Browse entries in the PDBbind-CN Database
HEADER ISOMERASE/VIRAL PROTEIN 25-JAN-12 4DGE TITLE TRIMCYP CYCLOPHILIN DOMAIN FROM MACACA MULATTA: H70C MUTANT, HIV-1 TITLE 2 CA(O-LOOP) COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: TRIMCYP; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: CYCLOPHILIN DOMAIN (UNP RESIDUES 304-468); COMPND 5 SYNONYM: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; COMPND 6 EC: 5.2.1.8; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: CAPSID PROTEIN; COMPND 11 CHAIN: C, D; COMPND 12 FRAGMENT: CYCLOPHILIN-BINDING DOMAIN (UNP RESIDUES 133-277); COMPND 13 ENGINEERED: YES; COMPND 14 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 3 ORGANISM_COMMON: RHESUS MACAQUE; SOURCE 4 ORGANISM_TAXID: 9544; SOURCE 5 GENE: TRIMCYP; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: C41(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: POPT; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 13 ORGANISM_COMMON: HIV-1; SOURCE 14 ORGANISM_TAXID: 11676; SOURCE 15 STRAIN: M-GROUP (NL4-3); SOURCE 16 GENE: GAG; SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 19 EXPRESSION_SYSTEM_STRAIN: C41(DE3); SOURCE 20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 21 EXPRESSION_SYSTEM_PLASMID: POPT KEYWDS ANTI-VIRAL PROTEIN, ISOMERASE-VIRAL PROTEIN COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR M.E.C.CAINES,K.BICHEL,A.J.PRICE,W.A.MCEWAN,L.C.JAMES REVDAT 3 18-APR-12 4DGE 1 JRNL REVDAT 2 28-MAR-12 4DGE 1 JRNL REVDAT 1 08-FEB-12 4DGE 0 JRNL AUTH M.E.CAINES,K.BICHEL,A.J.PRICE,W.A.MCEWAN,G.J.TOWERS, JRNL AUTH 2 B.J.WILLETT,S.M.FREUND,L.C.JAMES JRNL TITL DIVERSE HIV VIRUSES ARE TARGETED BY A CONFORMATIONALLY JRNL TITL 2 DYNAMIC ANTIVIRAL. JRNL REF NAT.STRUCT.MOL.BIOL. V. 19 411 2012 JRNL REFN ISSN 1545-9993 JRNL PMID 22407016 JRNL DOI 10.1038/NSMB.2253 REMARK 2 REMARK 2 RESOLUTION. 2.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.6.0091 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 63.87 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.8 REMARK 3 NUMBER OF REFLECTIONS : 27009 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.189 REMARK 3 R VALUE (WORKING SET) : 0.186 REMARK 3 FREE R VALUE : 0.255 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1350 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) : 2.20 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1703 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.29 REMARK 3 BIN R VALUE (WORKING SET) : 0.1920 REMARK 3 BIN FREE R VALUE SET COUNT : 88 REMARK 3 BIN FREE R VALUE : 0.2720 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4680 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 200 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 19.92 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.02 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.14000 REMARK 3 B22 (A**2) : -0.28000 REMARK 3 B33 (A**2) : 0.51000 REMARK 3 B12 (A**2) : 0.07000 REMARK 3 B13 (A**2) : 0.13000 REMARK 3 B23 (A**2) : -0.50000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.379 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.254 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.163 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.914 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.890 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4794 ; 0.013 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 3292 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6486 ; 1.374 ; 1.949 REMARK 3 BOND ANGLES OTHERS (DEGREES): 8050 ; 0.873 ; 3.001 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 604 ; 6.072 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 207 ;35.846 ;24.831 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 806 ;14.474 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;22.865 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 699 ; 0.076 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5348 ; 0.006 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): 926 ; 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): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : 2 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : A B REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 2 A 165 4 REMARK 3 1 B 2 B 165 4 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 1 A (A): 2148 ; 0.450 ; 0.500 REMARK 3 MEDIUM THERMAL 1 A (A**2): 2148 ; 0.620 ; 2.000 REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : C D REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 C 1 C 3 4 REMARK 3 1 D 1 D 3 4 REMARK 3 2 C 11 C 143 4 REMARK 3 2 D 11 D 143 4 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 2 C (A): 1775 ; 0.990 ; 0.500 REMARK 3 MEDIUM THERMAL 2 C (A**2): 1775 ; 1.820 ; 2.000 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 4 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 2 A 165 REMARK 3 ORIGIN FOR THE GROUP (A): -8.9701 -15.0035 28.2197 REMARK 3 T TENSOR REMARK 3 T11: 0.0283 T22: 0.0133 REMARK 3 T33: 0.0057 T12: 0.0013 REMARK 3 T13: 0.0014 T23: 0.0041 REMARK 3 L TENSOR REMARK 3 L11: 2.4478 L22: 1.9019 REMARK 3 L33: 1.6884 L12: -0.1925 REMARK 3 L13: 0.2469 L23: -0.5869 REMARK 3 S TENSOR REMARK 3 S11: -0.0237 S12: -0.1040 S13: -0.0345 REMARK 3 S21: 0.0355 S22: 0.0257 S23: -0.0244 REMARK 3 S31: -0.0024 S32: 0.0137 S33: -0.0021 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 2 B 165 REMARK 3 ORIGIN FOR THE GROUP (A): -34.0468 -17.9934 77.9030 REMARK 3 T TENSOR REMARK 3 T11: 0.0105 T22: 0.0063 REMARK 3 T33: 0.0035 T12: 0.0047 REMARK 3 T13: -0.0004 T23: 0.0025 REMARK 3 L TENSOR REMARK 3 L11: 2.1556 L22: 2.5615 REMARK 3 L33: 1.5739 L12: 0.6187 REMARK 3 L13: 0.1424 L23: 0.5533 REMARK 3 S TENSOR REMARK 3 S11: -0.0240 S12: 0.0143 S13: 0.0193 REMARK 3 S21: -0.0038 S22: -0.0129 S23: 0.0069 REMARK 3 S31: -0.0115 S32: -0.0264 S33: 0.0369 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 1 C 143 REMARK 3 ORIGIN FOR THE GROUP (A): -30.0698 11.2193 45.3764 REMARK 3 T TENSOR REMARK 3 T11: 0.0993 T22: 0.1174 REMARK 3 T33: 0.0275 T12: -0.0210 REMARK 3 T13: 0.0205 T23: 0.0096 REMARK 3 L TENSOR REMARK 3 L11: 2.6367 L22: 3.9479 REMARK 3 L33: 2.2372 L12: -1.1644 REMARK 3 L13: -0.6605 L23: 1.8683 REMARK 3 S TENSOR REMARK 3 S11: -0.0223 S12: 0.0378 S13: -0.0481 REMARK 3 S21: 0.1251 S22: -0.1165 S23: 0.2879 REMARK 3 S31: 0.0156 S32: -0.1773 S33: 0.1388 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 1 D 145 REMARK 3 ORIGIN FOR THE GROUP (A): -14.8269 6.5927 62.5227 REMARK 3 T TENSOR REMARK 3 T11: 0.0623 T22: 0.1051 REMARK 3 T33: 0.0304 T12: -0.0003 REMARK 3 T13: -0.0027 T23: -0.0049 REMARK 3 L TENSOR REMARK 3 L11: 0.9221 L22: 4.6692 REMARK 3 L33: 1.0899 L12: 0.3822 REMARK 3 L13: -0.2097 L23: -0.7576 REMARK 3 S TENSOR REMARK 3 S11: 0.0044 S12: -0.0096 S13: -0.0760 REMARK 3 S21: -0.1556 S22: 0.0421 S23: -0.2217 REMARK 3 S31: 0.0471 S32: 0.1133 S33: -0.0466 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS REMARK 3 U VALUES : WITH TLS ADDED REMARK 4 REMARK 4 4DGE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JAN-12. REMARK 100 THE RCSB ID CODE IS RCSB070295. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 29-JUL-10 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.6 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E+ SUPERBRIGHT REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS HTC REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27012 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200 REMARK 200 RESOLUTION RANGE LOW (A) : 63.870 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.8 REMARK 200 DATA REDUNDANCY : 1.700 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.05500 REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32 REMARK 200 COMPLETENESS FOR SHELL (%) : 89.1 REMARK 200 DATA REDUNDANCY IN SHELL : 1.60 REMARK 200 R MERGE FOR SHELL (I) : 0.14400 REMARK 200 R SYM FOR SHELL (I) : 0.14400 REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.900 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRIES 2WLW AND 1AK4 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 42.67 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 23.5% W/V PEG8000, 0.1 M HEPES, PH REMARK 280 7.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1030 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 14470 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1250 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 14830 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 MET A 1 REMARK 465 MET B 1 REMARK 465 MET C 0 REMARK 465 GLN C 4 REMARK 465 ASN C 5 REMARK 465 LEU C 6 REMARK 465 GLN C 7 REMARK 465 GLY C 8 REMARK 465 GLN C 9 REMARK 465 MET C 10 REMARK 465 MET C 144 REMARK 465 TYR C 145 REMARK 465 MET D 0 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ARG C 97 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 REMARK 500 REMARK: NULL 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 PHE A 60 -76.02 -123.67 REMARK 500 LYS A 133 -69.03 -98.39 REMARK 500 ASP B 13 48.04 35.56 REMARK 500 PHE B 60 -79.21 -140.84 REMARK 500 ALA C 31 -126.87 42.14 REMARK 500 ALA D 31 -129.40 52.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4DGA RELATED DB: PDB REMARK 900 TRIMCYP CYCLOPHILIN DOMAIN FROM MACACA MULATTA: HIV-1 CA(O- REMARK 900 LOOP) COMPLEX REMARK 900 RELATED ID: 4DGB RELATED DB: PDB REMARK 900 TRIMCYP CYCLOPHILIN DOMAIN FROM MACACA MULATTA: HIV-2 CA REMARK 900 CYCLOPHILIN-BINDING LOOP COMPLEX REMARK 900 RELATED ID: 4DGC RELATED DB: PDB REMARK 900 TRIMCYP CYCLOPHILIN DOMAIN FROM MACACA MULATTA: CYCLOSPORIN REMARK 900 A COMPLEX REMARK 900 RELATED ID: 4DGD RELATED DB: PDB REMARK 900 TRIMCYP CYCLOPHILIN DOMAIN FROM MACACA MULATTA: H70C MUTANT DBREF 4DGE A 1 165 UNP B0LJC8 B0LJC8_MACMU 304 468 DBREF 4DGE B 1 165 UNP B0LJC8 B0LJC8_MACMU 304 468 DBREF 4DGE C 1 145 UNP Q72497 Q72497_9HIV1 133 277 DBREF 4DGE D 1 145 UNP Q72497 Q72497_9HIV1 133 277 SEQADV 4DGE CYS A 70 UNP B0LJC8 HIS 373 ENGINEERED MUTATION SEQADV 4DGE CYS B 70 UNP B0LJC8 HIS 373 ENGINEERED MUTATION SEQADV 4DGE MET C 0 UNP Q72497 INITIATING METHIONINE SEQADV 4DGE THR C 83 UNP Q72497 LEU 215 ENGINEERED MUTATION SEQADV 4DGE PRO C 86 UNP Q72497 VAL 218 ENGINEERED MUTATION SEQADV 4DGE ALA C 87 UNP Q72497 HIS 219 ENGINEERED MUTATION SEQADV 4DGE MET C 88 UNP Q72497 ALA 220 ENGINEERED MUTATION SEQADV 4DGE LEU C 91 UNP Q72497 ILE 223 ENGINEERED MUTATION SEQADV 4DGE PRO C 92 UNP Q72497 ALA 224 ENGINEERED MUTATION SEQADV 4DGE ILE C 96 UNP Q72497 MET 228 ENGINEERED MUTATION SEQADV 4DGE THR C 100 UNP Q72497 ARG 232 ENGINEERED MUTATION SEQADV 4DGE MET D 0 UNP Q72497 INITIATING METHIONINE SEQADV 4DGE THR D 83 UNP Q72497 LEU 215 ENGINEERED MUTATION SEQADV 4DGE PRO D 86 UNP Q72497 VAL 218 ENGINEERED MUTATION SEQADV 4DGE ALA D 87 UNP Q72497 HIS 219 ENGINEERED MUTATION SEQADV 4DGE MET D 88 UNP Q72497 ALA 220 ENGINEERED MUTATION SEQADV 4DGE LEU D 91 UNP Q72497 ILE 223 ENGINEERED MUTATION SEQADV 4DGE PRO D 92 UNP Q72497 ALA 224 ENGINEERED MUTATION SEQADV 4DGE ILE D 96 UNP Q72497 MET 228 ENGINEERED MUTATION SEQADV 4DGE THR D 100 UNP Q72497 ARG 232 ENGINEERED MUTATION SEQRES 1 A 165 MET VAL ASN PRO THR VAL PHE PHE ASP ILE ALA VAL ASP SEQRES 2 A 165 GLY GLU PRO LEU GLY ARG VAL SER PHE GLU LEU PHE ALA SEQRES 3 A 165 ASP LYS VAL PRO LYS THR ALA GLU ASN PHE ARG ALA LEU SEQRES 4 A 165 SER THR GLY GLU LYS GLY PHE GLY TYR LYS GLY SER CYS SEQRES 5 A 165 PHE HIS ARG ILE ILE PRO GLY PHE MET CYS GLN GLY GLY SEQRES 6 A 165 ASN PHE THR HIS CYS ASN GLY THR GLY GLY LYS SER ILE SEQRES 7 A 165 TYR GLY GLU LYS PHE GLU ASP GLU ASN PHE ILE LEU LYS SEQRES 8 A 165 HIS THR GLY PRO GLY ILE LEU SER MET ALA ASN ALA GLY SEQRES 9 A 165 PRO ASN THR ASN GLY SER GLN PHE PHE ILE CYS THR ALA SEQRES 10 A 165 LYS THR GLU TRP LEU ASP GLY LYS HIS VAL VAL PHE GLY SEQRES 11 A 165 LYS VAL LYS GLU GLY MET ASN ILE VAL GLU ALA MET GLU SEQRES 12 A 165 ARG PHE GLY SER ARG ASN GLY LYS THR SER LYS LYS ILE SEQRES 13 A 165 THR ILE ALA ASP CYS GLY GLN LEU GLU SEQRES 1 B 165 MET VAL ASN PRO THR VAL PHE PHE ASP ILE ALA VAL ASP SEQRES 2 B 165 GLY GLU PRO LEU GLY ARG VAL SER PHE GLU LEU PHE ALA SEQRES 3 B 165 ASP LYS VAL PRO LYS THR ALA GLU ASN PHE ARG ALA LEU SEQRES 4 B 165 SER THR GLY GLU LYS GLY PHE GLY TYR LYS GLY SER CYS SEQRES 5 B 165 PHE HIS ARG ILE ILE PRO GLY PHE MET CYS GLN GLY GLY SEQRES 6 B 165 ASN PHE THR HIS CYS ASN GLY THR GLY GLY LYS SER ILE SEQRES 7 B 165 TYR GLY GLU LYS PHE GLU ASP GLU ASN PHE ILE LEU LYS SEQRES 8 B 165 HIS THR GLY PRO GLY ILE LEU SER MET ALA ASN ALA GLY SEQRES 9 B 165 PRO ASN THR ASN GLY SER GLN PHE PHE ILE CYS THR ALA SEQRES 10 B 165 LYS THR GLU TRP LEU ASP GLY LYS HIS VAL VAL PHE GLY SEQRES 11 B 165 LYS VAL LYS GLU GLY MET ASN ILE VAL GLU ALA MET GLU SEQRES 12 B 165 ARG PHE GLY SER ARG ASN GLY LYS THR SER LYS LYS ILE SEQRES 13 B 165 THR ILE ALA ASP CYS GLY GLN LEU GLU SEQRES 1 C 146 MET PRO ILE VAL GLN ASN LEU GLN GLY GLN MET VAL HIS SEQRES 2 C 146 GLN ALA ILE SER PRO ARG THR LEU ASN ALA TRP VAL LYS SEQRES 3 C 146 VAL VAL GLU GLU LYS ALA PHE SER PRO GLU VAL ILE PRO SEQRES 4 C 146 MET PHE SER ALA LEU SER GLU GLY ALA THR PRO GLN ASP SEQRES 5 C 146 LEU ASN THR MET LEU ASN THR VAL GLY GLY HIS GLN ALA SEQRES 6 C 146 ALA MET GLN MET LEU LYS GLU THR ILE ASN GLU GLU ALA SEQRES 7 C 146 ALA GLU TRP ASP ARG THR HIS PRO PRO ALA MET GLY PRO SEQRES 8 C 146 LEU PRO PRO GLY GLN ILE ARG GLU PRO THR GLY SER ASP SEQRES 9 C 146 ILE ALA GLY THR THR SER THR LEU GLN GLU GLN ILE GLY SEQRES 10 C 146 TRP MET THR HIS ASN PRO PRO ILE PRO VAL GLY GLU ILE SEQRES 11 C 146 TYR LYS ARG TRP ILE ILE LEU GLY LEU ASN LYS ILE VAL SEQRES 12 C 146 ARG MET TYR SEQRES 1 D 146 MET PRO ILE VAL GLN ASN LEU GLN GLY GLN MET VAL HIS SEQRES 2 D 146 GLN ALA ILE SER PRO ARG THR LEU ASN ALA TRP VAL LYS SEQRES 3 D 146 VAL VAL GLU GLU LYS ALA PHE SER PRO GLU VAL ILE PRO SEQRES 4 D 146 MET PHE SER ALA LEU SER GLU GLY ALA THR PRO GLN ASP SEQRES 5 D 146 LEU ASN THR MET LEU ASN THR VAL GLY GLY HIS GLN ALA SEQRES 6 D 146 ALA MET GLN MET LEU LYS GLU THR ILE ASN GLU GLU ALA SEQRES 7 D 146 ALA GLU TRP ASP ARG THR HIS PRO PRO ALA MET GLY PRO SEQRES 8 D 146 LEU PRO PRO GLY GLN ILE ARG GLU PRO THR GLY SER ASP SEQRES 9 D 146 ILE ALA GLY THR THR SER THR LEU GLN GLU GLN ILE GLY SEQRES 10 D 146 TRP MET THR HIS ASN PRO PRO ILE PRO VAL GLY GLU ILE SEQRES 11 D 146 TYR LYS ARG TRP ILE ILE LEU GLY LEU ASN LYS ILE VAL SEQRES 12 D 146 ARG MET TYR FORMUL 5 HOH *200(H2 O) HELIX 1 1 VAL A 29 GLY A 42 1 14 HELIX 2 2 THR A 119 ASP A 123 5 5 HELIX 3 3 GLY A 135 ARG A 144 1 10 HELIX 4 4 VAL B 29 GLY B 42 1 14 HELIX 5 5 THR B 119 ASP B 123 5 5 HELIX 6 6 GLY B 135 ARG B 144 1 10 HELIX 7 7 SER C 16 ALA C 31 1 16 HELIX 8 8 GLU C 35 SER C 44 1 10 HELIX 9 9 THR C 48 THR C 58 1 11 HELIX 10 10 HIS C 62 HIS C 84 1 23 HELIX 11 11 THR C 100 ALA C 105 1 6 HELIX 12 12 THR C 110 THR C 119 1 10 HELIX 13 13 PRO C 125 ARG C 143 1 19 HELIX 14 14 SER D 16 ALA D 31 1 16 HELIX 15 15 GLU D 35 SER D 44 1 10 HELIX 16 16 THR D 48 THR D 58 1 11 HELIX 17 17 HIS D 62 HIS D 84 1 23 HELIX 18 18 THR D 100 ALA D 105 1 6 HELIX 19 19 THR D 110 THR D 119 1 10 HELIX 20 20 PRO D 125 VAL D 142 1 18 HELIX 21 21 ARG D 143 TYR D 145 5 3 SHEET 1 A 8 PHE A 53 ILE A 57 0 SHEET 2 A 8 MET A 61 GLY A 64 -1 O MET A 61 N ILE A 57 SHEET 3 A 8 PHE A 112 CYS A 115 -1 O ILE A 114 N CYS A 62 SHEET 4 A 8 ILE A 97 MET A 100 -1 N SER A 99 O PHE A 113 SHEET 5 A 8 VAL A 128 VAL A 132 -1 O GLY A 130 N LEU A 98 SHEET 6 A 8 GLU A 15 LEU A 24 -1 N GLU A 23 O LYS A 131 SHEET 7 A 8 THR A 5 VAL A 12 -1 N PHE A 8 O VAL A 20 SHEET 8 A 8 ILE A 156 GLU A 165 -1 O GLU A 165 N THR A 5 SHEET 1 B 8 ARG B 55 ILE B 57 0 SHEET 2 B 8 MET B 61 GLY B 64 -1 O GLN B 63 N ARG B 55 SHEET 3 B 8 PHE B 112 CYS B 115 -1 O ILE B 114 N CYS B 62 SHEET 4 B 8 ILE B 97 MET B 100 -1 N ILE B 97 O CYS B 115 SHEET 5 B 8 VAL B 128 GLU B 134 -1 O GLY B 130 N LEU B 98 SHEET 6 B 8 GLU B 15 LEU B 24 -1 N SER B 21 O LYS B 133 SHEET 7 B 8 THR B 5 VAL B 12 -1 N ILE B 10 O GLY B 18 SHEET 8 B 8 ILE B 156 GLU B 165 -1 O ASP B 160 N ASP B 9 SHEET 1 C 2 ILE D 2 GLN D 4 0 SHEET 2 C 2 MET D 10 HIS D 12 -1 O VAL D 11 N VAL D 3 SSBOND 1 CYS A 52 CYS A 70 1555 1555 2.05 SSBOND 2 CYS B 52 CYS B 70 1555 1555 2.09 CISPEP 1 GLY C 89 PRO C 90 0 13.36 CISPEP 2 ASN C 121 PRO C 122 0 -1.61 CISPEP 3 GLY D 89 PRO D 90 0 18.72 CISPEP 4 ASN D 121 PRO D 122 0 0.21 CRYST1 39.070 59.710 70.470 65.08 83.87 79.65 P 1 2 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 0.025595 -0.004674 -0.000907 0.00000 SCALE2 0.000000 0.017025 -0.007679 0.00000 SCALE3 0.000000 0.000000 0.015657 0.00000 ATOM 1 N VAL A 2 -9.309 -23.458 8.589 1.00 24.71 N ANISOU 1 N VAL A 2 4289 3345 1755 188 -63 -1161 N ATOM 2 CA VAL A 2 -9.157 -24.074 9.942 1.00 23.30 C ANISOU 2 CA VAL A 2 4039 2993 1819 183 -54 -1140 C ATOM 3 C VAL A 2 -9.238 -23.021 11.053 1.00 21.00 C ANISOU 3 C VAL A 2 3610 2716 1650 141 -40 -943 C ATOM 4 O VAL A 2 -8.677 -21.944 10.932 1.00 20.57 O ANISOU 4 O VAL A 2 3505 2776 1534 165 38 -832 O ATOM 5 CB VAL A 2 -7.829 -24.805 10.019 1.00 24.01 C ANISOU 5 CB VAL A 2 4148 3032 1943 302 84 -1220 C ATOM 6 CG1 VAL A 2 -7.682 -25.492 11.355 1.00 23.15 C ANISOU 6 CG1 VAL A 2 3973 2750 2070 300 81 -1190 C ATOM 7 CG2 VAL A 2 -7.718 -25.828 8.849 1.00 26.48 C ANISOU 7 CG2 VAL A 2 4612 3330 2117 362 83 -1442 C ATOM 8 N ASN A 3 -9.935 -23.324 12.140 1.00 19.71 N ANISOU 8 N ASN A 3 3391 2435 1661 78 -114 -899 N ATOM 9 CA ASN A 3 -9.973 -22.404 13.279 1.00 17.68 C ANISOU 9 CA ASN A 3 3016 2186 1514 51 -94 -736 C ATOM 10 C ASN A 3 -8.554 -22.094 13.776 1.00 16.88 C ANISOU 10 C ASN A 3 2860 2104 1447 130 42 -681 C ATOM 11 O ASN A 3 -7.756 -23.012 13.927 1.00 17.43 O ANISOU 11 O ASN A 3 2950 2104 1567 195 100 -754 O ATOM 12 CB ASN A 3 -10.797 -23.009 14.415 1.00 17.05 C ANISOU 12 CB ASN A 3 2890 1978 1608 -11 -170 -710 C ATOM 13 CG ASN A 3 -12.268 -22.700 14.302 1.00 17.08 C ANISOU 13 CG ASN A 3 2872 2001 1614 -105 -295 -674 C ATOM 14 OD1 ASN A 3 -12.665 -21.768 13.611 1.00 17.28 O ANISOU 14 OD1 ASN A 3 2895 2138 1530 -120 -324 -631 O ATOM 15 ND2 ASN A 3 -13.083 -23.456 15.006 1.00 16.99 N ANISOU 15 ND2 ASN A 3 2834 1883 1738 -168 -368 -673 N ATOM 16 N PRO A 4 -8.228 -20.806 14.036 1.00 15.72 N ANISOU 16 N PRO A 4 2640 2045 1287 125 87 -552 N ATOM 17 CA PRO A 4 -6.885 -20.492 14.542 1.00 15.16 C ANISOU 17 CA PRO A 4 2503 1993 1264 183 199 -496 C ATOM 18 C PRO A 4 -6.601 -21.002 15.961 1.00 14.10 C ANISOU 18 C PRO A 4 2306 1754 1295 189 197 -467 C ATOM 19 O PRO A 4 -7.512 -21.191 16.753 1.00 13.39 O ANISOU 19 O PRO A 4 2203 1595 1286 135 119 -445 O ATOM 20 CB PRO A 4 -6.840 -18.957 14.538 1.00 14.52 C ANISOU 20 CB PRO A 4 2362 2003 1150 149 214 -364 C ATOM 21 CG PRO A 4 -8.228 -18.506 14.589 1.00 14.10 C ANISOU 21 CG PRO A 4 2319 1942 1095 80 106 -332 C ATOM 22 CD PRO A 4 -9.085 -19.605 13.971 1.00 15.07 C ANISOU 22 CD PRO A 4 2524 2028 1172 64 28 -450 C ATOM 23 N THR A 5 -5.331 -21.211 16.248 1.00 14.19 N ANISOU 23 N THR A 5 2273 1767 1349 257 286 -458 N ATOM 24 CA THR A 5 -4.863 -21.670 17.543 1.00 13.60 C ANISOU 24 CA THR A 5 2135 1614 1416 275 287 -418 C ATOM 25 C THR A 5 -3.852 -20.666 18.063 1.00 13.02 C ANISOU 25 C THR A 5 1963 1613 1368 282 342 -315 C ATOM 26 O THR A 5 -2.997 -20.196 17.311 1.00 13.62 O ANISOU 26 O THR A 5 2016 1776 1383 317 422 -303 O ATOM 27 CB THR A 5 -4.180 -23.056 17.441 1.00 14.73 C ANISOU 27 CB THR A 5 2307 1674 1613 361 329 -506 C ATOM 28 OG1 THR A 5 -5.139 -24.021 17.010 1.00 15.42 O ANISOU 28 OG1 THR A 5 2491 1668 1696 340 262 -610 O ATOM 29 CG2 THR A 5 -3.582 -23.519 18.822 1.00 14.25 C ANISOU 29 CG2 THR A 5 2170 1541 1700 388 326 -437 C ATOM 30 N VAL A 6 -3.957 -20.360 19.351 1.00 12.01 N ANISOU 30 N VAL A 6 1778 1454 1329 247 297 -243 N ATOM 31 CA VAL A 6 -3.092 -19.412 20.031 1.00 11.54 C ANISOU 31 CA VAL A 6 1628 1446 1307 236 318 -155 C ATOM 32 C VAL A 6 -2.499 -20.117 21.276 1.00 11.35 C ANISOU 32 C VAL A 6 1550 1371 1389 268 302 -128 C ATOM 33 O VAL A 6 -3.135 -21.003 21.838 1.00 11.20 O ANISOU 33 O VAL A 6 1567 1274 1414 269 256 -146 O ATOM 34 CB VAL A 6 -3.905 -18.160 20.391 1.00 10.76 C ANISOU 34 CB VAL A 6 1526 1369 1190 158 264 -101 C ATOM 35 CG1 VAL A 6 -3.417 -17.479 21.702 1.00 10.29 C ANISOU 35 CG1 VAL A 6 1395 1312 1202 133 237 -35 C ATOM 36 CG2 VAL A 6 -3.943 -17.202 19.179 1.00 11.23 C ANISOU 36 CG2 VAL A 6 1604 1502 1161 139 297 -83 C ATOM 37 N PHE A 7 -1.282 -19.739 21.665 1.00 11.38 N ANISOU 37 N PHE A 7 1463 1422 1437 290 334 -73 N ATOM 38 CA PHE A 7 -0.697 -20.159 22.918 1.00 11.33 C ANISOU 38 CA PHE A 7 1394 1391 1518 311 299 -25 C ATOM 39 C PHE A 7 -0.374 -18.986 23.820 1.00 10.86 C ANISOU 39 C PHE A 7 1269 1383 1472 249 252 42 C ATOM 40 O PHE A 7 -0.017 -17.898 23.326 1.00 10.80 O ANISOU 40 O PHE A 7 1230 1432 1442 210 276 64 O ATOM 41 CB PHE A 7 0.576 -20.941 22.680 1.00 12.41 C ANISOU 41 CB PHE A 7 1466 1534 1713 404 363 -25 C ATOM 42 CG PHE A 7 1.738 -20.110 22.222 1.00 12.93 C ANISOU 42 CG PHE A 7 1433 1697 1780 409 425 18 C ATOM 43 CD1 PHE A 7 1.957 -19.883 20.860 1.00 13.57 C ANISOU 43 CD1 PHE A 7 1529 1834 1793 433 518 -15 C ATOM 44 CD2 PHE A 7 2.653 -19.611 23.140 1.00 13.03 C ANISOU 44 CD2 PHE A 7 1332 1754 1863 389 389 98 C ATOM 45 CE1 PHE A 7 3.083 -19.135 20.417 1.00 14.33 C ANISOU 45 CE1 PHE A 7 1516 2028 1898 435 590 47 C ATOM 46 CE2 PHE A 7 3.746 -18.875 22.731 1.00 13.72 C ANISOU 46 CE2 PHE A 7 1310 1927 1974 381 442 150 C ATOM 47 CZ PHE A 7 3.963 -18.625 21.360 1.00 14.41 C ANISOU 47 CZ PHE A 7 1402 2069 2001 403 550 132 C ATOM 48 N PHE A 8 -0.546 -19.213 25.128 1.00 10.55 N ANISOU 48 N PHE A 8 1220 1322 1467 237 184 75 N ATOM 49 CA PHE A 8 0.096 -18.423 26.181 1.00 10.58 C ANISOU 49 CA PHE A 8 1153 1373 1491 200 129 128 C ATOM 50 C PHE A 8 1.168 -19.264 26.884 1.00 11.39 C ANISOU 50 C PHE A 8 1177 1485 1665 259 111 177 C ATOM 51 O PHE A 8 0.909 -20.427 27.227 1.00 11.55 O ANISOU 51 O PHE A 8 1225 1450 1710 311 105 184 O ATOM 52 CB PHE A 8 -0.884 -18.041 27.268 1.00 9.99 C ANISOU 52 CB PHE A 8 1128 1288 1378 151 59 132 C ATOM 53 CG PHE A 8 -1.966 -17.098 26.848 1.00 9.38 C ANISOU 53 CG PHE A 8 1113 1202 1247 99 61 97 C ATOM 54 CD1 PHE A 8 -1.957 -16.451 25.619 1.00 9.39 C ANISOU 54 CD1 PHE A 8 1122 1212 1232 82 107 80 C ATOM 55 CD2 PHE A 8 -2.997 -16.832 27.737 1.00 9.01 C ANISOU 55 CD2 PHE A 8 1111 1147 1162 73 19 92 C ATOM 56 CE1 PHE A 8 -2.962 -15.564 25.276 1.00 8.94 C ANISOU 56 CE1 PHE A 8 1116 1144 1134 41 99 63 C ATOM 57 CE2 PHE A 8 -4.019 -15.949 27.402 1.00 8.56 C ANISOU 57 CE2 PHE A 8 1100 1080 1070 38 21 65 C ATOM 58 CZ PHE A 8 -3.995 -15.312 26.174 1.00 8.55 C ANISOU 58 CZ PHE A 8 1105 1077 1066 23 54 54 C ATOM 59 N ASP A 9 2.349 -18.670 27.110 1.00 11.92 N ANISOU 59 N ASP A 9 1138 1615 1773 247 97 220 N ATOM 60 CA ASP A 9 3.323 -19.200 28.046 1.00 12.72 C ANISOU 60 CA ASP A 9 1150 1745 1938 286 45 283 C ATOM 61 C ASP A 9 3.196 -18.418 29.353 1.00 12.43 C ANISOU 61 C ASP A 9 1112 1746 1861 212 -65 304 C ATOM 62 O ASP A 9 3.457 -17.220 29.391 1.00 12.39 O ANISOU 62 O ASP A 9 1079 1777 1848 137 -96 293 O ATOM 63 CB ASP A 9 4.733 -19.095 27.499 1.00 13.88 C ANISOU 63 CB ASP A 9 1161 1948 2161 319 91 321 C ATOM 64 CG ASP A 9 4.952 -19.994 26.286 1.00 14.53 C ANISOU 64 CG ASP A 9 1247 2002 2270 417 210 290 C ATOM 65 OD1 ASP A 9 4.505 -21.153 26.281 1.00 14.70 O ANISOU 65 OD1 ASP A 9 1332 1948 2302 489 226 263 O ATOM 66 OD2 ASP A 9 5.573 -19.543 25.324 1.00 15.14 O ANISOU 66 OD2 ASP A 9 1264 2130 2356 422 292 290 O ATOM 67 N ILE A 10 2.792 -19.111 30.408 1.00 12.32 N ANISOU 67 N ILE A 10 1135 1723 1823 235 -122 334 N ATOM 68 CA ILE A 10 2.474 -18.486 31.687 1.00 12.25 C ANISOU 68 CA ILE A 10 1154 1759 1740 178 -218 339 C ATOM 69 C ILE A 10 3.683 -18.570 32.635 1.00 13.33 C ANISOU 69 C ILE A 10 1187 1969 1907 186 -312 407 C ATOM 70 O ILE A 10 4.393 -19.574 32.682 1.00 13.99 O ANISOU 70 O ILE A 10 1201 2053 2061 260 -310 475 O ATOM 71 CB ILE A 10 1.270 -19.209 32.346 1.00 11.89 C ANISOU 71 CB ILE A 10 1205 1681 1630 197 -221 351 C ATOM 72 CG1 ILE A 10 0.052 -19.238 31.402 1.00 10.96 C ANISOU 72 CG1 ILE A 10 1173 1494 1497 188 -142 293 C ATOM 73 CG2 ILE A 10 0.960 -18.618 33.730 1.00 12.09 C ANISOU 73 CG2 ILE A 10 1263 1775 1555 154 -307 356 C ATOM 74 CD1 ILE A 10 -0.595 -17.886 31.079 1.00 10.31 C ANISOU 74 CD1 ILE A 10 1135 1421 1361 121 -135 224 C ATOM 75 N ALA A 11 3.907 -17.497 33.385 1.00 13.56 N ANISOU 75 N ALA A 11 1207 2055 1887 110 -403 383 N ATOM 76 CA ALA A 11 4.954 -17.447 34.366 1.00 14.74 C ANISOU 76 CA ALA A 11 1267 2287 2047 99 -519 437 C ATOM 77 C ALA A 11 4.376 -17.023 35.704 1.00 15.00 C ANISOU 77 C ALA A 11 1384 2371 1944 58 -617 409 C ATOM 78 O ALA A 11 3.351 -16.304 35.766 1.00 14.19 O ANISOU 78 O ALA A 11 1388 2241 1760 18 -594 327 O ATOM 79 CB ALA A 11 6.086 -16.475 33.902 1.00 15.39 C ANISOU 79 CB ALA A 11 1230 2399 2216 33 -550 429 C ATOM 80 N VAL A 12 5.015 -17.498 36.773 1.00 16.24 N ANISOU 80 N VAL A 12 1492 2607 2070 79 -722 481 N ATOM 81 CA VAL A 12 4.680 -17.124 38.148 1.00 17.01 C ANISOU 81 CA VAL A 12 1661 2786 2016 46 -828 461 C ATOM 82 C VAL A 12 5.901 -16.405 38.750 1.00 18.56 C ANISOU 82 C VAL A 12 1762 3065 2222 -17 -980 454 C ATOM 83 O VAL A 12 6.957 -16.994 38.859 1.00 19.49 O ANISOU 83 O VAL A 12 1755 3231 2420 13 -1037 551 O ATOM 84 CB VAL A 12 4.291 -18.359 39.012 1.00 17.49 C ANISOU 84 CB VAL A 12 1757 2885 2000 122 -837 568 C ATOM 85 CG1 VAL A 12 3.825 -17.916 40.387 1.00 18.25 C ANISOU 85 CG1 VAL A 12 1943 3085 1906 93 -926 542 C ATOM 86 CG2 VAL A 12 3.168 -19.164 38.329 1.00 16.28 C ANISOU 86 CG2 VAL A 12 1676 2634 1874 173 -697 585 C ATOM 87 N ASP A 13 5.754 -15.114 39.070 1.00 18.92 N ANISOU 87 N ASP A 13 1864 3119 2206 -108 -1044 337 N ATOM 88 CA ASP A 13 6.871 -14.255 39.497 1.00 20.52 C ANISOU 88 CA ASP A 13 1979 3375 2441 -197 -1196 307 C ATOM 89 C ASP A 13 8.116 -14.472 38.652 1.00 21.02 C ANISOU 89 C ASP A 13 1859 3433 2695 -202 -1190 393 C ATOM 90 O ASP A 13 9.217 -14.653 39.170 1.00 22.52 O ANISOU 90 O ASP A 13 1922 3707 2926 -216 -1313 462 O ATOM 91 CB ASP A 13 7.188 -14.467 40.978 1.00 22.12 C ANISOU 91 CB ASP A 13 2197 3707 2499 -197 -1356 330 C ATOM 92 CG ASP A 13 6.103 -13.916 41.883 1.00 22.26 C ANISOU 92 CG ASP A 13 2392 3750 2315 -209 -1373 216 C ATOM 93 OD1 ASP A 13 5.330 -12.996 41.486 1.00 21.44 O ANISOU 93 OD1 ASP A 13 2383 3560 2201 -246 -1307 91 O ATOM 94 OD2 ASP A 13 6.025 -14.401 43.029 1.00 23.52 O ANISOU 94 OD2 ASP A 13 2594 4023 2316 -174 -1452 257 O ATOM 95 N GLY A 14 7.911 -14.484 37.342 1.00 19.93 N ANISOU 95 N GLY A 14 1703 3206 2664 -184 -1041 394 N ATOM 96 CA GLY A 14 9.007 -14.591 36.380 1.00 20.43 C ANISOU 96 CA GLY A 14 1595 3266 2900 -183 -998 467 C ATOM 97 C GLY A 14 9.535 -15.981 36.109 1.00 20.74 C ANISOU 97 C GLY A 14 1534 3330 3013 -61 -939 586 C ATOM 98 O GLY A 14 10.462 -16.124 35.315 1.00 21.55 O ANISOU 98 O GLY A 14 1489 3443 3256 -42 -888 646 O ATOM 99 N GLU A 15 8.974 -16.999 36.749 1.00 20.47 N ANISOU 99 N GLU A 15 1576 3305 2895 24 -941 626 N ATOM 100 CA GLU A 15 9.383 -18.382 36.521 1.00 20.87 C ANISOU 100 CA GLU A 15 1550 3349 3027 151 -885 738 C ATOM 101 C GLU A 15 8.371 -19.131 35.661 1.00 19.38 C ANISOU 101 C GLU A 15 1470 3051 2839 226 -723 713 C ATOM 102 O GLU A 15 7.165 -19.121 35.949 1.00 18.31 O ANISOU 102 O GLU A 15 1485 2878 2591 212 -700 663 O ATOM 103 CB GLU A 15 9.557 -19.120 37.839 1.00 22.06 C ANISOU 103 CB GLU A 15 1698 3576 3108 196 -1011 830 C ATOM 104 CG GLU A 15 10.477 -18.396 38.788 1.00 23.72 C ANISOU 104 CG GLU A 15 1817 3906 3290 114 -1198 844 C ATOM 105 CD GLU A 15 11.093 -19.310 39.816 1.00 25.42 C ANISOU 105 CD GLU A 15 1958 4212 3487 184 -1321 981 C ATOM 106 OE1 GLU A 15 10.792 -19.145 41.016 1.00 26.18 O ANISOU 106 OE1 GLU A 15 2135 4391 3419 150 -1447 980 O ATOM 107 OE2 GLU A 15 11.896 -20.189 39.434 1.00 26.29 O ANISOU 107 OE2 GLU A 15 1928 4316 3744 281 -1291 1094 O ATOM 108 N PRO A 16 8.850 -19.795 34.604 1.00 19.44 N ANISOU 108 N PRO A 16 1399 3013 2974 308 -610 744 N ATOM 109 CA PRO A 16 7.875 -20.455 33.737 1.00 18.28 C ANISOU 109 CA PRO A 16 1365 2757 2821 368 -471 698 C ATOM 110 C PRO A 16 7.070 -21.495 34.481 1.00 18.14 C ANISOU 110 C PRO A 16 1448 2696 2748 424 -490 743 C ATOM 111 O PRO A 16 7.624 -22.256 35.266 1.00 19.07 O ANISOU 111 O PRO A 16 1505 2844 2897 485 -562 848 O ATOM 112 CB PRO A 16 8.738 -21.116 32.646 1.00 18.93 C ANISOU 112 CB PRO A 16 1335 2813 3043 466 -363 727 C ATOM 113 CG PRO A 16 9.999 -20.368 32.640 1.00 20.06 C ANISOU 113 CG PRO A 16 1307 3052 3260 423 -413 766 C ATOM 114 CD PRO A 16 10.220 -19.887 34.061 1.00 20.69 C ANISOU 114 CD PRO A 16 1367 3214 3278 347 -594 806 C ATOM 115 N LEU A 17 5.760 -21.461 34.247 1.00 17.01 N ANISOU 115 N LEU A 17 1449 2486 2527 397 -431 677 N ATOM 116 CA LEU A 17 4.831 -22.469 34.761 1.00 17.00 C ANISOU 116 CA LEU A 17 1544 2426 2489 438 -422 722 C ATOM 117 C LEU A 17 4.480 -23.446 33.637 1.00 16.82 C ANISOU 117 C LEU A 17 1556 2274 2560 511 -306 697 C ATOM 118 O LEU A 17 4.495 -24.655 33.853 1.00 17.59 O ANISOU 118 O LEU A 17 1657 2301 2724 589 -301 771 O ATOM 119 CB LEU A 17 3.566 -21.810 35.301 1.00 16.08 C ANISOU 119 CB LEU A 17 1550 2328 2230 358 -436 669 C ATOM 120 CG LEU A 17 2.518 -22.710 35.950 1.00 16.11 C ANISOU 120 CG LEU A 17 1644 2292 2184 380 -426 732 C ATOM 121 CD1 LEU A 17 3.050 -23.402 37.215 1.00 17.47 C ANISOU 121 CD1 LEU A 17 1776 2528 2332 422 -521 871 C ATOM 122 CD2 LEU A 17 1.298 -21.853 36.256 1.00 15.19 C ANISOU 122 CD2 LEU A 17 1627 2205 1937 305 -412 661 C ATOM 123 N GLY A 18 4.160 -22.933 32.449 1.00 16.00 N ANISOU 123 N GLY A 18 1485 2135 2458 484 -218 593 N ATOM 124 CA GLY A 18 3.965 -23.793 31.274 1.00 16.10 C ANISOU 124 CA GLY A 18 1530 2038 2546 554 -113 546 C ATOM 125 C GLY A 18 3.089 -23.146 30.217 1.00 15.08 C ANISOU 125 C GLY A 18 1486 1884 2358 497 -42 435 C ATOM 126 O GLY A 18 2.770 -21.971 30.310 1.00 14.23 O ANISOU 126 O GLY A 18 1394 1838 2173 411 -64 401 O ATOM 127 N ARG A 19 2.701 -23.936 29.217 1.00 15.36 N ANISOU 127 N ARG A 19 1579 1822 2433 547 35 376 N ATOM 128 CA ARG A 19 2.001 -23.448 28.029 1.00 14.70 C ANISOU 128 CA ARG A 19 1567 1722 2294 508 102 274 C ATOM 129 C ARG A 19 0.535 -23.845 28.007 1.00 14.19 C ANISOU 129 C ARG A 19 1620 1577 2191 465 91 239 C ATOM 130 O ARG A 19 0.176 -25.005 28.232 1.00 14.67 O ANISOU 130 O ARG A 19 1722 1540 2311 503 83 259 O ATOM 131 CB ARG A 19 2.673 -23.961 26.749 1.00 15.57 C ANISOU 131 CB ARG A 19 1658 1802 2453 595 199 213 C ATOM 132 CG ARG A 19 1.867 -23.686 25.464 1.00 15.04 C ANISOU 132 CG ARG A 19 1685 1717 2312 565 262 107 C ATOM 133 CD ARG A 19 2.710 -23.745 24.206 1.00 15.94 C ANISOU 133 CD ARG A 19 1764 1862 2429 639 368 51 C ATOM 134 NE ARG A 19 3.816 -22.785 24.218 1.00 16.20 N ANISOU 134 NE ARG A 19 1671 2014 2470 628 391 110 N ATOM 135 CZ ARG A 19 4.640 -22.565 23.192 1.00 17.11 C ANISOU 135 CZ ARG A 19 1726 2195 2578 677 494 91 C ATOM 136 NH1 ARG A 19 4.491 -23.225 22.043 1.00 17.83 N ANISOU 136 NH1 ARG A 19 1887 2252 2632 752 587 -1 N ATOM 137 NH2 ARG A 19 5.628 -21.675 23.308 1.00 17.46 N ANISOU 137 NH2 ARG A 19 1638 2344 2649 648 506 166 N ATOM 138 N VAL A 20 -0.316 -22.868 27.727 1.00 13.34 N ANISOU 138 N VAL A 20 1562 1508 1999 385 90 194 N ATOM 139 CA VAL A 20 -1.704 -23.145 27.459 1.00 13.09 C ANISOU 139 CA VAL A 20 1622 1413 1937 342 87 155 C ATOM 140 C VAL A 20 -1.990 -22.790 26.023 1.00 13.12 C ANISOU 140 C VAL A 20 1670 1416 1900 332 140 62 C ATOM 141 O VAL A 20 -1.573 -21.738 25.555 1.00 12.88 O ANISOU 141 O VAL A 20 1608 1461 1823 312 163 48 O ATOM 142 CB VAL A 20 -2.626 -22.318 28.376 1.00 12.21 C ANISOU 142 CB VAL A 20 1529 1354 1756 265 39 188 C ATOM 143 CG1 VAL A 20 -4.075 -22.764 28.185 1.00 11.90 C ANISOU 143 CG1 VAL A 20 1559 1251 1708 225 36 169 C ATOM 144 CG2 VAL A 20 -2.179 -22.470 29.810 1.00 12.55 C ANISOU 144 CG2 VAL A 20 1529 1436 1802 276 -13 279 C ATOM 145 N SER A 21 -2.721 -23.646 25.318 1.00 13.77 N ANISOU 145 N SER A 21 1825 1410 1996 340 151 2 N ATOM 146 CA SER A 21 -3.167 -23.294 23.971 1.00 13.91 C ANISOU 146 CA SER A 21 1896 1440 1946 322 184 -86 C ATOM 147 C SER A 21 -4.693 -23.313 23.825 1.00 13.68 C ANISOU 147 C SER A 21 1933 1374 1887 248 136 -111 C ATOM 148 O SER A 21 -5.391 -24.044 24.526 1.00 14.01 O ANISOU 148 O SER A 21 1991 1346 1984 224 95 -77 O ATOM 149 CB SER A 21 -2.507 -24.198 22.945 1.00 15.14 C ANISOU 149 CB SER A 21 2079 1546 2125 406 243 -167 C ATOM 150 OG SER A 21 -3.111 -25.471 22.988 1.00 15.99 O ANISOU 150 OG SER A 21 2252 1522 2301 418 212 -204 O ATOM 151 N PHE A 22 -5.197 -22.485 22.921 1.00 13.48 N ANISOU 151 N PHE A 22 1936 1404 1779 211 142 -153 N ATOM 152 CA PHE A 22 -6.629 -22.290 22.715 1.00 13.24 C ANISOU 152 CA PHE A 22 1947 1364 1718 141 92 -166 C ATOM 153 C PHE A 22 -7.006 -22.426 21.248 1.00 14.03 C ANISOU 153 C PHE A 22 2112 1464 1751 137 93 -258 C ATOM 154 O PHE A 22 -6.329 -21.854 20.387 1.00 14.20 O ANISOU 154 O PHE A 22 2139 1555 1701 167 142 -284 O ATOM 155 CB PHE A 22 -6.996 -20.869 23.086 1.00 12.32 C ANISOU 155 CB PHE A 22 1795 1331 1554 98 81 -113 C ATOM 156 CG PHE A 22 -6.562 -20.468 24.431 1.00 11.81 C ANISOU 156 CG PHE A 22 1677 1292 1519 100 77 -43 C ATOM 157 CD1 PHE A 22 -7.362 -20.725 25.521 1.00 11.68 C ANISOU 157 CD1 PHE A 22 1651 1257 1528 74 45 5 C ATOM 158 CD2 PHE A 22 -5.370 -19.783 24.610 1.00 11.80 C ANISOU 158 CD2 PHE A 22 1629 1343 1511 124 104 -22 C ATOM 159 CE1 PHE A 22 -6.988 -20.326 26.810 1.00 11.47 C ANISOU 159 CE1 PHE A 22 1586 1271 1500 79 37 63 C ATOM 160 CE2 PHE A 22 -4.969 -19.373 25.891 1.00 11.70 C ANISOU 160 CE2 PHE A 22 1572 1360 1514 119 80 31 C ATOM 161 CZ PHE A 22 -5.787 -19.647 26.997 1.00 11.53 C ANISOU 161 CZ PHE A 22 1557 1326 1495 100 46 68 C ATOM 162 N GLU A 23 -8.084 -23.153 20.957 1.00 14.64 N ANISOU 162 N GLU A 23 2238 1474 1847 93 35 -301 N ATOM 163 CA GLU A 23 -8.738 -23.036 19.655 1.00 15.28 C ANISOU 163 CA GLU A 23 2381 1581 1843 66 5 -379 C ATOM 164 C GLU A 23 -9.688 -21.851 19.756 1.00 14.41 C ANISOU 164 C GLU A 23 2235 1549 1691 6 -32 -313 C ATOM 165 O GLU A 23 -10.374 -21.702 20.768 1.00 13.86 O ANISOU 165 O GLU A 23 2116 1464 1683 -31 -60 -243 O ATOM 166 CB GLU A 23 -9.530 -24.287 19.294 1.00 16.60 C ANISOU 166 CB GLU A 23 2609 1638 2058 32 -60 -458 C ATOM 167 CG GLU A 23 -10.309 -24.155 17.976 1.00 17.51 C ANISOU 167 CG GLU A 23 2788 1791 2071 -7 -118 -543 C ATOM 168 CD GLU A 23 -11.141 -25.378 17.635 1.00 18.96 C ANISOU 168 CD GLU A 23 3032 1856 2313 -60 -206 -631 C ATOM 169 OE1 GLU A 23 -11.162 -26.340 18.434 1.00 19.42 O ANISOU 169 OE1 GLU A 23 3081 1790 2506 -69 -218 -614 O ATOM 170 OE2 GLU A 23 -11.783 -25.377 16.559 1.00 19.90 O ANISOU 170 OE2 GLU A 23 3209 2006 2346 -99 -273 -712 O ATOM 171 N LEU A 24 -9.725 -21.016 18.718 1.00 14.34 N ANISOU 171 N LEU A 24 2248 1624 1576 5 -28 -329 N ATOM 172 CA LEU A 24 -10.638 -19.877 18.668 1.00 13.82 C ANISOU 172 CA LEU A 24 2150 1621 1477 -38 -68 -265 C ATOM 173 C LEU A 24 -11.716 -20.140 17.629 1.00 14.59 C ANISOU 173 C LEU A 24 2293 1732 1518 -82 -149 -315 C ATOM 174 O LEU A 24 -11.419 -20.446 16.489 1.00 15.52 O ANISOU 174 O LEU A 24 2478 1876 1540 -64 -150 -391 O ATOM 175 CB LEU A 24 -9.890 -18.588 18.321 1.00 13.45 C ANISOU 175 CB LEU A 24 2086 1658 1365 -12 -13 -215 C ATOM 176 CG LEU A 24 -8.640 -18.278 19.158 1.00 12.98 C ANISOU 176 CG LEU A 24 1979 1597 1353 24 56 -176 C ATOM 177 CD1 LEU A 24 -8.099 -16.879 18.760 1.00 12.77 C ANISOU 177 CD1 LEU A 24 1928 1641 1280 24 93 -113 C ATOM 178 CD2 LEU A 24 -8.890 -18.378 20.664 1.00 12.00 C ANISOU 178 CD2 LEU A 24 1808 1427 1324 11 39 -134 C ATOM 179 N PHE A 25 -12.974 -19.981 18.018 1.00 14.46 N ANISOU 179 N PHE A 25 2232 1708 1552 -137 -219 -269 N ATOM 180 CA PHE A 25 -14.090 -20.436 17.193 1.00 15.35 C ANISOU 180 CA PHE A 25 2369 1821 1640 -194 -320 -314 C ATOM 181 C PHE A 25 -14.448 -19.364 16.149 1.00 15.53 C ANISOU 181 C PHE A 25 2401 1950 1547 -194 -354 -286 C ATOM 182 O PHE A 25 -15.517 -18.758 16.195 1.00 15.34 O ANISOU 182 O PHE A 25 2319 1961 1545 -227 -416 -219 O ATOM 183 CB PHE A 25 -15.283 -20.794 18.094 1.00 15.38 C ANISOU 183 CB PHE A 25 2299 1778 1767 -255 -376 -260 C ATOM 184 CG PHE A 25 -14.989 -21.886 19.097 1.00 15.35 C ANISOU 184 CG PHE A 25 2287 1670 1873 -261 -348 -264 C ATOM 185 CD1 PHE A 25 -14.306 -23.033 18.722 1.00 16.19 C ANISOU 185 CD1 PHE A 25 2470 1690 1989 -247 -345 -360 C ATOM 186 CD2 PHE A 25 -15.378 -21.759 20.406 1.00 14.74 C ANISOU 186 CD2 PHE A 25 2131 1583 1886 -271 -320 -169 C ATOM 187 CE1 PHE A 25 -14.036 -24.053 19.649 1.00 16.35 C ANISOU 187 CE1 PHE A 25 2483 1601 2125 -248 -324 -345 C ATOM 188 CE2 PHE A 25 -15.108 -22.759 21.322 1.00 14.94 C ANISOU 188 CE2 PHE A 25 2151 1521 2004 -277 -296 -150 C ATOM 189 CZ PHE A 25 -14.438 -23.908 20.939 1.00 15.68 C ANISOU 189 CZ PHE A 25 2317 1516 2124 -267 -302 -231 C ATOM 190 N ALA A 26 -13.516 -19.145 15.222 1.00 15.89 N ANISOU 190 N ALA A 26 2513 2051 1473 -149 -307 -325 N ATOM 191 CA ALA A 26 -13.663 -18.150 14.159 1.00 16.46 C ANISOU 191 CA ALA A 26 2604 2231 1417 -143 -326 -282 C ATOM 192 C ALA A 26 -14.808 -18.509 13.222 1.00 17.74 C ANISOU 192 C ALA A 26 2798 2430 1512 -195 -456 -324 C ATOM 193 O ALA A 26 -15.424 -17.622 12.643 1.00 18.22 O ANISOU 193 O ALA A 26 2839 2573 1510 -205 -511 -250 O ATOM 194 CB ALA A 26 -12.347 -18.005 13.358 1.00 16.75 C ANISOU 194 CB ALA A 26 2703 2328 1331 -85 -232 -312 C ATOM 195 N ASP A 27 -15.102 -19.802 13.083 1.00 18.59 N ANISOU 195 N ASP A 27 2951 2470 1641 -231 -515 -440 N ATOM 196 CA ASP A 27 -16.258 -20.233 12.287 1.00 20.02 C ANISOU 196 CA ASP A 27 3154 2674 1777 -300 -663 -490 C ATOM 197 C ASP A 27 -17.566 -19.640 12.805 1.00 19.68 C ANISOU 197 C ASP A 27 2993 2647 1837 -353 -746 -374 C ATOM 198 O ASP A 27 -18.445 -19.357 12.004 1.00 20.52 O ANISOU 198 O ASP A 27 3089 2828 1876 -391 -861 -356 O ATOM 199 CB ASP A 27 -16.343 -21.771 12.145 1.00 21.24 C ANISOU 199 CB ASP A 27 3379 2721 1970 -341 -720 -643 C ATOM 200 CG ASP A 27 -16.557 -22.502 13.478 1.00 20.62 C ANISOU 200 CG ASP A 27 3232 2504 2096 -374 -704 -619 C ATOM 201 OD1 ASP A 27 -15.971 -22.123 14.517 1.00 19.48 O ANISOU 201 OD1 ASP A 27 3032 2337 2031 -329 -597 -537 O ATOM 202 OD2 ASP A 27 -17.310 -23.493 13.491 1.00 21.83 O ANISOU 202 OD2 ASP A 27 3389 2569 2333 -452 -805 -680 O ATOM 203 N LYS A 28 -17.669 -19.403 14.125 1.00 18.43 N ANISOU 203 N LYS A 28 2742 2431 1829 -346 -684 -292 N ATOM 204 CA LYS A 28 -18.926 -18.916 14.740 1.00 18.26 C ANISOU 204 CA LYS A 28 2596 2422 1917 -383 -741 -186 C ATOM 205 C LYS A 28 -18.883 -17.515 15.338 1.00 16.77 C ANISOU 205 C LYS A 28 2338 2276 1756 -322 -668 -64 C ATOM 206 O LYS A 28 -19.903 -16.847 15.408 1.00 17.08 O ANISOU 206 O LYS A 28 2289 2357 1841 -328 -720 20 O ATOM 207 CB LYS A 28 -19.420 -19.908 15.803 1.00 18.55 C ANISOU 207 CB LYS A 28 2572 2361 2112 -436 -746 -190 C ATOM 208 CG LYS A 28 -20.243 -21.049 15.204 1.00 20.44 C ANISOU 208 CG LYS A 28 2825 2560 2380 -533 -883 -267 C ATOM 209 CD LYS A 28 -19.831 -22.356 15.796 1.00 20.84 C ANISOU 209 CD LYS A 28 2914 2476 2525 -564 -856 -337 C ATOM 210 CE LYS A 28 -20.312 -23.526 14.968 1.00 22.83 C ANISOU 210 CE LYS A 28 3227 2663 2784 -653 -991 -456 C ATOM 211 NZ LYS A 28 -19.691 -24.776 15.549 1.00 23.29 N ANISOU 211 NZ LYS A 28 3341 2564 2944 -662 -947 -524 N ATOM 212 N VAL A 29 -17.725 -17.074 15.798 1.00 15.41 N ANISOU 212 N VAL A 29 2200 2086 1569 -262 -551 -59 N ATOM 213 CA VAL A 29 -17.567 -15.703 16.306 1.00 14.31 C ANISOU 213 CA VAL A 29 2014 1968 1456 -208 -488 37 C ATOM 214 C VAL A 29 -16.322 -15.080 15.683 1.00 13.83 C ANISOU 214 C VAL A 29 2025 1937 1293 -166 -421 37 C ATOM 215 O VAL A 29 -15.323 -14.894 16.368 1.00 13.02 O ANISOU 215 O VAL A 29 1929 1798 1219 -136 -330 35 O ATOM 216 CB VAL A 29 -17.477 -15.662 17.879 1.00 13.32 C ANISOU 216 CB VAL A 29 1828 1782 1450 -188 -410 62 C ATOM 217 CG1 VAL A 29 -18.822 -15.354 18.482 1.00 13.53 C ANISOU 217 CG1 VAL A 29 1750 1819 1570 -196 -445 130 C ATOM 218 CG2 VAL A 29 -16.920 -16.943 18.428 1.00 13.08 C ANISOU 218 CG2 VAL A 29 1829 1688 1451 -211 -379 -7 C ATOM 219 N PRO A 30 -16.352 -14.808 14.365 1.00 14.54 N ANISOU 219 N PRO A 30 2164 2102 1256 -168 -470 45 N ATOM 220 CA PRO A 30 -15.132 -14.364 13.683 1.00 14.53 C ANISOU 220 CA PRO A 30 2228 2143 1147 -133 -394 53 C ATOM 221 C PRO A 30 -14.573 -13.005 14.165 1.00 13.74 C ANISOU 221 C PRO A 30 2091 2028 1100 -98 -321 157 C ATOM 222 O PRO A 30 -13.375 -12.845 14.257 1.00 13.38 O ANISOU 222 O PRO A 30 2068 1976 1040 -79 -232 154 O ATOM 223 CB PRO A 30 -15.560 -14.302 12.211 1.00 15.96 C ANISOU 223 CB PRO A 30 2463 2426 1173 -146 -476 59 C ATOM 224 CG PRO A 30 -17.058 -14.172 12.241 1.00 16.40 C ANISOU 224 CG PRO A 30 2452 2491 1286 -179 -600 103 C ATOM 225 CD PRO A 30 -17.469 -14.983 13.412 1.00 15.71 C ANISOU 225 CD PRO A 30 2310 2312 1344 -206 -598 49 C ATOM 226 N LYS A 31 -15.427 -12.046 14.487 1.00 13.57 N ANISOU 226 N LYS A 31 2009 1992 1153 -89 -360 246 N ATOM 227 CA LYS A 31 -14.928 -10.744 14.955 1.00 13.15 C ANISOU 227 CA LYS A 31 1933 1898 1166 -58 -301 331 C ATOM 228 C LYS A 31 -14.210 -10.871 16.306 1.00 12.00 C ANISOU 228 C LYS A 31 1766 1674 1117 -51 -225 282 C ATOM 229 O LYS A 31 -13.129 -10.296 16.516 1.00 11.73 O ANISOU 229 O LYS A 31 1743 1615 1098 -44 -159 303 O ATOM 230 CB LYS A 31 -16.061 -9.709 15.045 1.00 13.46 C ANISOU 230 CB LYS A 31 1914 1922 1278 -34 -359 426 C ATOM 231 CG LYS A 31 -15.550 -8.287 15.067 1.00 13.67 C ANISOU 231 CG LYS A 31 1940 1902 1352 -5 -318 523 C ATOM 232 CD LYS A 31 -16.684 -7.224 15.100 1.00 14.30 C ANISOU 232 CD LYS A 31 1964 1950 1517 36 -376 620 C ATOM 233 CE LYS A 31 -16.108 -5.824 15.285 1.00 14.54 C ANISOU 233 CE LYS A 31 2002 1893 1626 63 -332 703 C ATOM 234 NZ LYS A 31 -17.063 -4.730 14.882 1.00 15.66 N ANISOU 234 NZ LYS A 31 2108 2009 1832 112 -393 825 N ATOM 235 N THR A 32 -14.820 -11.627 17.210 1.00 11.52 N ANISOU 235 N THR A 32 1671 1582 1121 -57 -239 227 N ATOM 236 CA THR A 32 -14.312 -11.784 18.573 1.00 10.65 C ANISOU 236 CA THR A 32 1542 1415 1090 -47 -181 189 C ATOM 237 C THR A 32 -13.056 -12.618 18.568 1.00 10.41 C ANISOU 237 C THR A 32 1551 1383 1020 -56 -130 130 C ATOM 238 O THR A 32 -12.110 -12.303 19.278 1.00 9.86 O ANISOU 238 O THR A 32 1475 1284 986 -46 -77 127 O ATOM 239 CB THR A 32 -15.363 -12.462 19.486 1.00 10.42 C ANISOU 239 CB THR A 32 1461 1369 1127 -53 -204 166 C ATOM 240 OG1 THR A 32 -16.582 -11.714 19.430 1.00 10.78 O ANISOU 240 OG1 THR A 32 1453 1427 1216 -34 -247 225 O ATOM 241 CG2 THR A 32 -14.871 -12.503 20.913 1.00 9.74 C ANISOU 241 CG2 THR A 32 1361 1241 1098 -36 -144 141 C ATOM 242 N ALA A 33 -13.074 -13.689 17.770 1.00 10.91 N ANISOU 242 N ALA A 33 1652 1475 1015 -73 -152 77 N ATOM 243 CA ALA A 33 -11.907 -14.548 17.572 1.00 10.99 C ANISOU 243 CA ALA A 33 1703 1486 987 -64 -99 14 C ATOM 244 C ALA A 33 -10.738 -13.743 17.002 1.00 11.31 C ANISOU 244 C ALA A 33 1754 1564 976 -46 -35 56 C ATOM 245 O ALA A 33 -9.577 -13.926 17.412 1.00 10.98 O ANISOU 245 O ALA A 33 1701 1510 959 -30 29 42 O ATOM 246 CB ALA A 33 -12.245 -15.717 16.621 1.00 11.84 C ANISOU 246 CB ALA A 33 1864 1611 1020 -78 -142 -63 C ATOM 247 N GLU A 34 -11.038 -12.858 16.048 1.00 11.94 N ANISOU 247 N GLU A 34 1848 1695 992 -50 -55 122 N ATOM 248 CA GLU A 34 -9.971 -12.120 15.390 1.00 12.44 C ANISOU 248 CA GLU A 34 1918 1803 1006 -43 10 183 C ATOM 249 C GLU A 34 -9.296 -11.151 16.390 1.00 11.69 C ANISOU 249 C GLU A 34 1770 1646 1024 -50 47 237 C ATOM 250 O GLU A 34 -8.070 -11.064 16.431 1.00 11.79 O ANISOU 250 O GLU A 34 1764 1670 1046 -50 114 250 O ATOM 251 CB GLU A 34 -10.492 -11.421 14.142 1.00 13.57 C ANISOU 251 CB GLU A 34 2090 2017 1049 -47 -24 261 C ATOM 252 CG GLU A 34 -9.491 -10.481 13.496 1.00 14.47 C ANISOU 252 CG GLU A 34 2200 2174 1122 -48 46 363 C ATOM 253 CD GLU A 34 -8.237 -11.180 12.998 1.00 15.19 C ANISOU 253 CD GLU A 34 2307 2331 1133 -29 142 319 C ATOM 254 OE1 GLU A 34 -8.179 -12.461 12.976 1.00 15.36 O ANISOU 254 OE1 GLU A 34 2362 2362 1112 -6 148 197 O ATOM 255 OE2 GLU A 34 -7.307 -10.433 12.606 1.00 15.89 O ANISOU 255 OE2 GLU A 34 2370 2457 1209 -36 216 413 O ATOM 256 N ASN A 35 -10.096 -10.464 17.209 1.00 10.99 N ANISOU 256 N ASN A 35 1656 1495 1024 -54 2 261 N ATOM 257 CA ASN A 35 -9.571 -9.574 18.266 1.00 10.43 C ANISOU 257 CA ASN A 35 1550 1354 1058 -61 20 282 C ATOM 258 C ASN A 35 -8.573 -10.327 19.168 1.00 9.79 C ANISOU 258 C ASN A 35 1449 1262 1009 -63 58 218 C ATOM 259 O ASN A 35 -7.472 -9.849 19.427 1.00 9.94 O ANISOU 259 O ASN A 35 1440 1268 1067 -80 92 242 O ATOM 260 CB ASN A 35 -10.724 -9.004 19.100 1.00 10.09 C ANISOU 260 CB ASN A 35 1493 1251 1090 -45 -27 281 C ATOM 261 CG ASN A 35 -10.251 -8.110 20.260 1.00 9.94 C ANISOU 261 CG ASN A 35 1456 1154 1167 -48 -16 273 C ATOM 262 OD1 ASN A 35 -9.514 -7.125 20.067 1.00 10.28 O ANISOU 262 OD1 ASN A 35 1497 1158 1251 -70 -4 324 O ATOM 263 ND2 ASN A 35 -10.711 -8.440 21.477 1.00 9.43 N ANISOU 263 ND2 ASN A 35 1380 1065 1137 -28 -24 209 N ATOM 264 N PHE A 36 -8.954 -11.514 19.622 1.00 9.05 N ANISOU 264 N PHE A 36 1362 1171 905 -48 46 149 N ATOM 265 CA PHE A 36 -8.107 -12.273 20.532 1.00 8.51 C ANISOU 265 CA PHE A 36 1273 1089 871 -41 72 103 C ATOM 266 C PHE A 36 -6.847 -12.782 19.844 1.00 8.86 C ANISOU 266 C PHE A 36 1309 1175 880 -30 130 100 C ATOM 267 O PHE A 36 -5.764 -12.758 20.435 1.00 8.81 O ANISOU 267 O PHE A 36 1260 1165 920 -30 157 106 O ATOM 268 CB PHE A 36 -8.886 -13.431 21.130 1.00 8.09 C ANISOU 268 CB PHE A 36 1229 1020 826 -30 45 52 C ATOM 269 CG PHE A 36 -8.172 -14.152 22.221 1.00 7.78 C ANISOU 269 CG PHE A 36 1167 961 827 -18 60 27 C ATOM 270 CD1 PHE A 36 -8.323 -13.766 23.551 1.00 7.45 C ANISOU 270 CD1 PHE A 36 1103 899 826 -20 43 33 C ATOM 271 CD2 PHE A 36 -7.378 -15.257 21.930 1.00 8.05 C ANISOU 271 CD2 PHE A 36 1205 1000 853 3 89 -2 C ATOM 272 CE1 PHE A 36 -7.687 -14.469 24.581 1.00 7.37 C ANISOU 272 CE1 PHE A 36 1074 886 839 -8 46 23 C ATOM 273 CE2 PHE A 36 -6.724 -15.959 22.953 1.00 7.92 C ANISOU 273 CE2 PHE A 36 1161 964 882 21 95 -7 C ATOM 274 CZ PHE A 36 -6.890 -15.566 24.279 1.00 7.58 C ANISOU 274 CZ PHE A 36 1095 912 870 11 68 12 C ATOM 275 N ARG A 37 -7.003 -13.257 18.611 1.00 9.25 N ANISOU 275 N ARG A 37 1397 1272 843 -16 147 87 N ATOM 276 CA ARG A 37 -5.887 -13.736 17.827 1.00 9.83 C ANISOU 276 CA ARG A 37 1468 1399 866 9 219 76 C ATOM 277 C ARG A 37 -4.844 -12.641 17.634 1.00 10.11 C ANISOU 277 C ARG A 37 1450 1465 923 -10 270 163 C ATOM 278 O ARG A 37 -3.663 -12.851 17.894 1.00 10.26 O ANISOU 278 O ARG A 37 1414 1501 982 1 323 170 O ATOM 279 CB ARG A 37 -6.359 -14.226 16.457 1.00 10.68 C ANISOU 279 CB ARG A 37 1643 1564 849 27 224 42 C ATOM 280 CG ARG A 37 -5.272 -14.972 15.654 1.00 11.68 C ANISOU 280 CG ARG A 37 1779 1750 906 78 314 1 C ATOM 281 CD ARG A 37 -5.610 -15.060 14.140 1.00 12.83 C ANISOU 281 CD ARG A 37 1999 1984 890 93 327 -17 C ATOM 282 NE ARG A 37 -5.544 -13.742 13.517 1.00 13.32 N ANISOU 282 NE ARG A 37 2044 2112 904 62 344 104 N ATOM 283 CZ ARG A 37 -4.430 -13.036 13.303 1.00 13.87 C ANISOU 283 CZ ARG A 37 2055 2231 982 61 432 195 C ATOM 284 NH1 ARG A 37 -3.232 -13.492 13.640 1.00 14.06 N ANISOU 284 NH1 ARG A 37 2020 2263 1057 94 515 176 N ATOM 285 NH2 ARG A 37 -4.516 -11.847 12.736 1.00 14.41 N ANISOU 285 NH2 ARG A 37 2115 2341 1018 25 436 319 N ATOM 286 N ALA A 38 -5.289 -11.479 17.160 1.00 10.24 N ANISOU 286 N ALA A 38 1476 1486 926 -43 251 240 N ATOM 287 CA ALA A 38 -4.403 -10.328 16.946 1.00 10.73 C ANISOU 287 CA ALA A 38 1488 1558 1029 -79 291 342 C ATOM 288 C ALA A 38 -3.774 -9.794 18.253 1.00 10.29 C ANISOU 288 C ALA A 38 1371 1431 1106 -114 266 346 C ATOM 289 O ALA A 38 -2.593 -9.484 18.271 1.00 10.83 O ANISOU 289 O ALA A 38 1372 1519 1223 -139 310 395 O ATOM 290 CB ALA A 38 -5.137 -9.238 16.194 1.00 11.17 C ANISOU 290 CB ALA A 38 1575 1613 1054 -104 263 431 C ATOM 291 N LEU A 39 -4.533 -9.699 19.348 1.00 9.46 N ANISOU 291 N LEU A 39 1284 1253 1057 -117 197 296 N ATOM 292 CA LEU A 39 -3.918 -9.327 20.641 1.00 9.26 C ANISOU 292 CA LEU A 39 1214 1175 1129 -145 165 277 C ATOM 293 C LEU A 39 -2.901 -10.385 21.128 1.00 9.21 C ANISOU 293 C LEU A 39 1157 1208 1132 -123 191 240 C ATOM 294 O LEU A 39 -1.944 -10.069 21.802 1.00 9.41 O ANISOU 294 O LEU A 39 1121 1225 1228 -154 179 255 O ATOM 295 CB LEU A 39 -4.978 -9.035 21.708 1.00 8.64 C ANISOU 295 CB LEU A 39 1173 1029 1081 -139 98 225 C ATOM 296 CG LEU A 39 -5.890 -7.836 21.391 1.00 8.92 C ANISOU 296 CG LEU A 39 1242 1006 1139 -149 69 265 C ATOM 297 CD1 LEU A 39 -7.072 -7.795 22.360 1.00 8.48 C ANISOU 297 CD1 LEU A 39 1217 906 1096 -117 26 203 C ATOM 298 CD2 LEU A 39 -5.128 -6.537 21.417 1.00 9.67 C ANISOU 298 CD2 LEU A 39 1311 1039 1321 -204 60 322 C ATOM 299 N SER A 40 -3.105 -11.631 20.741 1.00 9.05 N ANISOU 299 N SER A 40 1161 1225 1049 -71 222 195 N ATOM 300 CA SER A 40 -2.149 -12.678 21.047 1.00 9.30 C ANISOU 300 CA SER A 40 1147 1286 1100 -33 254 170 C ATOM 301 C SER A 40 -0.825 -12.528 20.279 1.00 10.32 C ANISOU 301 C SER A 40 1201 1480 1238 -30 333 226 C ATOM 302 O SER A 40 0.231 -12.814 20.830 1.00 10.78 O ANISOU 302 O SER A 40 1179 1556 1361 -21 344 238 O ATOM 303 CB SER A 40 -2.775 -14.061 20.804 1.00 9.06 C ANISOU 303 CB SER A 40 1172 1252 1017 23 263 100 C ATOM 304 OG SER A 40 -3.771 -14.306 21.784 1.00 8.29 O ANISOU 304 OG SER A 40 1110 1102 937 16 196 68 O ATOM 305 N THR A 41 -0.869 -12.069 19.029 1.00 10.93 N ANISOU 305 N THR A 41 1297 1605 1251 -36 390 272 N ATOM 306 CA THR A 41 0.346 -11.967 18.232 1.00 12.09 C ANISOU 306 CA THR A 41 1367 1833 1393 -27 487 337 C ATOM 307 C THR A 41 1.053 -10.638 18.405 1.00 12.68 C ANISOU 307 C THR A 41 1360 1899 1557 -110 480 443 C ATOM 308 O THR A 41 2.208 -10.556 18.097 1.00 13.74 O ANISOU 308 O THR A 41 1396 2096 1728 -116 549 507 O ATOM 309 CB THR A 41 0.084 -12.157 16.738 1.00 12.85 C ANISOU 309 CB THR A 41 1519 2008 1353 9 565 346 C ATOM 310 OG1 THR A 41 -0.792 -11.122 16.271 1.00 12.78 O ANISOU 310 OG1 THR A 41 1566 1983 1306 -42 525 404 O ATOM 311 CG2 THR A 41 -0.530 -13.536 16.479 1.00 12.62 C ANISOU 311 CG2 THR A 41 1575 1978 1242 86 566 225 C ATOM 312 N GLY A 42 0.361 -9.596 18.868 1.00 12.26 N ANISOU 312 N GLY A 42 1343 1764 1548 -174 398 462 N ATOM 313 CA GLY A 42 0.964 -8.265 19.026 1.00 12.98 C ANISOU 313 CA GLY A 42 1371 1816 1744 -264 378 556 C ATOM 314 C GLY A 42 1.063 -7.504 17.715 1.00 14.00 C ANISOU 314 C GLY A 42 1496 1989 1833 -292 448 678 C ATOM 315 O GLY A 42 1.719 -6.487 17.643 1.00 14.89 O ANISOU 315 O GLY A 42 1542 2076 2039 -371 451 781 O ATOM 316 N GLU A 43 0.405 -8.014 16.676 1.00 14.03 N ANISOU 316 N GLU A 43 1574 2060 1696 -233 499 670 N ATOM 317 CA GLU A 43 0.547 -7.493 15.330 1.00 15.28 C ANISOU 317 CA GLU A 43 1733 2297 1774 -243 579 789 C ATOM 318 C GLU A 43 -0.119 -6.115 15.107 1.00 15.52 C ANISOU 318 C GLU A 43 1801 2246 1848 -308 522 893 C ATOM 319 O GLU A 43 0.097 -5.514 14.097 1.00 16.63 O ANISOU 319 O GLU A 43 1931 2442 1945 -332 581 1025 O ATOM 320 CB GLU A 43 0.011 -8.519 14.300 1.00 15.49 C ANISOU 320 CB GLU A 43 1842 2428 1614 -156 634 729 C ATOM 321 CG GLU A 43 -1.514 -8.727 14.323 1.00 14.57 C ANISOU 321 CG GLU A 43 1841 2261 1431 -132 541 652 C ATOM 322 CD GLU A 43 -1.942 -9.921 13.465 1.00 14.89 C ANISOU 322 CD GLU A 43 1959 2392 1305 -56 575 560 C ATOM 323 OE1 GLU A 43 -1.600 -11.080 13.799 1.00 14.67 O ANISOU 323 OE1 GLU A 43 1927 2372 1274 -2 600 449 O ATOM 324 OE2 GLU A 43 -2.608 -9.703 12.436 1.00 15.60 O ANISOU 324 OE2 GLU A 43 2116 2542 1266 -48 571 598 O ATOM 325 N LYS A 44 -0.946 -5.638 16.033 1.00 14.60 N ANISOU 325 N LYS A 44 1731 2002 1815 -328 414 838 N ATOM 326 CA LYS A 44 -1.430 -4.252 15.941 1.00 15.17 C ANISOU 326 CA LYS A 44 1826 1969 1968 -383 361 936 C ATOM 327 C LYS A 44 -0.531 -3.321 16.741 1.00 15.76 C ANISOU 327 C LYS A 44 1824 1939 2222 -474 327 976 C ATOM 328 O LYS A 44 -0.747 -2.137 16.756 1.00 16.42 O ANISOU 328 O LYS A 44 1921 1910 2406 -529 282 1053 O ATOM 329 CB LYS A 44 -2.899 -4.122 16.381 1.00 14.22 C ANISOU 329 CB LYS A 44 1796 1765 1842 -343 270 860 C ATOM 330 CG LYS A 44 -3.861 -5.078 15.645 1.00 13.73 C ANISOU 330 CG LYS A 44 1801 1800 1615 -268 279 812 C ATOM 331 CD LYS A 44 -3.981 -4.778 14.150 1.00 14.93 C ANISOU 331 CD LYS A 44 1977 2045 1650 -263 326 942 C ATOM 332 CE LYS A 44 -4.918 -5.793 13.420 1.00 14.67 C ANISOU 332 CE LYS A 44 2016 2114 1443 -196 314 873 C ATOM 333 NZ LYS A 44 -4.736 -5.756 11.941 1.00 16.01 N ANISOU 333 NZ LYS A 44 2210 2417 1453 -186 375 978 N ATOM 334 N GLY A 45 0.499 -3.860 17.373 1.00 15.75 N ANISOU 334 N GLY A 45 1742 1973 2268 -491 343 928 N ATOM 335 CA GLY A 45 1.450 -3.051 18.110 1.00 16.70 C ANISOU 335 CA GLY A 45 1777 2009 2557 -590 298 962 C ATOM 336 C GLY A 45 1.232 -3.080 19.607 1.00 15.96 C ANISOU 336 C GLY A 45 1709 1818 2535 -596 187 817 C ATOM 337 O GLY A 45 1.915 -2.387 20.329 1.00 16.77 O ANISOU 337 O GLY A 45 1758 1840 2771 -680 123 818 O ATOM 338 N PHE A 46 0.262 -3.864 20.055 1.00 14.75 N ANISOU 338 N PHE A 46 1638 1677 2289 -511 162 696 N ATOM 339 CA PHE A 46 0.003 -4.092 21.477 1.00 14.14 C ANISOU 339 CA PHE A 46 1589 1543 2239 -498 75 559 C ATOM 340 C PHE A 46 -0.722 -5.402 21.626 1.00 13.04 C ANISOU 340 C PHE A 46 1498 1478 1975 -402 96 471 C ATOM 341 O PHE A 46 -1.164 -5.994 20.645 1.00 12.78 O ANISOU 341 O PHE A 46 1493 1516 1846 -350 160 498 O ATOM 342 CB PHE A 46 -0.833 -2.969 22.113 1.00 14.23 C ANISOU 342 CB PHE A 46 1678 1406 2322 -519 -8 514 C ATOM 343 CG PHE A 46 -2.111 -2.651 21.381 1.00 13.91 C ANISOU 343 CG PHE A 46 1718 1334 2232 -466 9 547 C ATOM 344 CD1 PHE A 46 -2.128 -1.734 20.341 1.00 14.95 C ANISOU 344 CD1 PHE A 46 1849 1425 2407 -502 34 682 C ATOM 345 CD2 PHE A 46 -3.302 -3.242 21.734 1.00 12.81 C ANISOU 345 CD2 PHE A 46 1646 1210 2010 -383 -2 458 C ATOM 346 CE1 PHE A 46 -3.325 -1.435 19.691 1.00 14.81 C ANISOU 346 CE1 PHE A 46 1898 1384 2344 -447 35 721 C ATOM 347 CE2 PHE A 46 -4.485 -2.943 21.058 1.00 12.71 C ANISOU 347 CE2 PHE A 46 1689 1176 1962 -334 2 496 C ATOM 348 CZ PHE A 46 -4.490 -2.064 20.061 1.00 13.66 C ANISOU 348 CZ PHE A 46 1809 1260 2119 -363 16 622 C ATOM 349 N GLY A 47 -0.876 -5.846 22.861 1.00 12.69 N ANISOU 349 N GLY A 47 1471 1417 1932 -382 37 366 N ATOM 350 CA GLY A 47 -1.510 -7.114 23.102 1.00 11.88 C ANISOU 350 CA GLY A 47 1405 1373 1733 -302 53 297 C ATOM 351 C GLY A 47 -1.092 -7.714 24.418 1.00 11.88 C ANISOU 351 C GLY A 47 1383 1387 1742 -294 1 225 C ATOM 352 O GLY A 47 -0.587 -7.017 25.298 1.00 12.32 O ANISOU 352 O GLY A 47 1418 1399 1863 -347 -67 201 O ATOM 353 N TYR A 48 -1.282 -9.024 24.506 1.00 11.52 N ANISOU 353 N TYR A 48 1343 1402 1630 -230 29 194 N ATOM 354 CA TYR A 48 -1.310 -9.726 25.764 1.00 11.57 C ANISOU 354 CA TYR A 48 1354 1421 1619 -204 -19 135 C ATOM 355 C TYR A 48 0.047 -10.021 26.371 1.00 12.61 C ANISOU 355 C TYR A 48 