40.542 -44.801 -5.910 1.00 25.93 C ANISOU 3343 CA GLY A 436 3312 4255 2287 684 671 526 C ATOM 3344 C GLY A 436 -39.989 -43.645 -5.086 1.00 26.28 C ANISOU 3344 C GLY A 436 3404 4364 2218 758 627 419 C ATOM 3345 O GLY A 436 -40.201 -43.594 -3.870 1.00 27.48 O ANISOU 3345 O GLY A 436 3582 4605 2253 846 665 438 O ATOM 3346 N GLY A 437 -39.270 -42.732 -5.736 1.00 25.59 N ANISOU 3346 N GLY A 437 3329 4230 2165 723 547 306 N ATOM 3347 CA GLY A 437 -38.855 -41.473 -5.115 1.00 25.92 C ANISOU 3347 CA GLY A 437 3411 4313 2125 779 501 187 C ATOM 3348 C GLY A 437 -37.524 -41.509 -4.379 1.00 26.39 C ANISOU 3348 C GLY A 437 3511 4421 2096 818 431 134 C ATOM 3349 O GLY A 437 -37.015 -42.578 -4.023 1.00 26.08 O ANISOU 3349 O GLY A 437 3475 4410 2023 831 432 206 O ATOM 3350 N ARG A 438 -36.964 -40.315 -4.179 1.00 26.26 N ANISOU 3350 N ARG A 438 3522 4409 2046 836 367 5 N ATOM 3351 CA ARG A 438 -35.807 -40.096 -3.307 1.00 26.83 C ANISOU 3351 CA ARG A 438 3631 4543 2019 886 294 -71 C ATOM 3352 C ARG A 438 -34.665 -41.087 -3.530 1.00 26.39 C ANISOU 3352 C ARG A 438 3565 4481 1980 855 246 -31 C ATOM 3353 O ARG A 438 -34.176 -41.715 -2.588 1.00 27.20 O ANISOU 3353 O ARG A 438 3687 4665 1981 919 237 2 O ATOM 3354 CB ARG A 438 -36.255 -40.090 -1.845 1.00 28.16 C ANISOU 3354 CB ARG A 438 3835 4828 2035 1001 335 -57 C ATOM 3355 CG ARG A 438 -37.174 -38.927 -1.527 1.00 28.53 C ANISOU 3355 CG ARG A 438 3900 4888 2051 1045 367 -125 C ATOM 3356 CD ARG A 438 -37.726 -38.980 -0.121 1.00 30.55 C ANISOU 3356 CD ARG A 438 4190 5264 2153 1165 421 -101 C ATOM 3357 NE ARG A 438 -38.480 -37.767 0.199 1.00 31.04 N ANISOU 3357 NE ARG A 438 4274 5337 2181 1215 443 -186 N ATOM 3358 CZ ARG A 438 -39.235 -37.605 1.281 1.00 31.91 C ANISOU 3358 CZ ARG A 438 4412 5543 2169 1322 506 -171 C ATOM 3359 NH1 ARG A 438 -39.355 -38.582 2.175 1.00 32.60 N ANISOU 3359 NH1 ARG A 438 4508 5726 2153 1391 558 -67 N ATOM 3360 NH2 ARG A 438 -39.876 -36.455 1.473 1.00 32.97 N ANISOU 3360 NH2 ARG A 438 4566 5677 2283 1364 521 -257 N ATOM 3361 N ASN A 439 -34.233 -41.221 -4.777 1.00 25.28 N ANISOU 3361 N ASN A 439 3394 4248 1963 762 215 -34 N ATOM 3362 CA ASN A 439 -33.112 -42.115 -5.069 1.00 25.06 C ANISOU 3362 CA ASN A 439 3355 4210 1959 734 169 -3 C ATOM 3363 C ASN A 439 -32.116 -41.593 -6.110 1.00 24.63 C ANISOU 3363 C ASN A 439 3279 4079 1999 655 94 -83 C ATOM 3364 O ASN A 439 -31.317 -42.365 -6.626 1.00 24.10 O ANISOU 3364 O ASN A 439 3194 3987 1977 620 66 -48 O ATOM 3365 CB ASN A 439 -33.645 -43.502 -5.462 1.00 24.81 C ANISOU 3365 CB ASN A 439 3303 4151 1974 712 235 139 C ATOM 3366 CG ASN A 439 -32.673 -44.629 -5.132 1.00 25.04 C ANISOU 3366 CG ASN A 439 3336 4210 1967 734 210 197 C ATOM 3367 OD1 ASN A 439 -31.928 -44.564 -4.149 1.00 26.57 O ANISOU 3367 OD1 ASN A 439 3554 4486 2054 802 168 164 O ATOM 3368 ND2 ASN A 439 -32.684 -45.675 -5.950 1.00 25.31 N ANISOU 3368 ND2 ASN A 439 3349 4179 2088 682 234 282 N ATOM 3369 N VAL A 440 -32.135 -40.289 -6.391 1.00 24.58 N ANISOU 3369 N VAL A 440 3277 4037 2024 632 64 -189 N ATOM 3370 CA VAL A 440 -31.121 -39.675 -7.251 1.00 24.39 C ANISOU 3370 CA VAL A 440 3234 3947 2085 564 -5 -270 C ATOM 3371 C VAL A 440 -29.882 -39.344 -6.414 1.00 25.25 C ANISOU 3371 C VAL A 440 3352 4118 2123 596 -88 -358 C ATOM 3372 O VAL A 440 -29.978 -38.563 -5.471 1.00 25.69 O ANISOU 3372 O VAL A 440 3436 4226 2098 651 -109 -437 O ATOM 3373 CB VAL A 440 -31.644 -38.364 -7.892 1.00 24.31 C ANISOU 3373 CB VAL A 440 3226 3865 2144 526 0 -344 C ATOM 3374 CG1 VAL A 440 -30.526 -37.654 -8.652 1.00 24.24 C ANISOU 3374 CG1 VAL A 440 3200 3792 2217 459 -69 -428 C ATOM 3375 CG2 VAL A 440 -32.820 -38.649 -8.824 1.00 23.02 C ANISOU 3375 CG2 VAL A 440 3047 3644 2056 492 71 -264 C ATOM 3376 N PRO A 441 -28.716 -39.934 -6.744 1.00 25.68 N ANISOU 3376 N PRO A 441 3380 4170 2206 567 -139 -350 N ATOM 3377 CA PRO A 441 -27.532 -39.626 -5.937 1.00 26.90 C ANISOU 3377 CA PRO A 441 3534 4391 2295 599 -224 -437 C ATOM 3378 C PRO A 441 -27.162 -38.147 -6.024 1.00 27.35 C ANISOU 3378 C PRO A 441 3590 4410 2391 564 -279 -577 C ATOM 3379 O PRO A 441 -27.238 -37.562 -7.103 1.00 26.74 O ANISOU 3379 O PRO A 441 3496 4236 2427 489 -270 -597 O ATOM 3380 CB PRO A 441 -26.434 -40.504 -6.546 1.00 26.55 C ANISOU 3380 CB PRO A 441 3452 4334 2304 562 -259 -395 C ATOM 3381 CG PRO A 441 -26.925 -40.955 -7.837 1.00 25.54 C ANISOU 3381 CG PRO A 441 3307 4113 2285 496 -204 -318 C ATOM 3382 CD PRO A 441 -28.411 -40.833 -7.870 1.00 24.91 C ANISOU 3382 CD PRO A 441 3251 4010 2202 507 -126 -272 C ATOM 3383 N ILE A 442 -26.776 -37.550 -4.899 1.00 28.77 N ANISOU 3383 N ILE A 442 3790 4663 2477 620 -336 -673 N ATOM 3384 CA ILE A 442 -26.503 -36.110 -4.863 1.00 29.49 C ANISOU 3384 CA ILE A 442 3888 4715 2604 591 -387 -815 C ATOM 3385 C ILE A 442 -25.372 -35.712 -5.829 1.00 29.18 C ANISOU 3385 C ILE A 442 3798 4599 2689 496 -443 -866 C ATOM 3386 O ILE A 442 -25.357 -34.590 -6.340 1.00 28.56 O ANISOU 3386 O ILE A 442 3718 4438 2696 440 -455 -946 O ATOM 3387 CB ILE A 442 -26.219 -35.608 -3.423 1.00 31.27 C ANISOU 3387 CB ILE A 442 4143 5040 2697 673 -448 -919 C ATOM 3388 CG1 ILE A 442 -26.290 -34.076 -3.362 1.00 32.32 C ANISOU 3388 CG1 ILE A 442 4295 5116 2868 649 -482 -1062 C ATOM 3389 CG2 ILE A 442 -24.876 -36.121 -2.931 1.00 32.08 C ANISOU 3389 CG2 ILE A 442 4214 5220 2754 688 -534 -947 C ATOM 3390 CD1 ILE A 442 -26.708 -33.526 -2.019 1.00 34.27 C ANISOU 3390 CD1 ILE A 442 4595 5446 2978 746 -499 -1146 C ATOM 3391 N ALA A 443 -24.460 -36.644 -6.111 1.00 29.04 N ANISOU 3391 N ALA A 443 3739 4606 2687 479 -471 -813 N ATOM 3392 CA ALA A 443 -23.352 -36.390 -7.041 1.00 29.18 C ANISOU 3392 CA ALA A 443 3703 4561 2823 393 -516 -848 C ATOM 3393 C ALA A 443 -23.815 -35.908 -8.420 1.00 28.60 C ANISOU 3393 C ALA A 443 3622 4364 2882 312 -462 -822 C ATOM 3394 O ALA A 443 -23.092 -35.167 -9.086 1.00 29.06 O ANISOU 3394 O ALA A 443 3648 4356 3039 242 -494 -882 O ATOM 3395 CB ALA A 443 -22.481 -37.637 -7.192 1.00 29.14 C ANISOU 3395 CB ALA A 443 3659 4604 2809 400 -535 -772 C ATOM 3396 N VAL A 444 -25.006 -36.328 -8.844 1.00 27.93 N ANISOU 3396 N VAL A 444 3564 4249 2798 324 -381 -731 N ATOM 3397 CA VAL A 444 -25.560 -35.913 -10.138 1.00 27.44 C ANISOU 3397 CA VAL A 444 3499 4080 2849 260 -329 -700 C ATOM 3398 C VAL A 444 -26.812 -35.038 -9.981 1.00 27.59 C ANISOU 3398 C VAL A 444 3561 4066 2857 281 -283 -726 C ATOM 3399 O VAL A 444 -27.662 -34.994 -10.870 1.00 26.79 O ANISOU 3399 O VAL A 444 3464 3901 2814 257 -224 -670 O ATOM 3400 CB VAL A 444 -25.868 -37.134 -11.046 1.00 26.50 C ANISOU 3400 CB VAL A 444 3365 3941 2764 244 -276 -574 C ATOM 3401 CG1 VAL A 444 -24.585 -37.893 -11.374 1.00 27.18 C ANISOU 3401 CG1 VAL A 444 3408 4044 2876 220 -318 -553 C ATOM 3402 CG2 VAL A 444 -26.885 -38.061 -10.399 1.00 26.96 C ANISOU 3402 CG2 VAL A 444 3452 4057 2735 309 -225 -490 C ATOM 3403 N GLN A 445 -26.912 -34.323 -8.863 1.00 28.59 N ANISOU 3403 N GLN A 445 3718 4238 2909 331 -313 -815 N ATOM 3404 CA GLN A 445 -28.093 -33.495 -8.609 1.00 29.24 C ANISOU 3404 CA GLN A 445 3843 4296 2971 364 -269 -843 C ATOM 3405 C GLN A 445 -28.284 -32.404 -9.668 1.00 28.97 C ANISOU 3405 C GLN A 445 3807 4142 3057 300 -252 -878 C ATOM 3406 O GLN A 445 -29.419 -32.091 -10.030 1.00 28.84 O ANISOU 3406 O GLN A 445 3812 4087 3057 314 -191 -845 O ATOM 3407 CB GLN A 445 -28.065 -32.887 -7.196 1.00 30.35 C ANISOU 3407 CB GLN A 445 4019 4508 3003 435 -310 -945 C ATOM 3408 CG GLN A 445 -27.006 -31.816 -6.951 1.00 31.35 C ANISOU 3408 CG GLN A 445 4139 4606 3166 400 -395 -1087 C ATOM 3409 CD GLN A 445 -27.141 -31.169 -5.581 1.00 33.70 C ANISOU 3409 CD GLN A 445 4481 4971 3352 476 -434 -1196 C ATOM 3410 OE1 GLN A 445 -28.249 -31.006 -5.063 1.00 34.59 O ANISOU 3410 OE1 GLN A 445 4638 5111 3393 544 -382 -1184 O ATOM 3411 NE2 GLN A 445 -26.017 -30.789 -4.992 1.00 34.26 N ANISOU 3411 NE2 GLN A 445 4536 5073 3407 468 -526 -1306 N ATOM 3412 N ALA A 446 -27.183 -31.842 -10.168 1.00 29.29 N ANISOU 3412 N ALA A 446 3819 4126 3182 233 -303 -940 N ATOM 3413 CA ALA A 446 -27.252 -30.770 -11.173 1.00 29.45 C ANISOU 3413 CA ALA A 446 3840 4028 3322 173 -286 -970 C ATOM 3414 C ALA A 446 -27.829 -31.267 -12.500 1.00 28.53 C ANISOU 3414 C ALA A 446 3709 3858 3273 140 -221 -857 C ATOM 3415 O ALA A 446 -28.539 -30.530 -13.189 1.00 28.35 O ANISOU 3415 O ALA A 446 3704 3757 3309 128 -179 -850 O ATOM 3416 CB ALA A 446 -25.876 -30.140 -11.386 1.00 29.91 C ANISOU 3416 CB ALA A 446 3863 4041 3459 105 -352 -1053 C ATOM 3417 N VAL A 447 -27.529 -32.517 -12.847 1.00 28.19 N ANISOU 3417 N VAL A 447 3636 3855 3219 132 -215 -771 N ATOM 3418 CA VAL A 447 -28.066 -33.137 -14.058 1.00 27.59 C ANISOU 3418 CA VAL A 447 3547 3739 3196 107 -161 -668 C ATOM 3419 C VAL A 447 -29.565 -33.382 -13.923 1.00 27.07 C ANISOU 3419 C VAL A 447 3509 3692 3085 157 -100 -611 C ATOM 3420 O VAL A 447 -30.330 -33.121 -14.853 1.00 26.24 O ANISOU 3420 O VAL A 447 3406 3529 3035 142 -56 -571 O ATOM 3421 CB VAL A 447 -27.369 -34.479 -14.372 1.00 27.26 C ANISOU 3421 CB VAL A 447 3470 3738 3149 93 -172 -596 C ATOM 3422 CG1 VAL A 447 -27.916 -35.059 -15.663 1.00 27.63 C ANISOU 3422 CG1 VAL A 447 3507 3738 3253 67 -121 -504 C ATOM 3423 CG2 VAL A 447 -25.866 -34.293 -14.466 1.00 28.70 C ANISOU 3423 CG2 VAL A 447 3615 3914 3374 49 -231 -648 C ATOM 3424 N ALA A 448 -29.984 -33.874 -12.759 1.00 27.44 N ANISOU 3424 N ALA A 448 3572 3823 3030 219 -97 -606 N ATOM 3425 CA ALA A 448 -31.403 -34.082 -12.485 1.00 27.25 C ANISOU 3425 CA ALA A 448 3567 3825 2960 269 -37 -554 C ATOM 3426 C ALA A 448 -32.171 -32.761 -12.476 1.00 27.67 C ANISOU 3426 C ALA A 448 3650 3831 3033 287 -15 -613 C ATOM 3427 O ALA A 448 -33.271 -32.682 -13.021 1.00 27.63 O ANISOU 3427 O ALA A 448 3645 3800 3052 297 38 -564 O ATOM 3428 CB ALA A 448 -31.594 -34.830 -11.170 1.00 28.03 C ANISOU 3428 CB ALA A 448 3679 4028 2942 337 -34 -535 C ATOM 3429 N LYS A 449 -31.593 -31.721 -11.879 1.00 28.17 N ANISOU 3429 N LYS A 449 3735 3879 3087 293 -59 -722 N ATOM 3430 CA LYS A 449 -32.230 -30.405 -11.891 1.00 28.74 C ANISOU 3430 CA LYS A 449 3840 3892 3186 311 -41 -786 C ATOM 3431 C LYS A 449 -32.348 -29.863 -13.324 1.00 27.96 C ANISOU 3431 C LYS A 449 3731 3688 3206 254 -17 -759 C ATOM 3432 O LYS A 449 -33.361 -29.257 -13.685 1.00 27.57 O ANISOU 3432 O LYS A 449 3698 3598 3178 278 29 -746 O ATOM 3433 CB LYS A 449 -31.469 -29.418 -11.010 1.00 29.89 C ANISOU 3433 CB LYS A 449 4013 4033 3312 320 -100 -917 C ATOM 3434 CG LYS A 449 -32.183 -28.090 -10.830 1.00 30.57 C ANISOU 3434 CG LYS A 449 4143 4061 3413 352 -80 -991 C ATOM 3435 CD LYS A 449 -31.402 -27.149 -9.933 1.00 32.43 C ANISOU 3435 CD LYS A 449 4405 4288 3631 358 -145 -1131 C ATOM 3436 CE LYS A 449 -32.109 -25.819 -9.789 1.00 33.25 C ANISOU 3436 CE LYS A 449 4558 4321 3756 392 -123 -1207 C ATOM 3437 NZ LYS A 449 -32.206 -25.083 -11.082 1.00 33.22 N ANISOU 3437 NZ LYS A 449 4549 4189 3883 335 -94 -1184 N ATOM 3438 N ALA A 450 -31.313 -30.088 -14.127 1.00 27.60 N ANISOU 3438 N ALA A 450 3655 3603 3230 187 -45 -746 N ATOM 3439 CA ALA A 450 -31.324 -29.688 -15.541 1.00 27.37 C ANISOU 3439 CA ALA A 450 3613 3481 3304 136 -20 -709 C ATOM 3440 C ALA A 450 -32.445 -30.382 -16.323 1.00 26.69 C ANISOU 3440 C ALA A 450 3517 3404 3219 152 35 -605 C ATOM 3441 O ALA A 450 -33.050 -29.783 -17.213 1.00 26.64 O ANISOU 3441 O ALA A 450 3518 3335 3270 148 69 -583 O ATOM 3442 CB ALA A 450 -29.976 -29.988 -16.185 1.00 27.11 C ANISOU 3442 CB ALA A 450 3545 3423 3333 68 -57 -704 C ATOM 3443 N SER A 451 -32.719 -31.642 -15.996 1.00 26.23 N ANISOU 3443 N SER A 451 3441 3424 3103 171 44 -543 N ATOM 3444 CA SER A 451 -33.816 -32.366 -16.630 1.00 25.81 C ANISOU 3444 CA SER A 451 3372 3383 3051 183 91 -452 C ATOM 3445 C SER A 451 -35.154 -31.670 -16.383 1.00 25.67 C ANISOU 3445 C SER A 451 3374 3364 3016 235 135 -456 C ATOM 3446 O SER A 451 -35.989 -31.589 -17.281 1.00 25.67 O ANISOU 3446 O SER A 451 3363 3334 3057 235 169 -408 O ATOM 3447 CB SER A 451 -33.885 -33.811 -16.136 1.00 25.82 C ANISOU 3447 CB SER A 451 3353 3462 2994 195 95 -389 C ATOM 3448 OG SER A 451 -32.793 -34.561 -16.623 1.00 27.28 O ANISOU 3448 OG SER A 451 3517 3642 3206 149 63 -368 O ATOM 3449 N ILE A 452 -35.348 -31.167 -15.168 1.00 25.88 N ANISOU 3449 N ILE A 452 3427 3428 2977 286 132 -516 N ATOM 3450 CA ILE A 452 -36.563 -30.441 -14.828 1.00 25.93 C ANISOU 3450 CA ILE A 452 3454 3437 2961 345 175 -529 C ATOM 3451 C ILE A 452 -36.584 -29.091 -15.539 1.00 25.77 C ANISOU 3451 C ILE A 452 3457 3320 3016 335 177 -577 C ATOM 3452 O ILE A 452 -37.569 -28.747 -16.194 1.00 25.68 O ANISOU 3452 O ILE A 452 3441 3280 3035 356 217 -539 O ATOM 3453 CB ILE A 452 -36.702 -30.206 -13.308 1.00 26.72 C ANISOU 3453 CB ILE A 452 3584 3605 2964 410 172 -589 C ATOM 3454 CG1 ILE A 452 -36.793 -31.538 -12.556 1.00 26.76 C ANISOU 3454 CG1 ILE A 452 3569 3709 2889 431 181 -528 C ATOM 3455 CG2 ILE A 452 -37.938 -29.363 -13.012 1.00 27.24 C ANISOU 3455 CG2 ILE A 452 3671 3668 3011 477 219 -606 C ATOM 3456 CD1 ILE A 452 -36.672 -31.391 -11.050 1.00 27.22 C ANISOU 3456 CD1 ILE A 452 3659 3844 2840 497 169 -587 C ATOM 3457 N ASP A 453 -35.499 -28.333 -15.409 1.00 25.79 N ANISOU 3457 N ASP A 453 3480 3269 3049 304 133 -658 N ATOM 3458 CA ASP A 453 -35.438 -26.981 -15.976 1.00 26.14 C ANISOU 3458 CA ASP A 453 3553 3210 3170 293 137 -707 C ATOM 3459 C ASP A 453 -35.593 -26.994 -17.500 1.00 25.23 C ANISOU 3459 C ASP A 453 3417 3031 3137 256 162 -633 C ATOM 3460 O ASP A 453 -36.285 -26.145 -18.065 1.00 25.45 O ANISOU 3460 O ASP A 453 3463 3000 3207 280 195 -626 O ATOM 3461 CB ASP A 453 -34.131 -26.279 -15.590 1.00 26.73 C ANISOU 3461 CB ASP A 453 3644 3235 3276 252 83 -805 C ATOM 3462 CG ASP A 453 -34.040 -25.981 -14.098 1.00 28.32 C ANISOU 3462 CG ASP A 453 3875 3489 3395 300 53 -899 C ATOM 3463 OD1 ASP A 453 -35.093 -25.788 -13.460 1.00 29.80 O ANISOU 3463 OD1 ASP A 453 4087 3716 3520 373 87 -906 O ATOM 3464 OD2 ASP A 453 -32.905 -25.932 -13.568 1.00 29.91 O ANISOU 3464 OD2 ASP A 453 4074 3697 3592 267 -4 -969 O ATOM 3465 N GLN A 454 -34.963 -27.959 -18.159 1.00 24.62 N ANISOU 3465 N GLN A 454 3304 2971 3079 205 147 -577 N ATOM 3466 CA GLN A 454 -35.021 -28.023 -19.627 1.00 24.16 C ANISOU 3466 CA GLN A 454 3229 2861 3090 173 167 -509 C ATOM 3467 C GLN A 454 -36.387 -28.476 -20.153 1.00 23.43 C ANISOU 3467 C GLN A 454 3121 2801 2981 212 208 -434 C ATOM 3468 O GLN A 454 -36.826 -28.008 -21.204 1.00 22.59 O ANISOU 3468 O GLN A 454 3016 2645 2924 216 231 -399 O ATOM 3469 CB GLN A 454 -33.867 -28.857 -20.176 1.00 23.97 C ANISOU 3469 CB GLN A 454 3175 2842 3091 111 138 -481 C ATOM 3470 CG GLN A 454 -32.535 -28.133 -19.963 1.00 26.24 C ANISOU 3470 CG GLN A 454 3470 3077 3424 66 102 -553 C ATOM 3471 CD GLN A 454 -31.327 -28.930 -20.382 1.00 28.42 C ANISOU 3471 CD GLN A 454 3711 3367 3722 10 73 -530 C ATOM 3472 OE1 GLN A 454 -31.392 -30.143 -20.567 1.00 30.20 O ANISOU 3472 OE1 GLN A 454 3911 3651 3913 10 72 -472 O ATOM 3473 NE2 GLN A 454 -30.198 -28.240 -20.535 1.00 31.59 N ANISOU 3473 NE2 GLN A 454 4107 3711 4187 -38 51 -578 N ATOM 3474 N SER A 455 -37.066 -29.355 -19.414 1.00 23.24 N ANISOU 3474 N SER A 455 3078 2861 2889 242 217 -409 N ATOM 3475 CA SER A 455 -38.466 -29.691 -19.709 1.00 23.14 C ANISOU 3475 CA SER A 455 3045 2886 2863 282 256 -348 C ATOM 3476 C SER A 455 -39.336 -28.438 -19.747 1.00 23.13 C ANISOU 3476 C SER A 455 3069 2845 2877 336 287 -374 C ATOM 3477 O SER A 455 -40.183 -28.281 -20.629 1.00 22.58 O ANISOU 3477 O SER A 455 2983 2760 2836 355 311 -327 O ATOM 3478 CB SER A 455 -39.042 -30.657 -18.665 1.00 23.54 C ANISOU 3478 CB SER A 455 3075 3029 2840 310 269 -325 C ATOM 3479 OG SER A 455 -38.483 -31.950 -18.797 1.00 25.79 O ANISOU 3479 OG SER A 455 3333 3348 3117 267 250 -281 O ATOM 3480 N ARG A 456 -39.125 -27.552 -18.778 1.00 23.49 N ANISOU 3480 N ARG A 456 3152 2873 2899 365 283 -452 N ATOM 3481 CA ARG A 456 -39.891 -26.317 -18.684 1.00 24.10 C ANISOU 3481 CA ARG A 456 3262 2907 2989 424 312 -487 C ATOM 3482 C ARG A 456 -39.534 -25.367 -19.818 1.00 24.13 C ANISOU 3482 C ARG A 456 3287 2805 3078 401 313 -488 C ATOM 3483 O ARG A 456 -40.411 -24.746 -20.415 1.00 24.29 O ANISOU 3483 O ARG A 456 3312 2793 3123 444 346 -461 O ATOM 3484 CB ARG A 456 -39.643 -25.636 -17.339 1.00 24.74 C ANISOU 3484 CB ARG A 456 3385 2993 3023 459 302 -581 C ATOM 3485 CG ARG A 456 -40.111 -26.473 -16.159 1.00 25.14 C ANISOU 3485 CG ARG A 456 3420 3153 2977 499 311 -575 C ATOM 3486 CD ARG A 456 -39.769 -25.821 -14.844 1.00 25.63 C ANISOU 3486 CD ARG A 456 3529 3227 2983 539 294 -675 C ATOM 3487 NE ARG A 456 -40.169 -26.652 -13.713 1.00 25.57 N ANISOU 3487 NE ARG A 456 3510 3332 2875 583 307 -661 N