1395 1594 1799 -224 -49 152 C ATOM 356 O TYR A 48 0.111 -10.281 27.554 1.00 12.78 O ANISOU 356 O TYR A 48 1421 1625 1808 -219 -113 113 O ATOM 357 CB TYR A 48 -2.063 -11.036 25.582 1.00 10.83 C ANISOU 357 CB TYR A 48 1300 1357 1456 -134 18 113 C ATOM 358 CG TYR A 48 -3.540 -10.889 25.289 1.00 10.24 C ANISOU 358 CG TYR A 48 1303 1251 1336 -114 24 90 C ATOM 359 CD1 TYR A 48 -4.342 -9.999 26.006 1.00 10.20 C ANISOU 359 CD1 TYR A 48 1340 1199 1336 -125 -18 58 C ATOM 360 CD2 TYR A 48 -4.155 -11.682 24.349 1.00 10.00 C ANISOU 360 CD2 TYR A 48 1301 1240 1259 -79 67 93 C ATOM 361 CE1 TYR A 48 -5.697 -9.895 25.756 1.00 9.76 C ANISOU 361 CE1 TYR A 48 1333 1124 1252 -99 -10 47 C ATOM 362 CE2 TYR A 48 -5.512 -11.587 24.115 1.00 9.65 C ANISOU 362 CE2 TYR A 48 1309 1175 1182 -67 58 80 C ATOM 363 CZ TYR A 48 -6.275 -10.684 24.820 1.00 9.54 C ANISOU 363 CZ TYR A 48 1316 1121 1184 -75 22 65 C ATOM 364 OH TYR A 48 -7.639 -10.581 24.557 1.00 9.53 O ANISOU 364 OH TYR A 48 1347 1108 1164 -55 17 62 O ATOM 365 N LYS A 49 1.120 -9.972 25.575 1.00 13.75 N ANISOU 365 N LYS A 49 1452 1776 1995 -245 -3 219 N ATOM 366 CA LYS A 49 2.471 -10.283 26.052 1.00 14.87 C ANISOU 366 CA LYS A 49 1480 1969 2200 -259 -28 251 C ATOM 367 C LYS A 49 2.838 -9.316 27.141 1.00 15.67 C ANISOU 367 C LYS A 49 1564 2034 2355 -341 -142 226 C ATOM 368 O LYS A 49 2.664 -8.132 26.993 1.00 15.94 O ANISOU 368 O LYS A 49 1623 2001 2432 -409 -169 225 O ATOM 369 CB LYS A 49 3.502 -10.180 24.902 1.00 15.91 C ANISOU 369 CB LYS A 49 1507 2151 2385 -273 57 339 C ATOM 370 CG LYS A 49 4.886 -10.714 25.249 1.00 17.06 C ANISOU 370 CG LYS A 49 1510 2367 2603 -264 50 384 C ATOM 371 CD LYS A 49 5.860 -10.709 24.063 1.00 18.16 C ANISOU 371 CD LYS A 49 1535 2575 2787 -259 163 475 C ATOM 372 CE LYS A 49 7.163 -11.381 24.457 1.00 19.32 C ANISOU 372 CE LYS A 49 1529 2798 3014 -228 162 520 C ATOM 373 NZ LYS A 49 8.219 -11.234 23.383 1.00 20.82 N ANISOU 373 NZ LYS A 49 1579 3068 3261 -229 280 621 N ATOM 374 N GLY A 50 3.352 -9.841 28.240 1.00 16.35 N ANISOU 374 N GLY A 50 1612 2160 2440 -331 -216 205 N ATOM 375 CA GLY A 50 3.650 -9.051 29.417 1.00 17.21 C ANISOU 375 CA GLY A 50 1721 2246 2570 -403 -344 157 C ATOM 376 C GLY A 50 2.480 -8.770 30.362 1.00 16.90 C ANISOU 376 C GLY A 50 1816 2164 2440 -386 -395 58 C ATOM 377 O GLY A 50 2.716 -8.205 31.421 1.00 17.59 O ANISOU 377 O GLY A 50 1919 2243 2519 -433 -503 0 O ATOM 378 N SER A 51 1.230 -9.106 29.996 1.00 16.05 N ANISOU 378 N SER A 51 1801 2034 2262 -321 -323 37 N ATOM 379 CA SER A 51 0.066 -8.805 30.875 1.00 16.00 C ANISOU 379 CA SER A 51 1907 1997 2173 -296 -353 -48 C ATOM 380 C SER A 51 -0.219 -9.901 31.918 1.00 16.27 C ANISOU 380 C SER A 51 1963 2106 2110 -236 -372 -61 C ATOM 381 O SER A 51 0.229 -11.056 31.789 1.00 15.79 O ANISOU 381 O SER A 51 1849 2101 2050 -196 -347 0 O ATOM 382 CB SER A 51 -1.205 -8.522 30.058 1.00 15.12 C ANISOU 382 CB SER A 51 1869 1830 2046 -263 -277 -55 C ATOM 383 OG SER A 51 -1.719 -9.684 29.444 1.00 13.87 O ANISOU 383 OG SER A 51 1711 1711 1846 -200 -201 -14 O ATOM 384 N CYS A 52 -0.987 -9.534 32.942 1.00 17.23 N ANISOU 384 N CYS A 52 2168 2227 2149 -221 -409 -137 N ATOM 385 CA CYS A 52 -1.192 -10.399 34.122 1.00 17.92 C ANISOU 385 CA CYS A 52 2279 2398 2130 -175 -438 -139 C ATOM 386 C CYS A 52 -2.594 -11.043 34.135 1.00 16.42 C ANISOU 386 C CYS A 52 2152 2216 1870 -107 -354 -131 C ATOM 387 O CYS A 52 -3.525 -10.570 33.443 1.00 15.98 O ANISOU 387 O CYS A 52 2133 2102 1837 -96 -294 -153 O ATOM 388 CB CYS A 52 -0.917 -9.597 35.431 1.00 20.51 C ANISOU 388 CB CYS A 52 2652 2751 2389 -208 -545 -229 C ATOM 389 SG CYS A 52 -2.438 -8.779 36.103 1.00 22.72 S ANISOU 389 SG CYS A 52 3065 3000 2566 -164 -512 -346 S ATOM 390 N PHE A 53 -2.739 -12.154 34.869 1.00 15.46 N ANISOU 390 N PHE A 53 2029 2167 1677 -64 -352 -84 N ATOM 391 CA PHE A 53 -4.055 -12.584 35.360 1.00 14.50 C ANISOU 391 CA PHE A 53 1964 2071 1471 -14 -294 -81 C ATOM 392 C PHE A 53 -4.286 -11.877 36.709 1.00 14.79 C ANISOU 392 C PHE A 53 2064 2165 1387 -7 -342 -158 C ATOM 393 O PHE A 53 -3.683 -12.222 37.722 1.00 15.53 O ANISOU 393 O PHE A 53 2157 2341 1401 -6 -407 -144 O ATOM 394 CB PHE A 53 -4.165 -14.111 35.494 1.00 14.38 C ANISOU 394 CB PHE A 53 1922 2095 1446 23 -264 20 C ATOM 395 CG PHE A 53 -4.264 -14.823 34.175 1.00 13.52 C ANISOU 395 CG PHE A 53 1779 1920 1437 29 -205 66 C ATOM 396 CD1 PHE A 53 -3.154 -14.969 33.371 1.00 13.52 C ANISOU 396 CD1 PHE A 53 1721 1894 1522 16 -217 84 C ATOM 397 CD2 PHE A 53 -5.457 -15.327 33.740 1.00 13.07 C ANISOU 397 CD2 PHE A 53 1744 1834 1384 47 -139 85 C ATOM 398 CE1 PHE A 53 -3.241 -15.611 32.148 1.00 13.05 C ANISOU 398 CE1 PHE A 53 1644 1783 1532 31 -158 108 C ATOM 399 CE2 PHE A 53 -5.553 -15.962 32.513 1.00 12.59 C ANISOU 399 CE2 PHE A 53 1666 1714 1402 49 -98 107 C ATOM 400 CZ PHE A 53 -4.447 -16.089 31.711 1.00 12.53 C ANISOU 400 CZ PHE A 53 1618 1683 1460 45 -105 111 C ATOM 401 N HIS A 54 -5.140 -10.862 36.700 1.00 14.08 N ANISOU 401 N HIS A 54 2033 2033 1282 3 -311 -245 N ATOM 402 CA HIS A 54 -5.346 -10.026 37.874 1.00 14.86 C ANISOU 402 CA HIS A 54 2205 2169 1269 18 -349 -351 C ATOM 403 C HIS A 54 -6.435 -10.574 38.812 1.00 14.96 C ANISOU 403 C HIS A 54 2259 2281 1144 88 -281 -334 C ATOM 404 O HIS A 54 -6.551 -10.136 39.960 1.00 16.04 O ANISOU 404 O HIS A 54 2459 2488 1145 114 -305 -412 O ATOM 405 CB HIS A 54 -5.718 -8.609 37.434 1.00 14.97 C ANISOU 405 CB HIS A 54 2264 2074 1347 9 -345 -458 C ATOM 406 CG HIS A 54 -7.048 -8.527 36.778 1.00 14.20 C ANISOU 406 CG HIS A 54 2173 1934 1285 61 -239 -441 C ATOM 407 ND1 HIS A 54 -7.220 -8.736 35.425 1.00 12.99 N ANISOU 407 ND1 HIS A 54 1971 1716 1249 45 -199 -368 N ATOM 408 CD2 HIS A 54 -8.280 -8.290 37.292 1.00 14.57 C ANISOU 408 CD2 HIS A 54 2264 2008 1262 134 -167 -483 C ATOM 409 CE1 HIS A 54 -8.506 -8.618 35.135 1.00 12.79 C ANISOU 409 CE1 HIS A 54 1955 1675 1229 97 -122 -364 C ATOM 410 NE2 HIS A 54 -9.165 -8.328 36.246 1.00 13.71 N ANISOU 410 NE2 HIS A 54 2120 1844 1244 154 -97 -430 N ATOM 411 N ARG A 55 -7.221 -11.530 38.329 1.00 13.83 N ANISOU 411 N ARG A 55 2077 2146 1031 114 -195 -232 N ATOM 412 CA ARG A 55 -8.358 -12.054 39.106 1.00 14.19 C ANISOU 412 CA ARG A 55 2140 2280 969 172 -114 -191 C ATOM 413 C ARG A 55 -8.524 -13.553 38.899 1.00 13.54 C ANISOU 413 C ARG A 55 2001 2225 918 168 -78 -41 C ATOM 414 O ARG A 55 -8.897 -13.974 37.821 1.00 12.47 O ANISOU 414 O ARG A 55 1823 2014 899 153 -41 5 O ATOM 415 CB ARG A 55 -9.625 -11.314 38.694 1.00 13.97 C ANISOU 415 CB ARG A 55 2126 2206 974 213 -28 -245 C ATOM 416 CG ARG A 55 -10.812 -11.530 39.565 1.00 14.79 C ANISOU 416 CG ARG A 55 2241 2410 967 278 64 -225 C ATOM 417 CD ARG A 55 -11.951 -10.739 38.999 1.00 14.63 C ANISOU 417 CD ARG A 55 2212 2331 1013 322 139 -275 C ATOM 418 NE ARG A 55 -13.210 -11.057 39.628 1.00 15.31 N ANISOU 418 NE ARG A 55 2274 2514 1026 386 249 -229 N ATOM 419 CZ ARG A 55 -14.324 -11.378 38.983 1.00 14.85 C ANISOU 419 CZ ARG A 55 2144 2442 1055 399 323 -155 C ATOM 420 NH1 ARG A 55 -14.363 -11.436 37.652 1.00 13.62 N ANISOU 420 NH1 ARG A 55 1945 2180 1050 355 294 -124 N ATOM 421 NH2 ARG A 55 -15.410 -11.644 39.687 1.00 15.77 N ANISOU 421 NH2 ARG A 55 2226 2664 1102 456 428 -106 N ATOM 422 N ILE A 56 -8.213 -14.349 39.932 1.00 14.36 N ANISOU 422 N ILE A 56 2108 2429 918 180 -99 34 N ATOM 423 CA ILE A 56 -8.316 -15.819 39.866 1.00 14.11 C ANISOU 423 CA ILE A 56 2028 2407 925 176 -74 188 C ATOM 424 C ILE A 56 -9.163 -16.336 41.025 1.00 15.27 C ANISOU 424 C ILE A 56 2190 2675 936 213 -11 271 C ATOM 425 O ILE A 56 -8.814 -16.165 42.204 1.00 16.48 O ANISOU 425 O ILE A 56 2385 2944 930 236 -45 264 O ATOM 426 CB ILE A 56 -6.918 -16.477 39.931 1.00 14.24 C ANISOU 426 CB ILE A 56 2015 2420 973 156 -167 247 C ATOM 427 CG1 ILE A 56 -6.080 -16.079 38.713 1.00 13.27 C ANISOU 427 CG1 ILE A 56 1860 2190 992 123 -208 188 C ATOM 428 CG2 ILE A 56 -7.024 -18.006 40.022 1.00 14.31 C ANISOU 428 CG2 ILE A 56 1985 2426 1024 165 -145 409 C ATOM 429 CD1 ILE A 56 -4.626 -16.392 38.857 1.00 13.66 C ANISOU 429 CD1 ILE A 56 1868 2253 1069 110 -302 220 C ATOM 430 N ILE A 57 -10.283 -16.955 40.697 1.00 15.09 N ANISOU 430 N ILE A 57 2130 2633 970 215 78 353 N ATOM 431 CA ILE A 57 -11.166 -17.523 41.695 1.00 16.35 C ANISOU 431 CA ILE A 57 2282 2906 1021 241 156 461 C ATOM 432 C ILE A 57 -11.193 -19.010 41.460 1.00 16.33 C ANISOU 432 C ILE A 57 2227 2855 1120 207 160 632 C ATOM 433 O ILE A 57 -11.786 -19.451 40.498 1.00 15.57 O ANISOU 433 O ILE A 57 2087 2658 1170 175 191 659 O ATOM 434 CB ILE A 57 -12.599 -16.951 41.590 1.00 16.52 C ANISOU 434 CB ILE A 57 2286 2951 1039 270 268 425 C ATOM 435 CG1 ILE A 57 -12.581 -15.437 41.780 1.00 16.74 C ANISOU 435 CG1 ILE A 57 2374 2997 988 315 264 244 C ATOM 436 CG2 ILE A 57 -13.505 -17.585 42.654 1.00 17.97 C ANISOU 436 CG2 ILE A 57 2446 3271 1110 296 365 557 C ATOM 437 CD1 ILE A 57 -13.933 -14.797 41.647 1.00 17.05 C ANISOU 437 CD1 ILE A 57 2387 3051 1037 362 373 203 C ATOM 438 N PRO A 58 -10.537 -19.793 42.333 1.00 17.46 N ANISOU 438 N PRO A 58 2379 3064 1191 214 119 746 N ATOM 439 CA PRO A 58 -10.554 -21.255 42.203 1.00 17.79 C ANISOU 439 CA PRO A 58 2376 3041 1340 187 120 922 C ATOM 440 C PRO A 58 -11.955 -21.841 42.040 1.00 18.14 C ANISOU 440 C PRO A 58 2372 3066 1452 159 222 1022 C ATOM 441 O PRO A 58 -12.867 -21.442 42.747 1.00 18.86 O ANISOU 441 O PRO A 58 2459 3279 1428 181 307 1040 O ATOM 442 CB PRO A 58 -9.930 -21.716 43.532 1.00 19.29 C ANISOU 442 CB PRO A 58 2590 3360 1379 215 80 1040 C ATOM 443 CG PRO A 58 -9.009 -20.612 43.887 1.00 19.27 C ANISOU 443 CG PRO A 58 2637 3428 1254 239 0 892 C ATOM 444 CD PRO A 58 -9.752 -19.373 43.513 1.00 18.58 C ANISOU 444 CD PRO A 58 2574 3341 1144 246 58 724 C ATOM 445 N GLY A 59 -12.123 -22.747 41.076 1.00 17.78 N ANISOU 445 N GLY A 59 2287 2870 1598 113 212 1076 N ATOM 446 CA GLY A 59 -13.436 -23.379 40.818 1.00 18.25 C ANISOU 446 CA GLY A 59 2287 2891 1754 65 288 1173 C ATOM 447 C GLY A 59 -14.439 -22.520 40.059 1.00 17.57 C ANISOU 447 C GLY A 59 2171 2796 1707 55 337 1060 C ATOM 448 O GLY A 59 -15.574 -22.936 39.820 1.00 17.95 O ANISOU 448 O GLY A 59 2154 2825 1840 12 392 1134 O ATOM 449 N PHE A 60 -14.027 -21.320 39.662 1.00 16.83 N ANISOU 449 N PHE A 60 2116 2710 1565 90 311 891 N ATOM 450 CA PHE A 60 -14.889 -20.419 38.888 1.00 16.30 C ANISOU 450 CA PHE A 60 2025 2626 1542 92 346 786 C ATOM 451 C PHE A 60 -14.173 -20.048 37.579 1.00 15.13 C ANISOU 451 C PHE A 60 1904 2353 1490 76 269 662 C ATOM 452 O PHE A 60 -14.517 -20.588 36.522 1.00 14.66 O ANISOU 452 O PHE A 60 1815 2189 1564 29 249 669 O ATOM 453 CB PHE A 60 -15.271 -19.204 39.756 1.00 16.84 C ANISOU 453 CB PHE A 60 2115 2832 1451 160 409 711 C ATOM 454 CG PHE A 60 -16.068 -18.129 39.050 1.00 16.33 C ANISOU 454 CG PHE A 60 2028 2746 1430 183 442 601 C ATOM 455 CD1 PHE A 60 -16.808 -18.387 37.893 1.00 15.71 C ANISOU 455 CD1 PHE A 60 1886 2576 1506 137 436 616 C ATOM 456 CD2 PHE A 60 -16.114 -16.845 39.590 1.00 16.67 C ANISOU 456 CD2 PHE A 60 2116 2862 1357 256 473 481 C ATOM 457 CE1 PHE A 60 -17.554 -17.386 37.278 1.00 15.40 C ANISOU 457 CE1 PHE A 60 1819 2527 1505 166 460 533 C ATOM 458 CE2 PHE A 60 -16.853 -15.834 38.965 1.00 16.38 C ANISOU 458 CE2 PHE A 60 2057 2794 1373 290 504 390 C ATOM 459 CZ PHE A 60 -17.586 -16.124 37.799 1.00 15.73 C ANISOU 459 CZ PHE A 60 1900 2629 1447 245 497 428 C ATOM 460 N MET A 61 -13.180 -19.154 37.647 1.00 14.86 N ANISOU 460 N MET A 61 1924 2333 1387 110 224 552 N ATOM 461 CA MET A 61 -12.442 -18.737 36.451 1.00 13.89 C ANISOU 461 CA MET A 61 1820 2109 1346 95 164 451 C ATOM 462 C MET A 61 -11.139 -17.947 36.731 1.00 13.50 C ANISOU 462 C MET A 61 1817 2080 1230 118 106 366 C ATOM 463 O MET A 61 -10.915 -17.449 37.849 1.00 14.04 O ANISOU 463 O MET A 61 1916 2244 1174 148 103 349 O ATOM 464 CB MET A 61 -13.356 -17.907 35.519 1.00 13.78 C ANISOU 464 CB MET A 61 1787 2061 1384 92 190 379 C ATOM 465 CG MET A 61 -13.925 -16.644 36.146 1.00 14.50 C ANISOU 465 CG MET A 61 1891 2230 1386 143 236 312 C ATOM 466 SD MET A 61 -12.766 -15.253 36.100 1.00 15.03 S ANISOU 466 SD MET A 61 2027 2276 1406 166 177 169 S ATOM 467 CE MET A 61 -12.923 -14.719 37.802 1.00 15.83 C ANISOU 467 CE MET A 61 2170 2509 1335 226 216 141 C ATOM 468 N CYS A 62 -10.321 -17.854 35.684 1.00 12.49 N ANISOU 468 N CYS A 62 1691 1867 1185 99 59 314 N ATOM 469 CA CYS A 62 -9.090 -17.054 35.613 1.00 12.26 C ANISOU 469 CA CYS A 62 1682 1835 1138 103 1 236 C ATOM 470 C CYS A 62 -9.275 -15.974 34.520 1.00 11.45 C ANISOU 470 C CYS A 62 1587 1673 1088 90 6 144 C ATOM 471 O CYS A 62 -9.528 -16.303 33.337 1.00 10.51 O ANISOU 471 O CYS A 62 1452 1487 1053 72 18 149 O ATOM 472 CB CYS A 62 -7.892 -17.934 35.214 1.00 12.31 C ANISOU 472 CB CYS A 62 1667 1797 1214 96 -43 278 C ATOM 473 SG CYS A 62 -7.511 -19.342 36.303 1.00 13.75 S ANISOU 473 SG CYS A 62 1833 2017 1371 116 -63 414 S ATOM 474 N GLN A 63 -9.163 -14.711 34.949 1.00 11.58 N ANISOU 474 N GLN A 63 1634 1713 1050 101 -7 62 N ATOM 475 CA GLN A 63 -9.415 -13.534 34.148 1.00 11.30 C ANISOU 475 CA GLN A 63 1612 1621 1060 96 -3 -11 C ATOM 476 C GLN A 63 -8.116 -12.749 33.954 1.00 11.43 C ANISOU 476 C GLN A 63 1637 1605 1100 67 -67 -66 C ATOM 477 O GLN A 63 -7.365 -12.518 34.916 1.00 11.95 O ANISOU 477 O GLN A 63 1719 1714 1106 63 -117 -94 O ATOM 478 CB GLN A 63 -10.430 -12.610 34.854 1.00 11.85 C ANISOU 478 CB GLN A 63 1711 1723 1069 138 34 -67 C ATOM 479 CG GLN A 63 -10.802 -11.352 34.062 1.00 11.64 C ANISOU 479 CG GLN A 63 1697 1620 1105 145 38 -133 C ATOM 480 CD GLN A 63 -11.901 -10.541 34.716 1.00 12.46 C ANISOU 480 CD GLN A 63 1821 1746 1165 207 89 -186 C ATOM 481 OE1 GLN A 63 -12.676 -11.070 35.520 1.00 13.05 O ANISOU 481 OE1 GLN A 63 1883 1904 1171 244 145 -153 O ATOM 482 NE2 GLN A 63 -11.979 -9.246 34.381 1.00 12.61 N ANISOU 482 NE2 GLN A 63 1871 1689 1231 225 77 -262 N ATOM 483 N GLY A 64 -7.878 -12.336 32.716 1.00 11.09 N ANISOU 483 N GLY A 64 1580 1493 1140 42 -67 -74 N ATOM 484 CA GLY A 64 -6.734 -11.493 32.385 1.00 11.62 C ANISOU 484 CA GLY A 64 1641 1523 1251 4 -116 -108 C ATOM 485 C GLY A 64 -6.970 -10.689 31.120 1.00 11.56 C ANISOU 485 C GLY A 64 1633 1443 1315 -13 -97 -113 C ATOM 486 O GLY A 64 -8.114 -10.490 30.712 1.00 11.19 O ANISOU 486 O GLY A 64 1601 1376 1273 12 -59 -111 O ATOM 487 N GLY A 65 -5.868 -10.238 30.512 1.00 11.96 N ANISOU 487 N GLY A 65 1657 1464 1423 -57 -123 -104 N ATOM 488 CA GLY A 65 -5.901 -9.492 29.262 1.00 12.08 C ANISOU 488 CA GLY A 65 1667 1420 1501 -79 -104 -83 C ATOM 489 C GLY A 65 -5.979 -7.978 29.356 1.00 12.86 C ANISOU 489 C GLY A 65 1797 1443 1646 -102 -134 -124 C ATOM 490 O GLY A 65 -6.107 -7.316 28.312 1.00 12.75 O ANISOU 490 O GLY A 65 1781 1375 1686 -118 -118 -86 O ATOM 491 N ASN A 66 -5.950 -7.422 30.570 1.00 13.76 N ANISOU 491 N ASN A 66 1945 1545 1735 -99 -178 -201 N ATOM 492 CA ASN A 66 -5.790 -5.966 30.731 1.00 15.20 C ANISOU 492 CA ASN A 66 2163 1630 1980 -129 -222 -258 C ATOM 493 C ASN A 66 -4.311 -5.645 30.558 1.00 16.16 C ANISOU 493 C ASN A 66 2236 1732 2170 -215 -279 -235 C ATOM 494 O ASN A 66 -3.540 -5.728 31.504 1.00 16.67 O ANISOU 494 O ASN A 66 2292 1830 2210 -244 -344 -281 O ATOM 495 CB ASN A 66 -6.313 -5.442 32.087 1.00 16.01 C ANISOU 495 CB ASN A 66 2334 1724 2022 -89 -249 -372 C ATOM 496 CG ASN A 66 -6.254 -3.908 32.190 1.00 17.22 C ANISOU 496 CG ASN A 66 2539 1745 2258 -112 -295 -449 C ATOM 497 OD1 ASN A 66 -5.675 -3.244 31.325 1.00 17.59 O ANISOU 497 OD1 ASN A 66 2562 1706 2416 -173 -317 -400 O ATOM 498 ND2 ASN A 66 -6.852 -3.344 33.252 1.00 17.96 N ANISOU 498 ND2 ASN A 66 2706 1817 2299 -59 -306 -568 N ATOM 499 N PHE A 67 -3.913 -5.298 29.334 1.00 16.84 N ANISOU 499 N PHE A 67 2282 1776 2338 -256 -255 -154 N ATOM 500 CA PHE A 67 -2.490 -5.058 29.038 1.00 17.92 C ANISOU 500 CA PHE A 67 2347 1910 2552 -340 -291 -106 C ATOM 501 C PHE A 67 -2.046 -3.660 29.442 1.00 19.80 C ANISOU 501 C PHE A 67 2605 2032 2886 -414 -370 -155 C ATOM 502 O PHE A 67 -0.902 -3.296 29.186 1.00 20.73 O ANISOU 502 O PHE A 67 2652 2133 3091 -500 -407 -106 O ATOM 503 CB PHE A 67 -2.164 -5.329 27.559 1.00 17.60 C ANISOU 503 CB PHE A 67 2247 1892 2545 -353 -219 10 C ATOM 504 CG PHE A 67 -3.054 -4.618 26.603 1.00 17.49 C ANISOU 504 CG PHE A 67 2276 1811 2556 -338 -180 53 C ATOM 505 CD1 PHE A 67 -2.924 -3.256 26.404 1.00 18.57 C ANISOU 505 CD1 PHE A 67 2428 1830 2796 -392 -214 71 C ATOM 506 CD2 PHE A 67 -4.060 -5.306 25.927 1.00 16.69 C ANISOU 506 CD2 PHE A 67 2201 1757 2383 -270 -120 78 C ATOM 507 CE1 PHE A 67 -3.780 -2.583 25.534 1.00 18.73 C ANISOU 507 CE1 PHE A 67 2487 1784 2845 -369 -184 127 C ATOM 508 CE2 PHE A 67 -4.910 -4.647 25.064 1.00 16.65 C ANISOU 508 CE2 PHE A 67 2229 1700 2395 -252 -98 126 C ATOM 509 CZ PHE A 67 -4.772 -3.292 24.860 1.00 17.66 C ANISOU 509 CZ PHE A 67 2370 1716 2623 -296 -127 157 C ATOM 510 N THR A 68 -2.931 -2.866 30.049 1.00 20.89 N ANISOU 510 N THR A 68 2833 2085 3019 -380 -395 -249 N ATOM 511 CA THR A 68 -2.528 -1.560 30.593 1.00 22.95 C ANISOU 511 CA THR A 68 3132 2214 3371 -446 -484 -328 C ATOM 512 C THR A 68 -2.171 -1.649 32.093 1.00 24.03 C ANISOU 512 C THR A 68 3306 2391 3433 -454 -573 -461 C ATOM 513 O THR A 68 -1.064 -1.257 32.505 1.00 25.62 O ANISOU 513 O THR A 68 3471 2568 3692 -550 -671 -487 O ATOM 514 CB THR A 68 -3.589 -0.461 30.257 1.00 23.85 C ANISOU 514 CB THR A 68 3325 2183 3551 -403 -462 -354 C ATOM 515 OG1 THR A 68 -4.858 -0.764 30.860 1.00 24.23 O ANISOU 515 OG1 THR A 68 3441 2267 3495 -288 -418 -434 O ATOM 516 CG2 THR A 68 -3.790 -0.405 28.758 1.00 23.10 C ANISOU 516 CG2 THR A 68 3186 2071 3517 -407 -391 -201 C ATOM 517 N HIS A 69 -3.066 -2.200 32.910 1.00 23.77 N ANISOU 517 N HIS A 69 3335 2430 3264 -359 -544 -537 N ATOM 518 CA HIS A 69 -2.751 -2.459 34.340 1.00 24.49 C ANISOU 518 CA HIS A 69 3463 2599 3241 -356 -620 -647 C ATOM 519 C HIS A 69 -3.100 -3.863 34.791 1.00 22.82 C ANISOU 519 C HIS A 69 3234 2550 2884 -284 -568 -608 C ATOM 520 O HIS A 69 -3.905 -4.536 34.182 1.00 21.55 O ANISOU 520 O HIS A 69 3059 2425 2702 -221 -470 -535 O ATOM 521 CB HIS A 69 -3.523 -1.527 35.285 1.00 26.09 C ANISOU 521 CB HIS A 69 3789 2725 3396 -305 -646 -812 C ATOM 522 CG HIS A 69 -3.406 -0.082 34.958 1.00 27.81 C ANISOU 522 CG HIS A 69 4051 2750 3766 -358 -697 -870 C ATOM 523 ND1 HIS A 69 -2.358 0.702 35.399 1.00 29.66 N ANISOU 523 ND1 HIS A 69 4293 2900 4076 -469 -828 -945 N ATOM 524 CD2 HIS A 69 -4.231 0.739 34.262 1.00 28.35 C ANISOU 524 CD2 HIS A 69 4158 2680 3934 -316 -641 -861 C ATOM 525 CE1 HIS A 69 -2.533 1.940 34.971 1.00 30.85 C ANISOU 525 CE1 HIS A 69 4490 2855 4376 -497 -847 -980 C ATOM 526 NE2 HIS A 69 -3.661 1.987 34.274 1.00 29.87 N ANISOU 526 NE2 HIS A 69 4386 2696 4268 -400 -733 -924 N ATOM 527 N CYS A 70 -2.525 -4.265 35.912 1.00 23.26 N ANISOU 527 N CYS A 70 3296 2700 2841 -296 -644 -658 N ATOM 528 CA CYS A 70 -2.887 -5.516 36.548 1.00 22.51 C ANISOU 528 CA CYS A 70 3197 2751 2603 -227 -605 -620 C ATOM 529 C CYS A 70 -4.118 -5.302 37.436 1.00 22.24 C ANISOU 529 C CYS A 70 3266 2742 2440 -137 -557 -719 C ATOM 530 O CYS A 70 -4.029 -5.278 38.668 1.00 23.25 O ANISOU 530 O CYS A 70 3452 2947 2434 -121 -613 -805 O ATOM 531 CB CYS A 70 -1.716 -6.090 37.351 1.00 23.86 C ANISOU 531 CB CYS A 70 3320 3026 2718 -273 -709 -604 C ATOM 532 SG CYS A 70 -1.996 -7.833 37.864 1.00 23.95 S ANISOU 532 SG CYS A 70 3301 3201 2596 -194 -655 -496 S ATOM 533 N ASN A 71 -5.258 -5.125 36.775 1.00 20.68 N ANISOU 533 N ASN A 71 3086 2490 2280 -77 -454 -702 N ATOM 534 CA ASN A 71 -6.558 -4.898 37.422 1.00 20.64 C ANISOU 534 CA ASN A 71 3154 2507 2180 21 -381 -777 C ATOM 535 C ASN A 71 -7.673 -5.023 36.367 1.00 19.23 C ANISOU 535 C ASN A 71 2943 2285 2078 73 -272 -697 C ATOM 536 O ASN A 71 -7.395 -5.306 35.196 1.00 17.87 O ANISOU 536 O ASN A 71 2706 2073 2008 30 -262 -596 O ATOM 537 CB ASN A 71 -6.613 -3.540 38.159 1.00 22.07 C ANISOU 537 CB ASN A 71 3436 2600 2348 33 -435 -952 C ATOM 538 CG ASN A 71 -6.550 -2.341 37.222 1.00 22.23 C ANISOU 538 CG ASN A 71 3465 2431 2548 -3 -455 -976 C ATOM 539 OD1 ASN A 71 -6.935 -2.422 36.065 1.00 20.94 O ANISOU 539 OD1 ASN A 71 3248 2217 2490 0 -394 -869 O ATOM 540 ND2 ASN A 71 -6.080 -1.208 37.739 1.00 23.66 N ANISOU 540 ND2 ASN A 71 3720 2503 2764 -41 -546 -1117 N ATOM 541 N GLY A 72 -8.917 -4.794 36.788 1.00 19.42 N ANISOU 541 N GLY A 72 3006 2324 2046 167 -194 -745 N ATOM 542 CA GLY A 72 -10.083 -5.071 35.954 1.00 18.43 C ANISOU 542 CA GLY A 72 2834 2191 1976 221 -98 -661 C ATOM 543 C GLY A 72 -10.585 -3.882 35.166 1.00 18.67 C ANISOU 543 C GLY A 72 2880 2077 2136 246 -88 -690 C ATOM 544 O GLY A 72 -11.647 -3.956 34.560 1.00 18.13 O ANISOU 544 O GLY A 72 2774 2004 2110 301 -19 -630 O ATOM 545 N THR A 73 -9.821 -2.790 35.180 1.00 19.39 N ANISOU 545 N THR A 73 3022 2046 2298 200 -165 -772 N ATOM 546 CA THR A 73 -10.185 -1.564 34.505 1.00 20.04 C ANISOU 546 CA THR A 73 3129 1966 2518 220 -167 -794 C ATOM 547 C THR A 73 -9.119 -1.249 33.447 1.00 19.59 C ANISOU 547 C THR A 73 3038 1817 2588 107 -235 -714 C ATOM 548 O THR A 73 -8.050 -0.716 33.761 1.00 20.27 O ANISOU 548 O THR A 73 3151 1840 2711 27 -321 -771 O ATOM 549 CB THR A 73 -10.288 -0.393 35.521 1.00 21.95 C ANISOU 549 CB THR A 73 3475 2113 2750 269 -196 -975 C ATOM 550 OG1 THR A 73 -11.206 -0.736 36.563 1.00 22.63 O ANISOU 550 OG1 THR A 73 3590 2314 2692 379 -118 -1049 O ATOM 551 CG2 THR A 73 -10.771 0.859 34.833 1.00 22.74 C ANISOU 551 CG2 THR A 73 3601 2025 3012 305 -193 -989 C ATOM 552 N GLY A 74 -9.390 -1.607 32.199 1.00 18.63 N ANISOU 552 N GLY A 74 2851 1698 2527 96 -196 -577 N ATOM 553 CA GLY A 74 -8.438 -1.306 31.115 1.00 18.32 C ANISOU 553 CA GLY A 74 2774 1591 2594 0 -239 -483 C ATOM 554 C GLY A 74 -8.411 -2.297 29.974 1.00 16.93 C ANISOU 554 C GLY A 74 2525 1503 2404 -21 -197 -343 C ATOM 555 O GLY A 74 -9.085 -3.330 30.006 1.00 16.09 O ANISOU 555 O GLY A 74 2393 1505 2214 25 -147 -316 O ATOM 556 N GLY A 75 -7.593 -1.974 28.969 1.00 16.79 N ANISOU 556 N GLY A 75 2472 1437 2468 -98 -217 -254 N ATOM 557 CA GLY A 75 -7.539 -2.739 27.732 1.00 15.54 C ANISOU 557 CA GLY A 75 2258 1352 2293 -114 -175 -130 C ATOM 558 C GLY A 75 -8.451 -2.175 26.669 1.00 15.45 C ANISOU 558 C GLY A 75 2251 1287 2331 -77 -149 -49 C ATOM 559 O GLY A 75 -9.437 -1.508 26.960 1.00 16.16 O ANISOU 559 O GLY A 75 2375 1308 2454 -10 -147 -87 O ATOM 560 N LYS A 76 -8.102 -2.430 25.418 1.00 14.78 N ANISOU 560 N LYS A 76 2129 1238 2246 -115 -130 64 N ATOM 561 CA LYS A 76 -8.939 -2.070 24.298 1.00 14.61 C ANISOU 561 CA LYS A 76 2107 1199 2243 -82 -113 160 C ATOM 562 C LYS A 76 -8.916 -3.184 23.286 1.00 13.41 C ANISOU 562 C LYS A 76 1922 1175 1997 -89 -79 231 C ATOM 563 O LYS A 76 -8.002 -4.005 23.287 1.00 12.82 O ANISOU 563 O LYS A 76 1822 1174 1875 -128 -62 223 O ATOM 564 CB LYS A 76 -8.467 -0.757 23.661 1.00 15.83 C ANISOU 564 CB LYS A 76 2270 1229 2513 -129 -137 243 C ATOM 565 CG LYS A 76 -7.178 -0.814 22.897 1.00 16.12 C ANISOU 565 CG LYS A 76 2267 1298 2559 -221 -124 335 C ATOM 566 CD LYS A 76 -6.892 0.580 22.251 1.00 17.61 C ANISOU 566 CD LYS A 76 2462 1350 2878 -269 -145 444 C ATOM 567 CE LYS A 76 -7.489 0.750 20.855 1.00 17.88 C ANISOU 567 CE LYS A 76 2492 1416 2882 -244 -119 595 C ATOM 568 NZ LYS A 76 -7.295 2.172 20.360 1.00 19.60 N ANISOU 568 NZ LYS A 76 2722 1480 3244 -286 -145 714 N ATOM 569 N SER A 77 -9.908 -3.208 22.407 1.00 13.05 N ANISOU 569 N SER A 77 1876 1155 1926 -49 -75 297 N ATOM 570 CA SER A 77 -9.912 -4.198 21.330 1.00 12.42 C ANISOU 570 CA SER A 77 1780 1191 1747 -59 -54 352 C ATOM 571 C SER A 77 -9.135 -3.618 20.187 1.00 13.00 C ANISOU 571 C SER A 77 1849 1262 1826 -106 -41 466 C ATOM 572 O SER A 77 -8.746 -2.432 20.233 1.00 13.70 O ANISOU 572 O SER A 77 1943 1248 2015 -135 -55 515 O ATOM 573 CB SER A 77 -11.326 -4.525 20.872 1.00 12.28 C ANISOU 573 CB SER A 77 1760 1216 1689 -4 -72 372 C ATOM 574 OG SER A 77 -11.855 -3.513 20.040 1.00 13.18 O ANISOU 574 OG SER A 77 1877 1284 1843 13 -97 473 O ATOM 575 N ILE A 78 -8.938 -4.436 19.155 1.00 12.75 N ANISOU 575 N ILE A 78 1813 1342 1689 -115 -13 508 N ATOM 576 CA ILE A 78 -8.319 -3.961 17.911 1.00 13.66 C ANISOU 576 CA ILE A 78 1925 1491 1774 -150 13 633 C ATOM 577 C ILE A 78 -9.289 -3.086 17.098 1.00 14.70 C ANISOU 577 C ILE A 78 2076 1593 1914 -124 -24 742 C ATOM 578 O ILE A 78 -8.897 -2.503 16.107 1.00 15.55 O ANISOU 578 O ILE A 78 2185 1718 2003 -152 -6 870 O ATOM 579 CB ILE A 78 -7.784 -5.114 17.011 1.00 13.43 C ANISOU 579 CB ILE A 78 1894 1602 1606 -153 64 633 C ATOM 580 CG1 ILE A 78 -8.920 -6.010 16.497 1.00 13.04 C ANISOU 580 CG1 ILE A 78 1876 1629 1449 -109 33 593 C ATOM 581 CG2 ILE A 78 -6.751 -5.956 17.749 1.00 12.70 C ANISOU 581 CG2 ILE A 78 1770 1533 1521 -168 103 546 C ATOM 582 CD1 ILE A 78 -8.434 -7.123 15.551 1.00 13.24 C ANISOU 582 CD1 ILE A 78 1920 1779 1331 -105 78 570 C ATOM 583 N TYR A 79 -10.548 -3.009 17.518 1.00 14.78 N ANISOU 583 N TYR A 79 2094 1567 1953 -69 -72 703 N ATOM 584 CA TYR A 79 -11.550 -2.258 16.783 1.00 16.02 C ANISOU 584 CA TYR A 79 2257 1703 2126 -31 -117 809 C ATOM 585 C TYR A 79 -11.791 -0.868 17.374 1.00 17.02 C ANISOU 585 C TYR A 79 2387 1663 2417 -8 -141 841 C ATOM 586 O TYR A 79 -12.459 -0.063 16.765 1.00 18.08 O ANISOU 586 O TYR A 79 2523 1753 2594 25 -177 952 O ATOM 587 CB TYR A 79 -12.857 -3.041 16.771 1.00 15.62 C ANISOU 587 CB TYR A 79 2193 1723 2016 21 -159 760 C ATOM 588 CG TYR A 79 -12.676 -4.473 16.318 1.00 15.01 C ANISOU 588 CG TYR A 79 2124 1780 1796 -2 -147 699 C ATOM 589 CD1 TYR A 79 -12.280 -4.756 15.016 1.00 15.66 C ANISOU 589 CD1 TYR A 79 2232 1965 1750 -26 -139 768 C ATOM 590 CD2 TYR A 79 -12.887 -5.536 17.188 1.00 13.99 C ANISOU 590 CD2 TYR A 79 1984 1672 1660 3 -140 574 C ATOM 591 CE1 TYR A 79 -12.096 -6.050 14.593 1.00 15.39 C ANISOU 591 CE1 TYR A 79 2218 2038 1589 -39 -127 692 C ATOM 592 CE2 TYR A 79 -12.723 -6.844 16.766 1.00 13.64 C ANISOU 592 CE2 TYR A 79 1954 1722 1506 -16 -133 515 C ATOM 593 CZ TYR A 79 -12.309 -7.088 15.466 1.00 14.38 C ANISOU 593 CZ TYR A 79 2080 1904 1478 -34 -127 564 C ATOM 594 OH TYR A 79 -12.122 -8.364 15.023 1.00 14.37 O ANISOU 594 OH TYR A 79 2106 1984 1370 -45 -120 486 O ATOM 595 N GLY A 80 -11.232 -0.605 18.555 1.00 17.06 N ANISOU 595 N GLY A 80 2397 1572 2513 -25 -127 741 N ATOM 596 CA GLY A 80 -11.541 0.579 19.348 1.00 18.00 C ANISOU 596 CA GLY A 80 2532 1521 2785 7 -152 715 C ATOM 597 C GLY A 80 -11.664 0.154 20.794 1.00 17.56 C ANISOU 597 C GLY A 80 2483 1449 2739 36 -144 543 C ATOM 598 O GLY A 80 -11.439 -1.028 21.130 1.00 16.32 O ANISOU 598 O GLY A 80 2311 1406 2482 20 -121 469 O ATOM 599 N GLU A 81 -12.064 1.093 21.648 1.00 18.70 N ANISOU 599 N GLU A 81 2653 1453 2999 84 -160 480 N ATOM 600 CA GLU A 81 -12.076 0.861 23.093 1.00 18.74 C ANISOU 600 CA GLU A 81 2677 1441 3002 111 -150 313 C ATOM 601 C GLU A 81 -13.015 -0.308 23.452 1.00 17.68 C ANISOU 601 C GLU A 81 2509 1445 2762 170 -122 260 C ATOM 602 O GLU A 81 -12.667 -1.178 24.274 1.00 16.76 O ANISOU 602 O GLU A 81 2391 1404 2571 152 -102 167 O ATOM 603 CB GLU A 81 -12.451 2.152 23.865 1.00 20.60 C ANISOU 603 CB GLU A 81 2957 1496 3373 171 -168 244 C ATOM 604 CG GLU A 81 -11.519 2.474 25.075 1.00 21.44 C ANISOU 604 CG GLU A 81 3113 1523 3510 124 -186 99 C ATOM 605 CD GLU A 81 -10.053 2.875 24.699 1.00 22.35 C ANISOU 605 CD GLU A 81 3229 1577 3684 -6 -222 154 C ATOM 606 OE1 GLU A 81 -9.092 2.463 25.404 1.00 22.47 O ANISOU 606 OE1 GLU A 81 3245 1631 3661 -74 -237 71 O ATOM 607 OE2 GLU A 81 -9.846 3.651 23.730 1.00 23.85 O ANISOU 607 OE2 GLU A 81 3414 1678 3969 -43 -237 290 O ATOM 608 N LYS A 82 -14.195 -0.344 22.839 1.00 17.59 N ANISOU 608 N LYS A 82 2463 1469 2750 235 -126 330 N ATOM 609 CA LYS A 82 -15.115 -1.432 23.106 1.00 16.84 C ANISOU 609 CA LYS A 82 2321 1499 2575 275 -107 297 C ATOM 610 C LYS A 82 -15.737 -1.919 21.814 1.00 16.52 C ANISOU 610 C LYS A 82 2240 1550 2486 268 -138 412 C ATOM 611 O LYS A 82 -15.780 -1.198 20.824 1.00 17.25 O ANISOU 611 O LYS A 82 2336 1603 2613 268 -171 522 O ATOM 612 CB LYS A 82 -16.182 -1.046 24.153 1.00 17.64 C ANISOU 612 CB LYS A 82 2406 1564 2730 380 -79 220 C ATOM 613 CG LYS A 82 -16.576 0.404 24.175 1.00 19.29 C ANISOU 613 CG LYS A 82 2636 1620 3072 455 -90 235 C ATOM 614 CD LYS A 82 -17.573 0.729 25.299 1.00 20.20 C ANISOU 614 CD LYS A 82 2737 1710 3228 575 -41 137 C ATOM 615 CE LYS A 82 -18.147 2.126 25.140 1.00 21.94 C ANISOU 615 CE LYS A 82 2967 1770 3596 673 -52 164 C ATOM 616 NZ LYS A 82 -19.648 2.143 25.284 1.00 22.71 N ANISOU 616 NZ LYS A 82 2980 1915 3734 804 -17 186 N ATOM 617 N PHE A 83 -16.168 -3.166 21.803 1.00 15.44 N ANISOU 617 N PHE A 83 2066 1534 2263 255 -134 389 N ATOM 618 CA PHE A 83 -17.011 -3.620 20.716 1.00 15.60 C ANISOU 618 CA PHE A 83 2043 1640 2242 256 -180 476 C ATOM 619 C PHE A 83 -18.197 -4.436 21.188 1.00 15.51 C ANISOU 619 C PHE A 83 1962 1704 2225 289 -180 446 C ATOM 620 O PHE A 83 -18.300 -4.837 22.345 1.00 14.85 O ANISOU 620 O PHE A 83 1866 1626 2148 307 -131 363 O ATOM 621 CB PHE A 83 -16.211 -4.316 19.608 1.00 15.02 C ANISOU 621 CB PHE A 83 2002 1643 2060 177 -199 515 C ATOM 622 CG PHE A 83 -15.581 -5.607 20.007 1.00 13.89 C ANISOU 622 CG PHE A 83 1873 1563 1841 126 -169 427 C ATOM 623 CD1 PHE A 83 -14.492 -5.628 20.841 1.00 13.21 C ANISOU 623 CD1 PHE A 83 1816 1436 1765 102 -124 360 C ATOM 624 CD2 PHE A 83 -16.052 -6.807 19.491 1.00 13.54 C ANISOU 624 CD2 PHE A 83 1811 1613 1719 100 -198 416 C ATOM 625 CE1 PHE A 83 -13.907 -6.805 21.164 1.00 12.44 C ANISOU 625 CE1 PHE A 83 1726 1393 1607 66 -101 297 C ATOM 626 CE2 PHE A 83 -15.483 -7.977 19.818 1.00 12.76 C ANISOU 626 CE2 PHE A 83 1728 1550 1568 61 -173 343 C ATOM 627 CZ PHE A 83 -14.415 -8.001 20.652 1.00 12.23 C ANISOU 627 CZ PHE A 83 1685 1445 1515 49 -122 289 C ATOM 628 N GLU A 84 -19.110 -4.632 20.249 1.00 16.33 N ANISOU 628 N GLU A 84 2015 1872 2317 295 -240 527 N ATOM 629 CA GLU A 84 -20.392 -5.238 20.504 1.00 16.83 C ANISOU 629 CA GLU A 84 1986 2004 2402 322 -257 531 C ATOM 630 C GLU A 84 -20.220 -6.711 20.823 1.00 15.50 C ANISOU 630 C GLU A 84 1815 1910 2164 251 -246 464 C ATOM 631 O GLU A 84 -19.179 -7.323 20.547 1.00 14.62 O ANISOU 631 O GLU A 84 1772 1807 1973 186 -242 425 O ATOM 632 CB GLU A 84 -21.306 -5.108 19.279 1.00 18.38 C ANISOU 632 CB GLU A 84 2127 2258 2598 328 -350 642 C ATOM 633 CG GLU A 84 -21.495 -3.661 18.824 1.00 20.06 C ANISOU 633 CG GLU A 84 2341 2392 2888 402 -372 738 C ATOM 634 CD GLU A 84 -20.436 -3.154 17.784 1.00 20.67 C ANISOU 634 CD GLU A 84 2510 2442 2901 355 -398 802 C ATOM 635 OE1 GLU A 84 -19.269 -3.676 17.717 1.00 20.16 O ANISOU 635 OE1 GLU A 84 2518 2389 2749 281 -364 747 O ATOM 636 OE2 GLU A 84 -20.797 -2.206 17.038 1.00 22.14 O ANISOU 636 OE2 GLU A 84 2684 2597 3130 398 -447 924 O ATOM 637 N ASP A 85 -21.267 -7.241 21.433 1.00 15.29 N ANISOU 637 N ASP A 85 1701 1930 2179 270 -237 460 N ATOM 638 CA ASP A 85 -21.411 -8.645 21.682 1.00 14.54 C ANISOU 638 CA ASP A 85 1582 1895 2047 202 -240 425 C ATOM 639 C ASP A 85 -21.806 -9.249 20.330 1.00 14.68 C ANISOU 639 C ASP A 85 1585 1970 2020 138 -347 469 C ATOM 640 O ASP A 85 -22.871 -8.941 19.784 1.00 15.63 O ANISOU 640 O ASP A 85 1624 2130 2182 158 -412 541 O ATOM 641 CB ASP A 85 -22.480 -8.839 22.769 1.00 15.03 C ANISOU 641 CB ASP A 85 1538 1989 2181 246 -188 432 C ATOM 642 CG ASP A 85 -21.988 -8.405 24.160 1.00 14.66 C ANISOU 642 CG ASP A 85 1528 1904 2138 304 -82 366 C ATOM 643 OD1 ASP A 85 -20.813 -8.629 24.473 1.00 13.78 O ANISOU 643 OD1 ASP A 85 1507 1760 1967 269 -59 305 O ATOM 644 OD2 ASP A 85 -22.762 -7.848 24.952 1.00 15.36 O ANISOU 644 OD2 ASP A 85 1552 2000 2283 389 -22 371 O ATOM 645 N GLU A 86 -20.918 -10.043 19.751 1.00 13.76 N ANISOU 645 N GLU A 86 1551 1862 1814 67 -368 422 N ATOM 646 CA GLU A 86 -21.121 -10.541 18.398 1.00 14.16 C ANISOU 646 CA GLU A 86 1620 1968 1791 12 -469 439 C ATOM 647 C GLU A 86 -22.351 -11.438 18.319 1.00 14.77 C ANISOU 647 C GLU A 86 1605 2096 1911 -35 -545 450 C ATOM 648 O GLU A 86 -23.253 -11.201 17.533 1.00 15.81 O ANISOU 648 O GLU A 86 1677 2279 2048 -39 -640 513 O ATOM 649 CB GLU A 86 -19.888 -11.318 17.969 1.00 13.53 C ANISOU 649 CB GLU A 86 1648 1881 1609 -39 -452 363 C ATOM 650 CG GLU A 86 -19.843 -11.680 16.517 1.00 14.24 C ANISOU 650 CG GLU A 86 1790 2031 1587 -81 -539 362 C ATOM 651 CD GLU A 86 -18.452 -12.101 16.092 1.00 13.77 C ANISOU 651 CD GLU A 86 1838 1966 1426 -98 -488 295 C ATOM 652 OE1 GLU A 86 -17.571 -12.294 16.983 1.00 12.74 O ANISOU 652 OE1 GLU A 86 1729 1782 1329 -88 -400 250 O ATOM 653 OE2 GLU A 86 -18.238 -12.200 14.862 1.00 14.47 O ANISOU 653 OE2 GLU A 86 1985 2114 1395 -115 -536 294 O ATOM 654 N ASN A 87 -22.365 -12.463 19.161 1.00 14.20 N ANISOU 654 N ASN A 87 1513 2006 1874 -76 -507 400 N ATOM 655 CA ASN A 87 -23.504 -13.356 19.328 1.00 14.91 C ANISOU 655 CA ASN A 87 1500 2128 2035 -133 -563 420 C ATOM 656 C ASN A 87 -23.274 -14.145 20.619 1.00 14.26 C ANISOU 656 C ASN A 87 1405 2008 2002 -150 -472 390 C ATOM 657 O ASN A 87 -22.173 -14.107 21.190 1.00 13.14 O ANISOU 657 O ASN A 87 1348 1823 1819 -124 -390 341 O ATOM 658 CB ASN A 87 -23.720 -14.279 18.107 1.00 15.65 C ANISOU 658 CB ASN A 87 1625 2249 2072 -226 -695 386 C ATOM 659 CG ASN A 87 -22.564 -15.244 17.869 1.00 15.07 C ANISOU 659 CG ASN A 87 1682 2127 1917 -273 -678 280 C ATOM 660 OD1 ASN A 87 -22.214 -16.032 18.755 1.00 14.50 O ANISOU 660 OD1 ASN A 87 1617 2000 1890 -294 -616 244 O ATOM 661 ND2 ASN A 87 -21.958 -15.189 16.670 1.00 15.24 N ANISOU 661 ND2 ASN A 87 1804 2171 1813 -281 -729 236 N ATOM 662 N PHE A 88 -24.324 -14.826 21.073 1.00 15.00 N ANISOU 662 N PHE A 88 1385 2127 2186 -195 -490 433 N ATOM 663 CA PHE A 88 -24.251 -15.710 22.220 1.00 14.79 C ANISOU 663 CA PHE A 88 1336 2075 2207 -225 -416 431 C ATOM 664 C PHE A 88 -24.583 -17.146 21.808 1.00 15.52 C ANISOU 664 C PHE A 88 1417 2139 2340 -346 -504 416 C ATOM 665 O PHE A 88 -25.240 -17.860 22.564 1.00 16.11 O ANISOU 665 O PHE A 88 1399 2214 2505 -394 -481 471 O ATOM 666 CB PHE A 88 -25.198 -15.247 23.341 1.00 15.27 C ANISOU 666 CB PHE A 88 1262 2188 2350 -168 -329 512 C ATOM 667 CG PHE A 88 -24.970 -13.835 23.767 1.00 14.90 C ANISOU 667 CG PHE A 88 1232 2151 2278 -44 -249 510 C ATOM 668 CD1 PHE A 88 -23.815 -13.500 24.510 1.00 13.87 C ANISOU 668 CD1 PHE A 88 1210 1980 2080 4 -161 449 C ATOM 669 CD2 PHE A 88 -25.876 -12.836 23.420 1.00 15.69 C ANISOU 669 CD2 PHE A 88 1240 2292 2429 22 -270 567 C ATOM 670 CE1 PHE A 88 -23.561 -12.188 24.885 1.00 13.70 C ANISOU 670 CE1 PHE A 88 1215 1946 2043 107 -100 431 C ATOM 671 CE2 PHE A 88 -25.647 -11.517 23.797 1.00 15.61 C ANISOU 671 CE2 PHE A 88 1256 2262 2411 140 -200 556 C ATOM 672 CZ PHE A 88 -24.464 -11.181 24.531 1.00 14.59 C ANISOU 672 CZ PHE A 88 1249 2080 2214 178 -116 480 C ATOM 673 N ILE A 89 -24.096 -17.588 20.647 1.00 15.62 N ANISOU 673 N ILE A 89 1528 2122 2285 -396 -600 340 N ATOM 674 CA ILE A 89 -24.380 -18.968 20.177 1.00 16.51 C ANISOU 674 CA ILE A 89 1650 2184 2439 -513 -698 298 C ATOM 675 C ILE A 89 -23.785 -20.034 21.117 1.00 16.10 C ANISOU 675 C ILE A 89 1636 2046 2434 -544 -627 281 C ATOM 676 O ILE A 89 -24.464 -20.970 21.512 1.00 16.90 O ANISOU 676 O ILE A 89 1665 2112 2645 -628 -656 323 O ATOM 677 CB ILE A 89 -23.883 -19.219 18.723 1.00 16.87 C ANISOU 677 CB ILE A 89 1817 2218 2374 -545 -806 195 C ATOM 678 CG1 ILE A 89 -24.663 -18.366 17.722 1.00 17.74 C ANISOU 678 CG1 ILE A 89 1878 2421 2442 -537 -909 234 C ATOM 679 CG2 ILE A 89 -24.049 -20.694 18.345 1.00 17.88 C ANISOU 679 CG2 ILE A 89 1980 2266 2548 -659 -902 122 C ATOM 680 CD1 ILE A 89 -23.945 -18.241 16.345 1.00 18.02 C ANISOU 680 CD1 ILE A 89 2053 2479 2314 -530 -977 146 C ATOM 681 N LEU A 90 -22.520 -19.874 21.481 1.00 14.96 N ANISOU 681 N LEU A 90 1597 1868 2218 -478 -538 233 N ATOM 682 CA LEU A 90 -21.826 -20.879 22.301 1.00 14.73 C ANISOU 682 CA LEU A 90 1614 1757 2226 -496 -480 222 C ATOM 683 C LEU A 90 -22.007 -20.622 23.802 1.00 14.44 C ANISOU 683 C LEU A 90 1500 1755 2232 -455 -367 319 C ATOM 684 O LEU A 90 -22.151 -19.489 24.236 1.00 13.86 O ANISOU 684 O LEU A 90 1386 1755 2122 -379 -305 353 O ATOM 685 CB LEU A 90 -20.347 -20.934 21.931 1.00 13.86 C ANISOU 685 CB LEU A 90 1642 1601 2021 -445 -449 127 C ATOM 686 CG LEU A 90 -20.057 -21.111 20.436 1.00 14.30 C ANISOU 686 CG LEU A 90 1788 1645 1999 -465 -537 23 C ATOM 687 CD1 LEU A 90 -18.566 -20.815 20.176 1.00 13.41 C ANISOU 687 CD1 LEU A 90 1783 1524 1785 -389 -469 -43 C ATOM 688 CD2 LEU A 90 -20.460 -22.494 19.956 1.00 15.48 C ANISOU 688 CD2 LEU A 90 1961 1704 2215 -560 -633 -33 C ATOM 689 N LYS A 91 -22.035 -21.699 24.578 1.00 15.13 N ANISOU 689 N LYS A 91 1569 1785 2394 -505 -344 364 N ATOM 690 CA LYS A 91 -22.350 -21.630 25.992 1.00 15.29 C ANISOU 690 CA LYS A 91 1510 1854 2445 -479 -241 471 C ATOM 691 C LYS A 91 -21.120 -21.937 26.829 1.00 14.33 C ANISOU 691 C LYS A 91 1476 1695 2272 -432 -168 462 C ATOM 692 O LYS A 91 -20.112 -22.443 26.344 1.00 13.91 O ANISOU 692 O LYS A 91 1526 1562 2198 -431 -199 386 O ATOM 693 CB LYS A 91 -23.438 -22.628 26.345 1.00 16.99 C ANISOU 693 CB LYS A 91 1614 2048 2792 -581 -265 572 C ATOM 694 CG LYS A 91 -24.773 -22.533 25.570 1.00 18.38 C ANISOU 694 CG LYS A 91 1673 2261 3048 -652 -357 600 C ATOM 695 CD LYS A 91 -25.195 -21.106 25.360 1.00 18.21 C ANISOU 695 CD LYS A 91 1599 2352 2967 -564 -334 600 C ATOM 696 CE LYS A 91 -26.704 -20.928 25.035 1.00 19.70 C ANISOU 696 CE LYS A 91 1617 2612 3256 -613 -392 682 C ATOM 697 NZ LYS A 91 -26.943 -19.402 24.985 1.00 19.52 N ANISOU 697 NZ LYS A 91 1556 2687 3171 -490 -345 684 N ATOM 698 N HIS A 92 -21.239 -21.627 28.104 1.00 14.12 N ANISOU 698 N HIS A 92 1401 1739 2224 -386 -71 543 N ATOM 699 CA HIS A 92 -20.212 -21.896 29.095 1.00 13.60 C ANISOU 699 CA HIS A 92 1398 1664 2104 -342 -7 560 C ATOM 700 C HIS A 92 -20.402 -23.341 29.603 1.00 14.67 C ANISOU 700 C HIS A 92 1510 1728 2337 -419 -13 656 C ATOM 701 O HIS A 92 -20.890 -23.572 30.714 1.00 15.42 O ANISOU 701 O HIS A 92 1536 1880 2441 -424 56 776 O ATOM 702 CB HIS A 92 -20.314 -20.870 30.224 1.00 13.26 C ANISOU 702 CB HIS A 92 1323 1739 1973 -258 91 595 C ATOM 703 CG HIS A 92 -20.011 -19.455 29.803 1.00 12.32 C ANISOU 703 CG HIS A 92 1241 1660 1779 -183 95 502 C ATOM 704 ND1 HIS A 92 -20.929 -18.650 29.165 1.00 12.42 N ANISOU 704 ND1 HIS A 92 1192 1708 1817 -170 77 491 N ATOM 705 CD2 HIS A 92 -18.903 -18.689 29.972 1.00 11.36 C ANISOU 705 CD2 HIS A 92 1204 1543 1570 -118 111 428 C ATOM 706 CE1 HIS A 92 -20.401 -17.458 28.953 1.00 11.60 C ANISOU 706 CE1 HIS A 92 1142 1617 1648 -99 86 418 C ATOM 707 NE2 HIS A 92 -19.174 -17.457 29.432 1.00 11.00 N ANISOU 707 NE2 HIS A 92 1152 1521 1505 -74 105 376 N ATOM 708 N THR A 93 -19.999 -24.309 28.773 1.00 14.93 N ANISOU 708 N THR A 93 1603 1629 2438 -475 -94 602 N ATOM 709 CA THR A 93 -20.335 -25.723 28.982 1.00 16.10 C ANISOU 709 CA THR A 93 1729 1668 2718 -566 -127 683 C ATOM 710 C THR A 93 -19.519 -26.417 30.046 1.00 16.20 C ANISOU 710 C THR A 93 1780 1644 2731 -537 -74 766 C ATOM 711 O THR A 93 -19.933 -27.451 30.548 1.00 17.35 O ANISOU 711 O THR A 93 1885 1721 2984 -606 -76 882 O ATOM 712 CB THR A 93 -20.137 -26.513 27.686 1.00 16.59 C ANISOU 712 CB THR A 93 1864 1586 2853 -625 -238 570 C ATOM 713 OG1 THR A 93 -18.798 -26.318 27.223 1.00 15.73 O ANISOU 713 OG1 THR A 93 1872 1445 2660 -544 -236 454 O ATOM 714 CG2 THR A 93 -21.095 -26.029 26.600 1.00 16.84 C ANISOU 714 CG2 THR A 93 1849 1654 2893 -676 -316 508 C ATOM 715 N GLY A 94 -18.348 -25.865 30.377 1.00 15.12 N ANISOU 715 N GLY A 94 1715 1548 2481 -440 -35 716 N ATOM 716 CA GLY A 94 -17.407 -26.548 31.274 1.00 15.29 C ANISOU 716 CA GLY A 94 1779 1532 2499 -405 -7 787 C ATOM 717 C GLY A 94 -16.017 -25.917 31.323 1.00 14.11 C ANISOU 717 C GLY A 94 1704 1416 2239 -307 5 703 C ATOM 718 O GLY A 94 -15.822 -24.839 30.778 1.00 13.05 O ANISOU 718 O GLY A 94 1587 1344 2024 -268 6 600 O ATOM 719 N PRO A 95 -15.062 -26.574 32.027 1.00 14.36 N ANISOU 719 N PRO A 95 1769 1410 2274 -269 12 764 N ATOM 720 CA PRO A 95 -13.676 -26.131 32.115 1.00 13.57 C ANISOU 720 CA PRO A 95 1722 1337 2094 -184 13 701 C ATOM 721 C PRO A 95 -13.040 -25.930 30.743 1.00 12.87 C ANISOU 721 C PRO A 95 1686 1182 2021 -164 -23 548 C ATOM 722 O PRO A 95 -13.247 -26.749 29.844 1.00 13.30 O ANISOU 722 O PRO A 95 1767 1113 2173 -201 -63 501 O ATOM 723 CB PRO A 95 -12.965 -27.278 32.846 1.00 14.54 C ANISOU 723 CB PRO A 95 1860 1386 2279 -165 5 810 C ATOM 724 CG PRO A 95 -14.031 -27.996 33.627 1.00 15.78 C ANISOU 724 CG PRO A 95 1965 1535 2494 -231 26 968 C ATOM 725 CD PRO A 95 -15.317 -27.789 32.829 1.00 15.75 C ANISOU 725 CD PRO A 95 1921 1518 2543 -310 18 920 C ATOM 726 N GLY A 96 -12.265 -24.857 30.602 1.00 11.84 N ANISOU 726 N GLY A 96 1572 1133 1792 -108 -10 473 N ATOM 727 CA GLY A 96 -11.540 -24.587 29.378 1.00 11.32 C ANISOU 727 CA GLY A 96 1548 1029 1721 -81 -27 348 C ATOM 728 C GLY A 96 -12.206 -23.543 28.506 1.00 10.68 C ANISOU 728 C GLY A 96 1465 1003 1588 -104 -32 271 C ATOM 729 O GLY A 96 -11.556 -22.935 27.676 1.00 10.16 O ANISOU 729 O GLY A 96 1428 953 1480 -75 -32 188 O ATOM 730 N ILE A 97 -13.501 -23.303 28.690 1.00 10.88 N ANISOU 730 N ILE A 97 1449 1064 1620 -153 -32 311 N ATOM 731 CA ILE A 97 -14.196 -22.277 27.909 1.00 10.42 C ANISOU 731 CA ILE A 97 1378 1059 1521 -166 -43 255 C ATOM 732 C ILE A 97 -13.475 -20.931 28.013 1.00 9.57 C ANISOU 732 C ILE A 97 1283 1029 1323 -110 -14 215 C ATOM 733 O ILE A 97 -13.127 -20.477 29.095 1.00 9.30 O ANISOU 733 O ILE A 97 1236 1050 1243 -77 17 251 O ATOM 734 CB ILE A 97 -15.673 -22.151 28.334 1.00 10.97 C ANISOU 734 CB ILE A 97 1374 1173 1619 -211 -36 326 C ATOM 735 CG1 ILE A 97 -16.404 -23.444 27.986 1.00 12.02 C ANISOU 735 CG1 ILE A 97 1490 1214 1863 -289 -83 358 C ATOM 736 CG2 ILE A 97 -16.341 -20.949 27.686 1.00 10.58 C ANISOU 736 CG2 ILE A 97 1300 1187 1529 -203 -44 285 C ATOM 737 CD1 ILE A 97 -16.325 -23.834 26.528 1.00 12.25 C ANISOU 737 CD1 ILE A 97 1572 1163 1918 -320 -155 253 C ATOM 738 N LEU A 98 -13.229 -20.323 26.853 1.00 9.23 N ANISOU 738 N LEU A 98 1269 986 1252 -104 -33 141 N ATOM 739 CA LEU A 98 -12.633 -18.999 26.770 1.00 8.66 C ANISOU 739 CA LEU A 98 1205 968 1116 -67 -14 110 C ATOM 740 C LEU A 98 -13.746 -18.023 26.370 1.00 8.61 C ANISOU 740 C LEU A 98 1172 1000 1097 -77 -23 112 C ATOM 741 O LEU A 98 -14.459 -18.236 25.364 1.00 8.85 O ANISOU 741 O LEU A 98 1201 1017 1144 -108 -63 97 O ATOM 742 CB LEU A 98 -11.503 -19.013 25.747 1.00 8.53 C ANISOU 742 CB LEU A 98 1231 928 1081 -49 -16 52 C ATOM 743 CG LEU A 98 -10.731 -17.752 25.410 1.00 8.12 C ANISOU 743 CG LEU A 98 1185 917 982 -26 0 30 C ATOM 744 CD1 LEU A 98 -10.077 -17.223 26.656 1.00 7.82 C ANISOU 744 CD1 LEU A 98 1128 907 936 -6 16 53 C ATOM 745 CD2 LEU A 98 -9.705 -18.078 24.298 1.00 8.34 C ANISOU 745 CD2 LEU A 98 1243 931 995 -11 12 -12 C ATOM 746 N SER A 99 -13.901 -16.973 27.168 1.00 8.49 N ANISOU 746 N SER A 99 1137 1032 1055 -45 5 126 N ATOM 747 CA SER A 99 -15.032 -16.052 27.037 1.00 8.77 C ANISOU 747 CA SER A 99 1135 1099 1096 -35 6 138 C ATOM 748 C SER A 99 -14.581 -14.624 27.309 1.00 8.70 C ANISOU 748 C SER A 99 1146 1103 1055 8 25 109 C ATOM 749 O SER A 99 -13.578 -14.398 27.949 1.00 8.43 O ANISOU 749 O SER A 99 1141 1068 992 23 39 86 O ATOM 750 CB SER A 99 -16.117 -16.468 28.016 1.00 9.29 C ANISOU 750 CB SER A 99 1141 1201 1187 -38 36 196 C ATOM 751 OG SER A 99 -17.318 -15.727 27.865 1.00 9.67 O ANISOU 751 OG SER A 99 1131 1284 1258 -20 41 217 O ATOM 752 N MET A 100 -15.334 -13.652 26.798 1.00 9.17 N ANISOU 752 N MET A 100 1187 1166 1131 28 17 113 N ATOM 753 CA MET A 100 -14.974 -12.258 26.944 1.00 9.21 C ANISOU 753 CA MET A 100 1216 1154 1129 67 28 85 C ATOM 754 C MET A 100 -15.467 -11.710 28.273 1.00 9.62 C ANISOU 754 C MET A 100 1252 1231 1172 119 73 70 C ATOM 755 O MET A 100 -16.643 -11.906 28.657 1.00 10.14 O ANISOU 755 O MET A 100 1261 1336 1254 142 102 103 O ATOM 756 CB MET A 100 -15.573 -11.452 25.800 1.00 9.69 C ANISOU 756 CB MET A 100 1264 1197 1217 75 -2 108 C ATOM 757 CG MET A 100 -14.925 -11.702 24.458 1.00 9.60 C ANISOU 757 CG MET A 100 1286 1175 1184 35 -40 114 C ATOM 758 SD MET A 100 -13.143 -11.330 24.414 1.00 9.58 S ANISOU 758 SD MET A 100 1338 1144 1157 21 -23 85 S ATOM 759 CE MET A 100 -13.106 -9.532 24.629 1.00 9.72 C ANISOU 759 CE MET A 100 1366 1109 1216 53 -21 90 C ATOM 760 N ALA A 101 -14.564 -11.059 28.999 1.00 9.42 N ANISOU 760 N ALA A 101 1273 1189 1116 136 82 19 N ATOM 761 CA ALA A 101 -14.943 -10.291 30.167 1.00 10.09 C ANISOU 761 CA ALA A 101 1367 1291 1175 195 120 -23 C ATOM 762 C ALA A 101 -15.715 -9.050 29.677 1.00 10.54 C ANISOU 762 C ALA A 101 1413 1299 1290 246 124 -33 C ATOM 763 O ALA A 101 -15.514 -8.583 28.555 1.00 10.41 O ANISOU 763 O ALA A 101 1404 1229 1322 225 84 -12 O ATOM 764 CB ALA A 101 -13.686 -9.881 30.975 1.00 10.12 C ANISOU 764 CB ALA A 101 1431 1281 1131 189 103 -89 C ATOM 765 N ASN A 102 -16.612 -8.519 30.487 1.00 11.33 N ANISOU 765 N ASN A 102 1494 1422 1387 320 176 -58 N ATOM 766 CA ASN A 102 -17.222 -7.246 30.142 1.00 11.99 C ANISOU 766 CA ASN A 102 1575 1442 1539 385 180 -76 C ATOM 767 C ASN A 102 -17.673 -6.524 31.369 1.00 13.09 C ANISOU 767 C ASN A 102 1732 1590 1650 478 243 -155 C ATOM 768 O ASN A 102 -17.623 -7.065 32.488 1.00 13.26 O ANISOU 768 O ASN A 102 1764 1693 1581 490 289 -184 O ATOM 769 CB ASN A 102 -18.382 -7.415 29.128 1.00 12.13 C ANISOU 769 CB ASN A 102 1507 1476 1625 395 170 12 C ATOM 770 CG ASN A 102 -19.559 -8.190 29.689 1.00 12.67 C ANISOU 770 CG ASN A 102 1485 1642 1687 421 226 57 C ATOM 771 OD1 ASN A 102 -20.010 -7.932 30.825 1.00 13.54 O ANISOU 771 OD1 ASN A 102 1583 1795 1765 494 302 20 O ATOM 772 ND2 ASN A 102 -20.094 -9.140 28.892 1.00 12.32 N ANISOU 772 ND2 ASN A 102 1372 1637 1670 361 190 139 N ATOM 773 N ALA A 103 -18.126 -5.296 31.144 1.00 13.88 N ANISOU 773 N ALA A 103 1840 1607 1823 550 248 -186 N ATOM 774 CA ALA A 103 -18.777 -4.500 32.173 1.00 15.27 C ANISOU 774 CA ALA A 103 2030 1782 1989 665 320 -271 C ATOM 775 C ALA A 103 -20.202 -4.230 31.750 1.00 15.99 C ANISOU 775 C ALA A 103 2021 1888 2166 751 364 -205 C ATOM 776 O ALA A 103 -20.661 -3.112 31.867 1.00 17.26 O ANISOU 776 O ALA A 103 2193 1970 2392 852 390 -255 O ATOM 777 CB ALA A 103 -18.014 -3.144 32.404 1.00 15.96 C ANISOU 777 CB ALA A 103 2225 1727 2112 691 283 -387 C ATOM 778 N GLY A 104 -20.900 -5.247 31.267 1.00 15.46 N ANISOU 778 N GLY A 104 1850 1914 2107 712 368 -93 N ATOM 779 CA GLY A 104 -22.258 -5.069 30.750 1.00 16.15 C ANISOU 779 CA GLY A 104 1818 2028 2289 778 390 -11 C ATOM 780 C GLY A 104 -22.300 -5.225 29.234 1.00 15.42 C ANISOU 780 C GLY A 104 1690 1900 2268 706 289 87 C ATOM 781 O GLY A 104 -21.282 -5.479 28.593 1.00 14.28 O ANISOU 781 O GLY A 104 1615 1714 2094 612 219 88 O ATOM 782 N PRO A 105 -23.491 -5.074 28.642 1.00 16.18 N ANISOU 782 N PRO A 105 1670 2023 2452 755 281 174 N ATOM 783 CA PRO A 105 -23.660 -5.262 27.188 1.00 15.75 C ANISOU 783 CA PRO A 105 1577 1961 2445 689 175 272 C ATOM 784 C PRO A 105 -22.748 -4.404 26.288 1.00 15.30 C ANISOU 784 C PRO A 105 1620 1787 2404 667 102 269 C ATOM 785 O PRO A 105 -22.534 -3.240 26.562 1.00 15.82 O ANISOU 785 O PRO A 105 1740 1750 2520 743 123 223 O ATOM 786 CB PRO A 105 -25.118 -4.884 26.977 1.00 17.15 C ANISOU 786 CB PRO A 105 1612 2178 2725 781 187 353 C ATOM 787 CG PRO A 105 -25.767 -5.250 28.260 1.00 17.88 C ANISOU 787 CG PRO A 105 1634 2357 2800 841 306 323 C ATOM 788 CD PRO A 105 -24.782 -4.841 29.308 1.00 17.58 C ANISOU 788 CD PRO A 105 1732 2267 2680 871 372 193 C ATOM 789 N ASN A 106 -22.221 -5.006 25.221 1.00 14.43 N ANISOU 789 N ASN A 106 1535 1692 2253 562 20 319 N ATOM 790 CA ASN A 106 -21.414 -4.305 24.207 1.00 14.21 C ANISOU 790 CA ASN A 106 1584 1582 2230 530 -43 350 C ATOM 791 C ASN A 106 -20.283 -3.474 24.799 1.00 14.07 C ANISOU 791 C ASN A 106 1674 1455 2215 539 -12 267 C ATOM 792 O ASN A 106 -20.100 -2.315 24.430 1.00 14.75 O ANISOU 792 O ASN A 106 1797 1433 2372 578 -33 290 O ATOM 793 CB ASN A 106 -22.293 -3.411 23.332 1.00 15.28 C ANISOU 793 CB ASN A 106 1662 1687 2456 598 -94 450 C ATOM 794 CG ASN A 106 -23.406 -4.165 22.654 1.00 15.62 C ANISOU 794 CG ASN A 106 1589 1841 2502 579 -152 537 C ATOM 795 OD1 ASN A 106 -23.263 -5.311 22.282 1.00 14.81 O ANISOU 795 OD1 ASN A 106 1484 1819 2325 483 -189 538 O ATOM 796 ND2 ASN A 106 -24.534 -3.499 22.479 1.00 17.00 N ANISOU 796 ND2 ASN A 106 1667 2017 2776 673 -166 611 N ATOM 797 N THR A 107 -19.553 -4.072 25.741 1.00 13.35 N ANISOU 797 N THR A 107 1628 1388 2053 501 30 178 N ATOM 798 CA THR A 107 -18.399 -3.437 26.368 1.00 13.27 C ANISOU 798 CA THR A 107 1714 1290 2035 489 42 91 C ATOM 799 C THR A 107 -17.164 -4.354 26.302 1.00 12.16 C ANISOU 799 C THR A 107 1617 1191 1809 382 24 72 C ATOM 800 O THR A 107 -16.290 -4.297 27.169 1.00 12.18 O ANISOU 800 O THR A 107 1675 1172 1779 363 39 -8 O ATOM 801 CB THR A 107 -18.694 -3.053 27.836 1.00 13.95 C ANISOU 801 CB THR A 107 1818 1365 2117 573 112 -17 C ATOM 802 OG1 THR A 107 -19.035 -4.226 28.577 1.00 13.52 O ANISOU 802 OG1 THR A 107 1721 1437 1979 562 159 -31 O ATOM 803 CG2 THR A 107 -19.853 -2.020 27.945 1.00 15.30 C ANISOU 803 CG2 THR A 107 1947 1478 2388 703 144 -13 C ATOM 804 N ASN A 108 -17.076 -5.187 25.274 1.00 11.42 N ANISOU 804 N ASN A 108 1500 1157 1679 317 -11 143 N ATOM 805 CA ASN A 108 -15.925 -6.069 25.117 1.00 10.47 C ANISOU 805 CA ASN A 108 1416 1072 1490 233 -20 127 C ATOM 806 C ASN A 108 -14.710 -5.275 24.683 1.00 10.52 C ANISOU 806 C ASN A 108 1477 1003 1516 194 -40 132 C ATOM 807 O ASN A 108 -14.811 -4.443 23.786 1.00 10.98 O ANISOU 807 O ASN A 108 1541 1010 1621 199 -66 198 O ATOM 808 CB ASN A 108 -16.177 -7.088 24.034 1.00 10.13 C ANISOU 808 CB ASN A 108 1345 1100 1403 186 -53 185 C ATOM 809 CG ASN A 108 -17.351 -7.942 24.310 1.00 10.23 C ANISOU 809 CG ASN A 108 1291 1181 1414 200 -49 197 C ATOM 810 OD1 ASN A 108 -17.295 -8.772 25.196 1.00 9.97 O ANISOU 810 OD1 ASN A 108 1249 1183 1354 188 -15 160 O ATOM 811 ND2 ASN A 108 -18.434 -7.766 23.538 1.00 10.83 N ANISOU 811 ND2 ASN A 108 1311 1280 1523 220 -88 262 N ATOM 812 N GLY A 109 -13.571 -5.545 25.311 1.00 10.12 N ANISOU 812 N GLY A 109 1458 950 1435 151 -31 76 N ATOM 813 CA GLY A 109 -12.293 -4.915 24.962 1.00 10.31 C ANISOU 813 CA GLY A 109 1514 914 1486 96 -49 87 C ATOM 814 C GLY A 109 -11.233 -5.977 24.722 1.00 9.63 C ANISOU 814 C GLY A 109 1421 897 1339 36 -42 91 C ATOM 815 O GLY A 109 -11.276 -6.717 23.712 1.00 9.42 O ANISOU 815 O GLY A 109 1381 931 1267 19 -39 141 O ATOM 816 N SER A 110 -10.288 -6.080 25.652 1.00 9.53 N ANISOU 816 N SER A 110 1418 879 1322 11 -45 32 N ATOM 817 CA SER A 110 -9.245 -7.112 25.589 1.00 8.99 C ANISOU 817 CA SER A 110 1331 874 1209 -29 -37 35 C ATOM 818 C SER A 110 -9.365 -8.190 26.660 1.00 8.59 C ANISOU 818 C SER A 110 1275 882 1106 -10 -29 -13 C ATOM 819 O SER A 110 -8.846 -9.295 26.489 1.00 8.21 O ANISOU 819 O SER A 110 1208 885 1025 -24 -19 0 O ATOM 820 CB SER A 110 -7.875 -6.457 25.724 1.00 9.44 C ANISOU 820 CB SER A 110 1382 891 1313 -84 -57 34 C ATOM 821 OG SER A 110 -7.760 -5.821 26.976 1.00 9.87 O ANISOU 821 OG SER A 110 1460 898 1390 -82 -90 -42 O ATOM 822 N GLN A 111 -10.011 -7.878 27.781 1.00 8.88 N ANISOU 822 N GLN A 111 1328 912 1132 27 -29 -67 N ATOM 823 CA GLN A 111 -10.047 -8.828 28.875 1.00 8.74 C ANISOU 823 CA GLN A 111 1306 958 1054 43 -20 -95 C ATOM 824 C GLN A 111 -10.896 -10.055 28.537 1.00 8.31 C ANISOU 824 C GLN A 111 1224 957 975 56 7 -49 C ATOM 825 O GLN A 111 -11.926 -9.950 27.888 1.00 8.31 O ANISOU 825 O GLN A 111 1209 951 995 73 17 -22 O ATOM 826 CB GLN A 111 -10.552 -8.171 30.154 1.00 9.35 C ANISOU 826 CB GLN A 111 1414 1033 1104 87 -15 -164 C ATOM 827 CG GLN A 111 -9.616 -7.098 30.749 1.00 10.06 C ANISOU 827 CG GLN A 111 1543 1066 1211 64 -62 -235 C ATOM 828 CD GLN A 111 -10.202 -6.543 32.044 1.00 10.88 C ANISOU 828 CD GLN A 111 1693 1177 1262 121 -53 -327 C ATOM 829 OE1 GLN A 111 -10.517 -7.296 32.929 1.00 10.88 O ANISOU 829 OE1 GLN A 111 1692 1265 1174 150 -27 -334 O ATOM 830 NE2 GLN A 111 -10.367 -5.233 32.133 1.00 11.74 N ANISOU 830 NE2 GLN A 111 1845 1189 1423 141 -68 -395 N ATOM 831 N PHE A 112 -10.466 -11.200 29.032 1.00 8.13 N ANISOU 831 N PHE A 112 1191 979 919 45 10 -38 N ATOM 832 CA PHE A 112 -11.129 -12.483 28.797 1.00 7.99 C ANISOU 832 CA PHE A 112 1150 990 894 44 27 2 C ATOM 833 C PHE A 112 -11.062 -13.311 30.083 1.00 8.21 C ANISOU 833 C PHE A 112 1174 1065 881 55 37 15 C ATOM 834 O PHE A 112 -10.371 -12.937 31.041 1.00 8.51 O ANISOU 834 O PHE A 112 1229 1124 880 64 24 -13 O ATOM 835 CB PHE A 112 -10.381 -13.259 27.698 1.00 7.69 C ANISOU 835 CB PHE A 112 1111 937 874 16 17 20 C ATOM 836 CG PHE A 112 -8.976 -13.546 28.067 1.00 7.75 C ANISOU 836 CG PHE A 112 1115 949 877 8 8 14 C ATOM 837 CD1 PHE A 112 -8.649 -14.707 28.750 1.00 7.81 C ANISOU 837 CD1 PHE A 112 1112 975 877 16 7 35 C ATOM 838 CD2 PHE A 112 -7.969 -12.599 27.802 1.00 7.95 C ANISOU 838 CD2 PHE A 112 1138 961 920 -8 -4 0 C ATOM 839 CE1 PHE A 112 -7.352 -14.946 29.149 1.00 8.03 C ANISOU 839 CE1 PHE A 112 1123 1016 909 17 -8 40 C ATOM 840 CE2 PHE A 112 -6.646 -12.848 28.167 1.00 8.10 C ANISOU 840 CE2 PHE A 112 1133 996 948 -18 -19 4 C ATOM 841 CZ PHE A 112 -6.342 -14.005 28.871 1.00 8.17 C ANISOU 841 CZ PHE A 112 1128 1031 944 0 -24 22 C ATOM 842 N PHE A 113 -11.738 -14.453 30.104 1.00 8.29 N ANISOU 842 N PHE A 113 1160 1089 899 49 53 63 N ATOM 843 CA PHE A 113 -11.556 -15.379 31.210 1.00 8.69 C ANISOU 843 CA PHE A 113 1205 1178 917 54 62 103 C ATOM 844 C PHE A 113 -11.623 -16.828 30.730 1.00 8.89 C ANISOU 844 C PHE A 113 1215 1170 993 27 57 155 C ATOM 845 O PHE A 113 -12.178 -17.128 29.660 1.00 8.74 O ANISOU 845 O PHE A 113 1188 1110 1021 4 49 152 O ATOM 846 CB PHE A 113 -12.557 -15.087 32.333 1.00 9.18 C ANISOU 846 CB PHE A 113 1255 1304 927 84 104 118 C ATOM 847 CG PHE A 113 -14.004 -15.270 31.939 1.00 9.30 C ANISOU 847 CG PHE A 113 1224 1323 984 82 137 156 C ATOM 848 CD1 PHE A 113 -14.704 -14.257 31.283 1.00 9.18 C ANISOU 848 CD1 PHE A 113 1197 1292 998 101 141 122 C ATOM 849 CD2 PHE A 113 -14.671 -16.446 32.232 1.00 9.66 C ANISOU 849 CD2 PHE A 113 1229 1387 1054 57 157 239 C ATOM 850 CE1 PHE A 113 -16.050 -14.420 30.918 1.00 9.46 C ANISOU 850 CE1 PHE A 113 1170 1341 1081 99 161 166 C ATOM 851 CE2 PHE A 113 -16.020 -16.612 31.880 1.00 9.99 C ANISOU 851 CE2 PHE A 113 1208 1437 1148 42 179 282 C ATOM 852 CZ PHE A 113 -16.706 -15.583 31.216 1.00 9.89 C ANISOU 852 CZ PHE A 113 1175 1422 1160 66 178 243 C ATOM 853 N ILE A 114 -11.002 -17.707 31.509 1.00 9.41 N ANISOU 853 N ILE A 114 1281 1245 1048 32 51 201 N ATOM 854 CA ILE A 114 -10.968 -19.126 31.240 1.00 9.78 C ANISOU 854 CA ILE A 114 1320 1238 1156 14 44 252 C ATOM 855 C ILE A 114 -11.761 -19.761 32.358 1.00 10.63 C ANISOU 855 C ILE A 114 1404 1383 1248 9 69 342 C ATOM 856 O ILE A 114 -11.401 -19.592 33.533 1.00 10.92 O ANISOU 856 O ILE A 114 1446 1491 1212 35 77 375 O ATOM 857 CB ILE A 114 -9.525 -19.691 31.306 1.00 9.89 C ANISOU 857 CB ILE A 114 1343 1226 1186 35 19 258 C ATOM 858 CG1 ILE A 114 -8.608 -18.962 30.339 1.00 9.55 C ANISOU 858 CG1 ILE A 114 1308 1170 1149 43 9 184 C ATOM 859 CG2 ILE A 114 -9.526 -21.183 30.985 1.00 10.30 C ANISOU 859 CG2 ILE A 114 1395 1195 1321 28 13 303 C ATOM 860 CD1 ILE A 114 -7.116 -19.171 30.607 1.00 9.76 C ANISOU 860 CD1 ILE A 114 1317 1203 1185 70 -10 193 C ATOM 861 N CYS A 115 -12.831 -20.470 32.015 1.00 11.17 N ANISOU 861 N CYS A 115 1446 1416 1382 -28 79 387 N ATOM 862 CA CYS A 115 -13.648 -21.156 33.012 1.00 12.26 C ANISOU 862 CA CYS A 115 1547 1589 1521 -45 113 497 C ATOM 863 C CYS A 115 -12.892 -22.362 33.537 1.00 12.80 C ANISOU 863 C CYS A 115 1629 1612 1623 -45 95 578 C ATOM 864 O CYS A 115 -12.181 -23.010 32.808 1.00 12.57 O ANISOU 864 O CYS A 115 1623 1486 1664 -47 57 549 O ATOM 865 CB CYS A 115 -14.954 -21.649 32.408 1.00 12.79 C ANISOU 865 CB CYS A 115 1566 1616 1677 -102 115 531 C ATOM 866 SG CYS A 115 -15.971 -20.332 31.775 1.00 13.14 S ANISOU 866 SG CYS A 115 1576 1714 1703 -94 129 464 S ATOM 867 N THR A 116 -13.040 -22.644 34.814 1.00 13.72 N ANISOU 867 N THR A 116 1729 1801 1681 -34 125 683 N ATOM 868 CA THR A 116 -12.516 -23.876 35.378 1.00 14.73 C ANISOU 868 CA THR A 116 1861 1882 1852 -36 108 796 C ATOM 869 C THR A 116 -13.672 -24.663 35.951 1.00 15.90 C ANISOU 869 C THR A 116 1962 2037 2042 -84 150 937 C ATOM 870 O THR A 116 -13.454 -25.507 36.804 1.00 17.12 O ANISOU 870 O THR A 116 2112 2193 2199 -83 153 1070 O ATOM 871 CB THR A 116 -11.481 -23.600 36.497 1.00 15.09 C ANISOU 871 CB THR A 116 1929 2024 1780 19 95 828 C ATOM 872 OG1 THR A 116 -12.093 -22.773 37.504 1.00 15.58 O ANISOU 872 OG1 THR A 116 1984 2232 1700 36 144 843 O ATOM 873 CG2 THR A 116 -10.254 -22.922 35.926 1.00 14.10 C ANISOU 873 CG2 THR A 116 1831 1884 1642 53 47 708 C ATOM 874 N ALA A 117 -14.893 -24.346 35.504 1.00 15.84 N ANISOU 874 N ALA A 117 1909 2040 2068 -126 180 919 N ATOM 875 CA ALA A 117 -16.107 -25.113 35.799 1.00 17.01 C ANISOU 875 CA ALA A 117 1987 2180 2294 -192 216 1052 C ATOM 876 C ALA A 117 -17.151 -24.674 34.790 1.00 16.66 C ANISOU 876 C ALA A 117 1896 2115 2318 -236 210 979 C ATOM 877 O ALA A 117 -16.914 -23.762 33.999 1.00 15.43 O ANISOU 877 O ALA A 117 1769 1962 2129 -206 185 842 O ATOM 878 CB ALA A 117 -16.622 -24.869 37.273 1.00 18.01 C ANISOU 878 CB ALA A 117 2074 2472 2295 -165 305 1179 C ATOM 879 N LYS A 118 -18.296 -25.333 34.809 1.00 17.81 N ANISOU 879 N LYS A 118 1962 2240 2563 -312 226 1084 N ATOM 880 CA LYS A 118 -19.471 -24.888 34.045 1.00 17.87 C ANISOU 880 CA LYS A 118 1895 2261 2631 -356 220 1046 C ATOM 881 C LYS A 118 -20.069 -23.635 34.710 1.00 17.70 C ANISOU 881 C LYS A 118 1824 2412 2489 -286 310 1042 C ATOM 882 O LYS A 118 -20.252 -23.605 35.919 1.00 18.60 O ANISOU 882 O LYS A 118 1910 2637 2519 -253 396 1143 O ATOM 883 CB LYS A 118 -20.500 -26.012 34.023 1.00 19.39 C ANISOU 883 CB LYS A 118 2000 2388 2978 -466 209 1180 C ATOM 884 CG LYS A 118 -21.742 -25.738 33.209 1.00 19.84 C ANISOU 884 CG LYS A 118 1961 2453 3123 -529 181 1158 C ATOM 885 CD LYS A 118 -22.427 -27.078 32.916 1.00 21.41 C ANISOU 885 CD LYS A 118 2100 2524 3509 -663 122 1259 C ATOM 886 CE LYS A 118 -23.912 -26.940 32.655 1.00 22.53 C ANISOU 886 CE LYS A 118 2091 2722 3744 -740 122 1323 C ATOM 887 NZ LYS A 118 -24.683 -27.528 33.814 1.00 24.36 N ANISOU 887 NZ LYS A 118 2203 3020 4029 -791 215 1541 N ATOM 888 N THR A 119 -20.344 -22.600 33.927 1.00 16.77 N ANISOU 888 N THR A 119 1701 2314 2356 -256 292 925 N ATOM 889 CA THR A 119 -20.818 -21.322 34.473 1.00 16.64 C ANISOU 889 CA THR A 119 1651 2433 2236 -171 373 895 C ATOM 890 C THR A 119 -22.011 -20.879 33.645 1.00 16.66 C ANISOU 890 C THR A 119 1556 2445 2326 -194 359 884 C ATOM 891 O THR A 119 -21.969 -19.873 32.936 1.00 15.75 O ANISOU 891 O THR A 119 1464 2327 2193 -149 330 777 O ATOM 892 CB THR A 119 -19.756 -20.215 34.439 1.00 15.45 C ANISOU 892 CB THR A 119 1603 2294 1970 -86 361 756 C ATOM 893 OG1 THR A 119 -19.448 -19.913 33.082 1.00 14.58 O ANISOU 893 OG1 THR A 119 1530 2092 1918 -106 276 652 O ATOM 894 CG2 THR A 119 -18.495 -20.618 35.172 1.00 15.31 C ANISOU 894 CG2 THR A 119 1672 2271 1872 -66 352 762 C ATOM 895 N GLU A 120 -23.060 -21.679 33.776 1.00 17.70 N ANISOU 895 N GLU A 120 1573 2587 2562 -270 376 1011 N ATOM 896 CA GLU A 120 -24.292 -21.565 33.013 1.00 18.24 C ANISOU 896 CA GLU A 120 1520 2664 2746 -319 345 1035 C ATOM 897 C GLU A 120 -24.990 -20.211 33.178 1.00 18.07 C ANISOU 897 C GLU A 120 1431 2760 2672 -216 417 1003 C ATOM 898 O GLU A 120 -25.642 -19.732 32.248 1.00 18.15 O ANISOU 898 O GLU A 120 1381 2762 2753 -223 360 969 O ATOM 899 CB GLU A 120 -25.218 -22.733 33.397 1.00 19.97 C ANISOU 899 CB GLU A 120 1615 2881 3089 -426 363 1205 C ATOM 900 CG GLU A 120 -25.706 -22.719 34.885 1.00 21.39 C ANISOU 900 CG GLU A 120 1715 3210 3202 -380 519 1348 C ATOM 901 CD GLU A 120 -24.707 -23.257 35.970 1.00 21.56 C ANISOU 901 CD GLU A 120 1837 3239 3113 -356 570 1402 C ATOM 902 OE1 GLU A 120 -23.545 -23.644 35.639 1.00 20.47 O ANISOU 902 OE1 GLU A 120 1830 2987 2961 -366 488 1328 O ATOM 903 OE2 GLU A 120 -25.121 -23.316 37.180 1.00 22.94 O ANISOU 903 OE2 GLU A 120 1951 3549 3214 -323 697 1531 O ATOM 904 N TRP A 121 -24.809 -19.592 34.343 1.00 17.95 N ANISOU 904 N TRP A 121 1438 2852 2531 -115 536 1007 N ATOM 905 CA TRP A 121 -25.366 -18.276 34.652 1.00 18.07 C ANISOU 905 CA TRP A 121 1410 2968 2487 4 620 957 C ATOM 906 C TRP A 121 -24.750 -17.123 33.856 1.00 16.56 C ANISOU 906 C TRP A 121 1315 2712 2263 70 555 801 C ATOM 907 O TRP A 121 -25.285 -16.026 33.847 1.00 16.85 O ANISOU 907 O TRP A 121 1313 2795 2292 163 600 757 O ATOM 908 CB TRP A 121 -25.268 -18.008 36.160 1.00 18.93 C ANISOU 908 CB TRP A 121 1537 3206 2450 94 762 987 C ATOM 909 CG TRP A 121 -23.907 -17.743 36.680 1.00 18.07 C ANISOU 909 CG TRP A 121 1592 3076 2195 139 748 890 C ATOM 910 CD1 TRP A 121 -23.321 -16.523 36.836 1.00 17.51 C ANISOU 910 CD1 TRP A 121 1618 3010 2023 239 755 744 C ATOM 911 CD2 TRP A 121 -22.974 -18.700 37.187 1.00 17.87 C ANISOU 911 CD2 TRP A 121 1645 3025 2118 85 721 939 C ATOM 912 NE1 TRP A 121 -22.088 -16.662 37.401 1.00 16.96 N ANISOU 912 NE1 TRP A 121 1674 2929 1839 243 728 697 N ATOM 913 CE2 TRP A 121 -21.841 -17.991 37.609 1.00 17.17 C ANISOU 913 CE2 TRP A 121 1690 2940 1892 155 706 818 C ATOM 914 CE3 TRP A 121 -22.988 -20.086 37.321 1.00 18.45 C ANISOU 914 CE3 TRP A 121 1685 3063 2260 -14 701 1080 C ATOM 915 CZ2 TRP A 121 -20.709 -18.623 38.126 1.00 16.94 C ANISOU 915 CZ2 TRP A 121 1752 2893 1788 132 667 836 C ATOM 916 CZ3 TRP A 121 -21.876 -20.717 37.852 1.00 18.21 C ANISOU 916 CZ3 TRP A 121 1754 3004 2158 -28 670 1101 C ATOM 917 CH2 TRP A 121 -20.747 -19.984 38.242 1.00 17.45 C ANISOU 917 CH2 TRP A 121 1781 2928 1921 47 653 981 C ATOM 918 N LEU A 122 -23.628 -17.372 33.192 1.00 14.98 N ANISOU 918 N LEU A 122 1235 2405 2051 25 455 725 N ATOM 919 CA LEU A 122 -23.022 -16.381 32.317 1.00 13.78 C ANISOU 919 CA LEU A 122 1166 2188 1881 66 389 601 C ATOM 920 C LEU A 122 -23.495 -16.486 30.843 1.00 13.48 C ANISOU 920 C LEU A 122 1085 2086 1949 4 281 598 C ATOM 921 O LEU A 122 -23.177 -15.628 30.049 1.00 12.79 O ANISOU 921 O LEU A 122 1048 1958 1851 38 232 523 O ATOM 922 CB LEU A 122 -21.498 -16.496 32.373 1.00 12.61 C ANISOU 922 CB LEU A 122 1161 1976 1655 60 349 524 C ATOM 923 CG LEU A 122 -20.825 -16.296 33.741 1.00 12.81 C ANISOU 923 CG LEU A 122 1249 2064 1555 119 423 509 C ATOM 924 CD1 LEU A 122 -19.291 -16.268 33.542 1.00 11.67 C ANISOU 924 CD1 LEU A 122 1225 1848 1358 109 358 428 C ATOM 925 CD2 LEU A 122 -21.302 -15.050 34.457 1.00 13.39 C ANISOU 925 CD2 LEU A 122 1311 2215 1561 229 509 458 C ATOM 926 N ASP A 123 -24.240 -17.538 30.494 1.00 14.13 N ANISOU 926 N ASP A 123 1079 2160 2129 -92 239 683 N ATOM 927 CA ASP A 123 -24.700 -17.770 29.109 1.00 14.16 C ANISOU 927 CA ASP A 123 1048 2110 2219 -165 117 674 C ATOM 928 C ASP A 123 -25.584 -16.629 28.668 1.00 14.66 C ANISOU 928 C ASP A 123 1027 2229 2313 -97 114 676 C ATOM 929 O ASP A 123 -26.442 -16.186 29.422 1.00 15.47 O ANISOU 929 O ASP A 123 1020 2418 2439 -35 206 738 O ATOM 930 CB ASP A 123 -25.476 -19.099 29.008 1.00 15.17 C ANISOU 930 CB ASP A 123 1080 2220 2461 -289 72 769 C ATOM 931 CG ASP A 123 -24.583 -20.320 29.161 1.00 14.83 C ANISOU 931 CG ASP A 123 1132 2084 2418 -363 45 762 C ATOM 932 OD1 ASP A 123 -23.335 -20.176 29.061 1.00 13.66 O ANISOU 932 OD1 ASP A 123 1121 1885 2184 -324 38 673 O ATOM 933 OD2 ASP A 123 -25.123 -21.427 29.373 1.00 15.80 O ANISOU 933 OD2 ASP A 123 1186 2178 2639 -459 29 853 O ATOM 934 N GLY A 124 -25.350 -16.105 27.467 1.00 14.27 N ANISOU 934 N GLY A 124 1028 2135 2258 -97 18 615 N ATOM 935 CA GLY A 124 -26.111 -14.937 27.006 1.00 14.90 C ANISOU 935 CA GLY A 124 1034 2256 2369 -20 7 628 C ATOM 936 C GLY A 124 -25.672 -13.615 27.632 1.00 14.67 C ANISOU 936 C GLY A 124 1063 2231 2279 113 98 574 C ATOM 937 O GLY A 124 -26.249 -12.572 27.341 1.00 15.30 O ANISOU 937 O GLY A 124 1091 2326 2394 195 99 584 O ATOM 938 N LYS A 125 -24.658 -13.639 28.498 1.00 14.04 N ANISOU 938 N LYS A 125 1089 2131 2112 137 167 517 N ATOM 939 CA LYS A 125 -24.118 -12.385 29.074 1.00 13.90 C ANISOU 939 CA LYS A 125 1147 2100 2034 250 234 442 C ATOM 940 C LYS A 125 -22.663 -12.118 28.646 1.00 12.64 C ANISOU 940 C LYS A 125 1138 1856 1807 230 183 356 C ATOM 941 O LYS A 125 -22.270 -10.973 28.502 1.00 12.69 O ANISOU 941 O LYS A 125 1201 1819 1802 295 185 303 O ATOM 942 CB LYS A 125 -24.242 -12.393 30.602 1.00 14.56 C ANISOU 942 CB LYS A 125 1215 2253 2061 312 362 443 C ATOM 943 CG LYS A 125 -25.662 -12.568 31.080 1.00 16.06 C ANISOU 943 CG LYS A 125 1243 2542 2316 343 437 538 C ATOM 944 CD LYS A 125 -25.747 -12.508 32.585 1.00 16.86 C ANISOU 944 CD LYS A 125 1341 2732 2333 417 578 536 C ATOM 945 CE LYS A 125 -27.131 -12.802 33.029 1.00 18.49 C ANISOU 945 CE LYS A 125 1370 3049 2605 440 665 649 C ATOM 946 NZ LYS A 125 -27.265 -14.214 33.431 1.00 18.82 N ANISOU 946 NZ LYS A 125 1359 3137 2654 327 677 759 N ATOM 947 N HIS A 126 -21.889 -13.175 28.447 1.00 11.86 N ANISOU 947 N HIS A 126 1095 1731 1678 143 142 350 N ATOM 948 CA HIS A 126 -20.509 -13.092 27.962 1.00 10.80 C ANISOU 948 CA HIS A 126 1081 1531 1491 119 99 283 C ATOM 949 C HIS A 126 -20.364 -13.912 26.688 1.00 10.41 C ANISOU 949 C HIS A 126 1045 1448 1460 35 8 291 C ATOM 950 O HIS A 126 -20.883 -15.031 26.600 1.00 10.80 O ANISOU 950 O HIS A 126 1047 1506 1547 -30 -17 331 O ATOM 951 CB HIS A 126 -19.560 -13.607 29.049 1.00 10.47 C ANISOU 951 CB HIS A 126 1099 1493 1383 114 146 257 C ATOM 952 CG HIS A 126 -19.660 -12.822 30.306 1.00 11.03 C ANISOU 952 CG HIS A 126 1174 1608 1407 196 228 231 C ATOM 953 ND1 HIS A 126 -18.781 -11.806 30.617 1.00 10.77 N ANISOU 953 ND1 HIS A 126 1223 1541 1327 242 233 149 N ATOM 954 CD2 HIS A 126 -20.614 -12.815 31.271 1.00 11.99 C ANISOU 954 CD2 HIS A 126 1225 1807 1522 244 309 269 C ATOM 955 CE1 HIS A 126 -19.156 -11.248 31.759 1.00 11.66 C ANISOU 955 CE1 HIS A 126 1331 1702 1395 317 307 121 C ATOM 956 NE2 HIS A 126 -20.266 -11.841 32.174 1.00 12.39 N ANISOU 956 NE2 HIS A 126 1331 1872 1504 326 363 195 N ATOM 957 N VAL A 127 -19.665 -13.353 25.706 1.00 9.85 N ANISOU 957 N VAL A 127 1042 1338 1362 35 -38 253 N ATOM 958 CA VAL A 127 -19.471 -14.003 24.398 1.00 9.70 C ANISOU 958 CA VAL A 127 1053 1300 1330 -29 -120 244 C ATOM 959 C VAL A 127 -18.387 -15.081 24.532 1.00 9.19 C ANISOU 959 C VAL A 127 1058 1199 1233 -71 -114 202 C ATOM 960 O VAL A 127 -17.245 -14.775 24.841 1.00 8.51 O ANISOU 960 O VAL A 127 1032 1093 1106 -46 -79 166 O ATOM 961 CB VAL A 127 -19.073 -12.979 23.322 1.00 9.55 C ANISOU 961 CB VAL A 127 1081 1268 1277 -6 -157 235 C ATOM 962 CG1 VAL A 127 -18.752 -13.664 22.002 1.00 9.60 C ANISOU 962 CG1 VAL A 127 1136 1274 1235 -64 -229 213 C ATOM 963 CG2 VAL A 127 -20.186 -11.946 23.139 1.00 10.24 C ANISOU 963 CG2 VAL A 127 1096 1379 1414 44 -172 290 C ATOM 964 N VAL A 128 -18.786 -16.344 24.355 1.00 9.63 N ANISOU 964 N VAL A 128 1094 1241 1322 -135 -151 210 N ATOM 965 CA VAL A 128 -17.868 -17.487 24.346 1.00 9.47 C ANISOU 965 CA VAL A 128 1137 1167 1293 -169 -154 171 C ATOM 966 C VAL A 128 -17.282 -17.549 22.937 1.00 9.57 C ANISOU 966 C VAL A 128 1221 1161 1253 -183 -207 108 C ATOM 967 O VAL A 128 -18.022 -17.457 21.937 1.00 10.21 O ANISOU 967 O VAL A 128 1289 1262 1326 -212 -276 106 O ATOM 968 CB VAL A 128 -18.598 -18.804 24.713 1.00 10.15 C ANISOU 968 CB VAL A 128 1176 1223 1455 -235 -176 209 C ATOM 969 CG1 VAL A 128 -17.678 -19.999 24.537 1.00 10.17 C ANISOU 969 CG1 VAL A 128 1252 1146 1465 -262 -190 163 C ATOM 970 CG2 VAL A 128 -19.129 -18.741 26.150 1.00 10.29 C ANISOU 970 CG2 VAL A 128 1121 1282 1504 -215 -104 288 C ATOM 971 N PHE A 129 -15.957 -17.617 22.849 1.00 9.18 N ANISOU 971 N PHE A 129 1240 1088 1158 -157 -173 63 N ATOM 972 CA PHE A 129 -15.279 -17.604 21.563 1.00 9.41 C ANISOU 972 CA PHE A 129 1336 1117 1119 -155 -196 8 C ATOM 973 C PHE A 129 -14.144 -18.590 21.428 1.00 9.61 C ANISOU 973 C PHE A 129 1421 1095 1133 -147 -171 -50 C ATOM 974 O PHE A 129 -13.486 -18.628 20.402 1.00 9.92 O ANISOU 974 O PHE A 129 1515 1144 1107 -133 -171 -102 O ATOM 975 CB PHE A 129 -14.775 -16.196 21.239 1.00 8.99 C ANISOU 975 CB PHE A 129 1293 1105 1014 -114 -168 27 C ATOM 976 CG PHE A 129 -13.657 -15.713 22.136 1.00 8.33 C ANISOU 976 CG PHE A 129 1215 1011 936 -78 -102 32 C ATOM 977 CD1 PHE A 129 -13.932 -15.156 23.377 1.00 8.05 C ANISOU 977 CD1 PHE A 129 1141 978 940 -58 -74 63 C ATOM 978 CD2 PHE A 129 -12.329 -15.795 21.722 1.00 8.27 C ANISOU 978 CD2 PHE A 129 1249 1001 892 -63 -68 3 C ATOM 979 CE1 PHE A 129 -12.911 -14.685 24.199 1.00 7.69 C ANISOU 979 CE1 PHE A 129 1104 926 890 -33 -34 56 C ATOM 980 CE2 PHE A 129 -11.283 -15.329 22.545 1.00 7.85 C ANISOU 980 CE2 PHE A 129 1185 943 853 -40 -24 12 C ATOM 981 CZ PHE A 129 -11.581 -14.756 23.776 1.00 7.59 C ANISOU 981 CZ PHE A 129 1122 907 854 -31 -16 35 C ATOM 982 N GLY A 130 -13.872 -19.399 22.439 1.00 9.82 N ANISOU 982 N GLY A 130 1436 1074 1221 -146 -146 -37 N ATOM 983 CA GLY A 130 -12.825 -20.409 22.263 1.00 10.26 C ANISOU 983 CA GLY A 130 1542 1071 1284 -126 -127 -89 C ATOM 984 C GLY A 130 -12.802 -21.398 23.362 1.00 10.69 C ANISOU 984 C GLY A 130 1577 1063 1422 -133 -117 -51 C ATOM 985 O GLY A 130 -13.700 -21.414 24.213 1.00 10.80 O ANISOU 985 O GLY A 130 1539 1085 1480 -164 -125 15 O ATOM 986 N LYS A 131 -11.766 -22.223 23.351 1.00 11.26 N ANISOU 986 N LYS A 131 1685 1077 1515 -98 -95 -85 N ATOM 987 CA LYS A 131 -11.614 -23.254 24.346 1.00 11.89 C ANISOU 987 CA LYS A 131 1751 1084 1680 -96 -89 -35 C ATOM 988 C LYS A 131 -10.167 -23.762 24.430 1.00 12.21 C ANISOU 988 C LYS A 131 1815 1087 1735 -26 -51 -57 C ATOM 989 O LYS A 131 -9.493 -23.931 23.406 1.00 12.42 O ANISOU 989 O LYS A 131 1886 1098 1734 10 -36 -141 O ATOM 990 CB LYS A 131 -12.545 -24.424 24.048 1.00 13.04 C ANISOU 990 CB LYS A 131 1915 1131 1909 -158 -146 -49 C ATOM 991 CG LYS A 131 -12.690 -25.339 25.229 1.00 13.63 C ANISOU 991 CG LYS A 131 1959 1138 2082 -175 -142 44 C ATOM 992 CD LYS A 131 -13.773 -26.426 25.076 1.00 14.86 C ANISOU 992 CD LYS A 131 2113 1187 2346 -260 -204 58 C ATOM 993 CE LYS A 131 -13.647 -27.385 26.241 1.00 15.53 C ANISOU 993 CE LYS A 131 2174 1194 2532 -265 -188 170 C ATOM 994 NZ LYS A 131 -14.867 -28.097 26.474 1.00 16.71 N ANISOU 994 NZ LYS A 131 2282 1278 2786 -364 -232 240 N ATOM 995 N VAL A 132 -9.714 -24.002 25.662 1.00 12.24 N ANISOU 995 N VAL A 132 1784 1088 1777 -3 -33 25 N ATOM 996 CA VAL A 132 -8.410 -24.617 25.911 1.00 12.92 C ANISOU 996 CA VAL A 132 1871 1134 1902 66 -8 30 C ATOM 997 C VAL A 132 -8.254 -25.963 25.207 1.00 14.37 C ANISOU 997 C VAL A 132 2108 1184 2168 87 -19 -32 C ATOM 998 O VAL A 132 -9.115 -26.839 25.291 1.00 14.80 O ANISOU 998 O VAL A 132 2183 1142 2298 38 -58 -18 O ATOM 999 CB VAL A 132 -8.151 -24.785 27.432 1.00 12.83 C ANISOU 999 CB VAL A 132 1815 1144 1916 78 -8 147 C ATOM 1000 CG1 VAL A 132 -6.967 -25.692 27.668 1.00 13.56 C ANISOU 1000 CG1 VAL A 132 1902 1172 2078 150 0 169 C ATOM 1001 CG2 VAL A 132 -7.961 -23.385 28.101 1.00 11.76 C ANISOU 1001 CG2 VAL A 132 1640 1139 1687 76 2 175 C ATOM 1002 N LYS A 133 -7.150 -26.111 24.482 1.00 15.49 N ANISOU 1002 N LYS A 133 2269 1315 2299 162 19 -104 N ATOM 1003 CA LYS A 133 -6.799 -27.384 23.853 1.00 17.19 C ANISOU 1003 CA LYS A 133 2541 1395 2593 211 22 -180 C ATOM 1004 C LYS A 133 -5.799 -28.051 24.768 1.00 17.89 C ANISOU 1004 C LYS A 133 2589 1434 2774 286 41 -101 C ATOM 1005 O LYS A 133 -6.104 -29.055 25.361 1.00 19.34 O ANISOU 1005 O LYS A 133 2784 1500 3065 277 9 -45 O ATOM 1006 CB LYS A 133 -6.179 -27.175 22.479 1.00 18.05 C ANISOU 1006 CB LYS A 133 2693 1537 2626 267 68 -309 C ATOM 1007 CG LYS A 133 -7.083 -27.286 21.249 1.00 18.95 C ANISOU 1007 CG LYS A 133 2890 1630 2680 217 32 -429 C ATOM 1008 CD LYS A 133 -6.483 -26.408 20.124 1.00 19.24 C ANISOU 1008 CD LYS A 133 2941 1790 2577 259 91 -500 C ATOM 1009 CE LYS A 133 -6.677 -26.943 18.730 1.00 20.78 C ANISOU 1009 CE LYS A 133 3237 1952 2703 276 86 -654 C ATOM 1010 NZ LYS A 133 -7.931 -27.730 18.667 1.00 21.87 N ANISOU 1010 NZ LYS A 133 3433 1975 2901 191 -15 -699 N ATOM 1011 N GLU A 134 -4.594 -27.515 24.875 1.00 17.75 N ANISOU 1011 N GLU A 134 2516 1501 2724 358 88 -84 N ATOM 1012 CA GLU A 134 -3.557 -28.091 25.739 1.00 18.34 C ANISOU 1012 CA GLU A 134 2534 1546 2885 437 97 1 C ATOM 1013 C GLU A 134 -3.333 -27.210 26.955 1.00 17.06 C ANISOU 1013 C GLU A 134 2296 1508 2675 408 73 121 C ATOM 1014 O GLU A 134 -3.631 -26.020 26.938 1.00 15.68 O ANISOU 1014 O GLU A 134 2107 1446 2401 352 73 112 O ATOM 1015 CB GLU A 134 -2.225 -28.192 25.017 1.00 19.38 C ANISOU 1015 CB GLU A 134 2639 1693 3031 548 164 -59 C ATOM 1016 CG GLU A 134 -2.178 -29.222 23.965 1.00 21.02 C ANISOU 1016 CG GLU A 134 2923 1770 3291 612 196 -184 C ATOM 1017 CD GLU A 134 -0.833 -29.270 23.296 1.00 22.16 C ANISOU 1017 CD GLU A 134 3026 1952 3440 737 284 -238 C ATOM 1018 OE1 GLU A 134 0.054 -30.027 23.766 1.00 23.59 O ANISOU 1018 OE1 GLU A 134 3157 2068 3737 838 300 -189 O ATOM 1019 OE2 GLU A 134 -0.662 -28.536 22.294 1.00 22.35 O ANISOU 1019 OE2 GLU A 134 3060 2078 3354 738 340 -320 O ATOM 1020 N GLY A 135 -2.770 -27.820 27.989 1.00 17.46 N ANISOU 1020 N GLY A 135 2303 1532 2796 452 50 229 N ATOM 1021 CA GLY A 135 -2.385 -27.100 29.185 1.00 16.92 C ANISOU 1021 CA GLY A 135 2168 1586 2674 437 17 334 C ATOM 1022 C GLY A 135 -3.532 -26.714 30.109 1.00 16.19 C ANISOU 1022 C GLY A 135 2095 1542 2515 350 -19 402 C ATOM 1023 O GLY A 135 -3.403 -25.742 30.841 1.00 15.64 O ANISOU 1023 O GLY A 135 1991 1596 2355 323 -38 435 O ATOM 1024 N MET A 136 -4.633 -27.471 30.116 1.00 16.32 N ANISOU 1024 N MET A 136 2161 1462 2577 305 -27 421 N ATOM 1025 CA MET A 136 -5.653 -27.260 31.133 1.00 16.04 C ANISOU 1025 CA MET A 136 2123 1480 2489 236 -47 514 C ATOM 1026 C MET A 136 -5.051 -27.549 32.498 1.00 16.36 C ANISOU 1026 C MET A 136 2123 1571 2520 271 -76 655 C ATOM 1027 O MET A 136 -5.466 -26.968 33.492 1.00 16.06 O ANISOU 1027 O MET A 136 2072 1646 2382 237 -87 722 O ATOM 1028 CB MET A 136 -6.903 -28.114 30.903 1.00 16.81 C ANISOU 1028 CB MET A 136 2261 1463 2662 174 -52 530 C ATOM 1029 CG MET A 136 -8.099 -27.675 31.749 1.00 16.77 C ANISOU 1029 CG MET A 136 2239 1542 2590 98 -50 612 C ATOM 1030 SD MET A 136 -8.650 -25.968 31.412 1.00 15.98 S ANISOU 1030 SD MET A 136 2130 1590 2349 62 -29 515 S ATOM 1031 CE MET A 136 -9.420 -25.527 32.985 1.00 16.06 C ANISOU 1031 CE MET A 136 2107 1730 2265 34 -13 641 C ATOM 1032 N ASN A 137 -4.053 -28.415 32.555 1.00 17.03 N ANISOU 1032 N ASN A 137 2187 1582 2700 349 -90 700 N ATOM 1033 CA ASN A 137 -3.305 -28.602 33.804 1.00 17.76 C ANISOU 1033 CA ASN A 137 2230 1742 2773 392 -133 840 C ATOM 1034 C ASN A 137 -2.595 -27.309 34.243 1.00 17.14 C ANISOU 1034 C ASN A 137 2106 1839 2567 392 -157 813 C ATOM 1035 O ASN A 137 -2.470 -27.051 35.436 1.00 17.61 O ANISOU 1035 O ASN A 137 2144 2006 2537 385 -201 908 O ATOM 1036 CB ASN A 137 -2.310 -29.775 33.708 1.00 18.97 C ANISOU 1036 CB ASN A 137 2359 1775 3073 490 -147 897 C ATOM 1037 CG ASN A 137 -1.187 -29.517 32.729 1.00 18.78 C ANISOU 1037 CG ASN A 137 2297 1747 3090 564 -119 784 C ATOM 1038 OD1 ASN A 137 -1.411 -29.039 31.634 1.00 17.78 O ANISOU 1038 OD1 ASN A 137 2200 1612 2943 543 -74 643 O ATOM 1039 ND2 ASN A 137 0.028 -29.874 33.113 1.00 19.79 N ANISOU 1039 ND2 ASN A 137 2352 1887 3278 656 -145 857 N ATOM 1040 N ILE A 138 -2.165 -26.483 33.290 1.00 16.31 N ANISOU 1040 N ILE A 138 1988 1761 2446 393 -131 684 N ATOM 1041 CA ILE A 138 -1.474 -25.247 33.621 1.00 15.99 C ANISOU 1041 CA ILE A 138 1902 1860 2312 379 -160 654 C ATOM 1042 C ILE A 138 -2.464 -24.213 34.185 1.00 15.47 C ANISOU 1042 C ILE A 138 1876 1887 2112 302 -165 629 C ATOM 1043 O ILE A 138 -2.095 -23.442 35.080 1.00 15.56 O ANISOU 1043 O ILE A 138 1868 2013 2029 287 -214 646 O ATOM 1044 CB ILE A 138 -0.715 -24.639 32.387 1.00 15.43 C ANISOU 1044 CB ILE A 138 1799 1789 2275 396 -121 541 C ATOM 1045 CG1 ILE A 138 0.380 -25.589 31.904 1.00 16.45 C ANISOU 1045 CG1 ILE A 138 1873 1849 2528 492 -103 561 C ATOM 1046 CG2 ILE A 138 -0.132 -23.278 32.712 1.00 14.95 C ANISOU 1046 CG2 ILE A 138 1691 1854 2132 357 -157 513 C ATOM 1047 CD1 ILE A 138 1.325 -26.089 32.990 1.00 17.63 C ANISOU 1047 CD1 ILE A 138 1948 2036 2715 549 -169 689 C ATOM 1048 N VAL A 139 -3.691 -24.203 33.657 1.00 15.09 N ANISOU 1048 N VAL A 139 1883 1789 2061 258 -120 584 N ATOM 1049 CA VAL A 139 -4.766 -23.341 34.172 1.00 14.93 C ANISOU 1049 CA VAL A 139 1894 1846 1932 201 -111 567 C ATOM 1050 C VAL A 139 -5.125 -23.693 35.603 1.00 16.06 C ANISOU 1050 C VAL A 139 2041 2058 2002 200 -132 687 C ATOM 1051 O VAL A 139 -5.251 -22.807 36.451 1.00 16.25 O ANISOU 1051 O VAL A 139 2074 2199 1902 187 -147 677 O ATOM 1052 CB VAL A 139 -6.042 -23.402 33.284 1.00 14.36 C ANISOU 1052 CB VAL A 139 1859 1705 1891 158 -63 514 C ATOM 1053 CG1 VAL A 139 -7.142 -22.504 33.835 1.00 13.90 C ANISOU 1053 CG1 VAL A 139 1816 1731 1734 117 -45 505 C ATOM 1054 CG2 VAL A 139 -5.706 -22.985 31.833 1.00 13.71 C ANISOU 1054 CG2 VAL A 139 1783 1576 1848 161 -43 398 C ATOM 1055 N GLU A 140 -5.272 -24.988 35.869 1.00 17.35 N ANISOU 1055 N GLU A 140 2202 2146 2241 217 -131 799 N ATOM 1056 CA GLU A 140 -5.521 -25.495 37.206 1.00 18.64 C ANISOU 1056 CA GLU A 140 2364 2374 2342 221 -148 947 C ATOM 1057 C GLU A 140 -4.382 -25.128 38.165 1.00 19.27 C ANISOU 1057 C GLU A 140 2418 2573 2330 261 -217 988 C ATOM 1058 O GLU A 140 -4.619 -24.858 39.337 1.00 19.47 O ANISOU 1058 O GLU A 140 2456 2723 2216 255 -235 1055 O ATOM 1059 CB GLU A 140 -5.697 -27.012 37.180 1.00 20.03 C ANISOU 1059 CB GLU A 140 2539 2417 2654 233 -143 1071 C ATOM 1060 CG GLU A 140 -7.008 -27.489 36.555 1.00 20.26 C ANISOU 1060 CG GLU A 140 2591 2341 2763 173 -93 1062 C ATOM 1061 CD GLU A 140 -7.080 -29.009 36.463 1.00 22.11 C ANISOU 1061 CD GLU A 140 2830 2409 3161 178 -102 1173 C ATOM 1062 OE1 GLU A 140 -6.403 -29.702 37.257 1.00 23.91 O ANISOU 1062 OE1 GLU A 140 3042 2632 3411 225 -136 1309 O ATOM 1063 OE2 GLU A 140 -7.820 -29.542 35.609 1.00 22.69 O ANISOU 1063 OE2 GLU A 140 2923 2349 3348 133 -84 1129 O ATOM 1064 N ALA A 141 -3.143 -25.135 37.667 1.00 19.37 N ANISOU 1064 N ALA A 141 2389 2556 2416 302 -258 950 N ATOM 1065 CA ALA A 141 -2.008 -24.834 38.524 1.00 20.40 C ANISOU 1065 CA ALA A 141 2475 2796 2478 332 -342 995 C ATOM 1066 C ALA A 141 -2.044 -23.348 38.882 1.00 20.00 C ANISOU 1066 C ALA A 141 2444 2873 2283 287 -367 884 C ATOM 1067 O ALA A 141 -1.667 -22.975 39.980 1.00 20.65 O ANISOU 1067 O ALA A 141 2525 3081 2240 287 -437 920 O ATOM 1068 CB ALA A 141 -0.681 -25.241 37.876 1.00 20.54 C ANISOU 1068 CB ALA A 141 2421 2752 2631 391 -372 993 C ATOM 1069 N MET A 142 -2.544 -22.508 37.976 1.00 19.36 N ANISOU 1069 N MET A 142 2386 2755 2214 249 -315 750 N ATOM 1070 CA MET A 142 -2.711 -21.069 38.274 1.00 19.39 C ANISOU 1070 CA MET A 142 2419 2848 2100 208 -332 639 C ATOM 1071 C MET A 142 -3.629 -20.836 39.487 1.00 20.15 C ANISOU 1071 C MET A 142 2572 3050 2034 199 -324 670 C ATOM 1072 O MET A 142 -3.362 -19.962 40.319 1.00 20.89 O ANISOU 1072 O MET A 142 2689 3250 1997 189 -379 619 O ATOM 1073 CB MET A 142 -3.223 -20.298 37.048 1.00 18.47 C ANISOU 1073 CB MET A 142 2319 2658 2037 176 -272 516 C ATOM 1074 CG MET A 142 -2.216 -20.204 35.904 1.00 18.32 C ANISOU 1074 CG MET A 142 2246 2575 2136 181 -275 471 C ATOM 1075 SD MET A 142 -2.987 -19.759 34.321 1.00 17.95 S ANISOU 1075 SD MET A 142 2230 2437 2154 155 -191 372 S ATOM 1076 CE MET A 142 -3.602 -18.141 34.779 1.00 17.10 C ANISOU 1076 CE MET A 142 2166 2391 1939 108 -204 282 C ATOM 1077 N GLU A 143 -4.671 -21.652 39.616 1.00 20.52 N ANISOU 1077 N GLU A 143 2638 3068 2088 204 -257 756 N ATOM 1078 CA GLU A 143 -5.673 -21.492 40.677 1.00 21.32 C ANISOU 1078 CA GLU A 143 2783 3277 2039 201 -218 799 C ATOM 1079 C GLU A 143 -5.050 -21.469 42.066 1.00 22.53 C ANISOU 1079 C GLU A 143 2950 3576 2034 224 -292 866 C ATOM 1080 O GLU A 143 -5.547 -20.786 42.966 1.00 23.03 O ANISOU 1080 O GLU A 143 3061 3764 1923 227 -280 829 O ATOM 1081 CB GLU A 143 -6.723 -22.601 40.591 1.00 22.02 C ANISOU 1081 CB GLU A 143 2864 3305 2194 194 -142 922 C ATOM 1082 CG GLU A 143 -7.642 -22.501 39.342 1.00 21.23 C ANISOU 1082 CG GLU A 143 2761 3091 2215 161 -74 845 C ATOM 1083 CD GLU A 143 -8.824 -23.441 39.438 1.00 22.18 C ANISOU 1083 CD GLU A 143 2868 3173 2386 136 -7 964 C ATOM 1084 OE1 GLU A 143 -8.639 -24.600 39.842 1.00 23.93 O ANISOU 1084 OE1 GLU A 143 3076 3358 2659 141 -21 1110 O ATOM 1085 OE2 GLU A 143 -9.961 -23.025 39.151 1.00 22.54 O ANISOU 1085 OE2 GLU A 143 2909 3225 2427 109 55 924 O ATOM 1086 N ARG A 144 -3.942 -22.185 42.234 1.00 22.83 N ANISOU 1086 N ARG A 144 2944 3604 2125 248 -372 957 N ATOM 1087 CA ARG A 144 -3.284 -22.228 43.524 1.00 24.26 C ANISOU 1087 CA ARG A 144 3130 3931 2154 270 -463 1036 C ATOM 1088 C ARG A 144 -2.969 -20.830 44.000 1.00 24.08 C ANISOU 1088 C ARG A 144 3146 4018 1983 248 -525 880 C ATOM 1089 O ARG A 144 -2.907 -20.590 45.186 1.00 25.45 O ANISOU 1089 O ARG A 144 3361 4342 1965 258 -577 901 O ATOM 1090 CB ARG A 144 -1.985 -23.042 43.478 1.00 25.08 C ANISOU 1090 CB ARG A 144 3162 4001 2366 303 -557 1141 C ATOM 1091 CG ARG A 144 -1.287 -23.075 44.828 1.00 27.06 C ANISOU 1091 CG ARG A 144 3412 4417 2450 324 -672 1233 C ATOM 1092 CD ARG A 144 -0.300 -24.186 44.948 1.00 28.25 C ANISOU 1092 CD ARG A 144 3487 4535 2711 374 -747 1400 C ATOM 1093 NE ARG A 144 0.859 -23.970 44.073 1.00 27.95 N ANISOU 1093 NE ARG A 144 3363 4422 2834 382 -802 1325 N ATOM 1094 CZ ARG A 144 2.135 -24.137 44.437 1.00 29.21 C ANISOU 1094 CZ ARG A 144 3439 4639 3019 412 -926 1392 C ATOM 1095 NH1 ARG A 144 2.441 -24.543 45.651 1.00 31.03 N ANISOU 1095 NH1 ARG A 144 3669 5001 3118 439 -1023 1537 N ATOM 1096 NH2 ARG A 144 3.116 -23.924 43.567 1.00 28.81 N ANISOU 1096 NH2 ARG A 144 3295 4522 3126 419 -953 1328 N ATOM 1097 N PHE A 145 -2.766 -19.912 43.060 1.00 22.52 N ANISOU 1097 N PHE A 145 2940 3741 1874 216 -523 723 N ATOM 1098 CA PHE A 145 -2.377 -18.538 43.387 1.00 22.44 C ANISOU 1098 CA PHE A 145 2965 3795 1765 185 -593 565 C ATOM 1099 C PHE A 145 -3.547 -17.546 43.473 1.00 21.80 C ANISOU 1099 C PHE A 145 2965 3727 1589 178 -511 434 C ATOM 1100 O PHE A 145 -3.337 -16.352 43.726 1.00 21.91 O ANISOU 1100 O PHE A 145 3023 3769 1531 156 -563 286 O ATOM 1101 CB PHE A 145 -1.298 -18.103 42.403 1.00 21.69 C ANISOU 1101 CB PHE A 145 2800 3609 1830 152 -651 496 C ATOM 1102 CG PHE A 145 -0.111 -19.023 42.410 1.00 22.33 C ANISOU 1102 CG PHE A 145 2789 3694 2001 175 -729 620 C ATOM 1103 CD1 PHE A 145 0.710 -19.091 43.523 1.00 23.89 C ANISOU 1103 CD1 PHE A 145 2968 4020 2089 179 -858 677 C ATOM 1104 CD2 PHE A 145 0.141 -19.872 41.351 1.00 21.53 C ANISOU 1104 CD2 PHE A 145 2620 3472 2085 201 -673 685 C ATOM 1105 CE1 PHE A 145 1.784 -19.964 43.568 1.00 24.67 C ANISOU 1105 CE1 PHE A 145 2968 4125 2279 213 -933 808 C ATOM 1106 CE2 PHE A 145 1.234 -20.748 41.391 1.00 22.34 C ANISOU 1106 CE2 PHE A 145 2633 3574 2281 242 -737 801 C ATOM 1107 CZ PHE A 145 2.049 -20.783 42.501 1.00 23.88 C ANISOU 1107 CZ PHE A 145 2796 3896 2381 249 -867 870 C ATOM 1108 N GLY A 146 -4.771 -18.053 43.307 1.00 21.04 N ANISOU 1108 N GLY A 146 2884 3608 1500 200 -388 493 N ATOM 1109 CA GLY A 146 -5.975 -17.237 43.443 1.00 20.94 C ANISOU 1109 CA GLY A 146 2931 3620 1405 211 -296 395 C ATOM 1110 C GLY A 146 -6.577 -17.299 44.843 1.00 22.48 C ANISOU 1110 C GLY A 146 3182 3982 1375 251 -264 437 C ATOM 1111 O GLY A 146 -5.988 -17.836 45.759 1.00 23.80 O ANISOU 1111 O GLY A 146 3355 4256 1429 263 -332 532 O ATOM 1112 N SER A 147 -7.768 -16.751 44.995 1.00 22.62 N ANISOU 1112 N SER A 147 3238 4031 1325 279 -156 375 N ATOM 1113 CA SER A 147 -8.489 -16.784 46.262 1.00 24.41 C ANISOU 1113 CA SER A 147 3515 4428 1329 328 -90 413 C ATOM 1114 C SER A 147 -9.974 -16.614 45.984 1.00 24.41 C ANISOU 1114 C SER A 147 3501 4418 1355 357 66 408 C ATOM 1115 O SER A 147 -10.377 -16.304 44.852 1.00 22.88 O ANISOU 1115 O SER A 147 3270 4086 1335 338 100 350 O ATOM 1116 CB SER A 147 -8.013 -15.651 47.166 1.00 25.55 C ANISOU 1116 CB SER A 147 3753 4677 1278 349 -166 243 C ATOM 1117 OG SER A 147 -8.336 -14.418 46.565 1.00 24.73 O ANISOU 1117 OG SER A 147 3680 4475 1240 352 -144 51 O ATOM 1118 N ARG A 148 -10.785 -16.772 47.028 1.00 26.47 N ANISOU 1118 N ARG A 148 3786 4838 1434 407 161 470 N ATOM 1119 CA ARG A 148 -12.241 -16.667 46.895 1.00 26.93 C ANISOU 1119 CA ARG A 148 3808 4914 1509 442 321 489 C ATOM 1120 C ARG A 148 -12.665 -15.275 46.441 1.00 26.39 C ANISOU 1120 C ARG A 148 3774 4783 1469 478 351 274 C ATOM 1121 O ARG A 148 -13.663 -15.146 45.766 1.00 25.92 O ANISOU 1121 O ARG A 148 3656 4661 1528 489 446 278 O ATOM 1122 CB ARG A 148 -12.940 -17.046 48.207 1.00 29.59 C ANISOU 1122 CB ARG A 148 4161 5460 1621 495 427 602 C ATOM 1123 CG ARG A 148 -14.122 -17.984 48.005 1.00 30.10 C ANISOU 1123 CG ARG A 148 4123 5530 1782 481 564 797 C ATOM 1124 CD ARG A 148 -14.696 -18.427 49.324 1.00 32.92 C ANISOU 1124 CD ARG A 148 4487 6107 1913 528 671 940 C ATOM 1125 NE ARG A 148 -13.708 -19.107 50.178 1.00 34.26 N ANISOU 1125 NE ARG A 148 4705 6370 1940 515 573 1057 N ATOM 1126 CZ ARG A 148 -13.780 -19.157 51.506 1.00 36.83 C ANISOU 1126 CZ ARG A 148 5087 6920 1986 568 617 1122 C ATOM 1127 NH1 ARG A 148 -14.802 -18.576 52.147 1.00 38.52 N ANISOU 1127 NH1 ARG A 148 5316 7290 2030 644 773 1073 N ATOM 1128 NH2 ARG A 148 -12.831 -19.785 52.207 1.00 37.84 N ANISOU 1128 NH2 ARG A 148 5253 7127 1996 555 507 1240 N ATOM 1129 N ASN A 149 -11.883 -14.250 46.772 1.00 26.66 N ANISOU 1129 N ASN A 149 3897 4820 1410 492 259 93 N ATOM 1130 CA ASN A 149 -12.154 -12.874 46.337 1.00 26.35 C ANISOU 1130 CA ASN A 149 3902 4691 1419 525 269 -114 C ATOM 1131 C ASN A 149 -11.523 -12.505 44.978 1.00 24.21 C ANISOU 1131 C ASN A 149 3599 4218 1379 458 179 -171 C ATOM 1132 O ASN A 149 -11.841 -11.459 44.410 1.00 23.65 O ANISOU 1132 O ASN A 149 3547 4046 1391 477 194 -306 O ATOM 1133 CB ASN A 149 -11.658 -11.899 47.409 1.00 28.36 C ANISOU 1133 CB ASN A 149 4278 5036 1459 568 209 -294 C ATOM 1134 CG ASN A 149 -10.198 -11.591 47.257 1.00 28.18 C ANISOU 1134 CG ASN A 149 4291 4941 1474 494 24 -372 C ATOM 1135 OD1 ASN A 149 -9.336 -12.192 47.889 1.00 29.10 O ANISOU 1135 OD1 ASN A 149 4418 5151 1488 462 -72 -299 O ATOM 1136 ND2 ASN A 149 -9.903 -10.683 46.362 1.00 27.59 N ANISOU 1136 ND2 ASN A 149 4221 4698 1563 462 -28 -500 N ATOM 1137 N GLY A 150 -10.606 -13.345 44.486 1.00 22.84 N ANISOU 1137 N GLY A 150 3379 3991 1305 387 90 -66 N ATOM 1138 CA GLY A 150 -9.954 -13.129 43.204 1.00 21.03 C ANISOU 1138 CA GLY A 150 3113 3597 1279 327 19 -99 C ATOM 1139 C GLY A 150 -8.497 -12.658 43.244 1.00 20.98 C ANISOU 1139 C GLY A 150 3135 3556 1279 277 -129 -179 C ATOM 1140 O GLY A 150 -7.771 -12.862 42.270 1.00 19.62 O ANISOU 1140 O GLY A 150 2910 3279 1264 223 -184 -149 O ATOM 1141 N LYS A 151 -8.076 -12.030 44.341 1.00 22.43 N ANISOU 1141 N LYS A 151 3397 3832 1292 293 -194 -283 N ATOM 1142 CA LYS A 151 -6.712 -11.512 44.477 1.00 23.01 C ANISOU 1142 CA LYS A 151 3490 3881 1369 235 -351 -365 C ATOM 1143 C LYS A 151 -5.709 -12.623 44.291 1.00 22.46 C ANISOU 1143 C LYS A 151 3341 3828 1364 191 -427 -213 C ATOM 1144 O LYS A 151 -5.881 -13.711 44.871 1.00 22.85 O ANISOU 1144 O LYS A 151 3371 3980 1329 218 -399 -68 O ATOM 1145 CB LYS A 151 -6.402 -10.979 45.891 1.00 25.30 C ANISOU 1145 CB LYS A 151 3878 4306 1427 257 -427 -476 C ATOM 1146 CG LYS A 151 -7.066 -9.693 46.380 1.00 26.70 C ANISOU 1146 CG LYS A 151 4164 4478 1503 308 -390 -681 C ATOM 1147 CD LYS A 151 -7.249 -8.608 45.326 1.00 25.93 C ANISOU 1147 CD LYS A 151 4067 4184 1599 289 -378 -800 C ATOM 1148 CE LYS A 151 -8.127 -7.474 45.873 1.00 27.41 C ANISOU 1148 CE LYS A 151 4361 4364 1689 370 -312 -987 C ATOM 1149 NZ LYS A 151 -9.220 -7.119 44.908 1.00 26.36 N ANISOU 1149 NZ LYS A 151 4190 4111 1712 418 -181 -981 N ATOM 1150 N THR A 152 -4.639 -12.324 43.559 1.00 21.63 N ANISOU 1150 N THR A 152 3187 3627 1402 127 -522 -240 N ATOM 1151 CA THR A 152 -3.542 -13.254 43.401 1.00 21.44 C ANISOU 1151 CA THR A 152 3080 3618 1448 96 -602 -112 C ATOM 1152 C THR A 152 -2.466 -12.957 44.449 1.00 23.13 C ANISOU 1152 C THR A 152 3312 3936 1539 67 -760 -154 C ATOM 1153 O THR A 152 -2.274 -11.808 44.847 1.00 24.09 O ANISOU 1153 O THR A 152 3498 4056 1599 39 -832 -315 O ATOM 1154 CB THR A 152 -2.994 -13.244 41.961 1.00 19.90 C ANISOU 1154 CB THR A 152 2802 3279 1480 53 -598 -94 C ATOM 1155 OG1 THR A 152 -2.418 -11.977 41.664 1.00 20.10 O ANISOU 1155 OG1 THR A 152 2839 3235 1563 -3 -671 -228 O ATOM 1156 CG2 THR A 152 -4.129 -13.496 40.970 1.00 18.41 C ANISOU 1156 CG2 THR A 152 2608 3002 1384 79 -459 -65 C ATOM 1157 N SER A 153 -1.829 -14.018 44.947 1.00 23.72 N ANISOU 1157 N SER A 153 3335 4102 1575 78 -819 -7 N ATOM 1158 CA SER A 153 -0.777 -13.913 45.965 1.00 25.51 C ANISOU 1158 CA SER A 153 3561 4449 1680 53 -986 -15 C ATOM 1159 C SER A 153 0.590 -13.896 45.305 1.00 25.27 C ANISOU 1159 C SER A 153 3415 4354 1830 -7 -1099 11 C ATOM 1160 O SER A 153 1.568 -13.576 45.938 1.00 26.54 O ANISOU 1160 O SER A 153 3556 4590 1938 -49 -1256 -18 O ATOM 1161 CB SER A 153 -0.873 -15.060 46.986 1.00 26.59 C ANISOU 1161 CB SER A 153 3704 4740 1658 108 -994 150 C ATOM 1162 OG SER A 153 -0.866 -16.325 46.345 1.00 25.72 O ANISOU 1162 OG SER A 153 3506 4569 1695 136 -927 336 O ATOM 1163 N LYS A 154 0.650 -14.243 44.021 1.00 23.89 N ANISOU 1163 N LYS A 154 3160 4050 1867 -10 -1016 67 N ATOM 1164 CA LYS A 154 1.844 -14.010 43.228 1.00 23.78 C ANISOU 1164 CA LYS A 154 3033 3966 2034 -66 -1089 71 C ATOM 1165 C LYS A 154 1.466 -13.426 41.874 1.00 22.31 C ANISOU 1165 C LYS A 154 2837 3628 2009 -91 -983 6 C ATOM 1166 O LYS A 154 0.305 -13.454 41.487 1.00 21.46 O ANISOU 1166 O LYS A 154 2793 3468 1890 -55 -857 -13 O ATOM 1167 CB LYS A 154 2.645 -15.301 43.094 1.00 23.99 C ANISOU 1167 CB LYS A 154 2944 4023 2148 -27 -1111 249 C ATOM 1168 CG LYS A 154 3.006 -15.869 44.456 1.00 25.82 C ANISOU 1168 CG LYS A 154 3185 4411 2214 0 -1225 335 C ATOM 1169 CD LYS A 154 4.220 -16.783 44.452 1.00 26.68 C ANISOU 1169 CD LYS A 154 3154 4555 2426 22 -1313 489 C ATOM 1170 CE LYS A 154 4.535 -17.216 45.854 1.00 28.60 C ANISOU 1170 CE LYS A 154 3416 4966 2486 45 -1443 576 C ATOM 1171 NZ LYS A 154 5.841 -17.876 45.863 1.00 29.79 N ANISOU 1171 NZ LYS A 154 3415 5152 2752 62 -1556 711 N ATOM 1172 N LYS A 155 2.447 -12.876 41.168 1.00 22.34 N ANISOU 1172 N LYS A 155 2754 3572 2162 -155 -1038 -16 N ATOM 1173 CA LYS A 155 2.191 -12.256 39.884 1.00 21.19 C ANISOU 1173 CA LYS A 155 2596 3294 2158 -184 -948 -62 C ATOM 1174 C LYS A 155 2.192 -13.323 38.784 1.00 19.67 C ANISOU 1174 C LYS A 155 2330 3056 2087 -132 -835 54 C ATOM 1175 O LYS A 155 3.227 -13.925 38.480 1.00 19.82 O ANISOU 1175 O LYS A 155 2235 3094 2202 -127 -864 143 O ATOM 1176 CB LYS A 155 3.219 -11.156 39.604 1.00 22.32 C ANISOU 1176 CB LYS A 155 2677 3393 2407 -283 -1048 -127 C ATOM 1177 CG LYS A 155 2.855 -10.307 38.379 1.00 21.77 C ANISOU 1177 CG LYS A 155 2617 3189 2463 -319 -959 -175 C ATOM 1178 CD LYS A 155 3.669 -9.037 38.354 1.00 23.22 C ANISOU 1178 CD LYS A 155 2770 3318 2734 -430 -1068 -251 C ATOM 1179 CE LYS A 155 3.542 -8.287 37.035 1.00 22.72 C ANISOU 1179 CE LYS A 155 2687 3126 2819 -471 -983 -252 C ATOM 1180 NZ LYS A 155 4.885 -7.653 36.753 1.00 24.09 N ANISOU 1180 NZ LYS A 155 2736 3278 3138 -581 -1079 -226 N ATOM 1181 N ILE A 156 1.007 -13.570 38.230 1.00 18.21 N ANISOU 1181 N ILE A 156 2210 2813 1893 -90 -709 49 N ATOM 1182 CA ILE A 156 0.796 -14.542 37.163 1.00 16.89 C ANISOU 1182 CA ILE A 156 2003 2590 1824 -44 -602 130 C ATOM 1183 C ILE A 156 0.752 -13.769 35.850 1.00 15.95 C ANISOU 1183 C ILE A 156 1870 2378 1811 -81 -540 81 C ATOM 1184 O ILE A 156 -0.177 -12.999 35.632 1.00 15.50 O ANISOU 1184 O ILE A 156 1888 2273 1726 -95 -500 8 O ATOM 1185 CB ILE A 156 -0.552 -15.303 37.381 1.00 16.27 C ANISOU 1185 CB ILE A 156 2001 2508 1669 11 -516 160 C ATOM 1186 CG1 ILE A 156 -0.652 -15.857 38.812 1.00 17.32 C ANISOU 1186 CG1 ILE A 156 2165 2747 1666 41 -572 213 C ATOM 1187 CG2 ILE A 156 -0.743 -16.419 36.363 1.00 15.38 C ANISOU 1187 CG2 ILE A 156 1856 2330 1658 53 -427 234 C ATOM 1188 CD1 ILE A 156 0.630 -16.510 39.341 1.00 18.36 C ANISOU 1188 CD1 ILE A 156 2214 2945 1817 52 -671 304 C ATOM 1189 N THR A 157 1.752 -13.964 34.990 1.00 15.89 N ANISOU 1189 N THR A 157 1763 2353 1922 -90 -530 129 N ATOM 1190 CA THR A 157 1.877 -13.229 33.721 1.00 15.29 C ANISOU 1190 CA THR A 157 1662 2208 1938 -128 -471 105 C ATOM 1191 C THR A 157 1.831 -14.100 32.434 1.00 14.47 C ANISOU 1191 C THR A 157 1525 2070 1900 -75 -357 157 C ATOM 1192 O THR A 157 2.159 -15.277 32.445 1.00 14.52 O ANISOU 1192 O THR A 157 1493 2097 1927 -13 -337 217 O ATOM 1193 CB THR A 157 3.215 -12.431 33.668 1.00 16.37 C ANISOU 1193 CB THR A 157 1695 2361 2162 -203 -547 112 C ATOM 1194 OG1 THR A 157 4.328 -13.333 33.786 1.00 17.15 O ANISOU 1194 OG1 THR A 157 1676 2523 2317 -169 -574 199 O ATOM 1195 CG2 THR A 157 3.297 -11.387 34.759 1.00 17.25 C ANISOU 1195 CG2 THR A 157 1849 2483 2221 -272 -670 33 C ATOM 1196 N ILE A 158 1.463 -13.467 31.322 1.00 13.71 N ANISOU 1196 N ILE A 158 1450 1920 1836 -99 -289 132 N ATOM 1197 CA ILE A 158 1.642 -14.020 29.992 1.00 13.35 C ANISOU 1197 CA ILE A 158 1370 1857 1842 -62 -192 166 C ATOM 1198 C ILE A 158 3.065 -13.612 29.539 1.00 14.27 C ANISOU 1198 C ILE A 158 1362 2008 2051 -95 -195 213 C ATOM 1199 O ILE A 158 3.271 -12.500 28.987 1.00 14.46 O ANISOU 1199 O ILE A 158 1369 2012 2113 -163 -189 211 O ATOM 1200 CB ILE A 158 0.538 -13.500 29.016 1.00 12.43 C ANISOU 1200 CB ILE A 158 1336 1688 1699 -73 -125 130 C ATOM 1201 CG1 ILE A 158 -0.838 -13.932 29.513 1.00 11.73 C ANISOU 1201 CG1 ILE A 158 1342 1577 1537 -43 -123 97 C ATOM 1202 CG2 ILE A 158 0.758 -14.010 27.592 1.00 12.46 C ANISOU 1202 CG2 ILE A 158 1315 1689 1729 -37 -29 156 C ATOM 1203 CD1 ILE A 158 -1.979 -13.345 28.787 1.00 11.04 C ANISOU 1203 CD1 ILE A 158 1323 1446 1426 -54 -83 66 C ATOM 1204 N ALA A 159 4.039 -14.488 29.825 1.00 14.84 N ANISOU 1204 N ALA A 159 1340 2129 2169 -49 -208 266 N ATOM 1205 CA ALA A 159 5.446 -14.209 29.552 1.00 16.04 C ANISOU 1205 CA ALA A 159 1344 2330 2419 -74 -216 325 C ATOM 1206 C ALA A 159 5.675 -14.181 28.044 1.00 16.14 C ANISOU 1206 C ALA A 159 1322 2341 2470 -53 -85 348 C ATOM 1207 O ALA A 159 6.539 -13.458 27.554 1.00 16.86 O ANISOU 1207 O ALA A 159 1311 2462 2633 -108 -68 394 O ATOM 1208 CB ALA A 159 6.370 -15.253 30.199 1.00 16.82 C ANISOU 1208 CB ALA A 159 1341 2485 2563 -8 -256 386 C ATOM 1209 N ASP A 160 4.914 -14.994 27.320 1.00 15.57 N ANISOU 1209 N ASP A 160 1331 2237 2346 21 4 319 N ATOM 1210 CA ASP A 160 4.973 -15.006 25.835 1.00 15.75 C ANISOU 1210 CA ASP A 160 1350 2269 2365 49 130 325 C ATOM 1211 C ASP A 160 3.639 -15.477 25.324 1.00 14.70 C ANISOU 1211 C ASP A 160 1359 2081 2144 86 171 261 C ATOM 1212 O ASP A 160 2.899 -16.132 26.051 1.00 13.95 O ANISOU 1212 O ASP A 160 1335 1947 2019 111 124 228 O ATOM 1213 CB ASP A 160 6.081 -15.930 25.334 1.00 16.90 C ANISOU 1213 CB ASP A 160 1382 2466 2572 140 211 366 C ATOM 1214 CG ASP A 160 6.494 -15.638 23.879 1.00 17.78 C ANISOU 1214 CG ASP A 160 1453 2624 2677 154 343 389 C ATOM 1215 OD1 ASP A 160 6.057 -14.622 23.278 1.00 17.63 O ANISOU 1215 OD1 ASP A 160 1479 2602 2617 79 361 396 O ATOM 1216 OD2 ASP A 160 7.282 -16.431 23.330 1.00 18.82 O ANISOU 1216 OD2 ASP A 160 1506 2801 2842 248 436 407 O ATOM 1217 N CYS A 161 3.316 -15.093 24.098 1.00 14.79 N ANISOU 1217 N CYS A 161 1408 2098 2112 79 251 253 N ATOM 1218 CA CYS A 161 2.118 -15.568 23.426 1.00 14.25 C ANISOU 1218 CA CYS A 161 1462 1990 1960 111 285 194 C ATOM 1219 C CYS A 161 2.206 -15.396 21.907 1.00 14.99 C ANISOU 1219 C CYS A 161 1569 2127 2000 129 388 198 C ATOM 1220 O CYS A 161 3.089 -14.707 21.388 1.00 15.60 O ANISOU 1220 O CYS A 161 1561 2261 2102 103 439 261 O ATOM 1221 CB CYS A 161 0.863 -14.881 23.968 1.00 13.31 C ANISOU 1221 CB CYS A 161 1433 1820 1801 50 211 167 C ATOM 1222 SG CYS A 161 0.948 -13.078 23.990 1.00 13.42 S ANISOU 1222 SG CYS A 161 1427 1831 1840 -50 174 207 S ATOM 1223 N GLY A 162 1.296 -16.052 21.196 1.00 15.00 N ANISOU 1223 N GLY A 162 1672 2105 1922 169 416 135 N ATOM 1224 CA GLY A 162 1.294 -15.994 19.739 1.00 15.95 C ANISOU 1224 CA GLY A 162 1823 2277 1956 194 507 126 C ATOM 1225 C GLY A 162 0.369 -16.998 19.092 1.00 16.18 C ANISOU 1225 C GLY A 162 1967 2275 1904 246 516 32 C ATOM 1226 O GLY A 162 -0.443 -17.640 19.765 1.00 15.41 O ANISOU 1226 O GLY A 162 1925 2101 1827 246 446 -14 O ATOM 1227 N GLN A 163 0.501 -17.141 17.781 1.00 17.51 N ANISOU 1227 N GLN A 163 2170 2505 1977 286 600 7 N ATOM 1228 CA GLN A 163 -0.353 -18.042 17.017 1.00 18.28 C ANISOU 1228 CA GLN A 163 2385 2578 1983 326 599 -97 C ATOM 1229 C GLN A 163 0.438 -19.295 16.606 1.00 20.00 C ANISOU 1229 C GLN A 163 2601 2793 2203 439 683 -176 C ATOM 1230 O GLN A 163 1.575 -19.188 16.168 1.00 20.99 O ANISOU 1230 O GLN A 163 2649 2998 2327 492 788 -143 O ATOM 1231 CB GLN A 163 -0.902 -17.308 15.788 1.00 18.67 C ANISOU 1231 CB GLN A 163 2497 2703 1893 295 619 -84 C ATOM 1232 CG GLN A 163 -1.879 -18.124 14.964 1.00 19.17 C ANISOU 1232 CG GLN A 163 2686 2750 1847 319 591 -197 C ATOM 1233 CD GLN A 163 -2.674 -17.319 13.953 1.00 19.46 C ANISOU 1233 CD GLN A 163 2787 2859 1748 273 567 -167 C ATOM 1234 OE1 GLN A 163 -2.576 -16.100 13.883 1.00 19.21 O ANISOU 1234 OE1 GLN A 163 2709 2875 1714 221 573 -52 O ATOM 1235 NE2 GLN A 163 -3.475 -18.018 13.155 1.00 20.29 N ANISOU 1235 NE2 GLN A 163 2999 2965 1745 288 531 -270 N ATOM 1236 N LEU A 164 -0.159 -20.475 16.752 1.00 20.74 N ANISOU 1236 N LEU A 164 2775 2789 2313 476 641 -278 N ATOM 1237 CA LEU A 164 0.510 -21.727 16.381 1.00 22.83 C ANISOU 1237 CA LEU A 164 3056 3021 2598 593 714 -369 C ATOM 1238 C LEU A 164 0.098 -22.151 14.976 1.00 25.14 C ANISOU 1238 C LEU A 164 3468 3344 2739 634 759 -490 C ATOM 1239 O LEU A 164 0.927 -22.604 14.177 1.00 27.07 O ANISOU 1239 O LEU A 164 3712 3642 2931 737 875 -549 O ATOM 1240 CB LEU A 164 0.159 -22.835 17.360 1.00 22.28 C ANISOU 1240 CB LEU A 164 3009 2804 2650 612 639 -407 C ATOM 1241 CG LEU A 164 0.689 -22.657 18.780 1.00 21.34 C ANISOU 1241 CG LEU A 164 2779 2661 2665 596 597 -298 C ATOM 1242 CD1 LEU A 164 0.054 -23.686 19.686 1.00 20.87 C ANISOU 1242 CD1 LEU A 164 2765 2464 2701 595 513 -317 C ATOM 1243 CD2 LEU A 164 2.218 -22.751 18.795 1.00 22.02 C ANISOU 1243 CD2 LEU A 164 2743 2807 2815 687 692 -253 C ATOM 1244 N GLU A 165 -1.200 -22.014 14.719 1.00 25.84 N ANISOU 1244 N GLU A 165 3654 3404 2757 556 662 -528 N ATOM 1245 CA GLU A 165 -1.819 -22.259 13.426 1.00 27.97 C ANISOU 1245 CA GLU A 165 4048 3715 2865 565 663 -637 C ATOM 1246 C GLU A 165 -2.921 -21.190 13.242 1.00 27.58 C ANISOU 1246 C GLU A 165 4022 3717 2739 452 572 -567 C ATOM 1247 O GLU A 165 -3.667 -20.826 14.168 1.00 25.35 O ANISOU 1247 O GLU A 165 3710 3372 2547 373 476 -503 O ATOM 1248 CB GLU A 165 -2.430 -23.679 13.365 1.00 29.39 C ANISOU 1248 CB GLU A 165 4335 3754 3077 595 601 -793 C ATOM 1249 CG GLU A 165 -1.611 -24.789 14.056 1.00 30.15 C ANISOU 1249 CG GLU A 165 4396 3731 3327 690 645 -832 C ATOM 1250 CD GLU A 165 -2.250 -26.171 13.950 1.00 31.56 C ANISOU 1250 CD GLU A 165 4691 3745 3555 710 577 -982 C ATOM 1251 OE1 GLU A 165 -3.497 -26.242 13.991 1.00 31.03 O ANISOU 1251 OE1 GLU A 165 4688 3620 3479 609 455 -1007 O ATOM 1252 OE2 GLU A 165 -1.497 -27.187 13.817 1.00 33.40 O ANISOU 1252 OE2 GLU A 165 4944 3898 3847 829 646 -1075 O ATOM 1253 OXT GLU A 165 -3.079 -20.639 12.138 1.00 29.69 O ANISOU 1253 OXT GLU A 165 4336 4098 2845 445 598 -565 O TER 1254 GLU A 165 ATOM 1255 N VAL B 2 -34.036 -16.669 98.631 1.00 23.36 N ANISOU 1255 N VAL B 2 4247 3676 951 -704 55 -221 N ATOM 1256 CA VAL B 2 -34.491 -17.902 97.901 1.00 22.42 C ANISOU 1256 CA VAL B 2 4088 3496 932 -680 91 -75 C ATOM 1257 C VAL B 2 -34.416 -17.751 96.370 1.00 20.07 C ANISOU 1257 C VAL B 2 3607 3099 918 -567 76 -82 C ATOM 1258 O VAL B 2 -35.178 -16.976 95.806 1.00 19.32 O ANISOU 1258 O VAL B 2 3407 2989 942 -536 195 -203 O ATOM 1259 CB VAL B 2 -35.924 -18.245 98.247 1.00 23.27 C ANISOU 1259 CB VAL B 2 4226 3648 965 -760 310 -104 C ATOM 1260 CG1 VAL B 2 -36.259 -19.685 97.705 1.00 22.83 C ANISOU 1260 CG1 VAL B 2 4166 3528 979 -763 319 65 C ATOM 1261 CG2 VAL B 2 -36.191 -18.057 99.793 1.00 25.79 C ANISOU 1261 CG2 VAL B 2 4727 4089 981 -890 385 -154 C ATOM 1262 N ASN B 3 -33.481 -18.448 95.714 1.00 19.08 N ANISOU 1262 N ASN B 3 3445 2906 896 -505 -72 40 N ATOM 1263 CA ASN B 3 -33.378 -18.392 94.249 1.00 17.11 C ANISOU 1263 CA ASN B 3 3040 2573 887 -411 -78 37 C ATOM 1264 C ASN B 3 -34.712 -18.796 93.659 1.00 16.59 C ANISOU 1264 C ASN B 3 2921 2488 893 -418 81 26 C ATOM 1265 O ASN B 3 -35.278 -19.831 94.036 1.00 17.24 O ANISOU 1265 O ASN B 3 3072 2576 899 -475 135 110 O ATOM 1266 CB ASN B 3 -32.290 -19.308 93.681 1.00 16.55 C ANISOU 1266 CB ASN B 3 2943 2436 908 -352 -230 165 C ATOM 1267 CG ASN B 3 -30.890 -18.772 93.884 1.00 16.83 C ANISOU 1267 CG ASN B 3 2961 2478 955 -322 -396 155 C ATOM 1268 OD1 ASN B 3 -30.702 -17.600 94.218 1.00 17.07 O ANISOU 1268 OD1 ASN B 3 2983 2547 954 -339 -398 42 O ATOM 1269 ND2 ASN B 3 -29.888 -19.636 93.701 1.00 16.92 N ANISOU 1269 ND2 ASN B 3 2958 2443 1025 -276 -539 265 N ATOM 1270 N PRO B 4 -35.246 -17.972 92.754 1.00 15.52 N ANISOU 1270 N PRO B 4 2663 2327 906 -367 151 -73 N ATOM 1271 CA PRO B 4 -36.564 -18.281 92.209 1.00 15.19 C ANISOU 1271 CA PRO B 4 2552 2276 942 -373 288 -97 C ATOM 1272 C PRO B 4 -36.573 -19.457 91.208 1.00 14.25 C ANISOU 1272 C PRO B 4 2390 2092 931 -345 256 9 C ATOM 1273 O PRO B 4 -35.573 -19.723 90.520 1.00 13.33 O ANISOU 1273 O PRO B 4 2248 1924 891 -288 140 69 O ATOM 1274 CB PRO B 4 -36.971 -16.973 91.490 1.00 14.54 C ANISOU 1274 CB PRO B 4 2353 2173 996 -310 329 -225 C ATOM 1275 CG PRO B 4 -36.004 -15.903 91.977 1.00 14.86 C ANISOU 1275 CG PRO B 4 2429 2220 994 -299 250 -287 C ATOM 1276 CD PRO B 4 -34.746 -16.664 92.298 1.00 14.94 C ANISOU 1276 CD PRO B 4 2516 2232 927 -312 110 -172 C ATOM 1277 N THR B 5 -37.723 -20.113 91.134 1.00 14.52 N ANISOU 1277 N THR B 5 2405 2131 978 -391 369 16 N ATOM 1278 CA THR B 5 -37.993 -21.155 90.167 1.00 13.89 C ANISOU 1278 CA THR B 5 2276 1989 1010 -377 362 84 C ATOM 1279 C THR B 5 -39.130 -20.687 89.259 1.00 13.28 C ANISOU 1279 C THR B 5 2064 1914 1067 -352 447 -9 C ATOM 1280 O THR B 5 -40.190 -20.266 89.722 1.00 14.10 O ANISOU 1280 O THR B 5 2132 2067 1156 -392 567 -91 O ATOM 1281 CB THR B 5 -38.349 -22.457 90.861 1.00 15.05 C ANISOU 1281 CB THR B 5 2522 2128 1068 -467 405 184 C ATOM 1282 OG1 THR B 5 -37.213 -22.882 91.597 1.00 15.80 O ANISOU 1282 OG1 THR B 5 2739 2209 1054 -472 289 286 O ATOM 1283 CG2 THR B 5 -38.682 -23.554 89.865 1.00 14.65 C ANISOU 1283 CG2 THR B 5 2419 2000 1145 -461 403 237 C ATOM 1284 N VAL B 6 -38.881 -20.753 87.965 1.00 12.08 N ANISOU 1284 N VAL B 6 1835 1710 1043 -285 380 0 N ATOM 1285 CA VAL B 6 -39.824 -20.347 86.965 1.00 11.60 C ANISOU 1285 CA VAL B 6 1653 1645 1108 -252 416 -70 C ATOM 1286 C VAL B 6 -40.084 -21.537 86.001 1.00 11.15 C ANISOU 1286 C VAL B 6 1565 1542 1127 -262 397 -19 C ATOM 1287 O VAL B 6 -39.203 -22.391 85.771 1.00 10.76 O ANISOU 1287 O VAL B 6 1573 1443 1070 -256 329 58 O ATOM 1288 CB VAL B 6 -39.305 -19.081 86.200 1.00 10.81 C ANISOU 1288 CB VAL B 6 1500 1529 1079 -166 346 -118 C ATOM 1289 CG1 VAL B 6 -39.235 -17.877 87.127 1.00 11.34 C ANISOU 1289 CG1 VAL B 6 1587 1627 1094 -162 376 -193 C ATOM 1290 CG2 VAL B 6 -37.964 -19.335 85.627 1.00 10.18 C ANISOU 1290 CG2 VAL B 6 1455 1408 1003 -129 241 -50 C ATOM 1291 N PHE B 7 -41.297 -21.617 85.476 1.00 11.21 N ANISOU 1291 N PHE B 7 1477 1561 1218 -279 453 -72 N ATOM 1292 CA PHE B 7 -41.627 -22.691 84.548 1.00 11.02 C ANISOU 1292 CA PHE B 7 1421 1496 1268 -299 433 -46 C ATOM 1293 C PHE B 7 -42.131 -22.135 83.235 1.00 10.41 C ANISOU 1293 C PHE B 7 1235 1423 1297 -242 384 -105 C ATOM 1294 O PHE B 7 -42.699 -21.065 83.202 1.00 10.35 O ANISOU 1294 O PHE B 7 1154 1448 1329 -204 396 -169 O ATOM 1295 CB PHE B 7 -42.663 -23.631 85.139 1.00 12.12 C ANISOU 1295 CB PHE B 7 1555 1643 1406 -402 536 -41 C ATOM 1296 CG PHE B 7 -44.029 -23.031 85.241 1.00 12.92 C ANISOU 1296 CG PHE B 7 1533 1803 1570 -424 627 -140 C ATOM 1297 CD1 PHE B 7 -44.399 -22.324 86.362 1.00 13.72 C ANISOU 1297 CD1 PHE B 7 1637 1964 1609 -449 726 -189 C ATOM 1298 CD2 PHE B 7 -44.943 -23.165 84.194 1.00 12.98 C ANISOU 1298 CD2 PHE B 7 1413 1811 1706 -417 607 -194 C ATOM 1299 CE1 PHE B 7 -45.637 -21.770 86.454 1.00 14.63 C ANISOU 1299 CE1 PHE B 7 1620 2130 1807 -459 818 -295 C ATOM 1300 CE2 PHE B 7 -46.179 -22.605 84.268 1.00 13.88 C ANISOU 1300 CE2 PHE B 7 1391 1976 1905 -425 676 -289 C ATOM 1301 CZ PHE B 7 -46.540 -21.902 85.413 1.00 14.74 C ANISOU 1301 CZ PHE B 7 1491 2139 1971 -442 790 -344 C ATOM 1302 N PHE B 8 -41.895 -22.886 82.166 1.00 10.04 N ANISOU 1302 N PHE B 8 1185 1336 1292 -235 323 -82 N ATOM 1303 CA PHE B 8 -42.491 -22.637 80.868 1.00 9.97 C ANISOU 1303 CA PHE B 8 1090 1336 1362 -204 269 -129 C ATOM 1304 C PHE B 8 -43.205 -23.912 80.466 1.00 10.57 C ANISOU 1304 C PHE B 8 1138 1389 1486 -275 286 -140 C ATOM 1305 O PHE B 8 -42.603 -25.016 80.492 1.00 10.49 O ANISOU 1305 O PHE B 8 1204 1323 1457 -309 286 -95 O ATOM 1306 CB PHE B 8 -41.421 -22.415 79.791 1.00 9.23 C ANISOU 1306 CB PHE B 8 1035 1217 1252 -145 179 -105 C ATOM 1307 CG PHE B 8 -40.665 -21.104 79.865 1.00 8.75 C ANISOU 1307 CG PHE B 8 994 1167 1164 -81 147 -96 C ATOM 1308 CD1 PHE B 8 -41.044 -20.067 80.680 1.00 9.04 C ANISOU 1308 CD1 PHE B 8 1004 1226 1204 -62 179 -125 C ATOM 1309 CD2 PHE B 8 -39.557 -20.925 79.040 1.00 8.23 C ANISOU 1309 CD2 PHE B 8 970 1082 1076 -45 90 -67 C ATOM 1310 CE1 PHE B 8 -40.328 -18.891 80.697 1.00 8.74 C ANISOU 1310 CE1 PHE B 8 988 1179 1152 -11 145 -121 C ATOM 1311 CE2 PHE B 8 -38.854 -19.766 79.046 1.00 7.93 C ANISOU 1311 CE2 PHE B 8 947 1043 1021 -3 64 -57 C ATOM 1312 CZ PHE B 8 -39.236 -18.740 79.870 1.00 8.17 C ANISOU 1312 CZ PHE B 8 957 1083 1061 13 85 -81 C ATOM 1313 N ASP B 9 -44.474 -23.779 80.111 1.00 11.22 N ANISOU 1313 N ASP B 9 1107 1507 1648 -297 295 -203 N ATOM 1314 CA ASP B 9 -45.180 -24.849 79.418 1.00 11.86 C ANISOU 1314 CA ASP B 9 1142 1570 1791 -362 283 -233 C ATOM 1315 C ASP B 9 -45.044 -24.578 77.930 1.00 11.44 C ANISOU 1315 C ASP B 9 1068 1524 1753 -309 163 -258 C ATOM 1316 O ASP B 9 -45.443 -23.531 77.438 1.00 11.40 O ANISOU 1316 O ASP B 9 995 1561 1773 -249 103 -284 O ATOM 1317 CB ASP B 9 -46.620 -24.940 79.866 1.00 13.12 C ANISOU 1317 CB ASP B 9 1179 1770 2036 -429 356 -293 C ATOM 1318 CG ASP B 9 -46.741 -25.491 81.288 1.00 13.91 C ANISOU 1318 CG ASP B 9 1329 1861 2096 -517 494 -259 C ATOM 1319 OD1 ASP B 9 -45.955 -26.404 81.649 1.00 13.82 O ANISOU 1319 OD1 ASP B 9 1442 1785 2021 -556 508 -184 O ATOM 1320 OD2 ASP B 9 -47.603 -25.012 82.056 1.00 14.79 O ANISOU 1320 OD2 ASP B 9 1357 2026 2235 -546 589 -307 O ATOM 1321 N ILE B 10 -44.381 -25.507 77.245 1.00 11.19 N ANISOU 1321 N ILE B 10 1109 1445 1695 -327 130 -247 N ATOM 1322 CA ILE B 10 -43.998 -25.335 75.859 1.00 10.93 C ANISOU 1322 CA ILE B 10 1093 1423 1635 -288 34 -268 C ATOM 1323 C ILE B 10 -45.053 -25.986 75.014 1.00 11.90 C ANISOU 1323 C ILE B 10 1145 1561 1815 -347 -14 -338 C ATOM 1324 O ILE B 10 -45.587 -27.040 75.374 1.00 12.52 O ANISOU 1324 O ILE B 10 1203 1602 1950 -430 37 -363 O ATOM 1325 CB ILE B 10 -42.631 -25.989 75.540 1.00 10.44 C ANISOU 1325 CB ILE B 10 1142 1305 1517 -274 37 -241 C ATOM 1326 CG1 ILE B 10 -41.553 -25.523 76.540 1.00 9.69 C ANISOU 1326 CG1 ILE B 10 1108 1192 1380 -228 79 -172 C ATOM 1327 CG2 ILE B 10 -42.224 -25.638 74.147 1.00 10.31 C ANISOU 1327 CG2 ILE B 10 1149 1319 1448 -241 -38 -268 C ATOM 1328 CD1 ILE B 10 -41.289 -24.076 76.493 1.00 9.08 C ANISOU 1328 CD1 ILE B 10 1018 1164 1269 -163 48 -154 C ATOM 1329 N ALA B 11 -45.383 -25.334 73.905 1.00 12.17 N ANISOU 1329 N ALA B 11 1143 1647 1833 -312 -120 -365 N ATOM 1330 CA ALA B 11 -46.322 -25.884 72.927 1.00 13.25 C ANISOU 1330 CA ALA B 11 1217 1809 2007 -365 -200 -438 C ATOM 1331 C ALA B 11 -45.657 -25.883 71.562 1.00 13.26 C ANISOU 1331 C ALA B 11 1305 1827 1904 -347 -288 -451 C ATOM 1332 O ALA B 11 -44.820 -25.021 71.279 1.00 12.49 O ANISOU 1332 O ALA B 11 1275 1745 1725 -282 -307 -397 O ATOM 1333 CB ALA B 11 -47.622 -25.063 72.889 1.00 14.01 C ANISOU 1333 CB ALA B 11 1165 1967 2189 -345 -268 -466 C ATOM 1334 N VAL B 12 -46.069 -26.843 70.730 1.00 14.23 N ANISOU 1334 N VAL B 12 1426 1949 2029 -418 -334 -528 N ATOM 1335 CA VAL B 12 -45.600 -27.009 69.371 1.00 14.71 C ANISOU 1335 CA VAL B 12 1572 2037 1978 -425 -410 -567 C ATOM 1336 C VAL B 12 -46.818 -26.963 68.446 1.00 16.18 C ANISOU 1336 C VAL B 12 1680 2292 2174 -464 -553 -630 C ATOM 1337 O VAL B 12 -47.725 -27.785 68.565 1.00 17.03 O ANISOU 1337 O VAL B 12 1703 2387 2379 -540 -560 -703 O ATOM 1338 CB VAL B 12 -44.908 -28.400 69.158 1.00 14.88 C ANISOU 1338 CB VAL B 12 1677 1985 1989 -482 -337 -633 C ATOM 1339 CG1 VAL B 12 -44.560 -28.550 67.712 1.00 15.64 C ANISOU 1339 CG1 VAL B 12 1855 2126 1961 -501 -405 -700 C ATOM 1340 CG2 VAL B 12 -43.674 -28.575 70.043 1.00 13.74 C ANISOU 1340 CG2 VAL B 12 1603 1766 1852 -439 -218 -573 C ATOM 1341 N ASP B 13 -46.809 -26.013 67.521 1.00 16.67 N ANISOU 1341 N ASP B 13 1773 2423 2136 -419 -672 -597 N ATOM 1342 CA ASP B 13 -48.010 -25.592 66.784 1.00 18.21 C ANISOU 1342 CA ASP B 13 1878 2691 2350 -425 -844 -622 C ATOM 1343 C ASP B 13 -49.246 -25.640 67.668 1.00 18.69 C ANISOU 1343 C ASP B 13 1754 2746 2600 -436 -841 -650 C ATOM 1344 O ASP B 13 -50.273 -26.216 67.295 1.00 20.02 O ANISOU 1344 O ASP B 13 1821 2943 2840 -502 -923 -734 O ATOM 1345 CB ASP B 13 -48.220 -26.458 65.532 1.00 19.68 C ANISOU 1345 CB ASP B 13 2118 2916 2443 -510 -938 -720 C ATOM 1346 CG ASP B 13 -47.416 -25.985 64.351 1.00 20.08 C ANISOU 1346 CG ASP B 13 2325 3019 2284 -495 -1001 -689 C ATOM 1347 OD1 ASP B 13 -46.739 -24.938 64.431 1.00 19.46 O ANISOU 1347 OD1 ASP B 13 2308 2943 2140 -421 -985 -582 O ATOM 1348 OD2 ASP B 13 -47.482 -26.659 63.304 1.00 21.49 O ANISOU 1348 OD2 ASP B 13 2570 3238 2355 -568 -1066 -778 O ATOM 1349 N GLY B 14 -49.137 -25.077 68.860 1.00 17.70 N ANISOU 1349 N GLY B 14 1581 2586 2556 -382 -735 -593 N ATOM 1350 CA GLY B 14 -50.264 -25.100 69.786 1.00 18.44 C ANISOU 1350 CA GLY B 14 1498 2681 2824 -399 -695 -629 C ATOM 1351 C GLY B 14 -50.520 -26.390 70.565 1.00 18.57 C ANISOU 1351 C GLY B 14 1481 2650 2926 -507 -559 -688 C ATOM 1352 O GLY B 14 -51.245 -26.344 71.536 1.00 18.90 O ANISOU 1352 O GLY B 14 1399 2690 3092 -526 -476 -702 O ATOM 1353 N GLU B 15 -49.933 -27.524 70.183 1.00 18.57 N ANISOU 1353 N GLU B 15 1589 2602 2863 -579 -525 -722 N ATOM 1354 CA GLU B 15 -50.085 -28.767 70.982 1.00 18.90 C ANISOU 1354 CA GLU B 15 1622 2568 2990 -683 -393 -756 C ATOM 1355 C GLU B 15 -49.105 -28.784 72.159 1.00 17.26 C ANISOU 1355 C GLU B 15 1511 2293 2754 -652 -241 -668 C ATOM 1356 O GLU B 15 -47.933 -28.507 71.976 1.00 16.06 O ANISOU 1356 O GLU B 15 1484 2123 2496 -585 -235 -617 O ATOM 1357 CB GLU B 15 -49.865 -30.026 70.141 1.00 19.91 C ANISOU 1357 CB GLU B 15 1828 2647 3088 -770 -420 -836 C ATOM 1358 CG GLU B 15 -50.756 -30.138 68.919 1.00 21.71 C ANISOU 1358 CG GLU B 15 1983 2945 3320 -817 -584 -935 C ATOM 1359 CD GLU B 15 -52.238 -30.181 69.267 1.00 23.43 C ANISOU 1359 CD GLU B 15 1995 3201 3706 -882 -615 -990 C ATOM 1360 OE1 GLU B 15 -52.672 -31.050 70.077 1.00 24.22 O ANISOU 1360 OE1 GLU B 15 2039 3237 3926 -982 -496 -1018 O ATOM 1361 OE2 GLU B 15 -52.989 -29.337 68.717 1.00 24.56 O ANISOU 1361 OE2 GLU B 15 2026 3436 3868 -836 -762 -1004 O ATOM 1362 N PRO B 16 -49.578 -29.122 73.375 1.00 17.35 N ANISOU 1362 N PRO B 16 1464 2271 2854 -709 -117 -652 N ATOM 1363 CA PRO B 16 -48.636 -29.057 74.512 1.00 16.10 C ANISOU 1363 CA PRO B 16 1409 2061 2645 -677 3 -559 C ATOM 1364 C PRO B 16 -47.536 -30.108 74.415 1.00 15.56 C ANISOU 1364 C PRO B 16 1493 1891 2528 -697 35 -534 C ATOM 1365 O PRO B 16 -47.817 -31.265 74.108 1.00 16.37 O ANISOU 1365 O PRO B 16 1605 1928 2687 -787 41 -587 O ATOM 1366 CB PRO B 16 -49.519 -29.292 75.746 1.00 16.96 C ANISOU 1366 CB PRO B 16 1431 2167 2845 -758 127 -554 C ATOM 1367 CG PRO B 16 -50.912 -29.514 75.256 1.00 18.53 C ANISOU 1367 CG PRO B 16 1461 2412 3166 -833 82 -652 C ATOM 1368 CD PRO B 16 -50.888 -29.677 73.761 1.00 18.78 C ANISOU 1368 CD PRO B 16 1499 2460 3174 -818 -76 -715 C ATOM 1369 N LEU B 17 -46.285 -29.684 74.619 1.00 14.21 N ANISOU 1369 N LEU B 17 1428 1701 2267 -610 48 -465 N ATOM 1370 CA LEU B 17 -45.109 -30.567 74.568 1.00 13.78 C ANISOU 1370 CA LEU B 17 1501 1548 2184 -602 75 -442 C ATOM 1371 C LEU B 17 -44.708 -31.009 75.990 1.00 13.64 C ANISOU 1371 C LEU B 17 1546 1455 2182 -622 172 -349 C ATOM 1372 O LEU B 17 -44.495 -32.187 76.246 1.00 14.36 O ANISOU 1372 O LEU B 17 1700 1435 2321 -677 209 -336 O ATOM 1373 CB LEU B 17 -43.924 -29.828 73.924 1.00 12.73 C ANISOU 1373 CB LEU B 17 1435 1446 1954 -499 28 -425 C ATOM 1374 CG LEU B 17 -42.675 -30.660 73.620 1.00 12.62 C ANISOU 1374 CG LEU B 17 1524 1343 1927 -475 47 -431 C ATOM 1375 CD1 LEU B 17 -43.031 -31.793 72.650 1.00 13.74 C ANISOU 1375 CD1 LEU B 17 1675 1433 2110 -544 24 -538 C ATOM 1376 CD2 LEU B 17 -41.545 -29.786 73.054 1.00 11.74 C ANISOU 1376 CD2 LEU B 17 1454 1281 1724 -384 23 -416 C ATOM 1377 N GLY B 18 -44.623 -30.066 76.918 1.00 12.92 N ANISOU 1377 N GLY B 18 1443 1418 2046 -580 208 -285 N ATOM 1378 CA GLY B 18 -44.114 -30.367 78.243 1.00 12.87 C ANISOU 1378 CA GLY B 18 1518 1357 2015 -594 283 -189 C ATOM 1379 C GLY B 18 -43.638 -29.111 78.931 1.00 11.95 C ANISOU 1379 C GLY B 18 1408 1312 1819 -517 290 -141 C ATOM 1380 O GLY B 18 -43.741 -28.005 78.386 1.00 11.30 O ANISOU 1380 O GLY B 18 1265 1308 1718 -454 243 -178 O ATOM 1381 N ARG B 19 -43.125 -29.283 80.140 1.00 12.02 N ANISOU 1381 N ARG B 19 1499 1288 1781 -528 340 -56 N ATOM 1382 CA ARG B 19 -42.736 -28.162 80.977 1.00 11.47 C ANISOU 1382 CA ARG B 19 1444 1283 1630 -476 355 -20 C ATOM 1383 C ARG B 19 -41.229 -28.163 81.252 1.00 10.92 C ANISOU 1383 C ARG B 19 1474 1169 1505 -405 304 49 C ATOM 1384 O ARG B 19 -40.618 -29.204 81.507 1.00 11.33 O ANISOU 1384 O ARG B 19 1606 1129 1570 -419 293 107 O ATOM 1385 CB ARG B 19 -43.538 -28.211 82.286 1.00 12.40 C ANISOU 1385 CB ARG B 19 1565 1427 1716 -563 461 8 C ATOM 1386 CG ARG B 19 -43.151 -27.139 83.303 1.00 12.08 C ANISOU 1386 CG ARG B 19 1558 1453 1578 -525 487 33 C ATOM 1387 CD ARG B 19 -43.965 -27.236 84.559 1.00 13.24 C ANISOU 1387 CD ARG B 19 1718 1637 1675 -623 612 47 C ATOM 1388 NE ARG B 19 -45.318 -26.752 84.361 1.00 13.79 N ANISOU 1388 NE ARG B 19 1641 1776 1821 -657 683 -53 N ATOM 1389 CZ ARG B 19 -46.171 -26.445 85.340 1.00 14.89 C ANISOU 1389 CZ ARG B 19 1744 1980 1933 -728 813 -86 C ATOM 1390 NH1 ARG B 19 -45.842 -26.591 86.614 1.00 15.61 N ANISOU 1390 NH1 ARG B 19 1957 2081 1892 -787 889 -20 N ATOM 1391 NH2 ARG B 19 -47.374 -26.004 85.044 1.00 15.51 N ANISOU 1391 NH2 ARG B 19 1660 2116 2115 -742 867 -191 N ATOM 1392 N VAL B 20 -40.635 -26.982 81.205 1.00 10.16 N ANISOU 1392 N VAL B 20 1364 1132 1363 -329 269 40 N ATOM 1393 CA VAL B 20 -39.265 -26.793 81.613 1.00 9.82 C ANISOU 1393 CA VAL B 20 1391 1067 1273 -269 223 97 C ATOM 1394 C VAL B 20 -39.261 -25.861 82.801 1.00 10.05 C ANISOU 1394 C VAL B 20 1442 1157 1219 -271 250 120 C ATOM 1395 O VAL B 20 -39.948 -24.836 82.778 1.00 9.81 O ANISOU 1395 O VAL B 20 1348 1195 1183 -264 279 64 O ATOM 1396 CB VAL B 20 -38.443 -26.176 80.482 1.00 8.95 C ANISOU 1396 CB VAL B 20 1248 971 1180 -190 163 58 C ATOM 1397 CG1 VAL B 20 -36.993 -26.093 80.867 1.00 8.64 C ANISOU 1397 CG1 VAL B 20 1257 906 1119 -135 118 106 C ATOM 1398 CG2 VAL B 20 -38.633 -26.999 79.195 1.00 9.03 C ANISOU 1398 CG2 VAL B 20 1235 942 1252 -199 148 6 C ATOM 1399 N SER B 21 -38.545 -26.233 83.865 1.00 10.73 N ANISOU 1399 N SER B 21 1620 1215 1240 -281 237 199 N ATOM 1400 CA SER B 21 -38.399 -25.345 85.008 1.00 11.15 C ANISOU 1400 CA SER B 21 1711 1332 1193 -287 252 211 C ATOM 1401 C SER B 21 -36.949 -24.907 85.135 1.00 10.89 C ANISOU 1401 C SER B 21 1709 1291 1135 -217 158 241 C ATOM 1402 O SER B 21 -36.048 -25.652 84.783 1.00 11.01 O ANISOU 1402 O SER B 21 1745 1240 1197 -179 92 285 O ATOM 1403 CB SER B 21 -38.864 -26.028 86.279 1.00 12.45 C ANISOU 1403 CB SER B 21 1966 1493 1271 -379 313 278 C ATOM 1404 OG SER B 21 -37.889 -26.969 86.681 1.00 13.06 O ANISOU 1404 OG SER B 21 2141 1491 1328 -371 236 383 O ATOM 1405 N PHE B 22 -36.740 -23.692 85.612 1.00 10.86 N ANISOU 1405 N PHE B 22 1700 1352 1074 -198 154 205 N ATOM 1406 CA PHE B 22 -35.418 -23.102 85.730 1.00 10.69 C ANISOU 1406 CA PHE B 22 1688 1333 1039 -143 67 216 C ATOM 1407 C PHE B 22 -35.212 -22.579 87.122 1.00 11.58 C ANISOU 1407 C PHE B 22 1875 1495 1028 -176 58 229 C ATOM 1408 O PHE B 22 -36.120 -22.020 87.691 1.00 11.82 O ANISOU 1408 O PHE B 22 1913 1579 999 -220 139 180 O ATOM 1409 CB PHE B 22 -35.264 -21.884 84.814 1.00 9.79 C ANISOU 1409 CB PHE B 22 1494 1245 982 -93 60 141 C ATOM 1410 CG PHE B 22 -35.665 -22.114 83.394 1.00 9.19 C ANISOU 1410 CG PHE B 22 1350 1144 993 -71 75 112 C ATOM 1411 CD1 PHE B 22 -34.745 -22.526 82.474 1.00 8.85 C ANISOU 1411 CD1 PHE B 22 1289 1065 1009 -32 31 122 C ATOM 1412 CD2 PHE B 22 -36.970 -21.870 82.977 1.00 9.22 C ANISOU 1412 CD2 PHE B 22 1307 1172 1023 -91 132 64 C ATOM 1413 CE1 PHE B 22 -35.100 -22.702 81.173 1.00 8.57 C ANISOU 1413 CE1 PHE B 22 1209 1020 1027 -22 45 88 C ATOM 1414 CE2 PHE B 22 -37.344 -22.056 81.687 1.00 8.84 C ANISOU 1414 CE2 PHE B 22 1207 1111 1038 -76 125 38 C ATOM 1415 CZ PHE B 22 -36.414 -22.476 80.776 1.00 8.60 C ANISOU 1415 CZ PHE B 22 1180 1049 1038 -47 83 50 C ATOM 1416 N GLU B 23 -33.995 -22.733 87.641 1.00 12.16 N ANISOU 1416 N GLU B 23 1995 1554 1069 -153 -43 284 N ATOM 1417 CA GLU B 23 -33.554 -22.010 88.830 1.00 13.01 C ANISOU 1417 CA GLU B 23 2166 1719 1056 -177 -83 279 C ATOM 1418 C GLU B 23 -32.876 -20.725 88.334 1.00 12.34 C ANISOU 1418 C GLU B 23 2005 1654 1028 -129 -119 199 C ATOM 1419 O GLU B 23 -32.016 -20.786 87.446 1.00 11.71 O ANISOU 1419 O GLU B 23 1858 1537 1055 -75 -176 205 O ATOM 1420 CB GLU B 23 -32.552 -22.838 89.634 1.00 14.20 C ANISOU 1420 CB GLU B 23 2401 1842 1150 -175 -204 385 C ATOM 1421 CG GLU B 23 -31.985 -22.099 90.839 1.00 15.27 C ANISOU 1421 CG GLU B 23 2607 2045 1148 -204 -273 377 C ATOM 1422 CD GLU B 23 -30.957 -22.898 91.639 1.00 16.71 C ANISOU 1422 CD GLU B 23 2872 2204 1273 -196 -427 492 C ATOM 1423 OE1 GLU B 23 -30.650 -24.075 91.299 1.00 17.07 O ANISOU 1423 OE1 GLU B 23 2920 2164 1401 -159 -480 586 O ATOM 1424 OE2 GLU B 23 -30.473 -22.342 92.659 1.00 17.88 O ANISOU 1424 OE2 GLU B 23 3087 2414 1292 -226 -504 487 O ATOM 1425 N LEU B 24 -33.261 -19.571 88.893 1.00 12.56 N ANISOU 1425 N LEU B 24 2043 1735 994 -155 -77 119 N ATOM 1426 CA LEU B 24 -32.596 -18.303 88.587 1.00 12.16 C ANISOU 1426 CA LEU B 24 1938 1688 993 -125 -115 47 C ATOM 1427 C LEU B 24 -31.586 -17.949 89.689 1.00 13.16 C ANISOU 1427 C LEU B 24 2123 1848 1027 -148 -214 47 C ATOM 1428 O LEU B 24 -31.948 -17.891 90.850 1.00 14.00 O ANISOU 1428 O LEU B 24 2320 2005 992 -202 -197 34 O ATOM 1429 CB LEU B 24 -33.633 -17.194 88.437 1.00 11.96 C ANISOU 1429 CB LEU B 24 1879 1676 987 -129 -17 -52 C ATOM 1430 CG LEU B 24 -34.777 -17.579 87.501 1.00 11.33 C ANISOU 1430 CG LEU B 24 1742 1576 987 -113 63 -53 C ATOM 1431 CD1 LEU B 24 -35.801 -16.449 87.416 1.00 11.38 C ANISOU 1431 CD1 LEU B 24 1701 1589 1033 -103 141 -152 C ATOM 1432 CD2 LEU B 24 -34.238 -18.030 86.116 1.00 10.31 C ANISOU 1432 CD2 LEU B 24 1552 1398 965 -67 17 -5 C ATOM 1433 N PHE B 25 -30.328 -17.694 89.321 1.00 13.11 N ANISOU 1433 N PHE B 25 2061 1821 1096 -115 -314 54 N ATOM 1434 CA PHE B 25 -29.274 -17.514 90.316 1.00 14.32 C ANISOU 1434 CA PHE B 25 2255 2007 1178 -135 -438 60 C ATOM 1435 C PHE B 25 -29.251 -16.059 90.827 1.00 14.89 C ANISOU 1435 C PHE B 25 2336 2111 1209 -172 -428 -54 C ATOM 1436 O PHE B 25 -28.280 -15.306 90.643 1.00 14.93 O ANISOU 1436 O PHE B 25 2282 2105 1285 -169 -499 -96 O ATOM 1437 CB PHE B 25 -27.909 -17.957 89.769 1.00 14.34 C ANISOU 1437 CB PHE B 25 2173 1975 1299 -85 -553 109 C ATOM 1438 CG PHE B 25 -27.855 -19.410 89.310 1.00 14.26 C ANISOU 1438 CG PHE B 25 2154 1916 1346 -41 -568 207 C ATOM 1439 CD1 PHE B 25 -28.242 -20.452 90.158 1.00 15.23 C ANISOU 1439 CD1 PHE B 25 2384 2037 1363 -60 -598 296 C ATOM 1440 CD2 PHE B 25 -27.388 -19.731 88.047 1.00 13.49 C ANISOU 1440 CD2 PHE B 25 1950 1769 1405 12 -550 207 C ATOM 1441 CE1 PHE B 25 -28.191 -21.794 89.724 1.00 15.28 C ANISOU 1441 CE1 PHE B 25 2387 1973 1443 -19 -614 384 C ATOM 1442 CE2 PHE B 25 -27.334 -21.061 87.607 1.00 13.61 C ANISOU 1442 CE2 PHE B 25 1957 1727 1485 56 -558 276 C ATOM 1443 CZ PHE B 25 -27.731 -22.084 88.443 1.00 14.45 C ANISOU 1443 CZ PHE B 25 2166 1814 1509 43 -595 364 C ATOM 1444 N ALA B 26 -30.336 -15.697 91.506 1.00 15.45 N ANISOU 1444 N ALA B 26 2480 2217 1170 -214 -332 -112 N ATOM 1445 CA ALA B 26 -30.550 -14.359 92.011 1.00 16.11 C ANISOU 1445 CA ALA B 26 2580 2319 1221 -246 -296 -242 C ATOM 1446 C ALA B 26 -29.455 -13.972 92.990 1.00 17.50 C ANISOU 1446 C ALA B 26 2805 2535 1306 -289 -428 -271 C ATOM 1447 O ALA B 26 -29.140 -12.791 93.105 1.00 17.70 O ANISOU 1447 O ALA B 26 2810 2548 1365 -307 -439 -379 O ATOM 1448 CB ALA B 26 -31.922 -14.276 92.689 1.00 16.65 C ANISOU 1448 CB ALA B 26 2717 2429 1180 -284 -158 -303 C ATOM 1449 N ASP B 27 -28.910 -14.967 93.700 1.00 18.51 N ANISOU 1449 N ASP B 27 3001 2706 1325 -306 -534 -174 N ATOM 1450 CA ASP B 27 -27.771 -14.766 94.600 1.00 20.19 C ANISOU 1450 CA ASP B 27 3253 2963 1454 -341 -700 -182 C ATOM 1451 C ASP B 27 -26.490 -14.227 93.920 1.00 19.99 C ANISOU 1451 C ASP B 27 3096 2897 1603 -309 -809 -206 C ATOM 1452 O ASP B 27 -25.695 -13.525 94.553 1.00 21.25 O ANISOU 1452 O ASP B 27 3259 3086 1729 -352 -916 -275 O ATOM 1453 CB ASP B 27 -27.450 -16.051 95.414 1.00 21.44 C ANISOU 1453 CB ASP B 27 3511 3162 1473 -353 -816 -45 C ATOM 1454 CG ASP B 27 -27.186 -17.289 94.540 1.00 20.67 C ANISOU 1454 CG ASP B 27 3345 2997 1511 -278 -847 91 C ATOM 1455 OD1 ASP B 27 -27.571 -17.338 93.353 1.00 19.24 O ANISOU 1455 OD1 ASP B 27 3067 2757 1486 -230 -743 83 O ATOM 1456 OD2 ASP B 27 -26.592 -18.248 95.062 1.00 21.97 O ANISOU 1456 OD2 ASP B 27 3560 3163 1622 -268 -985 206 O ATOM 1457 N LYS B 28 -26.296 -14.524 92.647 1.00 18.75 N ANISOU 1457 N LYS B 28 2821 2674 1626 -248 -773 -158 N ATOM 1458 CA LYS B 28 -25.113 -14.043 91.944 1.00 18.70 C ANISOU 1458 CA LYS B 28 2683 2633 1786 -231 -845 -182 C ATOM 1459 C LYS B 28 -25.431 -12.980 90.903 1.00 17.19 C ANISOU 1459 C LYS B 28 2423 2383 1725 -230 -725 -254 C ATOM 1460 O LYS B 28 -24.587 -12.156 90.628 1.00 17.49 O ANISOU 1460 O LYS B 28 2386 2397 1862 -255 -765 -309 O ATOM 1461 CB LYS B 28 -24.347 -15.214 91.309 1.00 18.92 C ANISOU 1461 CB LYS B 28 2624 2637 1925 -166 -913 -75 C ATOM 1462 CG LYS B 28 -23.462 -15.978 92.323 1.00 20.84 C ANISOU 1462 CG LYS B 28 2895 2920 2100 -161 -1103 -9 C ATOM 1463 CD LYS B 28 -23.276 -17.455 91.893 1.00 21.15 C ANISOU 1463 CD LYS B 28 2906 2918 2211 -84 -1138 114 C ATOM 1464 CE LYS B 28 -24.546 -18.356 92.152 1.00 21.06 C ANISOU 1464 CE LYS B 28 3032 2897 2072 -86 -1049 193 C ATOM 1465 NZ LYS B 28 -24.425 -19.875 91.867 1.00 21.32 N ANISOU 1465 NZ LYS B 28 3062 2868 2168 -19 -1091 318 N ATOM 1466 N VAL B 29 -26.625 -12.995 90.330 1.00 15.77 N ANISOU 1466 N VAL B 29 2268 2174 1548 -207 -588 -250 N ATOM 1467 CA VAL B 29 -27.008 -12.016 89.300 1.00 14.72 C ANISOU 1467 CA VAL B 29 2083 1975 1534 -199 -491 -298 C ATOM 1468 C VAL B 29 -28.419 -11.526 89.564 1.00 14.31 C ANISOU 1468 C VAL B 29 2098 1915 1424 -199 -382 -358 C ATOM 1469 O VAL B 29 -29.327 -11.828 88.801 1.00 13.40 O ANISOU 1469 O VAL B 29 1967 1775 1347 -160 -295 -324 O ATOM 1470 CB VAL B 29 -26.921 -12.601 87.859 1.00 13.63 C ANISOU 1470 CB VAL B 29 1864 1798 1514 -151 -445 -221 C ATOM 1471 CG1 VAL B 29 -25.793 -11.943 87.078 1.00 13.88 C ANISOU 1471 CG1 VAL B 29 1801 1793 1677 -170 -470 -234 C ATOM 1472 CG2 VAL B 29 -26.756 -14.096 87.887 1.00 13.52 C ANISOU 1472 CG2 VAL B 29 1849 1814 1472 -115 -482 -131 C ATOM 1473 N PRO B 30 -28.612 -10.768 90.653 1.00 15.12 N ANISOU 1473 N PRO B 30 2267 2040 1437 -244 -385 -459 N ATOM 1474 CA PRO B 30 -29.973 -10.445 91.104 1.00 15.30 C ANISOU 1474 CA PRO B 30 2348 2069 1396 -243 -270 -533 C ATOM 1475 C PRO B 30 -30.812 -9.635 90.104 1.00 14.50 C ANISOU 1475 C PRO B 30 2190 1880 1437 -197 -176 -568 C ATOM 1476 O PRO B 30 -31.995 -9.902 89.941 1.00 14.09 O ANISOU 1476 O PRO B 30 2137 1833 1383 -165 -84 -570 O ATOM 1477 CB PRO B 30 -29.742 -9.627 92.378 1.00 16.79 C ANISOU 1477 CB PRO B 30 2611 2290 1478 -305 -300 -659 C ATOM 1478 CG PRO B 30 -28.346 -9.128 92.285 1.00 17.18 C ANISOU 1478 CG PRO B 30 2617 2315 1594 -334 -425 -667 C ATOM 1479 CD PRO B 30 -27.593 -10.201 91.554 1.00 16.38 C ANISOU 1479 CD PRO B 30 2449 2226 1549 -301 -495 -526 C ATOM 1480 N LYS B 31 -30.200 -8.634 89.480 1.00 14.38 N ANISOU 1480 N LYS B 31 2131 1784 1546 -198 -207 -594 N ATOM 1481 CA LYS B 31 -30.893 -7.778 88.512 1.00 13.99 C ANISOU 1481 CA LYS B 31 2043 1636 1635 -155 -145 -609 C ATOM 1482 C LYS B 31 -31.328 -8.550 87.255 1.00 12.63 C ANISOU 1482 C LYS B 31 1822 1458 1518 -104 -119 -492 C ATOM 1483 O LYS B 31 -32.447 -8.393 86.764 1.00 12.45 O ANISOU 1483 O LYS B 31 1782 1402 1545 -56 -59 -496 O ATOM 1484 CB LYS B 31 -29.986 -6.604 88.133 1.00 14.50 C ANISOU 1484 CB LYS B 31 2088 1609 1813 -187 -193 -640 C ATOM 1485 CG LYS B 31 -30.645 -5.532 87.292 1.00 14.62 C ANISOU 1485 CG LYS B 31 2088 1498 1968 -149 -147 -655 C ATOM 1486 CD LYS B 31 -29.719 -4.312 87.093 1.00 15.47 C ANISOU 1486 CD LYS B 31 2193 1500 2182 -202 -190 -690 C ATOM 1487 CE LYS B 31 -30.297 -3.422 85.999 1.00 15.56 C ANISOU 1487 CE LYS B 31 2200 1374 2337 -161 -161 -650 C ATOM 1488 NZ LYS B 31 -29.518 -2.201 85.751 1.00 16.51 N ANISOU 1488 NZ LYS B 31 2331 1368 2573 -219 -191 -673 N ATOM 1489 N THR B 32 -30.440 -9.388 86.754 1.00 11.82 N ANISOU 1489 N THR B 32 1692 1389 1410 -113 -168 -400 N ATOM 1490 CA THR B 32 -30.709 -10.178 85.582 1.00 10.81 C ANISOU 1490 CA THR B 32 1526 1261 1318 -76 -145 -305 C ATOM 1491 C THR B 32 -31.704 -11.291 85.900 1.00 10.52 C ANISOU 1491 C THR B 32 1507 1283 1205 -52 -102 -284 C ATOM 1492 O THR B 32 -32.619 -11.574 85.111 1.00 9.96 O ANISOU 1492 O THR B 32 1413 1200 1171 -17 -58 -254 O ATOM 1493 CB THR B 32 -29.385 -10.764 84.986 1.00 10.42 C ANISOU 1493 CB THR B 32 1433 1228 1296 -94 -196 -236 C ATOM 1494 OG1 THR B 32 -28.438 -9.697 84.789 1.00 10.84 O ANISOU 1494 OG1 THR B 32 1462 1230 1424 -135 -225 -264 O ATOM 1495 CG2 THR B 32 -29.646 -11.481 83.670 1.00 9.47 C ANISOU 1495 CG2 THR B 32 1281 1104 1211 -62 -161 -158 C ATOM 1496 N ALA B 33 -31.540 -11.931 87.054 1.00 11.00 N ANISOU 1496 N ALA B 33 1613 1407 1156 -80 -120 -294 N ATOM 1497 CA ALA B 33 -32.545 -12.900 87.477 1.00 10.93 C ANISOU 1497 CA ALA B 33 1634 1447 1070 -78 -64 -275 C ATOM 1498 C ALA B 33 -33.930 -12.229 87.648 1.00 11.27 C ANISOU 1498 C ALA B 33 1669 1478 1132 -64 29 -358 C ATOM 1499 O ALA B 33 -34.954 -12.813 87.265 1.00 11.05 O ANISOU 1499 O ALA B 33 1614 1462 1123 -45 89 -339 O ATOM 1500 CB ALA B 33 -32.121 -13.618 88.740 1.00 11.64 C ANISOU 1500 CB ALA B 33 1796 1601 1022 -122 -104 -258 C ATOM 1501 N GLU B 34 -33.985 -11.021 88.194 1.00 11.97 N ANISOU 1501 N GLU B 34 1772 1541 1234 -70 43 -461 N ATOM 1502 CA GLU B 34 -35.295 -10.373 88.438 1.00 12.61 C ANISOU 1502 CA GLU B 34 1831 1605 1354 -46 139 -561 C ATOM 1503 C GLU B 34 -36.028 -10.072 87.139 1.00 11.94 C ANISOU 1503 C GLU B 34 1666 1451 1416 20 148 -531 C ATOM 1504 O GLU B 34 -37.249 -10.174 87.061 1.00 12.22 O ANISOU 1504 O GLU B 34 1653 1494 1493 50 216 -567 O ATOM 1505 CB GLU B 34 -35.151 -9.079 89.249 1.00 13.85 C ANISOU 1505 CB GLU B 34 2019 1727 1514 -60 151 -694 C ATOM 1506 CG GLU B 34 -36.456 -8.271 89.430 1.00 14.83 C ANISOU 1506 CG GLU B 34 2101 1811 1720 -17 252 -818 C ATOM 1507 CD GLU B 34 -37.470 -9.013 90.262 1.00 15.60 C ANISOU 1507 CD GLU B 34 2206 2005 1717 -44 365 -865 C ATOM 1508 OE1 GLU B 34 -37.086 -10.004 90.928 1.00 15.75 O ANISOU 1508 OE1 GLU B 34 2295 2114 1575 -110 360 -809 O ATOM 1509 OE2 GLU B 34 -38.655 -8.618 90.278 1.00 16.37 O ANISOU 1509 OE2 GLU B 34 2236 2084 1899 -4 460 -957 O ATOM 1510 N ASN B 35 -35.278 -9.677 86.121 1.00 11.22 N ANISOU 1510 N ASN B 35 1561 1298 1404 37 76 -467 N ATOM 1511 CA ASN B 35 -35.871 -9.356 84.823 1.00 10.75 C ANISOU 1511 CA ASN B 35 1449 1175 1461 93 63 -421 C ATOM 1512 C ASN B 35 -36.572 -10.593 84.263 1.00 10.03 C ANISOU 1512 C ASN B 35 1322 1140 1347 104 81 -358 C ATOM 1513 O ASN B 35 -37.710 -10.518 83.836 1.00 10.08 O ANISOU 1513 O ASN B 35 1274 1134 1422 147 103 -374 O ATOM 1514 CB ASN B 35 -34.794 -8.847 83.869 1.00 10.34 C ANISOU 1514 CB ASN B 35 1409 1060 1458 83 -5 -349 C ATOM 1515 CG ASN B 35 -35.316 -8.596 82.478 1.00 10.15 C ANISOU 1515 CG ASN B 35 1358 981 1518 127 -31 -279 C ATOM 1516 OD1 ASN B 35 -36.258 -7.794 82.283 1.00 10.74 O ANISOU 1516 OD1 ASN B 35 1407 987 1684 181 -32 -313 O ATOM 1517 ND2 ASN B 35 -34.705 -9.262 81.490 1.00 9.33 N ANISOU 1517 ND2 ASN B 35 1259 902 1383 107 -58 -184 N ATOM 1518 N PHE B 36 -35.896 -11.742 84.335 1.00 9.45 N ANISOU 1518 N PHE B 36 1276 1125 1187 66 67 -294 N ATOM 1519 CA PHE B 36 -36.440 -12.988 83.777 1.00 8.93 C ANISOU 1519 CA PHE B 36 1186 1100 1107 67 82 -237 C ATOM 1520 C PHE B 36 -37.650 -13.416 84.552 1.00 9.45 C ANISOU 1520 C PHE B 36 1231 1209 1148 56 160 -291 C ATOM 1521 O PHE B 36 -38.647 -13.830 83.969 1.00 9.42 O ANISOU 1521 O PHE B 36 1170 1213 1196 73 181 -287 O ATOM 1522 CB PHE B 36 -35.396 -14.094 83.795 1.00 8.45 C ANISOU 1522 CB PHE B 36 1161 1070 979 35 50 -168 C ATOM 1523 CG PHE B 36 -35.783 -15.312 83.023 1.00 8.03 C ANISOU 1523 CG PHE B 36 1087 1033 930 36 56 -114 C ATOM 1524 CD1 PHE B 36 -35.535 -15.388 81.664 1.00 7.59 C ANISOU 1524 CD1 PHE B 36 1008 953 920 55 24 -74 C ATOM 1525 CD2 PHE B 36 -36.349 -16.410 83.663 1.00 8.28 C ANISOU 1525 CD2 PHE B 36 1134 1100 912 6 97 -105 C ATOM 1526 CE1 PHE B 36 -35.875 -16.517 80.943 1.00 7.32 C ANISOU 1526 CE1 PHE B 36 962 933 887 51 28 -44 C ATOM 1527 CE2 PHE B 36 -36.694 -17.558 82.946 1.00 7.97 C ANISOU 1527 CE2 PHE B 36 1077 1059 889 0 101 -65 C ATOM 1528 CZ PHE B 36 -36.460 -17.609 81.595 1.00 7.55 C ANISOU 1528 CZ PHE B 36 997 985 886 24 65 -43 C ATOM 1529 N ARG B 37 -37.556 -13.307 85.868 1.00 10.12 N ANISOU 1529 N ARG B 37 1362 1329 1151 19 204 -346 N ATOM 1530 CA ARG B 37 -38.624 -13.718 86.752 1.00 10.99 C ANISOU 1530 CA ARG B 37 1465 1493 1215 -12 304 -402 C ATOM 1531 C ARG B 37 -39.874 -12.881 86.479 1.00 11.63 C ANISOU 1531 C ARG B 37 1452 1549 1418 37 358 -493 C ATOM 1532 O ARG B 37 -40.933 -13.443 86.167 1.00 11.78 O ANISOU 1532 O ARG B 37 1398 1590 1486 39 405 -499 O ATOM 1533 CB ARG B 37 -38.194 -13.574 88.213 1.00 11.89 C ANISOU 1533 CB ARG B 37 1667 1655 1194 -69 338 -451 C ATOM 1534 CG ARG B 37 -39.167 -14.174 89.203 1.00 12.97 C ANISOU 1534 CG ARG B 37 1821 1863 1242 -129 458 -493 C ATOM 1535 CD ARG B 37 -38.998 -13.519 90.561 1.00 14.26 C ANISOU 1535 CD ARG B 37 2063 2070 1284 -175 509 -590 C ATOM 1536 NE ARG B 37 -39.358 -12.106 90.491 1.00 14.79 N ANISOU 1536 NE ARG B 37 2071 2089 1459 -120 538 -722 N ATOM 1537 CZ ARG B 37 -40.600 -11.625 90.490 1.00 15.64 C ANISOU 1537 CZ ARG B 37 2087 2190 1664 -89 645 -830 C ATOM 1538 NH1 ARG B 37 -41.655 -12.432 90.558 1.00 16.09 N ANISOU 1538 NH1 ARG B 37 2090 2301 1723 -118 745 -829 N ATOM 1539 NH2 ARG B 37 -40.789 -10.314 90.421 1.00 16.20 N ANISOU 1539 NH2 ARG B 37 2112 2193 1850 -27 651 -946 N ATOM 1540 N ALA B 38 -39.729 -11.554 86.569 1.00 12.11 N ANISOU 1540 N ALA B 38 1505 1551 1542 79 343 -567 N ATOM 1541 CA ALA B 38 -40.832 -10.622 86.282 1.00 13.04 C ANISOU 1541 CA ALA B 38 1527 1618 1809 148 375 -655 C ATOM 1542 C ALA B 38 -41.458 -10.835 84.877 1.00 12.68 C ANISOU 1542 C ALA B 38 1396 1538 1880 205 308 -585 C ATOM 1543 O ALA B 38 -42.687 -10.776 84.713 1.00 13.45 O ANISOU 1543 O ALA B 38 1389 1640 2082 244 345 -641 O ATOM 1544 CB ALA B 38 -40.379 -9.182 86.462 1.00 13.45 C ANISOU 1544 CB ALA B 38 1602 1581 1925 187 345 -726 C ATOM 1545 N LEU B 39 -40.630 -11.094 83.874 1.00 11.81 N ANISOU 1545 N LEU B 39 1327 1404 1754 205 212 -472 N ATOM 1546 CA LEU B 39 -41.153 -11.337 82.525 1.00 11.71 C ANISOU 1546 CA LEU B 39 1258 1373 1817 245 141 -405 C ATOM 1547 C LEU B 39 -41.900 -12.688 82.443 1.00 11.73 C ANISOU 1547 C LEU B 39 1213 1452 1791 206 180 -392 C ATOM 1548 O LEU B 39 -42.807 -12.833 81.642 1.00 12.12 O ANISOU 1548 O LEU B 39 1181 1501 1923 238 143 -388 O ATOM 1549 CB LEU B 39 -40.035 -11.282 81.474 1.00 10.82 C ANISOU 1549 CB LEU B 39 1213 1225 1672 239 49 -297 C ATOM 1550 CG LEU B 39 -39.315 -9.947 81.217 1.00 11.12 C ANISOU 1550 CG LEU B 39 1295 1171 1759 265 -2 -284 C ATOM 1551 CD1 LEU B 39 -38.038 -10.141 80.353 1.00 10.29 C ANISOU 1551 CD1 LEU B 39 1258 1058 1592 226 -54 -183 C ATOM 1552 CD2 LEU B 39 -40.274 -8.895 80.603 1.00 12.08 C ANISOU 1552 CD2 LEU B 39 1360 1206 2022 346 -55 -298 C ATOM 1553 N SER B 40 -41.511 -13.668 83.257 1.00 11.61 N ANISOU 1553 N SER B 40 1252 1495 1662 135 244 -382 N ATOM 1554 CA SER B 40 -42.159 -14.984 83.252 1.00 11.78 C ANISOU 1554 CA SER B 40 1243 1571 1659 84 288 -364 C ATOM 1555 C SER B 40 -43.512 -14.961 83.943 1.00 13.06 C ANISOU 1555 C SER B 40 1310 1772 1879 71 392 -461 C ATOM 1556 O SER B 40 -44.402 -15.745 83.594 1.00 13.26 O ANISOU 1556 O SER B 40 1260 1826 1951 45 414 -464 O ATOM 1557 CB SER B 40 -41.286 -16.044 83.931 1.00 11.33 C ANISOU 1557 CB SER B 40 1286 1545 1471 12 314 -307 C ATOM 1558 OG SER B 40 -40.073 -16.220 83.240 1.00 10.37 O ANISOU 1558 OG SER B 40 1225 1395 1320 24 228 -229 O ATOM 1559 N THR B 41 -43.650 -14.086 84.938 1.00 14.16 N ANISOU 1559 N THR B 41 1450 1913 2017 82 465 -551 N ATOM 1560 CA THR B 41 -44.908 -13.929 85.657 1.00 15.74 C ANISOU 1560 CA THR B 41 1548 2152 2278 72 589 -668 C ATOM 1561 C THR B 41 -45.842 -12.959 84.943 1.00 16.68 C ANISOU 1561 C THR B 41 1524 2220 2592 173 546 -738 C ATOM 1562 O THR B 41 -47.056 -12.990 85.192 1.00 17.97 O ANISOU 1562 O THR B 41 1554 2415 2857 177 630 -831 O ATOM 1563 CB THR B 41 -44.729 -13.470 87.170 1.00 16.71 C ANISOU 1563 CB THR B 41 1739 2312 2298 28 712 -762 C ATOM 1564 OG1 THR B 41 -44.440 -12.072 87.248 1.00 17.06 O ANISOU 1564 OG1 THR B 41 1783 2291 2408 103 680 -837 O ATOM 1565 CG2 THR B 41 -43.646 -14.282 87.909 1.00 16.15 C ANISOU 1565 CG2 THR B 41 1827 2282 2025 -61 715 -678 C ATOM 1566 N GLY B 42 -45.295 -12.095 84.087 1.00 16.30 N ANISOU 1566 N GLY B 42 1499 2089 2603 253 417 -691 N ATOM 1567 CA GLY B 42 -46.101 -11.063 83.403 1.00 17.49 C ANISOU 1567 CA GLY B 42 1533 2168 2944 361 348 -737 C ATOM 1568 C GLY B 42 -46.613 -9.922 84.285 1.00 19.13 C ANISOU 1568 C GLY B 42 1679 2333 3255 418 432 -885 C ATOM 1569 O GLY B 42 -47.495 -9.146 83.880 1.00 20.39 O ANISOU 1569 O GLY B 42 1712 2431 3603 516 392 -944 O ATOM 1570 N GLU B 43 -46.036 -9.784 85.473 1.00 19.42 N ANISOU 1570 N GLU B 43 1807 2398 3172 361 539 -948 N ATOM 1571 CA GLU B 43 -46.526 -8.817 86.453 1.00 21.13 C ANISOU 1571 CA GLU B 43 1976 2589 3461 396 651 -1117 C ATOM 1572 C GLU B 43 -46.262 -7.367 86.096 1.00 21.36 C ANISOU 1572 C GLU B 43 2008 2477 3630 500 561 -1150 C ATOM 1573 O GLU B 43 -46.835 -6.491 86.724 1.00 22.71 O ANISOU 1573 O GLU B 43 2111 2601 3914 554 641 -1305 O ATOM 1574 CB GLU B 43 -45.956 -9.100 87.854 1.00 21.69 C ANISOU 1574 CB GLU B 43 2166 2740 3333 290 784 -1179 C ATOM 1575 CG GLU B 43 -44.440 -9.003 87.938 1.00 20.80 C ANISOU 1575 CG GLU B 43 2224 2605 3073 249 696 -1088 C ATOM 1576 CD GLU B 43 -43.875 -9.579 89.226 1.00 21.30 C ANISOU 1576 CD GLU B 43 2411 2766 2914 135 791 -1111 C ATOM 1577 OE1 GLU B 43 -44.125 -10.777 89.573 1.00 21.46 O ANISOU 1577 OE1 GLU B 43 2450 2884 2819 53 857 -1061 O ATOM 1578 OE2 GLU B 43 -43.145 -8.815 89.891 1.00 22.08 O ANISOU 1578 OE2 GLU B 43 2598 2839 2949 123 787 -1175 O ATOM 1579 N LYS B 44 -45.404 -7.082 85.115 1.00 19.96 N ANISOU 1579 N LYS B 44 1910 2221 3450 525 407 -1012 N ATOM 1580 CA LYS B 44 -45.302 -5.692 84.656 1.00 20.51 C ANISOU 1580 CA LYS B 44 1977 2135 3678 624 316 -1027 C ATOM 1581 C LYS B 44 -46.321 -5.368 83.527 1.00 20.99 C ANISOU 1581 C LYS B 44 1907 2124 3943 738 202 -986 C ATOM 1582 O LYS B 44 -46.319 -4.272 83.007 1.00 21.68 O ANISOU 1582 O LYS B 44 1994 2068 4174 827 103 -969 O ATOM 1583 CB LYS B 44 -43.880 -5.344 84.213 1.00 19.49 C ANISOU 1583 CB LYS B 44 2000 1944 3461 588 217 -908 C ATOM 1584 CG LYS B 44 -42.792 -5.465 85.285 1.00 19.08 C ANISOU 1584 CG LYS B 44 2069 1943 3237 490 290 -949 C ATOM 1585 CD LYS B 44 -42.939 -4.447 86.400 1.00 20.64 C ANISOU 1585 CD LYS B 44 2268 2085 3488 507 379 -1130 C ATOM 1586 CE LYS B 44 -41.819 -4.593 87.459 1.00 20.31 C ANISOU 1586 CE LYS B 44 2355 2107 3254 400 427 -1169 C ATOM 1587 NZ LYS B 44 -41.662 -3.350 88.266 1.00 21.64 N ANISOU 1587 NZ LYS B 44 2555 2183 3483 414 468 -1330 N ATOM 1588 N GLY B 45 -47.187 -6.309 83.158 1.00 20.63 N ANISOU 1588 N GLY B 45 1754 2172 3913 731 205 -968 N ATOM 1589 CA GLY B 45 -48.123 -6.105 82.048 1.00 21.29 C ANISOU 1589 CA GLY B 45 1711 2203 4172 830 69 -921 C ATOM 1590 C GLY B 45 -47.571 -6.510 80.688 1.00 19.96 C ANISOU 1590 C GLY B 45 1630 2031 3920 812 -96 -729 C ATOM 1591 O GLY B 45 -48.177 -6.241 79.669 1.00 20.70 O ANISOU 1591 O GLY B 45 1659 2075 4131 889 -242 -666 O ATOM 1592 N PHE B 46 -46.403 -7.142 80.671 1.00 18.09 N ANISOU 1592 N PHE B 46 1542 1848 3481 710 -77 -641 N ATOM 1593 CA PHE B 46 -45.844 -7.750 79.451 1.00 16.89 C ANISOU 1593 CA PHE B 46 1472 1721 3222 671 -195 -482 C ATOM 1594 C PHE B 46 -44.929 -8.849 79.890 1.00 15.25 C ANISOU 1594 C PHE B 46 1359 1614 2820 555 -107 -456 C ATOM 1595 O PHE B 46 -44.466 -8.851 81.010 1.00 15.00 O ANISOU 1595 O PHE B 46 1368 1605 2726 511 4 -524 O ATOM 1596 CB PHE B 46 -45.058 -6.747 78.576 1.00 16.88 C ANISOU 1596 CB PHE B 46 1583 1600 3230 705 -321 -366 C ATOM 1597 CG PHE B 46 -44.108 -5.854 79.340 1.00 16.74 C ANISOU 1597 CG PHE B 46 1657 1500 3200 690 -262 -402 C ATOM 1598 CD1 PHE B 46 -44.538 -4.644 79.863 1.00 18.18 C ANISOU 1598 CD1 PHE B 46 1794 1562 3549 773 -254 -496 C ATOM 1599 CD2 PHE B 46 -42.776 -6.204 79.514 1.00 15.42 C ANISOU 1599 CD2 PHE B 46 1614 1370 2872 594 -221 -351 C ATOM 1600 CE1 PHE B 46 -43.638 -3.792 80.573 1.00 18.22 C ANISOU 1600 CE1 PHE B 46 1891 1485 3546 749 -204 -543 C ATOM 1601 CE2 PHE B 46 -41.884 -5.376 80.216 1.00 15.44 C ANISOU 1601 CE2 PHE B 46 1694 1302 2870 571 -179 -391 C ATOM 1602 CZ PHE B 46 -42.316 -4.166 80.736 1.00 16.85 C ANISOU 1602 CZ PHE B 46 1838 1359 3202 642 -172 -488 C ATOM 1603 N GLY B 47 -44.629 -9.773 79.002 1.00 14.34 N ANISOU 1603 N GLY B 47 1285 1554 2606 506 -165 -357 N ATOM 1604 CA GLY B 47 -43.736 -10.853 79.370 1.00 13.02 C ANISOU 1604 CA GLY B 47 1202 1465 2279 410 -92 -330 C ATOM 1605 C GLY B 47 -43.758 -11.950 78.352 1.00 12.42 C ANISOU 1605 C GLY B 47 1136 1446 2135 369 -150 -256 C ATOM 1606 O GLY B 47 -44.204 -11.745 77.242 1.00 12.98 O ANISOU 1606 O GLY B 47 1183 1498 2249 407 -262 -206 O ATOM 1607 N TYR B 48 -43.268 -13.114 78.747 1.00 11.49 N ANISOU 1607 N TYR B 48 1061 1394 1910 292 -78 -250 N ATOM 1608 CA TYR B 48 -42.925 -14.153 77.824 1.00 10.90 C ANISOU 1608 CA TYR B 48 1027 1357 1757 246 -120 -186 C ATOM 1609 C TYR B 48 -44.122 -14.958 77.323 1.00 11.58 C ANISOU 1609 C TYR B 48 1017 1488 1893 234 -148 -214 C ATOM 1610 O TYR B 48 -44.000 -15.659 76.303 1.00 11.17 O ANISOU 1610 O TYR B 48 994 1459 1789 206 -210 -172 O ATOM 1611 CB TYR B 48 -41.920 -15.106 78.458 1.00 9.91 C ANISOU 1611 CB TYR B 48 979 1261 1523 178 -44 -171 C ATOM 1612 CG TYR B 48 -40.538 -14.539 78.729 1.00 9.34 C ANISOU 1612 CG TYR B 48 999 1157 1393 175 -40 -135 C ATOM 1613 CD1 TYR B 48 -39.820 -13.841 77.734 1.00 9.22 C ANISOU 1613 CD1 TYR B 48 1034 1102 1367 193 -109 -74 C ATOM 1614 CD2 TYR B 48 -39.915 -14.738 79.981 1.00 9.08 C ANISOU 1614 CD2 TYR B 48 1003 1136 1307 143 30 -158 C ATOM 1615 CE1 TYR B 48 -38.527 -13.349 77.986 1.00 8.82 C ANISOU 1615 CE1 TYR B 48 1050 1024 1277 176 -97 -48 C ATOM 1616 CE2 TYR B 48 -38.646 -14.244 80.247 1.00 8.70 C ANISOU 1616 CE2 TYR B 48 1022 1064 1218 135 21 -134 C ATOM 1617 CZ TYR B 48 -37.951 -13.562 79.239 1.00 8.61 C ANISOU 1617 CZ TYR B 48 1041 1013 1218 150 -38 -84 C ATOM 1618 OH TYR B 48 -36.696 -13.086 79.512 1.00 8.52 O ANISOU 1618 OH TYR B 48 1077 978 1181 131 -40 -68 O ATOM 1619 N LYS B 49 -45.258 -14.869 78.018 1.00 12.60 N ANISOU 1619 N LYS B 49 1028 1633 2124 249 -97 -296 N ATOM 1620 CA LYS B 49 -46.351 -15.788 77.743 1.00 13.42 C ANISOU 1620 CA LYS B 49 1027 1788 2282 214 -99 -336 C ATOM 1621 C LYS B 49 -46.819 -15.560 76.319 1.00 14.14 C ANISOU 1621 C LYS B 49 1082 1873 2414 257 -260 -299 C ATOM 1622 O LYS B 49 -47.044 -14.433 75.924 1.00 14.68 O ANISOU 1622 O LYS B 49 1127 1895 2555 340 -350 -282 O ATOM 1623 CB LYS B 49 -47.518 -15.608 78.709 1.00 14.55 C ANISOU 1623 CB LYS B 49 1027 1954 2545 221 -5 -441 C ATOM 1624 CG LYS B 49 -48.712 -16.501 78.368 1.00 15.49 C ANISOU 1624 CG LYS B 49 1012 2125 2746 177 -12 -489 C ATOM 1625 CD LYS B 49 -49.832 -16.391 79.414 1.00 16.79 C ANISOU 1625 CD LYS B 49 1023 2322 3031 166 117 -604 C ATOM 1626 CE LYS B 49 -51.016 -17.231 79.015 1.00 17.85 C ANISOU 1626 CE LYS B 49 1005 2507 3269 114 104 -656 C ATOM 1627 NZ LYS B 49 -51.919 -17.393 80.180 1.00 19.16 N ANISOU 1627 NZ LYS B 49 1043 2718 3518 63 282 -764 N ATOM 1628 N GLY B 50 -46.929 -16.639 75.551 1.00 14.27 N ANISOU 1628 N GLY B 50 1110 1932 2381 197 -302 -284 N ATOM 1629 CA GLY B 50 -47.334 -16.549 74.154 1.00 15.18 C ANISOU 1629 CA GLY B 50 1212 2057 2498 219 -464 -250 C ATOM 1630 C GLY B 50 -46.181 -16.299 73.203 1.00 14.85 C ANISOU 1630 C GLY B 50 1328 1996 2317 219 -531 -157 C ATOM 1631 O GLY B 50 -46.372 -16.375 72.018 1.00 15.53 O ANISOU 1631 O GLY B 50 1439 2103 2358 215 -655 -123 O ATOM 1632 N SER B 51 -44.983 -15.998 73.688 1.00 14.24 N ANISOU 1632 N SER B 51 1356 1886 2168 214 -451 -119 N ATOM 1633 CA SER B 51 -43.847 -15.790 72.777 1.00 14.20 C ANISOU 1633 CA SER B 51 1488 1869 2037 200 -492 -39 C ATOM 1634 C SER B 51 -43.247 -17.105 72.257 1.00 14.11 C ANISOU 1634 C SER B 51 1542 1902 1916 122 -455 -48 C ATOM 1635 O SER B 51 -43.542 -18.169 72.772 1.00 13.98 O ANISOU 1635 O SER B 51 1482 1907 1922 79 -390 -105 O ATOM 1636 CB SER B 51 -42.778 -14.929 73.425 1.00 13.46 C ANISOU 1636 CB SER B 51 1464 1721 1926 220 -428 -4 C ATOM 1637 OG SER B 51 -42.165 -15.571 74.504 1.00 12.72 O ANISOU 1637 OG SER B 51 1381 1638 1813 182 -305 -41 O ATOM 1638 N CYS B 52 -42.415 -17.018 71.231 1.00 14.78 N ANISOU 1638 N CYS B 52 1734 1995 1887 101 -490 3 N ATOM 1639 CA CYS B 52 -41.952 -18.181 70.512 1.00 15.18 C ANISOU 1639 CA CYS B 52 1841 2085 1840 36 -467 -22 C ATOM 1640 C CYS B 52 -40.441 -18.346 70.730 1.00 13.81 C ANISOU 1640 C CYS B 52 1750 1894 1602 14 -362 -5 C ATOM 1641 O CYS B 52 -39.771 -17.405 71.164 1.00 13.74 O ANISOU 1641 O CYS B 52 1766 1851 1603 41 -336 41 O ATOM 1642 CB CYS B 52 -42.334 -18.074 69.020 1.00 17.30 C ANISOU 1642 CB CYS B 52 2159 2396 2016 18 -591 1 C ATOM 1643 SG CYS B 52 -41.091 -17.161 68.136 1.00 19.26 S ANISOU 1643 SG CYS B 52 2553 2637 2128 6 -591 95 S ATOM 1644 N PHE B 53 -39.913 -19.559 70.527 1.00 12.80 N ANISOU 1644 N PHE B 53 1650 1782 1432 -31 -301 -53 N ATOM 1645 CA PHE B 53 -38.463 -19.750 70.408 1.00 11.70 C ANISOU 1645 CA PHE B 53 1576 1633 1235 -48 -219 -45 C ATOM 1646 C PHE B 53 -38.182 -19.635 68.936 1.00 11.87 C ANISOU 1646 C PHE B 53 1676 1698 1134 -85 -251 -37 C ATOM 1647 O PHE B 53 -38.482 -20.554 68.171 1.00 12.40 O ANISOU 1647 O PHE B 53 1761 1798 1149 -124 -265 -97 O ATOM 1648 CB PHE B 53 -38.000 -21.130 70.901 1.00 11.37 C ANISOU 1648 CB PHE B 53 1522 1571 1227 -69 -139 -106 C ATOM 1649 CG PHE B 53 -37.905 -21.239 72.375 1.00 10.71 C ANISOU 1649 CG PHE B 53 1394 1446 1226 -45 -95 -95 C ATOM 1650 CD1 PHE B 53 -39.034 -21.372 73.137 1.00 10.63 C ANISOU 1650 CD1 PHE B 53 1327 1431 1281 -44 -109 -106 C ATOM 1651 CD2 PHE B 53 -36.675 -21.193 73.012 1.00 10.31 C ANISOU 1651 CD2 PHE B 53 1360 1369 1187 -29 -39 -75 C ATOM 1652 CE1 PHE B 53 -38.976 -21.483 74.491 1.00 10.24 C ANISOU 1652 CE1 PHE B 53 1256 1355 1279 -37 -59 -94 C ATOM 1653 CE2 PHE B 53 -36.616 -21.309 74.392 1.00 9.88 C ANISOU 1653 CE2 PHE B 53 1282 1284 1186 -14 -13 -60 C ATOM 1654 CZ PHE B 53 -37.794 -21.458 75.124 1.00 9.88 C ANISOU 1654 CZ PHE B 53 1244 1284 1224 -22 -19 -68 C ATOM 1655 N HIS B 54 -37.627 -18.505 68.523 1.00 11.41 N ANISOU 1655 N HIS B 54 1674 1639 1021 -82 -262 35 N ATOM 1656 CA HIS B 54 -37.512 -18.218 67.089 1.00 12.07 C ANISOU 1656 CA HIS B 54 1853 1771 962 -128 -303 65 C ATOM 1657 C HIS B 54 -36.249 -18.823 66.481 1.00 11.94 C ANISOU 1657 C HIS B 54 1894 1785 857 -183 -186 20 C ATOM 1658 O HIS B 54 -36.139 -18.940 65.265 1.00 13.03 O ANISOU 1658 O HIS B 54 2116 1979 853 -238 -191 12 O ATOM 1659 CB HIS B 54 -37.534 -16.707 66.869 1.00 12.44 C ANISOU 1659 CB HIS B 54 1947 1790 990 -111 -368 178 C ATOM 1660 CG HIS B 54 -36.390 -15.997 67.514 1.00 11.75 C ANISOU 1660 CG HIS B 54 1863 1655 945 -108 -278 215 C ATOM 1661 ND1 HIS B 54 -36.362 -15.708 68.858 1.00 10.68 N ANISOU 1661 ND1 HIS B 54 1650 1464 942 -58 -254 205 N ATOM 1662 CD2 HIS B 54 -35.218 -15.544 67.003 1.00 12.08 C ANISOU 1662 CD2 HIS B 54 1974 1702 914 -161 -201 253 C ATOM 1663 CE1 HIS B 54 -35.227 -15.102 69.153 1.00 10.47 C ANISOU 1663 CE1 HIS B 54 1643 1409 927 -76 -183 233 C ATOM 1664 NE2 HIS B 54 -34.514 -14.983 68.044 1.00 11.31 N ANISOU 1664 NE2 HIS B 54 1829 1548 920 -139 -146 264 N ATOM 1665 N ARG B 55 -35.287 -19.191 67.322 1.00 10.76 N ANISOU 1665 N ARG B 55 1695 1601 789 -167 -81 -13 N ATOM 1666 CA ARG B 55 -33.951 -19.600 66.850 1.00 10.87 C ANISOU 1666 CA ARG B 55 1736 1637 758 -205 39 -59 C ATOM 1667 C ARG B 55 -33.465 -20.812 67.644 1.00 10.15 C ANISOU 1667 C ARG B 55 1571 1508 777 -175 108 -144 C ATOM 1668 O ARG B 55 -33.085 -20.693 68.825 1.00 9.14 O ANISOU 1668 O ARG B 55 1381 1331 758 -132 120 -122 O ATOM 1669 CB ARG B 55 -32.965 -18.434 66.975 1.00 10.79 C ANISOU 1669 CB ARG B 55 1740 1612 747 -219 88 14 C ATOM 1670 CG ARG B 55 -31.621 -18.646 66.304 1.00 11.48 C ANISOU 1670 CG ARG B 55 1845 1735 780 -273 221 -29 C ATOM 1671 CD ARG B 55 -30.803 -17.359 66.320 1.00 11.71 C ANISOU 1671 CD ARG B 55 1892 1750 804 -308 259 54 C ATOM 1672 NE ARG B 55 -29.424 -17.518 65.847 1.00 12.40 N ANISOU 1672 NE ARG B 55 1964 1872 873 -364 406 4 N ATOM 1673 CZ ARG B 55 -28.341 -17.368 66.605 1.00 12.04 C ANISOU 1673 CZ ARG B 55 1826 1798 950 -353 474 -13 C ATOM 1674 NH1 ARG B 55 -28.429 -17.027 67.891 1.00 10.95 N ANISOU 1674 NH1 ARG B 55 1621 1599 939 -293 406 16 N ATOM 1675 NH2 ARG B 55 -27.150 -17.524 66.065 1.00 12.97 N ANISOU 1675 NH2 ARG B 55 1913 1955 1059 -407 612 -69 N ATOM 1676 N ILE B 56 -33.536 -21.978 66.996 1.00 10.64 N ANISOU 1676 N ILE B 56 1648 1586 807 -198 140 -240 N ATOM 1677 CA ILE B 56 -33.088 -23.228 67.588 1.00 10.35 C ANISOU 1677 CA ILE B 56 1556 1495 882 -169 198 -321 C ATOM 1678 C ILE B 56 -31.999 -23.877 66.716 1.00 11.32 C ANISOU 1678 C ILE B 56 1692 1637 971 -194 313 -421 C ATOM 1679 O ILE B 56 -32.269 -24.355 65.609 1.00 12.22 O ANISOU 1679 O ILE B 56 1866 1795 981 -243 330 -498 O ATOM 1680 CB ILE B 56 -34.253 -24.202 67.828 1.00 10.27 C ANISOU 1680 CB ILE B 56 1532 1453 915 -167 136 -364 C ATOM 1681 CG1 ILE B 56 -35.289 -23.588 68.778 1.00 9.43 C ANISOU 1681 CG1 ILE B 56 1390 1332 859 -143 49 -282 C ATOM 1682 CG2 ILE B 56 -33.711 -25.486 68.434 1.00 10.23 C ANISOU 1682 CG2 ILE B 56 1486 1367 1031 -138 194 -431 C ATOM 1683 CD1 ILE B 56 -36.549 -24.398 68.922 1.00 9.59 C ANISOU 1683 CD1 ILE B 56 1388 1335 919 -161 -6 -321 C ATOM 1684 N ILE B 57 -30.766 -23.850 67.223 1.00 11.23 N ANISOU 1684 N ILE B 57 1619 1596 1048 -162 391 -428 N ATOM 1685 CA ILE B 57 -29.607 -24.420 66.515 1.00 12.41 C ANISOU 1685 CA ILE B 57 1749 1760 1205 -175 519 -535 C ATOM 1686 C ILE B 57 -29.190 -25.682 67.272 1.00 12.56 C ANISOU 1686 C ILE B 57 1690 1683 1396 -104 536 -605 C ATOM 1687 O ILE B 57 -28.603 -25.587 68.358 1.00 11.85 O ANISOU 1687 O ILE B 57 1527 1542 1432 -47 515 -555 O ATOM 1688 CB ILE B 57 -28.425 -23.427 66.397 1.00 12.62 C ANISOU 1688 CB ILE B 57 1744 1827 1222 -196 601 -499 C ATOM 1689 CG1 ILE B 57 -28.891 -22.138 65.691 1.00 12.76 C ANISOU 1689 CG1 ILE B 57 1858 1915 1073 -269 571 -404 C ATOM 1690 CG2 ILE B 57 -27.249 -24.075 65.634 1.00 13.95 C ANISOU 1690 CG2 ILE B 57 1871 2017 1410 -212 755 -632 C ATOM 1691 CD1 ILE B 57 -27.847 -21.011 65.566 1.00 13.09 C ANISOU 1691 CD1 ILE B 57 1885 1987 1100 -313 648 -348 C ATOM 1692 N PRO B 58 -29.543 -26.866 66.728 1.00 13.58 N ANISOU 1692 N PRO B 58 1845 1781 1533 -110 557 -717 N ATOM 1693 CA PRO B 58 -29.222 -28.102 67.442 1.00 13.93 C ANISOU 1693 CA PRO B 58 1830 1708 1755 -41 560 -772 C ATOM 1694 C PRO B 58 -27.739 -28.250 67.634 1.00 14.79 C ANISOU 1694 C PRO B 58 1843 1788 1988 14 645 -819 C ATOM 1695 O PRO B 58 -26.972 -27.919 66.725 1.00 15.77 O ANISOU 1695 O PRO B 58 1954 1983 2053 -18 757 -892 O ATOM 1696 CB PRO B 58 -29.762 -29.184 66.520 1.00 14.98 C ANISOU 1696 CB PRO B 58 2016 1820 1854 -76 589 -907 C ATOM 1697 CG PRO B 58 -30.973 -28.494 65.874 1.00 14.66 C ANISOU 1697 CG PRO B 58 2064 1875 1629 -156 519 -862 C ATOM 1698 CD PRO B 58 -30.450 -27.116 65.591 1.00 14.34 C ANISOU 1698 CD PRO B 58 2033 1932 1481 -180 546 -781 C ATOM 1699 N GLY B 59 -27.351 -28.707 68.818 1.00 14.70 N ANISOU 1699 N GLY B 59 1763 1679 2143 94 590 -773 N ATOM 1700 CA GLY B 59 -25.945 -28.847 69.180 1.00 15.66 C ANISOU 1700 CA GLY B 59 1769 1763 2415 163 636 -805 C ATOM 1701 C GLY B 59 -25.355 -27.545 69.703 1.00 15.16 C ANISOU 1701 C GLY B 59 1657 1770 2332 154 617 -707 C ATOM 1702 O GLY B 59 -24.148 -27.423 69.897 1.00 15.80 O ANISOU 1702 O GLY B 59 1628 1849 2526 193 657 -735 O ATOM 1703 N PHE B 60 -26.200 -26.562 69.948 1.00 14.29 N ANISOU 1703 N PHE B 60 1617 1715 2094 103 552 -599 N ATOM 1704 CA PHE B 60 -25.702 -25.254 70.330 1.00 14.06 C ANISOU 1704 CA PHE B 60 1557 1745 2039 81 540 -518 C ATOM 1705 C PHE B 60 -26.623 -24.684 71.409 1.00 13.07 C ANISOU 1705 C PHE B 60 1480 1605 1878 84 418 -395 C ATOM 1706 O PHE B 60 -26.301 -24.768 72.618 1.00 12.76 O ANISOU 1706 O PHE B 60 1397 1519 1932 135 344 -342 O ATOM 1707 CB PHE B 60 -25.535 -24.368 69.067 1.00 14.57 C ANISOU 1707 CB PHE B 60 1661 1910 1964 -6 642 -544 C ATOM 1708 CG PHE B 60 -25.128 -22.930 69.346 1.00 14.26 C ANISOU 1708 CG PHE B 60 1608 1917 1892 -47 634 -455 C ATOM 1709 CD1 PHE B 60 -24.436 -22.578 70.503 1.00 13.94 C ANISOU 1709 CD1 PHE B 60 1478 1843 1974 -5 577 -409 C ATOM 1710 CD2 PHE B 60 -25.436 -21.933 68.434 1.00 14.46 C ANISOU 1710 CD2 PHE B 60 1717 2013 1763 -134 674 -416 C ATOM 1711 CE1 PHE B 60 -24.097 -21.266 70.743 1.00 13.81 C ANISOU 1711 CE1 PHE B 60 1453 1859 1933 -52 568 -341 C ATOM 1712 CE2 PHE B 60 -25.079 -20.621 68.666 1.00 14.32 C ANISOU 1712 CE2 PHE B 60 1696 2016 1729 -178 667 -333 C ATOM 1713 CZ PHE B 60 -24.396 -20.287 69.812 1.00 13.96 C ANISOU 1713 CZ PHE B 60 1554 1933 1815 -139 621 -304 C ATOM 1714 N MET B 61 -27.772 -24.151 70.995 1.00 12.81 N ANISOU 1714 N MET B 61 1536 1614 1715 32 393 -356 N ATOM 1715 CA MET B 61 -28.695 -23.483 71.935 1.00 11.98 C ANISOU 1715 CA MET B 61 1466 1506 1580 33 298 -258 C ATOM 1716 C MET B 61 -30.104 -23.280 71.379 1.00 11.69 C ANISOU 1716 C MET B 61 1506 1498 1436 -6 265 -241 C ATOM 1717 O MET B 61 -30.330 -23.356 70.158 1.00 12.18 O ANISOU 1717 O MET B 61 1611 1603 1412 -48 302 -288 O ATOM 1718 CB MET B 61 -28.101 -22.148 72.410 1.00 11.87 C ANISOU 1718 CB MET B 61 1426 1520 1564 21 285 -196 C ATOM 1719 CG MET B 61 -27.832 -21.141 71.301 1.00 12.41 C ANISOU 1719 CG MET B 61 1522 1648 1542 -41 347 -193 C ATOM 1720 SD MET B 61 -29.245 -20.079 70.977 1.00 12.34 S ANISOU 1720 SD MET B 61 1609 1664 1412 -78 280 -115 S ATOM 1721 CE MET B 61 -29.304 -20.127 69.187 1.00 13.00 C ANISOU 1721 CE MET B 61 1767 1812 1359 -145 349 -151 C ATOM 1722 N CYS B 62 -31.051 -23.074 72.293 1.00 11.08 N ANISOU 1722 N CYS B 62 1440 1402 1365 4 192 -183 N ATOM 1723 CA CYS B 62 -32.400 -22.638 71.938 1.00 10.92 C ANISOU 1723 CA CYS B 62 1463 1413 1272 -24 145 -160 C ATOM 1724 C CYS B 62 -32.666 -21.213 72.432 1.00 10.17 C ANISOU 1724 C CYS B 62 1371 1337 1157 -21 104 -87 C ATOM 1725 O CYS B 62 -32.496 -20.920 73.608 1.00 9.84 O ANISOU 1725 O CYS B 62 1303 1269 1164 2 86 -55 O ATOM 1726 CB CYS B 62 -33.447 -23.558 72.554 1.00 11.01 C ANISOU 1726 CB CYS B 62 1472 1386 1325 -20 110 -168 C ATOM 1727 SG CYS B 62 -33.302 -25.305 72.205 1.00 12.41 S ANISOU 1727 SG CYS B 62 1652 1503 1559 -23 146 -252 S ATOM 1728 N GLN B 63 -33.120 -20.330 71.550 1.00 10.16 N ANISOU 1728 N GLN B 63 1407 1372 1079 -47 81 -62 N ATOM 1729 CA GLN B 63 -33.271 -18.923 71.889 1.00 9.64 C ANISOU 1729 CA GLN B 63 1349 1302 1011 -41 44 3 C ATOM 1730 C GLN B 63 -34.697 -18.432 71.695 1.00 9.63 C ANISOU 1730 C GLN B 63 1359 1306 991 -32 -33 28 C ATOM 1731 O GLN B 63 -35.301 -18.653 70.643 1.00 10.08 O ANISOU 1731 O GLN B 63 1448 1395 984 -53 -67 20 O ATOM 1732 CB GLN B 63 -32.313 -18.089 71.040 1.00 10.06 C ANISOU 1732 CB GLN B 63 1437 1373 1012 -78 83 31 C ATOM 1733 CG GLN B 63 -32.487 -16.571 71.128 1.00 10.10 C ANISOU 1733 CG GLN B 63 1469 1353 1014 -82 40 105 C ATOM 1734 CD GLN B 63 -31.471 -15.843 70.254 1.00 10.86 C ANISOU 1734 CD GLN B 63 1608 1460 1055 -140 95 140 C ATOM 1735 OE1 GLN B 63 -30.539 -16.471 69.745 1.00 11.25 O ANISOU 1735 OE1 GLN B 63 1648 1545 1081 -173 179 96 O ATOM 1736 NE2 GLN B 63 -31.637 -14.535 70.082 1.00 11.01 N ANISOU 1736 NE2 GLN B 63 1675 1445 1064 -156 56 217 N ATOM 1737 N GLY B 64 -35.209 -17.730 72.702 1.00 9.09 N ANISOU 1737 N GLY B 64 1260 1209 983 0 -64 51 N ATOM 1738 CA GLY B 64 -36.444 -16.978 72.542 1.00 9.36 C ANISOU 1738 CA GLY B 64 1286 1239 1030 22 -138 74 C ATOM 1739 C GLY B 64 -36.581 -15.771 73.444 1.00 9.21 C ANISOU 1739 C GLY B 64 1248 1176 1075 57 -153 96 C ATOM 1740 O GLY B 64 -35.591 -15.192 73.893 1.00 8.96 O ANISOU 1740 O GLY B 64 1233 1118 1054 50 -120 111 O ATOM 1741 N GLY B 65 -37.831 -15.390 73.689 1.00 9.65 N ANISOU 1741 N GLY B 65 1259 1220 1185 93 -204 86 N ATOM 1742 CA GLY B 65 -38.192 -14.325 74.616 1.00 9.94 C ANISOU 1742 CA GLY B 65 1265 1210 1300 135 -210 78 C ATOM 1743 C GLY B 65 -38.400 -12.999 73.920 1.00 10.89 C ANISOU 1743 C GLY B 65 1414 1276 1446 165 -285 135 C ATOM 1744 O GLY B 65 -38.440 -11.940 74.565 1.00 11.21 O ANISOU 1744 O GLY B 65 1446 1254 1559 199 -288 129 O ATOM 1745 N ASN B 66 -38.534 -13.032 72.600 1.00 11.66 N ANISOU 1745 N ASN B 66 1557 1390 1481 150 -349 190 N ATOM 1746 CA ASN B 66 -38.948 -11.843 71.889 1.00 12.90 C ANISOU 1746 CA ASN B 66 1750 1489 1661 183 -447 263 C ATOM 1747 C ASN B 66 -40.472 -11.822 71.878 1.00 13.85 C ANISOU 1747 C ASN B 66 1784 1609 1868 247 -536 235 C ATOM 1748 O ASN B 66 -41.104 -12.505 71.080 1.00 14.24 O ANISOU 1748 O ASN B 66 1821 1715 1872 235 -600 236 O ATOM 1749 CB ASN B 66 -38.372 -11.802 70.474 1.00 13.54 C ANISOU 1749 CB ASN B 66 1937 1592 1614 127 -481 347 C ATOM 1750 CG ASN B 66 -38.780 -10.565 69.731 1.00 14.87 C ANISOU 1750 CG ASN B 66 2165 1688 1795 156 -595 448 C ATOM 1751 OD1 ASN B 66 -39.554 -9.750 70.247 1.00 15.39 O ANISOU 1751 OD1 ASN B 66 2177 1678 1990 231 -658 446 O ATOM 1752 ND2 ASN B 66 -38.288 -10.412 68.507 1.00 15.60 N ANISOU 1752 ND2 ASN B 66 2372 1799 1754 95 -623 537 N ATOM 1753 N PHE B 67 -41.061 -11.054 72.789 1.00 14.40 N ANISOU 1753 N PHE B 67 1783 1618 2071 311 -538 195 N ATOM 1754 CA PHE B 67 -42.516 -10.998 72.891 1.00 15.42 C ANISOU 1754 CA PHE B 67 1797 1745 2314 379 -608 149 C ATOM 1755 C PHE B 67 -43.130 -9.954 71.967 1.00 17.19 C ANISOU 1755 C PHE B 67 2033 1898 2597 444 -764 230 C ATOM 1756 O PHE B 67 -44.343 -9.848 71.896 1.00 18.27 O ANISOU 1756 O PHE B 67 2063 2031 2845 510 -849 199 O ATOM 1757 CB PHE B 67 -42.970 -10.806 74.331 1.00 15.18 C ANISOU 1757 CB PHE B 67 1667 1695 2402 416 -518 44 C ATOM 1758 CG PHE B 67 -42.379 -9.609 75.005 1.00 15.26 C ANISOU 1758 CG PHE B 67 1717 1611 2468 445 -484 41 C ATOM 1759 CD1 PHE B 67 -42.849 -8.331 74.714 1.00 16.56 C ANISOU 1759 CD1 PHE B 67 1872 1666 2752 525 -577 71 C ATOM 1760 CD2 PHE B 67 -41.365 -9.757 75.934 1.00 14.25 C ANISOU 1760 CD2 PHE B 67 1635 1494 2283 394 -373 6 C ATOM 1761 CE1 PHE B 67 -42.305 -7.217 75.330 1.00 16.82 C ANISOU 1761 CE1 PHE B 67 1945 1594 2848 545 -545 57 C ATOM 1762 CE2 PHE B 67 -40.817 -8.651 76.579 1.00 14.49 C ANISOU 1762 CE2 PHE B 67 1700 1437 2365 410 -347 -12 C ATOM 1763 CZ PHE B 67 -41.288 -7.375 76.270 1.00 15.81 C ANISOU 1763 CZ PHE B 67 1862 1488 2655 482 -427 8 C ATOM 1764 N THR B 68 -42.322 -9.198 71.235 1.00 17.87 N ANISOU 1764 N THR B 68 2248 1927 2613 423 -808 339 N ATOM 1765 CA THR B 68 -42.891 -8.294 70.228 1.00 19.76 C ANISOU 1765 CA THR B 68 2527 2096 2884 476 -977 446 C ATOM 1766 C THR B 68 -43.092 -9.024 68.894 1.00 20.55 C ANISOU 1766 C THR B 68 2686 2287 2831 426 -1076 510 C ATOM 1767 O THR B 68 -44.096 -8.781 68.211 1.00 21.92 O ANISOU 1767 O THR B 68 2827 2451 3047 482 -1241 553 O ATOM 1768 CB THR B 68 -42.057 -7.011 70.048 1.00 20.38 C ANISOU 1768 CB THR B 68 2726 2049 2968 472 -989 548 C ATOM 1769 OG1 THR B 68 -40.886 -7.290 69.273 1.00 20.14 O ANISOU 1769 OG1 THR B 68 2836 2065 2751 362 -940 628 O ATOM 1770 CG2 THR B 68 -41.637 -6.459 71.397 1.00 19.58 C ANISOU 1770 CG2 THR B 68 2581 1876 2983 492 -871 460 C ATOM 1771 N HIS B 69 -42.169 -9.920 68.529 1.00 19.96 N ANISOU 1771 N HIS B 69 2693 2301 2589 326 -982 507 N ATOM 1772 CA HIS B 69 -42.299 -10.718 67.288 1.00 20.98 C ANISOU 1772 CA HIS B 69 2888 2528 2555 265 -1052 538 C ATOM 1773 C HIS B 69 -41.505 -12.040 67.315 1.00 19.82 C ANISOU 1773 C HIS B 69 2762 2480 2289 175 -910 460 C ATOM 1774 O HIS B 69 -40.607 -12.202 68.115 1.00 18.52 O ANISOU 1774 O HIS B 69 2592 2302 2140 152 -768 419 O ATOM 1775 CB HIS B 69 -41.843 -9.894 66.079 1.00 22.68 C ANISOU 1775 CB HIS B 69 3268 2709 2638 229 -1144 690 C ATOM 1776 CG HIS B 69 -42.615 -10.173 64.818 1.00 24.55 C ANISOU 1776 CG HIS B 69 3554 3011 2761 217 -1315 744 C ATOM 1777 ND1 HIS B 69 -42.688 -11.427 64.234 1.00 24.59 N ANISOU 1777 ND1 HIS B 69 3568 3144 2630 147 -1301 674 N ATOM 1778 CD2 HIS B 69 -43.330 -9.345 64.018 1.00 26.69 C ANISOU 1778 CD2 HIS B 69 3875 3234 3031 264 -1518 864 C ATOM 1779 CE1 HIS B 69 -43.418 -11.355 63.134 1.00 26.46 C ANISOU 1779 CE1 HIS B 69 3859 3419 2775 145 -1487 739 C ATOM 1780 NE2 HIS B 69 -43.816 -10.102 62.978 1.00 27.79 N ANISOU 1780 NE2 HIS B 69 4054 3484 3019 218 -1629 864 N ATOM 1781 N CYS B 70 -41.841 -12.974 66.429 1.00 20.54 N ANISOU 1781 N CYS B 70 2874 2661 2266 128 -959 436 N ATOM 1782 CA CYS B 70 -41.127 -14.248 66.319 1.00 19.89 C ANISOU 1782 CA CYS B 70 2818 2658 2082 49 -835 355 C ATOM 1783 C CYS B 70 -39.862 -14.110 65.467 1.00 19.57 C ANISOU 1783 C CYS B 70 2925 2639 1869 -30 -764 412 C ATOM 1784 O CYS B 70 -39.796 -14.610 64.346 1.00 20.27 O ANISOU 1784 O CYS B 70 3101 2801 1798 -94 -792 413 O ATOM 1785 CB CYS B 70 -42.043 -15.344 65.739 1.00 21.21 C ANISOU 1785 CB CYS B 70 2942 2904 2210 23 -910 281 C ATOM 1786 SG CYS B 70 -41.465 -17.082 66.084 1.00 21.41 S ANISOU 1786 SG CYS B 70 2943 2983 2207 -44 -749 143 S ATOM 1787 N ASN B 71 -38.859 -13.435 66.027 1.00 18.23 N ANISOU 1787 N ASN B 71 2780 2412 1735 -33 -664 449 N ATOM 1788 CA ASN B 71 -37.557 -13.261 65.385 1.00 18.15 C ANISOU 1788 CA ASN B 71 2882 2419 1593 -116 -564 492 C ATOM 1789 C ASN B 71 -36.585 -12.694 66.412 1.00 16.96 C ANISOU 1789 C ASN B 71 2696 2200 1546 -107 -453 493 C ATOM 1790 O ASN B 71 -36.943 -12.557 67.568 1.00 16.01 O ANISOU 1790 O ASN B 71 2479 2030 1571 -42 -455 452 O ATOM 1791 CB ASN B 71 -37.665 -12.358 64.155 1.00 19.79 C ANISOU 1791 CB ASN B 71 3230 2621 1665 -155 -665 625 C ATOM 1792 CG ASN B 71 -38.169 -10.951 64.481 1.00 20.29 C ANISOU 1792 CG ASN B 71 3297 2567 1843 -86 -778 736 C ATOM 1793 OD1 ASN B 71 -37.901 -10.393 65.536 1.00 19.23 O ANISOU 1793 OD1 ASN B 71 3096 2351 1858 -42 -725 721 O ATOM 1794 ND2 ASN B 71 -38.875 -10.373 63.545 1.00 21.92 N ANISOU 1794 ND2 ASN B 71 3588 2762 1978 -79 -940 844 N ATOM 1795 N GLY B 72 -35.364 -12.359 66.014 1.00 17.07 N ANISOU 1795 N GLY B 72 2784 2216 1485 -181 -354 531 N ATOM 1796 CA GLY B 72 -34.372 -11.903 66.995 1.00 16.17 C ANISOU 1796 CA GLY B 72 2621 2045 1475 -183 -254 516 C ATOM 1797 C GLY B 72 -34.223 -10.414 67.191 1.00 16.71 C ANISOU 1797 C GLY B 72 2733 2008 1608 -180 -292 614 C ATOM 1798 O GLY B 72 -33.199 -9.973 67.709 1.00 16.66 O ANISOU 1798 O GLY B 72 2711 1964 1655 -216 -204 609 O ATOM 1799 N THR B 73 -35.211 -9.630 66.757 1.00 17.53 N ANISOU 1799 N THR B 73 2888 2056 1716 -140 -431 703 N ATOM 1800 CA THR B 73 -35.164 -8.189 66.866 1.00 18.26 C ANISOU 1800 CA THR B 73 3032 2020 1883 -130 -482 804 C ATOM 1801 C THR B 73 -36.395 -7.714 67.611 1.00 18.04 C ANISOU 1801 C THR B 73 2926 1913 2014 -10 -601 785 C ATOM 1802 O THR B 73 -37.470 -7.619 67.052 1.00 18.75 O ANISOU 1802 O THR B 73 3028 1998 2098 42 -738 831 O ATOM 1803 CB THR B 73 -35.118 -7.572 65.470 1.00 20.20 C ANISOU 1803 CB THR B 73 3438 2254 1982 -198 -544 952 C ATOM 1804 OG1 THR B 73 -33.927 -8.031 64.814 1.00 20.53 O ANISOU 1804 OG1 THR B 73 3542 2380 1876 -321 -400 949 O ATOM 1805 CG2 THR B 73 -35.150 -6.034 65.532 1.00 21.35 C ANISOU 1805 CG2 THR B 73 3652 2237 2220 -186 -616 1076 C ATOM 1806 N GLY B 74 -36.246 -7.465 68.896 1.00 17.10 N ANISOU 1806 N GLY B 74 2717 1740 2038 32 -548 704 N ATOM 1807 CA GLY B 74 -37.352 -6.954 69.675 1.00 17.21 C ANISOU 1807 CA GLY B 74 2649 1678 2210 141 -631 665 C ATOM 1808 C GLY B 74 -37.312 -7.402 71.110 1.00 15.90 C ANISOU 1808 C GLY B 74 2369 1533 2136 173 -542 527 C ATOM 1809 O GLY B 74 -36.467 -8.209 71.516 1.00 14.74 O ANISOU 1809 O GLY B 74 2203 1462 1933 119 -437 469 O ATOM 1810 N GLY B 75 -38.250 -6.862 71.876 1.00 16.28 N ANISOU 1810 N GLY B 75 2342 1513 2329 264 -589 474 N ATOM 1811 CA GLY B 75 -38.382 -7.169 73.296 1.00 15.35 C ANISOU 1811 CA GLY B 75 2127 1415 2288 293 -507 343 C ATOM 1812 C GLY B 75 -37.713 -6.072 74.085 1.00 15.54 C ANISOU 1812 C GLY B 75 2176 1332 2396 287 -468 319 C ATOM 1813 O GLY B 75 -36.984 -5.282 73.531 1.00 16.33 O ANISOU 1813 O GLY B 75 2362 1356 2486 243 -484 404 O ATOM 1814 N LYS B 76 -38.003 -6.010 75.371 1.00 15.17 N ANISOU 1814 N LYS B 76 2056 1279 2428 323 -414 200 N ATOM 1815 CA LYS B 76 -37.377 -5.059 76.264 1.00 15.42 C ANISOU 1815 CA LYS B 76 2107 1220 2530 311 -373 146 C ATOM 1816 C LYS B 76 -37.385 -5.683 77.624 1.00 14.49 C ANISOU 1816 C LYS B 76 1927 1180 2396 306 -286 15 C ATOM 1817 O LYS B 76 -38.188 -6.590 77.875 1.00 13.91 O ANISOU 1817 O LYS B 76 1788 1195 2299 333 -265 -29 O ATOM 1818 CB LYS B 76 -38.164 -3.773 76.319 1.00 16.97 C ANISOU 1818 CB LYS B 76 2295 1266 2887 394 -439 136 C ATOM 1819 CG LYS B 76 -39.593 -3.937 76.748 1.00 17.50 C ANISOU 1819 CG LYS B 76 2252 1346 3050 495 -456 48 C ATOM 1820 CD LYS B 76 -40.244 -2.555 76.794 1.00 19.32 C ANISOU 1820 CD LYS B 76 2469 1401 3469 588 -524 32 C ATOM 1821 CE LYS B 76 -41.492 -2.532 77.622 1.00 20.09 C ANISOU 1821 CE LYS B 76 2433 1500 3697 685 -495 -111 C ATOM 1822 NZ LYS B 76 -42.658 -2.986 76.865 1.00 20.65 N ANISOU 1822 NZ LYS B 76 2419 1613 3813 756 -585 -70 N ATOM 1823 N SER B 77 -36.504 -5.192 78.492 1.00 14.37 N ANISOU 1823 N SER B 77 1938 1133 2387 262 -239 -42 N ATOM 1824 CA SER B 77 -36.469 -5.618 79.886 1.00 13.89 C ANISOU 1824 CA SER B 77 1841 1140 2295 251 -168 -164 C ATOM 1825 C SER B 77 -37.451 -4.787 80.714 1.00 15.01 C ANISOU 1825 C SER B 77 1941 1209 2550 320 -150 -281 C ATOM 1826 O SER B 77 -38.072 -3.838 80.211 1.00 15.89 O ANISOU 1826 O SER B 77 2044 1201 2789 385 -203 -266 O ATOM 1827 CB SER B 77 -35.057 -5.452 80.448 1.00 13.61 C ANISOU 1827 CB SER B 77 1850 1109 2211 169 -144 -182 C ATOM 1828 OG SER B 77 -34.792 -4.102 80.746 1.00 14.66 O ANISOU 1828 OG SER B 77 2013 1114 2442 165 -159 -225 O ATOM 1829 N ILE B 78 -37.573 -5.148 81.990 1.00 15.01 N ANISOU 1829 N ILE B 78 1919 1280 2504 304 -74 -399 N ATOM 1830 CA ILE B 78 -38.348 -4.368 82.955 1.00 16.41 C ANISOU 1830 CA ILE B 78 2061 1402 2772 353 -25 -544 C ATOM 1831 C ILE B 78 -37.627 -3.084 83.380 1.00 17.58 C ANISOU 1831 C ILE B 78 2265 1426 2988 334 -37 -605 C ATOM 1832 O ILE B 78 -38.182 -2.274 84.103 1.00 18.96 O ANISOU 1832 O ILE B 78 2420 1530 3255 377 0 -737 O ATOM 1833 CB ILE B 78 -38.677 -5.198 84.214 1.00 16.23 C ANISOU 1833 CB ILE B 78 2016 1507 2642 321 73 -651 C ATOM 1834 CG1 ILE B 78 -37.389 -5.599 84.984 