ATOM 3488 CZ ARG A 456 -40.083 -26.276 -12.439 1.00 26.50 C ANISOU 3488 CZ ARG A 456 3664 3490 2915 637 299 -737 C ATOM 3489 NH1 ARG A 456 -39.596 -25.081 -12.117 1.00 27.11 N ANISOU 3489 NH1 ARG A 456 3793 3501 3009 648 271 -844 N ATOM 3490 NH2 ARG A 456 -40.488 -27.100 -11.479 1.00 25.96 N ANISOU 3490 NH2 ARG A 456 3584 3530 2752 681 320 -707 N ATOM 3491 N GLU A 457 -38.242 -25.263 -20.109 1.00 24.28 N ANISOU 3491 N GLU A 457 3315 2771 3140 337 280 -514 N ATOM 3492 CA GLU A 457 -37.763 -24.418 -21.202 1.00 24.84 C ANISOU 3492 CA GLU A 457 3403 2739 3296 308 286 -505 C ATOM 3493 C GLU A 457 -38.369 -24.857 -22.530 1.00 23.32 C ANISOU 3493 C GLU A 457 3182 2552 3124 313 309 -411 C ATOM 3494 O GLU A 457 -38.721 -24.018 -23.362 1.00 23.61 O ANISOU 3494 O GLU A 457 3238 2523 3208 336 335 -388 O ATOM 3495 CB GLU A 457 -36.245 -24.492 -21.293 1.00 25.37 C ANISOU 3495 CB GLU A 457 3468 2768 3403 232 249 -536 C ATOM 3496 CG GLU A 457 -35.634 -23.487 -22.244 1.00 29.01 C ANISOU 3496 CG GLU A 457 3950 3115 3958 200 261 -535 C ATOM 3497 CD GLU A 457 -34.189 -23.800 -22.552 1.00 32.80 C ANISOU 3497 CD GLU A 457 4408 3574 4482 120 231 -541 C ATOM 3498 OE1 GLU A 457 -33.778 -23.555 -23.709 1.00 34.27 O ANISOU 3498 OE1 GLU A 457 4590 3700 4731 91 250 -491 O ATOM 3499 OE2 GLU A 457 -33.476 -24.304 -21.643 1.00 35.25 O ANISOU 3499 OE2 GLU A 457 4704 3932 4758 93 190 -592 O ATOM 3500 N MET A 458 -38.498 -26.171 -22.703 1.00 21.82 N ANISOU 3500 N MET A 458 2950 2442 2899 294 298 -359 N ATOM 3501 CA MET A 458 -39.092 -26.759 -23.907 1.00 20.82 C ANISOU 3501 CA MET A 458 2792 2336 2784 297 310 -278 C ATOM 3502 C MET A 458 -40.629 -26.794 -23.863 1.00 20.80 C ANISOU 3502 C MET A 458 2769 2382 2751 363 338 -246 C ATOM 3503 O MET A 458 -41.256 -27.375 -24.748 1.00 19.72 O ANISOU 3503 O MET A 458 2598 2277 2617 368 341 -186 O ATOM 3504 CB MET A 458 -38.533 -28.170 -24.129 1.00 20.24 C ANISOU 3504 CB MET A 458 2682 2317 2693 246 283 -243 C ATOM 3505 CG MET A 458 -37.041 -28.190 -24.447 1.00 20.10 C ANISOU 3505 CG MET A 458 2672 2254 2711 184 259 -260 C ATOM 3506 SD MET A 458 -36.402 -29.815 -24.891 1.00 20.75 S ANISOU 3506 SD MET A 458 2715 2392 2777 135 232 -213 S ATOM 3507 CE MET A 458 -36.469 -30.675 -23.309 1.00 20.26 C ANISOU 3507 CE MET A 458 2640 2409 2647 140 215 -242 C ATOM 3508 N LYS A 459 -41.219 -26.167 -22.840 1.00 20.95 N ANISOU 3508 N LYS A 459 2807 2411 2742 414 356 -291 N ATOM 3509 CA LYS A 459 -42.679 -26.029 -22.696 1.00 21.44 C ANISOU 3509 CA LYS A 459 2849 2519 2778 484 389 -266 C ATOM 3510 C LYS A 459 -43.431 -27.361 -22.771 1.00 20.64 C ANISOU 3510 C LYS A 459 2685 2512 2646 477 389 -206 C ATOM 3511 O LYS A 459 -44.439 -27.491 -23.476 1.00 20.43 O ANISOU 3511 O LYS A 459 2621 2512 2629 507 402 -157 O ATOM 3512 CB LYS A 459 -43.239 -25.025 -23.718 1.00 21.83 C ANISOU 3512 CB LYS A 459 2914 2508 2873 528 410 -241 C ATOM 3513 CG LYS A 459 -42.659 -23.608 -23.617 1.00 23.16 C ANISOU 3513 CG LYS A 459 3146 2570 3083 542 420 -296 C ATOM 3514 CD LYS A 459 -42.869 -22.936 -22.256 1.00 24.85 C ANISOU 3514 CD LYS A 459 3395 2781 3266 585 432 -373 C ATOM 3515 CE LYS A 459 -44.342 -22.760 -21.877 1.00 26.03 C ANISOU 3515 CE LYS A 459 3526 2988 3377 673 469 -358 C ATOM 3516 NZ LYS A 459 -45.109 -21.828 -22.767 1.00 25.49 N ANISOU 3516 NZ LYS A 459 3469 2868 3348 735 498 -324 N ATOM 3517 N TYR A 460 -42.941 -28.349 -22.028 1.00 20.22 N ANISOU 3517 N TYR A 460 2617 2508 2557 439 373 -211 N ATOM 3518 CA TYR A 460 -43.635 -29.630 -21.917 1.00 19.95 C ANISOU 3518 CA TYR A 460 2526 2556 2498 429 379 -157 C ATOM 3519 C TYR A 460 -45.000 -29.437 -21.264 1.00 20.29 C ANISOU 3519 C TYR A 460 2543 2656 2511 496 420 -146 C ATOM 3520 O TYR A 460 -45.122 -28.710 -20.277 1.00 20.54 O ANISOU 3520 O TYR A 460 2606 2691 2509 543 441 -193 O ATOM 3521 CB TYR A 460 -42.853 -30.599 -21.040 1.00 19.96 C ANISOU 3521 CB TYR A 460 2526 2595 2461 389 362 -166 C ATOM 3522 CG TYR A 460 -41.749 -31.386 -21.704 1.00 19.65 C ANISOU 3522 CG TYR A 460 2485 2534 2447 320 324 -150 C ATOM 3523 CD1 TYR A 460 -41.027 -30.883 -22.789 1.00 19.55 C ANISOU 3523 CD1 TYR A 460 2493 2453 2484 293 305 -156 C ATOM 3524 CD2 TYR A 460 -41.396 -32.634 -21.206 1.00 20.84 C ANISOU 3524 CD2 TYR A 460 2615 2732 2570 287 313 -127 C ATOM 3525 CE1 TYR A 460 -39.994 -31.618 -23.362 1.00 19.50 C ANISOU 3525 CE1 TYR A 460 2483 2432 2496 236 275 -142 C ATOM 3526 CE2 TYR A 460 -40.375 -33.367 -21.761 1.00 20.36 C ANISOU 3526 CE2 TYR A 460 2554 2653 2530 232 281 -115 C ATOM 3527 CZ TYR A 460 -39.673 -32.866 -22.840 1.00 19.74 C ANISOU 3527 CZ TYR A 460 2492 2511 2497 207 261 -124 C ATOM 3528 OH TYR A 460 -38.652 -33.620 -23.384 1.00 19.96 O ANISOU 3528 OH TYR A 460 2516 2526 2542 158 234 -111 O ATOM 3529 N GLN A 461 -46.008 -30.115 -21.809 1.00 20.12 N ANISOU 3529 N GLN A 461 2460 2682 2502 499 430 -87 N ATOM 3530 CA GLN A 461 -47.285 -30.267 -21.142 1.00 20.67 C ANISOU 3530 CA GLN A 461 2484 2824 2546 549 471 -64 C ATOM 3531 C GLN A 461 -47.113 -31.128 -19.877 1.00 20.87 C ANISOU 3531 C GLN A 461 2502 2908 2520 537 487 -60 C ATOM 3532 O GLN A 461 -46.038 -31.680 -19.612 1.00 20.48 O ANISOU 3532 O GLN A 461 2478 2846 2457 488 460 -72 O ATOM 3533 CB GLN A 461 -48.324 -30.890 -22.087 1.00 20.62 C ANISOU 3533 CB GLN A 461 2405 2855 2576 543 471 -3 C ATOM 3534 CG GLN A 461 -48.656 -30.030 -23.298 1.00 21.40 C ANISOU 3534 CG GLN A 461 2507 2911 2713 573 458 0 C ATOM 3535 CD GLN A 461 -49.781 -30.602 -24.139 1.00 21.75 C ANISOU 3535 CD GLN A 461 2473 3006 2786 577 452 52 C ATOM 3536 OE1 GLN A 461 -50.763 -31.132 -23.609 1.00 22.85 O ANISOU 3536 OE1 GLN A 461 2548 3215 2918 590 479 80 O ATOM 3537 NE2 GLN A 461 -49.651 -30.493 -25.461 1.00 19.81 N ANISOU 3537 NE2 GLN A 461 2226 2728 2570 567 418 65 N ATOM 3538 N SER A 462 -48.181 -31.237 -19.102 1.00 21.51 N ANISOU 3538 N SER A 462 2545 3056 2570 585 534 -37 N ATOM 3539 CA SER A 462 -48.132 -31.879 -17.797 1.00 21.95 C ANISOU 3539 CA SER A 462 2600 3173 2566 593 562 -30 C ATOM 3540 C SER A 462 -48.107 -33.399 -17.879 1.00 21.55 C ANISOU 3540 C SER A 462 2500 3158 2529 530 558 35 C ATOM 3541 O SER A 462 -48.408 -33.981 -18.925 1.00 20.90 O ANISOU 3541 O SER A 462 2373 3064 2505 485 538 74 O ATOM 3542 CB SER A 462 -49.358 -31.477 -16.989 1.00 22.97 C ANISOU 3542 CB SER A 462 2702 3367 2660 673 623 -19 C ATOM 3543 OG SER A 462 -50.518 -32.102 -17.512 1.00 23.90 O ANISOU 3543 OG SER A 462 2734 3530 2819 665 647 50 O ATOM 3544 N LEU A 463 -47.779 -34.019 -16.745 1.00 21.38 N ANISOU 3544 N LEU A 463 2490 3180 2452 532 577 45 N ATOM 3545 CA LEU A 463 -47.836 -35.472 -16.575 1.00 21.06 C ANISOU 3545 CA LEU A 463 2407 3175 2419 483 588 113 C ATOM 3546 C LEU A 463 -49.157 -36.041 -17.076 1.00 21.45 C ANISOU 3546 C LEU A 463 2370 3257 2521 472 619 178 C ATOM 3547 O LEU A 463 -49.170 -36.992 -17.856 1.00 21.07 O ANISOU 3547 O LEU A 463 2284 3192 2530 408 596 217 O ATOM 3548 CB LEU A 463 -47.664 -35.841 -15.096 1.00 21.44 C ANISOU 3548 CB LEU A 463 2477 3284 2387 519 625 124 C ATOM 3549 CG LEU A 463 -48.054 -37.266 -14.678 1.00 21.74 C ANISOU 3549 CG LEU A 463 2465 3368 2427 489 662 211 C ATOM 3550 CD1 LEU A 463 -47.112 -38.274 -15.324 1.00 21.47 C ANISOU 3550 CD1 LEU A 463 2438 3288 2434 410 613 229 C ATOM 3551 CD2 LEU A 463 -48.068 -37.399 -13.153 1.00 22.27 C ANISOU 3551 CD2 LEU A 463 2555 3506 2400 548 712 225 C ATOM 3552 N ASN A 464 -50.262 -35.460 -16.619 1.00 22.30 N ANISOU 3552 N ASN A 464 2447 3414 2613 536 670 187 N ATOM 3553 CA ASN A 464 -51.585 -35.989 -16.967 1.00 22.92 C ANISOU 3553 CA ASN A 464 2430 3536 2743 529 704 250 C ATOM 3554 C ASN A 464 -51.937 -35.838 -18.451 1.00 22.64 C ANISOU 3554 C ASN A 464 2357 3462 2783 497 658 246 C ATOM 3555 O ASN A 464 -52.617 -36.695 -19.016 1.00 22.76 O ANISOU 3555 O ASN A 464 2296 3494 2857 452 656 293 O ATOM 3556 CB ASN A 464 -52.678 -35.412 -16.060 1.00 23.86 C ANISOU 3556 CB ASN A 464 2518 3725 2821 612 775 263 C ATOM 3557 CG ASN A 464 -52.791 -36.158 -14.730 1.00 24.75 C ANISOU 3557 CG ASN A 464 2624 3902 2878 627 837 312 C ATOM 3558 OD1 ASN A 464 -52.240 -37.254 -14.567 1.00 24.03 O ANISOU 3558 OD1 ASN A 464 2533 3804 2792 569 829 350 O ATOM 3559 ND2 ASN A 464 -53.513 -35.572 -13.779 1.00 24.05 N ANISOU 3559 ND2 ASN A 464 2529 3877 2733 712 902 314 N ATOM 3560 N GLU A 465 -51.464 -34.775 -19.094 1.00 22.55 N ANISOU 3560 N GLU A 465 2398 3398 2771 521 621 189 N ATOM 3561 CA GLU A 465 -51.611 -34.668 -20.545 1.00 22.30 C ANISOU 3561 CA GLU A 465 2344 3330 2801 494 573 187 C ATOM 3562 C GLU A 465 -50.830 -35.790 -21.244 1.00 21.18 C ANISOU 3562 C GLU A 465 2202 3152 2694 407 524 202 C ATOM 3563 O GLU A 465 -51.327 -36.392 -22.196 1.00 21.21 O ANISOU 3563 O GLU A 465 2149 3158 2751 370 498 226 O ATOM 3564 CB GLU A 465 -51.158 -33.297 -21.059 1.00 22.37 C ANISOU 3564 CB GLU A 465 2417 3281 2801 538 550 132 C ATOM 3565 CG GLU A 465 -52.041 -32.127 -20.622 1.00 24.82 C ANISOU 3565 CG GLU A 465 2725 3616 3089 630 592 115 C ATOM 3566 CD GLU A 465 -53.503 -32.298 -21.003 1.00 27.95 C ANISOU 3566 CD GLU A 465 3025 4073 3520 657 615 161 C ATOM 3567 OE1 GLU A 465 -53.791 -32.747 -22.130 1.00 30.47 O ANISOU 3567 OE1 GLU A 465 3297 4390 3891 620 576 184 O ATOM 3568 OE2 GLU A 465 -54.374 -31.987 -20.169 1.00 32.16 O ANISOU 3568 OE2 GLU A 465 3527 4663 4028 718 670 173 O ATOM 3569 N TYR A 466 -49.618 -36.073 -20.774 1.00 20.47 N ANISOU 3569 N TYR A 466 2174 3032 2572 379 510 183 N ATOM 3570 CA TYR A 466 -48.828 -37.182 -21.322 1.00 19.76 C ANISOU 3570 CA TYR A 466 2088 2910 2511 305 470 197 C ATOM 3571 C TYR A 466 -49.451 -38.543 -21.036 1.00 20.11 C ANISOU 3571 C TYR A 466 2067 2990 2583 261 492 257 C ATOM 3572 O TYR A 466 -49.416 -39.435 -21.887 1.00 19.85 O ANISOU 3572 O TYR A 466 2006 2935 2602 204 458 274 O ATOM 3573 CB TYR A 466 -47.369 -37.123 -20.851 1.00 19.05 C ANISOU 3573 CB TYR A 466 2075 2784 2380 291 450 163 C ATOM 3574 CG TYR A 466 -46.585 -36.157 -21.702 1.00 18.64 C ANISOU 3574 CG TYR A 466 2074 2671 2337 296 410 113 C ATOM 3575 CD1 TYR A 466 -46.214 -36.502 -22.994 1.00 18.35 C ANISOU 3575 CD1 TYR A 466 2033 2595 2343 254 367 116 C ATOM 3576 CD2 TYR A 466 -46.277 -34.878 -21.249 1.00 18.94 C ANISOU 3576 CD2 TYR A 466 2163 2690 2342 345 420 64 C ATOM 3577 CE1 TYR A 466 -45.530 -35.616 -23.803 1.00 18.93 C ANISOU 3577 CE1 TYR A 466 2151 2616 2426 261 340 81 C ATOM 3578 CE2 TYR A 466 -45.586 -33.980 -22.053 1.00 18.74 C ANISOU 3578 CE2 TYR A 466 2182 2603 2337 346 390 25 C ATOM 3579 CZ TYR A 466 -45.217 -34.355 -23.329 1.00 19.05 C ANISOU 3579 CZ TYR A 466 2214 2607 2418 304 353 39 C ATOM 3580 OH TYR A 466 -44.536 -33.475 -24.141 1.00 19.23 O ANISOU 3580 OH TYR A 466 2278 2569 2459 307 332 12 O ATOM 3581 N ARG A 467 -50.030 -38.707 -19.854 1.00 20.85 N ANISOU 3581 N ARG A 467 2138 3138 2646 290 551 290 N ATOM 3582 CA ARG A 467 -50.746 -39.943 -19.552 1.00 21.66 C ANISOU 3582 CA ARG A 467 2171 3272 2785 250 584 356 C ATOM 3583 C ARG A 467 -51.904 -40.158 -20.536 1.00 21.99 C ANISOU 3583 C ARG A 467 2125 3326 2903 227 571 375 C ATOM 3584 O ARG A 467 -52.029 -41.233 -21.128 1.00 22.20 O ANISOU 3584 O ARG A 467 2111 3334 2992 160 548 400 O ATOM 3585 CB ARG A 467 -51.212 -39.965 -18.094 1.00 22.59 C ANISOU 3585 CB ARG A 467 2280 3453 2851 297 659 394 C ATOM 3586 CG ARG A 467 -50.085 -40.335 -17.139 1.00 22.63 C ANISOU 3586 CG ARG A 467 2354 3452 2791 299 665 394 C ATOM 3587 CD ARG A 467 -50.515 -40.386 -15.684 1.00 24.10 C ANISOU 3587 CD ARG A 467 2537 3708 2911 354 741 434 C ATOM 3588 NE ARG A 467 -51.519 -41.412 -15.394 1.00 25.43 N ANISOU 3588 NE ARG A 467 2625 3913 3125 327 798 520 N ATOM 3589 CZ ARG A 467 -51.273 -42.706 -15.171 1.00 25.50 C ANISOU 3589 CZ ARG A 467 2622 3908 3160 274 812 581 C ATOM 3590 NH1 ARG A 467 -50.040 -43.198 -15.227 1.00 25.28 N ANISOU 3590 NH1 ARG A 467 2657 3835 3114 245 769 567 N ATOM 3591 NH2 ARG A 467 -52.286 -43.523 -14.900 1.00 25.86 N ANISOU 3591 NH2 ARG A 467 2587 3982 3255 250 872 661 N ATOM 3592 N LYS A 468 -52.716 -39.127 -20.750 1.00 22.46 N ANISOU 3592 N LYS A 468 2158 3416 2960 284 582 357 N ATOM 3593 CA LYS A 468 -53.807 -39.217 -21.727 1.00 23.07 C ANISOU 3593 CA LYS A 468 2150 3513 3104 271 562 369 C ATOM 3594 C LYS A 468 -53.315 -39.550 -23.136 1.00 22.44 C ANISOU 3594 C LYS A 468 2080 3380 3066 221 484 340 C ATOM 3595 O LYS A 468 -53.922 -40.365 -23.840 1.00 22.50 O ANISOU 3595 O LYS A 468 2017 3393 3137 171 457 357 O ATOM 3596 CB LYS A 468 -54.631 -37.926 -21.740 1.00 23.92 C ANISOU 3596 CB LYS A 468 2239 3658 3192 355 583 351 C ATOM 3597 CG LYS A 468 -55.513 -37.770 -20.508 1.00 25.46 C ANISOU 3597 CG LYS A 468 2391 3922 3362 405 665 388 C ATOM 3598 CD LYS A 468 -56.556 -36.694 -20.677 1.00 27.86 C ANISOU 3598 CD LYS A 468 2651 4269 3664 484 685 379 C ATOM 3599 CE LYS A 468 -55.956 -35.309 -20.625 1.00 28.52 C ANISOU 3599 CE LYS A 468 2830 4318 3690 557 677 321 C ATOM 3600 NZ LYS A 468 -57.024 -34.264 -20.651 1.00 28.77 N ANISOU 3600 NZ LYS A 468 2822 4392 3717 645 707 317 N ATOM 3601 N ARG A 469 -52.206 -38.928 -23.529 1.00 21.81 N ANISOU 3601 N ARG A 469 2087 3250 2950 234 448 296 N ATOM 3602 CA ARG A 469 -51.592 -39.147 -24.843 1.00 21.30 C ANISOU 3602 CA ARG A 469 2045 3136 2910 198 380 269 C ATOM 3603 C ARG A 469 -51.225 -40.619 -25.084 1.00 21.34 C ANISOU 3603 C ARG A 469 2035 3118 2957 117 355 287 C ATOM 3604 O ARG A 469 -51.290 -41.095 -26.219 1.00 20.81 O ANISOU 3604 O ARG A 469 1946 3031 2928 83 302 274 O ATOM 3605 CB ARG A 469 -50.362 -38.240 -24.992 1.00 20.66 C ANISOU 3605 CB ARG A 469 2061 3006 2783 224 362 227 C ATOM 3606 CG ARG A 469 -49.455 -38.541 -26.183 1.00 20.81 C ANISOU 3606 CG ARG A 469 2117 2974 2817 187 303 205 C ATOM 3607 CD ARG A 469 -50.133 -38.302 -27.522 1.00 21.97 C ANISOU 3607 CD ARG A 469 2226 3128 2992 201 262 197 C ATOM 3608 NE ARG A 469 -49.164 -38.540 -28.596 1.00 22.47 N ANISOU 3608 NE ARG A 469 2335 3145 3057 175 212 176 N ATOM 3609 CZ ARG A 469 -48.812 -39.741 -29.059 1.00 22.72 C ANISOU 3609 CZ ARG A 469 2357 3161 3114 116 179 177 C ATOM 3610 NH1 ARG A 469 -49.359 -40.852 -28.575 1.00 22.22 N ANISOU 3610 NH1 ARG A 469 2240 3117 3087 70 188 200 N ATOM 3611 NH2 ARG A 469 -47.898 -39.834 -30.021 1.00 23.29 N ANISOU 3611 NH2 ARG A 469 2476 3195 3179 105 139 157 N ATOM 3612 N PHE A 470 -50.867 -41.330 -24.014 1.00 21.49 N ANISOU 3612 N PHE A 470 2066 3136 2963 93 393 317 N ATOM 3613 CA PHE A 470 -50.531 -42.751 -24.093 1.00 21.77 C ANISOU 3613 CA PHE A 470 2091 3142 3039 22 379 341 C ATOM 3614 C PHE A 470 -51.598 -43.671 -23.485 1.00 23.09 C ANISOU 3614 C PHE A 470 2174 3342 3256 -12 424 398 C ATOM 3615 O PHE A 470 -51.298 -44.767 -23.019 1.00 22.95 O ANISOU 3615 O PHE A 470 2159 3302 3260 -58 441 434 O ATOM 3616 CB PHE A 470 -49.138 -42.974 -23.489 1.00 21.27 C ANISOU 3616 CB PHE A 470 2111 3044 2928 16 382 336 C ATOM 3617 CG PHE A 470 -48.035 -42.433 -24.356 1.00 20.26 C ANISOU 3617 CG PHE A 470 2049 2871 2778 23 329 285 C ATOM 3618 CD1 PHE A 470 -47.435 -43.238 -25.315 1.00 19.66 C ANISOU 3618 CD1 PHE A 470 1986 2751 2734 -24 280 273 C ATOM 3619 CD2 PHE A 470 -47.632 -41.106 -24.251 1.00 20.54 C ANISOU 3619 CD2 PHE A 470 2133 2907 2765 77 332 250 C ATOM 3620 CE1 PHE A 470 -46.454 -42.739 -26.136 1.00 19.11 C ANISOU 3620 CE1 PHE A 470 1972 2646 2645 -15 240 233 C ATOM 3621 CE2 PHE A 470 -46.647 -40.596 -25.070 1.00 19.34 C ANISOU 3621 CE2 PHE A 470 2035 2712 2602 79 291 211 C ATOM 3622 CZ PHE A 470 -46.047 -41.412 -26.013 1.00 19.13 C ANISOU 3622 CZ PHE A 470 2017 2649 2602 35 247 205 C ATOM 3623 N SER A 471 -52.851 -43.219 -23.532 1.00 24.22 N ANISOU 3623 N SER A 471 2241 3537 3424 13 445 409 N ATOM 3624 CA SER A 471 -54.025 -44.034 -23.185 1.00 25.93 C ANISOU 3624 CA SER A 471 2358 3788 3707 -24 483 462 C ATOM 3625 C SER A 471 -54.088 -44.440 -21.717 1.00 26.34 C ANISOU 3625 C SER A 471 2409 3865 3734 -17 566 524 C ATOM 3626 O SER A 471 -54.636 -45.497 -21.379 1.00 26.81 O ANISOU 3626 O SER A 471 2406 3925 3854 -69 600 579 O ATOM 3627 CB SER A 471 -54.112 -45.278 -24.080 1.00 26.37 C ANISOU 3627 CB SER A 471 2372 3799 3847 -109 432 460 C ATOM 3628 OG SER A 471 -53.955 -44.925 -25.442 1.00 28.40 O ANISOU 3628 OG SER A 471 2640 4038 4112 -108 353 400 O ATOM 3629 N LEU A 472 -53.550 -43.588 -20.849 1.00 25.97 N ANISOU 3629 N LEU A 472 2430 3839 3599 50 600 516 N ATOM 3630 CA LEU A 472 -53.563 -43.830 -19.411 1.00 26.51 C ANISOU 3630 CA LEU A 472 2508 3941 3621 76 679 570 C ATOM 3631 C LEU A 472 -54.556 -42.887 -18.752 1.00 27.38 C ANISOU 3631 C LEU A 472 2577 4126 3698 150 738 582 C ATOM 3632 O LEU A 472 -54.805 -41.781 -19.248 1.00 27.31 O ANISOU 3632 O LEU A 472 2573 4131 3673 198 714 533 O ATOM 3633 CB