1.00 15.58 C ANISOU 1834 CG1 ILE B 78 2011 1495 2412 226 83 -654 C ATOM 1835 CG2 ILE B 78 -39.507 -6.437 83.810 1.00 15.53 C ANISOU 1835 CG2 ILE B 78 1865 1522 2511 334 92 -600 C ATOM 1836 CD1 ILE B 78 -37.640 -6.218 86.379 1.00 15.85 C ANISOU 1836 CD1 ILE B 78 2058 1641 2321 183 172 -758 C ATOM 1837 N TYR B 79 -36.387 -2.904 82.933 1.00 17.34 N ANISOU 1837 N TYR B 79 2299 1368 2920 265 -83 -519 N ATOM 1838 CA TYR B 79 -35.607 -1.736 83.300 1.00 18.44 C ANISOU 1838 CA TYR B 79 2490 1388 3126 225 -97 -573 C ATOM 1839 C TYR B 79 -35.604 -0.670 82.196 1.00 19.54 C ANISOU 1839 C TYR B 79 2662 1354 3407 253 -167 -476 C ATOM 1840 O TYR B 79 -35.181 0.455 82.431 1.00 20.76 O ANISOU 1840 O TYR B 79 2857 1369 3659 231 -180 -523 O ATOM 1841 CB TYR B 79 -34.180 -2.163 83.590 1.00 17.56 C ANISOU 1841 CB TYR B 79 2416 1353 2900 117 -102 -549 C ATOM 1842 CG TYR B 79 -34.089 -3.276 84.584 1.00 16.79 C ANISOU 1842 CG TYR B 79 2306 1418 2654 88 -60 -607 C ATOM 1843 CD1 TYR B 79 -34.656 -3.148 85.864 1.00 17.59 C ANISOU 1843 CD1 TYR B 79 2409 1552 2722 98 -3 -759 C ATOM 1844 CD2 TYR B 79 -33.440 -4.462 84.263 1.00 15.56 C ANISOU 1844 CD2 TYR B 79 2144 1378 2388 48 -73 -512 C ATOM 1845 CE1 TYR B 79 -34.565 -4.185 86.796 1.00 17.15 C ANISOU 1845 CE1 TYR B 79 2363 1645 2507 59 31 -793 C ATOM 1846 CE2 TYR B 79 -33.359 -5.481 85.158 1.00 15.14 C ANISOU 1846 CE2 TYR B 79 2092 1454 2207 24 -49 -546 C ATOM 1847 CZ TYR B 79 -33.913 -5.337 86.418 1.00 15.98 C ANISOU 1847 CZ TYR B 79 2213 1592 2263 25 0 -675 C ATOM 1848 OH TYR B 79 -33.806 -6.377 87.292 1.00 16.02 O ANISOU 1848 OH TYR B 79 2240 1724 2122 -10 17 -686 O ATOM 1849 N GLY B 80 -36.088 -1.031 81.012 1.00 19.40 N ANISOU 1849 N GLY B 80 2634 1342 3394 294 -216 -341 N ATOM 1850 CA GLY B 80 -35.859 -0.244 79.811 1.00 20.35 C ANISOU 1850 CA GLY B 80 2814 1327 3589 291 -291 -201 C ATOM 1851 C GLY B 80 -35.538 -1.141 78.637 1.00 19.59 C ANISOU 1851 C GLY B 80 2738 1330 3371 251 -317 -46 C ATOM 1852 O GLY B 80 -35.427 -2.349 78.794 1.00 18.11 O ANISOU 1852 O GLY B 80 2515 1302 3063 229 -277 -57 O ATOM 1853 N GLU B 81 -35.368 -0.548 77.457 1.00 20.85 N ANISOU 1853 N GLU B 81 2968 1391 3560 236 -381 97 N ATOM 1854 CA GLU B 81 -35.162 -1.336 76.228 1.00 20.65 C ANISOU 1854 CA GLU B 81 2977 1460 3408 197 -402 239 C ATOM 1855 C GLU B 81 -33.894 -2.186 76.321 1.00 19.32 C ANISOU 1855 C GLU B 81 2808 1421 3109 88 -323 235 C ATOM 1856 O GLU B 81 -33.838 -3.276 75.786 1.00 18.38 O ANISOU 1856 O GLU B 81 2676 1431 2875 72 -307 275 O ATOM 1857 CB GLU B 81 -35.068 -0.451 74.971 1.00 22.46 C ANISOU 1857 CB GLU B 81 3309 1558 3665 176 -478 403 C ATOM 1858 CG GLU B 81 -36.209 0.558 74.748 1.00 24.48 C ANISOU 1858 CG GLU B 81 3575 1646 4079 289 -586 435 C ATOM 1859 CD GLU B 81 -37.611 -0.056 74.671 1.00 24.69 C ANISOU 1859 CD GLU B 81 3512 1742 4128 411 -647 403 C ATOM 1860 OE1 GLU B 81 -38.069 -0.344 73.540 1.00 25.42 O ANISOU 1860 OE1 GLU B 81 3637 1863 4157 428 -736 529 O ATOM 1861 OE2 GLU B 81 -38.276 -0.174 75.737 1.00 24.92 O ANISOU 1861 OE2 GLU B 81 3437 1789 4242 484 -607 248 O ATOM 1862 N LYS B 82 -32.874 -1.670 76.995 1.00 19.57 N ANISOU 1862 N LYS B 82 2849 1412 3173 15 -280 180 N ATOM 1863 CA LYS B 82 -31.633 -2.419 77.205 1.00 18.63 C ANISOU 1863 CA LYS B 82 2705 1409 2963 -76 -218 161 C ATOM 1864 C LYS B 82 -31.078 -2.152 78.590 1.00 18.15 C ANISOU 1864 C LYS B 82 2607 1344 2943 -103 -194 25 C ATOM 1865 O LYS B 82 -31.330 -1.107 79.159 1.00 19.26 O ANISOU 1865 O LYS B 82 2767 1361 3187 -86 -213 -38 O ATOM 1866 CB LYS B 82 -30.602 -2.095 76.121 1.00 19.58 C ANISOU 1866 CB LYS B 82 2880 1499 3056 -181 -195 278 C ATOM 1867 CG LYS B 82 -30.424 -0.628 75.885 1.00 21.58 C ANISOU 1867 CG LYS B 82 3207 1569 3423 -221 -222 328 C ATOM 1868 CD LYS B 82 -29.331 -0.322 74.852 1.00 22.71 C ANISOU 1868 CD LYS B 82 3408 1690 3529 -352 -176 445 C ATOM 1869 CE LYS B 82 -29.682 -0.929 73.497 1.00 22.91 C ANISOU 1869 CE LYS B 82 3488 1787 3427 -350 -180 578 C ATOM 1870 NZ LYS B 82 -29.075 -0.108 72.402 1.00 24.71 N ANISOU 1870 NZ LYS B 82 3824 1923 3640 -463 -158 722 N ATOM 1871 N PHE B 83 -30.382 -3.127 79.163 1.00 16.74 N ANISOU 1871 N PHE B 83 2378 1299 2683 -138 -163 -23 N ATOM 1872 CA PHE B 83 -29.669 -2.902 80.416 1.00 16.67 C ANISOU 1872 CA PHE B 83 2342 1300 2689 -181 -160 -139 C ATOM 1873 C PHE B 83 -28.287 -3.523 80.378 1.00 16.16 C ANISOU 1873 C PHE B 83 2232 1325 2580 -265 -145 -125 C ATOM 1874 O PHE B 83 -28.007 -4.408 79.554 1.00 15.33 O ANISOU 1874 O PHE B 83 2106 1301 2417 -271 -120 -48 O ATOM 1875 CB PHE B 83 -30.484 -3.361 81.648 1.00 16.20 C ANISOU 1875 CB PHE B 83 2263 1305 2586 -116 -158 -253 C ATOM 1876 CG PHE B 83 -30.657 -4.862 81.780 1.00 15.01 C ANISOU 1876 CG PHE B 83 2076 1305 2320 -89 -143 -235 C ATOM 1877 CD1 PHE B 83 -31.568 -5.547 81.000 1.00 14.32 C ANISOU 1877 CD1 PHE B 83 1981 1253 2204 -31 -133 -168 C ATOM 1878 CD2 PHE B 83 -29.948 -5.574 82.745 1.00 14.72 C ANISOU 1878 CD2 PHE B 83 2016 1365 2208 -123 -150 -288 C ATOM 1879 CE1 PHE B 83 -31.749 -6.925 81.165 1.00 13.43 C ANISOU 1879 CE1 PHE B 83 1841 1261 2001 -14 -117 -159 C ATOM 1880 CE2 PHE B 83 -30.112 -6.945 82.903 1.00 13.75 C ANISOU 1880 CE2 PHE B 83 1872 1357 1993 -99 -142 -263 C ATOM 1881 CZ PHE B 83 -31.009 -7.615 82.117 1.00 13.14 C ANISOU 1881 CZ PHE B 83 1789 1304 1898 -47 -118 -201 C ATOM 1882 N GLU B 84 -27.434 -3.033 81.276 1.00 16.60 N ANISOU 1882 N GLU B 84 2268 1365 2673 -327 -164 -211 N ATOM 1883 CA GLU B 84 -26.027 -3.376 81.275 1.00 16.69 C ANISOU 1883 CA GLU B 84 2214 1439 2685 -412 -163 -210 C ATOM 1884 C GLU B 84 -25.801 -4.841 81.582 1.00 15.20 C ANISOU 1884 C GLU B 84 1969 1401 2405 -375 -172 -211 C ATOM 1885 O GLU B 84 -26.657 -5.479 82.140 1.00 14.16 O ANISOU 1885 O GLU B 84 1857 1321 2202 -303 -183 -235 O ATOM 1886 CB GLU B 84 -25.264 -2.479 82.261 1.00 18.20 C ANISOU 1886 CB GLU B 84 2393 1578 2944 -486 -204 -317 C ATOM 1887 CG GLU B 84 -25.214 -1.019 81.746 1.00 19.87 C ANISOU 1887 CG GLU B 84 2657 1615 3275 -546 -188 -299 C ATOM 1888 CD GLU B 84 -24.341 -0.099 82.578 1.00 21.58 C ANISOU 1888 CD GLU B 84 2856 1767 3577 -642 -225 -409 C ATOM 1889 OE1 GLU B 84 -23.930 -0.483 83.702 1.00 22.31 O ANISOU 1889 OE1 GLU B 84 2905 1948 3620 -651 -277 -514 O ATOM 1890 OE2 GLU B 84 -24.045 1.016 82.101 1.00 23.11 O ANISOU 1890 OE2 GLU B 84 3082 1814 3881 -717 -208 -385 O ATOM 1891 N ASP B 85 -24.642 -5.358 81.178 1.00 15.04 N ANISOU 1891 N ASP B 85 1874 1440 2401 -427 -159 -184 N ATOM 1892 CA ASP B 85 -24.226 -6.709 81.527 1.00 14.31 C ANISOU 1892 CA ASP B 85 1715 1466 2253 -392 -182 -189 C ATOM 1893 C ASP B 85 -23.858 -6.660 83.006 1.00 14.70 C ANISOU 1893 C ASP B 85 1749 1548 2286 -401 -269 -282 C ATOM 1894 O ASP B 85 -22.982 -5.925 83.392 1.00 15.59 O ANISOU 1894 O ASP B 85 1824 1633 2465 -475 -305 -336 O ATOM 1895 CB ASP B 85 -23.031 -7.135 80.693 1.00 14.63 C ANISOU 1895 CB ASP B 85 1664 1548 2347 -443 -141 -155 C ATOM 1896 CG ASP B 85 -23.356 -7.271 79.199 1.00 14.35 C ANISOU 1896 CG ASP B 85 1660 1500 2292 -446 -48 -67 C ATOM 1897 OD1 ASP B 85 -24.336 -7.959 78.848 1.00 13.42 O ANISOU 1897 OD1 ASP B 85 1592 1408 2099 -374 -36 -30 O ATOM 1898 OD2 ASP B 85 -22.606 -6.692 78.376 1.00 15.21 O ANISOU 1898 OD2 ASP B 85 1745 1578 2455 -532 14 -38 O ATOM 1899 N GLU B 86 -24.573 -7.397 83.838 1.00 14.12 N ANISOU 1899 N GLU B 86 1714 1532 2116 -337 -303 -301 N ATOM 1900 CA GLU B 86 -24.445 -7.239 85.289 1.00 14.78 C ANISOU 1900 CA GLU B 86 1822 1647 2145 -352 -383 -388 C ATOM 1901 C GLU B 86 -23.080 -7.721 85.807 1.00 15.41 C ANISOU 1901 C GLU B 86 1815 1794 2244 -389 -476 -404 C ATOM 1902 O GLU B 86 -22.352 -6.994 86.517 1.00 16.52 O ANISOU 1902 O GLU B 86 1936 1925 2415 -455 -546 -482 O ATOM 1903 CB GLU B 86 -25.588 -7.992 85.968 1.00 14.27 C ANISOU 1903 CB GLU B 86 1828 1634 1957 -286 -376 -388 C ATOM 1904 CG GLU B 86 -25.741 -7.689 87.448 1.00 15.20 C ANISOU 1904 CG GLU B 86 2008 1784 1982 -309 -431 -485 C ATOM 1905 CD GLU B 86 -26.951 -8.378 88.046 1.00 14.83 C ANISOU 1905 CD GLU B 86 2034 1788 1812 -261 -392 -483 C ATOM 1906 OE1 GLU B 86 -27.616 -9.194 87.338 1.00 13.90 O ANISOU 1906 OE1 GLU B 86 1908 1680 1690 -208 -337 -405 O ATOM 1907 OE2 GLU B 86 -27.243 -8.103 89.222 1.00 15.67 O ANISOU 1907 OE2 GLU B 86 2206 1925 1820 -285 -410 -568 O ATOM 1908 N ASN B 87 -22.732 -8.936 85.417 1.00 14.73 N ANISOU 1908 N ASN B 87 1672 1767 2155 -344 -482 -337 N ATOM 1909 CA ASN B 87 -21.409 -9.489 85.669 1.00 15.45 C ANISOU 1909 CA ASN B 87 1652 1912 2305 -359 -568 -341 C ATOM 1910 C ASN B 87 -21.246 -10.737 84.820 1.00 14.72 C ANISOU 1910 C ASN B 87 1498 1850 2244 -296 -527 -267 C ATOM 1911 O ASN B 87 -22.216 -11.242 84.250 1.00 13.77 O ANISOU 1911 O ASN B 87 1440 1720 2070 -247 -450 -217 O ATOM 1912 CB ASN B 87 -21.192 -9.797 87.166 1.00 16.31 C ANISOU 1912 CB ASN B 87 1791 2080 2322 -356 -709 -381 C ATOM 1913 CG ASN B 87 -22.140 -10.869 87.707 1.00 15.73 C ANISOU 1913 CG ASN B 87 1815 2050 2110 -286 -718 -327 C ATOM 1914 OD1 ASN B 87 -22.215 -11.987 87.185 1.00 15.17 O ANISOU 1914 OD1 ASN B 87 1718 1992 2051 -225 -696 -252 O ATOM 1915 ND2 ASN B 87 -22.858 -10.536 88.766 1.00 16.00 N ANISOU 1915 ND2 ASN B 87 1962 2102 2013 -302 -742 -373 N ATOM 1916 N PHE B 88 -20.036 -11.252 84.736 1.00 15.42 N ANISOU 1916 N PHE B 88 1458 1972 2428 -296 -579 -271 N ATOM 1917 CA PHE B 88 -19.808 -12.518 84.050 1.00 15.04 C ANISOU 1917 CA PHE B 88 1345 1946 2423 -227 -546 -222 C ATOM 1918 C PHE B 88 -19.216 -13.569 85.002 1.00 15.75 C ANISOU 1918 C PHE B 88 1388 2078 2519 -167 -693 -209 C ATOM 1919 O PHE B 88 -18.356 -14.370 84.622 1.00 16.15 O ANISOU 1919 O PHE B 88 1312 2138 2683 -124 -711 -203 O ATOM 1920 CB PHE B 88 -18.899 -12.298 82.830 1.00 15.53 C ANISOU 1920 CB PHE B 88 1278 1999 2621 -269 -447 -238 C ATOM 1921 CG PHE B 88 -19.407 -11.263 81.862 1.00 15.04 C ANISOU 1921 CG PHE B 88 1278 1890 2545 -336 -317 -228 C ATOM 1922 CD1 PHE B 88 -20.509 -11.516 81.073 1.00 13.96 C ANISOU 1922 CD1 PHE B 88 1243 1735 2326 -302 -227 -176 C ATOM 1923 CD2 PHE B 88 -18.766 -10.042 81.722 1.00 15.98 C ANISOU 1923 CD2 PHE B 88 1355 1976 2739 -438 -295 -265 C ATOM 1924 CE1 PHE B 88 -20.963 -10.566 80.134 1.00 13.79 C ANISOU 1924 CE1 PHE B 88 1284 1663 2289 -360 -128 -150 C ATOM 1925 CE2 PHE B 88 -19.229 -9.081 80.796 1.00 15.78 C ANISOU 1925 CE2 PHE B 88 1403 1889 2703 -502 -183 -235 C ATOM 1926 CZ PHE B 88 -20.320 -9.348 80.013 1.00 14.69 C ANISOU 1926 CZ PHE B 88 1371 1735 2476 -457 -108 -172 C ATOM 1927 N ILE B 89 -19.686 -13.583 86.244 1.00 15.96 N ANISOU 1927 N ILE B 89 1517 2124 2421 -162 -798 -203 N ATOM 1928 CA ILE B 89 -19.186 -14.563 87.228 1.00 17.03 C ANISOU 1928 CA ILE B 89 1639 2294 2536 -110 -960 -167 C ATOM 1929 C ILE B 89 -19.515 -16.011 86.830 1.00 16.50 C ANISOU 1929 C ILE B 89 1583 2208 2478 -18 -937 -89 C ATOM 1930 O ILE B 89 -18.677 -16.891 86.973 1.00 17.38 O ANISOU 1930 O ILE B 89 1602 2318 2682 41 -1035 -63 O ATOM 1931 CB ILE B 89 -19.753 -14.308 88.665 1.00 17.58 C ANISOU 1931 CB ILE B 89 1856 2399 2425 -138 -1063 -170 C ATOM 1932 CG1 ILE B 89 -19.339 -12.932 89.198 1.00 18.38 C ANISOU 1932 CG1 ILE B 89 1949 2514 2521 -230 -1109 -267 C ATOM 1933 CG2 ILE B 89 -19.296 -15.415 89.642 1.00 18.73 C ANISOU 1933 CG2 ILE B 89 2014 2575 2524 -85 -1240 -102 C ATOM 1934 CD1 ILE B 89 -20.218 -12.477 90.387 1.00 18.73 C ANISOU 1934 CD1 ILE B 89 2163 2586 2365 -270 -1140 -299 C ATOM 1935 N LEU B 90 -20.732 -16.254 86.334 1.00 15.27 N ANISOU 1935 N LEU B 90 1531 2028 2241 -5 -814 -56 N ATOM 1936 CA LEU B 90 -21.162 -17.618 85.962 1.00 14.91 C ANISOU 1936 CA LEU B 90 1510 1953 2201 68 -786 8 C ATOM 1937 C LEU B 90 -20.776 -17.996 84.510 1.00 14.68 C ANISOU 1937 C LEU B 90 1370 1895 2310 98 -671 -13 C ATOM 1938 O LEU B 90 -20.807 -17.150 83.592 1.00 14.29 O ANISOU 1938 O LEU B 90 1290 1849 2288 49 -557 -57 O ATOM 1939 CB LEU B 90 -22.665 -17.785 86.217 1.00 13.94 C ANISOU 1939 CB LEU B 90 1544 1824 1926 59 -720 45 C ATOM 1940 CG LEU B 90 -23.117 -17.716 87.699 1.00 14.53 C ANISOU 1940 CG LEU B 90 1743 1933 1841 31 -813 71 C ATOM 1941 CD1 LEU B 90 -24.624 -17.765 87.810 1.00 13.64 C ANISOU 1941 CD1 LEU B 90 1756 1821 1603 10 -709 86 C ATOM 1942 CD2 LEU B 90 -22.470 -18.839 88.553 1.00 15.84 C ANISOU 1942 CD2 LEU B 90 1920 2097 2001 77 -970 148 C ATOM 1943 N LYS B 91 -20.377 -19.251 84.320 1.00 15.17 N ANISOU 1943 N LYS B 91 1378 1926 2457 174 -703 14 N ATOM 1944 CA LYS B 91 -19.868 -19.725 83.030 1.00 15.29 C ANISOU 1944 CA LYS B 91 1280 1919 2609 206 -597 -27 C ATOM 1945 C LYS B 91 -20.875 -20.605 82.294 1.00 14.12 C ANISOU 1945 C LYS B 91 1214 1731 2417 237 -496 -4 C ATOM 1946 O LYS B 91 -21.764 -21.207 82.898 1.00 13.71 O ANISOU 1946 O LYS B 91 1280 1654 2273 255 -536 56 O ATOM 1947 CB LYS B 91 -18.583 -20.551 83.201 1.00 17.06 C ANISOU 1947 CB LYS B 91 1352 2122 3006 282 -694 -41 C ATOM 1948 CG LYS B 91 -17.428 -19.885 83.922 1.00 18.66 C ANISOU 1948 CG LYS B 91 1436 2363 3287 262 -822 -71 C ATOM 1949 CD LYS B 91 -17.178 -18.430 83.500 1.00 18.65 C ANISOU 1949 CD LYS B 91 1392 2410 3283 155 -735 -137 C ATOM 1950 CE LYS B 91 -15.786 -17.917 84.028 1.00 20.55 C ANISOU 1950 CE LYS B 91 1461 2685 3660 133 -855 -190 C ATOM 1951 NZ LYS B 91 -15.519 -16.437 83.716 1.00 20.71 N ANISOU 1951 NZ LYS B 91 1446 2735 3684 11 -777 -252 N ATOM 1952 N HIS B 92 -20.682 -20.717 80.984 1.00 13.71 N ANISOU 1952 N HIS B 92 1098 1677 2433 235 -364 -60 N ATOM 1953 CA HIS B 92 -21.480 -21.608 80.142 1.00 13.01 C ANISOU 1953 CA HIS B 92 1068 1552 2320 261 -271 -62 C ATOM 1954 C HIS B 92 -20.879 -23.009 80.209 1.00 14.06 C ANISOU 1954 C HIS B 92 1133 1620 2586 354 -320 -68 C ATOM 1955 O HIS B 92 -20.116 -23.428 79.324 1.00 14.80 O ANISOU 1955 O HIS B 92 1113 1702 2806 385 -245 -144 O ATOM 1956 CB HIS B 92 -21.478 -21.114 78.695 1.00 12.61 C ANISOU 1956 CB HIS B 92 989 1534 2265 211 -114 -124 C ATOM 1957 CG HIS B 92 -22.105 -19.764 78.514 1.00 11.69 C ANISOU 1957 CG HIS B 92 947 1457 2035 128 -72 -106 C ATOM 1958 ND1 HIS B 92 -21.419 -18.592 78.741 1.00 11.96 N ANISOU 1958 ND1 HIS B 92 929 1520 2093 72 -85 -118 N ATOM 1959 CD2 HIS B 92 -23.346 -19.403 78.113 1.00 10.69 C ANISOU 1959 CD2 HIS B 92 935 1335 1788 94 -26 -79 C ATOM 1960 CE1 HIS B 92 -22.214 -17.566 78.492 1.00 11.29 C ANISOU 1960 CE1 HIS B 92 934 1444 1909 12 -45 -95 C ATOM 1961 NE2 HIS B 92 -23.391 -18.030 78.109 1.00 10.47 N ANISOU 1961 NE2 HIS B 92 929 1330 1720 30 -14 -70 N ATOM 1962 N THR B 93 -21.239 -23.734 81.257 1.00 14.28 N ANISOU 1962 N THR B 93 1237 1600 2587 396 -440 9 N ATOM 1963 CA THR B 93 -20.597 -24.993 81.565 1.00 15.63 C ANISOU 1963 CA THR B 93 1352 1687 2897 492 -529 27 C ATOM 1964 C THR B 93 -21.181 -26.186 80.837 1.00 15.61 C ANISOU 1964 C THR B 93 1394 1603 2934 531 -451 10 C ATOM 1965 O THR B 93 -20.534 -27.220 80.744 1.00 16.92 O ANISOU 1965 O THR B 93 1487 1683 3257 618 -489 -7 O ATOM 1966 CB THR B 93 -20.648 -25.268 83.069 1.00 16.25 C ANISOU 1966 CB THR B 93 1510 1742 2921 513 -710 138 C ATOM 1967 OG1 THR B 93 -22.004 -25.284 83.493 1.00 15.21 O ANISOU 1967 OG1 THR B 93 1551 1612 2614 457 -685 204 O ATOM 1968 CG2 THR B 93 -19.894 -24.172 83.831 1.00 16.71 C ANISOU 1968 CG2 THR B 93 1511 1878 2959 479 -809 135 C ATOM 1969 N GLY B 94 -22.389 -26.081 80.312 1.00 14.48 N ANISOU 1969 N GLY B 94 1361 1476 2664 470 -350 8 N ATOM 1970 CA GLY B 94 -22.959 -27.231 79.607 1.00 14.68 C ANISOU 1970 CA GLY B 94 1428 1421 2728 495 -283 -20 C ATOM 1971 C GLY B 94 -24.437 -27.130 79.352 1.00 13.53 C ANISOU 1971 C GLY B 94 1412 1296 2434 422 -216 0 C ATOM 1972 O GLY B 94 -25.028 -26.102 79.624 1.00 12.70 O ANISOU 1972 O GLY B 94 1356 1267 2200 359 -209 29 O ATOM 1973 N PRO B 95 -25.049 -28.215 78.867 1.00 13.76 N ANISOU 1973 N PRO B 95 1489 1246 2493 432 -175 -20 N ATOM 1974 CA PRO B 95 -26.472 -28.238 78.561 1.00 12.97 C ANISOU 1974 CA PRO B 95 1490 1161 2274 362 -117 -13 C ATOM 1975 C PRO B 95 -27.327 -27.699 79.710 1.00 12.39 C ANISOU 1975 C PRO B 95 1506 1125 2076 311 -173 86 C ATOM 1976 O PRO B 95 -27.018 -27.965 80.851 1.00 13.11 O ANISOU 1976 O PRO B 95 1626 1180 2174 334 -268 169 O ATOM 1977 CB PRO B 95 -26.772 -29.729 78.351 1.00 13.85 C ANISOU 1977 CB PRO B 95 1638 1146 2477 391 -113 -27 C ATOM 1978 CG PRO B 95 -25.440 -30.395 78.101 1.00 15.14 C ANISOU 1978 CG PRO B 95 1699 1235 2819 486 -131 -83 C ATOM 1979 CD PRO B 95 -24.403 -29.534 78.737 1.00 15.21 C ANISOU 1979 CD PRO B 95 1626 1305 2845 517 -200 -49 C ATOM 1980 N GLY B 96 -28.374 -26.936 79.408 1.00 11.41 N ANISOU 1980 N GLY B 96 1423 1074 1838 244 -115 75 N ATOM 1981 CA GLY B 96 -29.277 -26.389 80.427 1.00 10.98 C ANISOU 1981 CA GLY B 96 1440 1059 1670 194 -140 143 C ATOM 1982 C GLY B 96 -28.947 -25.018 81.007 1.00 10.56 C ANISOU 1982 C GLY B 96 1372 1088 1551 180 -168 155 C ATOM 1983 O GLY B 96 -29.767 -24.440 81.693 1.00 10.21 O ANISOU 1983 O GLY B 96 1380 1084 1412 137 -165 181 O ATOM 1984 N ILE B 97 -27.750 -24.495 80.767 1.00 10.82 N ANISOU 1984 N ILE B 97 1328 1142 1640 212 -190 125 N ATOM 1985 CA ILE B 97 -27.404 -23.140 81.218 1.00 10.55 C ANISOU 1985 CA ILE B 97 1276 1175 1557 188 -214 123 C ATOM 1986 C ILE B 97 -28.341 -22.146 80.549 1.00 9.83 C ANISOU 1986 C ILE B 97 1206 1132 1395 142 -139 90 C ATOM 1987 O ILE B 97 -28.667 -22.297 79.342 1.00 9.59 O ANISOU 1987 O ILE B 97 1162 1102 1377 136 -72 52 O ATOM 1988 CB ILE B 97 -25.956 -22.787 80.888 1.00 11.06 C ANISOU 1988 CB ILE B 97 1235 1250 1716 217 -235 85 C ATOM 1989 CG1 ILE B 97 -25.001 -23.570 81.808 1.00 12.20 C ANISOU 1989 CG1 ILE B 97 1348 1350 1937 273 -349 126 C ATOM 1990 CG2 ILE B 97 -25.716 -21.281 80.962 1.00 10.75 C ANISOU 1990 CG2 ILE B 97 1175 1271 1636 172 -228 64 C ATOM 1991 CD1 ILE B 97 -25.020 -23.182 83.260 1.00 12.57 C ANISOU 1991 CD1 ILE B 97 1455 1421 1898 254 -457 188 C ATOM 1992 N LEU B 98 -28.806 -21.174 81.343 1.00 9.57 N ANISOU 1992 N LEU B 98 1210 1135 1289 111 -156 103 N ATOM 1993 CA LEU B 98 -29.709 -20.142 80.888 1.00 8.96 C ANISOU 1993 CA LEU B 98 1150 1089 1166 80 -105 78 C ATOM 1994 C LEU B 98 -28.935 -18.823 80.911 1.00 9.07 C ANISOU 1994 C LEU B 98 1130 1122 1191 66 -120 56 C ATOM 1995 O LEU B 98 -28.330 -18.461 81.925 1.00 9.42 O ANISOU 1995 O LEU B 98 1174 1176 1227 61 -178 59 O ATOM 1996 CB LEU B 98 -30.919 -20.106 81.805 1.00 8.98 C ANISOU 1996 CB LEU B 98 1212 1103 1096 58 -98 91 C ATOM 1997 CG LEU B 98 -32.003 -19.038 81.670 1.00 8.77 C ANISOU 1997 CG LEU B 98 1192 1099 1038 39 -58 59 C ATOM 1998 CD1 LEU B 98 -32.702 -19.090 80.303 1.00 8.47 C ANISOU 1998 CD1 LEU B 98 1133 1057 1027 44 -22 45 C ATOM 1999 CD2 LEU B 98 -33.055 -19.189 82.798 1.00 9.02 C ANISOU 1999 CD2 LEU B 98 1270 1149 1008 14 -36 59 C ATOM 2000 N SER B 99 -28.940 -18.111 79.783 1.00 8.88 N ANISOU 2000 N SER B 99 1087 1102 1184 51 -73 38 N ATOM 2001 CA SER B 99 -28.059 -16.965 79.571 1.00 9.12 C ANISOU 2001 CA SER B 99 1083 1136 1245 25 -74 23 C ATOM 2002 C SER B 99 -28.761 -15.945 78.706 1.00 8.97 C ANISOU 2002 C SER B 99 1095 1108 1204 1 -35 28 C ATOM 2003 O SER B 99 -29.694 -16.294 77.996 1.00 8.54 O ANISOU 2003 O SER B 99 1069 1056 1118 11 -11 37 O ATOM 2004 CB SER B 99 -26.762 -17.451 78.907 1.00 9.60 C ANISOU 2004 CB SER B 99 1069 1200 1377 28 -53 8 C ATOM 2005 OG SER B 99 -25.796 -16.426 78.763 1.00 10.02 O ANISOU 2005 OG SER B 99 1074 1258 1474 -11 -46 -6 O ATOM 2006 N MET B 100 -28.328 -14.684 78.779 1.00 9.45 N ANISOU 2006 N MET B 100 1153 1150 1286 -30 -41 23 N ATOM 2007 CA MET B 100 -29.006 -13.595 78.085 1.00 9.66 C ANISOU 2007 CA MET B 100 1221 1144 1302 -47 -24 42 C ATOM 2008 C MET B 100 -28.524 -13.465 76.662 1.00 9.81 C ANISOU 2008 C MET B 100 1241 1167 1317 -82 25 71 C ATOM 2009 O MET B 100 -27.341 -13.416 76.417 1.00 10.25 O ANISOU 2009 O MET B 100 1252 1233 1408 -119 57 63 O ATOM 2010 CB MET B 100 -28.767 -12.243 78.768 1.00 10.42 C ANISOU 2010 CB MET B 100 1327 1196 1433 -72 -50 24 C ATOM 2011 CG MET B 100 -29.510 -11.966 80.051 1.00 10.57 C ANISOU 2011 CG MET B 100 1369 1207 1437 -48 -84 -17 C ATOM 2012 SD MET B 100 -31.277 -12.283 80.001 1.00 10.75 S ANISOU 2012 SD MET B 100 1422 1233 1427 2 -70 -17 S ATOM 2013 CE MET B 100 -31.808 -10.774 79.131 1.00 10.97 C ANISOU 2013 CE MET B 100 1476 1179 1510 5 -78 3 C ATOM 2014 N ALA B 101 -29.461 -13.426 75.725 1.00 9.64 N ANISOU 2014 N ALA B 101 1268 1143 1248 -76 32 103 N ATOM 2015 CA ALA B 101 -29.171 -13.085 74.341 1.00 10.01 C ANISOU 2015 CA ALA B 101 1350 1195 1256 -123 74 144 C ATOM 2016 C ALA B 101 -28.804 -11.592 74.302 1.00 10.49 C ANISOU 2016 C ALA B 101 1440 1194 1351 -168 69 182 C ATOM 2017 O ALA B 101 -29.162 -10.800 75.203 1.00 10.75 O ANISOU 2017 O ALA B 101 1476 1173 1433 -148 22 172 O ATOM 2018 CB ALA B 101 -30.380 -13.373 73.465 1.00 9.94 C ANISOU 2018 CB ALA B 101 1396 1200 1180 -102 51 172 C ATOM 2019 N ASN B 102 -28.039 -11.192 73.318 1.00 10.90 N ANISOU 2019 N ASN B 102 1512 1248 1380 -238 126 219 N ATOM 2020 CA ASN B 102 -27.676 -9.783 73.226 1.00 11.46 C ANISOU 2020 CA ASN B 102 1620 1244 1489 -296 126 266 C ATOM 2021 C ASN B 102 -27.156 -9.444 71.834 1.00 12.27 C ANISOU 2021 C ASN B 102 1780 1355 1524 -384 198 334 C ATOM 2022 O ASN B 102 -26.963 -10.324 71.009 1.00 12.28 O ANISOU 2022 O ASN B 102 1783 1434 1449 -400 258 323 O ATOM 2023 CB ASN B 102 -26.710 -9.370 74.354 1.00 11.53 C ANISOU 2023 CB ASN B 102 1554 1228 1597 -319 124 210 C ATOM 2024 CG ASN B 102 -25.342 -9.951 74.205 1.00 11.90 C ANISOU 2024 CG ASN B 102 1513 1335 1673 -369 196 170 C ATOM 2025 OD1 ASN B 102 -24.777 -9.915 73.132 1.00 12.69 O ANISOU 2025 OD1 ASN B 102 1621 1458 1741 -437 280 199 O ATOM 2026 ND2 ASN B 102 -24.774 -10.460 75.305 1.00 11.65 N ANISOU 2026 ND2 ASN B 102 1391 1329 1705 -339 162 101 N ATOM 2027 N ALA B 103 -26.978 -8.154 71.593 1.00 13.01 N ANISOU 2027 N ALA B 103 1933 1364 1643 -445 194 401 N ATOM 2028 CA ALA B 103 -26.537 -7.630 70.304 1.00 14.17 C ANISOU 2028 CA ALA B 103 2163 1506 1714 -547 262 490 C ATOM 2029 C ALA B 103 -25.161 -6.959 70.449 1.00 14.93 C ANISOU 2029 C ALA B 103 2208 1573 1888 -657 349 479 C ATOM 2030 O ALA B 103 -24.789 -6.094 69.636 1.00 16.26 O ANISOU 2030 O ALA B 103 2456 1693 2025 -761 401 568 O ATOM 2031 CB ALA B 103 -27.574 -6.631 69.775 1.00 14.84 C ANISOU 2031 CB ALA B 103 2378 1495 1764 -535 173 605 C ATOM 2032 N GLY B 104 -24.408 -7.375 71.472 1.00 14.17 N ANISOU 2032 N GLY B 104 1981 1508 1894 -639 360 376 N ATOM 2033 CA GLY B 104 -23.148 -6.719 71.849 1.00 14.96 C ANISOU 2033 CA GLY B 104 2002 1578 2101 -734 413 345 C ATOM 2034 C GLY B 104 -23.176 -6.294 73.314 1.00 14.29 C ANISOU 2034 C GLY B 104 1862 1436 2131 -687 316 278 C ATOM 2035 O GLY B 104 -24.097 -6.668 74.036 1.00 13.13 O ANISOU 2035 O GLY B 104 1728 1290 1970 -581 229 249 O ATOM 2036 N PRO B 105 -22.157 -5.529 73.762 1.00 15.13 N ANISOU 2036 N PRO B 105 1904 1497 2345 -776 335 245 N ATOM 2037 CA PRO B 105 -22.117 -5.081 75.151 1.00 14.87 C ANISOU 2037 CA PRO B 105 1828 1416 2407 -746 239 168 C ATOM 2038 C PRO B 105 -23.354 -4.279 75.587 1.00 14.59 C ANISOU 2038 C PRO B 105 1905 1271 2367 -685 153 192 C ATOM 2039 O PRO B 105 -23.838 -3.398 74.859 1.00 15.27 O ANISOU 2039 O PRO B 105 2097 1257 2445 -716 161 282 O ATOM 2040 CB PRO B 105 -20.863 -4.201 75.209 1.00 16.32 C ANISOU 2040 CB PRO B 105 1945 1553 2703 -883 285 146 C ATOM 2041 CG PRO B 105 -19.975 -4.742 74.119 1.00 17.04 C ANISOU 2041 CG PRO B 105 1972 1728 2772 -960 418 169 C ATOM 2042 CD PRO B 105 -20.907 -5.215 73.037 1.00 16.54 C ANISOU 2042 CD PRO B 105 2028 1692 2564 -914 456 257 C ATOM 2043 N ASN B 106 -23.862 -4.610 76.767 1.00 13.72 N ANISOU 2043 N ASN B 106 1770 1179 2261 -596 72 113 N ATOM 2044 CA ASN B 106 -24.895 -3.800 77.417 1.00 13.73 C ANISOU 2044 CA ASN B 106 1846 1080 2288 -541 3 93 C ATOM 2045 C ASN B 106 -26.138 -3.594 76.563 1.00 13.61 C ANISOU 2045 C ASN B 106 1932 1011 2227 -481 -5 184 C ATOM 2046 O ASN B 106 -26.675 -2.512 76.513 1.00 14.39 O ANISOU 2046 O ASN B 106 2101 979 2385 -477 -37 212 O ATOM 2047 CB ASN B 106 -24.290 -2.469 77.873 1.00 14.95 C ANISOU 2047 CB ASN B 106 2009 1114 2555 -628 -10 56 C ATOM 2048 CG ASN B 106 -23.116 -2.680 78.792 1.00 15.22 C ANISOU 2048 CG ASN B 106 1933 1210 2636 -684 -28 -44 C ATOM 2049 OD1 ASN B 106 -23.109 -3.624 79.580 1.00 14.40 O ANISOU 2049 OD1 ASN B 106 1774 1212 2485 -623 -70 -106 O ATOM 2050 ND2 ASN B 106 -22.101 -1.847 78.673 1.00 16.49 N ANISOU 2050 ND2 ASN B 106 2062 1309 2894 -806 -3 -54 N ATOM 2051 N THR B 107 -26.595 -4.662 75.914 1.00 12.84 N ANISOU 2051 N THR B 107 1834 1009 2033 -431 12 225 N ATOM 2052 CA THR B 107 -27.829 -4.621 75.128 1.00 12.79 C ANISOU 2052 CA THR B 107 1909 974 1977 -368 -18 303 C ATOM 2053 C THR B 107 -28.819 -5.671 75.629 1.00 11.62 C ANISOU 2053 C THR B 107 1727 907 1779 -262 -51 252 C ATOM 2054 O THR B 107 -29.717 -6.065 74.918 1.00 11.48 O ANISOU 2054 O THR B 107 1744 912 1706 -214 -72 302 O ATOM 2055 CB THR B 107 -27.572 -4.833 73.614 1.00 13.34 C ANISOU 2055 CB THR B 107 2034 1076 1957 -428 33 413 C ATOM 2056 OG1 THR B 107 -26.847 -6.061 73.408 1.00 12.74 O ANISOU 2056 OG1 THR B 107 1886 1134 1820 -449 102 373 O ATOM 2057 CG2 THR B 107 -26.797 -3.661 73.024 1.00 14.82 C ANISOU 2057 CG2 THR B 107 2280 1164 2186 -544 72 489 C ATOM 2058 N ASN B 108 -28.665 -6.132 76.853 1.00 10.98 N ANISOU 2058 N ASN B 108 1583 873 1715 -234 -60 154 N ATOM 2059 CA ASN B 108 -29.633 -7.061 77.389 1.00 10.10 C ANISOU 2059 CA ASN B 108 1450 828 1559 -151 -81 113 C ATOM 2060 C ASN B 108 -31.054 -6.523 77.298 1.00 10.33 C ANISOU 2060 C ASN B 108 1515 791 1616 -79 -123 123 C ATOM 2061 O ASN B 108 -31.299 -5.375 77.639 1.00 11.07 O ANISOU 2061 O ASN B 108 1634 779 1790 -70 -148 104 O ATOM 2062 CB ASN B 108 -29.314 -7.385 78.835 1.00 9.82 C ANISOU 2062 CB ASN B 108 1369 833 1529 -142 -92 16 C ATOM 2063 CG ASN B 108 -27.940 -8.036 78.984 1.00 9.78 C ANISOU 2063 CG ASN B 108 1305 895 1513 -195 -76 4 C ATOM 2064 OD1 ASN B 108 -27.758 -9.163 78.587 1.00 9.21 O ANISOU 2064 OD1 ASN B 108 1204 897 1397 -181 -55 25 O ATOM 2065 ND2 ASN B 108 -26.978 -7.304 79.530 1.00 10.51 N ANISOU 2065 ND2 ASN B 108 1374 954 1663 -255 -90 -36 N ATOM 2066 N GLY B 109 -31.980 -7.378 76.855 1.00 9.84 N ANISOU 2066 N GLY B 109 1446 788 1502 -26 -132 144 N ATOM 2067 CA GLY B 109 -33.405 -7.050 76.775 1.00 10.17 C ANISOU 2067 CA GLY B 109 1490 787 1584 50 -179 143 C ATOM 2068 C GLY B 109 -34.269 -8.105 77.432 1.00 9.47 C ANISOU 2068 C GLY B 109 1346 783 1467 99 -165 79 C ATOM 2069 O GLY B 109 -34.206 -8.277 78.660 1.00 9.28 O ANISOU 2069 O GLY B 109 1295 784 1446 102 -135 -3 O ATOM 2070 N SER B 110 -35.110 -8.756 76.624 1.00 9.30 N ANISOU 2070 N SER B 110 1314 802 1414 129 -191 117 N ATOM 2071 CA SER B 110 -35.955 -9.870 77.068 1.00 8.79 C ANISOU 2071 CA SER B 110 1195 817 1326 158 -172 66 C ATOM 2072 C SER B 110 -35.452 -11.219 76.550 1.00 8.06 C ANISOU 2072 C SER B 110 1107 810 1144 119 -146 90 C ATOM 2073 O SER B 110 -35.651 -12.230 77.202 1.00 7.63 O ANISOU 2073 O SER B 110 1021 810 1066 118 -113 48 O ATOM 2074 CB SER B 110 -37.424 -9.663 76.665 1.00 9.35 C ANISOU 2074 CB SER B 110 1227 868 1457 223 -226 64 C ATOM 2075 OG SER B 110 -37.578 -9.640 75.257 1.00 9.79 O ANISOU 2075 OG SER B 110 1319 919 1479 221 -293 153 O ATOM 2076 N GLN B 111 -34.751 -11.222 75.423 1.00 8.20 N ANISOU 2076 N GLN B 111 1169 831 1113 81 -152 154 N ATOM 2077 CA GLN B 111 -34.303 -12.453 74.816 1.00 7.80 C ANISOU 2077 CA GLN B 111 1121 853 990 49 -121 160 C ATOM 2078 C GLN B 111 -33.269 -13.213 75.656 1.00 7.33 C ANISOU 2078 C GLN B 111 1032 824 926 27 -67 119 C ATOM 2079 O GLN B 111 -32.397 -12.619 76.259 1.00 7.49 O ANISOU 2079 O GLN B 111 1049 819 975 8 -55 110 O ATOM 2080 CB GLN B 111 -33.790 -12.203 73.407 1.00 8.30 C ANISOU 2080 CB GLN B 111 1243 919 991 5 -123 226 C ATOM 2081 CG GLN B 111 -34.874 -11.780 72.455 1.00 9.01 C ANISOU 2081 CG GLN B 111 1370 994 1059 27 -201 279 C ATOM 2082 CD GLN B 111 -34.378 -11.638 71.025 1.00 9.77 C ANISOU 2082 CD GLN B 111 1550 1109 1052 -31 -201 351 C ATOM 2083 OE1 GLN B 111 -33.732 -12.547 70.500 1.00 9.60 O ANISOU 2083 OE1 GLN B 111 1538 1154 955 -76 -138 327 O ATOM 2084 NE2 GLN B 111 -34.668 -10.501 70.394 1.00 10.72 N ANISOU 2084 NE2 GLN B 111 1737 1167 1169 -32 -267 439 N ATOM 2085 N PHE B 112 -33.385 -14.535 75.659 1.00 7.06 N ANISOU 2085 N PHE B 112 978 838 863 30 -47 95 N ATOM 2086 CA PHE B 112 -32.512 -15.435 76.404 1.00 6.84 C ANISOU 2086 CA PHE B 112 926 831 842 23 -17 68 C ATOM 2087 C PHE B 112 -32.255 -16.673 75.549 1.00 6.94 C ANISOU 2087 C PHE B 112 936 873 827 14 10 60 C ATOM 2088 O PHE B 112 -32.912 -16.886 74.523 1.00 7.03 O ANISOU 2088 O PHE B 112 969 900 800 7 5 64 O ATOM 2089 CB PHE B 112 -33.174 -15.872 77.709 1.00 6.61 C ANISOU 2089 CB PHE B 112 883 806 821 44 -24 40 C ATOM 2090 CG PHE B 112 -34.469 -16.582 77.489 1.00 6.56 C ANISOU 2090 CG PHE B 112 870 816 807 55 -24 29 C ATOM 2091 CD1 PHE B 112 -34.494 -17.937 77.278 1.00 6.48 C ANISOU 2091 CD1 PHE B 112 857 821 785 46 -8 23 C ATOM 2092 CD2 PHE B 112 -35.656 -15.874 77.415 1.00 6.81 C ANISOU 2092 CD2 PHE B 112 886 838 860 75 -44 20 C ATOM 2093 CE1 PHE B 112 -35.684 -18.582 77.017 1.00 6.57 C ANISOU 2093 CE1 PHE B 112 854 843 798 42 -9 7 C ATOM 2094 CE2 PHE B 112 -36.839 -16.516 77.171 1.00 6.94 C ANISOU 2094 CE2 PHE B 112 874 875 886 79 -48 3 C ATOM 2095 CZ PHE B 112 -36.847 -17.866 76.959 1.00 6.79 C ANISOU 2095 CZ PHE B 112 857 876 847 55 -30 -3 C ATOM 2096 N PHE B 113 -31.310 -17.497 75.992 1.00 7.09 N ANISOU 2096 N PHE B 113 927 896 871 17 31 40 N ATOM 2097 CA PHE B 113 -31.092 -18.783 75.366 1.00 7.44 C ANISOU 2097 CA PHE B 113 962 949 913 19 61 14 C ATOM 2098 C PHE B 113 -30.777 -19.866 76.370 1.00 7.59 C ANISOU 2098 C PHE B 113 959 945 978 46 48 5 C ATOM 2099 O PHE B 113 -30.311 -19.595 77.473 1.00 7.61 O ANISOU 2099 O PHE B 113 950 939 1002 56 17 21 O ATOM 2100 CB PHE B 113 -30.020 -18.705 74.254 1.00 7.95 C ANISOU 2100 CB PHE B 113 1016 1033 972 -6 115 -2 C ATOM 2101 CG PHE B 113 -28.644 -18.348 74.738 1.00 8.16 C ANISOU 2101 CG PHE B 113 986 1052 1058 -10 131 -7 C ATOM 2102 CD1 PHE B 113 -28.291 -17.029 74.963 1.00 8.22 C ANISOU 2102 CD1 PHE B 113 995 1055 1071 -38 121 20 C ATOM 2103 CD2 PHE B 113 -27.701 -19.330 74.973 1.00 8.48 C ANISOU 2103 CD2 PHE B 113 967 1085 1169 16 147 -45 C ATOM 2104 CE1 PHE B 113 -27.021 -16.708 75.382 1.00 8.62 C ANISOU 2104 CE1 PHE B 113 982 1104 1189 -52 130 6 C ATOM 2105 CE2 PHE B 113 -26.430 -19.005 75.408 1.00 8.91 C ANISOU 2105 CE2 PHE B 113 948 1139 1297 16 148 -56 C ATOM 2106 CZ PHE B 113 -26.088 -17.692 75.598 1.00 8.97 C ANISOU 2106 CZ PHE B 113 951 1153 1301 -25 140 -32 C ATOM 2107 N ILE B 114 -31.101 -21.098 75.988 1.00 7.92 N ANISOU 2107 N ILE B 114 1007 973 1029 52 63 -18 N ATOM 2108 CA ILE B 114 -30.842 -22.242 76.787 1.00 8.38 C ANISOU 2108 CA ILE B 114 1058 987 1136 77 47 -14 C ATOM 2109 C ILE B 114 -29.793 -23.065 76.028 1.00 9.14 C ANISOU 2109 C ILE B 114 1118 1061 1293 98 82 -61 C ATOM 2110 O ILE B 114 -30.011 -23.450 74.888 1.00 9.48 O ANISOU 2110 O ILE B 114 1169 1113 1317 82 128 -111 O ATOM 2111 CB ILE B 114 -32.128 -23.087 76.998 1.00 8.43 C ANISOU 2111 CB ILE B 114 1100 973 1130 62 44 -11 C ATOM 2112 CG1 ILE B 114 -33.228 -22.228 77.614 1.00 8.10 C ANISOU 2112 CG1 ILE B 114 1072 962 1041 41 31 11 C ATOM 2113 CG2 ILE B 114 -31.823 -24.325 77.839 1.00 8.73 C ANISOU 2113 CG2 ILE B 114 1150 946 1221 80 25 11 C ATOM 2114 CD1 ILE B 114 -34.649 -22.795 77.397 1.00 8.26 C ANISOU 2114 CD1 ILE B 114 1099 982 1055 12 42 -5 C ATOM 2115 N CYS B 115 -28.657 -23.314 76.657 1.00 9.77 N ANISOU 2115 N CYS B 115 1151 1115 1446 135 58 -54 N ATOM 2116 CA CYS B 115 -27.603 -24.091 76.042 1.00 10.68 C ANISOU 2116 CA CYS B 115 1206 1200 1649 168 95 -111 C ATOM 2117 C CYS B 115 -28.027 -25.517 75.948 1.00 11.02 C ANISOU 2117 C CYS B 115 1274 1171 1739 192 95 -134 C ATOM 2118 O CYS B 115 -28.686 -26.041 76.855 1.00 10.72 O ANISOU 2118 O CYS B 115 1285 1089 1700 195 42 -77 O ATOM 2119 CB CYS B 115 -26.316 -24.007 76.845 1.00 11.40 C ANISOU 2119 CB CYS B 115 1222 1277 1833 211 45 -97 C ATOM 2120 SG CYS B 115 -25.691 -22.336 76.885 1.00 11.87 S ANISOU 2120 SG CYS B 115 1241 1408 1859 167 51 -88 S ATOM 2121 N THR B 116 -27.685 -26.132 74.824 1.00 11.64 N ANISOU 2121 N THR B 116 1328 1237 1855 198 166 -221 N ATOM 2122 CA THR B 116 -27.785 -27.568 74.722 1.00 12.55 C ANISOU 2122 CA THR B 116 1454 1259 2055 231 169 -263 C ATOM 2123 C THR B 116 -26.426 -28.247 74.620 1.00 13.71 C ANISOU 2123 C THR B 116 1509 1346 2351 304 187 -323 C ATOM 2124 O THR B 116 -26.375 -29.451 74.410 1.00 14.88 O ANISOU 2124 O THR B 116 1657 1399 2595 342 197 -375 O ATOM 2125 CB THR B 116 -28.663 -27.992 73.530 1.00 12.81 C ANISOU 2125 CB THR B 116 1537 1305 2025 182 232 -341 C ATOM 2126 OG1 THR B 116 -28.134 -27.412 72.327 1.00 13.26 O ANISOU 2126 OG1 THR B 116 1569 1440 2026 156 316 -418 O ATOM 2127 CG2 THR B 116 -30.146 -27.589 73.779 1.00 11.85 C ANISOU 2127 CG2 THR B 116 1485 1218 1797 124 192 -283 C ATOM 2128 N ALA B 117 -25.344 -27.482 74.752 1.00 13.76 N ANISOU 2128 N ALA B 117 1431 1402 2395 323 190 -323 N ATOM 2129 CA ALA B 117 -23.977 -28.007 74.810 1.00 14.90 C ANISOU 2129 CA ALA B 117 1455 1496 2707 400 192 -378 C ATOM 2130 C ALA B 117 -23.207 -27.049 75.706 1.00 14.56 C ANISOU 2130 C ALA B 117 1347 1501 2684 408 118 -311 C ATOM 2131 O ALA B 117 -23.759 -26.062 76.161 1.00 13.50 O ANISOU 2131 O ALA B 117 1271 1427 2429 353 84 -240 O ATOM 2132 CB ALA B 117 -23.341 -28.055 73.409 1.00 15.74 C ANISOU 2132 CB ALA B 117 1495 1645 2840 386 339 -519 C ATOM 2133 N LYS B 118 -21.956 -27.363 75.991 1.00 15.60 N ANISOU 2133 N LYS B 118 1350 1597 2977 480 86 -343 N ATOM 2134 CA LYS B 118 -21.052 -26.422 76.640 1.00 15.72 C ANISOU 2134 CA LYS B 118 1275 1668 3028 478 24 -311 C ATOM 2135 C LYS B 118 -20.683 -25.355 75.612 1.00 15.49 C ANISOU 2135 C LYS B 118 1196 1742 2946 398 161 -381 C ATOM 2136 O LYS B 118 -20.245 -25.692 74.552 1.00 16.30 O ANISOU 2136 O LYS B 118 1238 1854 3100 398 287 -486 O ATOM 2137 CB LYS B 118 -19.807 -27.169 77.113 1.00 17.35 C ANISOU 2137 CB LYS B 118 1337 1805 3449 583 -53 -338 C ATOM 2138 CG LYS B 118 -18.755 -26.332 77.763 1.00 17.92 C ANISOU 2138 CG LYS B 118 1287 1932 3589 585 -132 -323 C ATOM 2139 CD LYS B 118 -17.627 -27.212 78.352 1.00 19.75 C ANISOU 2139 CD LYS B 118 1373 2080 4048 708 -252 -335 C ATOM 2140 CE LYS B 118 -16.731 -26.394 79.249 1.00 20.32 C ANISOU 2140 CE LYS B 118 1342 2208 4169 704 -381 -300 C ATOM 2141 NZ LYS B 118 -15.842 -27.262 80.044 1.00 22.20 N ANISOU 2141 NZ LYS B 118 1470 2360 4604 828 -554 -275 N ATOM 2142 N THR B 119 -20.854 -24.073 75.929 1.00 14.64 N ANISOU 2142 N THR B 119 1122 1705 2736 326 141 -324 N ATOM 2143 CA THR B 119 -20.585 -22.993 74.974 1.00 14.54 C ANISOU 2143 CA THR B 119 1088 1774 2662 237 265 -365 C ATOM 2144 C THR B 119 -19.643 -21.961 75.589 1.00 14.92 C ANISOU 2144 C THR B 119 1038 1860 2770 206 218 -349 C ATOM 2145 O THR B 119 -19.995 -20.786 75.787 1.00 14.04 O ANISOU 2145 O THR B 119 988 1784 2560 133 205 -297 O ATOM 2146 CB THR B 119 -21.879 -22.332 74.513 1.00 13.27 C ANISOU 2146 CB THR B 119 1081 1647 2312 163 298 -315 C ATOM 2147 OG1 THR B 119 -22.553 -21.729 75.634 1.00 12.28 O ANISOU 2147 OG1 THR B 119 1027 1514 2122 157 181 -222 O ATOM 2148 CG2 THR B 119 -22.798 -23.370 73.858 1.00 13.12 C ANISOU 2148 CG2 THR B 119 1146 1597 2241 183 336 -344 C ATOM 2149 N GLU B 120 -18.432 -22.418 75.865 1.00 16.32 N ANISOU 2149 N GLU B 120 1053 2020 3125 264 190 -403 N ATOM 2150 CA GLU B 120 -17.457 -21.644 76.633 1.00 17.07 C ANISOU 2150 CA GLU B 120 1030 2142 3311 247 109 -395 C ATOM 2151 C GLU B 120 -16.961 -20.351 75.947 1.00 17.09 C ANISOU 2151 C GLU B 120 986 2216 3291 129 228 -428 C ATOM 2152 O GLU B 120 -16.633 -19.382 76.626 1.00 17.04 O ANISOU 2152 O GLU B 120 954 2229 3290 78 155 -397 O ATOM 2153 CB GLU B 120 -16.260 -22.543 77.040 1.00 19.00 C ANISOU 2153 CB GLU B 120 1090 2348 3781 350 36 -451 C ATOM 2154 CG GLU B 120 -15.236 -22.825 75.943 1.00 20.74 C ANISOU 2154 CG GLU B 120 1136 2591 4151 353 199 -584 C ATOM 2155 CD GLU B 120 -15.743 -23.756 74.836 1.00 21.01 C ANISOU 2155 CD GLU B 120 1231 2598 4153 378 344 -652 C ATOM 2156 OE1 GLU B 120 -16.853 -24.343 74.955 1.00 20.15 O ANISOU 2156 OE1 GLU B 120 1282 2438 3934 406 300 -595 O ATOM 2157 OE2 GLU B 120 -15.018 -23.903 73.827 1.00 22.54 O ANISOU 2157 OE2 GLU B 120 1307 2825 4432 360 511 -773 O ATOM 2158 N TRP B 121 -16.911 -20.343 74.615 1.00 17.20 N ANISOU 2158 N TRP B 121 999 2263 3271 76 411 -490 N ATOM 2159 CA TRP B 121 -16.602 -19.128 73.854 1.00 17.38 C ANISOU 2159 CA TRP B 121 1019 2345 3238 -54 540 -497 C ATOM 2160 C TRP B 121 -17.592 -17.999 74.110 1.00 15.89 C ANISOU 2160 C TRP B 121 998 2153 2884 -125 488 -393 C ATOM 2161 O TRP B 121 -17.288 -16.862 73.819 1.00 16.20 O ANISOU 2161 O TRP B 121 1038 2215 2901 -229 546 -376 O ATOM 2162 CB TRP B 121 -16.507 -19.387 72.339 1.00 18.13 C ANISOU 2162 CB TRP B 121 1124 2484 3281 -108 749 -571 C ATOM 2163 CG TRP B 121 -17.826 -19.721 71.697 1.00 17.00 C ANISOU 2163 CG TRP B 121 1173 2334 2950 -109 774 -533 C ATOM 2164 CD1 TRP B 121 -18.671 -18.868 71.098 1.00 16.29 C ANISOU 2164 CD1 TRP B 121 1242 2269 2678 -198 811 -461 C ATOM 2165 CD2 TRP B 121 -18.456 -21.002 71.663 1.00 16.61 C ANISOU 2165 CD2 TRP B 121 1172 2242 2896 -14 741 -562 C ATOM 2166 NE1 TRP B 121 -19.794 -19.529 70.661 1.00 15.50 N ANISOU 2166 NE1 TRP B 121 1275 2158 2456 -166 801 -449 N ATOM 2167 CE2 TRP B 121 -19.680 -20.846 70.998 1.00 15.69 C ANISOU 2167 CE2 TRP B 121 1235 2141 2586 -60 765 -515 C ATOM 2168 CE3 TRP B 121 -18.095 -22.266 72.122 1.00 17.15 C ANISOU 2168 CE3 TRP B 121 1148 2251 3117 102 687 -621 C ATOM 2169 CZ2 TRP B 121 -20.540 -21.910 70.760 1.00 15.30 C ANISOU 2169 CZ2 TRP B 121 1266 2057 2489 -5 747 -539 C ATOM 2170 CZ3 TRP B 121 -18.942 -23.326 71.877 1.00 16.76 C ANISOU 2170 CZ3 TRP B 121 1192 2154 3022 158 677 -638 C ATOM 2171 CH2 TRP B 121 -20.151 -23.142 71.213 1.00 15.84 C ANISOU 2171 CH2 TRP B 121 1246 2061 2709 99 709 -602 C ATOM 2172 N LEU B 122 -18.768 -18.288 74.657 1.00 14.40 N ANISOU 2172 N LEU B 122 947 1929 2594 -73 386 -327 N ATOM 2173 CA LEU B 122 -19.685 -17.217 75.028 1.00 13.21 C ANISOU 2173 CA LEU B 122 930 1767 2320 -123 329 -244 C ATOM 2174 C LEU B 122 -19.318 -16.591 76.393 1.00 13.19 C ANISOU 2174 C LEU B 122 886 1748 2376 -121 192 -223 C ATOM 2175 O LEU B 122 -19.904 -15.573 76.796 1.00 12.46 O ANISOU 2175 O LEU B 122 885 1640 2209 -166 150 -176 O ATOM 2176 CB LEU B 122 -21.137 -17.711 74.995 1.00 11.95 C ANISOU 2176 CB LEU B 122 920 1586 2034 -80 295 -196 C ATOM 2177 CG LEU B 122 -21.574 -18.283 73.625 1.00 12.06 C ANISOU 2177 CG LEU B 122 989 1622 1971 -94 414 -225 C ATOM 2178 CD1 LEU B 122 -22.988 -18.783 73.632 1.00 10.91 C ANISOU 2178 CD1 LEU B 122 967 1455 1720 -58 366 -187 C ATOM 2179 CD2 LEU B 122 -21.376 -17.223 72.531 1.00 12.59 C ANISOU 2179 CD2 LEU B 122 1093 1726 1965 -203 528 -212 C ATOM 2180 N ASP B 123 -18.360 -17.199 77.105 1.00 14.01 N ANISOU 2180 N ASP B 123 855 1852 2615 -65 113 -262 N ATOM 2181 CA ASP B 123 -17.997 -16.704 78.434 1.00 14.26 C ANISOU 2181 CA ASP B 123 854 1879 2684 -63 -37 -247 C ATOM 2182 C ASP B 123 -17.437 -15.284 78.312 1.00 14.80 C ANISOU 2182 C ASP B 123 883 1960 2779 -177 0 -265 C ATOM 2183 O ASP B 123 -16.659 -14.989 77.416 1.00 15.66 O ANISOU 2183 O ASP B 123 895 2091 2962 -241 121 -307 O ATOM 2184 CB ASP B 123 -17.012 -17.651 79.162 1.00 15.36 C ANISOU 2184 CB ASP B 123 849 2015 2972 21 -152 -279 C ATOM 2185 CG ASP B 123 -17.679 -18.960 79.636 1.00 14.90 C ANISOU 2185 CG ASP B 123 866 1916 2878 129 -232 -234 C ATOM 2186 OD1 ASP B 123 -18.917 -19.021 79.734 1.00 13.70 O ANISOU 2186 OD1 ASP B 123 875 1748 2581 129 -227 -180 O ATOM 2187 OD2 ASP B 123 -16.966 -19.941 79.943 1.00 15.98 O ANISOU 2187 OD2 ASP B 123 897 2029 3145 215 -307 -252 O ATOM 2188 N GLY B 124 -17.889 -14.399 79.187 1.00 14.41 N ANISOU 2188 N GLY B 124 918 1892 2663 -211 -91 -235 N ATOM 2189 CA GLY B 124 -17.451 -13.010 79.161 1.00 15.07 C ANISOU 2189 CA GLY B 124 982 1964 2777 -323 -67 -252 C ATOM 2190 C GLY B 124 -18.207 -12.172 78.132 1.00 14.57 C ANISOU 2190 C GLY B 124 1041 1870 2623 -393 59 -208 C ATOM 2191 O GLY B 124 -17.967 -10.986 78.031 1.00 15.03 O ANISOU 2191 O GLY B 124 1110 1897 2703 -489 86 -207 O ATOM 2192 N LYS B 125 -19.117 -12.792 77.369 1.00 13.70 N ANISOU 2192 N LYS B 125 1026 1763 2416 -348 125 -169 N ATOM 2193 CA LYS B 125 -19.911 -12.070 76.364 1.00 13.38 C ANISOU 2193 CA LYS B 125 1111 1695 2277 -404 218 -113 C ATOM 2194 C LYS B 125 -21.404 -12.047 76.656 1.00 12.04 C ANISOU 2194 C LYS B 125 1088 1494 1991 -346 159 -63 C ATOM 2195 O LYS B 125 -22.078 -11.057 76.365 1.00 11.88 O ANISOU 2195 O LYS B 125 1167 1426 1921 -386 170 -18 O ATOM 2196 CB LYS B 125 -19.707 -12.679 74.983 1.00 13.92 C ANISOU 2196 CB LYS B 125 1165 1804 2319 -422 358 -117 C ATOM 2197 CG LYS B 125 -18.367 -12.399 74.412 1.00 15.54 C ANISOU 2197 CG LYS B 125 1239 2038 2624 -510 466 -164 C ATOM 2198 CD LYS B 125 -18.091 -13.340 73.281 1.00 16.20 C ANISOU 2198 CD LYS B 125 1287 2177 2690 -502 601 -203 C ATOM 2199 CE LYS B 125 -17.056 -12.739 72.329 1.00 17.97 C ANISOU 2199 CE LYS B 125 1437 2434 2956 -633 766 -229 C ATOM 2200 NZ LYS B 125 -16.678 -13.777 71.302 1.00 18.85 N ANISOU 2200 NZ LYS B 125 1492 2610 3058 -620 912 -301 N ATOM 2201 N HIS B 126 -21.923 -13.150 77.187 1.00 11.17 N ANISOU 2201 N HIS B 126 987 1404 1852 -255 101 -70 N ATOM 2202 CA HIS B 126 -23.317 -13.243 77.536 1.00 10.09 C ANISOU 2202 CA HIS B 126 965 1247 1621 -205 55 -36 C ATOM 2203 C HIS B 126 -23.426 -13.555 79.003 1.00 9.95 C ANISOU 2203 C HIS B 126 942 1231 1604 -158 -54 -55 C ATOM 2204 O HIS B 126 -22.693 -14.416 79.489 1.00 10.29 O ANISOU 2204 O HIS B 126 910 1300 1699 -123 -99 -75 O ATOM 2205 CB HIS B 126 -23.945 -14.342 76.726 1.00 9.55 C ANISOU 2205 CB HIS B 126 929 1202 1498 -160 103 -24 C ATOM 2206 CG HIS B 126 -23.930 -14.072 75.257 1.00 9.90 C ANISOU 2206 CG HIS B 126 1002 1256 1501 -213 206 -5 C ATOM 2207 ND1 HIS B 126 -24.995 -13.503 74.599 1.00 9.60 N ANISOU 2207 ND1 HIS B 126 1072 1199 1374 -229 215 46 N ATOM 2208 CD2 HIS B 126 -22.966 -14.253 74.330 1.00 10.74 C ANISOU 2208 CD2 HIS B 126 1047 1395 1637 -260 306 -33 C ATOM 2209 CE1 HIS B 126 -24.699 -13.378 73.319 1.00 10.32 C ANISOU 2209 CE1 HIS B 126 1187 1313 1422 -287 305 62 C ATOM 2210 NE2 HIS B 126 -23.469 -13.818 73.130 1.00 10.98 N ANISOU 2210 NE2 HIS B 126 1168 1431 1570 -313 375 9 N ATOM 2211 N VAL B 127 -24.344 -12.862 79.698 1.00 9.58 N ANISOU 2211 N VAL B 127 979 1157 1501 -157 -96 -48 N ATOM 2212 CA VAL B 127 -24.550 -13.026 81.135 1.00 9.59 C ANISOU 2212 CA VAL B 127 1003 1169 1469 -130 -187 -70 C ATOM 2213 C VAL B 127 -25.372 -14.273 81.459 1.00 9.18 C ANISOU 2213 C VAL B 127 994 1140 1353 -67 -201 -43 C ATOM 2214 O VAL B 127 -26.576 -14.370 81.117 1.00 8.62 O ANISOU 2214 O VAL B 127 987 1059 1228 -49 -159 -25 O ATOM 2215 CB VAL B 127 -25.233 -11.777 81.742 1.00 9.58 C ANISOU 2215 CB VAL B 127 1073 1130 1437 -158 -203 -95 C ATOM 2216 CG1 VAL B 127 -25.624 -12.023 83.207 1.00 9.67 C ANISOU 2216 CG1 VAL B 127 1128 1167 1375 -137 -275 -126 C ATOM 2217 CG2 VAL B 127 -24.309 -10.577 81.626 1.00 10.36 C ANISOU 2217 CG2 VAL B 127 1131 1191 1612 -230 -205 -125 C ATOM 2218 N VAL B 128 -24.720 -15.237 82.102 1.00 9.68 N ANISOU 2218 N VAL B 128 1016 1226 1433 -36 -266 -38 N ATOM 2219 CA VAL B 128 -25.394 -16.435 82.606 1.00 9.49 C ANISOU 2219 CA VAL B 128 1044 1208 1353 10 -291 -3 C ATOM 2220 C VAL B 128 -26.136 -16.080 83.897 1.00 9.70 C ANISOU 2220 C VAL B 128 1158 1249 1278 -4 -336 -6 C ATOM 2221 O VAL B 128 -25.581 -15.413 84.761 1.00 10.30 O ANISOU 2221 O VAL B 128 1234 1340 1340 -33 -403 -36 O ATOM 2222 CB VAL B 128 -24.403 -17.570 82.940 1.00 10.16 C ANISOU 2222 CB VAL B 128 1066 1293 1500 54 -364 15 C ATOM 2223 CG1 VAL B 128 -25.160 -18.776 83.492 1.00 10.06 C ANISOU 2223 CG1 VAL B 128 1128 1266 1427 92 -391 67 C ATOM 2224 CG2 VAL B 128 -23.558 -17.974 81.729 1.00 10.38 C ANISOU 2224 CG2 VAL B 128 989 1310 1642 72 -305 -6 C ATOM 2225 N PHE B 129 -27.369 -16.566 84.051 1.00 9.41 N ANISOU 2225 N PHE B 129 1193 1212 1168 7 -296 14 N ATOM 2226 CA PHE B 129 -28.171 -16.203 85.219 1.00 9.82 C ANISOU 2226 CA PHE B 129 1326 1286 1118 -15 -305 -2 C ATOM 2227 C PHE B 129 -29.088 -17.295 85.754 1.00 10.14 C ANISOU 2227 C PHE B 129 1433 1337 1080 -9 -286 40 C ATOM 2228 O PHE B 129 -29.814 -17.075 86.736 1.00 10.50 O ANISOU 2228 O PHE B 129 1549 1411 1027 -39 -270 22 O ATOM 2229 CB PHE B 129 -28.993 -14.955 84.914 1.00 9.41 C ANISOU 2229 CB PHE B 129 1287 1218 1068 -33 -239 -56 C ATOM 2230 CG PHE B 129 -30.044 -15.159 83.866 1.00 8.66 C ANISOU 2230 CG PHE B 129 1187 1105 998 -10 -163 -41 C ATOM 2231 CD1 PHE B 129 -29.736 -15.057 82.512 1.00 8.29 C ANISOU 2231 CD1 PHE B 129 1095 1033 1020 0 -139 -23 C ATOM 2232 CD2 PHE B 129 -31.361 -15.396 84.221 1.00 8.57 C ANISOU 2232 CD2 PHE B 129 1212 1105 937 -7 -115 -51 C ATOM 2233 CE1 PHE B 129 -30.730 -15.244 81.538 1.00 7.74 C ANISOU 2233 CE1 PHE B 129 1028 954 957 15 -90 -9 C ATOM 2234 CE2 PHE B 129 -32.349 -15.555 83.249 1.00 8.06 C ANISOU 2234 CE2 PHE B 129 1129 1027 906 12 -64 -43 C ATOM 2235 CZ PHE B 129 -32.029 -15.495 81.919 1.00 7.62 C ANISOU 2235 CZ PHE B 129 1038 949 907 25 -63 -20 C ATOM 2236 N GLY B 130 -29.064 -18.464 85.116 1.00 10.19 N ANISOU 2236 N GLY B 130 1420 1318 1131 20 -278 89 N ATOM 2237 CA GLY B 130 -29.851 -19.605 85.570 1.00 10.67 C ANISOU 2237 CA GLY B 130 1544 1371 1136 16 -262 140 C ATOM 2238 C GLY B 130 -29.456 -20.911 84.904 1.00 10.92 C ANISOU 2238 C GLY B 130 1548 1352 1247 54 -277 187 C ATOM 2239 O GLY B 130 -28.491 -20.961 84.107 1.00 10.94 O ANISOU 2239 O GLY B 130 1473 1335 1346 90 -296 171 O ATOM 2240 N LYS B 131 -30.226 -21.949 85.221 1.00 11.53 N ANISOU 2240 N LYS B 131 1686 1404 1288 41 -255 235 N ATOM 2241 CA LYS B 131 -30.003 -23.306 84.724 1.00 12.06 C ANISOU 2241 CA LYS B 131 1745 1402 1433 73 -269 276 C ATOM 2242 C LYS B 131 -31.319 -24.093 84.738 1.00 12.24 C ANISOU 2242 C LYS B 131 1826 1401 1423 31 -197 299 C ATOM 2243 O LYS B 131 -32.145 -23.916 85.654 1.00 12.53 O ANISOU 2243 O LYS B 131 1930 1473 1358 -23 -166 318 O ATOM 2244 CB LYS B 131 -29.007 -24.010 85.636 1.00 13.31 C ANISOU 2244 CB LYS B 131 1933 1524 1597 102 -386 350 C ATOM 2245 CG LYS B 131 -28.414 -25.264 85.058 1.00 13.91 C ANISOU 2245 CG LYS B 131 1975 1509 1801 160 -419 378 C ATOM 2246 CD LYS B 131 -27.345 -25.847 85.983 1.00 15.40 C ANISOU 2246 CD LYS B 131 2179 1655 2017 205 -564 456 C ATOM 2247 CE LYS B 131 -26.898 -27.240 85.476 1.00 16.34 C ANISOU 2247 CE LYS B 131 2270 1653 2283 274 -595 485 C ATOM 2248 NZ LYS B 131 -26.666 -27.236 83.992 1.00 15.55 N ANISOU 2248 NZ LYS B 131 2059 1541 2308 309 -502 378 N ATOM 2249 N VAL B 132 -31.499 -24.986 83.762 1.00 12.31 N ANISOU 2249 N VAL B 132 1807 1351 1518 48 -166 288 N ATOM 2250 CA VAL B 132 -32.655 -25.882 83.759 1.00 12.79 C ANISOU 2250 CA VAL B 132 1914 1375 1570 0 -108 308 C ATOM 2251 C VAL B 132 -32.606 -26.775 84.998 1.00 14.27 C ANISOU 2251 C VAL B 132 2200 1513 1709 -26 -153 411 C ATOM 2252 O VAL B 132 -31.574 -27.369 85.288 1.00 14.84 O ANISOU 2252 O VAL B 132 2287 1523 1826 22 -244 466 O ATOM 2253 CB VAL B 132 -32.737 -26.761 82.505 1.00 12.61 C ANISOU 2253 CB VAL B 132 1851 1287 1651 20 -80 267 C ATOM 2254 CG1 VAL B 132 -33.879 -27.782 82.666 1.00 13.07 C ANISOU 2254 CG1 VAL B 132 1961 1293 1711 -43 -32 292 C ATOM 2255 CG2 VAL B 132 -32.933 -25.881 81.211 1.00 11.61 C ANISOU 2255 CG2 VAL B 132 1650 1220 1539 30 -35 176 C ATOM 2256 N LYS B 133 -33.729 -26.841 85.710 1.00 15.20 N ANISOU 2256 N LYS B 133 2380 1656 1736 -106 -88 436 N ATOM 2257 CA LYS B 133 -33.897 -27.642 86.924 1.00 17.21 C ANISOU 2257 CA LYS B 133 2753 1874 1910 -162 -108 545 C ATOM 2258 C LYS B 133 -34.545 -29.016 86.562 1.00 17.85 C ANISOU 2258 C LYS B 133 2865 1848 2067 -202 -66 584 C ATOM 2259 O LYS B 133 -34.015 -30.065 86.900 1.00 19.44 O ANISOU 2259 O LYS B 133 3135 1943 2305 -188 -135 678 O ATOM 2260 CB LYS B 133 -34.752 -26.817 87.914 1.00 17.95 C ANISOU 2260 CB LYS B 133 2895 2071 1854 -242 -33 531 C ATOM 2261 CG LYS B 133 -34.840 -27.282 89.371 1.00 20.07 C ANISOU 2261 CG LYS B 133 3307 2343 1973 -316 -47 640 C ATOM 2262 CD LYS B 133 -35.007 -26.022 90.306 1.00 20.72 C ANISOU 2262 CD LYS B 133 3419 2552 1901 -354 -14 588 C ATOM 2263 CE LYS B 133 -35.185 -26.347 91.799 1.00 22.87 C ANISOU 2263 CE LYS B 133 3851 2857 1979 -448 -9 681 C ATOM 2264 NZ LYS B 133 -34.575 -25.271 92.708 1.00 23.80 N ANISOU 2264 NZ LYS B 133 4015 3072 1953 -448 -68 646 N ATOM 2265 N GLU B 134 -35.675 -28.987 85.864 1.00 17.21 N ANISOU 2265 N GLU B 134 2729 1788 2021 -250 34 510 N ATOM 2266 CA GLU B 134 -36.423 -30.183 85.421 1.00 17.58 C ANISOU 2266 CA GLU B 134 2789 1741 2148 -305 83 519 C ATOM 2267 C GLU B 134 -36.839 -29.923 83.982 1.00 15.91 C ANISOU 2267 C GLU B 134 2463 1551 2029 -280 118 396 C ATOM 2268 O GLU B 134 -37.019 -28.765 83.572 1.00 14.66 O ANISOU 2268 O GLU B 134 2231 1494 1843 -254 135 321 O ATOM 2269 CB GLU B 134 -37.712 -30.359 86.238 1.00 18.97 C ANISOU 2269 CB GLU B 134 3013 1948 2244 -431 188 550 C ATOM 2270 CG GLU B 134 -37.684 -31.345 87.356 1.00 21.10 C ANISOU 2270 CG GLU B 134 3425 2137 2452 -503 181 691 C ATOM 2271 CD GLU B 134 -39.084 -31.571 87.947 1.00 22.58 C ANISOU 2271 CD GLU B 134 3641 2360 2578 -648 321 700 C ATOM 2272 OE1 GLU B 134 -39.590 -32.719 87.913 1.00 24.05 O ANISOU 2272 OE1 GLU B 134 3873 2439 2826 -728 359 753 O ATOM 2273 OE2 GLU B 134 -39.690 -30.589 88.447 1.00 22.86 O ANISOU 2273 OE2 GLU B 134 3646 2526 2515 -687 403 646 O ATOM 2274 N GLY B 135 -37.021 -30.983 83.224 1.00 15.73 N ANISOU 2274 N GLY B 135 2435 1431 2111 -291 123 374 N ATOM 2275 CA GLY B 135 -37.518 -30.857 81.867 1.00 14.90 C ANISOU 2275 CA GLY B 135 2238 1350 2070 -286 149 257 C ATOM 2276 C GLY B 135 -36.442 -30.618 80.819 1.00 14.01 C ANISOU 2276 C GLY B 135 2080 1234 2007 -189 98 195 C ATOM 2277 O GLY B 135 -36.726 -30.060 79.746 1.00 13.23 O ANISOU 2277 O GLY B 135 1915 1201 1911 -179 112 104 O ATOM 2278 N MET B 136 -35.206 -31.032 81.100 1.00 14.09 N ANISOU 2278 N MET B 136 2123 1173 2058 -120 39 242 N ATOM 2279 CA MET B 136 -34.189 -30.974 80.055 1.00 13.64 C ANISOU 2279 CA MET B 136 2009 1105 2067 -38 15 167 C ATOM 2280 C MET B 136 -34.632 -31.855 78.881 1.00 13.51 C ANISOU 2280 C MET B 136 1976 1025 2130 -61 53 73 C ATOM 2281 O MET B 136 -34.308 -31.543 77.749 1.00 12.94 O ANISOU 2281 O MET B 136 1854 996 2066 -31 69 -22 O ATOM 2282 CB MET B 136 -32.806 -31.399 80.545 1.00 14.60 C ANISOU 2282 CB MET B 136 2143 1148 2256 44 -56 222 C ATOM 2283 CG MET B 136 -31.670 -30.969 79.603 1.00 14.47 C ANISOU 2283 CG MET B 136 2041 1161 2294 125 -60 137 C ATOM 2284 SD MET B 136 -31.546 -29.178 79.392 1.00 13.82 S ANISOU 2284 SD MET B 136 1903 1245 2100 122 -43 107 S ATOM 2285 CE MET B 136 -30.699 -29.049 77.775 1.00 13.21 C ANISOU 2285 CE MET B 136 1745 1189 2084 166 5 -17 C ATOM 2286 N ASN B 137 -35.391 -32.925 79.147 1.00 13.87 N ANISOU 2286 N ASN B 137 2071 973 2223 -126 70 96 N ATOM 2287 CA ASN B 137 -35.918 -33.759 78.054 1.00 14.15 C ANISOU 2287 CA ASN B 137 2094 949 2333 -164 101 -8 C ATOM 2288 C ASN B 137 -36.810 -32.945 77.103 1.00 13.26 C ANISOU 2288 C ASN B 137 1920 969 2149 -208 129 -102 C ATOM 2289 O ASN B 137 -36.787 -33.161 75.908 1.00 13.28 O ANISOU 2289 O ASN B 137 1898 974 2170 -205 137 -212 O ATOM 2290 CB ASN B 137 -36.599 -35.050 78.558 1.00 15.29 C ANISOU 2290 CB ASN B 137 2304 951 2555 -242 115 36 C ATOM 2291 CG ASN B 137 -37.740 -34.786 79.534 1.00 15.29 C ANISOU 2291 CG ASN B 137 2326 1002 2479 -344 151 118 C ATOM 2292 OD1 ASN B 137 -37.818 -33.734 80.173 1.00 14.42 O ANISOU 2292 OD1 ASN B 137 2201 1009 2265 -337 155 165 O ATOM 2293 ND2 ASN B 137 -38.622 -35.739 79.648 1.00 16.29 N ANISOU 2293 ND2 ASN B 137 2484 1038 2665 -444 187 123 N ATOM 2294 N ILE B 138 -37.512 -31.941 77.633 1.00 12.55 N ANISOU 2294 N ILE B 138 1805 988 1973 -239 138 -61 N ATOM 2295 CA ILE B 138 -38.381 -31.087 76.833 1.00 12.01 C ANISOU 2295 CA ILE B 138 1674 1038 1851 -267 142 -131 C ATOM 2296 C ILE B 138 -37.568 -30.097 75.960 1.00 11.37 C ANISOU 2296 C ILE B 138 1567 1038 1715 -195 118 -172 C ATOM 2297 O ILE B 138 -37.885 -29.905 74.778 1.00 11.23 O ANISOU 2297 O ILE B 138 1525 1070 1670 -207 108 -254 O ATOM 2298 CB ILE B 138 -39.420 -30.366 77.715 1.00 11.72 C ANISOU 2298 CB ILE B 138 1607 1076 1769 -315 165 -84 C ATOM 2299 CG1 ILE B 138 -40.262 -31.394 78.471 1.00 12.75 C ANISOU 2299 CG1 ILE B 138 1763 1130 1949 -410 210 -49 C ATOM 2300 CG2 ILE B 138 -40.316 -29.421 76.877 1.00 11.28 C ANISOU 2300 CG2 ILE B 138 1471 1131 1682 -324 147 -154 C ATOM 2301 CD1 ILE B 138 -41.083 -32.347 77.571 1.00 13.59 C ANISOU 2301 CD1 ILE B 138 1842 1186 2134 -484 214 -137 C ATOM 2302 N VAL B 139 -36.503 -29.525 76.518 1.00 11.16 N ANISOU 2302 N VAL B 139 1550 1022 1667 -130 108 -116 N ATOM 2303 CA VAL B 139 -35.571 -28.714 75.734 1.00 10.93 C ANISOU 2303 CA VAL B 139 1499 1051 1601 -75 101 -150 C ATOM 2304 C VAL B 139 -34.934 -29.542 74.603 1.00 11.85 C ANISOU 2304 C VAL B 139 1619 1120 1762 -59 122 -241 C ATOM 2305 O VAL B 139 -34.760 -29.022 73.501 1.00 11.82 O ANISOU 2305 O VAL B 139 1604 1185 1701 -59 134 -303 O ATOM 2306 CB VAL B 139 -34.465 -28.037 76.618 1.00 10.58 C ANISOU 2306 CB VAL B 139 1453 1017 1549 -17 84 -81 C ATOM 2307 CG1 VAL B 139 -33.407 -27.347 75.737 1.00 10.29 C ANISOU 2307 CG1 VAL B 139 1384 1028 1496 24 93 -124 C ATOM 2308 CG2 VAL B 139 -35.091 -27.014 77.620 1.00 9.94 C ANISOU 2308 CG2 VAL B 139 1372 999 1404 -36 73 -19 C ATOM 2309 N GLU B 140 -34.630 -30.819 74.849 1.00 12.92 N ANISOU 2309 N GLU B 140 1778 1135 1995 -50 129 -252 N ATOM 2310 CA GLU B 140 -34.134 -31.708 73.783 1.00 14.15 C ANISOU 2310 CA GLU B 140 1936 1231 2209 -36 160 -365 C ATOM 2311 C GLU B 140 -35.201 -31.939 72.714 1.00 14.52 C ANISOU 2311 C GLU B 140 1992 1315 2207 -111 169 -461 C ATOM 2312 O GLU B 140 -34.895 -31.912 71.520 1.00 14.72 O ANISOU 2312 O GLU B 140 2019 1382 2190 -113 196 -564 O ATOM 2313 CB GLU B 140 -33.631 -33.069 74.330 1.00 15.39 C ANISOU 2313 CB GLU B 140 2116 1222 2508 -3 155 -356 C ATOM 2314 CG GLU B 140 -32.363 -32.938 75.221 1.00 15.67 C ANISOU 2314 CG GLU B 140 2132 1217 2604 86 123 -275 C ATOM 2315 CD GLU B 140 -32.146 -34.074 76.249 1.00 17.04 C ANISOU 2315 CD GLU B 140 2349 1226 2897 113 76 -192 C ATOM 2316 OE1 GLU B 140 -33.004 -35.014 76.400 1.00 17.84 O ANISOU 2316 OE1 GLU B 140 2506 1229 3042 52 80 -183 O ATOM 2317 OE2 GLU B 140 -31.078 -33.998 76.926 1.00 17.57 O ANISOU 2317 OE2 GLU B 140 2394 1261 3018 193 27 -129 O ATOM 2318 N ALA B 141 -36.440 -32.180 73.141 1.00 14.67 N ANISOU 2318 N ALA B 141 2018 1324 2232 -180 147 -431 N ATOM 2319 CA ALA B 141 -37.545 -32.333 72.190 1.00 15.37 C ANISOU 2319 CA ALA B 141 2098 1458 2281 -256 132 -520 C ATOM 