LEU A 472 -52.174 -43.604 -18.817 1.00 25.72 C ANISOU 3633 CB LEU A 472 2518 3817 3438 103 670 545 C ATOM 3634 CG LEU A 472 -51.015 -44.278 -19.553 1.00 24.14 C ANISOU 3634 CG LEU A 472 2371 3544 3258 48 605 520 C ATOM 3635 CD1 LEU A 472 -49.688 -43.935 -18.891 1.00 23.63 C ANISOU 3635 CD1 LEU A 472 2402 3468 3109 82 598 494 C ATOM 3636 CD2 LEU A 472 -51.229 -45.779 -19.618 1.00 24.03 C ANISOU 3636 CD2 LEU A 472 2313 3501 3317 -26 615 577 C ATOM 3637 N LYS A 473 -55.111 -43.323 -17.629 1.00 28.47 N ANISOU 3637 N LYS A 473 2679 4313 3825 163 820 650 N ATOM 3638 CA LYS A 473 -56.056 -42.502 -16.873 1.00 29.68 C ANISOU 3638 CA LYS A 473 2793 4545 3940 241 889 667 C ATOM 3639 C LYS A 473 -55.307 -41.419 -16.108 1.00 28.71 C ANISOU 3639 C LYS A 473 2770 4436 3702 328 899 620 C ATOM 3640 O LYS A 473 -54.332 -41.723 -15.427 1.00 28.32 O ANISOU 3640 O LYS A 473 2794 4371 3594 330 903 622 O ATOM 3641 CB LYS A 473 -56.844 -43.355 -15.876 1.00 31.21 C ANISOU 3641 CB LYS A 473 2917 4788 4153 231 982 762 C ATOM 3642 CG LYS A 473 -57.998 -44.136 -16.488 1.00 34.33 C ANISOU 3642 CG LYS A 473 3185 5190 4670 161 990 808 C ATOM 3643 CD LYS A 473 -58.691 -45.045 -15.468 1.00 37.72 C ANISOU 3643 CD LYS A 473 3545 5659 5127 143 1091 912 C ATOM 3644 CE LYS A 473 -59.221 -44.277 -14.252 1.00 40.29 C ANISOU 3644 CE LYS A 473 3868 6076 5365 245 1185 945 C ATOM 3645 NZ LYS A 473 -58.201 -44.151 -13.162 1.00 41.13 N ANISOU 3645 NZ LYS A 473 4088 6188 5350 303 1215 948 N ATOM 3646 N PRO A 474 -55.766 -40.157 -16.192 1.00 28.48 N ANISOU 3646 N PRO A 474 2742 4437 3642 401 902 575 N ATOM 3647 CA PRO A 474 -55.121 -39.117 -15.385 1.00 28.04 C ANISOU 3647 CA PRO A 474 2780 4392 3482 484 914 525 C ATOM 3648 C PRO A 474 -55.148 -39.434 -13.891 1.00 28.48 C ANISOU 3648 C PRO A 474 2851 4507 3462 528 994 572 C ATOM 3649 O PRO A 474 -56.148 -39.959 -13.391 1.00 28.66 O ANISOU 3649 O PRO A 474 2794 4588 3507 533 1066 646 O ATOM 3650 CB PRO A 474 -55.966 -37.869 -15.669 1.00 28.47 C ANISOU 3650 CB PRO A 474 2809 4475 3534 556 923 489 C ATOM 3651 CG PRO A 474 -56.613 -38.130 -16.970 1.00 28.91 C ANISOU 3651 CG PRO A 474 2785 4513 3687 504 879 496 C ATOM 3652 CD PRO A 474 -56.837 -39.608 -17.043 1.00 28.84 C ANISOU 3652 CD PRO A 474 2710 4504 3745 415 889 564 C ATOM 3653 N TYR A 475 -54.059 -39.124 -13.192 1.00 27.94 N ANISOU 3653 N TYR A 475 2882 4429 3306 562 981 532 N ATOM 3654 CA TYR A 475 -54.037 -39.229 -11.732 1.00 28.63 C ANISOU 3654 CA TYR A 475 2997 4582 3298 626 1052 565 C ATOM 3655 C TYR A 475 -54.945 -38.161 -11.131 1.00 29.49 C ANISOU 3655 C TYR A 475 3092 4758 3356 727 1110 547 C ATOM 3656 O TYR A 475 -54.969 -37.018 -11.602 1.00 28.79 O ANISOU 3656 O TYR A 475 3030 4646 3264 765 1075 472 O ATOM 3657 CB TYR A 475 -52.613 -39.080 -11.178 1.00 28.16 C ANISOU 3657 CB TYR A 475 3046 4499 3153 642 1010 511 C ATOM 3658 CG TYR A 475 -51.748 -40.309 -11.355 1.00 27.48 C ANISOU 3658 CG TYR A 475 2976 4371 3095 564 978 551 C ATOM 3659 CD1 TYR A 475 -50.562 -40.256 -12.083 1.00 26.03 C ANISOU 3659 CD1 TYR A 475 2847 4114 2927 517 892 491 C ATOM 3660 CD2 TYR A 475 -52.113 -41.525 -10.789 1.00 28.25 C ANISOU 3660 CD2 TYR A 475 3030 4499 3204 540 1039 651 C ATOM 3661 CE1 TYR A 475 -49.760 -41.389 -12.243 1.00 25.13 C ANISOU 3661 CE1 TYR A 475 2747 3962 2837 454 865 526 C ATOM 3662 CE2 TYR A 475 -51.326 -42.658 -10.946 1.00 27.59 C ANISOU 3662 CE2 TYR A 475 2964 4371 3148 475 1013 689 C ATOM 3663 CZ TYR A 475 -50.151 -42.584 -11.674 1.00 26.51 C ANISOU 3663 CZ TYR A 475 2884 4164 3023 434 924 623 C ATOM 3664 OH TYR A 475 -49.374 -43.712 -11.825 1.00 26.02 O ANISOU 3664 OH TYR A 475 2839 4059 2988 377 900 660 O ATOM 3665 N THR A 476 -55.697 -38.549 -10.100 1.00 30.64 N ANISOU 3665 N THR A 476 3196 4984 3462 772 1203 619 N ATOM 3666 CA THR A 476 -56.658 -37.659 -9.440 1.00 31.84 C ANISOU 3666 CA THR A 476 3324 5211 3561 875 1273 614 C ATOM 3667 C THR A 476 -56.121 -37.044 -8.145 1.00 32.09 C ANISOU 3667 C THR A 476 3450 5290 3452 975 1302 572 C ATOM 3668 O THR A 476 -56.752 -36.153 -7.574 1.00 32.91 O ANISOU 3668 O THR A 476 3557 5449 3497 1073 1351 546 O ATOM 3669 CB THR A 476 -57.978 -38.401 -9.133 1.00 33.01 C ANISOU 3669 CB THR A 476 3354 5430 3757 870 1368 725 C ATOM 3670 OG1 THR A 476 -57.701 -39.568 -8.350 1.00 34.50 O ANISOU 3670 OG1 THR A 476 3544 5642 3922 842 1417 809 O ATOM 3671 CG2 THR A 476 -58.667 -38.813 -10.428 1.00 33.34 C ANISOU 3671 CG2 THR A 476 3294 5434 3938 783 1334 749 C ATOM 3672 N SER A 477 -54.967 -37.519 -7.680 1.00 31.46 N ANISOU 3672 N SER A 477 3446 5192 3315 956 1269 561 N ATOM 3673 CA SER A 477 -54.309 -36.939 -6.509 1.00 31.80 C ANISOU 3673 CA SER A 477 3584 5277 3221 1047 1277 505 C ATOM 3674 C SER A 477 -52.819 -37.254 -6.518 1.00 30.78 C ANISOU 3674 C SER A 477 3536 5095 3062 1002 1196 460 C ATOM 3675 O SER A 477 -52.361 -38.137 -7.248 1.00 29.58 O ANISOU 3675 O SER A 477 3365 4887 2988 907 1155 496 O ATOM 3676 CB SER A 477 -54.929 -37.472 -5.211 1.00 33.04 C ANISOU 3676 CB SER A 477 3719 5541 3295 1118 1385 593 C ATOM 3677 OG SER A 477 -54.532 -38.814 -4.969 1.00 33.35 O ANISOU 3677 OG SER A 477 3747 5581 3345 1059 1401 684 O ATOM 3678 N PHE A 478 -52.070 -36.542 -5.685 1.00 31.01 N ANISOU 3678 N PHE A 478 3656 5147 2980 1075 1173 379 N ATOM 3679 CA PHE A 478 -50.643 -36.815 -5.530 1.00 30.70 C ANISOU 3679 CA PHE A 478 3690 5075 2901 1044 1098 335 C ATOM 3680 C PHE A 478 -50.412 -38.134 -4.796 1.00 31.25 C ANISOU 3680 C PHE A 478 3752 5193 2927 1036 1140 436 C ATOM 3681 O PHE A 478 -49.455 -38.838 -5.093 1.00 30.49 O ANISOU 3681 O PHE A 478 3677 5054 2854 972 1085 445 O ATOM 3682 CB PHE A 478 -49.937 -35.664 -4.818 1.00 31.07 C ANISOU 3682 CB PHE A 478 3830 5134 2843 1124 1057 212 C ATOM 3683 CG PHE A 478 -49.884 -34.408 -5.632 1.00 30.87 C ANISOU 3683 CG PHE A 478 3824 5032 2872 1118 1003 109 C ATOM 3684 CD1 PHE A 478 -50.889 -33.456 -5.526 1.00 32.20 C ANISOU 3684 CD1 PHE A 478 3980 5222 3033 1191 1050 82 C ATOM 3685 CD2 PHE A 478 -48.846 -34.188 -6.525 1.00 30.61 C ANISOU 3685 CD2 PHE A 478 3822 4906 2903 1042 910 46 C ATOM 3686 CE1 PHE A 478 -50.848 -32.295 -6.284 1.00 31.90 C ANISOU 3686 CE1 PHE A 478 3965 5108 3048 1190 1004 -7 C ATOM 3687 CE2 PHE A 478 -48.800 -33.027 -7.287 1.00 30.00 C ANISOU 3687 CE2 PHE A 478 3765 4753 2879 1037 868 -39 C ATOM 3688 CZ PHE A 478 -49.804 -32.081 -7.160 1.00 30.58 C ANISOU 3688 CZ PHE A 478 3831 4844 2944 1112 915 -65 C ATOM 3689 N GLU A 479 -51.298 -38.479 -3.863 1.00 32.63 N ANISOU 3689 N GLU A 479 3896 5459 3043 1102 1240 518 N ATOM 3690 CA GLU A 479 -51.220 -39.777 -3.189 1.00 33.56 C ANISOU 3690 CA GLU A 479 4000 5621 3129 1096 1295 634 C ATOM 3691 C GLU A 479 -51.431 -40.948 -4.157 1.00 33.17 C ANISOU 3691 C GLU A 479 3878 5505 3220 977 1296 725 C ATOM 3692 O GLU A 479 -50.782 -41.988 -4.015 1.00 33.01 O ANISOU 3692 O GLU A 479 3872 5469 3202 938 1288 784 O ATOM 3693 CB GLU A 479 -52.198 -39.853 -2.010 1.00 35.31 C ANISOU 3693 CB GLU A 479 4200 5956 3262 1195 1414 710 C ATOM 3694 CG GLU A 479 -51.819 -38.919 -0.863 1.00 36.67 C ANISOU 3694 CG GLU A 479 4458 6204 3270 1322 1413 625 C ATOM 3695 CD GLU A 479 -52.592 -39.177 0.421 1.00 40.13 C ANISOU 3695 CD GLU A 479 4887 6765 3597 1429 1533 711 C ATOM 3696 OE1 GLU A 479 -53.514 -40.023 0.427 1.00 40.57 O ANISOU 3696 OE1 GLU A 479 4860 6845 3709 1404 1627 843 O ATOM 3697 OE2 GLU A 479 -52.267 -38.521 1.432 1.00 41.99 O ANISOU 3697 OE2 GLU A 479 5198 7073 3686 1541 1533 645 O ATOM 3698 N GLU A 480 -52.310 -40.783 -5.148 1.00 32.93 N ANISOU 3698 N GLU A 480 3771 5435 3306 923 1301 732 N ATOM 3699 CA GLU A 480 -52.477 -41.819 -6.175 1.00 32.70 C ANISOU 3699 CA GLU A 480 3674 5334 3414 807 1286 797 C ATOM 3700 C GLU A 480 -51.196 -42.006 -6.990 1.00 31.19 C ANISOU 3700 C GLU A 480 3537 5055 3260 736 1178 736 C ATOM 3701 O GLU A 480 -50.805 -43.135 -7.281 1.00 30.99 O ANISOU 3701 O GLU A 480 3500 4987 3289 666 1167 795 O ATOM 3702 CB GLU A 480 -53.638 -41.519 -7.122 1.00 32.93 C ANISOU 3702 CB GLU A 480 3611 5345 3555 768 1298 802 C ATOM 3703 CG GLU A 480 -54.031 -42.743 -7.962 1.00 34.38 C ANISOU 3703 CG GLU A 480 3714 5475 3875 657 1301 883 C ATOM 3704 CD GLU A 480 -55.122 -42.478 -8.989 1.00 36.99 C ANISOU 3704 CD GLU A 480 3948 5788 4318 614 1297 879 C ATOM 3705 OE1 GLU A 480 -55.675 -43.469 -9.507 1.00 39.86 O ANISOU 3705 OE1 GLU A 480 4231 6124 4790 532 1314 950 O ATOM 3706 OE2 GLU A 480 -55.419 -41.303 -9.295 1.00 37.22 O ANISOU 3706 OE2 GLU A 480 3981 5828 4331 662 1275 805 O ATOM 3707 N LEU A 481 -50.559 -40.895 -7.355 1.00 30.11 N ANISOU 3707 N LEU A 481 3455 4887 3097 754 1103 618 N ATOM 3708 CA LEU A 481 -49.283 -40.924 -8.083 1.00 28.91 C ANISOU 3708 CA LEU A 481 3354 4658 2972 696 1003 554 C ATOM 3709 C LEU A 481 -48.197 -41.711 -7.345 1.00 28.94 C ANISOU 3709 C LEU A 481 3414 4676 2908 702 989 579 C ATOM 3710 O LEU A 481 -47.575 -42.603 -7.923 1.00 28.06 O ANISOU 3710 O LEU A 481 3299 4508 2854 631 951 608 O ATOM 3711 CB LEU A 481 -48.790 -39.495 -8.362 1.00 28.40 C ANISOU 3711 CB LEU A 481 3344 4567 2880 729 940 427 C ATOM 3712 CG LEU A 481 -47.346 -39.321 -8.848 1.00 27.71 C ANISOU 3712 CG LEU A 481 3318 4414 2796 687 843 351 C ATOM 3713 CD1 LEU A 481 -47.105 -40.081 -10.155 1.00 25.69 C ANISOU 3713 CD1 LEU A 481 3026 4079 2655 585 800 379 C ATOM 3714 CD2 LEU A 481 -47.011 -37.842 -9.008 1.00 27.52 C ANISOU 3714 CD2 LEU A 481 3342 4365 2750 723 796 233 C ATOM 3715 N THR A 482 -47.972 -41.380 -6.076 1.00 29.66 N ANISOU 3715 N THR A 482 3555 4845 2870 795 1017 566 N ATOM 3716 CA THR A 482 -46.843 -41.939 -5.325 1.00 29.72 C ANISOU 3716 CA THR A 482 3623 4876 2794 818 990 573 C ATOM 3717 C THR A 482 -47.171 -43.241 -4.594 1.00 30.68 C ANISOU 3717 C THR A 482 3722 5042 2893 829 1070 709 C ATOM 3718 O THR A 482 -46.274 -44.027 -4.302 1.00 30.56 O ANISOU 3718 O THR A 482 3742 5023 2848 822 1047 740 O ATOM 3719 CB THR A 482 -46.328 -40.948 -4.267 1.00 30.43 C ANISOU 3719 CB THR A 482 3785 5034 2744 918 970 484 C ATOM 3720 OG1 THR A 482 -47.322 -40.781 -3.244 1.00 30.65 O ANISOU 3720 OG1 THR A 482 3802 5154 2689 1008 1065 530 O ATOM 3721 CG2 THR A 482 -45.996 -39.602 -4.902 1.00 29.81 C ANISOU 3721 CG2 THR A 482 3734 4904 2690 910 897 350 C ATOM 3722 N GLY A 483 -48.447 -43.455 -4.280 1.00 31.72 N ANISOU 3722 N GLY A 483 3795 5217 3040 849 1168 792 N ATOM 3723 CA GLY A 483 -48.862 -44.601 -3.464 1.00 33.03 C ANISOU 3723 CA GLY A 483 3938 5431 3180 869 1261 929 C ATOM 3724 C GLY A 483 -48.455 -44.486 -2.001 1.00 34.54 C ANISOU 3724 C GLY A 483 4197 5724 3203 986 1295 939 C ATOM 3725 O GLY A 483 -48.447 -45.481 -1.268 1.00 35.06 O ANISOU 3725 O GLY A 483 4266 5828 3228 1011 1358 1051 O ATOM 3726 N GLU A 484 -48.130 -43.270 -1.569 1.00 35.01 N ANISOU 3726 N GLU A 484 4311 5829 3163 1062 1253 823 N ATOM 3727 CA GLU A 484 -47.742 -43.009 -0.182 1.00 36.33 C ANISOU 3727 CA GLU A 484 4546 6101 3158 1183 1273 810 C ATOM 3728 C GLU A 484 -48.202 -41.606 0.225 1.00 36.95 C ANISOU 3728 C GLU A 484 4646 6231 3160 1267 1277 706 C ATOM 3729 O GLU A 484 -48.890 -40.933 -0.544 1.00 36.50 O ANISOU 3729 O GLU A 484 4548 6131 3190 1232 1276 664 O ATOM 3730 CB GLU A 484 -46.228 -43.205 -0.004 1.00 36.14 C ANISOU 3730 CB GLU A 484 4592 6066 3074 1184 1177 754 C ATOM 3731 CG GLU A 484 -45.351 -42.408 -0.961 1.00 35.02 C ANISOU 3731 CG GLU A 484 4472 5841 2993 1121 1055 615 C ATOM 3732 CD GLU A 484 -45.185 -40.963 -0.540 1.00 36.00 C ANISOU 3732 CD GLU A 484 4645 6001 3032 1193 1012 475 C ATOM 3733 OE1 GLU A 484 -44.389 -40.704 0.392 1.00 35.41 O ANISOU 3733 OE1 GLU A 484 4634 5991 2828 1269 973 418 O ATOM 3734 OE2 GLU A 484 -45.849 -40.086 -1.142 1.00 36.49 O ANISOU 3734 OE2 GLU A 484 4683 6025 3156 1175 1014 419 O ATOM 3735 N LYS A 485 -47.824 -41.170 1.425 1.00 37.86 N ANISOU 3735 N LYS A 485 4830 6441 3113 1381 1279 662 N ATOM 3736 CA LYS A 485 -48.348 -39.932 1.995 1.00 38.82 C ANISOU 3736 CA LYS A 485 4978 6623 3148 1479 1299 574 C ATOM 3737 C LYS A 485 -47.342 -38.786 2.038 1.00 38.27 C ANISOU 3737 C LYS A 485 4985 6535 3022 1504 1184 399 C ATOM 3738 O LYS A 485 -47.692 -37.652 1.729 1.00 38.18 O ANISOU 3738 O LYS A 485 4979 6496 3032 1518 1165 301 O ATOM 3739 CB LYS A 485 -48.849 -40.198 3.416 1.00 40.62 C ANISOU 3739 CB LYS A 485 5227 6985 3222 1607 1401 649 C ATOM 3740 CG LYS A 485 -49.809 -41.379 3.545 1.00 42.66 C ANISOU 3740 CG LYS A 485 5411 7269 3529 1588 1526 834 C ATOM 3741 CD LYS A 485 -51.208 -41.033 3.049 1.00 44.73 C ANISOU 3741 CD LYS A 485 5589 7522 3886 1569 1605 869 C ATOM 3742 CE LYS A 485 -52.294 -41.750 3.855 1.00 47.05 C ANISOU 3742 CE LYS A 485 5830 7906 4143 1626 1756 1026 C ATOM 3743 NZ LYS A 485 -53.643 -41.156 3.600 1.00 48.81 N ANISOU 3743 NZ LYS A 485 5975 8146 4423 1641 1831 1037 N ATOM 3744 N GLU A 486 -46.102 -39.078 2.426 1.00 38.23 N ANISOU 3744 N GLU A 486 5035 6542 2948 1511 1109 363 N ATOM 3745 CA GLU A 486 -45.131 -38.025 2.754 1.00 38.34 C ANISOU 3745 CA GLU A 486 5122 6560 2884 1552 1006 198 C ATOM 3746 C GLU A 486 -44.686 -37.213 1.536 1.00 36.77 C ANISOU 3746 C GLU A 486 4917 6239 2815 1456 915 87 C ATOM 3747 O GLU A 486 -44.821 -35.988 1.526 1.00 36.83 O ANISOU 3747 O GLU A 486 4952 6228 2813 1488 887 -31 O ATOM 3748 CB GLU A 486 -43.914 -38.611 3.475 1.00 38.77 C ANISOU 3748 CB GLU A 486 5227 6667 2835 1584 946 192 C ATOM 3749 CG GLU A 486 -42.924 -37.556 3.964 1.00 39.97 C ANISOU 3749 CG GLU A 486 5450 6839 2897 1634 839 19 C ATOM 3750 CD GLU A 486 -41.842 -38.128 4.863 1.00 41.31 C ANISOU 3750 CD GLU A 486 5666 7090 2940 1689 787 17 C ATOM 3751 OE1 GLU A 486 -40.652 -38.033 4.495 1.00 41.09 O ANISOU 3751 OE1 GLU A 486 5652 7016 2945 1634 677 -63 O ATOM 3752 OE2 GLU A 486 -42.180 -38.671 5.934 1.00 42.98 O ANISOU 3752 OE2 GLU A 486 5898 7415 3019 1792 857 99 O ATOM 3753 N MET A 487 -44.149 -37.887 0.522 1.00 35.21 N ANISOU 3753 N MET A 487 4685 5955 2737 1343 871 126 N ATOM 3754 CA MET A 487 -43.755 -37.210 -0.715 1.00 33.96 C ANISOU 3754 CA MET A 487 4516 5681 2706 1249 795 40 C ATOM 3755 C MET A 487 -44.959 -36.566 -1.394 1.00 33.41 C ANISOU 3755 C MET A 487 4404 5569 2721 1236 847 43 C ATOM 3756 O MET A 487 -44.846 -35.483 -1.967 1.00 32.83 O ANISOU 3756 O MET A 487 4347 5430 2698 1217 799 -61 O ATOM 3757 CB MET A 487 -43.081 -38.179 -1.685 1.00 33.06 C ANISOU 3757 CB MET A 487 4369 5492 2700 1139 753 98 C ATOM 3758 CG MET A 487 -41.733 -38.690 -1.212 1.00 33.80 C ANISOU 3758 CG MET A 487 4502 5612 2729 1144 683 78 C ATOM 3759 SD MET A 487 -40.937 -39.722 -2.451 1.00 33.99 S ANISOU 3759 SD MET A 487 4488 5539 2887 1018 634 135 S ATOM 3760 CE MET A 487 -42.097 -41.092 -2.532 1.00 34.27 C ANISOU 3760 CE MET A 487 4466 5586 2967 1001 749 315 C ATOM 3761 N ALA A 488 -46.109 -37.233 -1.322 1.00 33.35 N ANISOU 3761 N ALA A 488 4340 5598 2732 1246 947 164 N ATOM 3762 CA ALA A 488 -47.337 -36.709 -1.915 1.00 33.06 C ANISOU 3762 CA ALA A 488 4253 5537 2773 1241 1002 179 C ATOM 3763 C ALA A 488 -47.726 -35.363 -1.313 1.00 33.78 C ANISOU 3763 C ALA A 488 4386 5663 2785 1340 1012 75 C ATOM 3764 O ALA A 488 -48.138 -34.452 -2.035 1.00 33.36 O ANISOU 3764 O ALA A 488 4322 5548 2804 1325 998 15 O ATOM 3765 CB ALA A 488 -48.470 -37.704 -1.765 1.00 33.45 C ANISOU 3765 CB ALA A 488 4229 5635 2846 1241 1111 328 C ATOM 3766 N ALA A 489 -47.594 -35.247 0.007 1.00 34.74 N ANISOU 3766 N ALA A 489 4560 5883 2757 1446 1036 54 N ATOM 3767 CA ALA A 489 -47.917 -34.011 0.715 1.00 35.67 C ANISOU 3767 CA ALA A 489 4729 6042 2783 1553 1046 -52 C ATOM 3768 C ALA A 489 -46.973 -32.876 0.337 1.00 35.12 C ANISOU 3768 C ALA A 489 4719 5889 2736 1530 935 -214 C ATOM 3769 O ALA A 489 -47.411 -31.741 0.147 1.00 35.22 O ANISOU 3769 O ALA A 489 4749 5865 2769 1564 934 -298 O ATOM 3770 CB ALA A 489 -47.900 -34.241 2.232 1.00 36.89 C ANISOU 3770 CB ALA A 489 4929 6327 2760 1676 1091 -38 C ATOM 3771 N GLU A 490 -45.684 -33.181 0.223 1.00 34.85 N ANISOU 3771 N GLU A 490 4714 5822 2705 1473 845 -254 N ATOM 3772 CA GLU A 490 -44.704 -32.179 -0.197 1.00 34.71 C ANISOU 3772 CA GLU A 490 4743 5718 2726 1435 739 -401 C ATOM 3773 C GLU A 490 -44.996 -31.722 -1.633 1.00 33.58 C ANISOU 3773 C GLU A 490 4561 5454 2744 1345 726 -404 C ATOM 3774 O GLU A 490 -44.930 -30.527 -1.937 1.00 33.37 O ANISOU 3774 O GLU A 490 4567 5360 2753 1351 690 -513 O ATOM 3775 CB GLU A 490 -43.276 -32.723 -0.090 1.00 34.68 C ANISOU 3775 CB GLU A 490 4763 5711 2703 1387 650 -427 C ATOM 3776 CG GLU A 490 -42.816 -33.111 1.326 1.00 37.03 C ANISOU 3776 CG GLU A 490 5106 6131 2832 1482 645 -437 C ATOM 3777 CD GLU A 490 -42.648 -31.927 2.278 1.00 40.07 C ANISOU 3777 CD GLU A 490 5564 6557 3105 1581 610 -587 C ATOM 3778 OE1 GLU A 490 -42.460 -32.165 3.491 1.00 43.46 O ANISOU 3778 OE1 GLU A 490 6032 7099 3380 1678 615 -596 O ATOM 3779 OE2 GLU A 490 -42.697 -30.760 1.832 1.00 41.54 O ANISOU 3779 OE2 GLU A 490 5770 6661 3353 1566 576 -697 O ATOM 3780 N LEU A 491 -45.339 -32.669 -2.504 1.00 32.57 N ANISOU 3780 N LEU A 491 4365 5298 2712 1265 755 -287 N ATOM 3781 CA LEU A 491 -45.679 -32.345 -3.892 1.00 31.64 C ANISOU 3781 CA LEU A 491 4207 5078 2739 1185 745 -279 C ATOM 3782 C LEU A 491 -46.951 -31.501 -3.987 1.00 32.42 C ANISOU 3782 C LEU A 491 4288 5178 2853 1245 809 -286 C ATOM 3783 O LEU A 491 -46.999 -30.536 -4.755 1.00 32.17 O ANISOU 3783 O LEU A 491 4266 5061 2895 1226 779 -352 O ATOM 3784 CB LEU A 491 -45.820 -33.616 -4.731 1.00 30.61 C ANISOU 3784 CB LEU A 491 4007 4927 2696 1095 762 -154 C ATOM 3785 CG LEU A 491 -44.503 -34.310 -5.088 1.00 30.27 C ANISOU 3785 CG LEU A 491 3976 4846 2680 1016 687 -156 C ATOM 3786 CD1 LEU A 491 -44.770 -35.684 -5.687 1.00 29.79 C ANISOU 3786 CD1 LEU A 491 3853 4780 2688 947 718 -27 C ATOM 3787 CD2 LEU A 491 -43.673 -33.460 -6.052 1.00 29.59 C ANISOU 3787 CD2 LEU A 491 3912 4653 2677 953 604 -252 C ATOM 3788 N LYS A 492 -47.971 -31.849 -3.205 1.00 33.38 N ANISOU 3788 N LYS A 492 4383 5395 2903 1323 900 -215 N ATOM 3789 CA LYS A 492 -49.211 -31.071 -3.203 1.00 34.27 C ANISOU 3789 CA LYS A 492 4474 5523 3023 1392 967 -218 C ATOM 3790 C LYS A 492 -48.966 -29.627 -2.764 1.00 34.82 C ANISOU 3790 C LYS A 492 4623 5566 3040 1468 933 -364 C ATOM 3791 O LYS A 492 -49.551 -28.703 -3.326 1.00 34.65 O ANISOU 3791 O LYS A 492 4597 5489 3078 1485 942 -403 O ATOM 3792 CB LYS A 492 -50.288 -31.712 -2.323 1.00 35.42 C ANISOU 3792 CB LYS A 492 4576 5787 3093 1468 1076 -115 C ATOM 3793 CG LYS A 492 -51.646 -31.009 -2.441 1.00 36.89 C ANISOU 3793 CG LYS A 492 4722 5992 3302 1534 1151 -103 C ATOM 3794 CD LYS A 492 -52.786 -31.816 -1.842 1.00 39.27 C ANISOU 3794 CD LYS A 492 4952 6401 3567 1582 1266 25 C ATOM 3795 CE LYS A 492 -54.096 -31.027 -1.874 1.00 40.65 C ANISOU 3795 CE LYS A 492 5086 6604 3754 1661 1339 27 C ATOM 3796 NZ LYS A 492 -54.395 -30.483 -3.238 1.00 40.84 N ANISOU 3796 NZ LYS A 492 5072 6530 3916 1598 1298 5 N ATOM 3797 N ALA A 493 -48.101 -29.434 -1.773 1.00 35.42 N ANISOU 3797 N ALA A 493 4771 5681 3007 1514 891 -446 N ATOM 3798 CA ALA A 493 -47.777 -28.088 -1.300 1.00 36.38 C ANISOU 3798 CA ALA A 493 4972 5771 3079 1582 850 -598 C ATOM 3799 C ALA A 493 -47.024 -27.285 -2.370 1.00 35.71 C ANISOU 3799 C ALA A 493 4909 5545 3114 1496 764 -685 C ATOM 3800 O ALA A 493 -47.235 -26.080 -2.507 1.00 36.33 O ANISOU 3800 O ALA A 493 5027 5561 3216 1534 755 -777 O ATOM 3801 CB ALA A 493 -46.974 -28.152 -0.004 1.00 37.25 C ANISOU 3801 CB ALA A 493 5149 5960 3042 1647 814 -668 C ATOM 3802 N LEU A 494 -46.163 -27.956 -3.131 1.00 34.83 N ANISOU 3802 N LEU A 494 4774 5383 3078 1384 707 -650 N ATOM 3803 CA LEU A 494 -45.396 -27.301 -4.190 1.00 34.29 C ANISOU 3803 CA LEU A 494 4720 5185 3126 1298 633 -716 C ATOM 3804 C LEU A 494 -46.236 -26.994 -5.439 1.00 33.80 C ANISOU 3804 C LEU A 494 4610 5047 3184 1262 667 -663 C ATOM 3805 O LEU A 494 -46.165 -25.886 -5.973 1.00 34.06 O ANISOU 3805 O LEU A 494 4675 4987 3280 1260 642 -738 O ATOM 3806 CB LEU A 494 -44.186 -28.156 -4.584 1.00 33.52 C ANISOU 3806 CB LEU A 494 4608 5065 3062 1197 565 -694 C ATOM 3807 CG LEU A 494 -43.079 -28.277 -3.534 1.00 34.10 C ANISOU 3807 CG LEU A 494 4731 5191 3035 1219 504 -770 C ATOM 3808 CD1 LEU A 494 -42.084 -29.357 -3.919 1.00 33.13 C ANISOU 3808 CD1 LEU A 494 4579 5067 2943 1130 456 -715 C ATOM 3809 CD2 LEU A 494 -42.379 -26.941 -3.328 1.00 35.59 C ANISOU 3809 CD2 LEU A 494 4986 5310 3228 1231 435 -931 C ATOM 3810 N TYR A 495 -47.022 -27.973 -5.892 1.00 33.23 N ANISOU 3810 N TYR A 495 4464 5018 3145 1237 722 -533 N ATOM 3811 CA TYR A 495 -47.736 -27.891 -7.180 1.00 32.45 C ANISOU 3811 CA TYR A 495 4309 4858 3163 1192 741 -473 C ATOM 3812 C TYR A 495 -49.211 -27.491 -7.084 1.00 33.59 C ANISOU 3812 C TYR A 495 4417 5044 3300 1275 824 -436 C ATOM 3813 O TYR A 495 -49.775 -27.007 -8.069 1.00 33.09 O ANISOU 3813 O TYR A 495 4326 4923 3325 1262 830 -421 O ATOM 3814 CB TYR A 495 -47.655 -29.233 -7.918 1.00 31.23 C ANISOU 3814 CB TYR A 495 4086 4712 3067 1099 739 -361 C ATOM 3815 CG TYR A 495 -46.306 -29.547 -8.527 1.00 29.39 C ANISOU 3815 CG TYR A 495 3872 4411 2884 1003 658 -386 C ATOM 3816 CD1 TYR A 495 -45.371 -30.312 -7.840 1.00 28.20 C ANISOU 3816 CD1 TYR A 495 3741 4303 2671 984 626 -386 C ATOM 3817 CD2 TYR A 495 -45.978 -29.106 -9.809 1.00 28.09 C ANISOU 3817 CD2 TYR A 495 3703 4144 2825 937 616 -402 C ATOM 3818 CE1 TYR A 495 -44.135 -30.613 -8.400 1.00 27.42 C ANISOU 3818 CE1 TYR A 495 3653 4147 2619 900 554 -407 C ATOM 3819 CE2 TYR A 495 -44.748 -29.403 -10.378 1.00 26.71 C ANISOU 3819 CE2 TYR A 495 3541 3913 2696 852 549 -420 C ATOM 3820 CZ TYR A 495 -43.828 -30.157 -9.666 1.00 26.76 C ANISOU 3820 CZ TYR A 495 3563 3963 2643 833 518 -424 C ATOM 3821 OH TYR A 495 -42.605 -30.462 -10.218 1.00 26.31 O ANISOU 3821 OH TYR A 495 3512 3854 2630 754 453 -440 O ATOM 3822 N SER A 496 -49.836 -27.748 -5.932 1.00 34.94 N ANISOU 3822 N SER A 496 4584 5322 3368 1361 888 -412 N ATOM 3823 CA SER A 496 -51.256 -27.434 -5.665 1.00 36.22 C ANISOU 3823 CA SER A 496 4707 5545 3511 1452 976 -372 C ATOM 3824 C SER A 496 -52.262 -28.328 -6.398 1.00 35.60 C ANISOU 3824 C SER A 496 4521 5498 3508 1409 1028 -240 C ATOM 3825 O SER A 496 -53.174 -28.877 -5.770 1.00 36.57 O ANISOU 3825 O SER A 496 4591 5719 3585 1459 1109 -162 O ATOM 3826 CB SER A 496 -51.582 -25.955 -5.937 1.00 36.90 C ANISOU 3826 CB SER A 496 4836 5560 3624 1514 971 -465 C ATOM 3827 OG SER A 496 -50.886 -25.111 -5.038 1.00 39.44 O ANISOU 3827 OG SER A 496 5253 5867 3864 1573 938 -591 O ATOM 3828 N ASP A 497 -52.101 -28.454 -7.714 1.00 34.21 N ANISOU 3828 N ASP A 497 4311 5241 3447 1318 983 -216 N ATOM 3829 CA ASP A 497 -53.020 -29.202 -8.566 1.00 33.60 C ANISOU 3829 CA ASP A 497 4131 5182 3453 1271 1016 -108 C ATOM 3830 C ASP A 497 -52.284 -30.368 -9.236 1.00 31.97 C ANISOU 3830 C ASP A 497 3898 4945 3303 1151 968 -54 C ATOM 3831 O ASP A 497 -51.253 -30.170 -9.886 1.00 31.00 O ANISOU 3831 O ASP A 497 3819 4739 3221 1089 893 -105 O ATOM 3832 CB ASP A 497 -53.597 -28.250 -9.622 1.00 33.70 C ANISOU 3832 CB ASP A 497 4127 5129 3548 1284 1005 -132 C ATOM 3833 CG ASP A 497 -54.670 -28.892 -10.498 1.00 34.11 C ANISOU 3833 CG ASP A 497 4068 5209 3683 1249 1035 -32 C ATOM 3834 OD1 ASP A 497 -55.284 -28.139 -11.288 1.00 36.34 O ANISOU 3834 OD1 ASP A 497 4329 5456 4022 1276 1033 -42 O ATOM 3835 OD2 ASP A 497 -54.911 -30.116 -10.407 1.00 33.49 O ANISOU 3835 OD2 ASP A 497 3924 5185 3616 1197 1059 54 O ATOM 3836 N ILE A 498 -52.822 -31.578 -9.078 1.00 31.39 N ANISOU 3836 N ILE A 498 3752 4937 3239 1121 1014 49 N ATOM 3837 CA ILE A 498 -52.257 -32.782 -9.709 1.00 29.98 C ANISOU 3837 CA ILE A 498 3542 4730 3119 1012 976 108 C ATOM 3838 C ILE A 498 -52.172 -32.650 -11.234 1.00 28.95 C ANISOU 3838 C ILE A 498 3386 4515 3100 938 917 101 C ATOM 3839 O ILE A 498 -51.281 -33.221 -11.855 1.00 27.79 O ANISOU 3839 O ILE A 498 3252 4314 2993 855 859 103 O ATOM 3840 CB ILE A 498 -53.073 -34.057 -9.332 1.00 30.29 C ANISOU 3840 CB ILE A 498 3498 4846 3166 994 1046 227 C ATOM 3841 CG1 ILE A 498 -52.419 -35.340 -9.857 1.00 28.91 C ANISOU 3841 CG1 ILE A 498 3302 4636 3046 887 1008 282 C ATOM 3842 CG2 ILE A 498 -54.508 -33.957 -9.851 1.00 30.56 C ANISOU 3842 CG2 ILE A 498 3435 4909 3266 1009 1097 280 C ATOM 3843 CD1 ILE A 498 -50.998 -35.583 -9.373 1.00 27.29 C ANISOU 3843 CD1 ILE A 498 3179 4409 2780 870 957 241 C ATOM 3844 N ASP A 499 -53.091 -31.892 -11.828 1.00 28.96 N ANISOU 3844 N ASP A 499 3351 4507 3146 974 933 95 N ATOM 3845 CA ASP A 499 -53.080 -31.667 -13.273 1.00 28.52 C ANISOU 3845 CA ASP A 499 3274 4379 3184 920 880 89 C ATOM 3846 C ASP A 499 -51.946 -30.754 -13.758 1.00 27.79 C ANISOU 3846 C ASP A 499 3269 4191 3098 907 813 1 C ATOM 3847 O ASP A 499 -51.796 -30.558 -14.956 1.00 27.53 O ANISOU 3847 O ASP A 499 3229 4096 3136 865 769 -2 O ATOM 3848 CB ASP A 499 -54.433 -31.114 -13.741 1.00 28.98 C ANISOU 3848 CB ASP A 499 3264 4463 3282 974 918 113 C ATOM 3849 CG ASP A 499 -55.533 -32.157 -13.714 1.00 30.03 C ANISOU 3849 CG ASP A 499 3286 4674 3450 952 969 209 C ATOM 3850 OD1 ASP A 499 -55.234 -33.373 -13.798 1.00 29.56 O ANISOU 3850 OD1 ASP A 499 3196 4620 3416 872 959 261 O ATOM 3851 OD2 ASP A 499 -56.710 -31.750 -13.622 1.00 30.82 O ANISOU 3851 OD2 ASP A 499 3326 4827 3558 1016 1021 232 O ATOM 3852 N VAL A 500 -51.155 -30.199 -12.840 1.00 28.21 N ANISOU 3852 N VAL A 500 3403 4235 3080 944 804 -70 N ATOM 3853 CA VAL A 500 -49.977 -29.408 -13.209 1.00 27.78 C ANISOU 3853 CA VAL A 500 3428 4089 3039 920 740 -154 C ATOM 3854 C VAL A 500 -48.659 -30.089 -12.793 1.00 27.00 C ANISOU 3854 C VAL A 500 3368 3983 2909 861 695 -173 C ATOM 3855 O VAL A 500 -47.578 -29.546 -13.020 1.00 25.92 O ANISOU 3855 O VAL A 500 3289 3776 2785 833 640 -241 O ATOM 3856 CB VAL A 500 -50.096 -27.974 -12.644 1.00 29.24 C ANISOU 3856 CB VAL A 500 3676 4249 3185 1010 753 -241 C ATOM 3857 CG1 VAL A 500 -48.769 -27.224 -12.711 1.00 29.92 C ANISOU 3857 CG1 VAL A 500 3846 4245 3277 982 690 -335 C ATOM 3858 CG2 VAL A 500 -51.172 -27.216 -13.418 1.00 29.65 C ANISOU 3858 CG2 VAL A 500 3695 4280 3291 1056 780 -225 C ATOM 3859 N MET A 501 -48.743 -31.290 -12.218 1.00 26.37 N ANISOU 3859 N MET A 501 3253 3973 2794 843 719 -108 N ATOM 3860 CA MET A 501 -47.546 -32.076 -11.942 1.00 25.75 C ANISOU 3860 CA MET A 501 3203 3890 2692 787 676 -110 C ATOM 3861 C MET A 501 -46.771 -32.301 -13.243 1.00 24.70 C ANISOU 3861 C MET A 501 3066 3675 2645 698 615 -110 C ATOM 3862 O MET A 501 -47.367 -32.511 -14.303 1.00 24.28 O ANISOU 3862 O MET A 501 2963 3598 2664 665 617 -64 O ATOM 3863 CB MET A 501 -47.913 -33.427 -11.316 1.00 25.78 C ANISOU 3863 CB MET A 501 3160 3973 2662 778 720 -19 C ATOM 3864 CG MET A 501 -46.727 -34.290 -10.938 1.00 25.79 C ANISOU 3864 CG MET A 501 3190 3977 2631 735 682 -14 C ATOM 3865 SD MET A 501 -45.588 -33.451 -9.822 1.00 26.08 S ANISOU 3865 SD MET A 501 3318 4024 2568 788 641 -124 S ATOM 3866 CE MET A 501 -44.286 -34.676 -9.691 1.00 23.60 C ANISOU 3866 CE MET A 501 3014 3713 2239 725 593 -94 C ATOM 3867 N GLU A 502 -45.446 -32.250 -13.146 1.00 24.37 N ANISOU 3867 N GLU A 502 3074 3595 2590 663 560 -162 N ATOM 3868 CA GLU A 502 -44.563 -32.366 -14.308 1.00 23.37 C ANISOU 3868 CA GLU A 502 2951 3392 2537 586 504 -169 C ATOM 3869 C GLU A 502 -44.185 -33.812 -14.576 1.00 22.58 C ANISOU 3869 C GLU A 502 2816 3309 2452 523 491 -100 C ATOM 3870 O GLU A 502 -44.128 -34.629 -13.651 1.00 23.15 O ANISOU 3870 O GLU A 502 2885 3444 2468 535 511 -67 O ATOM 3871 CB GLU A 502 -43.290 -31.554 -14.087 1.00 23.79 C ANISOU 3871 CB GLU A 502 3067 3393 2578 578 451 -261 C ATOM 3872 CG GLU A 502 -43.516 -30.056 -14.070 1.00 24.49 C ANISOU 3872 CG GLU A 502 3197 3434 2676 626 455 -337 C ATOM 3873 CD GLU A 502 -42.271 -29.300 -13.670 1.00 26.20 C ANISOU 3873 CD GLU A 502 3472 3602 2880 615 404 -434 C ATOM 3874 OE1 GLU A 502 -41.525 -28.876 -14.577 1.00 25.50 O ANISOU 3874 OE1 GLU A 502 3395 3431 2862 562 367 -457 O ATOM 3875 OE2 GLU A 502 -42.027 -29.146 -12.450 1.00 27.07 O ANISOU 3875 OE2 GLU A 502 3616 3760 2912 659 400 -487 O ATOM 3876 N LEU A 503 -43.898 -34.111 -15.840 1.00 21.68 N ANISOU 3876 N LEU A 503 2683 3140 2414 460 460 -79 N ATOM 3877 CA LEU A 503 -43.612 -35.473 -16.281 1.00 21.19 C ANISOU 3877 CA LEU A 503 2589 3083 2380 400 447 -16 C ATOM 3878 C LEU A 503 -42.360 -36.075 -15.636 1.00 21.12 C ANISOU 3878 C LEU A 503 2612 3084 2330 379 416 -29 C ATOM 3879 O LEU A 503 -42.428 -37.150 -15.049 1.00 20.89 O ANISOU 3879 O LEU A 503 2566 3101 2271 376 436 25 O ATOM 3880 CB LEU A 503 -43.481 -35.523 -17.811 1.00 20.58 C ANISOU 3880 CB LEU A 503 2493 2943 2384 346 414 -6 C ATOM 3881 CG LEU A 503 -43.135 -36.879 -18.436 1.00 19.87 C ANISOU 3881 CG LEU A 503 2375 2845 2331 284 394 47 C ATOM 3882 CD1 LEU A 503 -44.218 -37.915 -18.112 1.00 19.97 C ANISOU 3882 CD1 LEU A 503 2333 2909 2347 282 437 119 C ATOM 3883 CD2 LEU A 503 -42.922 -36.738 -19.953 1.00 18.52 C ANISOU 3883 CD2 LEU A 503 2197 2614 2226 244 359 42 C ATOM 3884 N TYR A 504 -41.218 -35.400 -15.746 1.00 21.22 N ANISOU 3884 N TYR A 504 2667 3054 2343 367 369 -97 N ATOM 3885 CA TYR A 504 -39.955 -36.004 -15.292 1.00 21.36 C ANISOU 3885 CA TYR A 504 2705 3081 2330 343 331 -109 C ATOM 3886 C TYR A 504 -39.922 -36.338 -13.784 1.00 21.76 C ANISOU 3886 C TYR A 504 2773 3210 2285 396 349 -108 C ATOM 3887 O TYR A 504 -39.656 -37.484 -13.420 1.00 21.67 O ANISOU 3887 O TYR A 504 2751 3234 2250 386 353 -54 O ATOM 3888 CB TYR A 504 -38.730 -35.165 -15.687 1.00 21.21 C ANISOU 3888 CB TYR A 504 2719 3004 2337 316 277 -185 C ATOM 3889 CG TYR A 504 -37.445 -35.822 -15.238 1.00 22.66 C ANISOU 3889 CG TYR A 504 2913 3205 2492 295 236 -196 C ATOM 3890 CD1 TYR A 504 -37.062 -37.049 -15.765 1.00 23.59 C ANISOU 3890 CD1 TYR A 504 3006 3321 2635 254 227 -135 C ATOM 3891 CD2 TYR A 504 -36.642 -35.251 -14.254 1.00 25.37 C ANISOU 3891 CD2 TYR A 504 3288 3571 2779 321 204 -269 C ATOM 3892 CE1 TYR A 504 -35.908 -37.683 -15.349 1.00 25.01 C ANISOU 3892 CE1 TYR A 504 3193 3521 2787 242 191 -139 C ATOM 3893 CE2 TYR A 504 -35.468 -35.886 -13.832 1.00 26.43 C ANISOU 3893 CE2 TYR A 504 3426 3732 2885 306 162 -277 C ATOM 3894 CZ TYR A 504 -35.115 -37.101 -14.389 1.00 25.55 C ANISOU 3894 CZ TYR A 504 3289 3618 2800 269 158 -208 C ATOM 3895 OH TYR A 504 -33.967 -37.756 -13.996 1.00 28.16 O ANISOU 3895 OH TYR A 504 3620 3976 3103 261 118 -211 O ATOM 3896 N PRO A 505 -40.191 -35.351 -12.908 1.00 22.28 N ANISOU 3896 N PRO A 505 2869 3303 2294 456 361 -168 N ATOM 3897 CA PRO A 505 -40.183 -35.713 -11.484 1.00 22.87 C ANISOU 3897 CA PRO A 505 2962 3461 2265 515 379 -163 C ATOM 3898 C PRO A 505 -41.222 -36.793 -11.157 1.00 22.93 C ANISOU 3898 C PRO A 505 2931 3526 2255 532 445 -58 C ATOM 3899 O PRO A 505 -40.982 -37.635 -10.298 1.00 23.48 O ANISOU 3899 O PRO A 505 3005 3654 2261 554 459 -16 O ATOM 3900 CB PRO A 505 -40.491 -34.388 -10.769 1.00 23.69 C ANISOU 3900 CB PRO A 505 3104 3577 2319 581 386 -248 C ATOM 3901 CG PRO A 505 -41.071 -33.496 -11.803 1.00 23.86 C ANISOU 3901 CG PRO A 505 3116 3527 2422 564 394 -268 C ATOM 3902 CD PRO A 505 -40.502 -33.926 -13.119 1.00 22.36 C ANISOU 3902 CD PRO A 505 2902 3270 2323 482 360 -239 C ATOM 3903 N ALA A 506 -42.346 -36.786 -11.870 1.00 22.60 N ANISOU 3903 N ALA A 506 2847 3466 2274 519 486 -14 N ATOM 3904 CA ALA A 506 -43.402 -37.773 -11.656 1.00 22.80 C ANISOU 3904 CA ALA A 506 2823 3537 2302 525 550 85 C ATOM 3905 C ALA A 506 -42.918 -39.200 -11.930 1.00 22.58 C ANISOU 3905 C ALA A 506 2776 3500 2305 468 540 157 C ATOM 3906 O ALA A 506 -43.239 -40.116 -11.179 1.00 22.83 O ANISOU 3906 O ALA A 506 2794 3582 2298 486 586 230 O ATOM 3907 CB ALA A 506 -44.610 -37.456 -12.527 1.00 22.71 C ANISOU 3907 CB ALA A 506 2762 3503 2363 513 581 109 C ATOM 3908 N LEU A 507 -42.145 -39.376 -12.999 1.00 22.03 N ANISOU 3908 N LEU A 507 2707 3363 2301 404 486 139 N ATOM 3909 CA LEU A 507 -41.608 -40.694 -13.360 1.00 21.94 C ANISOU 3909 CA LEU A 507 2683 3331 2324 352 471 198 C ATOM 3910 C LEU A 507 -40.730 -41.266 -12.251 1.00 22.84 C ANISOU 3910 C LEU A 507 2831 3492 2356 383 464 209 C ATOM 3911 O LEU A 507 -40.736 -42.474 -12.004 1.00 23.03 O ANISOU 3911 O LEU A 507 2841 3528 2380 372 488 287 O ATOM 3912 CB LEU A 507 -40.798 -40.606 -14.654 1.00 21.41 C ANISOU 3912 CB LEU A 507 2619 3189 2327 291 411 161 C ATOM 3913 CG LEU A 507 -41.575 -40.267 -15.928 1.00 21.35 C ANISOU 3913 CG LEU A 507 2576 3134 2402 257 411 161 C ATOM 3914 CD1 LEU A 507 -40.604 -39.846 -17.042 1.00 21.27 C ANISOU 3914 CD1 LEU A 507 2585 3058 2438 217 353 111 C ATOM 3915 CD2 LEU A 507 -42.442 -41.431 -16.365 1.00 21.73 C ANISOU 3915 CD2 LEU A 507 2573 3180 2504 221 441 241 C ATOM 3916 N LEU A 508 -39.987 -40.390 -11.582 1.00 23.12 N ANISOU 3916 N LEU A 508 2910 3552 2324 425 431 132 N ATOM 3917 CA LEU A 508 -39.064 -40.802 -10.528 1.00 23.76 C ANISOU 3917 CA LEU A 508 3025 3685 2319 463 411 129 C ATOM 3918 C LEU A 508 -39.710 -40.959 -9.143 1.00 24.33 C ANISOU 3918 C LEU A 508 3108 3847 2290 542 470 167 C ATOM 3919 O LEU A 508 -39.110 -41.585 -8.268 1.00 25.10 O ANISOU 3919 O LEU A 508 3228 3996 2313 578 466 193 O ATOM 3920 CB LEU A 508 -37.897 -39.811 -10.434 1.00 23.96 C ANISOU 3920 CB LEU A 508 3086 3698 2318 468 340 19 C ATOM 3921 CG LEU A 508 -36.980 -39.639 -11.652 1.00 24.72 C ANISOU 3921 CG LEU A 508 3175 3715 2501 397 281 -20 C ATOM 3922 CD1 LEU A 508 -35.708 -38.898 -11.245 1.00 26.01 C ANISOU 3922 CD1 LEU A 508 3369 3885 2629 406 215 -115 C ATOM 