2320 C ALA B 141 -37.669 -31.073 71.282 1.00 15.08 C ANISOU 2320 C ALA B 141 2044 1571 2114 -250 106 -541 C ATOM 2321 O ALA B 141 -37.867 -31.208 70.072 1.00 15.41 O ANISOU 2321 O ALA B 141 2101 1656 2097 -283 95 -640 O ATOM 2322 CB ALA B 141 -38.871 -32.639 72.910 1.00 15.35 C ANISOU 2322 CB ALA B 141 2078 1435 2320 -334 118 -479 C ATOM 2323 N MET B 142 -37.510 -29.876 71.853 1.00 14.64 N ANISOU 2323 N MET B 142 1967 1585 2009 -212 92 -449 N ATOM 2324 CA MET B 142 -37.582 -28.627 71.057 1.00 14.88 C ANISOU 2324 CA MET B 142 1992 1734 1928 -204 60 -446 C ATOM 2325 C MET B 142 -36.462 -28.546 70.018 1.00 15.36 C ANISOU 2325 C MET B 142 2088 1820 1926 -183 99 -504 C ATOM 2326 O MET B 142 -36.680 -28.126 68.882 1.00 15.82 O ANISOU 2326 O MET B 142 2173 1957 1878 -213 78 -548 O ATOM 2327 CB MET B 142 -37.522 -27.389 71.953 1.00 14.33 C ANISOU 2327 CB MET B 142 1896 1707 1840 -165 46 -342 C ATOM 2328 CG MET B 142 -38.744 -27.178 72.836 1.00 14.57 C ANISOU 2328 CG MET B 142 1882 1744 1907 -190 22 -300 C ATOM 2329 SD MET B 142 -38.350 -26.076 74.232 1.00 14.81 S ANISOU 2329 SD MET B 142 1900 1788 1937 -141 37 -201 S ATOM 2330 CE MET B 142 -37.732 -24.657 73.304 1.00 13.82 C ANISOU 2330 CE MET B 142 1786 1735 1730 -101 6 -189 C ATOM 2331 N GLU B 143 -35.272 -28.968 70.427 1.00 15.62 N ANISOU 2331 N GLU B 143 2119 1789 2027 -134 156 -505 N ATOM 2332 CA GLU B 143 -34.080 -29.031 69.575 1.00 16.50 C ANISOU 2332 CA GLU B 143 2242 1914 2113 -112 221 -577 C ATOM 2333 C GLU B 143 -34.322 -29.822 68.285 1.00 17.61 C ANISOU 2333 C GLU B 143 2422 2061 2205 -162 248 -714 C ATOM 2334 O GLU B 143 -33.744 -29.522 67.252 1.00 18.16 O ANISOU 2334 O GLU B 143 2519 2199 2181 -176 298 -778 O ATOM 2335 CB GLU B 143 -32.942 -29.687 70.354 1.00 17.21 C ANISOU 2335 CB GLU B 143 2298 1904 2336 -45 261 -571 C ATOM 2336 CG GLU B 143 -31.578 -29.051 70.194 1.00 17.72 C ANISOU 2336 CG GLU B 143 2325 2006 2399 0 315 -572 C ATOM 2337 CD GLU B 143 -30.481 -29.778 70.978 1.00 18.61 C ANISOU 2337 CD GLU B 143 2385 2015 2669 76 330 -571 C ATOM 2338 OE1 GLU B 143 -30.724 -30.240 72.114 1.00 19.19 O ANISOU 2338 OE1 GLU B 143 2461 2006 2824 102 271 -494 O ATOM 2339 OE2 GLU B 143 -29.351 -29.911 70.459 1.00 20.39 O ANISOU 2339 OE2 GLU B 143 2564 2239 2941 111 400 -648 O ATOM 2340 N ARG B 144 -35.179 -30.831 68.336 1.00 18.01 N ANISOU 2340 N ARG B 144 2482 2044 2314 -199 219 -766 N ATOM 2341 CA ARG B 144 -35.456 -31.638 67.154 1.00 19.34 C ANISOU 2341 CA ARG B 144 2693 2213 2440 -254 236 -914 C ATOM 2342 C ARG B 144 -36.221 -30.891 66.074 1.00 19.27 C ANISOU 2342 C ARG B 144 2724 2341 2257 -319 179 -935 C ATOM 2343 O ARG B 144 -36.266 -31.334 64.938 1.00 20.71 O ANISOU 2343 O ARG B 144 2957 2557 2352 -370 194 -1060 O ATOM 2344 CB ARG B 144 -36.179 -32.911 67.545 1.00 20.32 C ANISOU 2344 CB ARG B 144 2816 2215 2689 -288 216 -962 C ATOM 2345 CG ARG B 144 -35.268 -33.864 68.318 1.00 20.94 C ANISOU 2345 CG ARG B 144 2880 2136 2937 -222 270 -963 C ATOM 2346 CD ARG B 144 -35.851 -35.266 68.388 1.00 22.39 C ANISOU 2346 CD ARG B 144 3085 2176 3243 -267 265 -1040 C ATOM 2347 NE ARG B 144 -36.701 -35.390 69.543 1.00 22.22 N ANISOU 2347 NE ARG B 144 3051 2100 3290 -296 216 -917 N ATOM 2348 CZ ARG B 144 -36.276 -35.659 70.781 1.00 22.33 C ANISOU 2348 CZ ARG B 144 3061 2011 3409 -247 217 -801 C ATOM 2349 NH1 ARG B 144 -34.980 -35.858 71.037 1.00 22.54 N ANISOU 2349 NH1 ARG B 144 3082 1969 3511 -151 247 -791 N ATOM 2350 NH2 ARG B 144 -37.160 -35.720 71.782 1.00 22.14 N ANISOU 2350 NH2 ARG B 144 3037 1959 3415 -296 187 -694 N ATOM 2351 N PHE B 145 -36.794 -29.747 66.429 1.00 17.86 N ANISOU 2351 N PHE B 145 2526 2236 2024 -315 107 -814 N ATOM 2352 CA PHE B 145 -37.465 -28.886 65.457 1.00 17.92 C ANISOU 2352 CA PHE B 145 2571 2365 1872 -360 29 -803 C ATOM 2353 C PHE B 145 -36.522 -27.828 64.892 1.00 17.48 C ANISOU 2353 C PHE B 145 2561 2388 1690 -344 71 -756 C ATOM 2354 O PHE B 145 -36.913 -27.072 64.016 1.00 17.91 O ANISOU 2354 O PHE B 145 2671 2538 1596 -382 8 -730 O ATOM 2355 CB PHE B 145 -38.729 -28.256 66.082 1.00 17.20 C ANISOU 2355 CB PHE B 145 2422 2296 1814 -361 -80 -709 C ATOM 2356 CG PHE B 145 -39.761 -29.282 66.474 1.00 17.66 C ANISOU 2356 CG PHE B 145 2433 2292 1983 -405 -114 -765 C ATOM 2357 CD1 PHE B 145 -40.630 -29.788 65.541 1.00 18.88 C ANISOU 2357 CD1 PHE B 145 2600 2483 2087 -478 -187 -863 C ATOM 2358 CD2 PHE B 145 -39.806 -29.796 67.775 1.00 17.04 C ANISOU 2358 CD2 PHE B 145 2304 2116 2054 -384 -70 -721 C ATOM 2359 CE1 PHE B 145 -41.568 -30.757 65.891 1.00 19.51 C ANISOU 2359 CE1 PHE B 145 2627 2500 2283 -533 -212 -921 C ATOM 2360 CE2 PHE B 145 -40.744 -30.777 68.131 1.00 17.65 C ANISOU 2360 CE2 PHE B 145 2343 2127 2234 -443 -86 -767 C ATOM 2361 CZ PHE B 145 -41.619 -31.257 67.192 1.00 18.80 C ANISOU 2361 CZ PHE B 145 2487 2305 2348 -519 -153 -870 C ATOM 2362 N GLY B 146 -35.284 -27.789 65.379 1.00 16.62 N ANISOU 2362 N GLY B 146 2431 2238 1646 -294 172 -741 N ATOM 2363 CA GLY B 146 -34.331 -26.776 64.950 1.00 16.48 C ANISOU 2363 CA GLY B 146 2441 2287 1532 -290 229 -694 C ATOM 2364 C GLY B 146 -33.669 -27.074 63.628 1.00 17.79 C ANISOU 2364 C GLY B 146 2675 2513 1567 -344 320 -808 C ATOM 2365 O GLY B 146 -33.967 -28.063 62.982 1.00 18.68 O ANISOU 2365 O GLY B 146 2821 2619 1655 -381 331 -937 O ATOM 2366 N SER B 147 -32.727 -26.214 63.255 1.00 18.07 N ANISOU 2366 N SER B 147 2733 2606 1523 -354 396 -769 N ATOM 2367 CA SER B 147 -31.911 -26.401 62.072 1.00 19.66 C ANISOU 2367 CA SER B 147 2995 2876 1598 -412 521 -877 C ATOM 2368 C SER B 147 -30.608 -25.598 62.190 1.00 19.68 C ANISOU 2368 C SER B 147 2963 2901 1613 -404 637 -828 C ATOM 2369 O SER B 147 -30.413 -24.860 63.149 1.00 18.30 O ANISOU 2369 O SER B 147 2729 2690 1535 -357 600 -709 O ATOM 2370 CB SER B 147 -32.699 -25.955 60.833 1.00 20.82 C ANISOU 2370 CB SER B 147 3272 3134 1505 -503 450 -868 C ATOM 2371 OG SER B 147 -33.021 -24.575 60.929 1.00 20.24 O ANISOU 2371 OG SER B 147 3231 3101 1357 -510 362 -696 O ATOM 2372 N ARG B 148 -29.740 -25.740 61.199 1.00 21.48 N ANISOU 2372 N ARG B 148 3227 3192 1739 -461 783 -931 N ATOM 2373 CA ARG B 148 -28.406 -25.102 61.194 1.00 22.13 C ANISOU 2373 CA ARG B 148 3259 3302 1844 -471 924 -915 C ATOM 2374 C ARG B 148 -28.423 -23.568 61.328 1.00 21.49 C ANISOU 2374 C ARG B 148 3218 3262 1684 -506 873 -733 C ATOM 2375 O ARG B 148 -27.593 -23.011 62.043 1.00 20.78 O ANISOU 2375 O ARG B 148 3039 3140 1715 -477 917 -677 O ATOM 2376 CB ARG B 148 -27.624 -25.492 59.940 1.00 24.51 C ANISOU 2376 CB ARG B 148 3609 3686 2018 -548 1106 -1069 C ATOM 2377 CG ARG B 148 -26.217 -24.969 59.972 1.00 25.46 C ANISOU 2377 CG ARG B 148 3645 3831 2196 -562 1271 -1076 C ATOM 2378 CD ARG B 148 -25.386 -25.391 58.768 1.00 28.12 C ANISOU 2378 CD ARG B 148 4011 4254 2418 -642 1485 -1249 C ATOM 2379 NE ARG B 148 -24.072 -24.749 58.879 1.00 28.93 N ANISOU 2379 NE ARG B 148 4012 4383 2594 -664 1640 -1239 N ATOM 2380 CZ ARG B 148 -22.955 -25.177 58.298 1.00 30.99 C ANISOU 2380 CZ ARG B 148 4200 4687 2885 -694 1861 -1406 C ATOM 2381 NH1 ARG B 148 -22.932 -26.277 57.542 1.00 32.73 N ANISOU 2381 NH1 ARG B 148 4446 4925 3065 -701 1965 -1612 N ATOM 2382 NH2 ARG B 148 -21.840 -24.496 58.477 1.00 31.53 N ANISOU 2382 NH2 ARG B 148 4161 4780 3036 -721 1985 -1381 N ATOM 2383 N ASN B 149 -29.370 -22.922 60.646 1.00 21.88 N ANISOU 2383 N ASN B 149 3397 3372 1543 -568 771 -645 N ATOM 2384 CA ASN B 149 -29.568 -21.480 60.707 1.00 21.62 C ANISOU 2384 CA ASN B 149 3420 3355 1438 -597 697 -465 C ATOM 2385 C ASN B 149 -30.546 -21.043 61.793 1.00 19.83 C ANISOU 2385 C ASN B 149 3148 3052 1332 -517 521 -351 C ATOM 2386 O ASN B 149 -30.708 -19.852 62.020 1.00 19.57 O ANISOU 2386 O ASN B 149 3143 3006 1286 -521 456 -212 O ATOM 2387 CB ASN B 149 -29.998 -20.912 59.341 1.00 23.60 C ANISOU 2387 CB ASN B 149 3846 3706 1415 -706 671 -414 C ATOM 2388 CG ASN B 149 -31.276 -21.568 58.784 1.00 24.28 C ANISOU 2388 CG ASN B 149 4007 3823 1393 -713 532 -460 C ATOM 2389 OD1 ASN B 149 -32.287 -21.734 59.478 1.00 23.36 O ANISOU 2389 OD1 ASN B 149 3838 3650 1385 -642 380 -428 O ATOM 2390 ND2 ASN B 149 -31.219 -21.946 57.527 1.00 26.52 N ANISOU 2390 ND2 ASN B 149 4411 4205 1460 -807 590 -547 N ATOM 2391 N GLY B 150 -31.177 -21.982 62.495 1.00 18.70 N ANISOU 2391 N GLY B 150 2935 2854 1317 -447 456 -413 N ATOM 2392 CA GLY B 150 -32.001 -21.637 63.652 1.00 17.02 C ANISOU 2392 CA GLY B 150 2661 2572 1231 -375 325 -324 C ATOM 2393 C GLY B 150 -33.494 -21.668 63.383 1.00 17.03 C ANISOU 2393 C GLY B 150 2706 2589 1173 -377 171 -297 C ATOM 2394 O GLY B 150 -34.307 -21.679 64.305 1.00 15.64 O ANISOU 2394 O GLY B 150 2465 2362 1115 -321 80 -262 O ATOM 2395 N LYS B 151 -33.853 -21.694 62.103 1.00 18.60 N ANISOU 2395 N LYS B 151 3012 2866 1186 -448 143 -319 N ATOM 2396 CA LYS B 151 -35.238 -21.736 61.702 1.00 19.15 C ANISOU 2396 CA LYS B 151 3117 2963 1193 -456 -19 -302 C ATOM 2397 C LYS B 151 -35.844 -23.028 62.217 1.00 18.50 C ANISOU 2397 C LYS B 151 2954 2837 1236 -428 -37 -416 C ATOM 2398 O LYS B 151 -35.224 -24.077 62.106 1.00 18.71 O ANISOU 2398 O LYS B 151 2969 2848 1290 -441 72 -542 O ATOM 2399 CB LYS B 151 -35.326 -21.676 60.170 1.00 21.43 C ANISOU 2399 CB LYS B 151 3551 3354 1235 -550 -39 -322 C ATOM 2400 CG LYS B 151 -36.710 -21.431 59.604 1.00 22.48 C ANISOU 2400 CG LYS B 151 3734 3530 1277 -564 -242 -273 C ATOM 2401 CD LYS B 151 -36.829 -22.048 58.214 1.00 24.67 C ANISOU 2401 CD LYS B 151 4136 3908 1327 -662 -251 -371 C ATOM 2402 CE LYS B 151 -37.961 -21.418 57.402 1.00 26.22 C ANISOU 2402 CE LYS B 151 4421 4168 1370 -691 -471 -277 C ATOM 2403 NZ LYS B 151 -38.111 -22.084 56.072 1.00 28.40 N ANISOU 2403 NZ LYS B 151 4829 4554 1406 -795 -493 -386 N ATOM 2404 N THR B 152 -37.047 -22.936 62.783 1.00 17.78 N ANISOU 2404 N THR B 152 2803 2720 1232 -392 -170 -376 N ATOM 2405 CA THR B 152 -37.771 -24.066 63.323 1.00 17.40 C ANISOU 2405 CA THR B 152 2676 2624 1307 -381 -194 -465 C ATOM 2406 C THR B 152 -38.805 -24.529 62.295 1.00 18.87 C ANISOU 2406 C THR B 152 2906 2873 1387 -442 -310 -534 C ATOM 2407 O THR B 152 -39.270 -23.723 61.501 1.00 19.81 O ANISOU 2407 O THR B 152 3091 3063 1371 -466 -421 -467 O ATOM 2408 CB THR B 152 -38.448 -23.695 64.683 1.00 16.13 C ANISOU 2408 CB THR B 152 2408 2402 1319 -315 -246 -389 C ATOM 2409 OG1 THR B 152 -39.457 -22.687 64.482 1.00 16.35 O ANISOU 2409 OG1 THR B 152 2428 2464 1318 -301 -388 -303 O ATOM 2410 CG2 THR B 152 -37.396 -23.174 65.677 1.00 14.83 C ANISOU 2410 CG2 THR B 152 2212 2184 1236 -262 -148 -325 C ATOM 2411 N SER B 153 -39.112 -25.827 62.262 1.00 19.19 N ANISOU 2411 N SER B 153 2921 2884 1484 -474 -290 -666 N ATOM 2412 CA SER B 153 -40.070 -26.380 61.298 1.00 20.71 C ANISOU 2412 CA SER B 153 3149 3135 1583 -544 -402 -757 C ATOM 2413 C SER B 153 -41.496 -26.375 61.844 1.00 20.59 C ANISOU 2413 C SER B 153 3025 3104 1692 -533 -544 -730 C ATOM 2414 O SER B 153 -42.419 -26.683 61.131 1.00 21.88 O ANISOU 2414 O SER B 153 3192 3319 1799 -588 -668 -791 O ATOM 2415 CB SER B 153 -39.707 -27.818 60.940 1.00 21.45 C ANISOU 2415 CB SER B 153 3267 3192 1689 -594 -307 -934 C ATOM 2416 OG SER B 153 -39.723 -28.640 62.102 1.00 20.43 O ANISOU 2416 OG SER B 153 3041 2943 1777 -557 -243 -961 O ATOM 2417 N LYS B 154 -41.654 -26.076 63.123 1.00 19.30 N ANISOU 2417 N LYS B 154 2760 2873 1700 -469 -518 -654 N ATOM 2418 CA LYS B 154 -42.961 -25.812 63.713 1.00 19.32 C ANISOU 2418 CA LYS B 154 2644 2870 1823 -451 -631 -617 C ATOM 2419 C LYS B 154 -42.830 -24.634 64.665 1.00 18.04 C ANISOU 2419 C LYS B 154 2433 2683 1737 -367 -617 -485 C ATOM 2420 O LYS B 154 -41.755 -24.356 65.162 1.00 16.82 O ANISOU 2420 O LYS B 154 2313 2492 1584 -332 -505 -440 O ATOM 2421 CB LYS B 154 -43.497 -27.048 64.451 1.00 19.30 C ANISOU 2421 CB LYS B 154 2553 2795 1981 -486 -584 -707 C ATOM 2422 CG LYS B 154 -43.949 -28.145 63.488 1.00 20.97 C ANISOU 2422 CG LYS B 154 2797 3027 2144 -577 -633 -850 C ATOM 2423 CD LYS B 154 -44.787 -29.275 64.133 1.00 21.37 C ANISOU 2423 CD LYS B 154 2747 3003 2367 -632 -620 -932 C ATOM 2424 CE LYS B 154 -44.760 -30.487 63.184 1.00 22.87 C ANISOU 2424 CE LYS B 154 3005 3182 2503 -722 -622 -1094 C ATOM 2425 NZ LYS B 154 -45.879 -31.447 63.360 1.00 24.03 N ANISOU 2425 NZ LYS B 154 3059 3285 2783 -806 -670 -1189 N ATOM 2426 N LYS B 155 -43.935 -23.945 64.905 1.00 18.42 N ANISOU 2426 N LYS B 155 2391 2750 1857 -336 -736 -436 N ATOM 2427 CA LYS B 155 -43.939 -22.839 65.846 1.00 17.60 C ANISOU 2427 CA LYS B 155 2231 2613 1842 -256 -723 -335 C ATOM 2428 C LYS B 155 -43.811 -23.375 67.276 1.00 16.22 C ANISOU 2428 C LYS B 155 1980 2369 1812 -244 -592 -355 C ATOM 2429 O LYS B 155 -44.703 -24.071 67.754 1.00 16.37 O ANISOU 2429 O LYS B 155 1904 2375 1940 -275 -593 -412 O ATOM 2430 CB LYS B 155 -45.225 -22.022 65.670 1.00 18.90 C ANISOU 2430 CB LYS B 155 2304 2810 2066 -219 -888 -297 C ATOM 2431 CG LYS B 155 -45.215 -20.734 66.453 1.00 18.58 C ANISOU 2431 CG LYS B 155 2221 2729 2109 -130 -886 -201 C ATOM 2432 CD LYS B 155 -46.341 -19.783 66.043 1.00 20.07 C ANISOU 2432 CD LYS B 155 2335 2937 2350 -75 -1069 -155 C ATOM 2433 CE LYS B 155 -46.110 -18.421 66.670 1.00 19.73 C ANISOU 2433 CE LYS B 155 2284 2835 2375 14 -1060 -61 C ATOM 2434 NZ LYS B 155 -45.033 -17.760 65.895 1.00 19.99 N ANISOU 2434 NZ LYS B 155 2486 2864 2244 8 -1067 33 N ATOM 2435 N ILE B 156 -42.691 -23.068 67.937 1.00 14.95 N ANISOU 2435 N ILE B 156 1865 2166 1647 -209 -482 -305 N ATOM 2436 CA ILE B 156 -42.422 -23.520 69.306 1.00 13.84 C ANISOU 2436 CA ILE B 156 1680 1964 1613 -197 -368 -306 C ATOM 2437 C ILE B 156 -42.718 -22.340 70.209 1.00 13.29 C ANISOU 2437 C ILE B 156 1552 1887 1609 -136 -375 -239 C ATOM 2438 O ILE B 156 -42.001 -21.343 70.170 1.00 13.14 O ANISOU 2438 O ILE B 156 1582 1864 1545 -93 -374 -175 O ATOM 2439 CB ILE B 156 -40.953 -23.921 69.520 1.00 13.20 C ANISOU 2439 CB ILE B 156 1676 1842 1494 -192 -260 -301 C ATOM 2440 CG1 ILE B 156 -40.414 -24.817 68.371 1.00 13.97 C ANISOU 2440 CG1 ILE B 156 1848 1952 1507 -239 -245 -377 C ATOM 2441 CG2 ILE B 156 -40.783 -24.587 70.863 1.00 12.60 C ANISOU 2441 CG2 ILE B 156 1566 1701 1518 -190 -173 -298 C ATOM 2442 CD1 ILE B 156 -41.045 -26.181 68.209 1.00 14.65 C ANISOU 2442 CD1 ILE B 156 1913 2009 1644 -298 -245 -474 C ATOM 2443 N THR B 157 -43.795 -22.405 70.978 1.00 13.24 N ANISOU 2443 N THR B 157 1439 1877 1713 -137 -377 -261 N ATOM 2444 CA THR B 157 -44.201 -21.273 71.803 1.00 12.93 C ANISOU 2444 CA THR B 157 1334 1831 1746 -76 -377 -224 C ATOM 2445 C THR B 157 -44.170 -21.582 73.322 1.00 12.19 C ANISOU 2445 C THR B 157 1204 1705 1719 -86 -253 -233 C ATOM 2446 O THR B 157 -44.053 -22.720 73.739 1.00 11.79 O ANISOU 2446 O THR B 157 1168 1634 1677 -143 -183 -258 O ATOM 2447 CB THR B 157 -45.629 -20.815 71.463 1.00 14.04 C ANISOU 2447 CB THR B 157 1356 2006 1973 -56 -485 -251 C ATOM 2448 OG1 THR B 157 -46.520 -21.886 71.705 1.00 14.60 O ANISOU 2448 OG1 THR B 157 1339 2089 2119 -122 -461 -325 O ATOM 2449 CG2 THR B 157 -45.764 -20.346 69.995 1.00 14.96 C ANISOU 2449 CG2 THR B 157 1516 2157 2009 -41 -640 -222 C ATOM 2450 N ILE B 158 -44.287 -20.522 74.115 1.00 12.00 N ANISOU 2450 N ILE B 158 1145 1674 1740 -33 -232 -212 N ATOM 2451 CA ILE B 158 -44.432 -20.590 75.562 1.00 11.76 C ANISOU 2451 CA ILE B 158 1081 1630 1755 -44 -122 -227 C ATOM 2452 C ILE B 158 -45.914 -20.376 75.820 1.00 12.93 C ANISOU 2452 C ILE B 158 1086 1808 2020 -44 -127 -287 C ATOM 2453 O ILE B 158 -46.407 -19.243 75.847 1.00 13.35 O ANISOU 2453 O ILE B 158 1072 1862 2137 23 -169 -298 O ATOM 2454 CB ILE B 158 -43.549 -19.522 76.254 1.00 11.13 C ANISOU 2454 CB ILE B 158 1056 1526 1643 8 -90 -188 C ATOM 2455 CG1 ILE B 158 -42.062 -19.787 75.957 1.00 10.21 C ANISOU 2455 CG1 ILE B 158 1057 1389 1433 2 -85 -137 C ATOM 2456 CG2 ILE B 158 -43.807 -19.457 77.784 1.00 11.22 C ANISOU 2456 CG2 ILE B 158 1040 1539 1682 -7 19 -216 C ATOM 2457 CD1 ILE B 158 -41.134 -18.645 76.374 1.00 9.74 C ANISOU 2457 CD1 ILE B 158 1045 1306 1348 47 -78 -101 C ATOM 2458 N ALA B 159 -46.634 -21.496 75.949 1.00 13.58 N ANISOU 2458 N ALA B 159 1111 1903 2143 -122 -87 -332 N ATOM 2459 CA ALA B 159 -48.090 -21.512 76.136 1.00 14.88 C ANISOU 2459 CA ALA B 159 1113 2102 2436 -142 -82 -404 C ATOM 2460 C ALA B 159 -48.472 -20.901 77.473 1.00 15.24 C ANISOU 2460 C ALA B 159 1097 2156 2536 -128 37 -434 C ATOM 2461 O ALA B 159 -49.515 -20.286 77.613 1.00 16.25 O ANISOU 2461 O ALA B 159 1080 2310 2784 -95 33 -497 O ATOM 2462 CB ALA B 159 -48.635 -22.974 76.036 1.00 15.42 C ANISOU 2462 CB ALA B 159 1150 2174 2533 -255 -46 -444 C ATOM 2463 N ASP B 160 -47.616 -21.095 78.466 1.00 14.65 N ANISOU 2463 N ASP B 160 1132 2061 2373 -155 143 -397 N ATOM 2464 CA ASP B 160 -47.841 -20.549 79.776 1.00 15.07 C ANISOU 2464 CA ASP B 160 1158 2129 2436 -154 265 -430 C ATOM 2465 C ASP B 160 -46.506 -20.519 80.512 1.00 14.10 C ANISOU 2465 C ASP B 160 1196 1979 2180 -156 308 -364 C ATOM 2466 O ASP B 160 -45.558 -21.218 80.144 1.00 13.22 O ANISOU 2466 O ASP B 160 1192 1837 1992 -174 270 -298 O ATOM 2467 CB ASP B 160 -48.861 -21.400 80.543 1.00 16.34 C ANISOU 2467 CB ASP B 160 1233 2322 2650 -259 393 -483 C ATOM 2468 CG ASP B 160 -49.524 -20.620 81.678 1.00 17.40 C ANISOU 2468 CG ASP B 160 1283 2495 2831 -251 520 -559 C ATOM 2469 OD1 ASP B 160 -49.469 -19.384 81.660 1.00 17.47 O ANISOU 2469 OD1 ASP B 160 1260 2497 2878 -150 482 -591 O ATOM 2470 OD2 ASP B 160 -50.092 -21.220 82.591 1.00 18.40 O ANISOU 2470 OD2 ASP B 160 1380 2653 2955 -349 666 -591 O ATOM 2471 N CYS B 161 -46.420 -19.684 81.531 1.00 14.33 N ANISOU 2471 N CYS B 161 1234 2021 2190 -132 382 -392 N ATOM 2472 CA CYS B 161 -45.178 -19.521 82.273 1.00 13.67 C ANISOU 2472 CA CYS B 161 1290 1919 1983 -131 404 -339 C ATOM 2473 C CYS B 161 -45.487 -18.794 83.541 1.00 14.76 C ANISOU 2473 C CYS B 161 1417 2088 2103 -137 513 -403 C ATOM 2474 O CYS B 161 -46.540 -18.163 83.657 1.00 15.87 O ANISOU 2474 O CYS B 161 1431 2249 2346 -111 558 -494 O ATOM 2475 CB CYS B 161 -44.127 -18.762 81.450 1.00 12.48 C ANISOU 2475 CB CYS B 161 1199 1729 1812 -52 288 -293 C ATOM 2476 SG CYS B 161 -44.698 -17.146 80.752 1.00 12.62 S ANISOU 2476 SG CYS B 161 1120 1726 1946 55 208 -343 S ATOM 2477 N GLY B 162 -44.577 -18.857 84.505 1.00 15.02 N ANISOU 2477 N GLY B 162 1574 2122 2008 -168 552 -367 N ATOM 2478 CA GLY B 162 -44.839 -18.288 85.827 1.00 16.30 C ANISOU 2478 CA GLY B 162 1751 2326 2115 -196 669 -436 C ATOM 2479 C GLY B 162 -43.787 -18.719 86.816 1.00 16.74 C ANISOU 2479 C GLY B 162 1966 2390 2001 -252 684 -369 C ATOM 2480 O GLY B 162 -42.749 -19.294 86.443 1.00 15.75 O ANISOU 2480 O GLY B 162 1925 2229 1828 -247 591 -272 O ATOM 2481 N GLN B 163 -44.036 -18.401 88.074 1.00 18.61 N ANISOU 2481 N GLN B 163 2241 2679 2149 -302 797 -427 N ATOM 2482 CA GLN B 163 -43.089 -18.661 89.153 1.00 19.54 C ANISOU 2482 CA GLN B 163 2519 2818 2086 -358 799 -370 C ATOM 2483 C GLN B 163 -43.671 -19.756 90.005 1.00 21.50 C ANISOU 2483 C GLN B 163 2823 3109 2236 -481 918 -331 C ATOM 2484 O GLN B 163 -44.846 -19.680 90.343 1.00 22.72 O ANISOU 2484 O GLN B 163 2892 3310 2427 -529 1059 -419 O ATOM 2485 CB GLN B 163 -42.877 -17.408 90.002 1.00 20.17 C ANISOU 2485 CB GLN B 163 2628 2928 2107 -337 836 -472 C ATOM 2486 CG GLN B 163 -41.723 -17.577 91.017 1.00 20.48 C ANISOU 2486 CG GLN B 163 2837 2990 1952 -386 792 -411 C ATOM 2487 CD GLN B 163 -41.320 -16.294 91.715 1.00 20.97 C ANISOU 2487 CD GLN B 163 2935 3072 1960 -363 795 -518 C ATOM 2488 OE1 GLN B 163 -41.821 -15.204 91.398 1.00 21.03 O ANISOU 2488 OE1 GLN B 163 2843 3057 2090 -298 826 -637 O ATOM 2489 NE2 GLN B 163 -40.423 -16.420 92.694 1.00 21.30 N ANISOU 2489 NE2 GLN B 163 3122 3150 1821 -417 754 -479 N ATOM 2490 N LEU B 164 -42.880 -20.791 90.310 1.00 22.45 N ANISOU 2490 N LEU B 164 3076 3205 2247 -532 862 -199 N ATOM 2491 CA LEU B 164 -43.302 -21.831 91.259 1.00 24.79 C ANISOU 2491 CA LEU B 164 3466 3529 2421 -663 967 -135 C ATOM 2492 C LEU B 164 -42.903 -21.498 92.709 1.00 27.05 C ANISOU 2492 C LEU B 164 3900 3884 2492 -728 1017 -135 C ATOM 2493 O LEU B 164 -43.677 -21.697 93.631 1.00 29.15 O ANISOU 2493 O LEU B 164 4204 4215 2654 -838 1173 -164 O ATOM 2494 CB LEU B 164 -42.693 -23.173 90.870 1.00 24.48 C ANISOU 2494 CB LEU B 164 3507 3410 2384 -684 872 16 C ATOM 2495 CG LEU B 164 -43.065 -23.681 89.481 1.00 23.46 C ANISOU 2495 CG LEU B 164 3257 3215 2438 -641 827 14 C ATOM 2496 CD1 LEU B 164 -42.274 -24.954 89.123 1.00 23.21 C ANISOU 2496 CD1 LEU B 164 3316 3089 2413 -648 726 148 C ATOM 2497 CD2 LEU B 164 -44.571 -23.905 89.427 1.00 24.22 C ANISOU 2497 CD2 LEU B 164 3237 3348 2617 -719 973 -60 C ATOM 2498 N GLU B 165 -41.682 -21.030 92.909 1.00 27.73 N ANISOU 2498 N GLU B 165 4071 3959 2504 -671 884 -104 N ATOM 2499 CA GLU B 165 -41.156 -20.788 94.264 1.00 30.36 C ANISOU 2499 CA GLU B 165 4563 4357 2614 -735 891 -94 C ATOM 2500 C GLU B 165 -40.234 -19.565 94.242 1.00 29.47 C ANISOU 2500 C GLU B 165 4444 4248 2502 -647 783 -169 C ATOM 2501 O GLU B 165 -39.809 -19.128 93.160 1.00 26.82 O ANISOU 2501 O GLU B 165 4008 3850 2330 -543 686 -184 O ATOM 2502 CB GLU B 165 -40.353 -22.004 94.792 1.00 32.08 C ANISOU 2502 CB GLU B 165 4949 4543 2694 -794 793 91 C ATOM 2503 CG GLU B 165 -41.036 -23.373 94.669 1.00 33.53 C ANISOU 2503 CG GLU B 165 5155 4682 2902 -878 863 199 C ATOM 2504 CD GLU B 165 -42.157 -23.607 95.691 1.00 36.90 C ANISOU 2504 CD GLU B 165 5639 5190 3188 -1029 1071 173 C ATOM 2505 OE1 GLU B 165 -42.377 -22.743 96.589 1.00 38.98 O ANISOU 2505 OE1 GLU B 165 5942 5555 3312 -1070 1167 67 O ATOM 2506 OE2 GLU B 165 -42.819 -24.682 95.602 1.00 38.34 O ANISOU 2506 OE2 GLU B 165 5831 5334 3401 -1116 1150 252 O ATOM 2507 OXT GLU B 165 -39.909 -19.022 95.317 1.00 30.89 O ANISOU 2507 OXT GLU B 165 4728 4493 2512 -692 796 -217 O TER 2508 GLU B 165 ATOM 2509 N PRO C 1 -41.355 7.072 45.370 1.00 43.16 N ANISOU 2509 N PRO C 1 4147 5755 6494 -687 868 -1253 N ATOM 2510 CA PRO C 1 -40.498 6.213 46.197 1.00 42.13 C ANISOU 2510 CA PRO C 1 4255 5494 6259 -800 1080 -1054 C ATOM 2511 C PRO C 1 -40.779 4.717 46.014 1.00 43.43 C ANISOU 2511 C PRO C 1 4346 5535 6622 -954 1232 -1153 C ATOM 2512 O PRO C 1 -41.709 4.339 45.302 1.00 44.73 O ANISOU 2512 O PRO C 1 4242 5719 7034 -994 1188 -1407 O ATOM 2513 CB PRO C 1 -40.834 6.654 47.638 1.00 42.71 C ANISOU 2513 CB PRO C 1 4405 5510 6310 -851 1333 -983 C ATOM 2514 CG PRO C 1 -42.122 7.432 47.536 1.00 44.45 C ANISOU 2514 CG PRO C 1 4349 5808 6729 -821 1314 -1207 C ATOM 2515 CD PRO C 1 -42.103 8.057 46.174 1.00 43.80 C ANISOU 2515 CD PRO C 1 4151 5862 6629 -659 958 -1300 C ATOM 2516 N ILE C 2 -39.963 3.889 46.661 1.00 42.84 N ANISOU 2516 N ILE C 2 4509 5325 6441 -1026 1399 -964 N ATOM 2517 CA ILE C 2 -40.235 2.461 46.820 1.00 44.37 C ANISOU 2517 CA ILE C 2 4690 5340 6827 -1189 1628 -1015 C ATOM 2518 C ILE C 2 -40.746 2.279 48.242 1.00 45.57 C ANISOU 2518 C ILE C 2 4938 5353 7023 -1306 1996 -940 C ATOM 2519 O ILE C 2 -40.077 2.671 49.172 1.00 45.01 O ANISOU 2519 O ILE C 2 5128 5270 6703 -1246 2060 -720 O ATOM 2520 CB ILE C 2 -38.947 1.617 46.549 1.00 43.13 C ANISOU 2520 CB ILE C 2 4764 5108 6515 -1162 1563 -845 C ATOM 2521 CG1 ILE C 2 -38.566 1.719 45.072 1.00 42.03 C ANISOU 2521 CG1 ILE C 2 4513 5105 6351 -1062 1242 -952 C ATOM 2522 CG2 ILE C 2 -39.133 0.151 46.905 1.00 45.15 C ANISOU 2522 CG2 ILE C 2 5070 5132 6949 -1322 1835 -851 C ATOM 2523 CD1 ILE C 2 -37.195 1.193 44.753 1.00 40.46 C ANISOU 2523 CD1 ILE C 2 4525 4876 5970 -1001 1144 -790 C ATOM 2524 N VAL C 3 -41.952 1.741 48.403 1.00 48.45 N ANISOU 2524 N VAL C 3 5084 5619 7704 -1466 2239 -1142 N ATOM 2525 CA VAL C 3 -42.487 1.380 49.725 1.00 50.44 C ANISOU 2525 CA VAL C 3 5443 5703 8018 -1605 2663 -1073 C ATOM 2526 C VAL C 3 -42.785 -0.114 49.800 1.00 52.68 C ANISOU 2526 C VAL C 3 5732 5738 8544 -1799 2956 -1115 C ATOM 2527 O VAL C 3 -42.733 -0.808 48.784 1.00 52.33 O ANISOU 2527 O VAL C 3 5545 5671 8665 -1832 2813 -1255 O ATOM 2528 CB VAL C 3 -43.770 2.159 50.049 1.00 52.16 C ANISOU 2528 CB VAL C 3 5387 5994 8437 -1651 2785 -1285 C ATOM 2529 CG1 VAL C 3 -43.579 3.620 49.656 1.00 49.79 C ANISOU 2529 CG1 VAL C 3 5023 5929 7964 -1450 2440 -1298 C ATOM 2530 CG2 VAL C 3 -44.990 1.538 49.361 1.00 54.33 C ANISOU 2530 CG2 VAL C 3 5260 6221 9162 -1803 2866 -1635 C ATOM 2531 N VAL C 11 -42.725 -2.280 46.647 1.00 38.78 N ANISOU 2531 N VAL C 11 3512 3913 7308 -1898 2518 -1606 N ATOM 2532 CA VAL C 11 -43.229 -1.717 45.402 1.00 38.49 C ANISOU 2532 CA VAL C 11 3142 4100 7381 -1807 2168 -1899 C ATOM 2533 C VAL C 11 -42.858 -0.224 45.163 1.00 35.83 C ANISOU 2533 C VAL C 11 2844 4026 6741 -1581 1850 -1805 C ATOM 2534 O VAL C 11 -42.811 0.585 46.093 1.00 35.01 O ANISOU 2534 O VAL C 11 2870 3950 6479 -1543 1954 -1638 O ATOM 2535 CB VAL C 11 -44.765 -1.931 45.293 1.00 41.90 C ANISOU 2535 CB VAL C 11 3161 4495 8262 -1967 2321 -2276 C ATOM 2536 CG1 VAL C 11 -45.115 -3.386 45.605 1.00 44.84 C ANISOU 2536 CG1 VAL C 11 3509 4565 8960 -2216 2689 -2359 C ATOM 2537 CG2 VAL C 11 -45.533 -0.997 46.215 1.00 42.60 C ANISOU 2537 CG2 VAL C 11 3170 4634 8379 -1981 2496 -2278 C ATOM 2538 N HIS C 12 -42.593 0.118 43.901 1.00 34.67 N ANISOU 2538 N HIS C 12 2599 4060 6512 -1430 1476 -1916 N ATOM 2539 CA HIS C 12 -42.368 1.500 43.497 1.00 32.81 C ANISOU 2539 CA HIS C 12 2379 4049 6036 -1220 1180 -1861 C ATOM 2540 C HIS C 12 -43.679 2.250 43.288 1.00 34.53 C ANISOU 2540 C HIS C 12 2269 4386 6463 -1182 1098 -2137 C ATOM 2541 O HIS C 12 -44.653 1.685 42.816 1.00 37.06 O ANISOU 2541 O HIS C 12 2284 4693 7104 -1263 1102 -2456 O ATOM 2542 CB HIS C 12 -41.551 1.589 42.202 1.00 31.35 C ANISOU 2542 CB HIS C 12 2259 3999 5651 -1058 836 -1852 C ATOM 2543 CG HIS C 12 -41.317 2.996 41.755 1.00 29.81 C ANISOU 2543 CG HIS C 12 2111 4000 5215 -847 567 -1778 C ATOM 2544 ND1 HIS C 12 -42.132 3.634 40.846 1.00 31.03 N ANISOU 2544 ND1 HIS C 12 2042 4314 5432 -711 312 -2011 N ATOM 2545 CD2 HIS C 12 -40.401 3.915 42.147 1.00 27.62 C ANISOU 2545 CD2 HIS C 12 2078 3767 4648 -745 526 -1506 C ATOM 2546 CE1 HIS C 12 -41.715 4.878 40.679 1.00 29.54 C ANISOU 2546 CE1 HIS C 12 1987 4242 4993 -533 139 -1857 C ATOM 2547 NE2 HIS C 12 -40.662 5.073 41.454 1.00 27.41 N ANISOU 2547 NE2 HIS C 12 1989 3902 4522 -565 273 -1559 N ATOM 2548 N GLN C 13 -43.688 3.528 43.640 1.00 33.36 N ANISOU 2548 N GLN C 13 2175 4351 6149 -1051 1015 -2032 N ATOM 2549 CA GLN C 13 -44.847 4.399 43.438 1.00 34.99 C ANISOU 2549 CA GLN C 13 2091 4681 6522 -966 898 -2276 C ATOM 2550 C GLN C 13 -44.340 5.733 42.917 1.00 33.06 C ANISOU 2550 C GLN C 13 1975 4602 5982 -717 584 -2145 C ATOM 2551 O GLN C 13 -43.260 6.159 43.304 1.00 30.63 O ANISOU 2551 O GLN C 13 1969 4280 5388 -673 597 -1847 O ATOM 2552 CB GLN C 13 -45.601 4.616 44.762 1.00 36.31 C ANISOU 2552 CB GLN C 13 2186 4756 6852 -1097 1241 -2289 C ATOM 2553 CG GLN C 13 -46.414 3.433 45.214 1.00 39.18 C ANISOU 2553 CG GLN C 13 2358 4949 7580 -1346 1583 -2480 C ATOM 2554 CD GLN C 13 -47.404 3.770 46.326 1.00 41.25 C ANISOU 2554 CD GLN C 13 2474 5152 8046 -1459 1910 -2571 C ATOM 2555 OE1 GLN C 13 -47.272 4.784 47.006 1.00 40.19 O ANISOU 2555 OE1 GLN C 13 2468 5078 7723 -1365 1931 -2422 O ATOM 2556 NE2 GLN C 13 -48.391 2.911 46.515 1.00 44.40 N ANISOU 2556 NE2 GLN C 13 2600 5425 8844 -1667 2186 -2831 N ATOM 2557 N ALA C 14 -45.110 6.406 42.061 1.00 34.42 N ANISOU 2557 N ALA C 14 1925 4921 6229 -547 305 -2371 N ATOM 2558 CA ALA C 14 -44.712 7.748 41.614 1.00 33.08 C ANISOU 2558 CA ALA C 14 1901 4876 5789 -304 38 -2233 C ATOM 2559 C ALA C 14 -44.660 8.680 42.821 1.00 32.21 C ANISOU 2559 C ALA C 14 1901 4721 5615 -316 219 -2062 C ATOM 2560 O ALA C 14 -45.418 8.514 43.782 1.00 33.45 O ANISOU 2560 O ALA C 14 1910 4809 5988 -452 478 -2164 O ATOM 2561 CB ALA C 14 -45.657 8.289 40.549 1.00 35.19 C ANISOU 2561 CB ALA C 14 1923 5295 6152 -92 -291 -2512 C ATOM 2562 N ILE C 15 -43.725 9.627 42.782 1.00 30.22 N ANISOU 2562 N ILE C 15 1917 4497 5067 -184 106 -1807 N ATOM 2563 CA ILE C 15 -43.571 10.607 43.854 1.00 29.43 C ANISOU 2563 CA ILE C 15 1938 4361 4883 -173 238 -1656 C ATOM 2564 C ILE C 15 -44.893 11.354 44.001 1.00 31.56 C ANISOU 2564 C ILE C 15 1937 4684 5370 -86 200 -1891 C ATOM 2565 O ILE C 15 -45.522 11.735 43.008 1.00 33.03 O ANISOU 2565 O ILE C 15 1957 4968 5623 88 -71 -2071 O ATOM 2566 CB ILE C 15 -42.406 11.587 43.545 1.00 27.41 C ANISOU 2566 CB ILE C 15 1970 4126 4317 -28 77 -1397 C ATOM 2567 CG1 ILE C 15 -42.108 12.471 44.745 1.00 26.54 C ANISOU 2567 CG1 ILE C 15 1996 3962 4125 -44 230 -1252 C ATOM 2568 CG2 ILE C 15 -42.707 12.413 42.265 1.00 28.28 C ANISOU 2568 CG2 ILE C 15 2037 4339 4367 212 -250 -1472 C ATOM 2569 CD1 ILE C 15 -41.372 13.738 44.397 1.00 25.38 C ANISOU 2569 CD1 ILE C 15 2040 3829 3773 119 58 -1087 C ATOM 2570 N SER C 16 -45.340 11.525 45.237 1.00 32.06 N ANISOU 2570 N SER C 16 1953 4685 5542 -195 471 -1908 N ATOM 2571 CA SER C 16 -46.625 12.160 45.503 1.00 34.27 C ANISOU 2571 CA SER C 16 1948 5006 6064 -133 484 -2156 C ATOM 2572 C SER C 16 -46.585 13.631 45.063 1.00 33.86 C ANISOU 2572 C SER C 16 1959 5024 5881 128 208 -2110 C ATOM 2573 O SER C 16 -45.646 14.333 45.406 1.00 31.85 O ANISOU 2573 O SER C 16 1985 4732 5381 171 208 -1859 O ATOM 2574 CB SER C 16 -46.929 12.031 46.995 1.00 34.86 C ANISOU 2574 CB SER C 16 2027 4990 6227 -312 879 -2139 C ATOM 2575 OG SER C 16 -48.087 12.736 47.344 1.00 37.05 O ANISOU 2575 OG SER C 16 2041 5305 6729 -251 920 -2370 O ATOM 2576 N PRO C 17 -47.590 14.103 44.290 1.00 36.05 N ANISOU 2576 N PRO C 17 1978 5392 6328 312 -36 -2361 N ATOM 2577 CA PRO C 17 -47.591 15.514 43.855 1.00 36.11 C ANISOU 2577 CA PRO C 17 2072 5436 6209 586 -297 -2306 C ATOM 2578 C PRO C 17 -47.757 16.521 44.993 1.00 36.07 C ANISOU 2578 C PRO C 17 2105 5374 6226 594 -128 -2259 C ATOM 2579 O PRO C 17 -47.231 17.631 44.904 1.00 35.05 O ANISOU 2579 O PRO C 17 2187 5215 5914 752 -254 -2089 O ATOM 2580 CB PRO C 17 -48.783 15.624 42.901 1.00 39.11 C ANISOU 2580 CB PRO C 17 2130 5925 6802 785 -582 -2632 C ATOM 2581 CG PRO C 17 -49.327 14.242 42.735 1.00 40.53 C ANISOU 2581 CG PRO C 17 2043 6133 7223 601 -487 -2873 C ATOM 2582 CD PRO C 17 -48.783 13.377 43.823 1.00 38.95 C ANISOU 2582 CD PRO C 17 1955 5818 7024 287 -82 -2724 C ATOM 2583 N ARG C 18 -48.480 16.138 46.040 1.00 37.35 N ANISOU 2583 N ARG C 18 2070 5510 6610 424 171 -2415 N ATOM 2584 CA ARG C 18 -48.638 16.995 47.208 1.00 37.57 C ANISOU 2584 CA ARG C 18 2139 5488 6646 416 368 -2388 C ATOM 2585 C ARG C 18 -47.434 16.969 48.176 1.00 35.00 C ANISOU 2585 C ARG C 18 2166 5079 6051 274 589 -2087 C ATOM 2586 O ARG C 18 -47.208 17.920 48.920 1.00 34.65 O ANISOU 2586 O ARG C 18 2251 4998 5915 326 652 -2009 O ATOM 2587 CB ARG C 18 -49.951 16.667 47.903 1.00 40.50 C ANISOU 2587 CB ARG C 18 2154 5872 7362 310 611 -2696 C ATOM 2588 CG ARG C 18 -51.128 16.971 46.981 1.00 43.34 C ANISOU 2588 CG ARG C 18 2146 6325 7995 508 335 -3024 C ATOM 2589 CD ARG C 18 -52.437 16.982 47.684 1.00 46.54 C ANISOU 2589 CD ARG C 18 2173 6744 8766 446 554 -3354 C ATOM 2590 NE ARG C 18 -53.031 15.656 47.766 1.00 48.31 N ANISOU 2590 NE ARG C 18 2134 6960 9261 206 784 -3563 N ATOM 2591 CZ ARG C 18 -54.294 15.419 48.098 1.00 51.73 C ANISOU 2591 CZ ARG C 18 2149 7411 10095 131 961 -3925 C ATOM 2592 NH1 ARG C 18 -55.130 16.420 48.383 1.00 53.84 N ANISOU 2592 NH1 ARG C 18 2198 7721 10537 293 920 -4130 N ATOM 2593 NH2 ARG C 18 -54.726 14.169 48.140 1.00 53.34 N ANISOU 2593 NH2 ARG C 18 2139 7576 10550 -112 1193 -4096 N ATOM 2594 N THR C 19 -46.664 15.890 48.150 1.00 33.45 N ANISOU 2594 N THR C 19 2119 4854 5737 111 686 -1941 N ATOM 2595 CA THR C 19 -45.380 15.850 48.831 1.00 31.09 C ANISOU 2595 CA THR C 19 2161 4491 5158 27 802 -1658 C ATOM 2596 C THR C 19 -44.375 16.736 48.083 1.00 29.21 C ANISOU 2596 C THR C 19 2141 4255 4699 191 523 -1470 C ATOM 2597 O THR C 19 -43.621 17.489 48.717 1.00 28.01 O ANISOU 2597 O THR C 19 2199 4058 4383 211 558 -1319 O ATOM 2598 CB THR C 19 -44.869 14.419 48.937 1.00 30.34 C ANISOU 2598 CB THR C 19 2154 4355 5018 -164 961 -1567 C ATOM 2599 OG1 THR C 19 -45.774 13.671 49.760 1.00 32.41 O ANISOU 2599 OG1 THR C 19 2252 4577 5483 -331 1282 -1718 O ATOM 2600 CG2 THR C 19 -43.484 14.377 49.540 1.00 28.09 C ANISOU 2600 CG2 THR C 19 2213 4019 4441 -210 1022 -1291 C ATOM 2601 N LEU C 20 -44.390 16.638 46.748 1.00 29.25 N ANISOU 2601 N LEU C 20 2095 4309 4707 305 262 -1495 N ATOM 2602 CA LEU C 20 -43.699 17.578 45.835 1.00 28.34 C ANISOU 2602 CA LEU C 20 2160 4190 4417 492 0 -1349 C ATOM 2603 C LEU C 20 -44.021 19.032 46.126 1.00 29.09 C ANISOU 2603 C LEU C 20 2270 4247 4534 655 -64 -1365 C ATOM 2604 O LEU C 20 -43.136 19.876 46.216 1.00 27.87 O ANISOU 2604 O LEU C 20 2345 4022 4220 705 -97 -1185 O ATOM 2605 CB LEU C 20 -44.100 17.326 44.371 1.00 29.42 C ANISOU 2605 CB LEU C 20 2193 4403 4582 637 -270 -1445 C ATOM 2606 CG LEU C 20 -43.053 16.862 43.374 1.00 28.06 C ANISOU 2606 CG LEU C 20 2220 4240 4199 646 -395 -1275 C ATOM 2607 CD1 LEU C 20 -43.642 16.866 41.922 1.00 29.78 C ANISOU 2607 CD1 LEU C 20 2344 4549 4421 855 -697 -1403 C ATOM 2608 CD2 LEU C 20 -41.827 17.746 43.474 1.00 26.32 C ANISOU 2608 CD2 LEU C 20 2302 3940 3759 679 -392 -1012 C ATOM 2609 N ASN C 21 -45.305 19.325 46.239 1.00 31.38 N ANISOU 2609 N ASN C 21 2299 4575 5047 740 -83 -1603 N ATOM 2610 CA ASN C 21 -45.748 20.680 46.498 1.00 32.53 C ANISOU 2610 CA ASN C 21 2430 4679 5248 915 -152 -1653 C ATOM 2611 C ASN C 21 -45.385 21.176 47.897 1.00 31.69 C ANISOU 2611 C ASN C 21 2435 4502 5101 806 93 -1591 C ATOM 2612 O ASN C 21 -45.055 22.354 48.072 1.00 31.52 O ANISOU 2612 O ASN C 21 2553 4403 5017 922 34 -1515 O ATOM 2613 CB ASN C 21 -47.236 20.789 46.237 1.00 35.55 C ANISOU 2613 CB ASN C 21 2470 5131 5904 1047 -247 -1958 C ATOM 2614 CG ASN C 21 -47.525 21.129 44.800 1.00 36.93 C ANISOU 2614 CG ASN C 21 2623 5351 6058 1307 -608 -1996 C ATOM 2615 OD1 ASN C 21 -47.375 22.286 44.399 1.00 37.56 O ANISOU 2615 OD1 ASN C 21 2853 5368 6047 1528 -785 -1902 O ATOM 2616 ND2 ASN C 21 -47.922 20.131 44.003 1.00 37.84 N ANISOU 2616 ND2 ASN C 21 2570 5564 6243 1295 -721 -2134 N ATOM 2617 N ALA C 22 -45.417 20.277 48.878 1.00 31.28 N ANISOU 2617 N ALA C 22 2344 4467 5072 592 369 -1623 N ATOM 2618 CA ALA C 22 -44.939 20.606 50.223 1.00 30.58 C ANISOU 2618 CA ALA C 22 2411 4328 4880 493 597 -1550 C ATOM 2619 C ALA C 22 -43.476 21.009 50.156 1.00 28.23 C ANISOU 2619 C ALA C 22 2421 3968 4335 494 513 -1303 C ATOM 2620 O ALA C 22 -43.090 22.027 50.721 1.00 28.07 O ANISOU 2620 O ALA C 22 2524 3888 4254 549 520 -1266 O ATOM 2621 CB ALA C 22 -45.123 19.434 51.190 1.00 30.83 C ANISOU 2621 CB ALA C 22 2411 4378 4925 276 910 -1585 C ATOM 2622 N TRP C 23 -42.666 20.221 49.456 1.00 26.64 N ANISOU 2622 N TRP C 23 2327 3778 4014 433 437 -1158 N ATOM 2623 CA TRP C 23 -41.242 20.543 49.272 1.00 24.71 C ANISOU 2623 CA TRP C 23 2341 3479 3568 427 359 -945 C ATOM 2624 C TRP C 23 -41.043 21.917 48.596 1.00 25.08 C ANISOU 2624 C TRP C 23 2467 3451 3611 605 170 -895 C ATOM 2625 O TRP C 23 -40.229 22.705 49.041 1.00 24.38 O ANISOU 2625 O TRP C 23 2539 3282 3442 604 188 -808 O ATOM 2626 CB TRP C 23 -40.528 19.421 48.492 1.00 23.26 C ANISOU 2626 CB TRP C 23 2223 3326 3289 346 308 -829 C ATOM 2627 CG TRP C 23 -39.161 19.777 48.009 1.00 21.62 C ANISOU 2627 CG TRP C 23 2230 3067 2917 360 208 -640 C ATOM 2628 CD1 TRP C 23 -38.729 19.825 46.710 1.00 21.20 C ANISOU 2628 CD1 TRP C 23 2239 3010 2807 436 42 -549 C ATOM 2629 CD2 TRP C 23 -38.041 20.157 48.814 1.00 20.56 C ANISOU 2629 CD2 TRP C 23 2270 2878 2664 298 276 -538 C ATOM 2630 NE1 TRP C 23 -37.408 20.203 46.662 1.00 19.92 N ANISOU 2630 NE1 TRP C 23 2268 2782 2518 405 37 -393 N ATOM 2631 CE2 TRP C 23 -36.957 20.398 47.939 1.00 19.53 C ANISOU 2631 CE2 TRP C 23 2273 2704 2444 319 164 -397 C ATOM 2632 CE3 TRP C 23 -37.844 20.311 50.189 1.00 20.61 C ANISOU 2632 CE3 TRP C 23 2331 2872 2626 234 420 -570 C ATOM 2633 CZ2 TRP C 23 -35.709 20.806 48.399 1.00 18.68 C ANISOU 2633 CZ2 TRP C 23 2311 2536 2249 267 190 -310 C ATOM 2634 CZ3 TRP C 23 -36.599 20.707 50.643 1.00 19.72 C ANISOU 2634 CZ3 TRP C 23 2380 2714 2398 203 410 -485 C ATOM 2635 CH2 TRP C 23 -35.554 20.955 49.756 1.00 18.80 C ANISOU 2635 CH2 TRP C 23 2355 2550 2238 214 295 -368 C ATOM 2636 N VAL C 24 -41.804 22.195 47.541 1.00 26.55 N ANISOU 2636 N VAL C 24 2544 3654 3888 764 -7 -961 N ATOM 2637 CA VAL C 24 -41.745 23.492 46.845 1.00 27.62 C ANISOU 2637 CA VAL C 24 2780 3697 4017 964 -181 -902 C ATOM 2638 C VAL C 24 -41.979 24.665 47.809 1.00 28.72 C ANISOU 2638 C VAL C 24 2927 3746 4237 1015 -105 -970 C ATOM 2639 O VAL C 24 -41.200 25.614 47.842 1.00 28.33 O ANISOU 2639 O VAL C 24 3062 3572 4127 1050 -123 -854 O ATOM 2640 CB VAL C 24 -42.768 23.551 45.684 1.00 29.46 C ANISOU 2640 CB VAL C 24 2876 3982 4335 1169 -400 -1004 C ATOM 2641 CG1 VAL C 24 -42.961 24.974 45.195 1.00 31.01 C ANISOU 2641 CG1 VAL C 24 3175 4062 4545 1410 -556 -966 C ATOM 2642 CG2 VAL C 24 -42.312 22.670 44.529 1.00 28.72 C ANISOU 2642 CG2 VAL C 24 2847 3951 4113 1161 -516 -910 C ATOM 2643 N LYS C 25 -43.060 24.558 48.576 1.00 30.38 N ANISOU 2643 N LYS C 25 2925 4015 4600 1009 -4 -1174 N ATOM 2644 CA LYS C 25 -43.419 25.473 49.656 1.00 31.72 C ANISOU 2644 CA LYS C 25 3066 4128 4855 1038 107 -1287 C ATOM 2645 C LYS C 25 -42.308 25.722 50.683 1.00 30.65 C ANISOU 2645 C LYS C 25 3130 3934 4580 903 252 -1191 C ATOM 2646 O LYS C 25 -42.091 26.847 51.107 1.00 31.08 O ANISOU 2646 O LYS C 25 3268 3883 4656 971 249 -1207 O ATOM 2647 CB LYS C 25 -44.628 24.909 50.413 1.00 33.23 C ANISOU 2647 CB LYS C 25 2996 4422 5208 983 271 -1518 C ATOM 2648 CG LYS C 25 -45.970 25.455 49.997 1.00 35.82 C ANISOU 2648 CG LYS C 25 3076 4765 5765 1179 154 -1730 C ATOM 2649 CD LYS C 25 -46.374 26.673 50.829 1.00 37.31 C ANISOU 2649 CD LYS C 25 3246 4876 6053 1281 217 -1849 C ATOM 2650 CE LYS C 25 -47.839 27.004 50.639 1.00 40.14 C ANISOU 2650 CE LYS C 25 3297 5276 6677 1454 148 -2115 C ATOM 2651 NZ LYS C 25 -48.283 28.078 51.567 1.00 41.73 N ANISOU 2651 NZ LYS C 25 3456 5408 6990 1537 250 -2260 N ATOM 2652 N VAL C 26 -41.662 24.655 51.122 1.00 29.58 N ANISOU 2652 N VAL C 26 3058 3866 4313 724 373 -1118 N ATOM 2653 CA VAL C 26 -40.550 24.745 52.061 1.00 28.90 C ANISOU 2653 CA VAL C 26 3155 3749 4074 614 472 -1043 C ATOM 2654 C VAL C 26 -39.398 25.603 51.489 1.00 28.51 C ANISOU 2654 C VAL C 26 3283 3577 3970 655 338 -902 C ATOM 2655 O VAL C 26 -38.857 26.463 52.190 1.00 28.56 O ANISOU 2655 O VAL C 26 3384 3503 3963 653 367 -929 O ATOM 2656 CB VAL C 26 -40.044 23.313 52.459 1.00 27.67 C ANISOU 2656 CB VAL C 26 3050 3683 3778 446 592 -969 C ATOM 2657 CG1 VAL C 26 -38.758 23.370 53.274 1.00 26.63 C ANISOU 2657 CG1 VAL C 26 3118 3529 3471 370 631 -889 C ATOM 2658 CG2 VAL C 26 -41.129 22.550 53.219 1.00 28.83 C ANISOU 2658 CG2 VAL C 26 3055 3912 3987 381 795 -1105 C ATOM 2659 N VAL C 27 -39.046 25.393 50.219 1.00 28.56 N ANISOU 2659 N VAL C 27 3332 3563 3954 689 205 -769 N ATOM 2660 CA VAL C 27 -37.953 26.159 49.589 1.00 28.76 C ANISOU 2660 CA VAL C 27 3531 3456 3938 711 123 -625 C ATOM 2661 C VAL C 27 -38.332 27.634 49.369 1.00 31.14 C ANISOU 2661 C VAL C 27 3868 3601 4360 871 59 -655 C ATOM 2662 O VAL C 27 -37.550 28.521 49.671 1.00 31.12 O ANISOU 2662 O VAL C 27 3985 3462 4377 849 86 -627 O ATOM 2663 CB VAL C 27 -37.485 25.505 48.266 1.00 27.90 C ANISOU 2663 CB VAL C 27 3481 3369 3747 711 29 -471 C ATOM 2664 CG1 VAL C 27 -36.415 26.356 47.578 1.00 27.90 C ANISOU 2664 CG1 VAL C 27 3666 3213 3720 730 -6 -322 C ATOM 2665 CG2 VAL C 27 -36.950 24.111 48.538 1.00 26.25 C ANISOU 2665 CG2 VAL C 27 3258 3282 3433 552 98 -439 C ATOM 2666 N GLU C 28 -39.537 27.885 48.870 1.00 33.76 N ANISOU 2666 N GLU C 28 4089 3946 4792 1036 -28 -729 N ATOM 2667 CA GLU C 28 -40.008 29.252 48.626 1.00 36.80 C ANISOU 2667 CA GLU C 28 4511 4172 5297 1224 -106 -758 C ATOM 2668 C GLU C 28 -39.987 30.114 49.886 1.00 38.56 C ANISOU 2668 C GLU C 28 4727 4314 5607 1196 4 -891 C ATOM 2669 O GLU C 28 -39.642 31.294 49.820 1.00 39.70 O ANISOU 2669 O GLU C 28 4993 4266 5822 1270 -14 -861 O ATOM 2670 CB GLU C 28 -41.436 29.251 48.068 1.00 38.78 C ANISOU 2670 CB GLU C 28 4593 4487 5655 1423 -234 -872 C ATOM 2671 CG GLU C 28 -41.561 28.757 46.621 1.00 39.17 C ANISOU 2671 CG GLU C 28 4677 4582 5622 1534 -407 -760 C ATOM 2672 CD GLU C 28 -43.017 28.751 46.124 1.00 41.58 C ANISOU 2672 CD GLU C 28 4778 4968 6051 1752 -570 -927 C ATOM 2673 OE1 GLU C 28 -43.942 28.868 46.968 1.00 42.92 O ANISOU 2673 OE1 GLU C 28 4734 5188 6385 1767 -508 -1141 O ATOM 2674 OE2 GLU C 28 -43.234 28.634 44.892 1.00 42.57 O ANISOU 2674 OE2 GLU C 28 4952 5112 6107 1917 -762 -859 O ATOM 2675 N GLU C 29 -40.364 29.515 51.018 1.00 39.44 N ANISOU 2675 N GLU C 29 4711 4562 5710 1093 133 -1041 N ATOM 2676 CA GLU C 29 -40.414 30.202 52.312 1.00 41.19 C ANISOU 2676 CA GLU C 29 4925 4746 5980 1071 249 -1198 C ATOM 2677 C GLU C 29 -39.090 30.258 53.069 1.00 40.39 C ANISOU 2677 C GLU C 29 4971 4612 5763 919 320 -1163 C ATOM 2678 O GLU C 29 -38.797 31.254 53.698 1.00 41.40 O ANISOU 2678 O GLU C 29 5154 4623 5951 938 345 -1253 O ATOM 2679 CB GLU C 29 -41.439 29.539 53.226 1.00 42.47 C ANISOU 2679 CB GLU C 29 4906 5069 6160 1037 385 -1378 C ATOM 2680 CG GLU C 29 -42.873 29.681 52.746 1.00 44.75 C ANISOU 2680 CG GLU C 29 4986 5387 6627 1198 328 -1506 C ATOM 2681 CD GLU C 29 -43.881 29.162 53.756 1.00 46.47 C ANISOU 2681 CD GLU C 29 5011 5739 6905 1146 519 -1714 C ATOM 2682 OE1 GLU C 29 -43.458 28.789 54.882 1.00 46.56 O ANISOU 2682 OE1 GLU C 29 5096 5807 6785 1004 701 -1741 O ATOM 2683 OE2 GLU C 29 -45.092 29.136 53.425 1.00 48.58 O ANISOU 2683 OE2 GLU C 29 5056 6053 7350 1257 490 -1859 O ATOM 2684 N LYS C 30 -38.323 29.178 53.055 1.00 39.06 N ANISOU 2684 N LYS C 30 4850 4548 5443 778 344 -1060 N ATOM 2685 CA LYS C 30 -37.059 29.128 53.783 1.00 38.68 C ANISOU 2685 CA LYS C 30 4918 4493 5285 653 382 -1053 C ATOM 2686 C LYS C 30 -35.826 29.261 52.875 1.00 38.12 C ANISOU 2686 C LYS C 30 4958 4316 5207 598 303 -891 C ATOM 2687 O LYS C 30 -34.701 29.175 53.350 1.00 37.58 O ANISOU 2687 O LYS C 30 4956 4244 5076 496 313 -898 O ATOM 2688 CB LYS C 30 -36.962 27.827 54.589 1.00 37.98 C ANISOU 2688 CB LYS C 30 4822 4587 5021 545 476 -1067 C ATOM 2689 CG LYS C 30 -37.746 27.838 55.905 1.00 39.56 C ANISOU 2689 CG LYS C 30 4979 4869 5181 561 615 -1245 C ATOM 2690 CD LYS C 30 -39.154 27.267 55.768 1.00 40.42 C ANISOU 2690 CD LYS C 30 4931 5065 5361 595 706 -1296 C ATOM 2691 CE LYS C 30 -40.092 27.801 56.874 1.00 42.54 C ANISOU 2691 CE LYS C 30 5131 5358 5673 649 852 -1504 C ATOM 2692 NZ LYS C 30 -39.557 27.583 58.264 1.00 42.77 N ANISOU 2692 NZ LYS C 30 5298 5456 5494 586 977 -1570 N ATOM 2693 N ALA C 31 -36.026 29.488 51.582 1.00 38.70 N ANISOU 2693 N ALA C 31 5053 4304 5343 677 228 -759 N ATOM 2694 CA ALA C 31 -34.917 29.503 50.641 1.00 38.36 C ANISOU 2694 CA ALA C 31 5125 4170 5279 619 195 -593 C ATOM 2695 C ALA C 31 -33.992 28.339 50.999 1.00 37.25 C ANISOU 2695 C ALA C 31 4983 4168 5000 467 223 -565 C ATOM 2696 O ALA C 31 -34.450 27.190 51.117 1.00 36.98 O ANISOU 2696 O ALA C 31 4884 4300 4866 444 232 -561 O ATOM 2697 CB ALA C 31 -34.200 30.843 50.682 1.00 39.56 C ANISOU 2697 CB ALA C 31 5374 4092 5562 617 218 -606 C ATOM 2698 N PHE C 32 -32.706 28.611 51.191 1.00 37.32 N ANISOU 2698 N PHE C 32 5054 4103 5021 367 239 -563 N ATOM 2699 CA PHE C 32 -31.760 27.568 51.604 1.00 35.85 C ANISOU 2699 CA PHE C 32 4863 4043 4713 250 241 -560 C ATOM 2700 C PHE C 32 -31.144 27.883 52.977 1.00 36.16 C ANISOU 2700 C PHE C 32 4899 4098 4739 203 247 -736 C ATOM 2701 O PHE C 32 -29.959 27.651 53.213 1.00 36.24 O ANISOU 2701 O PHE C 32 4919 4121 4729 121 220 -765 O ATOM 2702 CB PHE C 32 -30.723 27.356 50.505 1.00 35.29 C ANISOU 2702 CB PHE C 32 4841 3911 4655 183 234 -417 C ATOM 2703 CG PHE C 32 -31.301 26.681 49.305 1.00 34.94 C ANISOU 2703 CG PHE C 32 4809 3918 4547 235 210 -264 C ATOM 2704 CD1 PHE C 32 -31.359 25.299 49.239 1.00 33.85 C ANISOU 2704 CD1 PHE C 32 4629 3946 4284 197 194 -228 C ATOM 2705 CD2 PHE C 32 -31.857 27.416 48.277 1.00 36.03 C ANISOU 2705 CD2 PHE C 32 5007 3936 4744 342 193 -171 C ATOM 2706 CE1 PHE C 32 -31.934 24.653 48.146 1.00 33.53 C ANISOU 2706 CE1 PHE C 32 4583 3961 4194 249 158 -124 C ATOM 2707 CE2 PHE C 32 -32.426 26.783 47.190 1.00 35.69 C ANISOU 2707 CE2 PHE C 32 4976 3962 4622 416 140 -60 C ATOM 2708 CZ PHE C 32 -32.460 25.398 47.117 1.00 34.46 C ANISOU 2708 CZ PHE C 32 4754 3982 4356 362 120 -49 C ATOM 2709 N SER C 33 -31.983 28.399 53.878 1.00 36.22 N ANISOU 2709 N SER C 33 4886 4117 4757 270 275 -874 N ATOM 2710 CA SER C 33 -31.642 28.527 55.288 1.00 36.28 C ANISOU 2710 CA SER C 33 4906 4187 4688 258 277 -1058 C ATOM 2711 C SER C 33 -31.575 27.100 55.873 1.00 34.41 C ANISOU 2711 C SER C 33 4696 4150 4227 233 289 -1025 C ATOM 2712 O SER C 33 -32.007 26.145 55.221 1.00 33.12 O ANISOU 2712 O SER C 33 4517 4055 4012 221 314 -884 O ATOM 2713 CB SER C 33 -32.677 29.405 56.030 1.00 37.94 C ANISOU 2713 CB SER C 33 5095 4363 4955 348 328 -1211 C ATOM 2714 OG SER C 33 -33.829 28.665 56.434 1.00 38.12 O ANISOU 2714 OG SER C 33 5087 4529 4866 394 407 -1214 O ATOM 2715 N PRO C 34 -31.016 26.950 57.090 1.00 34.14 N ANISOU 2715 N PRO C 34 4715 4198 4055 236 264 -1159 N ATOM 2716 CA PRO C 34 -30.774 25.638 57.723 1.00 33.02 C ANISOU 2716 CA PRO C 34 4648 4219 3678 233 269 -1118 C ATOM 2717 C PRO C 34 -31.981 24.685 57.867 1.00 31.87 C ANISOU 2717 C PRO C 34 4522 4169 3417 251 404 -1030 C ATOM 2718 O PRO C 34 -31.796 23.456 57.865 1.00 30.70 O ANISOU 2718 O PRO C 34 4429 4103 3132 226 424 -920 O ATOM 2719 CB PRO C 34 -30.246 26.021 59.111 1.00 34.66 C ANISOU 2719 CB PRO C 34 4931 4480 3756 286 216 -1318 C ATOM 2720 CG PRO C 34 -29.588 27.319 58.899 1.00 35.70 C ANISOU 2720 CG PRO C 34 4991 4470 4103 262 136 -1451 C ATOM 2721 CD PRO C 34 -30.443 28.043 57.904 1.00 35.58 C ANISOU 2721 CD PRO C 34 4905 4314 4299 252 212 -1368 C ATOM 2722 N GLU C 35 -33.175 25.261 57.991 1.00 32.03 N ANISOU 2722 N GLU C 35 4486 4163 3519 291 503 -1094 N ATOM 2723 CA GLU C 35 -34.422 24.524 58.208 1.00 32.01 C ANISOU 2723 CA GLU C 35 4461 4237 3464 296 663 -1066 C ATOM 2724 C GLU C 35 -34.858 23.666 57.015 1.00 29.76 C ANISOU 2724 C GLU C 35 4088 3955 3262 249 673 -913 C ATOM 2725 O GLU C 35 -35.650 22.759 57.183 1.00 29.82 O ANISOU 2725 O GLU C 35 4077 4028 3226 222 806 -885 O ATOM 2726 CB GLU C 35 -35.554 25.502 58.550 1.00 33.99 C ANISOU 2726 CB GLU C 35 4630 4451 3834 360 751 -1212 C ATOM 2727 CG GLU C 35 -35.338 26.255 59.851 1.00 36.21 C ANISOU 2727 CG GLU C 35 4998 4746 4011 414 773 -1394 C ATOM 2728 CD GLU C 35 -36.166 27.550 59.951 1.00 38.18 C ANISOU 2728 CD GLU C 35 5152 4909 4444 486 805 -1553 C ATOM 2729 OE1 GLU C 35 -36.391 28.225 58.918 1.00 38.52 O ANISOU 2729 OE1 GLU C 35 5092 4832 4710 509 728 -1516 O ATOM 2730 OE2 GLU C 35 -36.586 27.908 61.072 1.00 40.29 O ANISOU 2730 OE2 GLU C 35 5463 5223 4621 536 909 -1716 O ATOM 2731 N VAL C 36 -34.343 23.957 55.824 1.00 27.74 N ANISOU 2731 N VAL C 36 3785 3624 3128 237 546 -827 N ATOM 2732 CA VAL C 36 -34.662 23.181 54.639 1.00 26.09 C ANISOU 2732 CA VAL C 36 3508 3427 2978 209 528 -700 C ATOM 2733 C VAL C 36 -34.115 21.730 54.683 1.00 24.61 C ANISOU 2733 C VAL C 36 3384 3318 2648 137 551 -596 C ATOM 2734 O VAL C 36 -34.691 20.837 54.074 1.00 24.08 O ANISOU 2734 O VAL C 36 3256 3284 2609 106 592 -534 O ATOM 2735 CB VAL C 36 -34.150 23.898 53.362 1.00 25.53 C ANISOU 2735 CB VAL C 36 3418 3251 3031 229 400 -623 C ATOM 2736 CG1 VAL C 36 -32.650 23.704 53.188 1.00 24.59 C ANISOU 2736 CG1 VAL C 36 3377 3110 2853 166 329 -555 C ATOM 2737 CG2 VAL C 36 -34.881 23.383 52.138 1.00 25.15 C ANISOU 2737 CG2 VAL C 36 3286 3219 3048 252 372 -540 C ATOM 2738 N ILE C 37 -33.016 21.492 55.397 1.00 23.87 N ANISOU 2738 N ILE C 37 3407 3248 2413 122 514 -593 N ATOM 2739 CA ILE C 37 -32.336 20.196 55.321 1.00 22.73 C ANISOU 2739 CA ILE C 37 3333 3154 2148 80 502 -487 C ATOM 2740 C ILE C 37 -33.145 19.078 56.002 1.00 23.02 C ANISOU 2740 C ILE C 37 3425 3247 2073 61 668 -459 C ATOM 2741 O ILE C 37 -33.386 18.055 55.374 1.00 22.25 O ANISOU 2741 O ILE C 37 3297 3153 2002 11 708 -370 O ATOM 2742 CB ILE C 37 -30.851 20.260 55.806 1.00 22.74 C ANISOU 2742 CB ILE C 37 3425 3164 2049 94 379 -509 C ATOM 2743 CG1 ILE C 37 -30.070 21.313 55.008 1.00 22.39 C ANISOU 2743 CG1 ILE C 37 3305 3035 2167 77 265 -537 C ATOM 2744 CG2 ILE C 37 -30.153 18.897 55.632 1.00 22.04 C ANISOU 2744 CG2 ILE C 37 3401 3117 1855 73 352 -398 C ATOM 2745 CD1 ILE C 37 -28.722 21.672 55.606 1.00 22.91 C ANISOU 2745 CD1 ILE C 37 3404 3100 2199 87 150 -635 C ATOM 2746 N PRO C 38 -33.588 19.285 57.263 1.00 24.20 N ANISOU 2746 N PRO C 38 3661 3428 2105 98 784 -542 N ATOM 2747 CA PRO C 38 -34.550 18.389 57.900 1.00 25.20 C ANISOU 2747 CA PRO C 38 3839 3580 2154 69 1007 -522 C ATOM 2748 C PRO C 38 -35.818 18.124 57.072 1.00 24.94 C ANISOU 2748 C PRO C 38 3615 3527 2333 6 1116 -534 C ATOM 2749 O PRO C 38 -36.301 16.993 57.027 1.00 25.21 O ANISOU 2749 O PRO C 38 3652 3556 2370 -61 1261 -476 O ATOM 2750 CB PRO C 38 -34.948 19.146 59.173 1.00 27.01 C ANISOU 2750 CB PRO C 38 4150 3839 2273 131 1109 -650 C ATOM 2751 CG PRO C 38 -33.830 20.028 59.460 1.00 26.91 C ANISOU 2751 CG PRO C 38 4196 3831 2196 199 911 -717 C ATOM 2752 CD PRO C 38 -33.197 20.385 58.164 1.00 25.15 C ANISOU 2752 CD PRO C 38 3842 3554 2159 167 729 -672 C ATOM 2753 N MET C 39 -36.367 19.170 56.457 1.00 24.62 N ANISOU 2753 N MET C 39 3411 3466 2476 39 1044 -623 N ATOM 2754 CA MET C 39 -37.572 19.019 55.656 1.00 24.82 C ANISOU 2754 CA MET C 39 3234 3486 2709 15 1098 -673 C ATOM 2755 C MET C 39 -37.254 18.180 54.440 1.00 23.32 C ANISOU 2755 C MET C 39 2992 3290 2576 -28 993 -570 C ATOM 2756 O MET C 39 -37.995 17.283 54.111 1.00 23.50 O ANISOU 2756 O MET C 39 2916 3321 2688 -89 1091 -584 O ATOM 2757 CB MET C 39 -38.152 20.376 55.235 1.00 25.27 C ANISOU 2757 CB MET C 39 3152 3515 2932 103 1005 -786 C ATOM 2758 CG MET C 39 -38.616 21.211 56.386 1.00 26.92 C ANISOU 2758 CG MET C 39 3383 3728 3117 150 1120 -919 C ATOM 2759 SD MET C 39 -39.877 20.386 57.382 1.00 29.18 S ANISOU 2759 SD MET C 39 3622 4063 3401 82 1447 -1012 S ATOM 2760 CE MET C 39 -39.751 21.306 58.914 1.00 30.62 C ANISOU 2760 CE MET C 39 3957 4262 3413 148 1553 -1123 C ATOM 2761 N PHE C 40 -36.131 18.460 53.785 1.00 21.84 N ANISOU 2761 N PHE C 40 2868 3084 2346 -2 809 -484 N ATOM 2762 CA PHE C 40 -35.755 17.668 52.636 1.00 20.70 C ANISOU 2762 CA PHE C 40 2691 2939 2232 -37 718 -393 C ATOM 2763 C PHE C 40 -35.698 16.210 53.027 1.00 20.81 C ANISOU 2763 C PHE C 40 2770 2965 2169 -119 844 -335 C ATOM 2764 O PHE C 40 -36.238 15.341 52.341 1.00 20.81 O ANISOU 2764 O PHE C 40 2673 2966 2265 -170 878 -336 O ATOM 2765 CB PHE C 40 -34.396 18.066 52.085 1.00 19.46 C ANISOU 2765 CB PHE C 40 2618 2757 2017 -15 556 -307 C ATOM 2766 CG PHE C 40 -33.969 17.217 50.942 1.00 18.48 C ANISOU 2766 CG PHE C 40 2475 2641 1906 -47 483 -221 C ATOM 2767 CD1 PHE C 40 -34.640 17.293 49.736 1.00 18.52 C ANISOU 2767 CD1 PHE C 40 2365 2650 2019 -15 415 -235 C ATOM 2768 CD2 PHE C 40 -32.956 16.290 51.077 1.00 17.83 C ANISOU 2768 CD2 PHE C 40 2488 2565 1719 -91 476 -142 C ATOM 2769 CE1 PHE C 40 -34.267 16.500 48.678 1.00 17.82 C ANISOU 2769 CE1 PHE C 40 2268 2579 1923 -36 349 -174 C ATOM 2770 CE2 PHE C 40 -32.587 15.499 50.006 1.00 17.02 C ANISOU 2770 CE2 PHE C 40 2361 2469 1635 -116 417 -80 C ATOM 2771 CZ PHE C 40 -33.240 15.602 48.823 1.00 16.99 C ANISOU 2771 CZ PHE C 40 2252 2475 1727 -94 361 -98 C ATOM 2772 N SER C 41 -35.006 15.975 54.128 1.00 21.13 N ANISOU 2772 N SER C 41 2986 3007 2034 -117 902 -291 N ATOM 2773 CA SER C 41 -34.764 14.643 54.664 1.00 21.65 C ANISOU 2773 CA SER C 41 3183 3058 1982 -165 1021 -206 C ATOM 2774 C SER C 41 -36.079 13.933 54.963 1.00 23.12 C ANISOU 2774 C SER C 41 3305 3220 2259 -242 1264 -250 C ATOM 2775 O SER C 41 -36.307 12.823 54.504 1.00 23.33 O ANISOU 2775 O SER C 41 3299 3208 2355 -316 1336 -211 O ATOM 2776 CB SER C 41 -33.931 14.773 55.951 1.00 22.30 C ANISOU 2776 CB SER C 41 3485 3155 1832 -101 1025 -177 C ATOM 2777 OG SER C 41 -33.158 13.626 56.170 1.00 22.35 O ANISOU 2777 OG SER C 41 3647 3140 1704 -99 1025 -64 O ATOM 2778 N ALA C 42 -36.942 14.597 55.723 1.00 24.47 N ANISOU 2778 N ALA C 42 3441 3406 2450 -230 1402 -351 N ATOM 2779 CA ALA C 42 -38.260 14.060 56.053 1.00 26.37 C ANISOU 2779 CA ALA C 42 3583 3619 2814 -315 1668 -428 C ATOM 2780 C ALA C 42 -39.107 13.782 54.825 1.00 26.26 C ANISOU 2780 C ALA C 42 3299 3603 3074 -370 1627 -519 C ATOM 2781 O ALA C 42 -39.801 12.802 54.794 1.00 27.41 O ANISOU 2781 O ALA C 42 3372 3703 3337 -473 1813 -550 O ATOM 2782 CB ALA C 42 -39.010 14.989 57.000 1.00 27.85 C ANISOU 2782 CB ALA C 42 3752 3834 2994 -278 1809 -550 C ATOM 2783 N LEU C 43 -39.033 14.632 53.809 1.00 25.28 N ANISOU 2783 N LEU C 43 3036 3519 3047 -294 1385 -568 N ATOM 2784 CA LEU C 43 -39.937 14.531 52.668 1.00 25.78 C ANISOU 2784 CA LEU C 43 2844 3601 3349 -300 1309 -687 C ATOM 2785 C LEU C 43 -39.526 13.527 51.565 1.00 25.17 C ANISOU 2785 C LEU C 43 2741 3515 3305 -342 1197 -629 C ATOM 2786 O LEU C 43 -40.306 13.270 50.658 1.00 25.72 O ANISOU 2786 O LEU C 43 2603 3607 3562 -348 1137 -751 O ATOM 2787 CB LEU C 43 -40.175 15.920 52.078 1.00 25.44 C ANISOU 2787 CB LEU C 43 2691 3594 3378 -167 1107 -765 C ATOM 2788 CG LEU C 43 -41.053 16.833 52.950 1.00 26.97 C ANISOU 2788 CG LEU C 43 2807 3795 3643 -125 1229 -901 C ATOM 2789 CD1 LEU C 43 -41.125 18.242 52.382 1.00 26.71 C ANISOU 2789 CD1 LEU C 43 2713 3767 3668 25 1015 -950 C ATOM 2790 CD2 LEU C 43 -42.461 16.232 53.108 1.00 29.03 C ANISOU 2790 CD2 LEU C 43 2837 4065 4128 -203 1435 -1078 C ATOM 2791 N SER C 44 -38.340 12.934 51.679 1.00 24.43 N ANISOU 2791 N SER C 44 2849 3394 3038 -363 1168 -470 N ATOM 2792 CA SER C 44 -37.769 12.082 50.634 1.00 23.72 C ANISOU 2792 CA SER C 44 2757 3297 2958 -386 1047 -413 C ATOM 2793 C SER C 44 -37.478 10.671 51.118 1.00 24.50 C ANISOU 2793 C SER C 44 2975 3318 3013 -487 1217 -333 C ATOM 2794 O SER C 44 -36.527 10.047 50.670 1.00 23.61 O ANISOU 2794 O SER C 44 2960 3188 2821 -484 1124 -236 O ATOM 2795 CB SER C 44 -36.450 12.694 50.165 1.00 21.92 C ANISOU 2795 CB SER C 44 2654 3094 2581 -302 837 -299 C ATOM 2796 OG SER C 44 -35.481 12.641 51.213 1.00 21.64 O ANISOU 2796 OG SER C 44 2824 3033 2363 -299 887 -192 O ATOM 2797 N GLU C 45 -38.265 10.133 52.032 1.00 26.76 N ANISOU 2797 N GLU C 45 3270 3544 3353 -574 1483 -368 N ATOM 2798 CA GLU C 45 -37.888 8.824 52.559 1.00 27.66 C ANISOU 2798 CA GLU C 45 3558 3551 3397 -652 1658 -255 C ATOM 2799 C GLU C 45 -38.300 7.682 51.595 1.00 27.92 C ANISOU 2799 C GLU C 45 3442 3525 3640 -751 1681 -327 C ATOM 2800 O GLU C 45 -39.416 7.677 51.038 1.00 29.08 O ANISOU 2800 O GLU C 45 3330 3689 4030 -810 1714 -510 O ATOM 2801 CB GLU C 45 -38.307 8.664 54.035 1.00 30.06 C ANISOU 2801 CB GLU C 45 4025 3789 3605 -692 1961 -212 C ATOM 2802 CG GLU C 45 -37.084 9.073 54.942 