3923 CD2 LEU A 508 -36.623 -40.952 -12.323 1.00 26.39 C ANISOU 3923 CD2 LEU A 508 3364 3900 2764 349 278 55 C ATOM 3924 N VAL A 509 -40.899 -40.384 -8.928 1.00 24.30 N ANISOU 3924 N VAL A 509 3090 3866 2278 576 524 172 N ATOM 3925 CA VAL A 509 -41.623 -40.546 -7.648 1.00 24.93 C ANISOU 3925 CA VAL A 509 3175 4035 2261 656 592 218 C ATOM 3926 C VAL A 509 -42.820 -41.489 -7.745 1.00 25.14 C ANISOU 3926 C VAL A 509 3148 4073 2332 641 675 336 C ATOM 3927 O VAL A 509 -43.458 -41.779 -6.734 1.00 26.03 O ANISOU 3927 O VAL A 509 3257 4259 2373 703 744 395 O ATOM 3928 CB VAL A 509 -42.140 -39.197 -7.054 1.00 25.55 C ANISOU 3928 CB VAL A 509 3278 4151 2277 727 606 138 C ATOM 3929 CG1 VAL A 509 -40.982 -38.239 -6.775 1.00 26.08 C ANISOU 3929 CG1 VAL A 509 3401 4212 2298 745 526 14 C ATOM 3930 CG2 VAL A 509 -43.194 -38.554 -7.956 1.00 24.04 C ANISOU 3930 CG2 VAL A 509 3049 3914 2173 702 633 131 C ATOM 3931 N GLU A 510 -43.128 -41.956 -8.954 1.00 24.42 N ANISOU 3931 N GLU A 510 3011 3910 2356 561 669 370 N ATOM 3932 CA GLU A 510 -44.316 -42.774 -9.186 1.00 24.70 C ANISOU 3932 CA GLU A 510 2985 3946 2455 533 739 470 C ATOM 3933 C GLU A 510 -44.276 -44.061 -8.371 1.00 25.26 C ANISOU 3933 C GLU A 510 3055 4054 2491 546 790 574 C ATOM 3934 O GLU A 510 -43.216 -44.671 -8.215 1.00 25.23 O ANISOU 3934 O GLU A 510 3085 4038 2463 539 752 581 O ATOM 3935 CB GLU A 510 -44.443 -43.130 -10.672 1.00 23.89 C ANISOU 3935 CB GLU A 510 2840 3756 2479 442 706 474 C ATOM 3936 CG GLU A 510 -45.797 -43.734 -11.060 1.00 24.31 C ANISOU 3936 CG GLU A 510 2819 3806 2613 407 767 554 C ATOM 3937 CD GLU A 510 -45.986 -43.827 -12.569 1.00 24.08 C ANISOU 3937 CD GLU A 510 2751 3701 2699 329 723 535 C ATOM 3938 OE1 GLU A 510 -44.995 -44.085 -13.282 1.00 24.04 O ANISOU 3938 OE1 GLU A 510 2774 3639 2723 285 659 503 O ATOM 3939 OE2 GLU A 510 -47.129 -43.644 -13.042 1.00 25.22 O ANISOU 3939 OE2 GLU A 510 2836 3847 2901 315 751 551 O ATOM 3940 N LYS A 511 -45.436 -44.470 -7.864 1.00 26.17 N ANISOU 3940 N LYS A 511 3125 4211 2606 568 878 660 N ATOM 3941 CA LYS A 511 -45.574 -45.773 -7.222 1.00 27.06 C ANISOU 3941 CA LYS A 511 3228 4345 2710 570 940 779 C ATOM 3942 C LYS A 511 -45.030 -46.842 -8.164 1.00 26.48 C ANISOU 3942 C LYS A 511 3142 4182 2737 481 901 811 C ATOM 3943 O LYS A 511 -45.515 -46.976 -9.286 1.00 26.05 O ANISOU 3943 O LYS A 511 3039 4063 2794 407 885 805 O ATOM 3944 CB LYS A 511 -47.041 -46.076 -6.916 1.00 28.22 C ANISOU 3944 CB LYS A 511 3307 4526 2888 576 1042 870 C ATOM 3945 CG LYS A 511 -47.259 -47.361 -6.116 1.00 30.46 C ANISOU 3945 CG LYS A 511 3579 4834 3159 586 1122 1003 C ATOM 3946 CD LYS A 511 -48.733 -47.727 -6.026 1.00 32.97 C ANISOU 3946 CD LYS A 511 3814 5171 3541 570 1222 1096 C ATOM 3947 CE LYS A 511 -48.937 -48.958 -5.149 1.00 35.22 C ANISOU 3947 CE LYS A 511 4091 5479 3811 584 1312 1237 C ATOM 3948 NZ LYS A 511 -50.372 -49.233 -4.858 1.00 38.24 N ANISOU 3948 NZ LYS A 511 4390 5896 4244 580 1422 1333 N ATOM 3949 N PRO A 512 -44.008 -47.597 -7.729 1.00 26.49 N ANISOU 3949 N PRO A 512 3189 4182 2695 494 881 840 N ATOM 3950 CA PRO A 512 -43.557 -48.667 -8.613 1.00 26.03 C ANISOU 3950 CA PRO A 512 3120 4036 2734 415 850 874 C ATOM 3951 C PRO A 512 -44.584 -49.786 -8.712 1.00 26.72 C ANISOU 3951 C PRO A 512 3150 4092 2910 368 927 988 C ATOM 3952 O PRO A 512 -45.402 -49.960 -7.805 1.00 27.24 O ANISOU 3952 O PRO A 512 3196 4216 2939 410 1014 1066 O ATOM 3953 CB PRO A 512 -42.284 -49.182 -7.926 1.00 26.31 C ANISOU 3953 CB PRO A 512 3216 4091 2688 459 822 887 C ATOM 3954 CG PRO A 512 -41.860 -48.079 -7.010 1.00 26.54 C ANISOU 3954 CG PRO A 512 3290 4207 2587 545 801 815 C ATOM 3955 CD PRO A 512 -43.133 -47.447 -6.555 1.00 27.01 C ANISOU 3955 CD PRO A 512 3319 4320 2624 580 871 828 C ATOM 3956 N ARG A 513 -44.551 -50.532 -9.812 1.00 26.53 N ANISOU 3956 N ARG A 513 3099 3976 3004 282 898 997 N ATOM 3957 CA ARG A 513 -45.245 -51.818 -9.849 1.00 27.51 C ANISOU 3957 CA ARG A 513 3180 4054 3217 232 961 1106 C ATOM 3958 C ARG A 513 -44.663 -52.701 -8.736 1.00 28.47 C ANISOU 3958 C ARG A 513 3349 4201 3269 285 1007 1198 C ATOM 3959 O ARG A 513 -43.553 -52.438 -8.258 1.00 28.26 O ANISOU 3959 O ARG A 513 3386 4209 3143 343 964 1161 O ATOM 3960 CB ARG A 513 -45.104 -52.489 -11.217 1.00 26.86 C ANISOU 3960 CB ARG A 513 3076 3866 3265 136 907 1084 C ATOM 3961 CG ARG A 513 -46.279 -52.252 -12.158 1.00 26.22 C ANISOU 3961 CG ARG A 513 2917 3756 3289 71 908 1062 C ATOM 3962 CD ARG A 513 -46.446 -50.798 -12.589 1.00 25.52 C ANISOU 3962 CD ARG A 513 2822 3708 3166 94 864 960 C ATOM 3963 NE ARG A 513 -47.512 -50.710 -13.590 1.00 25.45 N ANISOU 3963 NE ARG A 513 2737 3669 3263 32 858 944 N ATOM 3964 CZ ARG A 513 -47.364 -50.928 -14.896 1.00 24.20 C ANISOU 3964 CZ ARG A 513 2565 3439 3189 -34 790 893 C ATOM 3965 NH1 ARG A 513 -46.169 -51.199 -15.422 1.00 23.89 N ANISOU 3965 NH1 ARG A 513 2584 3349 3144 -47 726 851 N ATOM 3966 NH2 ARG A 513 -48.421 -50.834 -15.697 1.00 25.13 N ANISOU 3966 NH2 ARG A 513 2610 3545 3393 -82 786 880 N ATOM 3967 N PRO A 514 -45.412 -53.731 -8.298 1.00 30.06 N ANISOU 3967 N PRO A 514 3515 4385 3519 267 1095 1320 N ATOM 3968 CA PRO A 514 -44.954 -54.561 -7.176 1.00 31.22 C ANISOU 3968 CA PRO A 514 3709 4561 3595 328 1151 1423 C ATOM 3969 C PRO A 514 -43.556 -55.136 -7.383 1.00 31.14 C ANISOU 3969 C PRO A 514 3762 4503 3566 333 1083 1404 C ATOM 3970 O PRO A 514 -43.337 -55.900 -8.321 1.00 31.09 O ANISOU 3970 O PRO A 514 3747 4396 3671 258 1050 1404 O ATOM 3971 CB PRO A 514 -46.001 -55.681 -7.116 1.00 32.28 C ANISOU 3971 CB PRO A 514 3784 4643 3837 272 1246 1549 C ATOM 3972 CG PRO A 514 -47.220 -55.084 -7.701 1.00 31.96 C ANISOU 3972 CG PRO A 514 3661 4606 3874 220 1262 1516 C ATOM 3973 CD PRO A 514 -46.760 -54.123 -8.754 1.00 30.41 C ANISOU 3973 CD PRO A 514 3475 4393 3687 195 1152 1372 C ATOM 3974 N ASP A 515 -42.620 -54.739 -6.520 1.00 31.30 N ANISOU 3974 N ASP A 515 3844 4600 3447 425 1058 1383 N ATOM 3975 CA ASP A 515 -41.219 -55.158 -6.605 1.00 31.18 C ANISOU 3975 CA ASP A 515 3887 4561 3399 445 990 1360 C ATOM 3976 C ASP A 515 -40.586 -54.894 -7.978 1.00 29.46 C ANISOU 3976 C ASP A 515 3664 4266 3262 374 891 1252 C ATOM 3977 O ASP A 515 -39.710 -55.639 -8.426 1.00 29.10 O ANISOU 3977 O ASP A 515 3645 4159 3252 355 850 1256 O ATOM 3978 CB ASP A 515 -41.086 -56.634 -6.199 1.00 32.50 C ANISOU 3978 CB ASP A 515 4072 4679 3597 450 1049 1494 C ATOM 3979 CG ASP A 515 -41.526 -56.880 -4.771 1.00 35.75 C ANISOU 3979 CG ASP A 515 4498 5176 3908 537 1147 1607 C ATOM 3980 OD1 ASP A 515 -41.073 -56.135 -3.875 1.00 38.95 O ANISOU 3980 OD1 ASP A 515 4942 5692 4167 632 1131 1573 O ATOM 3981 OD2 ASP A 515 -42.329 -57.809 -4.539 1.00 39.13 O ANISOU 3981 OD2 ASP A 515 4900 5564 4404 512 1240 1730 O ATOM 3982 N ALA A 516 -41.007 -53.802 -8.617 1.00 28.18 N ANISOU 3982 N ALA A 516 3473 4113 3122 343 856 1156 N ATOM 3983 CA ALA A 516 -40.522 -53.430 -9.941 1.00 26.76 C ANISOU 3983 CA ALA A 516 3286 3868 3013 280 770 1056 C ATOM 3984 C ALA A 516 -39.672 -52.162 -9.891 1.00 25.74 C ANISOU 3984 C ALA A 516 3188 3794 2799 321 698 942 C ATOM 3985 O ALA A 516 -39.705 -51.410 -8.915 1.00 26.08 O ANISOU 3985 O ALA A 516 3249 3924 2736 391 712 926 O ATOM 3986 CB ALA A 516 -41.689 -53.247 -10.893 1.00 26.27 C ANISOU 3986 CB ALA A 516 3162 3759 3061 204 784 1040 C ATOM 3987 N ILE A 517 -38.904 -51.940 -10.950 1.00 24.84 N ANISOU 3987 N ILE A 517 3080 3627 2732 279 621 864 N ATOM 3988 CA ILE A 517 -38.022 -50.772 -11.035 1.00 23.85 C ANISOU 3988 CA ILE A 517 2978 3536 2547 304 551 756 C ATOM 3989 C ILE A 517 -38.770 -49.505 -11.454 1.00 23.48 C ANISOU 3989 C ILE A 517 2905 3501 2514 288 545 684 C ATOM 3990 O ILE A 517 -38.346 -48.399 -11.108 1.00 22.74 O ANISOU 3990 O ILE A 517 2832 3453 2353 326 511 607 O ATOM 3991 CB ILE A 517 -36.821 -51.037 -11.980 1.00 23.37 C ANISOU 3991 CB ILE A 517 2933 3418 2530 270 478 709 C ATOM 3992 CG1 ILE A 517 -35.747 -49.961 -11.807 1.00 23.14 C ANISOU 3992 CG1 ILE A 517 2927 3432 2431 303 411 612 C ATOM 3993 CG2 ILE A 517 -37.258 -51.118 -13.441 1.00 22.45 C ANISOU 3993 CG2 ILE A 517 2784 3217 2529 190 460 682 C ATOM 3994 CD1 ILE A 517 -34.443 -50.302 -12.492 1.00 23.69 C ANISOU 3994 CD1 ILE A 517 3010 3463 2528 284 348 579 C ATOM 3995 N PHE A 518 -39.886 -49.676 -12.171 1.00 23.06 N ANISOU 3995 N PHE A 518 2807 3405 2550 235 577 708 N ATOM 3996 CA PHE A 518 -40.634 -48.565 -12.761 1.00 22.78 C ANISOU 3996 CA PHE A 518 2743 3371 2543 218 569 645 C ATOM 3997 C PHE A 518 -42.101 -48.594 -12.375 1.00 23.21 C ANISOU 3997 C PHE A 518 2751 3455 2615 222 644 702 C ATOM 3998 O PHE A 518 -42.644 -49.650 -12.049 1.00 23.83 O ANISOU 3998 O PHE A 518 2807 3524 2725 207 700 795 O ATOM 3999 CB PHE A 518 -40.607 -48.641 -14.295 1.00 21.86 C ANISOU 3999 CB PHE A 518 2603 3174 2528 145 522 606 C ATOM 4000 CG PHE A 518 -39.243 -48.555 -14.908 1.00 21.47 C ANISOU 4000 CG PHE A 518 2589 3091 2478 134 451 548 C ATOM 4001 CD1 PHE A 518 -38.314 -47.617 -14.478 1.00 21.26 C ANISOU 4001 CD1 PHE A 518 2597 3102 2378 175 412 481 C ATOM 4002 CD2 PHE A 518 -38.905 -49.391 -15.965 1.00 21.44 C ANISOU 4002 CD2 PHE A 518 2580 3016 2552 80 422 555 C ATOM 4003 CE1 PHE A 518 -37.067 -47.537 -15.066 1.00 21.54 C ANISOU 4003 CE1 PHE A 518 2655 3108 2421 160 351 431 C ATOM 4004 CE2 PHE A 518 -37.658 -49.310 -16.564 1.00 21.31 C ANISOU 4004 CE2 PHE A 518 2591 2972 2535 74 363 505 C ATOM 4005 CZ PHE A 518 -36.733 -48.384 -16.108 1.00 20.75 C ANISOU 4005 CZ PHE A 518 2548 2942 2395 112 329 446 C ATOM 4006 N GLY A 519 -42.744 -47.429 -12.459 1.00 22.96 N ANISOU 4006 N GLY A 519 2702 3452 2569 240 647 649 N ATOM 4007 CA GLY A 519 -44.198 -47.336 -12.402 1.00 23.26 C ANISOU 4007 CA GLY A 519 2682 3512 2644 235 710 691 C ATOM 4008 C GLY A 519 -44.829 -47.336 -13.789 1.00 22.60 C ANISOU 4008 C GLY A 519 2547 3368 2672 164 683 669 C ATOM 4009 O GLY A 519 -44.137 -47.378 -14.808 1.00 21.41 O ANISOU 4009 O GLY A 519 2412 3159 2565 123 619 621 O ATOM 4010 N GLU A 520 -46.156 -47.272 -13.817 1.00 22.97 N ANISOU 4010 N GLU A 520 2530 3435 2761 156 734 704 N ATOM 4011 CA GLU A 520 -46.941 -47.377 -15.049 1.00 22.73 C ANISOU 4011 CA GLU A 520 2440 3360 2838 93 713 692 C ATOM 4012 C GLU A 520 -46.549 -46.399 -16.156 1.00 21.80 C ANISOU 4012 C GLU A 520 2339 3212 2732 85 639 598 C ATOM 4013 O GLU A 520 -46.460 -46.787 -17.321 1.00 21.27 O ANISOU 4013 O GLU A 520 2256 3088 2738 28 592 578 O ATOM 4014 CB GLU A 520 -48.428 -47.179 -14.732 1.00 23.46 C ANISOU 4014 CB GLU A 520 2457 3501 2955 104 780 736 C ATOM 4015 CG GLU A 520 -49.343 -47.210 -15.960 1.00 23.94 C ANISOU 4015 CG GLU A 520 2444 3529 3122 45 755 719 C ATOM 4016 CD GLU A 520 -50.774 -46.810 -15.647 1.00 27.16 C ANISOU 4016 CD GLU A 520 2774 3997 3550 66 816 752 C ATOM 4017 OE1 GLU A 520 -51.690 -47.299 -16.346 1.00 27.86 O ANISOU 4017 OE1 GLU A 520 2782 4068 3736 10 816 773 O ATOM 4018 OE2 GLU A 520 -50.986 -46.007 -14.711 1.00 28.40 O ANISOU 4018 OE2 GLU A 520 2946 4220 3625 141 862 752 O ATOM 4019 N THR A 521 -46.345 -45.132 -15.801 1.00 21.88 N ANISOU 4019 N THR A 521 2382 3259 2672 144 632 540 N ATOM 4020 CA THR A 521 -46.065 -44.099 -16.799 1.00 21.15 C ANISOU 4020 CA THR A 521 2305 3137 2593 142 574 459 C ATOM 4021 C THR A 521 -44.749 -44.356 -17.539 1.00 20.49 C ANISOU 4021 C THR A 521 2269 2995 2522 107 507 421 C ATOM 4022 O THR A 521 -44.687 -44.166 -18.750 1.00 20.07 O ANISOU 4022 O THR A 521 2206 2898 2520 74 463 386 O ATOM 4023 CB THR A 521 -46.074 -42.672 -16.189 1.00 21.54 C ANISOU 4023 CB THR A 521 2387 3228 2570 213 583 404 C ATOM 4024 OG1 THR A 521 -47.265 -42.485 -15.417 1.00 21.97 O ANISOU 4024 OG1 THR A 521 2399 3344 2605 254 652 444 O ATOM 4025 CG2 THR A 521 -46.026 -41.603 -17.291 1.00 20.23 C ANISOU 4025 CG2 THR A 521 2228 3025 2434 210 535 336 C ATOM 4026 N MET A 522 -43.711 -44.802 -16.829 1.00 20.41 N ANISOU 4026 N MET A 522 2304 2988 2461 119 501 429 N ATOM 4027 CA MET A 522 -42.428 -45.086 -17.478 1.00 20.13 C ANISOU 4027 CA MET A 522 2308 2903 2437 90 443 397 C ATOM 4028 C MET A 522 -42.563 -46.183 -18.538 1.00 19.82 C ANISOU 4028 C MET A 522 2240 2807 2483 27 424 425 C ATOM 4029 O MET A 522 -42.020 -46.061 -19.628 1.00 19.32 O ANISOU 4029 O MET A 522 2188 2699 2453 0 374 383 O ATOM 4030 CB MET A 522 -41.362 -45.490 -16.457 1.00 20.55 C ANISOU 4030 CB MET A 522 2406 2979 2422 119 441 409 C ATOM 4031 CG MET A 522 -39.972 -45.652 -17.054 1.00 20.20 C ANISOU 4031 CG MET A 522 2397 2893 2384 98 381 371 C ATOM 4032 SD MET A 522 -39.193 -44.062 -17.404 1.00 21.62 S ANISOU 4032 SD MET A 522 2609 3069 2538 116 333 271 S ATOM 4033 CE MET A 522 -38.663 -43.597 -15.767 1.00 22.71 C ANISOU 4033 CE MET A 522 2783 3276 2569 181 343 253 C ATOM 4034 N VAL A 523 -43.302 -47.242 -18.224 1.00 20.57 N ANISOU 4034 N VAL A 523 2299 2902 2615 4 465 495 N ATOM 4035 CA VAL A 523 -43.427 -48.364 -19.145 1.00 20.31 C ANISOU 4035 CA VAL A 523 2242 2808 2666 -58 446 517 C ATOM 4036 C VAL A 523 -44.290 -47.991 -20.349 1.00 20.35 C ANISOU 4036 C VAL A 523 2200 2796 2735 -89 420 483 C ATOM 4037 O VAL A 523 -43.928 -48.266 -21.492 1.00 19.56 O ANISOU 4037 O VAL A 523 2106 2648 2678 -123 370 450 O ATOM 4038 CB VAL A 523 -44.017 -49.603 -18.452 1.00 21.11 C ANISOU 4038 CB VAL A 523 2315 2906 2801 -79 502 604 C ATOM 4039 CG1 VAL A 523 -44.177 -50.743 -19.448 1.00 20.49 C ANISOU 4039 CG1 VAL A 523 2212 2754 2819 -147 477 616 C ATOM 4040 CG2 VAL A 523 -43.133 -50.025 -17.276 1.00 21.85 C ANISOU 4040 CG2 VAL A 523 2458 3020 2822 -38 527 645 C ATOM 4041 N GLU A 524 -45.425 -47.350 -20.092 1.00 20.73 N ANISOU 4041 N GLU A 524 2202 2888 2785 -71 454 491 N ATOM 4042 CA GLU A 524 -46.386 -47.075 -21.153 1.00 20.98 C ANISOU 4042 CA GLU A 524 2179 2914 2878 -96 432 467 C ATOM 4043 C GLU A 524 -45.961 -45.959 -22.111 1.00 20.52 C ANISOU 4043 C GLU A 524 2149 2846 2801 -75 379 396 C ATOM 4044 O GLU A 524 -46.472 -45.879 -23.227 1.00 20.28 O ANISOU 4044 O GLU A 524 2087 2802 2819 -96 344 371 O ATOM 4045 CB GLU A 524 -47.762 -46.811 -20.546 1.00 21.82 C ANISOU 4045 CB GLU A 524 2219 3075 2996 -80 489 506 C ATOM 4046 CG GLU A 524 -48.307 -48.033 -19.792 1.00 23.20 C ANISOU 4046 CG GLU A 524 2354 3250 3211 -112 545 587 C ATOM 4047 CD GLU A 524 -48.483 -49.256 -20.692 1.00 25.15 C ANISOU 4047 CD GLU A 524 2567 3432 3555 -190 514 598 C ATOM 4048 OE1 GLU A 524 -49.154 -49.136 -21.737 1.00 25.65 O ANISOU 4048 OE1 GLU A 524 2582 3487 3678 -219 475 563 O ATOM 4049 OE2 GLU A 524 -47.947 -50.340 -20.363 1.00 24.66 O ANISOU 4049 OE2 GLU A 524 2530 3329 3512 -218 526 638 O ATOM 4050 N LEU A 525 -45.029 -45.115 -21.674 1.00 20.41 N ANISOU 4050 N LEU A 525 2194 2841 2719 -33 374 363 N ATOM 4051 CA LEU A 525 -44.381 -44.139 -22.553 1.00 19.76 C ANISOU 4051 CA LEU A 525 2148 2737 2624 -19 328 302 C ATOM 4052 C LEU A 525 -43.118 -44.727 -23.172 1.00 19.26 C ANISOU 4052 C LEU A 525 2126 2625 2568 -47 285 285 C ATOM 4053 O LEU A 525 -42.896 -44.605 -24.379 1.00 19.24 O ANISOU 4053 O LEU A 525 2127 2591 2591 -62 244 255 O ATOM 4054 CB LEU A 525 -44.033 -42.850 -21.798 1.00 19.87 C ANISOU 4054 CB LEU A 525 2200 2778 2573 36 343 270 C ATOM 4055 CG LEU A 525 -45.135 -41.790 -21.696 1.00 20.31 C ANISOU 4055 CG LEU A 525 2227 2868 2623 78 369 259 C ATOM 4056 CD1 LEU A 525 -46.330 -42.298 -20.905 1.00 20.37 C ANISOU 4056 CD1 LEU A 525 2178 2924 2638 84 424 313 C ATOM 4057 CD2 LEU A 525 -44.589 -40.494 -21.083 1.00 20.31 C ANISOU 4057 CD2 LEU A 525 2278 2876 2564 129 375 212 C ATOM 4058 N GLY A 526 -42.287 -45.356 -22.343 1.00 19.28 N ANISOU 4058 N GLY A 526 2159 2626 2541 -47 295 306 N ATOM 4059 CA GLY A 526 -40.998 -45.887 -22.792 1.00 18.66 C ANISOU 4059 CA GLY A 526 2119 2507 2462 -65 258 291 C ATOM 4060 C GLY A 526 -41.107 -46.947 -23.871 1.00 18.77 C ANISOU 4060 C GLY A 526 2117 2476 2539 -110 231 299 C ATOM 4061 O GLY A 526 -40.355 -46.926 -24.841 1.00 18.50 O ANISOU 4061 O GLY A 526 2106 2410 2514 -118 192 266 O ATOM 4062 N ALA A 527 -42.056 -47.872 -23.711 1.00 19.08 N ANISOU 4062 N ALA A 527 2116 2511 2624 -138 253 341 N ATOM 4063 CA ALA A 527 -42.158 -49.021 -24.610 1.00 18.75 C ANISOU 4063 CA ALA A 527 2059 2418 2646 -185 226 345 C ATOM 4064 C ALA A 527 -42.475 -48.631 -26.063 1.00 18.65 C ANISOU 4064 C ALA A 527 2032 2392 2663 -195 179 295 C ATOM 4065 O ALA A 527 -41.776 -49.069 -26.975 1.00 18.16 O ANISOU 4065 O ALA A 527 1996 2291 2612 -207 140 268 O ATOM 4066 CB ALA A 527 -43.166 -50.042 -24.073 1.00 19.26 C ANISOU 4066 CB ALA A 527 2078 2476 2764 -219 264 402 C ATOM 4067 N PRO A 528 -43.509 -47.791 -26.289 1.00 18.84 N ANISOU 4067 N PRO A 528 2015 2450 2691 -183 183 284 N ATOM 4068 CA PRO A 528 -43.754 -47.321 -27.658 1.00 18.82 C ANISOU 4068 CA PRO A 528 2004 2443 2703 -180 137 239 C ATOM 4069 C PRO A 528 -42.537 -46.667 -28.315 1.00 18.28 C ANISOU 4069 C PRO A 528 1994 2359 2593 -153 110 202 C ATOM 4070 O PRO A 528 -42.183 -47.026 -29.442 1.00 18.41 O ANISOU 4070 O PRO A 528 2023 2348 2623 -163 69 175 O ATOM 4071 CB PRO A 528 -44.883 -46.301 -27.483 1.00 19.24 C ANISOU 4071 CB PRO A 528 2014 2546 2751 -153 157 240 C ATOM 4072 CG PRO A 528 -45.596 -46.747 -26.271 1.00 19.81 C ANISOU 4072 CG PRO A 528 2048 2642 2838 -164 209 290 C ATOM 4073 CD PRO A 528 -44.568 -47.349 -25.365 1.00 19.60 C ANISOU 4073 CD PRO A 528 2068 2594 2783 -168 231 315 C ATOM 4074 N PHE A 529 -41.899 -45.721 -27.627 1.00 18.19 N ANISOU 4074 N PHE A 529 2016 2364 2533 -120 132 199 N ATOM 4075 CA PHE A 529 -40.719 -45.056 -28.199 1.00 17.75 C ANISOU 4075 CA PHE A 529 2008 2291 2447 -100 111 168 C ATOM 4076 C PHE A 529 -39.621 -46.078 -28.505 1.00 17.78 C ANISOU 4076 C PHE A 529 2040 2259 2456 -121 91 167 C ATOM 4077 O PHE A 529 -38.979 -46.034 -29.559 1.00 17.00 O ANISOU 4077 O PHE A 529 1964 2139 2357 -117 63 143 O ATOM 4078 CB PHE A 529 -40.130 -44.012 -27.250 1.00 17.69 C ANISOU 4078 CB PHE A 529 2027 2299 2394 -71 136 161 C ATOM 4079 CG PHE A 529 -40.986 -42.787 -27.036 1.00 17.52 C ANISOU 4079 CG PHE A 529 1991 2304 2361 -39 156 153 C ATOM 4080 CD1 PHE A 529 -41.302 -42.377 -25.746 1.00 18.52 C ANISOU 4080 CD1 PHE A 529 2115 2461 2460 -19 191 162 C ATOM 4081 CD2 PHE A 529 -41.422 -42.012 -28.104 1.00 17.95 C ANISOU 4081 CD2 PHE A 529 2039 2354 2425 -21 140 135 C ATOM 4082 CE1 PHE A 529 -42.067 -41.233 -25.518 1.00 18.74 C ANISOU 4082 CE1 PHE A 529 2133 2511 2475 18 212 151 C ATOM 4083 CE2 PHE A 529 -42.196 -40.865 -27.886 1.00 18.69 C ANISOU 4083 CE2 PHE A 529 2122 2468 2509 16 161 129 C ATOM 4084 CZ PHE A 529 -42.515 -40.477 -26.589 1.00 19.39 C ANISOU 4084 CZ PHE A 529 2208 2584 2575 35 197 135 C ATOM 4085 N SER A 530 -39.409 -46.993 -27.565 1.00 18.06 N ANISOU 4085 N SER A 530 2077 2289 2495 -136 109 198 N ATOM 4086 CA SER A 530 -38.308 -47.950 -27.644 1.00 18.30 C ANISOU 4086 CA SER A 530 2138 2288 2528 -147 95 202 C ATOM 4087 C SER A 530 -38.473 -48.935 -28.804 1.00 18.59 C ANISOU 4087 C SER A 530 2170 2285 2608 -171 63 189 C ATOM 4088 O SER A 530 -37.579 -49.080 -29.648 1.00 18.28 O ANISOU 4088 O SER A 530 2160 2225 2562 -163 38 165 O ATOM 4089 CB SER A 530 -38.182 -48.706 -26.313 1.00 18.60 C ANISOU 4089 CB SER A 530 2178 2331 2557 -150 126 246 C ATOM 4090 OG SER A 530 -37.266 -49.779 -26.409 1.00 20.33 O ANISOU 4090 OG SER A 530 2423 2515 2786 -157 114 257 O ATOM 4091 N LEU A 531 -39.613 -49.610 -28.843 1.00 19.00 N ANISOU 4091 N LEU A 531 2184 2328 2705 -201 64 203 N ATOM 4092 CA LEU A 531 -39.835 -50.673 -29.826 1.00 19.56 C ANISOU 4092 CA LEU A 531 2250 2357 2825 -229 30 184 C ATOM 4093 C LEU A 531 -39.946 -50.121 -31.249 1.00 19.50 C ANISOU 4093 C LEU A 531 2244 2356 2809 -214 -12 135 C ATOM 4094 O LEU A 531 -39.473 -50.741 -32.199 1.00 19.37 O ANISOU 4094 O LEU A 531 2250 2309 2800 -215 -45 106 O ATOM 4095 CB LEU A 531 -41.072 -51.494 -29.459 1.00 20.01 C ANISOU 4095 CB LEU A 531 2257 2402 2943 -272 42 210 C ATOM 4096 CG LEU A 531 -41.000 -52.207 -28.098 1.00 20.57 C ANISOU 4096 CG LEU A 531 2330 2462 3026 -285 90 270 C ATOM 4097 CD1 LEU A 531 -42.279 -52.983 -27.817 1.00 21.77 C ANISOU 4097 CD1 LEU A 531 2425 2598 3248 -331 109 301 C ATOM 4098 CD2 LEU A 531 -39.782 -53.135 -28.022 1.00 21.27 C ANISOU 4098 CD2 LEU A 531 2468 2503 3109 -280 85 279 C ATOM 4099 N LYS A 532 -40.552 -48.946 -31.389 1.00 19.84 N ANISOU 4099 N LYS A 532 2266 2441 2832 -193 -8 127 N ATOM 4100 CA LYS A 532 -40.629 -48.276 -32.682 1.00 20.39 C ANISOU 4100 CA LYS A 532 2342 2524 2882 -167 -42 90 C ATOM 4101 C LYS A 532 -39.227 -47.927 -33.197 1.00 20.09 C ANISOU 4101 C LYS A 532 2357 2473 2803 -137 -46 76 C ATOM 4102 O LYS A 532 -38.927 -48.120 -34.378 1.00 20.39 O ANISOU 4102 O LYS A 532 2413 2501 2832 -123 -77 48 O ATOM 4103 CB LYS A 532 -41.507 -47.022 -32.563 1.00 20.56 C ANISOU 4103 CB LYS A 532 2334 2590 2889 -142 -28 94 C ATOM 4104 CG LYS A 532 -41.497 -46.089 -33.747 1.00 21.45 C ANISOU 4104 CG LYS A 532 2459 2719 2971 -101 -52 69 C ATOM 4105 CD LYS A 532 -42.090 -46.676 -34.999 1.00 22.29 C ANISOU 4105 CD LYS A 532 2547 2828 3093 -104 -103 36 C ATOM 4106 CE LYS A 532 -42.226 -45.560 -36.041 1.00 22.75 C ANISOU 4106 CE LYS A 532 2617 2917 3112 -51 -119 23 C ATOM 4107 NZ LYS A 532 -42.552 -46.043 -37.389 1.00 22.43 N ANISOU 4107 NZ LYS A 532 2571 2885 3066 -39 -173 -14 N ATOM 4108 N GLY A 533 -38.369 -47.430 -32.310 1.00 19.92 N ANISOU 4108 N GLY A 533 2358 2455 2756 -127 -14 96 N ATOM 4109 CA GLY A 533 -37.002 -47.076 -32.673 1.00 19.72 C ANISOU 4109 CA GLY A 533 2373 2419 2700 -105 -13 87 C ATOM 4110 C GLY A 533 -36.180 -48.282 -33.098 1.00 20.04 C ANISOU 4110 C GLY A 533 2437 2428 2750 -112 -30 79 C ATOM 4111 O GLY A 533 -35.304 -48.175 -33.962 1.00 20.62 O ANISOU 4111 O GLY A 533 2537 2496 2804 -90 -40 64 O ATOM 4112 N LEU A 534 -36.470 -49.437 -32.503 1.00 19.34 N ANISOU 4112 N LEU A 534 2339 2317 2693 -140 -31 94 N ATOM 4113 CA LEU A 534 -35.727 -50.656 -32.805 1.00 19.19 C ANISOU 4113 CA LEU A 534 2346 2260 2688 -144 -44 89 C ATOM 4114 C LEU A 534 -36.194 -51.274 -34.125 1.00 19.34 C ANISOU 4114 C LEU A 534 2366 2257 2726 -147 -84 50 C ATOM 4115 O LEU A 534 -35.382 -51.557 -35.005 1.00 19.07 O ANISOU 4115 O LEU A 534 2363 2209 2674 -123 -100 26 O ATOM 4116 CB LEU A 534 -35.854 -51.662 -31.652 1.00 19.26 C ANISOU 4116 CB LEU A 534 2349 2245 2726 -170 -25 125 C ATOM 4117 CG LEU A 534 -35.159 -51.237 -30.351 1.00 18.87 C ANISOU 4117 CG LEU A 534 2305 2219 2644 -156 7 159 C ATOM 4118 CD1 LEU A 534 -35.682 -52.025 -29.163 1.00 18.48 C ANISOU 4118 CD1 LEU A 534 2243 2160 2617 -177 33 204 C ATOM 4119 CD2 LEU A 534 -33.638 -51.383 -30.466 1.00 18.88 C ANISOU 4119 CD2 LEU A 534 2339 2215 2620 -130 4 154 C ATOM 4120 N MET A 535 -37.500 -51.471 -34.268 1.00 19.35 N ANISOU 4120 N MET A 535 2332 2259 2762 -173 -101 40 N ATOM 4121 CA MET A 535 -38.036 -52.120 -35.458 1.00 19.71 C ANISOU 4121 CA MET A 535 2374 2287 2828 -179 -147 -5 C ATOM 4122 C MET A 535 -38.089 -51.198 -36.683 1.00 19.82 C ANISOU 4122 C MET A 535 2395 2339 2796 -138 -172 -38 C ATOM 4123 O MET A 535 -38.171 -51.687 -37.811 1.00 20.16 O ANISOU 4123 O MET A 535 2450 2373 2835 -126 -213 -82 O ATOM 4124 CB MET A 535 -39.424 -52.708 -35.179 1.00 20.33 C ANISOU 4124 CB MET A 535 2402 2354 2969 -227 -160 -6 C ATOM 4125 CG MET A 535 -39.465 -53.752 -34.054 1.00 20.74 C ANISOU 4125 CG MET A 535 2447 2360 3073 -269 -131 33 C ATOM 4126 SD MET A 535 -38.213 -55.053 -34.181 1.00 21.88 S ANISOU 4126 SD MET A 535 2650 2437 3228 -263 -136 27 S ATOM 4127 CE MET A 535 -38.721 -55.848 -35.708 1.00 20.89 C ANISOU 4127 CE MET A 535 2525 2275 3135 -274 -203 -50 C ATOM 4128 N GLY A 536 -38.052 -49.886 -36.464 1.00 19.34 N ANISOU 4128 N GLY A 536 2330 2319 2701 -114 -147 -17 N ATOM 4129 CA GLY A 536 -38.074 -48.914 -37.562 1.00 19.90 C ANISOU 4129 CA GLY A 536 2411 2424 2728 -69 -160 -34 C ATOM 4130 C GLY A 536 -36.779 -48.868 -38.375 1.00 19.73 C ANISOU 4130 C GLY A 536 2437 2396 2664 -30 -157 -43 C ATOM 4131 O GLY A 536 -36.733 -48.290 -39.456 1.00 20.95 O ANISOU 4131 O GLY A 536 2607 2575 2780 11 -169 -56 O ATOM 4132 N ASN A 537 -35.725 -49.475 -37.856 1.00 19.43 N ANISOU 4132 N ASN A 537 2421 2328 2632 -40 -138 -31 N ATOM 4133 CA ASN A 537 -34.425 -49.504 -38.524 1.00 18.93 C ANISOU 4133 CA ASN A 537 2397 2262 2535 -3 -129 -35 C ATOM 4134 C ASN A 537 -34.530 -50.144 -39.915 1.00 18.80 C ANISOU 4134 C ASN A 537 2402 2243 2497 26 -168 -80 C ATOM 4135 O ASN A 537 -35.248 -51.134 -40.085 1.00 18.83 O ANISOU 4135 O ASN A 537 2397 2225 2531 4 -206 -113 O ATOM 4136 CB ASN A 537 -33.442 -50.277 -37.646 1.00 18.63 C ANISOU 4136 CB ASN A 537 2370 2192 2515 -19 -110 -18 C ATOM 4137 CG ASN A 537 -32.012 -50.078 -38.057 1.00 18.52 C ANISOU 4137 CG ASN A 537 2383 2185 2470 16 -89 -11 C ATOM 4138 OD1 ASN A 537 -31.572 -50.620 -39.065 1.00 19.18 O ANISOU 4138 OD1 ASN A 537 2492 2262 2535 47 -102 -35 O ATOM 4139 ND2 ASN A 537 -31.269 -49.294 -37.275 1.00 17.48 N ANISOU 4139 ND2 ASN A 537 2243 2066 2334 13 -55 19 N ATOM 4140 N PRO A 538 -33.834 -49.582 -40.921 1.00 18.39 N ANISOU 4140 N PRO A 538 2377 2216 2396 77 -159 -81 N ATOM 4141 CA PRO A 538 -33.941 -50.188 -42.247 1.00 18.73 C ANISOU 4141 CA PRO A 538 2445 2266 2407 115 -197 -127 C ATOM 4142 C PRO A 538 -33.500 -51.647 -42.331 1.00 18.97 C ANISOU 4142 C PRO A 538 2498 2253 2458 108 -218 -162 C ATOM 4143 O PRO A 538 -33.996 -52.369 -43.193 1.00 19.64 O ANISOU 4143 O PRO A 538 2596 2332 2536 121 -265 -215 O ATOM 4144 CB PRO A 538 -33.014 -49.322 -43.113 1.00 19.13 C ANISOU 4144 CB PRO A 538 2523 2348 2398 174 -165 -107 C ATOM 4145 CG PRO A 538 -32.116 -48.670 -42.166 1.00 18.43 C ANISOU 4145 CG PRO A 538 2426 2252 2327 156 -112 -58 C ATOM 4146 CD PRO A 538 -32.938 -48.412 -40.951 1.00 18.09 C ANISOU 4146 CD PRO A 538 2348 2198 2328 104 -113 -44 C ATOM 4147 N ILE A 539 -32.597 -52.095 -41.459 1.00 18.86 N ANISOU 4147 N ILE A 539 2490 2207 2468 91 -188 -136 N ATOM 4148 CA ILE A 539 -32.177 -53.497 -41.525 1.00 19.16 C ANISOU 4148 CA ILE A 539 2554 2198 2529 90 -206 -165 C ATOM 4149 C ILE A 539 -33.339 -54.441 -41.207 1.00 19.56 C ANISOU 4149 C ILE A 539 2588 2206 2638 39 -246 -195 C ATOM 4150 O ILE A 539 -33.283 -55.615 -41.556 1.00 19.89 O ANISOU 4150 O ILE A 539 2653 2201 2701 39 -273 -235 O ATOM 4151 CB ILE A 539 -30.923 -53.847 -40.671 1.00 19.22 C ANISOU 4151 CB ILE A 539 2572 2184 2549 91 -167 -128 C ATOM 4152 CG1 ILE A 539 -31.232 -53.903 -39.172 1.00 19.77 C ANISOU 4152 CG1 ILE A 539 2611 2234 2665 38 -150 -88 C ATOM 4153 CG2 ILE A 539 -29.772 -52.882 -40.973 1.00 19.13 C ANISOU 4153 CG2 ILE A 539 2564 2213 2490 133 -126 -98 C ATOM 4154 CD1 ILE A 539 -30.309 -54.857 -38.435 1.00 20.67 C ANISOU 4154 CD1 ILE A 539 2742 2311 2802 40 -133 -68 C ATOM 4155 N CYS A 540 -34.389 -53.919 -40.567 1.00 19.39 N ANISOU 4155 N CYS A 540 2524 2198 2645 -3 -247 -176 N ATOM 4156 CA CYS A 540 -35.589 -54.706 -40.282 1.00 19.84 C ANISOU 4156 CA CYS A 540 2552 2221 2764 -56 -281 -199 C ATOM 4157 C CYS A 540 -36.581 -54.753 -41.444 1.00 20.32 C ANISOU 4157 C CYS A 540 2602 2302 2817 -48 -340 -261 C ATOM 4158 O CYS A 540 -37.544 -55.513 -41.398 1.00 20.53 O ANISOU 4158 O CYS A 540 2602 2298 2902 -93 -377 -292 O ATOM 4159 CB CYS A 540 -36.289 -54.180 -39.031 1.00 19.60 C ANISOU 4159 CB CYS A 540 2476 2203 2770 -101 -252 -149 C ATOM 4160 SG CYS A 540 -35.274 -54.274 -37.573 1.00 20.36 S ANISOU 4160 SG CYS A 540 2582 2279 2875 -111 -195 -84 S ATOM 4161 N SER A 541 -36.342 -53.964 -42.493 1.00 19.94 N ANISOU 4161 N SER A 541 2572 2307 2698 11 -349 -277 N ATOM 4162 CA SER A 541 -37.253 -53.935 -43.632 1.00 20.59 C ANISOU 4162 CA SER A 541 2645 2421 2757 31 -409 -336 C ATOM 4163 C SER A 541 -37.030 -55.171 -44.514 1.00 21.41 C ANISOU 4163 C SER A 541 2786 2487 2861 46 -457 -409 C ATOM 4164 O SER A 541 -35.934 -55.739 -44.529 1.00 21.04 O ANISOU 4164 O SER A 541 2785 2406 2805 69 -434 -408 O ATOM 4165 CB SER A 541 -37.091 -52.633 -44.435 1.00 20.31 C ANISOU 4165 CB SER A 541 2620 2457 2641 97 -398 -319 C ATOM 4166 OG SER A 541 -35.857 -52.591 -45.135 1.00 19.99 O ANISOU 4166 OG SER A 541 2632 2423 2538 157 -375 -318 O ATOM 4167 N PRO A 542 -38.072 -55.602 -45.240 1.00 22.07 N ANISOU 4167 N PRO A 542 2851 2577 2959 36 -527 -478 N ATOM 4168 CA PRO A 542 -37.959 -56.816 -46.053 1.00 23.26 C ANISOU 4168 CA PRO A 542 3038 2685 3116 47 -580 -560 C ATOM 4169 C PRO A 542 -36.815 -56.826 -47.072 1.00 23.68 C ANISOU 4169 C PRO A 542 3159 2759 3079 134 -573 -584 C ATOM 4170 O PRO A 542 -36.235 -57.878 -47.304 1.00 23.92 O ANISOU 4170 O PRO A 542 3232 2735 3123 143 -584 -626 O ATOM 4171 CB PRO A 542 -39.320 -56.921 -46.761 1.00 24.15 C ANISOU 4171 CB PRO A 542 3108 2825 3241 31 -661 -631 C ATOM 4172 CG PRO A 542 -40.168 -55.821 -46.237 1.00 23.53 C ANISOU 4172 CG PRO A 542 2969 2803 3170 10 -644 -578 C ATOM 4173 CD PRO A 542 -39.461 -55.118 -45.140 1.00 22.55 C ANISOU 4173 CD PRO A 542 2847 2674 3047 3 -559 -483 C ATOM 4174 N GLN A 543 -36.464 -55.687 -47.672 1.00 24.02 N ANISOU 4174 N GLN A 543 3214 2878 3035 200 -549 -553 N ATOM 4175 CA GLN A 543 -35.364 -55.713 -48.651 1.00 24.47 C ANISOU 4175 CA GLN A 543 3333 2958 3007 285 -534 -568 C ATOM 4176 C GLN A 543 -33.979 -55.827 -48.023 1.00 23.44 C ANISOU 4176 C GLN A 543 3229 2795 2882 293 -462 -512 C ATOM 4177 O GLN A 543 -33.040 -56.247 -48.699 1.00 24.22 O ANISOU 4177 O GLN A 543 3377 2894 2933 353 -451 -533 O ATOM 4178 CB GLN A 543 -35.431 -54.544 -49.644 1.00 25.24 C ANISOU 4178 CB GLN A 543 3438 3145 3005 361 -531 -553 C ATOM 4179 CG GLN A 543 -36.442 -54.745 -50.778 1.00 27.50 C ANISOU 4179 CG GLN A 543 3724 3475 3249 395 -616 -637 C ATOM 4180 CD GLN A 543 -36.127 -55.938 -51.683 1.00 31.29 C ANISOU 4180 CD GLN A 543 4256 3931 3701 434 -667 -731 C ATOM 4181 OE1 GLN A 543 -36.188 -57.097 -51.259 1.00 33.50 O ANISOU 4181 OE1 GLN A 543 4538 4132 4056 380 -693 -778 O ATOM 4182 NE2 GLN A 543 -35.810 -55.657 -52.939 1.00 32.88 N ANISOU 4182 NE2 GLN A 543 4502 4199 3793 531 -680 -759 N ATOM 4183 N TYR A 544 -33.853 -55.484 -46.742 1.00 22.03 N ANISOU 4183 N TYR A 544 3018 2593 2760 237 -416 -443 N ATOM 4184 CA TYR A 544 -32.588 -55.656 -46.014 1.00 21.11 C ANISOU 4184 CA TYR A 544 2917 2447 2656 239 -356 -392 C ATOM 4185 C TYR A 544 -32.511 -56.962 -45.227 1.00 21.23 C ANISOU 4185 C TYR A 544 2938 2380 2748 192 -364 -407 C ATOM 4186 O TYR A 544 -31.422 -57.512 -45.075 1.00 21.25 O ANISOU 4186 O TYR A 544 2971 2354 2749 218 -335 -396 O ATOM 4187 CB TYR A 544 -32.362 -54.513 -45.032 1.00 20.15 C ANISOU 4187 CB TYR A 544 2760 2350 2544 214 -300 -311 C ATOM 4188 CG TYR A 544 -31.833 -53.233 -45.638 1.00 18.99 C ANISOU 4188 CG TYR A 544 2619 2268 2329 268 -262 -273 C ATOM 4189 CD1 TYR A 544 -30.535 -52.811 -45.376 1.00 18.32 C ANISOU 4189 CD1 TYR A 544 2542 2192 2228 290 -202 -223 C ATOM 4190 CD2 TYR A 544 -32.636 -52.424 -46.437 1.00 19.33 C ANISOU 4190 CD2 TYR A 544 2655 2361 2327 295 -284 -283 C ATOM 4191 CE1 TYR A 544 -30.037 -51.633 -45.911 1.00 18.22 C ANISOU 4191 CE1 TYR A 544 2531 2228 2164 333 -161 -183 C ATOM 4192 CE2 TYR A 544 -32.137 -51.237 -46.982 1.00 18.28 C ANISOU 4192 CE2 TYR A 544 2531 2280 2135 346 -241 -239 C ATOM 4193 CZ TYR A 544 -30.836 -50.854 -46.704 1.00 18.43 C ANISOU 4193 CZ TYR A 544 2558 2298 2148 361 -178 -188 C ATOM 4194 OH TYR A 544 -30.323 -49.685 -47.218 1.00 18.70 O ANISOU 4194 OH TYR A 544 2596 2373 2136 404 -130 -139 O ATOM 4195 N TRP A 545 -33.644 -57.439 -44.708 1.00 21.19 N ANISOU 4195 N TRP A 545 2902 2337 2813 124 -400 -426 N ATOM 4196 CA TRP A 545 -33.643 -58.597 -43.799 1.00 21.18 C ANISOU 4196 CA TRP A 545 2902 2252 2896 72 -397 -422 C ATOM 4197 C TRP A 545 -33.527 -59.910 -44.567 1.00 22.08 C ANISOU 4197 C TRP A 545 3061 2304 3025 90 -441 -501 C ATOM 4198 O TRP A 545 -34.496 -60.665 -44.731 1.00 22.18 O ANISOU 4198 O TRP A 545 3062 2269 3096 45 -493 -557 O ATOM 4199 CB TRP A 545 -34.874 -58.596 -42.892 1.00 21.22 C ANISOU 4199 CB TRP A 545 2850 2236 2974 -9 -407 -402 C ATOM 4200 CG TRP A 545 -34.779 -59.603 -41.766 1.00 21.29 C ANISOU 4200 CG TRP A 545 2859 2165 3065 -59 -384 -370 C ATOM 4201 CD1 TRP A 545 -35.555 -60.709 -41.592 1.00 22.21 C ANISOU 4201 CD1 TRP A 545 2967 2207 3267 -115 -414 -402 C ATOM 4202 CD2 TRP A 545 -33.849 -59.590 -40.675 1.00 20.61 C ANISOU 4202 CD2 TRP A 545 2781 2066 2983 -56 -325 -297 C ATOM 4203 NE1 TRP A 545 -35.170 -61.390 -40.459 1.00 21.88 N ANISOU 4203 NE1 TRP A 545 2931 2103 3280 -143 -372 -346 N ATOM 4204 CE2 TRP A 545 -34.127 -60.721 -39.875 1.00 21.13 C ANISOU 4204 CE2 TRP A 545 2847 2050 3132 -104 -319 -282 C ATOM 4205 CE3 TRP A 545 -32.813 -58.729 -40.291 1.00 20.45 C ANISOU 4205 CE3 TRP A 545 2766 2098 2908 -17 -277 -243 C ATOM 4206 CZ2 TRP A 545 -33.405 -61.014 -38.719 1.00 21.49 C ANISOU 4206 CZ2 TRP A 545 2900 2069 3194 -106 -269 -213 C ATOM 4207 CZ3 TRP A 545 -32.097 -59.017 -39.138 1.00 20.60 C ANISOU 4207 CZ3 TRP A 545 2788 2093 2948 -24 -234 -183 C ATOM 4208 CH2 TRP A 545 -32.400 -60.152 -38.363 1.00 20.90 C ANISOU 4208 CH2 TRP A 545 2829 2055 3057 -63 -231 -167 C ATOM 4209 N LYS A 546 -32.315 -60.168 -45.040 1.00 22.17 N ANISOU 4209 N LYS A 546 3121 2315 2987 158 -418 -507 N ATOM 4210 CA LYS A 546 -32.000 -61.393 -45.757 1.00 23.29 C ANISOU 4210 CA LYS A 546 3316 2398 3135 190 -451 -581 C ATOM 4211 C LYS A 546 -30.505 -61.670 -45.617 1.00 22.87 C ANISOU 4211 C LYS A 546 3302 2335 3053 250 -399 -546 C ATOM 4212 O LYS A 546 -29.730 -60.753 -45.350 1.00 21.77 O ANISOU 4212 O LYS A 546 3148 2255 2868 277 -347 -481 O ATOM 4213 CB LYS A 546 -32.422 -61.300 -47.232 1.00 24.53 C ANISOU 4213 CB LYS A 546 3496 2598 3226 240 -509 -668 C ATOM 4214 CG LYS A 546 -32.000 -60.035 -47.951 1.00 24.99 C ANISOU 4214 CG LYS A 546 3555 2760 3180 308 -484 -641 C ATOM 4215 CD LYS A 546 -32.438 -60.009 -49.427 1.00 25.91 C ANISOU 4215 CD LYS A 546 3699 2924 3220 368 -544 -726 C ATOM 4216 CE LYS A 546 -33.889 -59.577 -49.626 1.00 27.09 C ANISOU 4216 CE LYS A 546 3803 3105 3384 325 -604 -758 C ATOM 4217 NZ LYS A 546 -34.194 -59.245 -51.063 1.00 27.58 N ANISOU 4217 NZ LYS A 546 3889 3242 3348 401 -654 -824 N ATOM 4218 N PRO A 547 -30.092 -62.938 -45.765 1.00 23.67 N ANISOU 4218 N PRO A 547 3449 2358 3186 269 -411 -589 N ATOM 4219 CA PRO A 547 -28.688 -63.287 -45.513 1.00 23.81 C ANISOU 4219 CA PRO A 547 3498 2364 3185 326 -359 -552 C ATOM 4220 C PRO A 547 -27.646 -62.494 -46.310 1.00 23.53 C ANISOU 4220 C PRO A 547 3475 2415 3048 412 -325 -538 C ATOM 4221 O PRO A 547 -26.603 -62.150 -45.760 1.00 22.97 O ANISOU 4221 O PRO A 547 3392 2372 2965 436 -269 -471 O ATOM 4222 CB PRO A 547 -28.617 -64.764 -45.902 1.00 24.79 C ANISOU 4222 CB PRO A 547 3678 2390 3350 344 -392 -625 C ATOM 4223 CG PRO A 547 -29.990 -65.269 -45.733 1.00 25.60 C ANISOU 4223 CG PRO A 547 3764 2430 3534 261 -446 -669 C ATOM 4224 CD PRO A 547 -30.914 -64.130 -46.042 1.00 25.03 C ANISOU 4224 CD PRO A 547 3643 2441 3426 232 -471 -671 C ATOM 4225 N SER A 548 -27.926 -62.208 -47.581 1.00 23.93 N ANISOU 4225 N SER A 548 3547 2514 3031 459 -356 -600 N ATOM 4226 CA SER A 548 -26.940 -61.548 -48.443 1.00 24.02 C ANISOU 4226 CA SER A 548 3576 2606 2946 549 -318 -586 C ATOM 4227 C SER A 548 -26.552 -60.155 -47.940 1.00 22.75 C ANISOU 4227 C SER A 548 3364 2518 2761 536 -261 -493 C ATOM 4228 O SER A 548 -25.429 -59.701 -48.170 1.00 22.83 O ANISOU 4228 O SER A 548 3375 2576 2723 593 -207 -451 O ATOM 4229 CB SER A 548 -27.428 -61.480 -49.893 1.00 24.88 C ANISOU 4229 CB SER A 548 3719 2757 2977 605 -364 -667 C ATOM 4230 OG SER A 548 -28.710 -60.886 -49.988 1.00 25.88 O ANISOU 4230 OG SER A 548 3813 2909 3111 554 -410 -683 O ATOM 4231 N THR A 549 -27.467 -59.492 -47.243 1.00 21.90 N ANISOU 4231 N THR A 549 3212 2418 2693 462 -273 -462 N ATOM 4232 CA THR A 549 -27.185 -58.175 -46.666 1.00 20.72 C ANISOU 4232 CA THR A 549 3017 2325 2532 443 -224 -380 C ATOM 4233 C THR A 549 -26.017 -58.238 -45.686 1.00 20.40 C ANISOU 4233 C THR A 549 2959 2273 2518 440 -170 -317 C ATOM 4234 O THR A 549 -25.247 -57.275 -45.554 1.00 19.74 O ANISOU 4234 O THR A 549 2850 2243 2409 456 -121 -261 O ATOM 4235 CB THR A 549 -28.412 -57.617 -45.925 1.00 20.42 C ANISOU 4235 CB THR A 549 2935 2283 2539 363 -247 -363 C ATOM 4236 OG1 THR A 549 -29.514 -57.514 -46.828 1.00 21.26 O ANISOU 4236 OG1 THR A 549 3048 2410 2621 366 -301 -421 O ATOM 4237 CG2 THR A 549 -28.113 -56.243 -45.315 1.00 19.61 C ANISOU 4237 CG2 THR A 549 2790 2233 2426 345 -197 -286 C ATOM 4238 N PHE A 550 -25.885 -59.380 -45.010 1.00 20.06 N ANISOU 4238 N PHE A 550 2930 2159 2532 422 -181 -327 N ATOM 4239 CA PHE A 550 -24.917 -59.540 -43.937 1.00 19.89 C ANISOU 4239 CA PHE A 550 2891 2127 2541 417 -139 -267 C ATOM 4240 C PHE A 550 -23.768 -60.471 -44.317 1.00 20.56 C ANISOU 4240 C PHE A 550 3011 2190 2611 489 -122 -282 C ATOM 4241 O PHE A 550 -23.071 -60.999 -43.452 1.00 20.58 O ANISOU 4241 O PHE A 550 3008 2165 2648 491 -101 -246 O ATOM 4242 CB PHE A 550 -25.649 -60.011 -42.680 1.00 19.95 C ANISOU 4242 CB PHE A 550 2880 2075 2623 343 -155 -246 C ATOM 4243 CG PHE A 550 -26.860 -59.178 -42.357 1.00 19.42 C ANISOU 4243 CG PHE A 550 2778 2029 2571 278 -173 -237 C ATOM 4244 CD1 PHE A 550 -28.139 -59.640 -42.645 1.00 20.01 C ANISOU 4244 CD1 PHE A 550 2859 2065 2679 238 -221 -287 C ATOM 4245 CD2 PHE A 550 -26.713 -57.907 -41.810 1.00 19.61 C ANISOU 4245 CD2 PHE A 550 2760 2112 2579 258 -142 -183 C ATOM 4246 CE1 PHE A 550 -29.261 -58.860 -42.360 1.00 19.99 C ANISOU 4246 CE1 PHE A 550 2818 2088 2690 184 -236 -277 C ATOM 4247 CE2 PHE A 550 -27.821 -57.117 -41.519 1.00 19.01 C ANISOU 4247 CE2 PHE A 550 2654 2055 2515 207 -155 -176 C ATOM 4248 CZ PHE A 550 -29.099 -57.590 -41.795 1.00 19.02 C ANISOU 4248 CZ PHE A 550 2658 2024 2546 172 -201 -220 C ATOM 4249 N GLY A 551 -23.545 -60.633 -45.616 1.00 21.10 N ANISOU 4249 N GLY A 551 3116 2278 2621 556 -128 -333 N ATOM 4250 CA GLY A 551 -22.470 -61.482 -46.115 1.00 21.96 C ANISOU 4250 CA GLY A 551 3262 2373 2707 637 -108 -353 C ATOM 4251 C GLY A 551 -22.777 -62.969 -46.138 1.00 22.91 C ANISOU 4251 C GLY A 551 3436 2398 2872 643 -147 -414 C ATOM 4252 O GLY A 551 -21.864 -63.784 -46.266 1.00 23.58 O ANISOU 4252 O GLY A 551 3550 2456 2953 706 -128 -423 O ATOM 4253 N GLY A 552 -24.057 -63.322 -46.045 1.00 23.34 N ANISOU 4253 N GLY A 552 3499 2398 2971 580 -200 -457 N ATOM 4254 CA GLY A 552 -24.486 -64.718 -46.141 1.00 24.42 C ANISOU 4254 CA GLY A 552 3686 2432 3162 575 -242 -523 C ATOM 4255 C GLY A 552 -24.943 -65.252 -44.799 1.00 24.55 C ANISOU 4255 C GLY A 552 3683 2372 3273 498 -243 -480 C ATOM 4256 O GLY A 552 -25.011 -64.510 -43.818 1.00 23.25 O ANISOU 4256 O GLY A 552 3468 2242 3125 449 -217 -406 O ATOM 4257 N GLU A 553 -25.247 -66.548 -44.752 1.00 25.84 N ANISOU 4257 N GLU A 553 3890 2429 3499 489 -271 -526 N ATOM 4258 CA GLU A 553 -25.817 -67.152 -43.547 1.00 26.70 C ANISOU 4258 CA GLU A 553 3985 2455 3704 414 -270 -485 C ATOM 4259 C GLU A 553 -24.908 -67.025 -42.322 1.00 26.16 C ANISOU 4259 C GLU A 553 3892 2401 3644 424 -214 -384 C ATOM 4260 O GLU A 553 -25.399 -66.911 -41.199 1.00 25.39 O ANISOU 4260 O GLU A 553 3762 2289 3597 359 -203 -323 O ATOM 4261 CB GLU A 553 -26.197 -68.622 -43.791 1.00 28.26 C ANISOU 4261 CB GLU A 553 4240 2523 3974 408 -305 -552 C ATOM 4262 CG GLU A 553 -27.326 -68.826 -44.818 1.00 30.85 C ANISOU 4262 CG GLU A 553 4583 2826 4313 377 -374 -658 C ATOM 4263 CD GLU A 553 -28.709 -68.391 -44.324 1.00 33.09 C ANISOU 4263 CD GLU A 553 4811 3109 4653 270 -401 -646 C ATOM 4264 OE1 GLU A 553 -28.847 -67.975 -43.154 1.00 33.31 O ANISOU 4264 OE1 GLU A 553 4793 3150 4713 220 -364 -555 O ATOM 4265 OE2 GLU A 553 -29.672 -68.467 -45.122 1.00 36.42 O ANISOU 4265 OE2 GLU A 553 5232 3522 5084 241 -462 -731 O ATOM 4266 N VAL A 554 -23.593 -67.010 -42.530 1.00 26.29 N ANISOU 4266 N VAL A 554 3921 2458 3610 508 -180 -365 N ATOM 4267 CA VAL A 554 -22.653 -66.877 -41.412 1.00 26.34 C ANISOU 4267 CA VAL A 554 3899 2490 3619 525 -133 -275 C ATOM 4268 C VAL A 554 -22.814 -65.522 -40.712 1.00 25.15 C ANISOU 4268 C VAL A 554 3680 2429 3445 475 -116 -214 C ATOM 4269 O VAL A 554 -22.822 -65.445 -39.482 1.00 24.76 O ANISOU 4269 O VAL A 554 3604 2379 3427 440 -99 -147 O ATOM 4270 CB VAL A 554 -21.185 -67.082 -41.865 1.00 26.79 C ANISOU 4270 CB VAL A 554 3972 2582 3626 629 -101 -272 C ATOM 4271 CG1 VAL A 554 -20.215 -66.932 -40.682 1.00 27.39 C ANISOU 4271 CG1 VAL A 554 4009 2693 3705 647 -61 -182 C ATOM 4272 CG2 VAL A 554 -21.022 -68.449 -42.493 1.00 28.67 C ANISOU 4272 CG2 VAL A 554 4282 2725 3888 684 -116 -334 C ATOM 4273 N GLY A 555 -22.962 -64.457 -41.496 1.00 24.48 N ANISOU 4273 N GLY A 555 3574 2423 3305 475 -121 -237 N ATOM 4274 CA GLY A 555 -23.200 -63.127 -40.945 1.00 23.46 C ANISOU 4274 CA GLY A 555 3387 2370 3158 428 -107 -189 C ATOM 4275 C GLY A 555 -24.565 -63.003 -40.297 1.00 22.87 C ANISOU 4275 C GLY A 555 3294 2264 3132 341 -131 -182 C ATOM 4276 O GLY A 555 -24.700 -62.446 -39.215 1.00 22.57 O ANISOU 4276 O GLY A 555 3217 2251 3108 300 -114 -125 O ATOM 4277 N PHE A 556 -25.579 -63.531 -40.972 1.00 23.09 N ANISOU 4277 N PHE A 556 3348 2240 3186 316 -172 -246 N ATOM 4278 CA PHE A 556 -26.961 -63.479 -40.493 1.00 23.21 C ANISOU 4278 CA PHE A 556 3340 2224 3254 233 -197 -246 C ATOM 4279 C PHE A 556 -27.075 -64.200 -39.143 1.00 23.51 C ANISOU 4279 C PHE A 556 3374 2200 3360 195 -177 -187 C ATOM 4280 O PHE A 556 -27.771 -63.736 -38.236 1.00 23.23 O ANISOU 4280 O PHE A 556 3299 2178 3348 137 -168 -142 O ATOM 4281 CB PHE A 556 -27.868 -64.125 -41.551 1.00 23.97 C ANISOU 4281 CB PHE A 556 3467 2269 3372 221 -250 -336 C ATOM 4282 CG PHE A 556 -29.319 -63.705 -41.500 1.00 24.39 C ANISOU 4282 CG PHE A 556 3482 2327 3458 145 -283 -352 C ATOM 4283 CD1 PHE A 556 -29.698 -62.392 -41.224 1.00 24.01 C ANISOU 4283 CD1 PHE A 556 3385 2362 3377 121 -271 -315 C ATOM 4284 CD2 PHE A 556 -30.312 -64.630 -41.803 1.00 26.28 C ANISOU 4284 CD2 PHE A 556 3734 2488 3765 101 -329 -412 C ATOM 4285 CE1 PHE A 556 -31.047 -62.028 -41.212 1.00 24.48 C ANISOU 4285 CE1 PHE A 556 3406 2428 3465 59 -301 -331 C ATOM 4286 CE2 PHE A 556 -31.655 -64.268 -41.801 1.00 26.87 C ANISOU 4286 CE2 PHE A 556 3765 2572 3873 33 -362 -430 C ATOM 4287 CZ PHE A 556 -32.018 -62.966 -41.506 1.00 25.12 C ANISOU 4287 CZ PHE A 556 3493 2437 3612 16 -347 -388 C ATOM 4288 N LYS A 557 -26.370 -65.322 -39.009 1.00 23.87 N ANISOU 4288 N LYS A 557 3461 2179 3431 235 -167 -184 N ATOM 4289 CA LYS A 557 -26.360 -66.088 -37.758 1.00 24.46 C ANISOU 4289 CA LYS A 557 3539 2191 3564 214 -142 -119 C ATOM 4290 C LYS A 557 -25.760 -65.300 -36.591 1.00 23.44 C ANISOU 4290 C LYS A 557 3369 2136 3401 219 -104 -35 C ATOM 4291 O LYS A 557 -26.209 -65.442 -35.448 1.00 23.26 O ANISOU 4291 O LYS A 557 3329 2094 3414 179 -87 24 O ATOM 4292 CB LYS A 557 -25.607 -67.416 -37.936 1.00 25.72 C ANISOU 4292 CB LYS A 557 3757 2265 3752 271 -137 -132 C ATOM 4293 CG LYS A 557 -25.255 -68.089 -36.609 1.00 28.34 C ANISOU 4293 CG LYS A 557 4094 2551 4124 275 -101 -47 C ATOM 4294 CD LYS A 557 -24.736 -69.506 -36.743 1.00 32.50 C ANISOU 4294 CD LYS A 557 4682 2971 4695 325 -96 -57 C ATOM 4295 CE LYS A 557 -24.569 -70.119 -35.344 1.00 34.08 C ANISOU 4295 CE LYS A 557 4885 3127 4936 325 -58 39 C ATOM 4296 NZ LYS A 557 -23.555 -71.206 -35.298 1.00 36.97 N ANISOU 4296 NZ LYS A 557 5304 3429 5315 407 -40 54 N ATOM 4297 N ILE A 558 -24.754 -64.471 -36.869 1.00 22.43 N ANISOU 4297 N ILE A 558 3223 2093 3205 269 -91 -30 N ATOM 4298 CA ILE A 558 -24.157 -63.643 -35.822 1.00 21.78 C ANISOU 4298 CA ILE A 558 3099 2086 3091 272 -64 36 C ATOM 4299 C ILE A 558 -25.230 -62.752 -35.198 1.00 21.07 C ANISOU 4299 C ILE A 558 2969 2029 3008 200 -66 57 C ATOM 4300 O ILE A 558 -25.272 -62.586 -33.976 1.00 20.77 O ANISOU 4300 O ILE A 558 2909 2008 2974 182 -47 116 O ATOM 4301 CB ILE A 558 -22.972 -62.791 -36.341 1.00 21.42 C ANISOU 4301 CB ILE A 558 3030 2126 2981 325 -51 31 C ATOM 4302 CG1 ILE A 558 -21.798 -63.695 -36.735 1.00 21.91 C ANISOU 4302 CG1 ILE A 558 3124 2164 3036 405 -40 24 C ATOM 4303 CG2 ILE A 558 -22.513 -61.790 -35.276 1.00 20.67 C ANISOU 4303 CG2 ILE A 558 2884 2109 2861 313 -32 86 C ATOM 4304 CD1 ILE A 558 -20.718 -62.994 -37.549 1.00 22.15 C ANISOU 4304 CD1 ILE A 558 3135 2272 3011 459 -25 9 C ATOM 4305 N ILE A 559 -26.114 -62.206 -36.033 1.00 20.33 N ANISOU 4305 N ILE A 559 2867 1946 2912 166 -89 8 N ATOM 4306 CA ILE A 559 -27.192 -61.356 -35.540 1.00 20.10 C ANISOU 4306 CA ILE A 559 2799 1948 2890 104 -91 23 C ATOM 4307 C ILE A 559 -28.206 -62.170 -34.752 1.00 20.27 C ANISOU 4307 C ILE A 559 2822 1902 2978 52 -90 49 C ATOM 4308 O ILE A 559 -28.564 -61.823 -33.627 1.00 19.90 O ANISOU 4308 O ILE A 559 2748 1877 2937 23 -68 103 O ATOM 4309 CB ILE A 559 -27.945 -60.650 -36.690 1.00 19.83 C ANISOU 4309 CB ILE A 559 2756 1940 2838 87 -119 -35 C ATOM 4310 CG1 ILE A 559 -27.038 -59.628 -37.379 1.00 19.36 C ANISOU 4310 CG1 ILE A 559 2689 1956 2712 133 -109 -45 C ATOM 4311 CG2 ILE A 559 -29.217 -59.985 -36.166 1.00 19.86 C ANISOU 4311 CG2 ILE A 559 2721 1963 2862 24 -123 -20 C ATOM 4312 CD1 ILE A 559 -27.635 -59.051 -38.646 1.00 20.04 C ANISOU 4312 CD1 ILE A 559 2777 2067 2771 136 -134 -98 C ATOM 4313 N ASN A 560 -28.672 -63.259 -35.351 1.00 21.23 N ANISOU 4313 N ASN A 560 2975 1939 3152 40 -112 9 N ATOM 4314 CA ASN A 560 -29.805 -63.985 -34.792 1.00 21.87 C ANISOU 4314 CA ASN A 560 3051 1950 3310 -22 -112 27 C ATOM 4315 C ASN A 560 -29.475 -64.853 -33.568 1.00 22.39 C ANISOU 4315 C ASN A 560 3131 1964 3411 -16 -74 103 C ATOM 4316 O ASN A 560 -30.391 -65.357 -32.910 1.00 22.99 O ANISOU 4316 O ASN A 560 3196 1988 3551 -69 -60 138 O ATOM 4317 CB ASN A 560 -30.496 -64.784 -35.898 1.00 22.72 C ANISOU 4317 CB ASN A 560 3180 1982 3468 -44 -154 -51 C ATOM 4318 CG ASN A 560 -31.262 -63.889 -36.857 1.00 23.16 C ANISOU 4318 CG ASN A 560 3208 2094 3497 -65 -192 -113 C ATOM 4319 OD1 ASN A 560 -32.087 -63.079 -36.434 1.00 25.53 O ANISOU 4319 OD1 ASN A 560 3461 2441 3797 -108 -188 -90 O ATOM 4320 ND2 ASN A 560 -30.977 -64.013 -38.148 1.00 24.70 N ANISOU 4320 ND2 ASN A 560 3434 2289 3663 -27 -228 -189 N ATOM 4321 N THR A 561 -28.183 -64.996 -33.257 1.00 22.20 N ANISOU 4321 N THR A 561 3130 1960 3347 50 -55 133 N ATOM 4322 CA THR A 561 -27.726 -65.707 -32.056 1.00 22.69 C ANISOU 4322 CA THR A 561 3206 1990 3425 72 -19 212 C ATOM 4323 C THR A 561 -27.032 -64.791 -31.034 1.00 22.05 C ANISOU 4323 C THR A 561 3094 2009 3275 101 4 270 C ATOM 4324 O THR A 561 -26.508 -65.278 -30.026 1.00 22.59 O ANISOU 4324 O THR A 561 3173 2071 3338 134 30 336 O ATOM 4325 CB THR A 561 -26.746 -66.845 -32.416 1.00 23.23 C ANISOU 4325 CB THR A 561 3328 1991 3508 136 -18 204 C ATOM 4326 OG1 THR A 561 -25.523 -66.295 -32.931 1.00 22.70 O ANISOU 4326 OG1 THR A 561 3260 1996 3371 202 -24 180 O ATOM 4327 CG2 THR A 561 -27.370 -67.786 -33.445 1.00 24.59 C ANISOU 4327 CG2 THR A 561 3537 2059 3748 111 -46 135 C ATOM 4328 N ALA A 562 -27.017 -63.484 -31.289 1.00 21.26 N ANISOU 4328 N ALA A 562 2957 1998 3123 92 -7 244 N ATOM 4329 CA ALA A 562 -26.341 -62.543 -30.397 1.00 20.81 C ANISOU 4329 CA ALA A 562 2869 2032 3004 115 7 283 C ATOM 4330 C ALA A 562 -26.992 -62.522 -29.019 1.00 20.90 C ANISOU 4330 C ALA A 562 2865 2053 3021 89 33 349 C ATOM 4331 O ALA A 562 -28.199 -62.749 -28.880 1.00 21.01 O ANISOU 4331 O ALA A 562 2874 2028 3082 35 41 358 O ATOM 4332 CB ALA A 562 -26.325 -61.129 -30.993 1.00 20.24 C ANISOU 4332 CB ALA A 562 2763 2038 2889 103 -8 239 C ATOM 4333 N SER A 563 -26.172 -62.258 -28.006 1.00 20.86 N ANISOU 4333 N SER A 563 2851 2107 2968 130 46 396 N ATOM 4334 CA SER A 563 -26.641 -62.110 -26.637 1.00 20.82 C ANISOU 4334 CA SER A 563 2832 2132 2946 120 72 459 C ATOM 4335 C SER A 563 -25.602 -61.342 -25.835 1.00 20.45 C ANISOU 4335 C SER A 563 2764 2180 2826 167 68 475 C ATOM 4336 O SER A 563 -24.431 -61.287 -26.217 1.00 20.32 O ANISOU 4336 O SER A 563 2747 2190 2786 211 51 454 O ATOM 4337 CB SER A 563 -26.893 -63.475 -25.989 1.00 21.90 C ANISOU 4337 CB SER A 563 3003 2191 3127 131 101 526 C ATOM 4338 OG SER A 563 -25.681 -64.151 -25.700 1.00 21.60 O ANISOU 4338 OG SER A 563 2990 2149 3067 202 103 556 O ATOM 4339 N ILE A 564 -26.021 -60.749 -24.722 1.00 20.26 N ANISOU 4339 N ILE A 564 2721 2212 2766 158 82 510 N ATOM 4340 CA ILE A 564 -25.068 -60.047 -23.861 1.00 20.36 C ANISOU 4340 CA ILE A 564 2712 2316 2707 202 71 519 C ATOM 4341 C ILE A 564 -23.983 -61.016 -23.361 1.00 20.82 C ANISOU 4341 C ILE A 564 2791 2370 2748 272 73 564 C ATOM 4342 O ILE A 564 -22.802 -60.656 -23.314 1.00 20.01 O ANISOU 4342 O ILE A 564 2670 2327 2607 315 49 546 O ATOM 4343 CB ILE A 564 -25.774 -59.287 -22.694 1.00 20.50 C ANISOU 4343 CB ILE A 564 2712 2395 2684 188 86 544 C ATOM 4344 CG1 ILE A 564 -24.797 -58.351 -21.971 1.00 21.51 C ANISOU 4344 CG1 ILE A 564 2815 2621 2739 225 62 527 C ATOM 4345 CG2 ILE A 564 -26.427 -60.250 -21.718 1.00 21.42 C ANISOU 4345 CG2 ILE A 564 2852 2478 2809 198 125 625 C ATOM 4346 CD1 ILE A 564 -24.315 -57.178 -22.810 1.00 21.37 C ANISOU 4346 CD1 ILE A 564 2765 2636 2718 203 32 453 C ATOM 4347 N GLN A 565 -24.366 -62.251 -23.030 1.00 21.71 N ANISOU 4347 N GLN A 565 2940 2411 2896 284 101 624 N ATOM 4348 CA GLN A 565 -23.382 -63.245 -22.594 1.00 22.72 C ANISOU 4348 CA GLN A 565 3095 2527 3012 358 105 673 C ATOM 4349 C GLN A 565 -22.383 -63.581 -23.701 1.00 22.72 C ANISOU 4349 C GLN A 565 3101 2501 3032 388 82 627 C ATOM 4350 O GLN A 565 -21.180 -63.678 -23.442 1.00 22.79 O ANISOU 4350 O GLN A 565 3100 2557 3002 454 68 637 O ATOM 4351 CB GLN A 565 -24.049 -64.531 -22.093 1.00 23.75 C ANISOU 4351 CB GLN A 565 3267 2568 3188 362 147 751 C ATOM 4352 CG GLN A 565 -23.048 -65.606 -21.626 1.00 26.03 C ANISOU 4352 CG GLN A 565 3588 2836 3464 447 155 810 C ATOM 4353 CD GLN A 565 -22.203 -65.173 -20.428 1.00 28.02 C ANISOU 4353 CD GLN A 565 3821 3202 3624 516 144 849 C ATOM 4354 OE1 GLN A 565 -22.592 -65.393 -19.280 1.00 28.48 O ANISOU 4354 OE1 GLN A 565 3891 3280 3649 538 173 922 O ATOM 4355 NE2 GLN A 565 -21.032 -64.569 -20.692 1.00 25.87 N ANISOU 4355 NE2 GLN A 565 3516 3005 3309 553 103 799 N ATOM 4356 N SER A 566 -22.866 -63.769 -24.926 1.00 22.49 N ANISOU 4356 N SER A 566 3085 2401 3059 346 78 577 N ATOM 4357 CA SER A 566 -21.959 -64.110 -26.028 1.00 23.11 C ANISOU 4357 CA SER A 566 3173 2456 3151 381 61 532 C ATOM 4358 C SER A 566 -21.092 -62.910 -26.439 1.00 21.99 C ANISOU 4358 C SER A 566 2984 2409 2963 390 36 481 C ATOM 4359 O SER A 566 -19.931 -63.087 -26.795 1.00 21.78 O ANISOU 4359 O SER A 566 2949 2404 2921 445 27 470 O ATOM 4360 CB SER A 566 -22.706 -64.724 -27.230 1.00 23.10 C ANISOU 4360 CB SER A 566 3206 2355 3218 342 61 488 C ATOM 4361 OG SER A 566 -23.461 -63.763 -27.930 1.00 25.91 O ANISOU 4361 OG SER A 566 3537 2732 3577 280 47 431 O ATOM 4362 N LEU A 567 -21.642 -61.697 -26.368 1.00 21.27 N ANISOU 4362 N LEU A 567 2859 2370 2852 338 28 453 N ATOM 4363 CA LEU A 567 -20.860 -60.483 -26.630 1.00 20.82 C ANISOU 4363 CA LEU A 567 2756 2398 2758 339 9 411 C ATOM 4364 C LEU A 567 -19.640 -60.429 -25.707 1.00 21.06 C ANISOU 4364 C LEU A 567 2759 2501 2743 398 -3 439 C ATOM 4365 O LEU A 567 -18.515 -60.203 -26.153 1.00 21.39 O ANISOU 4365 O LEU A 567 2771 2582 2774 431 -16 417 O ATOM 4366 CB LEU A 567 -21.714 -59.226 -26.439 1.00 20.43 C ANISOU 4366 CB LEU A 567 2680 2386 2695 278 5 387 C ATOM 4367 CG LEU A 567 -21.043 -57.886 -26.773 1.00 20.05 C ANISOU 4367 CG LEU A 567 2586 2409 2623 267 -11 342 C ATOM 4368 CD1 LEU A 567 -20.762 -57.774 -28.269 1.00 20.81 C ANISOU 4368 CD1 LEU A 567 2684 2481 2743 264 -11 299 C ATOM 4369 CD2 LEU A 567 -21.923 -56.738 -26.284 1.00 19.88 C ANISOU 4369 CD2 LEU A 567 2546 2420 2587 217 -12 328 C ATOM 4370 N ILE A 568 -19.872 -60.659 -24.422 1.00 20.94 N ANISOU 4370 N ILE A 568 2749 2507 2699 414 2 491 N ATOM 4371 CA ILE A 568 -18.792 -60.667 -23.430 1.00 21.51 C ANISOU 4371 CA ILE A 568 2797 2656 2720 476 -15 519 C ATOM 4372 C ILE A 568 -17.872 -61.881 -23.599 1.00 22.14 C ANISOU 4372 C ILE A 568 2897 2705 2810 551 -12 552 C ATOM 4373 O ILE A 568 -16.650 -61.745 -23.561 1.00 22.26 O ANISOU 4373 O ILE A 568 2875 2781 2801 600 -33 543 O ATOM 4374 CB ILE A 568 -19.367 -60.570 -21.987 1.00 21.61 C ANISOU 4374 CB ILE A 568 2815 2706 2687 481 -10 567 C ATOM 4375 CG1 ILE A 568 -19.542 -59.096 -21.586 1.00 21.04 C ANISOU 4375 CG1 ILE A 568 2702 2713 2579 440 -31 521 C ATOM 4376 CG2 ILE A 568 -18.464 -61.272 -20.976 1.00 21.63 C ANISOU 4376 CG2 ILE A 568 2821 2753 2645 566 -18 623 C ATOM 4377 CD1 ILE A 568 -20.497 -58.281 -22.491 1.00 20.55 C ANISOU 4377 CD1 ILE A 568 2637 2615 2556 362 -22 471 C ATOM 4378 N CYS A 569 -18.450 -63.062 -23.804 1.00 22.72 N ANISOU 4378 N CYS A 569 3026 2681 2925 559 15 588 N ATOM 4379 CA CYS A 569 -17.656 -64.289 -23.927 1.00 23.89 C ANISOU 4379 CA CYS A 569 3203 2787 3087 635 23 623 C ATOM 4380 C CYS A 569 -16.654 -64.219 -25.086 1.00 23.61 C ANISOU 4380 C CYS A 569 3147 2760 3064 662 10 571 C ATOM 4381 O CYS A 569 -15.496 -64.625 -24.947 1.00 24.05 O ANISOU 4381 O CYS A 569 3187 2851 3101 738 2 588 O ATOM 4382 CB CYS A 569 -18.573 -65.502 -24.108 1.00 24.59 C ANISOU 4382 CB CYS A 569 3358 2750 3234 624 56 659 C ATOM 4383 SG CYS A 569 -17.748 -67.081 -23.895 1.00 27.55 S ANISOU 4383 SG CYS A 569 3780 3061 3625 724 72 722 S ATOM 4384 N ASN A 570 -17.103 -63.699 -26.222 1.00 23.26 N ANISOU 4384 N ASN A 570 3100 2689 3049 606 11 510 N ATOM 4385 CA ASN A 570 -16.256 -63.597 -27.409 1.00 23.33 C ANISOU 4385 CA ASN A 570 3092 2706 3066 631 7 463 C ATOM 4386 C ASN A 570 -15.163 -62.535 -27.317 1.00 23.10 C ANISOU 4386 C ASN A 570 2989 2788 3001 644 -12 441 C ATOM 4387 O ASN A 570 -14.155 -62.631 -28.024 1.00 23.77 O ANISOU 4387 O ASN A 570 3051 2895 3087 689 -10 423 O ATOM 4388 CB ASN A 570 -17.110 -63.318 -28.648 1.00 22.95 C ANISOU 4388 CB ASN A 570 3065 2603 3051 572 12 407 C ATOM 4389 CG ASN A 570 -17.905 -64.528 -29.103 1.00 24.24 C ANISOU 4389 CG ASN A 570 3297 2649 3263 569 26 409 C ATOM 4390 OD1 ASN A 570 -17.434 -65.666 -29.023 1.00 27.56 O ANISOU 4390 OD1 ASN A 570 3754 3019 3700 630 35 436 O ATOM 4391 ND2 ASN A 570 -19.115 -64.288 -29.595 1.00 23.49 N ANISOU 4391 ND2 ASN A 570 3219 2508 3196 499 24 377 N ATOM 4392 N ASN A 571 -15.359 -61.521 -26.476 1.00 22.37 N ANISOU 4392 N ASN A 571 2857 2763 2879 604 -29 441 N ATOM 4393 CA ASN A 571 -14.492 -60.334 -26.497 1.00 22.22 C ANISOU 4393 CA ASN A 571 2765 2838 2839 594 -48 407 C ATOM 4394 C ASN A 571 -13.819 -59.964 -25.179 1.00 22.41 C ANISOU 4394 C ASN A 571 2742 2953 2820 621 -78 428 C ATOM 4395 O ASN A 571 -13.123 -58.948 -25.107 1.00 23.32 O ANISOU 4395 O ASN A 571 2792 3144 2926 604 -99 395 O ATOM 4396 CB ASN A 571 -15.290 -59.132 -26.996 1.00 21.41 C ANISOU 4396 CB ASN A 571 2651 2736 2748 511 -46 363 C ATOM 4397 CG ASN A 571 -15.819 -59.332 -28.392 1.00 21.01 C ANISOU 4397 CG ASN A 571 2636 2616 2732 490 -24 334 C ATOM 4398 OD1 ASN A 571 -15.052 -59.397 -29.351 1.00 21.88 O ANISOU 4398 OD1 ASN A 571 2731 2731 2850 519 -14 315 O ATOM 4399 ND2 ASN A 571 -17.139 -59.434 -28.517 1.00 19.64 N ANISOU 4399 ND2 ASN A 571 2506 2382 2574 442 -17 330 N ATOM 4400 N VAL A 572 -14.024 -60.761 -24.139 1.00 22.65 N ANISOU 4400 N VAL A 572 2805 2977 2825 662 -80 481 N ATOM 4401 CA VAL A 572 -13.437 -60.472 -22.839 1.00 22.63 C ANISOU 4401 CA VAL A 572 2764 3067 2769 698 -112 501 C ATOM 4402 C VAL A 572 -12.665 -61.705 -22.388 1.00 23.76 C ANISOU 4402 C VAL A 572 2922 3212 2895 796 -113 558 C ATOM 4403 O VAL A 572 -13.196 -62.816 -22.402 1.00 23.67 O ANISOU 4403 O VAL A 572 2977 3118 2901 823 -84 606 O ATOM 4404 CB VAL A 572 -14.509 -60.069 -21.802 1.00 22.32 C ANISOU 4404 CB VAL A 572 2748 3037 2697 661 -114 516 C ATOM 4405 CG1 VAL A 572 -13.884 -59.864 -20.420 1.00 22.35 C ANISOU 4405 CG1 VAL A 572 2719 3142 2633 712 -151 535 C ATOM 4406 CG2 VAL A 572 -15.248 -58.794 -22.258 1.00 20.96 C ANISOU 4406 CG2 VAL A 572 2559 2863 2541 571 -114 458 C ATOM 4407 N LYS A 573 -11.406 -61.498 -22.013 1.00 24.62 N ANISOU 4407 N LYS A 573 2966 3413 2976 849 -146 552 N ATOM 4408 CA LYS A 573 -10.511 -62.591 -21.621 1.00 25.94 C ANISOU 4408 CA LYS A 573 3136 3596 3123 953 -151 605 C ATOM 4409 C LYS A 573 -11.146 -63.443 -20.528 1.00 26.41 C ANISOU 4409 C LYS A 573 3259 3628 3146 996 -140 678 C ATOM 4410 O LYS A 573 -11.684 -62.918 -19.548 1.00 26.12 O ANISOU 4410 O LYS A 573 3223 3637 3065 974 -155 686 O ATOM 4411 CB LYS A 573 -9.160 -62.041 -21.147 1.00 26.68 C ANISOU 4411 CB LYS A 573 3137 3815 3184 996 -200 584 C ATOM 4412 CG LYS A 573 -8.071 -63.088 -20.922 1.00 29.60 C ANISOU 4412 CG LYS A 573 3495 4213 3538 1111 -207 631 C ATOM 4413 CD LYS A 573 -6.804 -62.431 -20.382 1.00 32.11 C ANISOU 4413 CD LYS A 573 3708 4667 3824 1144 -263 604 C ATOM 4414 CE LYS A 573 -5.618 -63.373 -20.396 1.00 35.39 C ANISOU 4414 CE LYS A 573 4096 5116 4234 1258 -269 643 C ATOM 4415 NZ LYS A 573 -4.383 -62.701 -19.901 1.00 37.06 N ANISOU 4415 NZ LYS A 573 4193 5467 4421 1285 -328 611 N ATOM 4416 N GLY A 574 -11.100 -64.758 -20.722 1.00 27.08 N ANISOU 4416 N GLY A 574 3400 3635 3252 1060 -110 734 N ATOM 4417 CA GLY A 574 -11.602 -65.710 -19.736 1.00 27.97 C ANISOU 4417 CA GLY A 574 3577 3712 3340 1111 -90 818 C ATOM 4418 C GLY A 574 -13.093 -65.982 -19.822 1.00 27.58 C ANISOU 4418 C GLY A 574 3596 3555 3326 1042 -47 839 C ATOM 4419 O GLY A 574 -13.611 -66.790 -19.052 1.00 28.44 O ANISOU 4419 O GLY A 574 3759 3621 3424 1076 -19 916 O ATOM 4420 N CYS A 575 -13.779 -65.323 -20.757 1.00 26.85 N ANISOU 4420 N CYS A 575 3501 3421 3279 948 -39 776 N ATOM 4421 CA CYS A 575 -15.229 -65.465 -20.935 1.00 26.49 C ANISOU 4421 CA CYS A 575 3508 3282 3274 874 -4 784 C ATOM 4422 C CYS A 575 -15.993 -65.495 -19.605 1.00 26.47 C ANISOU 4422 C CYS A 575 3527 3301 3228 875 10 848 C ATOM 4423 O CYS A 575 -16.616 -66.501 -19.259 1.00 26.96 O ANISOU 4423 O CYS A 575 3648 3283 3314 891 50 919 O ATOM 4424 CB CYS A 575 -15.543 -66.705 -21.789 1.00 27.15 C ANISOU 4424 CB CYS A 575 3656 3231 3430 883 32 802 C ATOM 4425 SG CYS A 575 -17.327 -67.118 -21.907 1.00 28.35 S ANISOU 4425 SG CYS A 575 3869 3260 3645 795 74 822 S ATOM 4426 N PRO A 576 -15.951 -64.386 -18.851 1.00 25.72 N ANISOU 4426 N PRO A 576 3388 3314 3071 858 -19 824 N ATOM 4427 CA PRO A 576 -16.644 -64.343 -17.570 1.00 25.96 C ANISOU 4427 CA PRO A 576 3438 3379 3047 868 -5 881 C ATOM 4428 C PRO A 576 -18.152 -64.385 -17.758 1.00 25.77 C ANISOU 4428 C PRO A 576 3453 3270 3070 788 40 894 C ATOM 4429 O PRO A 576 -18.660 -63.887 -18.770 1.00 24.36 O ANISOU 4429 O PRO A 576 3263 3046 2944 710 40 831 O ATOM 4430 CB PRO A 576 -16.235 -62.984 -17.000 1.00 25.57 C ANISOU 4430 CB PRO A 576 3327 3458 2930 857 -54 823 C ATOM 4431 CG PRO A 576 -16.008 -62.147 -18.200 1.00 24.95 C ANISOU 4431 CG PRO A 576 3207 3371 2900 789 -74 733 C ATOM 4432 CD PRO A 576 -15.366 -63.078 -19.193 1.00 25.38 C ANISOU 4432 CD PRO A 576 3275 3357 3009 822 -63 740 C ATOM 4433 N PHE A 577 -18.852 -64.972 -16.791 1.00 26.55 N ANISOU 4433 N PHE A 577 3591 3350 3148 811 79 978 N ATOM 4434 CA PHE A 577 -20.304 -64.952 -16.789 1.00 27.06 C ANISOU 4434 CA PHE A 577 3679 3349 3252 736 123 997 C ATOM 4435 C PHE A 577 -20.798 -63.513 -16.696 1.00 26.35 C ANISOU 4435 C PHE A 577 3547 3335 3129 674 101 929 C ATOM 4436 O PHE A 577 -20.241 -62.703 -15.955 1.00 26.12 O ANISOU 4436 O PHE A 577 3486 3417 3020 707 66 906 O ATOM 4437 CB PHE A 577 -20.869 -65.752 -15.609 1.00 28.62 C ANISOU 4437 CB PHE A 577 3919 3532 3422 780 174 1110 C ATOM 4438 CG PHE A 577 -22.355 -65.596 -15.442 1.00 30.28 C ANISOU 4438 CG PHE A 577 4140 3699 3666 706 221 1133 C ATOM 4439 CD1 PHE A 577 -23.232 -66.334 -16.224 1.00 32.46 C ANISOU 4439 CD1 PHE A 577 4443 3844 4048 642 260 1146 C ATOM 4440 CD2 PHE A 577 -22.876 -64.684 -14.530 1.00 32.48 C ANISOU 4440 CD2 PHE A 577 4399 4071 3872 699 225 1134 C ATOM 4441 CE1 PHE A 577 -24.609 -66.176 -16.093 1.00 33.12 C ANISOU 4441 CE1 PHE A 577 4525 3891 4168 570 302 1165 C ATOM 4442 CE2 PHE A 577 -24.250 -64.524 -14.389 1.00 32.74 C ANISOU 4442 CE2 PHE A 577 4435 4069 3937 634 272 1156 C ATOM 4443 CZ PHE A 577 -25.116 -65.269 -15.173 1.00 32.90 C ANISOU 4443 CZ PHE A 577 4473 3960 4066 568 311 1174 C ATOM 4444 N THR A 578 -21.849 -63.193 -17.441 1.00 25.51 N ANISOU 4444 N THR A 578 3442 3167 3086 587 120 893 N ATOM 4445 CA THR A 578 -22.501 -61.913 -17.258 1.00 25.32 C ANISOU 4445 CA THR A 578 3386 3202 3033 533 110 842 C ATOM 4446 C THR A 578 -24.002 -61.996 -17.484 1.00 25.46 C ANISOU 4446 C THR A 578 3418 3150 3107 461 155 859 C ATOM 4447 O THR A 578 -24.520 -62.978 -18.020 1.00 26.40 O ANISOU 4447 O THR A 578 3564 3165 3301 437 186 892 O ATOM 4448 CB THR A 578 -21.884 -60.813 -18.140 1.00 24.53 C ANISOU 4448 CB THR A 578 3242 3141 2938 500 61 741 C ATOM 4449 OG1 THR A 578 -22.215 -59.538 -17.581 1.00 24.55 O ANISOU 4449 OG1 THR A 578 3215 3223 2889 475 46 700 O ATOM 4450 CG2 THR A 578 -22.387 -60.895 -19.591 1.00 22.59 C ANISOU 4450 CG2 THR A 578 3001 2805 2778 433 68 696 C ATOM 4451 N SER A 579 -24.680 -60.945 -17.052 1.00 25.18 N ANISOU 4451 N SER A 579 3359 3173 3036 429 156 833 N ATOM 4452 CA SER A 579 -26.127 -60.885 -17.044 1.00 25.31 C ANISOU 4452 CA SER A 579 3377 3148 3092 369 199 853 C ATOM 4453 C SER A 579 -26.491 -59.439 -16.752 1.00 24.71 C ANISOU 4453 C SER A 579 3269 3155 2966 345 182 795 C ATOM 4454 O SER A 579 -25.635 -58.673 -16.306 1.00 23.98 O ANISOU 4454 O SER A 579 3160 3147 2804 382 143 755 O ATOM 4455 CB SER A 579 -26.672 -61.790 -15.937 1.00 26.39 C ANISOU 4455 CB SER A 579 3543 3272 3211 405 256 962 C ATOM 4456 OG SER A 579 -28.075 -61.692 -15.834 1.00 27.63 O ANISOU 4456 OG SER A 579 3692 3399 3406 348 302 987 O ATOM 4457 N PHE A 580 -27.742 -59.062 -17.006 1.00 24.22 N ANISOU 4457 N PHE A 580 3195 3066 2942 285 209 786 N ATOM 4458 CA PHE A 580 -28.240 -57.757 -16.570 1.00 24.40 C ANISOU 4458 CA PHE A 580 3193 3162 2916 271 204 743 C ATOM 4459 C PHE A 580 -28.860 -57.787 -15.165 1.00 25.83 C ANISOU 4459 C PHE A 580 3384 3400 3031 309 248 811 C ATOM 4460 O PHE A 580 -29.287 -56.749 -14.654 1.00 25.26 O ANISOU 4460 O PHE A 580 3296 3392 2908 310 248 779 O ATOM 4461 CB PHE A 580 -29.239 -57.176 -17.586 1.00 23.45 C ANISOU 4461 CB PHE A 580 3051 2999 2862 195 207 693 C ATOM 4462 CG PHE A 580 -28.613 -56.747 -18.890 1.00 21.89 C ANISOU 4462 CG PHE A 580 2841 2774 2702 166 161 615 C ATOM 4463 CD1 PHE A 580 -29.216 -57.072 -20.098 1.00 20.99 C ANISOU 4463 CD1 PHE A 580 2724 2583 2669 113 163 595 C ATOM 4464 CD2 PHE A 580 -27.444 -55.989 -18.914 1.00 21.62 C ANISOU 4464 CD2 PHE A 580 2796 2796 2624 193 117 561 C ATOM 4465 CE1 PHE A 580 -28.664 -56.672 -21.300 1.00 20.44 C ANISOU 4465 CE1 PHE A 580 2647 2495 2625 94 126 528 C ATOM 4466 CE2 PHE A 580 -26.882 -55.588 -20.120 1.00 20.24 C ANISOU 4466 CE2 PHE A 580 2608 2597 2485 168 84 499 C ATOM 4467 CZ PHE A 580 -27.487 -55.929 -21.312 1.00 20.02 C ANISOU 4467 CZ PHE A 580 2583 2496 2527 123 91 484 C ATOM 4468 N AASN A 581 -28.912 -58.964 -14.549 0.50 27.03 N ANISOU 4468 N AASN A 581 3564 3525 3183 346 289 906 N ATOM 4469 N BASN A 581 -28.886 -58.974 -14.554 0.50 27.07 N ANISOU 4469 N BASN A 581 3568 3529 3187 347 288 905 N ATOM 4470 CA AASN A 581 -29.408 -59.078 -13.191 0.50 28.37 C ANISOU 4470 CA AASN A 581 3746 3752 3282 394 337 982 C ATOM 4471 CA BASN A 581 -29.435 -59.186 -13.218 0.50 28.46 C ANISOU 4471 CA BASN A 581 3759 3756 3300 393 341 988 C ATOM 4472 C AASN A 581 -28.346 -59.675 -12.282 0.50 29.62 C ANISOU 4472 C AASN A 581 3933 3959 3362 486 328 1035 C ATOM 4473 C BASN A 581 -28.328 -59.680 -12.286 0.50 29.65 C ANISOU 4473 C BASN A 581 3936 3963 3365 486 327 1035 C ATOM 4474 O AASN A 581 -27.574 -60.539 -12.702 0.50 29.63 O ANISOU 4474 O AASN A 581 3951 3910 3398 504 313 1055 O ATOM 4475 O BASN A 581 -27.492 -60.486 -12.702 0.50 29.64 O ANISOU 4475 O BASN A 581 3951 3916 3394 506 308 1050 O ATOM 4476 CB AASN A 581 -30.678 -59.923 -13.163 0.50 28.93 C ANISOU 4476 CB AASN A 581 3819 3748 3424 354 412 1066 C ATOM 4477 CB BASN A 581 -30.551 -60.234 -13.303 0.50 29.05 C ANISOU 4477 CB BASN A 581 3841 3740 3456 354 412 1075 C ATOM 4478 CG AASN A 581 -30.467 -61.301 -13.737 0.50 29.53 C ANISOU 4478 CG AASN A 581 3919 3714 3586 341 427 1118 C ATOM 4479 CG BASN A 581 -31.480 -60.224 -12.095 0.50 30.35 C ANISOU 4479 CG BASN A 581 4006 3954 3570 381 480 1156 C ATOM 4480 OD1AASN A 581 -29.916 -62.181 -13.077 0.50 31.54 O ANISOU 4480 OD1AASN A 581 4208 3965 3812 404 447 1195 O ATOM 4481 OD1BASN A 581 -32.665 -60.535 -12.215 0.50 31.91 O ANISOU 4481 OD1BASN A 581 4188 4101 3835 329 536 1200 O ATOM 4482 ND2AASN A 581 -30.916 -61.503 -14.970 0.50 29.05 N ANISOU 4482 ND2AASN A 581 3845 3564 3631 265 416 1074 N ATOM 4483 ND2BASN A 581 -30.950 -59.879 -10.931 0.50 31.03 N ANISOU 4483 ND2BASN A 581 4110 4144 3537 464 476 1177 N ATOM 4484 N VAL A 582 -28.303 -59.196 -11.041 1.00 30.68 N ANISOU 4484 N VAL A 582 4073 4197 3386 549 334 1054 N ATOM 4485 CA VAL A 582 -27.406 -59.751 -10.024 1.00 32.59 C ANISOU 4485 CA VAL A 582 4343 4502 3538 648 327 1114 C ATOM 4486 C VAL A 582 -27.864 -61.179 -9.722 1.00 35.13 C ANISOU 4486 C VAL A 582 4699 4750 3900 668 401 1245 C ATOM 4487 O VAL A 582 -29.057 -61.464 -9.774 1.00 35.57 O ANISOU 4487 O VAL A 582 4753 4750 4013 619 467 1296 O ATOM 4488 CB VAL A 582 -27.395 -58.920 -8.714 1.00 32.95 C ANISOU 4488 CB VAL A 582 4391 4679 3449 716 319 1105 C ATOM 4489 CG1 VAL A 582 -26.897 -57.516 -8.975 1.00 31.33 C ANISOU 4489 CG1 VAL A 582 4153 4537 3213 695 245 972 C ATOM 4490 CG2 VAL A 582 -28.776 -58.899 -8.054 1.00 33.27 C ANISOU 4490 CG2 VAL A 582 4439 4728 3475 710 400 1171 C ATOM 4491 N GLN A 583 -26.921 -62.070 -9.436 1.00 37.76 N ANISOU 4491 N GLN A 583 5059 5079 4209 738 391 1300 N ATOM 4492 CA GLN A 583 -27.236 -63.491 -9.235 1.00 40.16 C ANISOU 4492 CA GLN A 583 5401 5294 4562 758 461 1427 C ATOM 4493 C GLN A 583 -27.501 -63.780 -7.766 1.00 41.86 C ANISOU 4493 C GLN A 583 5646 5586 4675 846 517 1536 C ATOM 4494 O GLN A 583 -26.572 -63.950 -6.973 1.00 43.27 O ANISOU 4494 O GLN A 583 5845 5844 4752 947 491 1566 O ATOM 4495 CB GLN A 583 -26.099 -64.387 -9.753 1.00 40.58 C ANISOU 4495 CB GLN A 583 5475 5293 4652 795 428 1436 C ATOM 4496 CG GLN A 583 -25.903 -64.352 -11.268 1.00 41.41 C ANISOU 4496 CG GLN A 583 5560 5307 4867 714 388 1346 C ATOM 4497 CD GLN A 583 -27.052 -64.997 -12.039 1.00 42.83 C ANISOU 4497 CD GLN A 583 5746 5352 5177 624 443 1373 C ATOM 4498 OE1 GLN A 583 -27.439 -66.137 -11.765 1.00 46.01 O ANISOU 4498 OE1 GLN A 583 6181 5672 5626 635 504 1476 O ATOM 4499 NE2 GLN A 583 -27.594 -64.270 -13.016 1.00 43.66 N ANISOU 4499 NE2 GLN A 583 5817 5432 5341 535 419 1281 N CONECT 26 25 106 CONECT 32 31 1032 CONECT 59 58 186 CONECT 106 26 105 CONECT 186 59 185 CONECT 200 199 279 CONECT 279 200 278 CONECT 1032 32 1031 CONECT 4383 4382 4425 CONECT 4425 4383 4424 END If 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