1.00 29.73 C ANISOU 2802 CG GLU C 45 4279 3773 3241 -570 1874 -57 C ATOM 2803 CD GLU C 45 -37.369 9.253 56.422 1.00 31.96 C ANISOU 2803 CD GLU C 45 4760 4032 3348 -551 2110 -20 C ATOM 2804 OE1 GLU C 45 -38.059 8.409 57.023 1.00 34.77 O ANISOU 2804 OE1 GLU C 45 5194 4284 3734 -645 2422 4 O ATOM 2805 OE2 GLU C 45 -36.865 10.239 57.014 1.00 31.93 O ANISOU 2805 OE2 GLU C 45 4855 4109 3168 -441 1997 -19 O ATOM 2806 N GLY C 46 -37.354 6.770 51.348 1.00 26.66 N ANISOU 2806 N GLY C 46 3430 3304 3393 -753 1631 -206 N ATOM 2807 CA GLY C 46 -37.526 5.713 50.360 1.00 26.50 C ANISOU 2807 CA GLY C 46 3288 3228 3549 -830 1612 -277 C ATOM 2808 C GLY C 46 -37.372 6.180 48.923 1.00 24.83 C ANISOU 2808 C GLY C 46 2900 3136 3396 -761 1320 -374 C ATOM 2809 O GLY C 46 -37.701 5.443 47.993 1.00 25.31 O ANISOU 2809 O GLY C 46 2818 3181 3617 -811 1277 -487 O ATOM 2810 N ALA C 47 -36.848 7.390 48.730 1.00 22.95 N ANISOU 2810 N ALA C 47 2689 3008 3022 -642 1125 -332 N ATOM 2811 CA ALA C 47 -36.760 7.995 47.404 1.00 21.68 C ANISOU 2811 CA ALA C 47 2400 2951 2882 -557 874 -403 C ATOM 2812 C ALA C 47 -35.753 7.253 46.532 1.00 20.38 C ANISOU 2812 C ALA C 47 2307 2781 2653 -543 754 -342 C ATOM 2813 O ALA C 47 -34.734 6.782 47.022 1.00 19.74 O ANISOU 2813 O ALA C 47 2404 2645 2449 -547 790 -206 O ATOM 2814 CB ALA C 47 -36.350 9.489 47.514 1.00 20.64 C ANISOU 2814 CB ALA C 47 2324 2897 2621 -442 741 -345 C ATOM 2815 N THR C 48 -36.078 7.129 45.250 1.00 20.17 N ANISOU 2815 N THR C 48 2137 2816 2709 -514 607 -461 N ATOM 2816 CA THR C 48 -35.127 6.721 44.241 1.00 19.08 C ANISOU 2816 CA THR C 48 2058 2705 2485 -471 468 -420 C ATOM 2817 C THR C 48 -34.346 7.957 43.811 1.00 17.59 C ANISOU 2817 C THR C 48 1954 2598 2131 -355 314 -325 C ATOM 2818 O THR C 48 -34.796 9.094 44.036 1.00 17.58 O ANISOU 2818 O THR C 48 1925 2635 2120 -297 281 -332 O ATOM 2819 CB THR C 48 -35.810 6.155 42.970 1.00 20.11 C ANISOU 2819 CB THR C 48 2017 2883 2741 -465 360 -605 C ATOM 2820 OG1 THR C 48 -36.550 7.193 42.321 1.00 20.58 O ANISOU 2820 OG1 THR C 48 1960 3051 2809 -358 206 -704 O ATOM 2821 CG2 THR C 48 -36.735 4.980 43.293 1.00 21.87 C ANISOU 2821 CG2 THR C 48 2107 3009 3193 -601 523 -749 C ATOM 2822 N PRO C 49 -33.179 7.745 43.170 1.00 16.38 N ANISOU 2822 N PRO C 49 1900 2459 1866 -322 236 -246 N ATOM 2823 CA PRO C 49 -32.489 8.860 42.558 1.00 15.42 C ANISOU 2823 CA PRO C 49 1845 2396 1617 -228 121 -172 C ATOM 2824 C PRO C 49 -33.407 9.650 41.631 1.00 16.07 C ANISOU 2824 C PRO C 49 1840 2553 1711 -132 -2 -259 C ATOM 2825 O PRO C 49 -33.395 10.875 41.669 1.00 15.98 O ANISOU 2825 O PRO C 49 1873 2552 1645 -59 -44 -204 O ATOM 2826 CB PRO C 49 -31.353 8.184 41.794 1.00 15.00 C ANISOU 2826 CB PRO C 49 1860 2347 1490 -224 85 -131 C ATOM 2827 CG PRO C 49 -31.051 6.975 42.582 1.00 15.02 C ANISOU 2827 CG PRO C 49 1892 2268 1546 -306 190 -117 C ATOM 2828 CD PRO C 49 -32.360 6.519 43.170 1.00 16.11 C ANISOU 2828 CD PRO C 49 1936 2362 1823 -373 285 -207 C ATOM 2829 N GLN C 50 -34.223 8.963 40.832 1.00 16.98 N ANISOU 2829 N GLN C 50 1834 2711 1905 -119 -68 -407 N ATOM 2830 CA GLN C 50 -35.193 9.641 39.968 1.00 18.06 C ANISOU 2830 CA GLN C 50 1879 2930 2051 5 -222 -520 C ATOM 2831 C GLN C 50 -36.078 10.600 40.793 1.00 18.37 C ANISOU 2831 C GLN C 50 1844 2957 2177 30 -195 -547 C ATOM 2832 O GLN C 50 -36.293 11.753 40.417 1.00 18.58 O ANISOU 2832 O GLN C 50 1906 3014 2140 162 -302 -520 O ATOM 2833 CB GLN C 50 -36.059 8.626 39.216 1.00 19.54 C ANISOU 2833 CB GLN C 50 1901 3166 2358 1 -298 -733 C ATOM 2834 CG GLN C 50 -37.058 9.271 38.256 1.00 21.24 C ANISOU 2834 CG GLN C 50 2015 3485 2568 170 -507 -880 C ATOM 2835 CD GLN C 50 -38.091 8.299 37.732 1.00 23.13 C ANISOU 2835 CD GLN C 50 2028 3772 2985 155 -587 -1154 C ATOM 2836 OE1 GLN C 50 -38.058 7.929 36.565 1.00 24.05 O ANISOU 2836 OE1 GLN C 50 2148 3971 3018 250 -748 -1253 O ATOM 2837 NE2 GLN C 50 -39.008 7.873 38.592 1.00 23.91 N ANISOU 2837 NE2 GLN C 50 1930 3819 3336 32 -462 -1293 N ATOM 2838 N ASP C 51 -36.577 10.101 41.918 1.00 18.47 N ANISOU 2838 N ASP C 51 1771 2912 2333 -91 -35 -596 N ATOM 2839 CA ASP C 51 -37.426 10.895 42.806 1.00 19.03 C ANISOU 2839 CA ASP C 51 1762 2970 2497 -84 29 -641 C ATOM 2840 C ASP C 51 -36.690 12.103 43.388 1.00 17.76 C ANISOU 2840 C ASP C 51 1762 2781 2205 -35 41 -479 C ATOM 2841 O ASP C 51 -37.231 13.204 43.457 1.00 18.19 O ANISOU 2841 O ASP C 51 1784 2848 2279 59 -15 -507 O ATOM 2842 CB ASP C 51 -37.895 10.055 43.977 1.00 19.64 C ANISOU 2842 CB ASP C 51 1774 2975 2713 -240 256 -690 C ATOM 2843 CG ASP C 51 -38.923 9.037 43.608 1.00 21.40 C ANISOU 2843 CG ASP C 51 1784 3197 3148 -311 288 -898 C ATOM 2844 OD1 ASP C 51 -39.722 9.268 42.661 1.00 22.83 O ANISOU 2844 OD1 ASP C 51 1795 3462 3417 -215 115 -1072 O ATOM 2845 OD2 ASP C 51 -38.955 8.001 44.318 1.00 21.82 O ANISOU 2845 OD2 ASP C 51 1843 3156 3290 -460 495 -897 O ATOM 2846 N LEU C 52 -35.460 11.865 43.825 1.00 16.32 N ANISOU 2846 N LEU C 52 1739 2553 1908 -96 111 -332 N ATOM 2847 CA LEU C 52 -34.600 12.928 44.322 1.00 15.43 C ANISOU 2847 CA LEU C 52 1764 2409 1689 -64 114 -206 C ATOM 2848 C LEU C 52 -34.380 14.003 43.246 1.00 15.56 C ANISOU 2848 C LEU C 52 1833 2442 1634 61 -27 -161 C ATOM 2849 O LEU C 52 -34.477 15.184 43.538 1.00 15.64 O ANISOU 2849 O LEU C 52 1879 2420 1644 123 -41 -134 O ATOM 2850 CB LEU C 52 -33.288 12.362 44.848 1.00 14.31 C ANISOU 2850 CB LEU C 52 1752 2228 1457 -137 180 -96 C ATOM 2851 CG LEU C 52 -33.486 11.427 46.056 1.00 14.54 C ANISOU 2851 CG LEU C 52 1791 2216 1515 -230 331 -106 C ATOM 2852 CD1 LEU C 52 -32.219 10.691 46.383 1.00 13.82 C ANISOU 2852 CD1 LEU C 52 1826 2091 1331 -263 352 -11 C ATOM 2853 CD2 LEU C 52 -33.975 12.199 47.251 1.00 15.00 C ANISOU 2853 CD2 LEU C 52 1861 2257 1578 -227 419 -123 C ATOM 2854 N ASN C 53 -34.163 13.589 42.006 1.00 15.78 N ANISOU 2854 N ASN C 53 1878 2512 1604 108 -122 -159 N ATOM 2855 CA ASN C 53 -34.005 14.545 40.919 1.00 16.50 C ANISOU 2855 CA ASN C 53 2061 2610 1595 245 -236 -99 C ATOM 2856 C ASN C 53 -35.276 15.331 40.614 1.00 18.11 C ANISOU 2856 C ASN C 53 2188 2840 1853 388 -352 -190 C ATOM 2857 O ASN C 53 -35.195 16.534 40.368 1.00 18.62 O ANISOU 2857 O ASN C 53 2356 2854 1863 497 -396 -110 O ATOM 2858 CB ASN C 53 -33.434 13.873 39.660 1.00 16.55 C ANISOU 2858 CB ASN C 53 2133 2665 1488 273 -296 -76 C ATOM 2859 CG ASN C 53 -31.958 13.557 39.806 1.00 15.28 C ANISOU 2859 CG ASN C 53 2078 2462 1263 175 -193 36 C ATOM 2860 OD1 ASN C 53 -31.225 14.289 40.449 1.00 14.60 O ANISOU 2860 OD1 ASN C 53 2061 2309 1177 136 -119 124 O ATOM 2861 ND2 ASN C 53 -31.522 12.461 39.218 1.00 15.18 N ANISOU 2861 ND2 ASN C 53 2062 2491 1215 139 -194 9 N ATOM 2862 N THR C 54 -36.432 14.673 40.684 1.00 19.23 N ANISOU 2862 N THR C 54 2140 3042 2123 387 -390 -365 N ATOM 2863 CA THR C 54 -37.711 15.355 40.578 1.00 21.13 C ANISOU 2863 CA THR C 54 2253 3313 2461 522 -500 -496 C ATOM 2864 C THR C 54 -37.799 16.434 41.661 1.00 21.17 C ANISOU 2864 C THR C 54 2280 3241 2520 517 -410 -449 C ATOM 2865 O THR C 54 -38.167 17.569 41.384 1.00 22.06 O ANISOU 2865 O THR C 54 2432 3325 2622 672 -507 -436 O ATOM 2866 CB THR C 54 -38.914 14.388 40.738 1.00 22.29 C ANISOU 2866 CB THR C 54 2139 3525 2804 470 -504 -732 C ATOM 2867 OG1 THR C 54 -38.787 13.294 39.829 1.00 22.58 O ANISOU 2867 OG1 THR C 54 2145 3622 2811 452 -576 -800 O ATOM 2868 CG2 THR C 54 -40.215 15.091 40.473 1.00 24.26 C ANISOU 2868 CG2 THR C 54 2226 3822 3169 637 -652 -901 C ATOM 2869 N MET C 55 -37.443 16.079 42.890 1.00 20.49 N ANISOU 2869 N MET C 55 2189 3115 2481 356 -229 -426 N ATOM 2870 CA MET C 55 -37.437 17.064 43.987 1.00 20.74 C ANISOU 2870 CA MET C 55 2255 3080 2544 348 -138 -398 C ATOM 2871 C MET C 55 -36.535 18.254 43.677 1.00 20.64 C ANISOU 2871 C MET C 55 2429 2989 2424 425 -185 -248 C ATOM 2872 O MET C 55 -36.953 19.408 43.799 1.00 21.50 O ANISOU 2872 O MET C 55 2550 3043 2573 531 -224 -260 O ATOM 2873 CB MET C 55 -37.024 16.417 45.304 1.00 19.90 C ANISOU 2873 CB MET C 55 2165 2952 2444 183 51 -381 C ATOM 2874 CG MET C 55 -38.004 15.354 45.774 1.00 20.77 C ANISOU 2874 CG MET C 55 2109 3098 2685 93 162 -520 C ATOM 2875 SD MET C 55 -37.711 14.783 47.456 1.00 20.64 S ANISOU 2875 SD MET C 55 2166 3035 2641 -58 411 -483 S ATOM 2876 CE MET C 55 -38.363 16.172 48.412 1.00 21.50 C ANISOU 2876 CE MET C 55 2244 3127 2796 10 464 -555 C ATOM 2877 N LEU C 56 -35.325 17.971 43.221 1.00 20.10 N ANISOU 2877 N LEU C 56 2496 2900 2238 372 -172 -120 N ATOM 2878 CA LEU C 56 -34.366 19.019 42.896 1.00 20.44 C ANISOU 2878 CA LEU C 56 2710 2849 2207 410 -172 15 C ATOM 2879 C LEU C 56 -34.813 19.847 41.706 1.00 22.34 C ANISOU 2879 C LEU C 56 3029 3061 2398 594 -298 57 C ATOM 2880 O LEU C 56 -34.670 21.069 41.728 1.00 23.10 O ANISOU 2880 O LEU C 56 3229 3043 2502 666 -291 125 O ATOM 2881 CB LEU C 56 -32.983 18.427 42.612 1.00 19.36 C ANISOU 2881 CB LEU C 56 2669 2706 1980 306 -113 116 C ATOM 2882 CG LEU C 56 -32.339 17.629 43.750 1.00 18.23 C ANISOU 2882 CG LEU C 56 2490 2580 1857 159 -14 94 C ATOM 2883 CD1 LEU C 56 -30.891 17.341 43.405 1.00 17.49 C ANISOU 2883 CD1 LEU C 56 2483 2463 1698 91 22 181 C ATOM 2884 CD2 LEU C 56 -32.449 18.377 45.100 1.00 18.33 C ANISOU 2884 CD2 LEU C 56 2491 2543 1929 133 47 50 C ATOM 2885 N ASN C 57 -35.365 19.189 40.683 1.00 23.58 N ANISOU 2885 N ASN C 57 3148 3311 2500 682 -417 11 N ATOM 2886 CA ASN C 57 -35.754 19.867 39.451 1.00 25.80 C ANISOU 2886 CA ASN C 57 3542 3581 2681 894 -563 57 C ATOM 2887 C ASN C 57 -37.048 20.676 39.598 1.00 27.61 C ANISOU 2887 C ASN C 57 3679 3801 3009 1066 -685 -49 C ATOM 2888 O ASN C 57 -37.447 21.385 38.688 1.00 29.44 O ANISOU 2888 O ASN C 57 4021 4006 3157 1282 -826 -9 O ATOM 2889 CB ASN C 57 -35.838 18.859 38.270 1.00 26.63 C ANISOU 2889 CB ASN C 57 3647 3804 2665 949 -674 20 C ATOM 2890 CG ASN C 57 -34.442 18.338 37.834 1.00 25.77 C ANISOU 2890 CG ASN C 57 3682 3680 2427 832 -559 153 C ATOM 2891 OD1 ASN C 57 -33.426 18.716 38.422 1.00 24.99 O ANISOU 2891 OD1 ASN C 57 3660 3486 2348 708 -407 260 O ATOM 2892 ND2 ASN C 57 -34.397 17.457 36.804 1.00 26.68 N ANISOU 2892 ND2 ASN C 57 3815 3895 2424 875 -637 118 N ATOM 2893 N THR C 58 -37.691 20.564 40.749 1.00 27.41 N ANISOU 2893 N THR C 58 3462 3794 3156 983 -623 -185 N ATOM 2894 CA THR C 58 -38.896 21.320 41.053 1.00 29.23 C ANISOU 2894 CA THR C 58 3570 4015 3519 1128 -709 -315 C ATOM 2895 C THR C 58 -38.549 22.639 41.741 1.00 29.40 C ANISOU 2895 C THR C 58 3709 3883 3576 1146 -625 -226 C ATOM 2896 O THR C 58 -39.379 23.522 41.824 1.00 31.15 O ANISOU 2896 O THR C 58 3889 4059 3886 1305 -705 -296 O ATOM 2897 CB THR C 58 -39.849 20.508 41.972 1.00 29.26 C ANISOU 2897 CB THR C 58 3292 4114 3711 1020 -644 -532 C ATOM 2898 OG1 THR C 58 -41.195 20.690 41.541 1.00 31.66 O ANISOU 2898 OG1 THR C 58 3413 4484 4132 1202 -813 -721 O ATOM 2899 CG2 THR C 58 -39.719 20.931 43.446 1.00 28.31 C ANISOU 2899 CG2 THR C 58 3147 3926 3684 891 -454 -542 C ATOM 2900 N VAL C 59 -37.329 22.760 42.248 1.00 28.07 N ANISOU 2900 N VAL C 59 3670 3634 3360 986 -471 -99 N ATOM 2901 CA VAL C 59 -36.830 24.034 42.743 1.00 28.52 C ANISOU 2901 CA VAL C 59 3855 3526 3453 995 -396 -20 C ATOM 2902 C VAL C 59 -36.829 25.037 41.610 1.00 30.56 C ANISOU 2902 C VAL C 59 4312 3664 3636 1197 -493 110 C ATOM 2903 O VAL C 59 -36.033 24.913 40.664 1.00 30.73 O ANISOU 2903 O VAL C 59 4507 3654 3514 1200 -482 261 O ATOM 2904 CB VAL C 59 -35.385 23.894 43.246 1.00 26.97 C ANISOU 2904 CB VAL C 59 3756 3274 3216 796 -242 76 C ATOM 2905 CG1 VAL C 59 -34.682 25.258 43.346 1.00 27.54 C ANISOU 2905 CG1 VAL C 59 3989 3146 3326 812 -174 171 C ATOM 2906 CG2 VAL C 59 -35.375 23.121 44.567 1.00 25.51 C ANISOU 2906 CG2 VAL C 59 3426 3178 3087 633 -145 -39 C ATOM 2907 N GLY C 60 -37.726 26.019 41.697 1.00 32.34 N ANISOU 2907 N GLY C 60 4522 3813 3951 1377 -578 53 N ATOM 2908 CA GLY C 60 -37.760 27.110 40.738 1.00 34.49 C ANISOU 2908 CA GLY C 60 5021 3929 4152 1597 -661 194 C ATOM 2909 C GLY C 60 -36.710 28.136 41.114 1.00 34.40 C ANISOU 2909 C GLY C 60 5196 3692 4181 1501 -487 330 C ATOM 2910 O GLY C 60 -36.704 28.628 42.247 1.00 34.17 O ANISOU 2910 O GLY C 60 5077 3600 4305 1411 -400 234 O ATOM 2911 N GLY C 61 -35.818 28.447 40.168 1.00 34.79 N ANISOU 2911 N GLY C 61 5500 3619 4099 1515 -423 535 N ATOM 2912 CA GLY C 61 -34.741 29.394 40.405 1.00 34.77 C ANISOU 2912 CA GLY C 61 5666 3381 4164 1401 -230 656 C ATOM 2913 C GLY C 61 -33.774 28.849 41.430 1.00 32.17 C ANISOU 2913 C GLY C 61 5195 3106 3922 1113 -82 574 C ATOM 2914 O GLY C 61 -33.545 27.652 41.508 1.00 30.33 O ANISOU 2914 O GLY C 61 4842 3060 3621 999 -92 526 O ATOM 2915 N HIS C 62 -33.244 29.749 42.247 1.00 32.24 N ANISOU 2915 N HIS C 62 5217 2942 4088 1015 38 542 N ATOM 2916 CA HIS C 62 -32.136 29.448 43.126 1.00 30.46 C ANISOU 2916 CA HIS C 62 4899 2731 3941 769 168 469 C ATOM 2917 C HIS C 62 -31.030 28.850 42.295 1.00 29.78 C ANISOU 2917 C HIS C 62 4903 2658 3752 659 262 598 C ATOM 2918 O HIS C 62 -30.548 27.762 42.568 1.00 27.95 O ANISOU 2918 O HIS C 62 4551 2593 3472 530 263 543 O ATOM 2919 CB HIS C 62 -32.568 28.520 44.248 1.00 28.51 C ANISOU 2919 CB HIS C 62 4423 2703 3704 691 108 287 C ATOM 2920 CG HIS C 62 -33.591 29.131 45.135 1.00 29.22 C ANISOU 2920 CG HIS C 62 4418 2780 3903 782 58 143 C ATOM 2921 ND1 HIS C 62 -33.316 30.222 45.936 1.00 30.16 N ANISOU 2921 ND1 HIS C 62 4555 2732 4169 750 129 66 N ATOM 2922 CD2 HIS C 62 -34.894 28.830 45.330 1.00 29.28 C ANISOU 2922 CD2 HIS C 62 4299 2913 3913 904 -46 41 C ATOM 2923 CE1 HIS C 62 -34.405 30.552 46.605 1.00 30.74 C ANISOU 2923 CE1 HIS C 62 4529 2837 4312 854 73 -69 C ATOM 2924 NE2 HIS C 62 -35.372 29.717 46.262 1.00 30.34 N ANISOU 2924 NE2 HIS C 62 4381 2964 4182 945 -25 -88 N ATOM 2925 N GLN C 63 -30.649 29.590 41.262 1.00 31.56 N ANISOU 2925 N GLN C 63 5356 2691 3943 722 352 775 N ATOM 2926 CA GLN C 63 -29.724 29.085 40.259 1.00 31.50 C ANISOU 2926 CA GLN C 63 5467 2687 3813 652 461 913 C ATOM 2927 C GLN C 63 -28.345 28.821 40.874 1.00 30.27 C ANISOU 2927 C GLN C 63 5197 2518 3785 393 617 837 C ATOM 2928 O GLN C 63 -27.791 27.750 40.683 1.00 28.70 O ANISOU 2928 O GLN C 63 4921 2476 3505 301 623 823 O ATOM 2929 CB GLN C 63 -29.633 30.068 39.089 1.00 34.30 C ANISOU 2929 CB GLN C 63 6129 2805 4097 784 565 1131 C ATOM 2930 CG GLN C 63 -29.409 29.410 37.751 1.00 34.94 C ANISOU 2930 CG GLN C 63 6375 2964 3933 855 583 1286 C ATOM 2931 CD GLN C 63 -30.510 28.448 37.378 1.00 34.03 C ANISOU 2931 CD GLN C 63 6183 3108 3635 1029 329 1231 C ATOM 2932 OE1 GLN C 63 -30.239 27.327 37.021 1.00 32.82 O ANISOU 2932 OE1 GLN C 63 5960 3141 3367 970 303 1206 O ATOM 2933 NE2 GLN C 63 -31.752 28.878 37.483 1.00 34.91 N ANISOU 2933 NE2 GLN C 63 6286 3228 3748 1241 142 1187 N ATOM 2934 N ALA C 64 -27.818 29.783 41.630 1.00 31.08 N ANISOU 2934 N ALA C 64 5274 2434 4099 289 725 763 N ATOM 2935 CA ALA C 64 -26.462 29.680 42.183 1.00 30.86 C ANISOU 2935 CA ALA C 64 5125 2373 4225 59 859 658 C ATOM 2936 C ALA C 64 -26.381 28.614 43.278 1.00 28.68 C ANISOU 2936 C ALA C 64 4613 2346 3937 -19 726 471 C ATOM 2937 O ALA C 64 -25.379 27.921 43.398 1.00 27.68 O ANISOU 2937 O ALA C 64 4385 2299 3830 -153 769 414 O ATOM 2938 CB ALA C 64 -25.993 31.020 42.717 1.00 32.56 C ANISOU 2938 CB ALA C 64 5361 2319 4690 -23 991 590 C ATOM 2939 N ALA C 65 -27.443 28.496 44.071 1.00 28.22 N ANISOU 2939 N ALA C 65 4476 2398 3846 76 576 378 N ATOM 2940 CA ALA C 65 -27.557 27.422 45.041 1.00 26.65 C ANISOU 2940 CA ALA C 65 4107 2428 3588 33 467 240 C ATOM 2941 C ALA C 65 -27.543 26.063 44.351 1.00 25.69 C ANISOU 2941 C ALA C 65 3970 2488 3300 37 423 317 C ATOM 2942 O ALA C 65 -26.820 25.168 44.781 1.00 24.64 O ANISOU 2942 O ALA C 65 3739 2471 3149 -61 414 250 O ATOM 2943 CB ALA C 65 -28.814 27.584 45.867 1.00 26.49 C ANISOU 2943 CB ALA C 65 4031 2474 3558 140 362 147 C ATOM 2944 N MET C 66 -28.315 25.909 43.277 1.00 26.57 N ANISOU 2944 N MET C 66 4182 2620 3291 165 383 445 N ATOM 2945 CA MET C 66 -28.363 24.639 42.516 1.00 26.07 C ANISOU 2945 CA MET C 66 4109 2723 3073 179 334 499 C ATOM 2946 C MET C 66 -27.033 24.268 41.823 1.00 26.12 C ANISOU 2946 C MET C 66 4157 2704 3061 67 456 566 C ATOM 2947 O MET C 66 -26.632 23.089 41.805 1.00 24.45 O ANISOU 2947 O MET C 66 3863 2636 2788 8 430 532 O ATOM 2948 CB MET C 66 -29.483 24.688 41.471 1.00 27.50 C ANISOU 2948 CB MET C 66 4390 2927 3130 365 241 591 C ATOM 2949 CG MET C 66 -30.878 24.821 42.060 1.00 28.00 C ANISOU 2949 CG MET C 66 4361 3052 3224 483 111 493 C ATOM 2950 SD MET C 66 -31.277 23.436 43.150 1.00 27.22 S ANISOU 2950 SD MET C 66 4044 3167 3131 389 56 334 S ATOM 2951 CE MET C 66 -31.283 22.130 41.920 1.00 26.26 C ANISOU 2951 CE MET C 66 3933 3184 2860 413 -1 391 C ATOM 2952 N GLN C 67 -26.359 25.273 41.261 1.00 27.91 N ANISOU 2952 N GLN C 67 4512 2734 3356 37 605 655 N ATOM 2953 CA GLN C 67 -25.033 25.089 40.661 1.00 28.75 C ANISOU 2953 CA GLN C 67 4643 2789 3491 -90 770 697 C ATOM 2954 C GLN C 67 -24.054 24.544 41.692 1.00 27.62 C ANISOU 2954 C GLN C 67 4295 2720 3480 -245 768 526 C ATOM 2955 O GLN C 67 -23.362 23.565 41.434 1.00 26.75 O ANISOU 2955 O GLN C 67 4116 2718 3329 -306 782 505 O ATOM 2956 CB GLN C 67 -24.493 26.402 40.078 1.00 31.50 C ANISOU 2956 CB GLN C 67 5157 2871 3940 -121 976 803 C ATOM 2957 CG GLN C 67 -23.348 26.196 39.095 1.00 33.04 C ANISOU 2957 CG GLN C 67 5424 3008 4120 -221 1187 887 C ATOM 2958 CD GLN C 67 -23.334 27.230 37.972 1.00 36.26 C ANISOU 2958 CD GLN C 67 6116 3181 4477 -160 1386 1093 C ATOM 2959 OE1 GLN C 67 -22.282 27.787 37.629 1.00 38.53 O ANISOU 2959 OE1 GLN C 67 6454 3283 4900 -300 1647 1127 O ATOM 2960 NE2 GLN C 67 -24.507 27.498 37.390 1.00 37.16 N ANISOU 2960 NE2 GLN C 67 6423 3294 4401 58 1269 1227 N ATOM 2961 N MET C 68 -24.021 25.167 42.868 1.00 27.65 N ANISOU 2961 N MET C 68 4204 2668 3631 -289 733 393 N ATOM 2962 CA MET C 68 -23.183 24.693 43.974 1.00 27.02 C ANISOU 2962 CA MET C 68 3941 2673 3650 -393 682 209 C ATOM 2963 C MET C 68 -23.516 23.256 44.379 1.00 24.54 C ANISOU 2963 C MET C 68 3551 2587 3185 -350 535 175 C ATOM 2964 O MET C 68 -22.618 22.463 44.608 1.00 23.81 O ANISOU 2964 O MET C 68 3359 2577 3109 -412 518 101 O ATOM 2965 CB MET C 68 -23.318 25.635 45.178 1.00 28.29 C ANISOU 2965 CB MET C 68 4044 2753 3951 -407 640 62 C ATOM 2966 CG MET C 68 -22.513 25.248 46.408 1.00 28.39 C ANISOU 2966 CG MET C 68 3888 2859 4037 -475 551 -148 C ATOM 2967 SD MET C 68 -22.053 26.678 47.454 1.00 31.34 S ANISOU 2967 SD MET C 68 4188 3063 4654 -542 571 -359 S ATOM 2968 CE MET C 68 -23.423 27.845 47.267 1.00 31.42 C ANISOU 2968 CE MET C 68 4354 2918 4663 -440 610 -253 C ATOM 2969 N LEU C 69 -24.804 22.931 44.452 1.00 23.14 N ANISOU 2969 N LEU C 69 3416 2495 2880 -240 438 222 N ATOM 2970 CA LEU C 69 -25.243 21.571 44.744 1.00 21.51 C ANISOU 2970 CA LEU C 69 3155 2469 2547 -209 337 204 C ATOM 2971 C LEU C 69 -24.749 20.573 43.688 1.00 20.82 C ANISOU 2971 C LEU C 69 3080 2448 2381 -226 364 278 C ATOM 2972 O LEU C 69 -24.238 19.521 44.030 1.00 19.78 O ANISOU 2972 O LEU C 69 2876 2414 2224 -260 325 226 O ATOM 2973 CB LEU C 69 -26.774 21.523 44.834 1.00 21.11 C ANISOU 2973 CB LEU C 69 3129 2471 2420 -102 264 227 C ATOM 2974 CG LEU C 69 -27.503 20.234 45.193 1.00 20.17 C ANISOU 2974 CG LEU C 69 2952 2504 2205 -77 193 199 C ATOM 2975 CD1 LEU C 69 -27.030 19.628 46.509 1.00 19.53 C ANISOU 2975 CD1 LEU C 69 2815 2488 2118 -129 172 103 C ATOM 2976 CD2 LEU C 69 -29.008 20.492 45.250 1.00 20.41 C ANISOU 2976 CD2 LEU C 69 2975 2556 2225 16 149 187 C ATOM 2977 N LYS C 70 -24.930 20.920 42.417 1.00 21.58 N ANISOU 2977 N LYS C 70 3287 2486 2425 -184 429 398 N ATOM 2978 CA LYS C 70 -24.522 20.096 41.268 1.00 21.57 C ANISOU 2978 CA LYS C 70 3326 2544 2326 -184 470 467 C ATOM 2979 C LYS C 70 -23.020 19.826 41.297 1.00 21.56 C ANISOU 2979 C LYS C 70 3248 2523 2420 -304 569 411 C ATOM 2980 O LYS C 70 -22.555 18.731 40.985 1.00 20.86 O ANISOU 2980 O LYS C 70 3110 2531 2284 -322 558 390 O ATOM 2981 CB LYS C 70 -24.889 20.834 39.969 1.00 23.24 C ANISOU 2981 CB LYS C 70 3715 2667 2449 -99 541 609 C ATOM 2982 CG LYS C 70 -24.668 20.068 38.666 1.00 23.95 C ANISOU 2982 CG LYS C 70 3886 2826 2385 -63 577 682 C ATOM 2983 CD LYS C 70 -24.243 20.993 37.474 1.00 26.28 C ANISOU 2983 CD LYS C 70 4388 2977 2617 -34 750 829 C ATOM 2984 CE LYS C 70 -25.300 22.060 37.110 1.00 27.71 C ANISOU 2984 CE LYS C 70 4743 3060 2725 120 703 937 C ATOM 2985 NZ LYS C 70 -24.750 23.158 36.191 1.00 30.24 N ANISOU 2985 NZ LYS C 70 5299 3177 3013 134 916 1100 N ATOM 2986 N GLU C 71 -22.266 20.846 41.664 1.00 22.39 N ANISOU 2986 N GLU C 71 3327 2494 2684 -385 666 368 N ATOM 2987 CA GLU C 71 -20.830 20.730 41.824 1.00 22.97 C ANISOU 2987 CA GLU C 71 3280 2541 2905 -504 754 265 C ATOM 2988 C GLU C 71 -20.454 19.777 42.985 1.00 21.40 C ANISOU 2988 C GLU C 71 2924 2475 2730 -509 599 115 C ATOM 2989 O GLU C 71 -19.511 18.988 42.852 1.00 21.14 O ANISOU 2989 O GLU C 71 2795 2501 2735 -547 607 49 O ATOM 2990 CB GLU C 71 -20.258 22.142 42.001 1.00 25.20 C ANISOU 2990 CB GLU C 71 3560 2629 3386 -593 893 227 C ATOM 2991 CG GLU C 71 -18.785 22.257 42.375 1.00 26.67 C ANISOU 2991 CG GLU C 71 3567 2768 3799 -731 976 57 C ATOM 2992 CD GLU C 71 -18.352 23.717 42.443 1.00 29.10 C ANISOU 2992 CD GLU C 71 3878 2850 4329 -832 1141 16 C ATOM 2993 OE1 GLU C 71 -19.117 24.574 41.931 1.00 29.96 O ANISOU 2993 OE1 GLU C 71 4173 2824 4385 -786 1225 169 O ATOM 2994 OE2 GLU C 71 -17.266 24.012 43.016 1.00 30.60 O ANISOU 2994 OE2 GLU C 71 3880 2987 4756 -948 1179 -181 O ATOM 2995 N THR C 72 -21.203 19.824 44.093 1.00 20.10 N ANISOU 2995 N THR C 72 2750 2355 2531 -454 464 65 N ATOM 2996 CA THR C 72 -20.969 18.923 45.238 1.00 19.15 C ANISOU 2996 CA THR C 72 2541 2352 2381 -426 320 -48 C ATOM 2997 C THR C 72 -21.227 17.461 44.875 1.00 17.82 C ANISOU 2997 C THR C 72 2391 2301 2077 -378 268 11 C ATOM 2998 O THR C 72 -20.413 16.578 45.205 1.00 17.75 O ANISOU 2998 O THR C 72 2309 2354 2080 -374 210 -61 O ATOM 2999 CB THR C 72 -21.849 19.262 46.461 1.00 18.80 C ANISOU 2999 CB THR C 72 2524 2329 2287 -369 222 -94 C ATOM 3000 OG1 THR C 72 -21.433 20.511 47.013 1.00 20.03 O ANISOU 3000 OG1 THR C 72 2638 2381 2588 -413 244 -202 O ATOM 3001 CG2 THR C 72 -21.730 18.173 47.559 1.00 18.27 C ANISOU 3001 CG2 THR C 72 2433 2383 2125 -312 91 -166 C ATOM 3002 N ILE C 73 -22.357 17.232 44.217 1.00 16.92 N ANISOU 3002 N ILE C 73 2368 2209 1850 -331 278 125 N ATOM 3003 CA ILE C 73 -22.733 15.911 43.682 1.00 16.10 C ANISOU 3003 CA ILE C 73 2282 2195 1640 -295 246 172 C ATOM 3004 C ILE C 73 -21.687 15.320 42.736 1.00 16.33 C ANISOU 3004 C ILE C 73 2278 2236 1688 -330 308 171 C ATOM 3005 O ILE C 73 -21.292 14.165 42.876 1.00 15.63 O ANISOU 3005 O ILE C 73 2145 2210 1582 -317 259 132 O ATOM 3006 CB ILE C 73 -24.080 15.979 42.964 1.00 15.94 C ANISOU 3006 CB ILE C 73 2337 2189 1529 -239 241 256 C ATOM 3007 CG1 ILE C 73 -25.207 16.279 43.980 1.00 15.79 C ANISOU 3007 CG1 ILE C 73 2319 2177 1502 -202 185 231 C ATOM 3008 CG2 ILE C 73 -24.360 14.672 42.208 1.00 15.34 C ANISOU 3008 CG2 ILE C 73 2263 2193 1372 -214 217 273 C ATOM 3009 CD1 ILE C 73 -26.454 16.914 43.324 1.00 16.19 C ANISOU 3009 CD1 ILE C 73 2419 2212 1521 -133 176 282 C ATOM 3010 N ASN C 74 -21.228 16.122 41.783 1.00 17.40 N ANISOU 3010 N ASN C 74 2446 2300 1862 -369 433 214 N ATOM 3011 CA ASN C 74 -20.125 15.703 40.898 1.00 18.22 C ANISOU 3011 CA ASN C 74 2513 2407 2001 -416 538 198 C ATOM 3012 C ASN C 74 -18.852 15.340 41.650 1.00 18.47 C ANISOU 3012 C ASN C 74 2387 2452 2178 -463 511 54 C ATOM 3013 O ASN C 74 -18.214 14.370 41.293 1.00 18.74 O ANISOU 3013 O ASN C 74 2361 2540 2215 -457 513 10 O ATOM 3014 CB ASN C 74 -19.830 16.747 39.803 1.00 19.69 C ANISOU 3014 CB ASN C 74 2792 2488 2201 -457 725 281 C ATOM 3015 CG ASN C 74 -20.992 16.916 38.845 1.00 19.96 C ANISOU 3015 CG ASN C 74 3000 2530 2051 -365 723 419 C ATOM 3016 OD1 ASN C 74 -21.095 17.924 38.142 1.00 21.44 O ANISOU 3016 OD1 ASN C 74 3321 2615 2210 -355 843 520 O ATOM 3017 ND2 ASN C 74 -21.909 15.946 38.851 1.00 18.98 N ANISOU 3017 ND2 ASN C 74 2880 2519 1812 -286 580 416 N ATOM 3018 N GLU C 75 -18.492 16.081 42.691 1.00 18.83 N ANISOU 3018 N GLU C 75 2358 2451 2343 -492 469 -39 N ATOM 3019 CA GLU C 75 -17.334 15.706 43.508 1.00 19.44 C ANISOU 3019 CA GLU C 75 2273 2560 2550 -501 388 -208 C ATOM 3020 C GLU C 75 -17.538 14.350 44.205 1.00 18.23 C ANISOU 3020 C GLU C 75 2127 2513 2286 -398 217 -225 C ATOM 3021 O GLU C 75 -16.640 13.521 44.219 1.00 18.40 O ANISOU 3021 O GLU C 75 2054 2577 2359 -371 172 -312 O ATOM 3022 CB GLU C 75 -16.996 16.786 44.551 1.00 20.56 C ANISOU 3022 CB GLU C 75 2339 2643 2829 -533 344 -335 C ATOM 3023 CG GLU C 75 -16.502 18.098 43.942 1.00 22.30 C ANISOU 3023 CG GLU C 75 2525 2719 3225 -655 538 -353 C ATOM 3024 CD GLU C 75 -16.313 19.239 44.958 1.00 23.55 C ANISOU 3024 CD GLU C 75 2612 2798 3535 -694 496 -493 C ATOM 3025 OE1 GLU C 75 -16.900 19.207 46.079 1.00 23.13 O ANISOU 3025 OE1 GLU C 75 2588 2804 3393 -611 324 -535 O ATOM 3026 OE2 GLU C 75 -15.564 20.182 44.613 1.00 25.45 O ANISOU 3026 OE2 GLU C 75 2769 2907 3991 -813 657 -569 O ATOM 3027 N GLU C 76 -18.707 14.138 44.792 1.00 17.13 N ANISOU 3027 N GLU C 76 2099 2400 2006 -337 137 -147 N ATOM 3028 CA GLU C 76 -19.002 12.867 45.474 1.00 16.53 C ANISOU 3028 CA GLU C 76 2068 2390 1822 -248 17 -137 C ATOM 3029 C GLU C 76 -19.125 11.698 44.484 1.00 15.78 C ANISOU 3029 C GLU C 76 1997 2322 1676 -237 57 -74 C ATOM 3030 O GLU C 76 -18.656 10.585 44.753 1.00 15.71 O ANISOU 3030 O GLU C 76 1973 2339 1658 -178 -13 -109 O ATOM 3031 CB GLU C 76 -20.253 12.991 46.353 1.00 16.12 C ANISOU 3031 CB GLU C 76 2127 2344 1654 -208 -25 -77 C ATOM 3032 CG GLU C 76 -20.102 13.984 47.513 1.00 17.01 C ANISOU 3032 CG GLU C 76 2225 2443 1793 -194 -87 -167 C ATOM 3033 CD GLU C 76 -19.133 13.550 48.602 1.00 18.19 C ANISOU 3033 CD GLU C 76 2337 2635 1939 -111 -231 -291 C ATOM 3034 OE1 GLU C 76 -18.868 12.331 48.774 1.00 18.55 O ANISOU 3034 OE1 GLU C 76 2417 2715 1916 -35 -297 -273 O ATOM 3035 OE2 GLU C 76 -18.621 14.441 49.314 1.00 19.35 O ANISOU 3035 OE2 GLU C 76 2422 2775 2154 -108 -293 -421 O ATOM 3036 N ALA C 77 -19.731 11.963 43.330 1.00 15.27 N ANISOU 3036 N ALA C 77 1978 2246 1575 -279 160 8 N ATOM 3037 CA ALA C 77 -19.745 10.983 42.240 1.00 15.08 C ANISOU 3037 CA ALA C 77 1968 2252 1507 -271 202 35 C ATOM 3038 C ALA C 77 -18.323 10.617 41.759 1.00 15.91 C ANISOU 3038 C ALA C 77 1968 2364 1712 -288 247 -52 C ATOM 3039 O ALA C 77 -18.016 9.446 41.612 1.00 15.86 O ANISOU 3039 O ALA C 77 1940 2385 1701 -245 209 -86 O ATOM 3040 CB ALA C 77 -20.601 11.471 41.084 1.00 14.97 C ANISOU 3040 CB ALA C 77 2036 2237 1412 -285 282 121 C ATOM 3041 N ALA C 78 -17.461 11.606 41.536 1.00 16.87 N ANISOU 3041 N ALA C 78 2014 2447 1945 -353 341 -102 N ATOM 3042 CA ALA C 78 -16.068 11.332 41.131 1.00 18.00 C ANISOU 3042 CA ALA C 78 2019 2595 2225 -382 408 -218 C ATOM 3043 C ALA C 78 -15.328 10.536 42.217 1.00 18.33 C ANISOU 3043 C ALA C 78 1950 2669 2343 -304 240 -346 C ATOM 3044 O ALA C 78 -14.566 9.598 41.924 1.00 18.84 O ANISOU 3044 O ALA C 78 1932 2762 2462 -263 225 -425 O ATOM 3045 CB ALA C 78 -15.319 12.618 40.822 1.00 19.19 C ANISOU 3045 CB ALA C 78 2095 2673 2521 -487 567 -265 C ATOM 3046 N GLU C 79 -15.569 10.888 43.469 1.00 18.16 N ANISOU 3046 N GLU C 79 1941 2645 2312 -262 105 -369 N ATOM 3047 CA GLU C 79 -14.956 10.166 44.592 1.00 18.82 C ANISOU 3047 CA GLU C 79 1970 2763 2417 -146 -83 -476 C ATOM 3048 C GLU C 79 -15.440 8.693 44.647 1.00 18.15 C ANISOU 3048 C GLU C 79 1999 2693 2205 -46 -155 -395 C ATOM 3049 O GLU C 79 -14.656 7.773 44.911 1.00 18.91 O ANISOU 3049 O GLU C 79 2039 2801 2342 52 -255 -476 O ATOM 3050 CB GLU C 79 -15.242 10.916 45.903 1.00 19.03 C ANISOU 3050 CB GLU C 79 2030 2788 2410 -110 -202 -509 C ATOM 3051 CG GLU C 79 -14.592 10.332 47.142 1.00 20.25 C ANISOU 3051 CG GLU C 79 2159 2984 2548 39 -418 -625 C ATOM 3052 CD GLU C 79 -13.057 10.173 47.067 1.00 22.13 C ANISOU 3052 CD GLU C 79 2173 3249 2985 75 -490 -837 C ATOM 3053 OE1 GLU C 79 -12.351 10.799 46.223 1.00 22.95 O ANISOU 3053 OE1 GLU C 79 2104 3330 3284 -48 -348 -932 O ATOM 3054 OE2 GLU C 79 -12.540 9.404 47.897 1.00 23.26 O ANISOU 3054 OE2 GLU C 79 2315 3430 3091 240 -689 -918 O ATOM 3055 N TRP C 80 -16.728 8.479 44.389 1.00 16.93 N ANISOU 3055 N TRP C 80 1991 2523 1916 -69 -102 -249 N ATOM 3056 CA TRP C 80 -17.274 7.137 44.321 1.00 16.60 C ANISOU 3056 CA TRP C 80 2048 2468 1791 -9 -128 -182 C ATOM 3057 C TRP C 80 -16.538 6.326 43.237 1.00 17.12 C ANISOU 3057 C TRP C 80 2033 2540 1929 -7 -77 -241 C ATOM 3058 O TRP C 80 -16.126 5.194 43.470 1.00 17.55 O ANISOU 3058 O TRP C 80 2094 2574 2000 84 -151 -273 O ATOM 3059 CB TRP C 80 -18.773 7.175 44.039 1.00 15.58 C ANISOU 3059 CB TRP C 80 2037 2324 1558 -61 -59 -62 C ATOM 3060 CG TRP C 80 -19.378 5.836 43.934 1.00 15.53 C ANISOU 3060 CG TRP C 80 2111 2282 1507 -27 -60 -17 C ATOM 3061 CD1 TRP C 80 -19.430 5.056 42.823 1.00 15.53 C ANISOU 3061 CD1 TRP C 80 2091 2281 1528 -45 -7 -33 C ATOM 3062 CD2 TRP C 80 -20.001 5.084 44.985 1.00 15.78 C ANISOU 3062 CD2 TRP C 80 2265 2257 1474 28 -98 43 C ATOM 3063 NE1 TRP C 80 -20.063 3.881 43.104 1.00 15.67 N ANISOU 3063 NE1 TRP C 80 2192 2236 1527 -16 -16 0 N ATOM 3064 CE2 TRP C 80 -20.416 3.859 44.424 1.00 15.87 C ANISOU 3064 CE2 TRP C 80 2313 2215 1501 25 -55 58 C ATOM 3065 CE3 TRP C 80 -20.246 5.328 46.345 1.00 16.19 C ANISOU 3065 CE3 TRP C 80 2412 2289 1448 82 -148 82 C ATOM 3066 CZ2 TRP C 80 -21.064 2.861 45.173 1.00 16.51 C ANISOU 3066 CZ2 TRP C 80 2522 2200 1548 58 -38 123 C ATOM 3067 CZ3 TRP C 80 -20.913 4.336 47.103 1.00 16.83 C ANISOU 3067 CZ3 TRP C 80 2646 2289 1458 128 -125 162 C ATOM 3068 CH2 TRP C 80 -21.310 3.114 46.505 1.00 16.90 C ANISOU 3068 CH2 TRP C 80 2687 2223 1511 108 -59 187 C ATOM 3069 N ASP C 81 -16.360 6.931 42.069 1.00 17.17 N ANISOU 3069 N ASP C 81 1980 2568 1973 -97 57 -253 N ATOM 3070 CA ASP C 81 -15.738 6.263 40.963 1.00 17.86 C ANISOU 3070 CA ASP C 81 2005 2673 2107 -102 138 -312 C ATOM 3071 C ASP C 81 -14.270 5.929 41.223 1.00 19.26 C ANISOU 3071 C ASP C 81 2019 2857 2440 -48 92 -465 C ATOM 3072 O ASP C 81 -13.801 4.858 40.833 1.00 19.68 O ANISOU 3072 O ASP C 81 2035 2910 2532 12 79 -526 O ATOM 3073 CB ASP C 81 -15.905 7.089 39.694 1.00 17.99 C ANISOU 3073 CB ASP C 81 2037 2707 2088 -197 312 -274 C ATOM 3074 CG ASP C 81 -17.353 7.065 39.165 1.00 17.05 C ANISOU 3074 CG ASP C 81 2068 2598 1811 -206 324 -157 C ATOM 3075 OD1 ASP C 81 -18.092 6.117 39.443 1.00 16.53 O ANISOU 3075 OD1 ASP C 81 2057 2525 1697 -161 241 -137 O ATOM 3076 OD2 ASP C 81 -17.753 7.994 38.443 1.00 17.30 O ANISOU 3076 OD2 ASP C 81 2160 2637 1776 -251 421 -94 O ATOM 3077 N ARG C 82 -13.578 6.835 41.912 1.00 20.06 N ANISOU 3077 N ARG C 82 2011 2962 2647 -63 54 -548 N ATOM 3078 CA ARG C 82 -12.176 6.665 42.251 1.00 21.85 C ANISOU 3078 CA ARG C 82 2041 3206 3055 -7 -14 -736 C ATOM 3079 C ARG C 82 -11.982 5.507 43.225 1.00 22.51 C ANISOU 3079 C ARG C 82 2159 3284 3108 172 -235 -768 C ATOM 3080 O ARG C 82 -10.963 4.831 43.161 1.00 23.88 O ANISOU 3080 O ARG C 82 2198 3468 3405 261 -297 -908 O ATOM 3081 CB ARG C 82 -11.606 7.961 42.839 1.00 22.65 C ANISOU 3081 CB ARG C 82 2011 3307 3288 -68 -20 -843 C ATOM 3082 CG ARG C 82 -10.099 8.017 42.942 1.00 24.74 C ANISOU 3082 CG ARG C 82 2008 3592 3799 -49 -49 -1086 C ATOM 3083 CD ARG C 82 -9.651 9.279 43.656 1.00 25.73 C ANISOU 3083 CD ARG C 82 2001 3706 4068 -112 -79 -1216 C ATOM 3084 NE ARG C 82 -10.028 9.257 45.073 1.00 25.53 N ANISOU 3084 NE ARG C 82 2064 3705 3930 21 -337 -1216 N ATOM 3085 CZ ARG C 82 -9.404 8.559 46.027 1.00 26.77 C ANISOU 3085 CZ ARG C 82 2163 3908 4100 209 -592 -1348 C ATOM 3086 NH1 ARG C 82 -8.348 7.807 45.759 1.00 28.31 N ANISOU 3086 NH1 ARG C 82 2179 4129 4446 293 -647 -1510 N ATOM 3087 NH2 ARG C 82 -9.846 8.615 47.274 1.00 26.75 N ANISOU 3087 NH2 ARG C 82 2294 3926 3944 333 -797 -1322 N ATOM 3088 N THR C 83 -12.953 5.289 44.115 1.00 21.88 N ANISOU 3088 N THR C 83 2268 3179 2865 233 -338 -637 N ATOM 3089 CA THR C 83 -12.885 4.207 45.109 1.00 22.85 C ANISOU 3089 CA THR C 83 2495 3269 2918 416 -524 -623 C ATOM 3090 C THR C 83 -13.648 2.940 44.684 1.00 22.45 C ANISOU 3090 C THR C 83 2602 3149 2779 442 -474 -499 C ATOM 3091 O THR C 83 -13.399 1.864 45.240 1.00 23.43 O ANISOU 3091 O THR C 83 2805 3214 2881 596 -591 -493 O ATOM 3092 CB THR C 83 -13.393 4.669 46.501 1.00 22.85 C ANISOU 3092 CB THR C 83 2630 3269 2784 485 -653 -564 C ATOM 3093 OG1 THR C 83 -14.748 5.108 46.391 1.00 21.39 O ANISOU 3093 OG1 THR C 83 2587 3062 2476 369 -529 -405 O ATOM 3094 CG2 THR C 83 -12.542 5.800 47.038 1.00 23.84 C ANISOU 3094 CG2 THR C 83 2586 3455 3016 484 -741 -732 C ATOM 3095 N HIS C 84 -14.546 3.069 43.697 1.00 21.42 N ANISOU 3095 N HIS C 84 2515 3016 2606 304 -310 -414 N ATOM 3096 CA HIS C 84 -15.286 1.940 43.110 1.00 21.19 C ANISOU 3096 CA HIS C 84 2593 2924 2531 300 -249 -342 C ATOM 3097 C HIS C 84 -15.072 1.881 41.578 1.00 21.22 C ANISOU 3097 C HIS C 84 2498 2971 2592 214 -112 -409 C ATOM 3098 O HIS C 84 -15.999 2.102 40.786 1.00 20.37 O ANISOU 3098 O HIS C 84 2445 2882 2412 119 -10 -350 O ATOM 3099 CB HIS C 84 -16.790 2.048 43.407 1.00 20.21 C ANISOU 3099 CB HIS C 84 2629 2763 2284 233 -199 -199 C ATOM 3100 CG HIS C 84 -17.141 2.115 44.866 1.00 20.54 C ANISOU 3100 CG HIS C 84 2803 2762 2237 308 -286 -120 C ATOM 3101 ND1 HIS C 84 -16.688 3.111 45.701 1.00 20.94 N ANISOU 3101 ND1 HIS C 84 2820 2869 2267 340 -370 -153 N ATOM 3102 CD2 HIS C 84 -17.950 1.332 45.623 1.00 20.87 C ANISOU 3102 CD2 HIS C 84 3025 2707 2197 352 -281 -12 C ATOM 3103 CE1 HIS C 84 -17.179 2.919 46.917 1.00 21.37 C ANISOU 3103 CE1 HIS C 84 3039 2878 2202 419 -429 -69 C ATOM 3104 NE2 HIS C 84 -17.946 1.846 46.894 1.00 21.28 N ANISOU 3104 NE2 HIS C 84 3167 2767 2150 424 -360 28 N ATOM 3105 N PRO C 85 -13.845 1.567 41.140 1.00 22.40 N ANISOU 3105 N PRO C 85 2501 3143 2865 262 -112 -547 N ATOM 3106 CA PRO C 85 -13.601 1.576 39.697 1.00 22.58 C ANISOU 3106 CA PRO C 85 2448 3213 2916 184 45 -613 C ATOM 3107 C PRO C 85 -14.464 0.526 38.985 1.00 22.28 C ANISOU 3107 C PRO C 85 2521 3136 2807 184 81 -577 C ATOM 3108 O PRO C 85 -14.852 -0.470 39.604 1.00 22.53 O ANISOU 3108 O PRO C 85 2644 3076 2838 259 -8 -541 O ATOM 3109 CB PRO C 85 -12.103 1.267 39.581 1.00 24.25 C ANISOU 3109 CB PRO C 85 2470 3442 3299 255 31 -788 C ATOM 3110 CG PRO C 85 -11.728 0.601 40.845 1.00 24.99 C ANISOU 3110 CG PRO C 85 2578 3479 3437 416 -176 -808 C ATOM 3111 CD PRO C 85 -12.674 1.117 41.911 1.00 23.92 C ANISOU 3111 CD PRO C 85 2599 3320 3170 408 -258 -660 C ATOM 3112 N PRO C 86 -14.811 0.758 37.705 1.00 21.95 N ANISOU 3112 N PRO C 86 2489 3153 2698 103 215 -590 N ATOM 3113 CA PRO C 86 -15.763 -0.155 37.073 1.00 21.62 C ANISOU 3113 CA PRO C 86 2542 3083 2589 101 223 -585 C ATOM 3114 C PRO C 86 -15.108 -1.414 36.504 1.00 22.56 C ANISOU 3114 C PRO C 86 2610 3165 2794 172 232 -717 C ATOM 3115 O PRO C 86 -15.040 -1.588 35.301 1.00 23.37 O ANISOU 3115 O PRO C 86 2697 3326 2853 150 329 -800 O ATOM 3116 CB PRO C 86 -16.400 0.710 35.992 1.00 21.35 C ANISOU 3116 CB PRO C 86 2554 3141 2418 19 328 -554 C ATOM 3117 CG PRO C 86 -15.340 1.682 35.647 1.00 22.07 C ANISOU 3117 CG PRO C 86 2559 3289 2535 -13 441 -580 C ATOM 3118 CD PRO C 86 -14.656 2.000 36.934 1.00 21.98 C ANISOU 3118 CD PRO C 86 2463 3237 2651 9 355 -578 C ATOM 3119 N ALA C 87 -14.673 -2.302 37.393 1.00 22.71 N ANISOU 3119 N ALA C 87 2624 3082 2920 273 126 -734 N ATOM 3120 CA ALA C 87 -13.930 -3.496 37.010 1.00 23.72 C ANISOU 3120 CA ALA C 87 2697 3153 3161 367 117 -866 C ATOM 3121 C ALA C 87 -14.815 -4.400 36.168 1.00 23.51 C ANISOU 3121 C ALA C 87 2749 3081 3100 335 162 -906 C ATOM 3122 O ALA C 87 -15.990 -4.575 36.458 1.00 22.65 O ANISOU 3122 O ALA C 87 2750 2912 2943 286 140 -821 O ATOM 3123 CB ALA C 87 -13.456 -4.240 38.259 1.00 24.52 C ANISOU 3123 CB ALA C 87 2828 3128 3358 509 -29 -843 C ATOM 3124 N MET C 88 -14.248 -4.987 35.128 1.00 24.28 N ANISOU 3124 N MET C 88 2777 3208 3239 363 230 -1059 N ATOM 3125 CA MET C 88 -15.002 -5.899 34.297 1.00 24.48 C ANISOU 3125 CA MET C 88 2860 3193 3246 345 257 -1142 C ATOM 3126 C MET C 88 -15.323 -7.206 35.019 1.00 24.71 C ANISOU 3126 C MET C 88 2963 3017 3407 409 177 -1136 C ATOM 3127 O MET C 88 -14.521 -7.703 35.804 1.00 25.36 O ANISOU 3127 O MET C 88 3034 2998 3602 523 110 -1126 O ATOM 3128 CB MET C 88 -14.243 -6.184 33.015 1.00 25.97 C ANISOU 3128 CB MET C 88 2965 3469 3432 370 359 -1322 C ATOM 3129 CG MET C 88 -14.411 -5.093 31.967 1.00 25.86 C ANISOU 3129 CG MET C 88 2962 3632 3229 292 479 -1319 C ATOM 3130 SD MET C 88 -13.860 -5.685 30.358 1.00 27.91 S ANISOU 3130 SD MET C 88 3189 3981 3431 329 615 -1538 S ATOM 3131 CE MET C 88 -14.099 -4.172 29.399 1.00 27.75 C ANISOU 3131 CE MET C 88 3252 4146 3143 253 760 -1454 C ATOM 3132 N GLY C 89 -16.514 -7.742 34.733 1.00 24.28 N ANISOU 3132 N GLY C 89 2985 2895 3344 341 187 -1151 N ATOM 3133 CA GLY C 89 -16.958 -9.061 35.207 1.00 24.94 C ANISOU 3133 CA GLY C 89 3149 2753 3574 370 164 -1165 C ATOM 3134 C GLY C 89 -16.154 -10.161 34.553 1.00 26.37 C ANISOU 3134 C GLY C 89 3279 2862 3878 464 176 -1343 C ATOM 3135 O GLY C 89 -15.135 -9.884 33.933 1.00 26.70 O ANISOU 3135 O GLY C 89 3215 3031 3898 519 199 -1441 O ATOM 3136 N PRO C 90 -16.625 -11.417 34.625 1.00 27.37 N ANISOU 3136 N PRO C 90 3473 2777 4149 474 182 -1402 N ATOM 3137 CA PRO C 90 -17.942 -11.890 35.020 1.00 27.37 C ANISOU 3137 CA PRO C 90 3569 2615 4212 372 211 -1352 C ATOM 3138 C PRO C 90 -18.215 -11.978 36.521 1.00 27.09 C ANISOU 3138 C PRO C 90 3681 2399 4211 391 205 -1126 C ATOM 3139 O PRO C 90 -17.308 -12.119 37.331 1.00 27.40 O ANISOU 3139 O PRO C 90 3780 2365 4264 532 148 -1027 O ATOM 3140 CB PRO C 90 -18.017 -13.278 34.382 1.00 29.42 C ANISOU 3140 CB PRO C 90 3825 2702 4649 390 244 -1546 C ATOM 3141 CG PRO C 90 -16.606 -13.744 34.321 1.00 30.48 C ANISOU 3141 CG PRO C 90 3925 2808 4846 557 210 -1605 C ATOM 3142 CD PRO C 90 -15.760 -12.516 34.158 1.00 29.18 C ANISOU 3142 CD PRO C 90 3662 2904 4521 590 183 -1567 C ATOM 3143 N LEU C 91 -19.494 -11.882 36.862 1.00 26.66 N ANISOU 3143 N LEU C 91 3683 2280 4165 258 265 -1061 N ATOM 3144 CA LEU C 91 -19.933 -11.951 38.245 1.00 26.77 C ANISOU 3144 CA LEU C 91 3860 2121 4190 255 304 -847 C ATOM 3145 C LEU C 91 -20.440 -13.357 38.616 1.00 28.96 C ANISOU 3145 C LEU C 91 4268 2066 4669 237 408 -848 C ATOM 3146 O LEU C 91 -20.914 -14.094 37.766 1.00 29.91 O ANISOU 3146 O LEU C 91 4315 2110 4937 157 460 -1037 O ATOM 3147 CB LEU C 91 -20.999 -10.879 38.513 1.00 25.21 C ANISOU 3147 CB LEU C 91 3642 2052 3885 117 336 -764 C ATOM 3148 CG LEU C 91 -20.507 -9.442 38.261 1.00 23.27 C ANISOU 3148 CG LEU C 91 3299 2092 3448 137 251 -735 C ATOM 3149 CD1 LEU C 91 -21.535 -8.374 38.661 1.00 21.91 C ANISOU 3149 CD1 LEU C 91 3125 2020 3178 26 276 -640 C ATOM 3150 CD2 LEU C 91 -19.192 -9.187 38.977 1.00 23.19 C ANISOU 3150 CD2 LEU C 91 3330 2102 3379 292 168 -635 C ATOM 3151 N PRO C 92 -20.309 -13.732 39.902 1.00 30.02 N ANISOU 3151 N PRO C 92 4611 1990 4804 322 443 -638 N ATOM 3152 CA PRO C 92 -20.891 -14.970 40.444 1.00 32.44 C ANISOU 3152 CA PRO C 92 5097 1939 5290 292 592 -581 C ATOM 3153 C PRO C 92 -22.415 -14.939 40.417 1.00 32.62 C ANISOU 3153 C PRO C 92 5087 1896 5411 57 758 -614 C ATOM 3154 O PRO C 92 -22.980 -13.872 40.272 1.00 30.78 O ANISOU 3154 O PRO C 92 4736 1892 5066 -41 735 -624 O ATOM 3155 CB PRO C 92 -20.400 -15.007 41.898 1.00 33.23 C ANISOU 3155 CB PRO C 92 5456 1898 5271 458 578 -309 C ATOM 3156 CG PRO C 92 -19.334 -13.983 42.001 1.00 31.54 C ANISOU 3156 CG PRO C 92 5157 1962 4865 602 382 -285 C ATOM 3157 CD PRO C 92 -19.636 -12.945 40.954 1.00 29.21 C ANISOU 3157 CD PRO C 92 4605 1975 4518 453 350 -441 C ATOM 3158 N PRO C 93 -23.070 -16.100 40.572 1.00 35.15 N ANISOU 3158 N PRO C 93 5504 1890 5960 -27 931 -641 N ATOM 3159 CA PRO C 93 -24.499 -16.144 40.283 1.00 35.74 C ANISOU 3159 CA PRO C 93 5464 1918 6196 -268 1083 -766 C ATOM 3160 C PRO C 93 -25.310 -15.269 41.199 1.00 35.01 C ANISOU 3160 C PRO C 93 5423 1885 5991 -362 1177 -594 C ATOM 3161 O PRO C 93 -24.960 -15.090 42.360 1.00 35.02 O ANISOU 3161 O PRO C 93 5651 1810 5846 -259 1213 -335 O ATOM 3162 CB PRO C 93 -24.875 -17.611 40.481 1.00 38.89 C ANISOU 3162 CB PRO C 93 5992 1900 6885 -330 1282 -798 C ATOM 3163 CG PRO C 93 -23.624 -18.350 40.579 1.00 39.89 C ANISOU 3163 CG PRO C 93 6270 1887 6999 -109 1198 -734 C ATOM 3164 CD PRO C 93 -22.548 -17.413 40.984 1.00 37.80 C ANISOU 3164 CD PRO C 93 6047 1876 6440 92 1000 -575 C ATOM 3165 N GLY C 94 -26.362 -14.688 40.634 1.00 34.54 N ANISOU 3165 N GLY C 94 5148 1986 5987 -536 1194 -758 N ATOM 3166 CA GLY C 94 -27.302 -13.854 41.375 1.00 34.15 C ANISOU 3166 CA GLY C 94 5099 2001 5876 -647 1296 -649 C ATOM 3167 C GLY C 94 -26.805 -12.453 41.646 1.00 31.70 C ANISOU 3167 C GLY C 94 4780 1996 5265 -542 1133 -516 C ATOM 3168 O GLY C 94 -27.589 -11.572 42.007 1.00 30.82 O ANISOU 3168 O GLY C 94 4612 2004 5093 -629 1174 -479 O ATOM 3169 N GLN C 95 -25.510 -12.234 41.452 1.00 30.93 N ANISOU 3169 N GLN C 95 4721 2023 5006 -361 955 -466 N ATOM 3170 CA GLN C 95 -24.947 -10.921 41.689 1.00 28.96 C ANISOU 3170 CA GLN C 95 4453 2043 4505 -270 809 -361 C ATOM 3171 C GLN C 95 -25.184 -9.982 40.521 1.00 27.47 C ANISOU 3171 C GLN C 95 4028 2148 4259 -325 686 -536 C ATOM 3172 O GLN C 95 -25.240 -10.397 39.373 1.00 27.79 O ANISOU 3172 O GLN C 95 3935 2232 4392 -353 640 -743 O ATOM 3173 CB GLN C 95 -23.457 -11.004 41.938 1.00 28.83 C ANISOU 3173 CB GLN C 95 4537 2046 4368 -62 673 -270 C ATOM 3174 CG GLN C 95 -23.086 -11.562 43.275 1.00 30.39 C ANISOU 3174 CG GLN C 95 5009 2017 4521 59 733 -50 C ATOM 3175 CD GLN C 95 -21.626 -11.287 43.628 1.00 30.12 C ANISOU 3175 CD GLN C 95 5032 2078 4334 288 541 22 C ATOM 3176 OE1 GLN C 95 -21.001 -12.081 44.321 1.00 32.13 O ANISOU 3176 OE1 GLN C 95 5486 2136 4584 451 527 131 O ATOM 3177 NE2 GLN C 95 -21.072 -10.178 43.140 1.00 28.11 N ANISOU 3177 NE2 GLN C 95 4601 2111 3969 308 396 -48 N ATOM 3178 N ILE C 96 -25.298 -8.703 40.835 1.00 26.10 N ANISOU 3178 N ILE C 96 3826 2172 3917 -322 630 -448 N ATOM 3179 CA ILE C 96 -25.454 -7.713 39.801 1.00 24.92 C ANISOU 3179 CA ILE C 96 3502 2288 3679 -344 516 -571 C ATOM 3180 C ILE C 96 -24.341 -6.709 39.888 1.00 23.58 C ANISOU 3180 C ILE C 96 3348 2296 3313 -228 400 -471 C ATOM 3181 O ILE C 96 -23.615 -6.599 40.864 1.00 23.36 O ANISOU 3181 O ILE C 96 3440 2218 3214 -140 388 -319 O ATOM 3182 CB ILE C 96 -26.851 -7.027 39.843 1.00 24.67 C ANISOU 3182 CB ILE C 96 3372 2326 3673 -470 562 -615 C ATOM 3183 CG1 ILE C 96 -26.996 -6.116 41.068 1.00 23.80 C ANISOU 3183 CG1 ILE C 96 3359 2239 3445 -463 605 -416 C ATOM 3184 CG2 ILE C 96 -27.946 -8.094 39.799 1.00 26.68 C ANISOU 3184 CG2 ILE C 96 3576 2381 4177 -604 699 -749 C ATOM 3185 CD1 ILE C 96 -28.412 -5.479 41.224 1.00 23.85 C ANISOU 3185 CD1 ILE C 96 3261 2295 3505 -582 670 -466 C ATOM 3186 N ARG C 97 -24.245 -5.965 38.822 1.00 23.15 N ANISOU 3186 N ARG C 97 3173 2448 3174 -227 316 -573 N ATOM 3187 CA ARG C 97 -23.189 -5.023 38.602 1.00 22.42 C ANISOU 3187 CA ARG C 97 3063 2521 2932 -144 236 -523 C ATOM 3188 C ARG C 97 -23.322 -3.804 39.523 1.00 21.19 C ANISOU 3188 C ARG C 97 2945 2437 2667 -149 226 -372 C ATOM 3189 O ARG C 97 -24.416 -3.336 39.751 1.00 20.82 O ANISOU 3189 O ARG C 97 2883 2407 2618 -224 258 -355 O ATOM 3190 CB ARG C 97 -23.325 -4.616 37.140 1.00 22.69 C ANISOU 3190 CB ARG C 97 2991 2728 2898 -155 191 -671 C ATOM 3191 CG ARG C 97 -22.244 -3.804 36.621 1.00 22.34 C ANISOU 3191 CG ARG C 97 2927 2834 2728 -90 159 -652 C ATOM 3192 CD ARG C 97 -21.410 -4.502 35.560 1.00 23.54 C ANISOU 3192 CD ARG C 97 3039 3013 2893 -35 162 -794 C ATOM 3193 NE ARG C 97 -20.232 -3.675 35.582 1.00 23.33 N ANISOU 3193 NE ARG C 97 2995 3080 2786 14 171 -731 N ATOM 3194 CZ ARG C 97 -18.999 -4.064 35.825 1.00 23.82 C ANISOU 3194 CZ ARG C 97 3032 3102 2914 85 174 -745 C ATOM 3195 NH1 ARG C 97 -18.692 -5.352 35.905 1.00 24.98 N ANISOU 3195 NH1 ARG C 97 3185 3116 3187 138 165 -821 N ATOM 3196 NH2 ARG C 97 -18.071 -3.121 35.907 1.00 23.53 N ANISOU 3196 NH2 ARG C 97 2950 3158 2831 105 190 -703 N ATOM 3197 N GLU C 98 -22.211 -3.300 40.048 1.00 20.80 N ANISOU 3197 N GLU C 98 2927 2428 2545 -65 178 -288 N ATOM 3198 CA GLU C 98 -22.241 -2.116 40.930 1.00 19.97 C ANISOU 3198 CA GLU C 98 2853 2391 2344 -63 158 -171 C ATOM 3199 C GLU C 98 -22.496 -0.789 40.176 1.00 18.42 C ANISOU 3199 C GLU C 98 2571 2366 2061 -109 141 -194 C ATOM 3200 O GLU C 98 -22.051 -0.597 39.056 1.00 18.45 O ANISOU 3200 O GLU C 98 2510 2463 2037 -100 131 -272 O ATOM 3201 CB GLU C 98 -20.955 -2.014 41.789 1.00 20.76 C ANISOU 3201 CB GLU C 98 2997 2476 2412 50 89 -110 C ATOM 3202 CG GLU C 98 -21.037 -2.775 43.132 1.00 22.21 C ANISOU 3202 CG GLU C 98 3345 2495 2596 119 96 -2 C ATOM 3203 CD GLU C 98 -20.170 -2.150 44.231 1.00 22.87 C ANISOU 3203 CD GLU C 98 3483 2617 2587 233 -3 65 C ATOM 3204 OE1 GLU C 98 -20.682 -1.322 45.044 1.00 22.82 O ANISOU 3204 OE1 GLU C 98 3532 2646 2490 210 5 142 O ATOM 3205 OE2 GLU C 98 -18.958 -2.484 44.292 1.00 24.23 O ANISOU 3205 OE2 GLU C 98 3630 2788 2787 357 -102 19 O ATOM 3206 N PRO C 99 -23.231 0.143 40.796 1.00 17.26 N ANISOU 3206 N PRO C 99 2443 2251 1863 -148 150 -120 N ATOM 3207 CA PRO C 99 -23.472 1.414 40.102 1.00 16.11 C ANISOU 3207 CA PRO C 99 2242 2240 1638 -170 132 -127 C ATOM 3208 C PRO C 99 -22.204 2.282 40.024 1.00 15.36 C ANISOU 3208 C PRO C 99 2126 2214 1495 -131 113 -102 C ATOM 3209 O PRO C 99 -21.354 2.216 40.912 1.00 15.15 O ANISOU 3209 O PRO C 99 2116 2149 1492 -87 85 -71 O ATOM 3210 CB PRO C 99 -24.476 2.094 41.002 1.00 15.84 C ANISOU 3210 CB PRO C 99 2234 2193 1588 -208 149 -60 C ATOM 3211 CG PRO C 99 -24.052 1.625 42.390 1.00 16.25 C ANISOU 3211 CG PRO C 99 2378 2142 1652 -175 164 19 C ATOM 3212 CD PRO C 99 -23.631 0.198 42.210 1.00 17.22 C ANISOU 3212 CD PRO C 99 2531 2163 1849 -148 177 -16 C ATOM 3213 N THR C 100 -22.095 3.081 38.962 1.00 14.84 N ANISOU 3213 N THR C 100 2028 2242 1366 -142 131 -124 N ATOM 3214 CA THR C 100 -21.093 4.133 38.904 1.00 14.55 C ANISOU 3214 CA THR C 100 1968 2251 1308 -138 158 -97 C ATOM 3215 C THR C 100 -21.631 5.346 39.682 1.00 13.76 C ANISOU 3215 C THR C 100 1893 2152 1180 -162 146 -17 C ATOM 3216 O THR C 100 -22.771 5.338 40.117 1.00 13.41 O ANISOU 3216 O THR C 100 1880 2091 1122 -175 124 9 O ATOM 3217 CB THR C 100 -20.816 4.555 37.462 1.00 15.04 C ANISOU 3217 CB THR C 100 2029 2387 1296 -141 225 -128 C ATOM 3218 OG1 THR C 100 -21.968 5.235 36.961 1.00 14.89 O ANISOU 3218 OG1 THR C 100 2066 2411 1180 -142 211 -91 O ATOM 3219 CG2 THR C 100 -20.464 3.329 36.566 1.00 15.72 C ANISOU 3219 CG2 THR C 100 2095 2485 1392 -112 240 -232 C ATOM 3220 N GLY C 101 -20.827 6.390 39.837 1.00 13.63 N ANISOU 3220 N GLY C 101 1852 2149 1176 -175 174 0 N ATOM 3221 CA GLY C 101 -21.277 7.617 40.507 1.00 13.14 C ANISOU 3221 CA GLY C 101 1812 2078 1100 -196 168 58 C ATOM 3222 C GLY C 101 -22.398 8.325 39.760 1.00 12.91 C ANISOU 3222 C GLY C 101 1836 2075 991 -200 188 103 C ATOM 3223 O GLY C 101 -23.343 8.830 40.347 1.00 12.52 O ANISOU 3223 O GLY C 101 1809 2015 931 -200 157 136 O ATOM 3224 N SER C 102 -22.294 8.355 38.451 1.00 13.43 N ANISOU 3224 N SER C 102 1928 2180 992 -187 235 98 N ATOM 3225 CA SER C 102 -23.352 8.918 37.635 1.00 13.69 C ANISOU 3225 CA SER C 102 2030 2248 922 -149 219 131 C ATOM 3226 C SER C 102 -24.612 8.045 37.641 1.00 13.45 C ANISOU 3226 C SER C 102 1975 2246 890 -125 129 71 C ATOM 3227 O SER C 102 -25.683 8.566 37.388 1.00 13.69 O ANISOU 3227 O SER C 102 2024 2302 876 -84 77 75 O ATOM 3228 CB SER C 102 -22.858 9.165 36.213 1.00 14.77 C ANISOU 3228 CB SER C 102 2238 2422 949 -118 297 144 C ATOM 3229 OG SER C 102 -22.775 7.964 35.487 1.00 15.19 O ANISOU 3229 OG SER C 102 2276 2526 969 -94 280 59 O ATOM 3230 N ASP C 103 -24.492 6.744 37.950 1.00 13.21 N ANISOU 3230 N ASP C 103 1895 2195 928 -147 114 6 N ATOM 3231 CA ASP C 103 -25.679 5.878 38.131 1.00 13.32 C ANISOU 3231 CA ASP C 103 1867 2199 995 -156 65 -64 C ATOM 3232 C ASP C 103 -26.427 6.214 39.425 1.00 12.86 C ANISOU 3232 C ASP C 103 1794 2090 1000 -190 69 -25 C ATOM 3233 O ASP C 103 -27.657 6.284 39.442 1.00 13.23 O ANISOU 3233 O ASP C 103 1798 2149 1078 -192 42 -72 O ATOM 3234 CB ASP C 103 -25.313 4.387 38.173 1.00 13.55 C ANISOU 3234 CB ASP C 103 1868 2178 1099 -178 78 -134 C ATOM 3235 CG ASP C 103 -24.885 3.834 36.817 1.00 14.31 C ANISOU 3235 CG ASP C 103 1965 2331 1140 -142 71 -219 C ATOM 3236 OD1 ASP C 103 -25.252 4.405 35.758 1.00 14.75 O ANISOU 3236 OD1 ASP C 103 2049 2473 1080 -93 40 -242 O ATOM 3237 OD2 ASP C 103 -24.177 2.801 36.842 1.00 14.48 O ANISOU 3237 OD2 ASP C 103 1972 2306 1224 -148 95 -264 O ATOM 3238 N ILE C 104 -25.673 6.393 40.507 1.00 12.29 N ANISOU 3238 N ILE C 104 1750 1969 950 -207 100 39 N ATOM 3239 CA ILE C 104 -26.223 6.804 41.795 1.00 12.02 C ANISOU 3239 CA ILE C 104 1731 1895 940 -225 117 80 C ATOM 3240 C ILE C 104 -26.941 8.155 41.717 1.00 11.97 C ANISOU 3240 C ILE C 104 1716 1925 906 -210 101 99 C ATOM 3241 O ILE C 104 -28.016 8.315 42.330 1.00 12.13 O ANISOU 3241 O ILE C 104 1713 1934 962 -223 116 82 O ATOM 3242 CB ILE C 104 -25.119 6.841 42.885 1.00 11.79 C ANISOU 3242 CB ILE C 104 1748 1827 905 -213 120 127 C ATOM 3243 CG1 ILE C 104 -24.649 5.409 43.227 1.00 12.19 C ANISOU 3243 CG1 ILE C 104 1831 1814 986 -199 126 118 C ATOM 3244 CG2 ILE C 104 -25.607 7.558 44.111 1.00 11.68 C ANISOU 3244 CG2 ILE C 104 1770 1795 873 -214 132 162 C ATOM 3245 CD1 ILE C 104 -23.288 5.341 43.911 1.00 12.36 C ANISOU 3245 CD1 ILE C 104 1879 1819 995 -143 80 132 C ATOM 3246 N ALA C 105 -26.373 9.120 40.978 1.00 11.97 N ANISOU 3246 N ALA C 105 1739 1956 853 -181 90 131 N ATOM 3247 CA ALA C 105 -26.985 10.455 40.873 1.00 12.21 C ANISOU 3247 CA ALA C 105 1788 1993 859 -148 75 163 C ATOM 3248 C ALA C 105 -28.223 10.495 39.984 1.00 12.90 C ANISOU 3248 C ALA C 105 1852 2129 919 -90 13 115 C ATOM 3249 O ALA C 105 -28.881 11.515 39.917 1.00 13.19 O ANISOU 3249 O ALA C 105 1902 2167 942 -37 -17 132 O ATOM 3250 CB ALA C 105 -25.955 11.524 40.396 1.00 12.42 C ANISOU 3250 CB ALA C 105 1870 1997 850 -141 116 225 C ATOM 3251 N GLY C 106 -28.531 9.379 39.321 1.00 13.43 N ANISOU 3251 N GLY C 106 1878 2234 989 -88 -17 37 N ATOM 3252 CA GLY C 106 -29.651 9.283 38.384 1.00 14.52 C ANISOU 3252 CA GLY C 106 1972 2437 1106 -18 -110 -54 C ATOM 3253 C GLY C 106 -29.370 9.842 37.008 1.00 15.49 C ANISOU 3253 C GLY C 106 2192 2617 1075 85 -163 -24 C ATOM 3254 O GLY C 106 -30.282 9.956 36.174 1.00 16.76 O ANISOU 3254 O GLY C 106 2342 2844 1180 188 -276 -99 O ATOM 3255 N THR C 107 -28.117 10.173 36.727 1.00 15.36 N ANISOU 3255 N THR C 107 2274 2575 985 70 -80 73 N ATOM 3256 CA THR C 107 -27.786 10.734 35.413 1.00 16.60 C ANISOU 3256 CA THR C 107 2564 2769 974 165 -80 125 C ATOM 3257 C THR C 107 -27.839 9.663 34.298 1.00 17.56 C ANISOU 3257 C THR C 107 2688 2977 1006 213 -134 20 C ATOM 3258 O THR C 107 -28.385 9.907 33.223 1.00 18.97 O ANISOU 3258 O THR C 107 2948 3226 1032 344 -224 -6 O ATOM 3259 CB THR C 107 -26.399 11.436 35.429 1.00 16.47 C ANISOU 3259 CB THR C 107 2638 2683 936 112 70 246 C ATOM 3260 OG1 THR C 107 -26.301 12.267 36.597 1.00 15.76 O ANISOU 3260 OG1 THR C 107 2516 2512 960 53 107 300 O ATOM 3261 CG2 THR C 107 -26.196 12.277 34.197 1.00 17.91 C ANISOU 3261 CG2 THR C 107 2997 2866 939 210 117 337 C ATOM 3262 N THR C 108 -27.286 8.481 34.577 1.00 17.05 N ANISOU 3262 N THR C 108 2544 2903 1031 125 -92 -47 N ATOM 3263 CA THR C 108 -27.114 7.422 33.581 1.00 17.91 C ANISOU 3263 CA THR C 108 2653 3076 1076 156 -119 -159 C ATOM 3264 C THR C 108 -27.785 6.088 33.980 1.00 17.91 C ANISOU 3264 C THR C 108 2507 3065 1231 99 -180 -314 C ATOM 3265 O THR C 108 -27.477 5.053 33.418 1.00 18.49 O ANISOU 3265 O THR C 108 2560 3157 1307 94 -181 -417 O ATOM 3266 CB THR C 108 -25.613 7.141 33.384 1.00 17.67 C ANISOU 3266 CB THR C 108 2666 3020 1027 104 19 -112 C ATOM 3267 OG1 THR C 108 -25.037 6.851 34.661 1.00 16.33 O ANISOU 3267 OG1 THR C 108 2411 2766 1028 0 75 -82 O ATOM 3268 CG2 THR C 108 -24.902 8.333 32.766 1.00 18.32 C ANISOU 3268 CG2 THR C 108 2894 3099 968 143 126 18 C ATOM 3269 N SER C 109 -28.689 6.099 34.948 1.00 17.66 N ANISOU 3269 N SER C 109 2379 2990 1340 51 -208 -337 N ATOM 3270 CA SER C 109 -29.379 4.878 35.353 1.00 18.04 C ANISOU 3270 CA SER C 109 2298 2995 1559 -20 -220 -478 C ATOM 3271 C SER C 109 -30.855 5.126 35.193 1.00 19.24 C ANISOU 3271 C SER C 109 2346 3197 1767 22 -331 -604 C ATOM 3272 O SER C 109 -31.318 6.224 35.440 1.00 19.12 O ANISOU 3272 O SER C 109 2345 3202 1714 74 -365 -539 O ATOM 3273 CB SER C 109 -29.066 4.517 36.795 1.00 16.93 C ANISOU 3273 CB SER C 109 2139 2735 1559 -130 -107 -398 C ATOM 3274 OG SER C 109 -29.416 5.562 37.678 1.00 16.29 O ANISOU 3274 OG SER C 109 2067 2638 1484 -137 -87 -303 O ATOM 3275 N THR C 110 -31.591 4.113 34.762 1.00 20.74 N ANISOU 3275 N THR C 110 2416 3401 2064 6 -393 -805 N ATOM 3276 CA THR C 110 -33.020 4.270 34.523 1.00 22.34 C ANISOU 3276 CA THR C 110 2472 3662 2354 54 -518 -982 C ATOM 3277 C THR C 110 -33.687 4.019 35.862 1.00 22.06 C ANISOU 3277 C THR C 110 2314 3513 2553 -84 -395 -991 C ATOM 3278 O THR C 110 -33.052 3.516 36.766 1.00 21.06 O ANISOU 3278 O THR C 110 2239 3271 2489 -195 -239 -880 O ATOM 3279 CB THR C 110 -33.544 3.246 33.507 1.00 24.23 C ANISOU 3279 CB THR C 110 2603 3960 2644 84 -636 -1241 C ATOM 3280 OG1 THR C 110 -33.573 1.962 34.136 1.00 24.40 O ANISOU 3280 OG1 THR C 110 2523 3847 2899 -78 -507 -1325 O ATOM 3281 CG2 THR C 110 -32.652 3.171 32.252 1.00 24.70 C ANISOU 3281 CG2 THR C 110 2814 4112 2457 199 -704 -1230 C ATOM 3282 N LEU C 111 -34.968 4.331 35.993 1.00 23.44 N ANISOU 3282 N LEU C 111 2330 3719 2854 -67 -459 -1132 N ATOM 3283 CA LEU C 111 -35.692 3.972 37.217 1.00 23.79 C ANISOU 3283 CA LEU C 111 2249 3651 3139 -214 -301 -1169 C ATOM 3284 C LEU C 111 -35.619 2.464 37.445 1.00 24.53 C ANISOU 3284 C LEU C 111 2287 3619 3414 -362 -170 -1262 C ATOM 3285 O LEU C 111 -35.363 2.014 38.547 1.00 24.04 O ANISOU 3285 O LEU C 111 2280 3415 3436 -484 27 -1148 O ATOM 3286 CB LEU C 111 -37.151 4.435 37.163 1.00 25.44 C ANISOU 3286 CB LEU C 111 2245 3922 3497 -173 -392 -1368 C ATOM 3287 CG LEU C 111 -38.046 3.947 38.311 1.00 26.25 C ANISOU 3287 CG LEU C 111 2183 3905 3883 -341 -194 -1457 C ATOM 3288 CD1 LEU C 111 -37.666 4.633 39.614 1.00 24.62 C ANISOU 3288 CD1 LEU C 111 2110 3626 3616 -389 -21 -1223 C ATOM 3289 CD2 LEU C 111 -39.548 4.129 37.961 1.00 28.64 C ANISOU 3289 CD2 LEU C 111 2202 4284 4396 -301 -308 -1753 C ATOM 3290 N GLN C 112 -35.822 1.680 36.393 1.00 26.25 N ANISOU 3290 N GLN C 112 2416 3878 3679 -338 -281 -1468 N ATOM 3291 CA GLN C 112 -35.758 0.223 36.539 1.00 27.23 C ANISOU 3291 CA GLN C 112 2488 3857 3999 -478 -154 -1572 C ATOM 3292 C GLN C 112 -34.414 -0.251 37.104 1.00 25.42 C ANISOU 3292 C GLN C 112 2470 3511 3677 -523 -13 -1339 C ATOM 3293 O GLN C 112 -34.383 -1.093 37.993 1.00 25.54 O ANISOU 3293 O GLN C 112 2507 3347 3849 -651 176 -1294 O ATOM 3294 CB GLN C 112 -36.099 -0.498 35.226 1.00 29.30 C ANISOU 3294 CB GLN C 112 2627 4195 4311 -428 -322 -1856 C ATOM 3295 CG GLN C 112 -37.486 -0.188 34.659 1.00 31.66 C ANISOU 3295 CG GLN C 112 2682 4610 4736 -369 -496 -2146 C ATOM 3296 CD GLN C 112 -38.636 -0.385 35.661 1.00 33.16 C ANISOU 3296 CD GLN C 112 2659 4682 5257 -528 -333 -2261 C ATOM 3297 OE1 GLN C 112 -39.179 0.598 36.219 1.00 33.26 O ANISOU 3297 OE1 GLN C 112 2629 4740 5266 -495 -327 -2200 O ATOM 3298 NE2 GLN C 112 -39.047 -1.647 35.867 1.00 34.88 N ANISOU 3298 NE2 GLN C 112 2737 4740 5777 -702 -184 -2444 N ATOM 3299 N GLU C 113 -33.310 0.299 36.618 1.00 24.07 N ANISOU 3299 N GLU C 113 2455 3430 3257 -412 -95 -1193 N ATOM 3300 CA GLU C 113 -31.992 -0.055 37.171 1.00 22.75 C ANISOU 3300 CA GLU C 113 2458 3170 3016 -434 13 -996 C ATOM 3301 C GLU C 113 -31.836 0.337 38.643 1.00 21.46 C ANISOU 3301 C GLU C 113 2380 2909 2864 -490 156 -797 C ATOM 3302 O GLU C 113 -31.249 -0.417 39.416 1.00 21.21 O ANISOU 3302 O GLU C 113 2443 2735 2877 -541 279 -700 O ATOM 3303 CB GLU C 113 -30.868 0.543 36.334 1.00 22.14 C ANISOU 3303 CB GLU C 113 2498 3213 2698 -314 -82 -907 C ATOM 3304 CG GLU C 113 -30.765 -0.108 34.959 1.00 23.66 C ANISOU 3304 CG GLU C 113 2658 3480 2849 -255 -186 -1088 C ATOM 3305 CD GLU C 113 -29.891 0.665 34.002 1.00 23.63 C ANISOU 3305 CD GLU C 113 2774 3615 2587 -130 -260 -1014 C ATOM 3306 OE1 GLU C 113 -29.953 1.921 34.012 1.00 23.50 O ANISOU 3306 OE1 GLU C 113 2816 3678 2435 -64 -297 -896 O ATOM 3307 OE2 GLU C 113 -29.142 0.020 33.213 1.00 24.56 O ANISOU 3307 OE2 GLU C 113 2935 3754 2643 -96 -265 -1076 O ATOM 3308 N GLN C 114 -32.374 1.497 39.035 1.00 20.75 N ANISOU 3308 N GLN C 114 2268 2891 2724 -463 134 -745 N ATOM 3309 CA GLN C 114 -32.289 1.962 40.435 1.00 19.75 C ANISOU 3309 CA GLN C 114 2225 2690 2587 -503 261 -580 C ATOM 3310 C GLN C 114 -33.067 1.006 41.343 1.00 20.93 C ANISOU 3310 C GLN C 114 2336 2679 2937 -632 448 -624 C ATOM 3311 O GLN C 114 -32.585 0.618 42.397 1.00 20.75 O ANISOU 3311 O GLN C 114 2454 2534 2894 -666 584 -480 O ATOM 3312 CB GLN C 114 -32.856 3.388 40.579 1.00 19.24 C ANISOU 3312 CB GLN C 114 2122 2730 2456 -447 199 -556 C ATOM 3313 CG GLN C 114 -32.044 4.457 39.886 1.00 18.14 C ANISOU 3313 CG GLN C 114 2066 2706 2120 -331 68 -467 C ATOM 3314 CD GLN C 114 -32.806 5.763 39.573 1.00 18.30 C ANISOU 3314 CD GLN C 114 2034 2823 2094 -246 -31 -493 C ATOM 3315 OE1 GLN C 114 -33.784 6.145 40.239 1.00 18.68 O ANISOU 3315 OE1 GLN C 114 1996 2858 2243 -271 8 -539 O ATOM 3316 NE2 GLN C 114 -32.330 6.459 38.556 1.00 18.06 N ANISOU 3316 NE2 GLN C 114 2072 2881 1908 -136 -147 -459 N ATOM 3317 N ILE C 115 -34.279 0.644 40.926 1.00 22.42 N ANISOU 3317 N ILE C 115 2337 2864 3318 -696 457 -833 N ATOM 3318 CA ILE C 115 -35.107 -0.311 41.668 1.00 24.18 C ANISOU 3318 CA ILE C 115 2496 2911 3777 -845 675 -906 C ATOM 3319 C ILE C 115 -34.386 -1.665 41.796 1.00 24.62 C ANISOU 3319 C ILE C 115 2677 2791 3887 -899 783 -854 C ATOM 3320 O ILE C 115 -34.358 -2.260 42.878 1.00 25.41 O ANISOU 3320 O ILE C 115 2905 2708 4040 -975 999 -733 O ATOM 3321 CB ILE C 115 -36.500 -0.493 40.993 1.00 26.19 C ANISOU 3321 CB ILE C 115 2471 3204 4275 -905 638 -1203 C ATOM 3322 CG1 ILE C 115 -37.370 0.749 41.213 1.00 26.19 C ANISOU 3322 CG1 ILE C 115 2351 3329 4271 -859 585 -1247 C ATOM 3323 CG2 ILE C 115 -37.240 -1.725 41.542 1.00 28.47 C ANISOU 3323 CG2 ILE C 115 2678 3276 4863 -1090 892 -1316 C ATOM 3324 CD1 ILE C 115 -38.520 0.860 40.228 1.00 27.99 C ANISOU 3324 CD1 ILE C 115 2296 3668 4668 -830 424 -1556 C ATOM 3325 N GLY C 116 -33.790 -2.127 40.693 1.00 24.34 N ANISOU 3325 N GLY C 116 2624 2803 3819 -842 636 -939 N ATOM 3326 CA GLY C 116 -32.941 -3.313 40.700 1.00 24.61 C ANISOU 3326 CA GLY C 116 2781 2684 3883 -857 701 -890 C ATOM 3327 C GLY C 116 -31.850 -3.282 41.758 1.00 23.49 C ANISOU 3327 C GLY C 116 2882 2459 3582 -802 776 -623 C ATOM 3328 O GLY C 116 -31.608 -4.283 42.409 1.00 24.49 O ANISOU 3328 O GLY C 116 3136 2382 3786 -842 927 -546 O ATOM 3329 N TRP C 117 -31.175 -2.148 41.932 1.00 21.66 N ANISOU 3329 N TRP C 117 2720 2374 3133 -699 667 -489 N ATOM 3330 CA TRP C 117 -30.188 -2.042 43.003 1.00 20.98 C ANISOU 3330 CA TRP C 117 2839 2228 2902 -633 709 -273 C ATOM 3331 C TRP C 117 -30.852 -1.996 44.364 1.00 21.90 C ANISOU 3331 C TRP C 117 3051 2231 3039 -693 896 -168 C ATOM 3332 O TRP C 117 -30.456 -2.717 45.278 1.00 22.73 O ANISOU 3332 O TRP C 117 3344 2172 3119 -679 1017 -36 O ATOM 3333 CB TRP C 117 -29.271 -0.821 42.815 1.00 19.05 C ANISOU 3333 CB TRP C 117 2618 2162 2456 -522 550 -193 C ATOM 3334 CG TRP C 117 -28.206 -1.050 41.804 1.00 18.41 C ANISOU 3334 CG TRP C 117 2525 2146 2323 -450 427 -233 C ATOM 3335 CD1 TRP C 117 -27.299 -2.072 41.790 1.00 18.87 C ANISOU 3335 CD1 TRP C 117 2661 2102 2406 -410 434 -214 C ATOM 3336 CD2 TRP C 117 -27.930 -0.250 40.648 1.00 17.53 C ANISOU 3336 CD2 TRP C 117 2330 2207 2122 -401 298 -299 C ATOM 3337 NE1 TRP C 117 -26.480 -1.963 40.687 1.00 18.27 N ANISOU 3337 NE1 TRP C 117 2530 2136 2276 -350 325 -284 N ATOM 3338 CE2 TRP C 117 -26.838 -0.851 39.973 1.00 17.51 C ANISOU 3338 CE2 TRP C 117 2349 2205 2096 -346 252 -327 C ATOM 3339 CE3 TRP C 117 -28.483 0.926 40.126 1.00 16.96 C ANISOU 3339 CE3 TRP C 117 2184 2276 1980 -384 225 -330 C ATOM 3340 CZ2 TRP C 117 -26.287 -0.317 38.813 1.00 17.02 C ANISOU 3340 CZ2 TRP C 117 2247 2285 1935 -291 167 -379 C ATOM 3341 CZ3 TRP C 117 -27.933 1.452 38.959 1.00 16.62 C ANISOU 3341 CZ3 TRP C 117 2127 2362 1826 -316 126 -365 C ATOM 3342 CH2 TRP C 117 -26.851 0.812 38.309 1.00 16.67 C ANISOU 3342 CH2 TRP C 117 2163 2368 1803 -278 112 -389 C ATOM 3343 N MET C 118 -31.871 -1.157 44.495 1.00 22.10 N ANISOU 3343 N MET C 118 2959 2340 3099 -745 925 -229 N ATOM 3344 CA MET C 118 -32.481 -0.907 45.805 1.00 23.08 C ANISOU 3344 CA MET C 118 3172 2385 3210 -792 1113 -133 C ATOM 3345 C MET C 118 -33.210 -2.107 46.369 1.00 25.56 C ANISOU 3345 C MET C 118 3533 2469 3707 -919 1378 -145 C ATOM 3346 O MET C 118 -33.271 -2.268 47.594 1.00 26.56 O ANISOU 3346 O MET C 118 3853 2474 3763 -929 1569 3 O ATOM 3347 CB MET C 118 -33.441 0.286 45.730 1.00 22.76 C ANISOU 3347 CB MET C 118 2965 2488 3192 -812 1082 -226 C ATOM 3348 CG MET C 118 -32.742 1.609 45.565 1.00 20.84 C ANISOU 3348 CG MET C 118 2742 2421 2752 -691 888 -160 C ATOM 3349 SD MET C 118 -33.829 2.940 45.065 1.00 20.72 S ANISOU 3349 SD MET C 118 2518 2567 2787 -681 796 -296 S ATOM 3350 CE MET C 118 -34.878 3.097 46.519 1.00 22.11 C ANISOU 3350 CE MET C 118 2712 2656 3033 -766 1050 -277 C ATOM 3351 N THR C 119 -33.763 -2.948 45.485 1.00 26.90 N ANISOU 3351 N THR C 119 3539 2571 4109 -1015 1402 -329 N ATOM 3352 CA THR C 119 -34.476 -4.159 45.906 1.00 29.61 C ANISOU 3352 CA THR C 119 3904 2661 4685 -1163 1679 -369 C ATOM 3353 C THR C 119 -33.665 -5.435 45.737 1.00 30.62 C ANISOU 3353 C THR C 119 4184 2600 4848 -1143 1706 -311 C ATOM 3354 O THR C 119 -34.186 -6.516 45.964 1.00 32.88 O ANISOU 3354 O THR C 119 4497 2645 5350 -1268 1938 -349 O ATOM 3355 CB THR C 119 -35.795 -4.358 45.124 1.00 31.09 C ANISOU 3355 CB THR C 119 3772 2857 5183 -1310 1720 -666 C ATOM 3356 OG1 THR C 119 -35.501 -4.604 43.741 1.00 30.49 O ANISOU 3356 OG1 THR C 119 3546 2884 5155 -1264 1481 -843 O ATOM 3357 CG2 THR C 119 -36.695 -3.163 45.253 1.00 30.65 C ANISOU 3357 CG2 THR C 119 3540 2972 5131 -1318 1690 -753 C ATOM 3358 N HIS C 120 -32.405 -5.336 45.329 1.00 29.22 N ANISOU 3358 N HIS C 120 4099 2515 4487 -991 1487 -232 N ATOM 3359 CA HIS C 120 -31.547 -6.515 45.264 1.00 30.37 C ANISOU 3359 CA HIS C 120 4402 2479 4656 -942 1503 -168 C ATOM 3360 C HIS C 120 -31.216 -6.994 46.678 1.00 32.04 C ANISOU 3360 C HIS C 120 4935 2479 4759 -894 1696 82 C ATOM 3361 O HIS C 120 -31.400 -6.265 47.634 1.00 31.89 O ANISOU 3361 O HIS C 120 5022 2509 4585 -869 1763 211 O ATOM 3362 CB HIS C 120 -30.267 -6.194 44.509 1.00 28.41 C ANISOU 3362 CB HIS C 120 4150 2401 4244 -784 1230 -163 C ATOM 3363 CG HIS C 120 -29.423 -7.386 44.232 1.00 29.36 C ANISOU 3363 CG HIS C 120 4376 2358 4421 -725 1218 -153 C ATOM 3364 ND1 HIS C 120 -28.251 -7.628 44.910 1.00 29.38 N ANISOU 3364 ND1 HIS C 120 4604 2294 4264 -568 1171 32 N ATOM 3365 CD2 HIS C 120 -29.580 -8.413 43.365 1.00 30.64 C ANISOU 3365 CD2 HIS C 120 4443 2406 4791 -787 1238 -323 C ATOM 3366 CE1 HIS C 120 -27.716 -8.750 44.469 1.00 30.49 C ANISOU 3366 CE1 HIS C 120 4788 2281 4515 -531 1166 -12 C ATOM 3367 NE2 HIS C 120 -28.501 -9.249 43.530 1.00 31.23 N ANISOU 3367 NE2 HIS C 120 4694 2338 4832 -669 1215 -226 N ATOM 3368 N ASN C 121 -30.746 -8.228 46.799 1.00 34.10 N ANISOU 3368 N ASN C 121 5364 2499 5092 -868 1784 146 N ATOM 3369 CA ASN C 121 -30.397 -8.812 48.088 1.00 36.29 C ANISOU 3369 CA ASN C 121 5993 2546 5246 -789 1960 398 C ATOM 3370 C ASN C 121 -28.951 -9.319 48.079 1.00 36.34 C ANISOU 3370 C ASN C 121 6182 2513 5112 -575 1772 507 C ATOM 3371 O ASN C 121 -28.658 -10.302 47.398 1.00 37.35 O ANISOU 3371 O ASN C 121 6282 2501 5406 -579 1760 423 O ATOM 3372 CB ASN C 121 -31.337 -9.976 48.389 1.00 39.49 C ANISOU 3372 CB ASN C 121 6473 2617 5912 -962 2309 388 C ATOM 3373 CG ASN C 121 -30.962 -10.704 49.646 1.00 41.99 C ANISOU 3373 CG ASN C 121 7206 2657 6088 -862 2512 669 C ATOM 3374 OD1 ASN C 121 -30.755 -11.918 49.647 1.00 44.33 O ANISOU 3374 OD1 ASN C 121 7663 2663 6515 -858 2638 718 O ATOM 3375 ND2 ASN C 121 -30.867 -9.963 50.736 1.00 42.00 N ANISOU 3375 ND2 ASN C 121 7407 2739 5810 -764 2540 855 N ATOM 3376 N PRO C 122 -28.034 -8.654 48.813 1.00 35.60 N ANISOU 3376 N PRO C 122 6253 2544 4729 -380 1615 666 N ATOM 3377 CA PRO C 122 -28.266 -7.461 49.606 1.00 34.67 C ANISOU 3377 CA PRO C 122 6168 2599 4406 -356 1602 746 C ATOM 3378 C PRO C 122 -28.456 -6.259 48.693 1.00 32.01 C ANISOU 3378 C PRO C 122 5508 2559 4092 -422 1423 569 C ATOM 3379 O PRO C 122 -28.026 -6.275 47.538 1.00 30.59 O ANISOU 3379 O PRO C 122 5136 2484 3999 -419 1254 426 O ATOM 3380 CB PRO C 122 -26.982 -7.331 50.430 1.00 34.85 C ANISOU 3380 CB PRO C 122 6437 2652 4151 -99 1424 912 C ATOM 3381 CG PRO C 122 -25.936 -7.906 49.560 1.00 34.36 C ANISOU 3381 CG PRO C 122 6296 2592 4165 1 1225 832 C ATOM 3382 CD PRO C 122 -26.605 -9.029 48.807 1.00 35.60 C ANISOU 3382 CD PRO C 122 6379 2538 4606 -155 1400 734 C ATOM 3383 N PRO C 123 -29.136 -5.231 49.199 1.00 31.41 N ANISOU 3383 N PRO C 123 5389 2608 3936 -475 1476 580 N ATOM 3384 CA PRO C 123 -29.381 -4.062 48.388 1.00 29.20 C ANISOU 3384 CA PRO C 123 4837 2581 3674 -521 1319 432 C ATOM 3385 C PRO C 123 -28.158 -3.149 48.281 1.00 27.18 C ANISOU 3385 C PRO C 123 4575 2526 3224 -363 1054 461 C ATOM 3386 O PRO C 123 -27.314 -3.142 49.180 1.00 27.58 O ANISOU 3386 O PRO C 123 4829 2554 3096 -218 997 594 O ATOM 3387 CB PRO C 123 -30.548 -3.366 49.119 1.00 29.69 C ANISOU 3387 CB PRO C 123 4880 2665 3733 -621 1497 440 C ATOM 3388 CG PRO C 123 -30.494 -3.845 50.502 1.00 31.68 C ANISOU 3388 CG PRO C 123 5447 2743 3847 -568 1688 635 C ATOM 3389 CD PRO C 123 -29.785 -5.157 50.519 1.00 33.15 C ANISOU 3389 CD PRO C 123 5822 2718 4054 -496 1712 724 C ATOM 3390 N ILE C 124 -28.071 -2.424 47.163 1.00 25.21 N ANISOU 3390 N ILE C 124 4097 2461 3019 -389 898 325 N ATOM 3391 CA ILE C 124 -27.185 -1.276 47.025 1.00 23.40 C ANISOU 3391 CA ILE C 124 3818 2425 2647 -291 701 330 C ATOM 3392 C ILE C 124 -28.111 -0.070 47.035 1.00 22.54 C ANISOU 3392 C ILE C 124 3591 2442 2530 -364 721 284 C ATOM 3393 O ILE C 124 -28.851 0.148 46.053 1.00 22.31 O ANISOU 3393 O ILE C 124 3381 2478 2616 -446 710 159 O ATOM 3394 CB ILE C 124 -26.390 -1.299 45.720 1.00 22.37 C ANISOU 3394 CB ILE C 124 3546 2391 2561 -262 547 226 C ATOM 3395 CG1 ILE C 124 -25.507 -2.555 45.659 1.00 23.35 C ANISOU 3395 CG1 ILE C 124 3765 2382 2723 -184 529 246 C ATOM 3396 CG2 ILE C 124 -25.535 -0.015 45.594 1.00 20.74 C ANISOU 3396 CG2 ILE C 124 3281 2364 2236 -190 394 227 C ATOM 3397 CD1 ILE C 124 -26.261 -3.802 45.287 1.00 24.85 C ANISOU 3397 CD1 ILE C 124 3955 2399 3087 -277 668 189 C ATOM 3398 N PRO C 125 -28.116 0.694 48.146 1.00 22.24 N ANISOU 3398 N PRO C 125 3660 2435 2354 -318 742 372 N ATOM 3399 CA PRO C 125 -29.190 1.654 48.342 1.00 21.89 C ANISOU 3399 CA PRO C 125 3524 2464 2329 -391 809 328 C ATOM 3400 C PRO C 125 -28.865 2.969 47.645 1.00 19.96 C ANISOU 3400 C PRO C 125 3139 2395 2049 -359 639 267 C ATOM 3401 O PRO C 125 -28.582 3.974 48.282 1.00 19.78 O ANISOU 3401 O PRO C 125 3156 2442 1916 -307 589 302 O ATOM 3402 CB PRO C 125 -29.273 1.775 49.882 1.00 23.05 C ANISOU 3402 CB PRO C 125 3881 2550 2327 -344 924 448 C ATOM 3403 CG PRO C 125 -27.902 1.472 50.369 1.00 23.19 C ANISOU 3403 CG PRO C 125 4067 2551 2192 -195 796 538 C ATOM 3404 CD PRO C 125 -27.202 0.656 49.304 1.00 22.87 C ANISOU 3404 CD PRO C 125 3951 2481 2255 -184 700 495 C ATOM 3405 N VAL C 126 -28.895 2.944 46.325 1.00 18.95 N ANISOU 3405 N VAL C 126 2862 2326 2009 -386 557 173 N ATOM 3406 CA VAL C 126 -28.532 4.104 45.518 1.00 17.49 C ANISOU 3406 CA VAL C 126 2581 2281 1784 -349 419 135 C ATOM 3407 C VAL C 126 -29.347 5.368 45.898 1.00 17.06 C ANISOU 3407 C VAL C 126 2479 2289 1711 -359 431 123 C ATOM 3408 O VAL C 126 -28.851 6.497 45.780 1.00 15.92 O ANISOU 3408 O VAL C 126 2326 2221 1502 -312 344 139 O ATOM 3409 CB VAL C 126 -28.685 3.786 44.011 1.00 17.35 C ANISOU 3409 CB VAL C 126 2441 2310 1838 -367 355 32 C ATOM 3410 CG1 VAL C 126 -27.629 2.729 43.572 1.00 17.37 C ANISOU 3410 CG1 VAL C 126 2487 2266 1846 -339 326 34 C ATOM 3411 CG2 VAL C 126 -30.111 3.302 43.690 1.00 18.29 C ANISOU 3411 CG2 VAL C 126 2451 2400 2096 -445 424 -79 C ATOM 3412 N GLY C 127 -30.583 5.159 46.353 1.00 17.80 N ANISOU 3412 N GLY C 127 2536 2339 1887 -423 554 83 N ATOM 3413 CA GLY C 127 -31.434 6.243 46.830 1.00 17.91 C ANISOU 3413 CA GLY C 127 2499 2400 1904 -426 586 55 C ATOM 3414 C GLY C 127 -30.850 6.895 48.071 1.00 17.73 C ANISOU 3414 C GLY C 127 2617 2376 1743 -375 602 146 C ATOM 3415 O GLY C 127 -30.731 8.121 48.116 1.00 16.84 O ANISOU 3415 O GLY C 127 2479 2332 1587 -332 527 137 O ATOM 3416 N GLU C 128 -30.466 6.083 49.061 1.00 18.65 N ANISOU 3416 N GLU C 128 2894 2408 1783 -366 692 228 N ATOM 3417 CA GLU C 128 -29.889 6.618 50.311 1.00 19.11 C ANISOU 3417 CA GLU C 128 3108 2476 1677 -289 686 296 C ATOM 3418 C GLU C 128 -28.500 7.237 50.082 1.00 17.64 C ANISOU 3418 C GLU C 128 2927 2358 1415 -204 493 302 C ATOM 3419 O GLU C 128 -28.171 8.255 50.684 1.00 17.44 O ANISOU 3419 O GLU C 128 2926 2385 1314 -156 434 287 O ATOM 3420 CB GLU C 128 -29.818 5.556 51.415 1.00 21.13 C ANISOU 3420 CB GLU C 128 3575 2619 1833 -266 821 392 C ATOM 3421 CG GLU C 128 -31.160 4.890 51.788 1.00 23.11 C ANISOU 3421 CG GLU C 128 3836 2767 2175 -373 1077 390 C ATOM 3422 CD GLU C 128 -32.235 5.866 52.273 1.00 24.06 C ANISOU 3422 CD GLU C 128 3880 2940 2320 -415 1183 322 C ATOM 3423 OE1 GLU C 128 -31.983 7.087 52.333 1.00 23.99 O ANISOU 3423 OE1 GLU C 128 3823 3039 2251 -357 1054 283 O ATOM 3424 OE2 GLU C 128 -33.343 5.414 52.650 1.00 26.15 O ANISOU 3424 OE2 GLU C 128 4132 3125 2678 -509 1417 297 O ATOM 3425 N ILE C 129 -27.712 6.641 49.186 1.00 16.70 N ANISOU 3425 N ILE C 129 2768 2236 1341 -196 408 301 N ATOM 3426 CA ILE C 129 -26.363 7.133 48.890 1.00 15.66 C ANISOU 3426 CA ILE C 129 2611 2160 1179 -133 257 285 C ATOM 3427 C ILE C 129 -26.450 8.512 48.275 1.00 14.52 C ANISOU 3427 C ILE C 129 2351 2087 1079 -159 208 235 C ATOM 3428 O ILE C 129 -25.807 9.447 48.727 1.00 14.37 O ANISOU 3428 O ILE C 129 2334 2098 1027 -123 143 211 O ATOM 3429 CB ILE C 129 -25.595 6.187 47.946 1.00 15.54 C ANISOU 3429 CB ILE C 129 2558 2125 1220 -127 208 278 C ATOM 3430 CG1 ILE C 129 -25.386 4.818 48.601 1.00 16.57 C ANISOU 3430 CG1 ILE C 129 2827 2155 1311 -79 248 337 C ATOM 3431 CG2 ILE C 129 -24.256 6.800 47.577 1.00 15.11 C ANISOU 3431 CG2 ILE C 129 2439 2130 1170 -81 87 236 C ATOM 3432 CD1 ILE C 129 -24.829 3.756 47.681 1.00 16.56 C ANISOU 3432 CD1 ILE C 129 2788 2113 1389 -75 221 317 C ATOM 3433 N TYR C 130 -27.295 8.651 47.264 1.00 13.76 N ANISOU 3433 N TYR C 130 2159 2006 1061 -211 238 209 N ATOM 3434 CA TYR C 130 -27.461 9.935 46.609 1.00 13.05 C ANISOU 3434 CA TYR C 130 1996 1962 1000 -212 197 183 C ATOM 3435 C TYR C 130 -28.075 11.001 47.540 1.00 13.14 C ANISOU 3435 C TYR C 130 2022 1975 994 -201 224 168 C ATOM 3436 O TYR C 130 -27.681 12.166 47.507 1.00 12.83 O ANISOU 3436 O TYR C 130 1969 1945 961 -183 179 155 O ATOM 3437 CB TYR C 130 -28.317 9.747 45.367 1.00 12.96 C ANISOU 3437 CB TYR C 130 1902 1974 1046 -232 197 152 C ATOM 3438 CG TYR C 130 -28.453 10.926 44.444 1.00 12.76 C ANISOU 3438 CG TYR C 130 1840 1983 1024 -201 146 147 C ATOM 3439 CD1 TYR C 130 -27.441 11.862 44.284 1.00 12.54 C ANISOU 3439 CD1 TYR C 130 1843 1947 974 -186 122 181 C ATOM 3440 CD2 TYR C 130 -29.608 11.060 43.680 1.00 13.15 C ANISOU 3440 CD2 TYR C 130 1825 2063 1107 -179 122 101 C ATOM 3441 CE1 TYR C 130 -27.598 12.945 43.411 1.00 12.79 C ANISOU 3441 CE1 TYR C 130 1880 1977 1002 -153 104 202 C ATOM 3442 CE2 TYR C 130 -29.786 12.087 42.842 1.00 13.40 C ANISOU 3442 CE2 TYR C 130 1861 2115 1116 -118 66 112 C ATOM 3443 CZ TYR C 130 -28.778 13.040 42.681 1.00 13.29 C ANISOU 3443 CZ TYR C 130 1916 2070 1062 -105 69 180 C ATOM 3444 OH TYR C 130 -29.019 14.060 41.790 1.00 13.81 O ANISOU 3444 OH TYR C 130 2022 2128 1097 -35 37 214 O ATOM 3445 N LYS C 131 -29.012 10.596 48.381 1.00 13.55 N ANISOU 3445 N LYS C 131 2105 2007 1036 -217 316 163 N ATOM 3446 CA LYS C 131 -29.623 11.521 49.325 1.00 13.93 C ANISOU 3446 CA LYS C 131 2171 2061 1061 -201 361 134 C ATOM 3447 C LYS C 131 -28.571 12.086 50.276 1.00 13.97 C ANISOU 3447 C LYS C 131 2265 2072 970 -149 299 134 C ATOM 3448 O LYS C 131 -28.631 13.251 50.634 1.00 14.08 O ANISOU 3448 O LYS C 131 2264 2095 988 -129 277 87 O ATOM 3449 CB LYS C 131 -30.729 10.837 50.127 1.00 14.93 C ANISOU 3449 CB LYS C 131 2328 2156 1188 -237 515 127 C ATOM 3450 CG LYS C 131 -31.626 11.793 50.900 1.00 15.66 C ANISOU 3450 CG LYS C 131 2402 2262 1285 -227 588 70 C ATOM 3451 CD LYS C 131 -32.522 11.095 51.920 1.00 17.09 C ANISOU 3451 CD LYS C 131 2647 2403 1441 -267 788 69 C ATOM 3452 CE LYS C 131 -33.525 10.198 51.231 1.00 17.60 C ANISOU 3452 CE LYS C 131 2590 2434 1663 -352 890 29 C ATOM 3453 NZ LYS C 131 -34.389 9.431 52.165 1.00 19.35 N ANISOU 3453 NZ LYS C 131 2867 2585 1897 -419 1137 28 N ATOM 3454 N ARG C 132 -27.623 11.255 50.698 1.00 14.09 N ANISOU 3454 N ARG C 132 2369 2078 906 -115 261 168 N ATOM 3455 CA ARG C 132 -26.513 11.728 51.535 1.00 14.43 C ANISOU 3455 CA ARG C 132 2472 2142 866 -44 159 131 C ATOM 3456 C ARG C 132 -25.661 12.780 50.801 1.00 13.50 C ANISOU 3456 C ARG C 132 2239 2038 851 -61 64 71 C ATOM 3457 O ARG C 132 -25.265 13.760 51.416 1.00 13.87 O ANISOU 3457 O ARG C 132 2281 2094 895 -36 11 -4 O ATOM 3458 CB ARG C 132 -25.653 10.546 52.022 1.00 15.39 C ANISOU 3458 CB ARG C 132 2704 2250 891 25 108 171 C ATOM 3459 CG ARG C 132 -26.386 9.611 53.016 1.00 16.78 C ANISOU 3459 CG ARG C 132 3057 2382 935 57 230 247 C ATOM 3460 CD ARG C 132 -25.477 8.598 53.763 1.00 18.21 C ANISOU 3460 CD ARG C 132 3409 2536 973 178 160 298 C ATOM 3461 NE ARG C 132 -24.568 7.901 52.854 1.00 17.90 N ANISOU 3461 NE ARG C 132 3292 2481 1025 186 65 300 N ATOM 3462 CZ ARG C 132 -24.634 6.618 52.483 1.00 18.29 C ANISOU 3462 CZ ARG C 132 3398 2452 1100 181 124 375 C ATOM 3463 NH1 ARG C 132 -25.564 5.782 52.968 1.00 19.41 N ANISOU 3463 NH1 ARG C 132 3685 2500 1187 158 296 469 N ATOM 3464 NH2 ARG C 132 -23.717 6.159 51.640 1.00 17.86 N ANISOU 3464 NH2 ARG C 132 3251 2398 1134 196 26 347 N ATOM 3465 N TRP C 133 -25.402 12.587 49.494 1.00 12.31 N ANISOU 3465 N TRP C 133 2004 1879 791 -107 60 97 N ATOM 3466 CA TRP C 133 -24.630 13.570 48.692 1.00 11.82 C ANISOU 3466 CA TRP C 133 1856 1806 829 -137 26 61 C ATOM 3467 C TRP C 133 -25.350 14.899 48.610 1.00 11.64 C ANISOU 3467 C TRP C 133 1813 1752 854 -154 61 46 C ATOM 3468 O TRP C 133 -24.742 15.965 48.735 1.00 11.96 O ANISOU 3468 O TRP C 133 1823 1757 963 -165 41 -10 O ATOM 3469 CB TRP C 133 -24.373 13.081 47.268 1.00 11.27 C ANISOU 3469 CB TRP C 133 1737 1734 809 -172 48 105 C ATOM 3470 CG TRP C 133 -23.558 11.839 47.210 1.00 11.32 C ANISOU 3470 CG TRP C 133 1746 1757 798 -152 14 105 C ATOM 3471 CD1 TRP C 133 -22.910 11.235 48.245 1.00 11.90 C ANISOU 3471 CD1 TRP C 133 1863 1838 819 -91 -53 74 C ATOM 3472 CD2 TRP C 133 -23.296 11.041 46.052 1.00 11.03 C ANISOU 3472 CD2 TRP C 133 1676 1726 786 -171 34 128 C ATOM 3473 NE1 TRP C 133 -22.262 10.103 47.798 1.00 11.99 N ANISOU 3473 NE1 TRP C 133 1866 1849 841 -69 -76 82 N ATOM 3474 CE2 TRP C 133 -22.470 9.974 46.454 1.00 11.38 C ANISOU 3474 CE2 TRP C 133 1733 1771 818 -127 -15 107 C ATOM 3475 CE3 TRP C 133 -23.652 11.143 44.707 1.00 10.77 C ANISOU 3475 CE3 TRP C 133 1617 1701 772 -203 82 157 C ATOM 3476 CZ2 TRP C 133 -22.038 8.990 45.572 1.00 11.36 C ANISOU 3476 CZ2 TRP C 133 1702 1769 843 -127 -6 108 C ATOM 3477 CZ3 TRP C 133 -23.197 10.177 43.819 1.00 10.77 C ANISOU 3477 CZ3 TRP C 133 1597 1716 776 -204 90 153 C ATOM 3478 CH2 TRP C 133 -22.404 9.117 44.253 1.00 10.98 C ANISOU 3478 CH2 TRP C 133 1620 1737 814 -174 53 124 C ATOM 3479 N ILE C 134 -26.655 14.808 48.413 1.00 11.17 N ANISOU 3479 N ILE C 134 1762 1699 783 -152 114 82 N ATOM 3480 CA ILE C 134 -27.505 15.975 48.332 1.00 11.30 C ANISOU 3480 CA ILE C 134 1759 1685 848 -141 138 65 C ATOM 3481 C ILE C 134 -27.468 16.751 49.661 1.00 11.79 C ANISOU 3481 C ILE C 134 1851 1737 891 -118 133 -12 C ATOM 3482 O ILE C 134 -27.332 17.965 49.673 1.00 12.17 O ANISOU 3482 O ILE C 134 1882 1731 1009 -115 124 -55 O ATOM 3483 CB ILE C 134 -28.938 15.569 47.962 1.00 11.29 C ANISOU 3483 CB ILE C 134 1726 1707 853 -130 179 79 C ATOM 3484 CG1 ILE C 134 -28.946 14.983 46.543 1.00 10.93 C ANISOU 3484 CG1 ILE C 134 1651 1678 822 -134 154 125 C ATOM 3485 CG2 ILE C 134 -29.861 16.770 48.034 1.00 11.81 C ANISOU 3485 CG2 ILE C 134 1765 1744 976 -90 187 41 C ATOM 3486 CD1 ILE C 134 -30.202 14.152 46.181 1.00 11.12 C ANISOU 3486 CD1 ILE C 134 1616 1740 869 -132 174 98 C ATOM 3487 N ILE C 135 -27.542 16.038 50.777 1.00 11.96 N ANISOU 3487 N ILE C 135 1934 1798 809 -96 145 -32 N ATOM 3488 CA ILE C 135 -27.537 16.681 52.095 1.00 12.76 C ANISOU 3488 CA ILE C 135 2090 1908 848 -55 137 -117 C ATOM 3489 C ILE C 135 -26.194 17.341 52.390 1.00 13.11 C ANISOU 3489 C ILE C 135 2116 1941 925 -43 32 -206 C ATOM 3490 O ILE C 135 -26.147 18.415 52.973 1.00 13.85 O ANISOU 3490 O ILE C 135 2200 2009 1051 -29 11 -306 O ATOM 3491 CB ILE C 135 -27.945 15.681 53.214 1.00 13.40 C ANISOU 3491 CB ILE C 135 2288 2031 769 -16 196 -98 C ATOM 3492 CG1 ILE C 135 -29.458 15.459 53.155 1.00 13.52 C ANISOU 3492 CG1 ILE C 135 2285 2041 809 -46 340 -72 C ATOM 3493 CG2 ILE C 135 -27.522 16.171 54.629 1.00 14.65 C ANISOU 3493 CG2 ILE C 135 2544 2220 799 58 150 -193 C ATOM 3494 CD1 ILE C 135 -29.920 14.189 53.730 1.00 14.11 C ANISOU 3494 CD1 ILE C 135 2457 2119 782 -52 455 -12 C ATOM 3495 N LEU C 136 -25.104 16.711 51.980 1.00 12.78 N ANISOU 3495 N LEU C 136 2049 1910 896 -52 -32 -193 N ATOM 3496 CA LEU C 136 -23.783 17.345 52.068 1.00 13.39 C ANISOU 3496 CA LEU C 136 2053 1969 1064 -59 -124 -308 C ATOM 3497 C LEU C 136 -23.751 18.656 51.286 1.00 13.41 C ANISOU 3497 C LEU C 136 1976 1876 1241 -131 -71 -330 C ATOM 3498 O LEU C 136 -23.233 19.664 51.774 1.00 14.42 O ANISOU 3498 O LEU C 136 2059 1959 1460 -142 -105 -460 O ATOM 3499 CB LEU C 136 -22.676 16.396 51.590 1.00 13.24 C ANISOU 3499 CB LEU C 136 1991 1976 1063 -58 -184 -297 C ATOM 3500 CG LEU C 136 -22.387 15.142 52.453 1.00 13.70 C ANISOU 3500 CG LEU C 136 2145 2102 957 42 -267 -288 C ATOM 3501 CD1 LEU C 136 -21.267 14.336 51.836 1.00 13.64 C ANISOU 3501 CD1 LEU C 136 2066 2105 1011 48 -329 -296 C ATOM 3502 CD2 LEU C 136 -22.048 15.498 53.893 1.00 15.19 C ANISOU 3502 CD2 LEU C 136 2398 2335 1035 143 -381 -416 C ATOM 3503 N GLY C 137 -24.331 18.647 50.091 1.00 12.57 N ANISOU 3503 N GLY C 137 1866 1731 1178 -169 12 -209 N ATOM 3504 CA GLY C 137 -24.443 19.850 49.280 1.00 12.91 C ANISOU 3504 CA GLY C 137 1887 1664 1352 -211 78 -189 C ATOM 3505 C GLY C 137 -25.282 20.947 49.919 1.00 13.53 C ANISOU 3505 C GLY C 137 1990 1689 1459 -179 92 -244 C ATOM 3506 O GLY C 137 -24.900 22.113 49.904 1.00 14.44 O ANISOU 3506 O GLY C 137 2084 1694 1706 -210 116 -308 O ATOM 3507 N LEU C 138 -26.424 20.572 50.490 1.00 13.26 N ANISOU 3507 N LEU C 138 1996 1721 1320 -124 95 -231 N ATOM 3508 CA LEU C 138 -27.281 21.529 51.179 1.00 14.03 C ANISOU 3508 CA LEU C 138 2106 1781 1440 -83 116 -302 C ATOM 3509 C LEU C 138 -26.566 22.196 52.389 1.00 15.19 C ANISOU 3509 C LEU C 138 2251 1917 1602 -78 65 -469 C ATOM 3510 O LEU C 138 -26.762 23.368 52.638 1.00 16.05 O ANISOU 3510 O LEU C 138 2349 1938 1810 -71 80 -552 O ATOM 3511 CB LEU C 138 -28.583 20.872 51.623 1.00 13.76 C ANISOU 3511 CB LEU C 138 2095 1829 1304 -37 158 -280 C ATOM 3512 CG LEU C 138 -29.532 20.335 50.559 1.00 13.14 C ANISOU 3512 CG LEU C 138 1986 1766 1238 -28 191 -177 C ATOM 3513 CD1 LEU C 138 -30.643 19.523 51.213 1.00 13.26 C ANISOU 3513 CD1 LEU C 138 1995 1859 1181 -13 257 -195 C ATOM 3514 CD2 LEU C 138 -30.113 21.470 49.735 1.00 13.64 C ANISOU 3514 CD2 LEU C 138 2030 1737 1414 15 189 -158 C ATOM 3515 N ASN C 139 -25.754 21.435 53.120 1.00 15.43 N ANISOU 3515 N ASN C 139 2295 2035 1532 -65 -8 -527 N ATOM 3516 CA ASN C 139 -24.992 21.956 54.257 1.00 16.87 C ANISOU 3516 CA ASN C 139 2470 2232 1706 -36 -99 -714 C ATOM 3517 C ASN C 139 -23.958 23.010 53.831 1.00 17.84 C ANISOU 3517 C ASN C 139 2485 2236 2055 -111 -120 -824 C ATOM 3518 O ASN C 139 -23.653 23.946 54.578 1.00 19.23 O ANISOU 3518 O ASN C 139 2629 2368 2306 -105 -165 -1005 O ATOM 3519 CB ASN C 139 -24.315 20.811 55.008 1.00 17.09 C ANISOU 3519 CB ASN C 139 2549 2381 1561 27 -201 -741 C ATOM 3520 CG ASN C 139 -25.240 20.167 56.049 1.00 17.40 C ANISOU 3520 CG ASN C 139 2734 2511 1365 115 -167 -709 C ATOM 3521 OD1 ASN C 139 -25.519 20.768 57.073 1.00 18.66 O ANISOU 3521 OD1 ASN C 139 2947 2693 1447 173 -180 -831 O ATOM 3522 ND2 ASN C 139 -25.679 18.943 55.808 1.00 16.55 N ANISOU 3522 ND2 ASN C 139 2696 2446 1146 123 -107 -557 N ATOM 3523 N LYS C 140 -23.420 22.867 52.628 1.00 17.39 N ANISOU 3523 N LYS C 140 2375 2117 2115 -187 -68 -726 N ATOM 3524 CA LYS C 140 -22.494 23.878 52.102 1.00 18.58 C ANISOU 3524 CA LYS C 140 2430 2122 2504 -282 -24 -810 C ATOM 3525 C LYS C 140 -23.221 25.141 51.645 1.00 19.12 C ANISOU 3525 C LYS C 140 2539 2024 2699 -304 85 -766 C ATOM 3526 O LYS C 140 -22.722 26.247 51.837 1.00 20.61 O ANISOU 3526 O LYS C 140 2676 2075 3077 -360 114 -900 O ATOM 3527 CB LYS C 140 -21.713 23.301 50.939 1.00 18.14 C ANISOU 3527 CB LYS C 140 2327 2050 2516 -353 33 -710 C ATOM 3528 CG LYS C 140 -20.829 22.191 51.366 1.00 18.09 C ANISOU 3528 CG LYS C 140 2259 2177 2436 -324 -83 -783 C ATOM 3529 CD LYS C 140 -20.310 21.433 50.181 1.00 17.46 C ANISOU 3529 CD LYS C 140 2147 2100 2383 -375 -14 -664 C ATOM 3530 CE LYS C 140 -19.164 20.492 50.615 1.00 17.94 C ANISOU 3530 CE LYS C 140 2110 2267 2437 -343 -141 -785 C ATOM 3531 NZ LYS C 140 -18.900 19.568 49.502 1.00 17.10 N ANISOU 3531 NZ LYS C 140 1997 2183 2316 -370 -71 -654 N ATOM 3532 N ILE C 141 -24.396 24.961 51.043 1.00 18.16 N ANISOU 3532 N ILE C 141 2505 1908 2484 -253 140 -592 N ATOM 3533 CA ILE C 141 -25.223 26.074 50.589 1.00 18.87 C ANISOU 3533 CA ILE C 141 2652 1848 2667 -228 218 -536 C ATOM 3534 C ILE C 141 -25.729 26.934 51.741 1.00 20.00 C ANISOU 3534 C ILE C 141 2792 1962 2844 -181 186 -699 C ATOM 3535 O ILE C 141 -25.683 28.157 51.649 1.00 21.30 O ANISOU 3535 O ILE C 141 2963 1947 3182 -200 240 -754 O ATOM 3536 CB ILE C 141 -26.457 25.594 49.800 1.00 17.81 C ANISOU 3536 CB ILE C 141 2588 1763 2416 -149 238 -357 C ATOM 3537 CG1 ILE C 141 -26.046 24.992 48.466 1.00 17.19 C ANISOU 3537 CG1 ILE C 141 2536 1682 2311 -182 282 -197 C ATOM 3538 CG2 ILE C 141 -27.422 26.744 49.549 1.00 18.78 C ANISOU 3538 CG2 ILE C 141 2766 1748 2621 -76 276 -330 C ATOM 3539 CD1 ILE C 141 -27.197 24.230 47.779 1.00 16.20 C ANISOU 3539 CD1 ILE C 141 2452 1652 2049 -96 256 -67 C ATOM 3540 N VAL C 142 -26.245 26.302 52.801 1.00 19.75 N ANISOU 3540 N VAL C 142 2768 2090 2644 -115 117 -771 N ATOM 3541 CA VAL C 142 -26.811 27.051 53.939 1.00 21.01 C ANISOU 3541 CA VAL C 142 2939 2244 2800 -57 100 -934 C ATOM 3542 C VAL C 142 -25.751 27.964 54.514 1.00 22.76 C ANISOU 3542 C VAL C 142 3101 2370 3176 -109 57 -1145 C ATOM 3543 O VAL C 142 -26.049 29.002 55.071 1.00 24.11 O ANISOU 3543 O VAL C 142 3270 2447 3441 -86 67 -1284 O ATOM 3544 CB VAL C 142 -27.423 26.154 55.067 1.00 20.74 C ANISOU 3544 CB VAL C 142 2950 2400 2527 18 66 -979 C ATOM 3545 CG1 VAL C 142 -28.484 25.198 54.501 1.00 19.42 C ANISOU 3545 CG1 VAL C 142 2810 2314 2252 47 128 -799 C ATOM 3546 CG2 VAL C 142 -26.365 25.396 55.782 1.00 20.91 C ANISOU 3546 CG2 VAL C 142 2976 2539 2430 16 -35 -1063 C ATOM 3547 N ARG C 143 -24.504 27.560 54.364 1.00 23.00 N ANISOU 3547 N ARG C 143 3064 2421 3252 -180 8 -1189 N ATOM 3548 CA ARG C 143 -23.391 28.469 54.521 1.00 24.85 C ANISOU 3548 CA ARG C 143 3198 2523 3720 -266 -5 -1385 C ATOM 3549 C ARG C 143 -23.267 29.222 53.205 1.00 25.21 C ANISOU 3549 C ARG C 143 3248 2342 3988 -360 152 -1247 C ATOM 3550 O ARG C 143 -22.834 30.369 53.194 1.00 27.16 O ANISOU 3550 O ARG C 143 3452 2390 4476 -432 216 -1369 O ATOM 3551 CB ARG C 143 -22.129 27.656 54.781 1.00 25.04 C ANISOU 3551 CB ARG C 143 3125 2665 3721 -295 -117 -1490 C ATOM 3552 CG ARG C 143 -20.941 28.465 55.091 1.00 27.19 C ANISOU 3552 CG ARG C 143 3248 2834 4246 -381 -157 -1753 C ATOM 3553 CD ARG C 143 -19.711 27.567 55.302 1.00 27.50 C ANISOU 3553 CD ARG C 143 3167 3009 4269 -384 -292 -1870 C ATOM 3554 NE ARG C 143 -18.650 28.342 55.945 1.00 30.04 N ANISOU 3554 NE ARG C 143 3316 3272 4823 -436 -385 -2210 N ATOM 3555 CZ ARG C 143 -17.668 28.974 55.301 1.00 31.51 C ANISOU 3555 CZ ARG C 143 3333 3287 5351 -594 -284 -2321 C ATOM 3556 NH1 ARG C 143 -17.550 28.912 53.969 1.00 30.72 N ANISOU 3556 NH1 ARG C 143 3242 3059 5370 -710 -76 -2097 N ATOM 3557 NH2 ARG C 143 -16.779 29.653 55.996 1.00 34.05 N ANISOU 3557 NH2 ARG C 143 3475 3564 5897 -637 -383 -2672 N TER 3558 ARG C 143 ATOM 3559 N PRO D 1 -4.602 2.675 61.180 1.00 23.36 N ANISOU 3559 N PRO D 1 1996 2921 3957 309 570 17 N ATOM 3560 CA PRO D 1 -4.999 2.033 59.932 1.00 23.39 C ANISOU 3560 CA PRO D 1 2180 2860 3844 343 791 -38 C ATOM 3561 C PRO D 1 -4.838 0.504 59.958 1.00 24.05 C ANISOU 3561 C PRO D 1 2260 2863 4012 426 835 -31 C ATOM 3562 O PRO D 1 -4.461 -0.083 60.984 1.00 24.16 O ANISOU 3562 O PRO D 1 2124 2878 4177 461 681 26 O ATOM 3563 CB PRO D 1 -4.043 2.653 58.891 1.00 24.93 C ANISOU 3563 CB PRO D 1 2324 2973 4174 347 1052 -47 C ATOM 3564 CG PRO D 1 -3.301 3.775 59.612 1.00 25.30 C ANISOU 3564 CG PRO D 1 2153 3060 4399 298 939 4 C ATOM 3565 CD PRO D 1 -3.960 3.977 60.939 1.00 23.86 C ANISOU 3565 CD PRO D 1 1963 2987 4113 256 625 25 C ATOM 3566 N ILE D 2 -5.120 -0.107 58.811 1.00 24.35 N ANISOU 3566 N ILE D 2 2486 2820 3943 452 1040 -89 N ATOM 3567 CA ILE D 2 -5.119 -1.541 58.651 1.00 25.01 C ANISOU 3567 CA ILE D 2 2628 2812 4064 523 1109 -101 C ATOM 3568 C ILE D 2 -4.146 -1.854 57.557 1.00 27.04 C ANISOU 3568 C ILE D 2 2891 2916 4466 586 1436 -124 C ATOM 3569 O ILE D 2 -4.262 -1.299 56.491 1.00 27.41 O ANISOU 3569 O ILE D 2 3112 2928 4375 551 1616 -176 O ATOM 3570 CB ILE D 2 -6.510 -2.027 58.209 1.00 23.87 C ANISOU 3570 CB ILE D 2 2765 2685 3619 483 1055 -161 C ATOM 3571 CG1 ILE D 2 -7.479 -2.044 59.375 1.00 22.18 C ANISOU 3571 CG1 ILE D 2 2530 2589 3307 443 771 -127 C ATOM 3572 CG2 ILE D 2 -6.440 -3.423 57.619 1.00 25.04 C ANISOU 3572 CG2 ILE D 2 3037 2696 3778 546 1200 -196 C ATOM 3573 CD1 ILE D 2 -8.781 -2.772 59.016 1.00 21.55 C ANISOU 3573 CD1 ILE D 2 2677 2499 3010 410 715 -169 C ATOM 3574 N VAL D 3 -3.191 -2.739 57.810 1.00 28.60 N ANISOU 3574 N VAL D 3 2910 3008 4946 679 1525 -81 N ATOM 3575 CA VAL D 3 -2.233 -3.130 56.797 1.00 30.92 C ANISOU 3575 CA VAL D 3 3203 3129 5416 754 1882 -99 C ATOM 3576 C VAL D 3 -2.122 -4.648 56.764 1.00 31.99 C ANISOU 3576 C VAL D 3 3379 3138 5637 849 1966 -106 C ATOM 3577 O VAL D 3 -2.603 -5.325 57.665 1.00 31.10 O ANISOU 3577 O VAL D 3 3232 3080 5505 857 1725 -76 O ATOM 3578 CB VAL D 3 -0.850 -2.493 57.061 1.00 32.57 C ANISOU 3578 CB VAL D 3 3071 3296 6008 787 1971 -18 C ATOM 3579 CG1 VAL D 3 -0.979 -0.968 57.139 1.00 31.41 C ANISOU 3579 CG1 VAL D 3 2894 3268 5772 685 1875 -13 C ATOM 3580 CG2 VAL D 3 -0.240 -3.057 58.351 1.00 33.07 C ANISOU 3580 CG2 VAL D 3 2823 3364 6377 842 1740 83 C ATOM 3581 N GLN D 4 -1.511 -5.181 55.715 1.00 34.10 N ANISOU 3581 N GLN D 4 3742 3225 5990 919 2325 -146 N ATOM 3582 CA GLN D 4 -1.312 -6.625 55.604 1.00 35.55 C ANISOU 3582 CA GLN D 4 3971 3256 6277 1019 2449 -157 C ATOM 3583 C GLN D 4 0.144 -6.984 55.855 1.00 37.89 C ANISOU 3583 C GLN D 4 3924 3416 7055 1140 2628 -69 C ATOM 3584 O GLN D 4 1.040 -6.309 55.361 1.00 39.42 O ANISOU 3584 O GLN D 4 3984 3541 7451 1159 2868 -47 O ATOM 3585 CB GLN D 4 -1.753 -7.158 54.236 1.00 36.61 C ANISOU 3585 CB GLN D 4 4515 3248 6147 1016 2734 -274 C ATOM 3586 CG GLN D 4 -2.052 -8.658 54.264 1.00 37.38 C ANISOU 3586 CG GLN D 4 4747 3228 6226 1080 2748 -305 C ATOM 3587 CD GLN D 4 -2.722 -9.161 52.995 1.00 38.23 C ANISOU 3587 CD GLN D 4 5321 3206 5998 1043 2943 -431 C ATOM 3588 OE1 GLN D 4 -2.519 -8.609 51.920 1.00 39.48 O ANISOU 3588 OE1 GLN D 4 5687 3283 6028 1018 3204 -489 O ATOM 3589 NE2 GLN D 4 -3.520 -10.224 53.117 1.00 37.84 N ANISOU 3589 NE2 GLN D 4 5455 3122 5799 1033 2809 -471 N ATOM 3590 N ASN D 5 0.370 -8.042 56.639 1.00 38.33 N ANISOU 3590 N ASN D 5 3825 3423 7313 1222 2504 -8 N ATOM 3591 CA ASN D 5 1.734 -8.501 56.934 1.00 40.90 C ANISOU 3591 CA ASN D 5 3798 3601 8142 1348 2640 94 C ATOM 3592 C ASN D 5 2.161 -9.624 55.997 1.00 43.38 C ANISOU 3592 C ASN D 5 4244 3670 8567 1468 3045 44 C ATOM 3593 O ASN D 5 1.355 -10.110 55.189 1.00 42.88 O ANISOU 3593 O ASN D 5 4574 3557 8158 1442 3179 -73 O ATOM 3594 CB ASN D 5 1.900 -8.877 58.426 1.00 40.38 C ANISOU 3594 CB ASN D 5 3446 3609 8284 1371 2246 217 C ATOM 3595 CG ASN D 5 1.091 -10.100 58.853 1.00 39.45 C ANISOU 3595 CG ASN D 5 3508 3485 7996 1396 2091 198 C ATOM 3596 OD1 ASN D 5 0.821 -11.012 58.066 1.00 40.06 O ANISOU 3596 OD1 ASN D 5 3822 3429 7970 1447 2329 119 O ATOM 3597 ND2 ASN D 5 0.730 -10.129 60.135 1.00 38.02 N ANISOU 3597 ND2 ASN D 5 3224 3433 7788 1357 1692 276 N ATOM 3598 N LEU D 6 3.419 -10.043 56.127 1.00 46.22 N ANISOU 3598 N LEU D 6 4277 3864 9418 1595 3228 139 N ATOM 3599 CA LEU D 6 4.022 -11.000 55.201 1.00 49.17 C ANISOU 3599 CA LEU D 6 4740 3971 9970 1726 3686 101 C ATOM 3600 C LEU D 6 3.525 -12.442 55.339 1.00 49.32 C ANISOU 3600 C LEU D 6 4942 3896 9899 1794 3651 66 C ATOM 3601 O LEU D 6 3.848 -13.265 54.503 1.00 51.61 O ANISOU 3601 O LEU D 6 5393 3959 10256 1891 4036 9 O ATOM 3602 CB LEU D 6 5.560 -10.927 55.272 1.00 52.43 C ANISOU 3602 CB LEU D 6 4703 4217 10997 1848 3921 227 C ATOM 3603 CG LEU D 6 6.123 -9.556 54.856 1.00 52.93 C ANISOU 3603 CG LEU D 6 4626 4319 11164 1785 4070 246 C ATOM 3604 CD1 LEU D 6 7.620 -9.437 55.099 1.00 56.17 C ANISOU 3604 CD1 LEU D 6 4524 4577 12241 1889 4229 396 C ATOM 3605 CD2 LEU D 6 5.821 -9.261 53.399 1.00 53.47 C ANISOU 3605 CD2 LEU D 6 5115 4296 10905 1752 4508 104 C ATOM 3606 N GLN D 7 2.753 -12.755 56.374 1.00 47.15 N ANISOU 3606 N GLN D 7 4661 3777 9473 1742 3215 100 N ATOM 3607 CA GLN D 7 2.026 -14.033 56.432 1.00 46.96 C ANISOU 3607 CA GLN D 7 4884 3685 9271 1771 3162 49 C ATOM 3608 C GLN D 7 0.530 -13.810 56.082 1.00 44.25 C ANISOU 3608 C GLN D 7 4963 3487 8364 1621 3005 -77 C ATOM 3609 O GLN D 7 -0.301 -14.709 56.205 1.00 43.49 O ANISOU 3609 O GLN D 7 5086 3374 8064 1603 2887 -121 O ATOM 3610 CB GLN D 7 2.293 -14.724 57.792 1.00 47.10 C ANISOU 3610 CB GLN D 7 4602 3725 9569 1836 2832 191 C ATOM 3611 CG GLN D 7 1.287 -15.771 58.328 1.00 45.79 C ANISOU 3611 CG GLN D 7 4647 3584 9166 1816 2595 171 C ATOM 3612 CD GLN D 7 1.387 -17.158 57.710 1.00 47.86 C ANISOU 3612 CD GLN D 7 5090 3600 9495 1927 2879 117 C ATOM 3613 OE1 GLN D 7 2.457 -17.605 57.289 1.00 50.88 O ANISOU 3613 OE1 GLN D 7 5319 3766 10247 2068 3201 150 O ATOM 3614 NE2 GLN D 7 0.263 -17.864 57.692 1.00 46.48 N ANISOU 3614 NE2 GLN D 7 5233 3443 8982 1864 2759 39 N ATOM 3615 N GLY D 8 0.207 -12.611 55.601 1.00 43.04 N ANISOU 3615 N GLY D 8 4915 3456 7981 1513 3014 -129 N ATOM 3616 CA GLY D 8 -1.072 -12.358 54.958 1.00 41.29 C ANISOU 3616 CA GLY D 8 5103 3315 7267 1382 2947 -250 C ATOM 3617 C GLY D 8 -2.136 -11.790 55.866 1.00 38.32 C ANISOU 3617 C GLY D 8 4708 3187 6662 1261 2509 -223 C ATOM 3618 O GLY D 8 -3.189 -11.355 55.390 1.00 36.84 O ANISOU 3618 O GLY D 8 4801 3086 6110 1145 2422 -303 O ATOM 3619 N GLN D 9 -1.882 -11.772 57.174 1.00 37.67 N ANISOU 3619 N GLN D 9 4311 3209 6793 1284 2230 -107 N ATOM 3620 CA GLN D 9 -2.892 -11.305 58.120 1.00 35.08 C ANISOU 3620 CA GLN D 9 3984 3093 6250 1178 1844 -79 C ATOM 3621 C GLN D 9 -3.130 -9.817 57.969 1.00 33.74 C ANISOU 3621 C GLN D 9 3809 3078 5929 1076 1779 -96 C ATOM 3622 O GLN D 9 -2.193 -9.053 57.748 1.00 34.59 O ANISOU 3622 O GLN D 9 3738 3169 6232 1100 1918 -66 O ATOM 3623 CB GLN D 9 -2.463 -11.555 59.556 1.00 35.02 C ANISOU 3623 CB GLN D 9 3674 3140 6489 1223 1574 53 C ATOM 3624 CG GLN D 9 -2.326 -13.011 59.942 1.00 36.20 C ANISOU 3624 CG GLN D 9 3812 3156 6787 1318 1566 94 C ATOM 3625 CD GLN D 9 -1.447 -13.179 61.156 1.00 37.15 C ANISOU 3625 CD GLN D 9 3594 3274 7246 1390 1364 244 C ATOM 3626 OE1 GLN D 9 -0.531 -12.386 61.386 1.00 37.90 O ANISOU 3626 OE1 GLN D 9 3427 3391 7581 1405 1348 312 O ATOM 3627 NE2 GLN D 9 -1.714 -14.216 61.938 1.00 37.25 N ANISOU 3627 NE2 GLN D 9 3615 3249 7287 1428 1195 303 N ATOM 3628 N MET D 10 -4.387 -9.414 58.107 1.00 31.78 N ANISOU 3628 N MET D 10 3743 2970 5359 964 1571 -135 N ATOM 3629 CA MET D 10 -4.733 -8.000 58.173 1.00 30.49 C ANISOU 3629 CA MET D 10 3562 2965 5057 868 1459 -138 C ATOM 3630 C MET D 10 -4.573 -7.580 59.614 1.00 29.50 C ANISOU 3630 C MET D 10 3178 2969 5059 858 1173 -37 C ATOM 3631 O MET D 10 -5.226 -8.148 60.490 1.00 28.49 O ANISOU 3631 O MET D 10 3068 2891 4864 845 958 -3 O ATOM 3632 CB MET D 10 -6.179 -7.765 57.733 1.00 29.10 C ANISOU 3632 CB MET D 10 3675 2865 4514 758 1352 -211 C ATOM 3633 CG MET D 10 -6.441 -8.171 56.288 1.00 30.33 C ANISOU 3633 CG MET D 10 4151 2883 4491 745 1585 -314 C ATOM 3634 SD MET D 10 -5.598 -7.102 55.126 1.00 32.00 S ANISOU 3634 SD MET D 10 4413 3035 4709 744 1887 -353 S ATOM 3635 CE MET D 10 -5.907 -7.980 53.592 1.00 33.75 C ANISOU 3635 CE MET D 10 5075 3048 4700 739 2150 -472 C ATOM 3636 N VAL D 11 -3.708 -6.589 59.845 1.00 29.88 N ANISOU 3636 N VAL D 11 3009 3057 5285 856 1174 10 N ATOM 3637 CA VAL D 11 -3.302 -6.183 61.195 1.00 29.57 C ANISOU 3637 CA VAL D 11 2727 3106 5402 847 904 111 C ATOM 3638 C VAL D 11 -3.381 -4.673 61.380 1.00 28.56 C ANISOU 3638 C VAL D 11 2552 3105 5192 755 807 111 C ATOM 3639 O VAL D 11 -3.219 -3.907 60.425 1.00 28.72 O ANISOU 3639 O VAL D 11 2623 3115 5174 728 999 60 O ATOM 3640 CB VAL D 11 -1.853 -6.627 61.517 1.00 31.86 C ANISOU 3640 CB VAL D 11 2718 3273 6111 948 954 204 C ATOM 3641 CG1 VAL D 11 -1.721 -8.129 61.422 1.00 33.07 C ANISOU 3641 CG1 VAL D 11 2902 3287 6376 1051 1047 215 C ATOM 3642 CG2 VAL D 11 -0.849 -5.947 60.592 1.00 33.38 C ANISOU 3642 CG2 VAL D 11 2784 3386 6511 972 1232 193 C ATOM 3643 N HIS D 12 -3.606 -4.250 62.618 1.00 27.65 N ANISOU 3643 N HIS D 12 2363 3096 5046 706 516 169 N ATOM 3644 CA HIS D 12 -3.645 -2.847 62.918 1.00 26.93 C ANISOU 3644 CA HIS D 12 2232 3110 4888 621 410 170 C ATOM 3645 C HIS D 12 -2.241 -2.248 62.842 1.00 28.85 C ANISOU 3645 C HIS D 12 2211 3293 5456 639 469 224 C ATOM 3646 O HIS D 12 -1.270 -2.852 63.269 1.00 30.50 O ANISOU 3646 O HIS D 12 2209 3414 5966 706 428 304 O ATOM 3647 CB HIS D 12 -4.235 -2.600 64.296 1.00 25.81 C ANISOU 3647 CB HIS D 12 2118 3071 4617 564 102 215 C ATOM 3648 CG HIS D 12 -4.365 -1.149 64.628 1.00 25.01 C ANISOU 3648 CG HIS D 12 2012 3065 4422 473 0 206 C ATOM 3649 ND1 HIS D 12 -5.205 -0.303 63.934 1.00 23.59 N ANISOU 3649 ND1 HIS D 12 1987 2953 4022 415 96 131 N ATOM 3650 CD2 HIS D 12 -3.749 -0.391 65.563 1.00 25.51 C ANISOU 3650 CD2 HIS D 12 1948 3156 4589 428 -200 263 C ATOM 3651 CE1 HIS D 12 -5.104 0.914 64.435 1.00 23.35 C ANISOU 3651 CE1 HIS D 12 1918 2986 3967 345 -17 141 C ATOM 3652 NE2 HIS D 12 -4.217 0.890 65.416 1.00 24.55 N ANISOU 3652 NE2 HIS D 12 1907 3113 4306 347 -197 215 N ATOM 3653 N GLN D 13 -2.156 -1.071 62.245 1.00 28.77 N ANISOU 3653 N GLN D 13 2209 3320 5402 580 573 186 N ATOM 3654 CA GLN D 13 -0.986 -0.223 62.351 1.00 30.49 C ANISOU 3654 CA GLN D 13 2176 3503 5903 562 576 242 C ATOM 3655 C GLN D 13 -1.449 1.053 63.034 1.00 29.33 C ANISOU 3655 C GLN D 13 2075 3482 5587 452 356 236 C ATOM 3656 O GLN D 13 -2.482 1.619 62.645 1.00 27.51 O ANISOU 3656 O GLN D 13 2062 3333 5056 398 393 164 O ATOM 3657 CB GLN D 13 -0.439 0.079 60.972 1.00 31.54 C ANISOU 3657 CB GLN D 13 2301 3545 6137 587 937 202 C ATOM 3658 CG GLN D 13 0.864 0.816 60.958 1.00 33.53 C ANISOU 3658 CG GLN D 13 2260 3730 6749 579 997 269 C ATOM 3659 CD GLN D 13 1.310 1.123 59.541 1.00 34.77 C ANISOU 3659 CD GLN D 13 2454 3785 6969 601 1403 226 C ATOM 3660 OE1 GLN D 13 0.553 1.708 58.754 1.00 33.50 O ANISOU 3660 OE1 GLN D 13 2549 3673 6505 550 1526 146 O ATOM 3661 NE2 GLN D 13 2.525 0.706 59.198 1.00 37.28 N ANISOU 3661 NE2 GLN D 13 2528 3948 7686 681 1621 286 N ATOM 3662 N ALA D 14 -0.708 1.484 64.057 1.00 30.66 N ANISOU 3662 N ALA D 14 2048 3651 5949 416 116 314 N ATOM 3663 CA ALA D 14 -1.060 2.690 64.806 1.00 30.22 C ANISOU 3663 CA ALA D 14 2049 3690 5739 308 -100 308 C ATOM 3664 C ALA D 14 -1.082 3.905 63.885 1.00 30.21 C ANISOU 3664 C ALA D 14 2080 3710 5686 252 88 252 C ATOM 3665 O ALA D 14 -0.291 4.009 62.970 1.00 31.43 O ANISOU 3665 O ALA D 14 2105 3782 6053 281 323 258 O ATOM 3666 CB ALA D 14 -0.085 2.917 65.942 1.00 31.88 C ANISOU 3666 CB ALA D 14 2050 3864 6197 271 -390 404 C ATOM 3667 N ILE D 15 -2.017 4.811 64.110 1.00 29.33 N ANISOU 3667 N ILE D 15 2154 3695 5293 176 5 201 N ATOM 3668 CA ILE D 15 -2.000 6.102 63.415 1.00 29.73 C ANISOU 3668 CA ILE D 15 2231 3763 5303 112 133 163 C ATOM 3669 C ILE D 15 -0.665 6.872 63.678 1.00 32.07 C ANISOU 3669 C ILE D 15 2264 3994 5924 63 73 225 C ATOM 3670 O ILE D 15 -0.151 6.913 64.799 1.00 32.84 O ANISOU 3670 O ILE D 15 2242 4082 6154 27 -199 284 O ATOM 3671 CB ILE D 15 -3.201 6.943 63.835 1.00 27.94 C ANISOU 3671 CB ILE D 15 2221 3636 4756 43 14 113 C ATOM 3672 CG1 ILE D 15 -3.404 8.103 62.867 1.00 27.71 C ANISOU 3672 CG1 ILE D 15 2265 3617 4644 -3 189 69 C ATOM 3673 CG2 ILE D 15 -3.002 7.440 65.261 1.00 28.32 C ANISOU 3673 CG2 ILE D 15 2233 3708 4817 -22 -285 150 C ATOM 3674 CD1 ILE D 15 -4.660 8.941 63.177 1.00 26.15 C ANISOU 3674 CD1 ILE D 15 2276 3505 4155 -57 99 25 C ATOM 3675 N SER D 16 -0.091 7.449 62.631 1.00 33.69 N ANISOU 3675 N SER D 16 2391 4142 6268 56 324 217 N ATOM 3676 CA SER D 16 1.199 8.113 62.775 1.00 36.46 C ANISOU 3676 CA SER D 16 2463 4413 6976 10 299 284 C ATOM 3677 C SER D 16 1.022 9.355 63.652 1.00 36.26 C ANISOU 3677 C SER D 16 2477 4445 6852 -109 36 280 C ATOM 3678 O SER D 16 0.062 10.106 63.467 1.00 34.63 O ANISOU 3678 O SER D 16 2498 4315 6344 -152 62 212 O ATOM 3679 CB SER D 16 1.810 8.476 61.414 1.00 38.04 C ANISOU 3679 CB SER D 16 2591 4524 7335 28 673 278 C ATOM 3680 OG SER D 16 0.799 8.662 60.432 1.00 36.85 O ANISOU 3680 OG SER D 16 2735 4420 6844 37 883 195 O ATOM 3681 N PRO D 17 1.930 9.560 64.619 1.00 38.05 N ANISOU 3681 N PRO D 17 2493 4623 7338 -164 -228 354 N ATOM 3682 CA PRO D 17 1.868 10.732 65.491 1.00 38.05 C ANISOU 3682 CA PRO D 17 2549 4651 7254 -289 -491 347 C ATOM 3683 C PRO D 17 1.952 12.049 64.717 1.00 37.97 C ANISOU 3683 C PRO D 17 2550 4631 7245 -360 -310 311 C ATOM 3684 O PRO D 17 1.364 13.049 65.141 1.00 36.74 O ANISOU 3684 O PRO D 17 2567 4523 6867 -443 -429 264 O ATOM 3685 CB PRO D 17 3.110 10.584 66.386 1.00 40.75 C ANISOU 3685 CB PRO D 17 2612 4900 7968 -333 -777 452 C ATOM 3686 CG PRO D 17 3.505 9.166 66.280 1.00 41.65 C ANISOU 3686 CG PRO D 17 2579 4968 8278 -216 -725 511 C ATOM 3687 CD PRO D 17 3.098 8.714 64.916 1.00 40.51 C ANISOU 3687 CD PRO D 17 2503 4831 8054 -116 -303 454 C ATOM 3688 N ARG D 18 2.685 12.048 63.602 1.00 39.14 N ANISOU 3688 N ARG D 18 2525 4701 7645 -325 -8 337 N ATOM 3689 CA ARG D 18 2.778 13.240 62.760 1.00 39.17 C ANISOU 3689 CA ARG D 18 2553 4680 7647 -386 201 311 C ATOM 3690 C ARG D 18 1.491 13.577 62.006 1.00 36.28 C ANISOU 3690 C ARG D 18 2515 4399 6870 -366 381 222 C ATOM 3691 O ARG D 18 1.247 14.735 61.668 1.00 35.81 O ANISOU 3691 O ARG D 18 2553 4345 6707 -436 441 193 O ATOM 3692 CB ARG D 18 3.947 13.125 61.797 1.00 41.76 C ANISOU 3692 CB ARG D 18 2618 4881 8366 -355 500 372 C ATOM 3693 CG ARG D 18 5.259 13.481 62.473 1.00 44.83 C ANISOU 3693 CG ARG D 18 2653 5168 9210 -430 305 470 C ATOM 3694 CD ARG D 18 6.122 12.270 62.855 1.00 46.98 C ANISOU 3694 CD ARG D 18 2643 5362 9844 -352 228 561 C ATOM 3695 NE ARG D 18 7.311 12.229 62.008 1.00 50.11 N ANISOU 3695 NE ARG D 18 2723 5607 10706 -321 534 638 N ATOM 3696 CZ ARG D 18 8.247 13.183 61.998 1.00 52.41 C ANISOU 3696 CZ ARG D 18 2764 5804 11344 -421 522 703 C ATOM 3697 NH1 ARG D 18 8.136 14.262 62.784 1.00 52.29 N ANISOU 3697 NH1 ARG D 18 2797 5828 11242 -563 202 692 N ATOM 3698 NH2 ARG D 18 9.293 13.071 61.185 1.00 55.32 N ANISOU 3698 NH2 ARG D 18 2841 6023 12155 -381 851 778 N ATOM 3699 N THR D 19 0.678 12.559 61.753 1.00 34.31 N ANISOU 3699 N THR D 19 2428 4202 6406 -275 450 185 N ATOM 3700 CA THR D 19 -0.629 12.726 61.145 1.00 31.76 C ANISOU 3700 CA THR D 19 2405 3953 5706 -256 557 113 C ATOM 3701 C THR D 19 -1.614 13.251 62.193 1.00 29.57 C ANISOU 3701 C THR D 19 2292 3769 5175 -308 287 78 C ATOM 3702 O THR D 19 -2.407 14.153 61.902 1.00 28.43 O ANISOU 3702 O THR D 19 2323 3661 4817 -345 324 38 O ATOM 3703 CB THR D 19 -1.070 11.400 60.498 1.00 31.50 C ANISOU 3703 CB THR D 19 2473 3922 5573 -151 714 92 C ATOM 3704 OG1 THR D 19 -0.190 11.136 59.397 1.00 33.61 O ANISOU 3704 OG1 THR D 19 2641 4081 6048 -110 1025 114 O ATOM 3705 CG2 THR D 19 -2.492 11.445 59.994 1.00 29.60 C ANISOU 3705 CG2 THR D 19 2533 3754 4961 -140 754 29 C ATOM 3706 N LEU D 20 -1.546 12.727 63.415 1.00 29.05 N ANISOU 3706 N LEU D 20 2177 3725 5136 -311 26 100 N ATOM 3707 CA LEU D 20 -2.260 13.343 64.548 1.00 27.82 C ANISOU 3707 CA LEU D 20 2174 3623 4773 -373 -217 73 C ATOM 3708 C LEU D 20 -1.864 14.812 64.731 1.00 28.09 C ANISOU 3708 C LEU D 20 2187 3621 4862 -481 -276 68 C ATOM 3709 O LEU D 20 -2.730 15.677 64.859 1.00 26.92 O ANISOU 3709 O LEU D 20 2230 3508 4490 -517 -286 20 O ATOM 3710 CB LEU D 20 -1.991 12.614 65.867 1.00 28.51 C ANISOU 3710 CB LEU D 20 2217 3706 4906 -375 -497 111 C ATOM 3711 CG LEU D 20 -2.889 11.440 66.224 1.00 27.50 C ANISOU 3711 CG LEU D 20 2227 3633 4587 -297 -529 100 C ATOM 3712 CD1 LEU D 20 -2.337 10.711 67.460 1.00 28.70 C ANISOU 3712 CD1 LEU D 20 2312 3755 4836 -303 -804 158 C ATOM 3713 CD2 LEU D 20 -4.357 11.881 66.417 1.00 25.51 C ANISOU 3713 CD2 LEU D 20 2242 3451 3997 -304 -512 39 C ATOM 3714 N ASN D 21 -0.559 15.077 64.761 1.00 29.61 N ANISOU 3714 N ASN D 21 2139 3733 5378 -531 -316 122 N ATOM 3715 CA ASN D 21 -0.033 16.437 64.936 1.00 30.29 C ANISOU 3715 CA ASN D 21 2176 3765 5565 -647 -385 124 C ATOM 3716 C ASN D 21 -0.489 17.398 63.861 1.00 28.96 C ANISOU 3716 C ASN D 21 2118 3600 5284 -659 -132 85 C ATOM 3717 O ASN D 21 -0.837 18.545 64.153 1.00 28.57 O ANISOU 3717 O ASN D 21 2190 3547 5115 -736 -200 52 O ATOM 3718 CB ASN D 21 1.484 16.423 64.949 1.00 33.12 C ANISOU 3718 CB ASN D 21 2209 4020 6353 -692 -434 205 C ATOM 3719 CG ASN D 21 2.054 15.955 66.267 1.00 34.77 C ANISOU 3719 CG ASN D 21 2319 4198 6694 -733 -797 255 C ATOM 3720 OD1 ASN D 21 1.417 16.089 67.327 1.00 34.43 O ANISOU 3720 OD1 ASN D 21 2487 4193 6399 -773 -1043 220 O ATOM 3721 ND2 ASN D 21 3.275 15.420 66.222 1.00 37.04 N ANISOU 3721 ND2 ASN D 21 2288 4399 7386 -725 -834 345 N ATOM 3722 N ALA D 22 -0.482 16.918 62.618 1.00 28.26 N ANISOU 3722 N ALA D 22 2007 3505 5223 -583 158 92 N ATOM 3723 CA ALA D 22 -0.956 17.688 61.481 1.00 27.23 C ANISOU 3723 CA ALA D 22 2018 3370 4957 -586 403 65 C ATOM 3724 C ALA D 22 -2.413 18.085 61.717 1.00 24.81 C ANISOU 3724 C ALA D 22 1986 3144 4294 -578 329 7 C ATOM 3725 O ALA D 22 -2.777 19.246 61.551 1.00 24.41 O ANISOU 3725 O ALA D 22 2043 3082 4148 -632 352 -10 O ATOM 3726 CB ALA D 22 -0.813 16.884 60.189 1.00 27.41 C ANISOU 3726 CB ALA D 22 2038 3363 5010 -500 706 76 C ATOM 3727 N TRP D 23 -3.230 17.118 62.121 1.00 23.20 N ANISOU 3727 N TRP D 23 1882 3010 3922 -509 247 -12 N ATOM 3728 CA TRP D 23 -4.648 17.366 62.424 1.00 21.29 C ANISOU 3728 CA TRP D 23 1868 2833 3387 -493 182 -54 C ATOM 3729 C TRP D 23 -4.854 18.361 63.581 1.00 21.23 C ANISOU 3729 C TRP D 23 1929 2820 3318 -569 -10 -77 C ATOM 3730 O TRP D 23 -5.690 19.235 63.476 1.00 20.41 O ANISOU 3730 O TRP D 23 1976 2720 3057 -583 21 -103 O ATOM 3731 CB TRP D 23 -5.377 16.049 62.713 1.00 20.14 C ANISOU 3731 CB TRP D 23 1785 2747 3120 -412 133 -62 C ATOM 3732 CG TRP D 23 -6.793 16.191 63.218 1.00 18.65 C ANISOU 3732 CG TRP D 23 1788 2611 2685 -395 58 -92 C ATOM 3733 CD1 TRP D 23 -7.282 15.748 64.413 1.00 18.18 C ANISOU 3733 CD1 TRP D 23 1787 2582 2538 -386 -102 -100 C ATOM 3734 CD2 TRP D 23 -7.894 16.804 62.542 1.00 17.65 C ANISOU 3734 CD2 TRP D 23 1813 2497 2394 -382 152 -107 C ATOM 3735 NE1 TRP D 23 -8.601 16.042 64.523 1.00 17.05 N ANISOU 3735 NE1 TRP D 23 1805 2465 2206 -365 -85 -121 N ATOM 3736 CE2 TRP D 23 -9.011 16.687 63.385 1.00 16.72 C ANISOU 3736 CE2 TRP D 23 1809 2415 2127 -361 55 -122 C ATOM 3737 CE3 TRP D 23 -8.044 17.441 61.302 1.00 17.70 C ANISOU 3737 CE3 TRP D 23 1877 2477 2370 -387 308 -101 C ATOM 3738 CZ2 TRP D 23 -10.268 17.182 63.032 1.00 15.89 C ANISOU 3738 CZ2 TRP D 23 1833 2317 1885 -340 104 -125 C ATOM 3739 CZ3 TRP D 23 -9.287 17.934 60.951 1.00 16.77 C ANISOU 3739 CZ3 TRP D 23 1909 2370 2091 -371 325 -103 C ATOM 3740 CH2 TRP D 23 -10.383 17.797 61.813 1.00 15.92 C ANISOU 3740 CH2 TRP D 23 1873 2297 1877 -345 221 -113 C ATOM 3741 N VAL D 24 -4.098 18.225 64.669 1.00 22.22 N ANISOU 3741 N VAL D 24 1958 2920 3565 -619 -215 -63 N ATOM 3742 CA VAL D 24 -4.173 19.169 65.784 1.00 22.67 C ANISOU 3742 CA VAL D 24 2115 2945 3552 -705 -407 -90 C ATOM 3743 C VAL D 24 -3.864 20.561 65.282 1.00 23.37 C ANISOU 3743 C VAL D 24 2199 2975 3705 -782 -326 -98 C ATOM 3744 O VAL D 24 -4.551 21.525 65.624 1.00 22.84 O ANISOU 3744 O VAL D 24 2305 2892 3479 -816 -346 -139 O ATOM 3745 CB VAL D 24 -3.180 18.788 66.900 1.00 24.24 C ANISOU 3745 CB VAL D 24 2203 3101 3904 -764 -667 -59 C ATOM 3746 CG1 VAL D 24 -2.977 19.925 67.880 1.00 25.25 C ANISOU 3746 CG1 VAL D 24 2437 3162 3992 -883 -865 -87 C ATOM 3747 CG2 VAL D 24 -3.672 17.545 67.603 1.00 23.63 C ANISOU 3747 CG2 VAL D 24 2197 3075 3706 -696 -770 -53 C ATOM 3748 N LYS D 25 -2.821 20.637 64.458 1.00 24.66 N ANISOU 3748 N LYS D 25 2162 3093 4114 -804 -213 -56 N ATOM 3749 CA LYS D 25 -2.338 21.890 63.844 1.00 25.74 C ANISOU 3749 CA LYS D 25 2259 3158 4361 -880 -105 -50 C ATOM 3750 C LYS D 25 -3.392 22.526 62.920 1.00 24.21 C ANISOU 3750 C LYS D 25 2254 2986 3956 -840 93 -74 C ATOM 3751 O LYS D 25 -3.547 23.746 62.919 1.00 24.24 O ANISOU 3751 O LYS D 25 2344 2941 3922 -903 101 -90 O ATOM 3752 CB LYS D 25 -1.010 21.595 63.091 1.00 27.61 C ANISOU 3752 CB LYS D 25 2225 3333 4929 -894 22 12 C ATOM 3753 CG LYS D 25 -0.271 22.765 62.522 1.00 29.28 C ANISOU 3753 CG LYS D 25 2348 3453 5324 -984 135 37 C ATOM 3754 CD LYS D 25 0.564 23.516 63.579 1.00 31.16 C ANISOU 3754 CD LYS D 25 2474 3612 5751 -1118 -128 47 C ATOM 3755 CE LYS D 25 1.673 24.340 62.942 1.00 33.29 C ANISOU 3755 CE LYS D 25 2541 3769 6335 -1208 -2 99 C ATOM 3756 NZ LYS D 25 1.188 25.607 62.266 1.00 33.00 N ANISOU 3756 NZ LYS D 25 2672 3700 6163 -1247 167 74 N ATOM 3757 N VAL D 26 -4.111 21.701 62.159 1.00 22.91 N ANISOU 3757 N VAL D 26 2161 2883 3662 -740 233 -72 N ATOM 3758 CA VAL D 26 -5.153 22.191 61.255 1.00 21.97 C ANISOU 3758 CA VAL D 26 2221 2776 3348 -701 381 -80 C ATOM 3759 C VAL D 26 -6.282 22.827 62.078 1.00 21.17 C ANISOU 3759 C VAL D 26 2291 2692 3057 -703 260 -118 C ATOM 3760 O VAL D 26 -6.713 23.951 61.801 1.00 21.06 O ANISOU 3760 O VAL D 26 2382 2637 2981 -730 311 -122 O ATOM 3761 CB VAL D 26 -5.703 21.073 60.309 1.00 21.13 C ANISOU 3761 CB VAL D 26 2171 2717 3139 -605 513 -69 C ATOM 3762 CG1 VAL D 26 -6.928 21.545 59.556 1.00 20.10 C ANISOU 3762 CG1 VAL D 26 2241 2596 2799 -572 586 -69 C ATOM 3763 CG2 VAL D 26 -4.632 20.643 59.293 1.00 22.37 C ANISOU 3763 CG2 VAL D 26 2209 2824 3467 -600 710 -35 C ATOM 3764 N VAL D 27 -6.701 22.142 63.133 1.00 20.76 N ANISOU 3764 N VAL D 27 2271 2686 2929 -676 111 -141 N ATOM 3765 CA VAL D 27 -7.719 22.682 64.039 1.00 20.37 C ANISOU 3765 CA VAL D 27 2389 2634 2715 -675 26 -178 C ATOM 3766 C VAL D 27 -7.279 23.948 64.810 1.00 21.71 C ANISOU 3766 C VAL D 27 2609 2722 2917 -774 -65 -208 C ATOM 3767 O VAL D 27 -8.063 24.906 64.934 1.00 21.50 O ANISOU 3767 O VAL D 27 2730 2655 2785 -777 -26 -231 O ATOM 3768 CB VAL D 27 -8.226 21.603 65.001 1.00 19.74 C ANISOU 3768 CB VAL D 27 2351 2606 2541 -626 -84 -191 C ATOM 3769 CG1 VAL D 27 -9.363 22.143 65.867 1.00 19.32 C ANISOU 3769 CG1 VAL D 27 2487 2532 2320 -613 -111 -225 C ATOM 3770 CG2 VAL D 27 -8.716 20.393 64.196 1.00 18.69 C ANISOU 3770 CG2 VAL D 27 2181 2541 2378 -535 5 -165 C ATOM 3771 N GLU D 28 -6.045 23.995 65.299 1.00 23.33 N ANISOU 3771 N GLU D 28 2693 2886 3283 -859 -191 -204 N ATOM 3772 CA GLU D 28 -5.586 25.206 65.963 1.00 24.88 C ANISOU 3772 CA GLU D 28 2947 2989 3516 -971 -297 -233 C ATOM 3773 C GLU D 28 -5.670 26.420 65.033 1.00 25.10 C ANISOU 3773 C GLU D 28 3000 2962 3575 -997 -136 -226 C ATOM 3774 O GLU D 28 -6.097 27.489 65.449 1.00 25.22 O ANISOU 3774 O GLU D 28 3168 2910 3505 -1038 -151 -263 O ATOM 3775 CB GLU D 28 -4.157 25.066 66.442 1.00 26.88 C ANISOU 3775 CB GLU D 28 3025 3194 3992 -1069 -472 -210 C ATOM 3776 CG GLU D 28 -4.008 24.170 67.633 1.00 27.51 C ANISOU 3776 CG GLU D 28 3131 3292 4027 -1074 -698 -217 C ATOM 3777 CD GLU D 28 -2.542 23.942 68.036 1.00 29.74 C ANISOU 3777 CD GLU D 28 3200 3518 4579 -1168 -904 -172 C ATOM 3778 OE1 GLU D 28 -1.615 24.618 67.502 1.00 31.11 O ANISOU 3778 OE1 GLU D 28 3203 3625 4990 -1246 -874 -142 O ATOM 3779 OE2 GLU D 28 -2.338 23.072 68.914 1.00 30.54 O ANISOU 3779 OE2 GLU D 28 3304 3632 4666 -1166 -1103 -159 O ATOM 3780 N GLU D 29 -5.256 26.261 63.779 1.00 25.28 N ANISOU 3780 N GLU D 29 2891 2997 3713 -974 29 -177 N ATOM 3781 CA GLU D 29 -5.205 27.401 62.855 1.00 25.86 C ANISOU 3781 CA GLU D 29 2994 3006 3824 -1009 183 -158 C ATOM 3782 C GLU D 29 -6.555 27.731 62.244 1.00 24.42 C ANISOU 3782 C GLU D 29 2988 2842 3445 -925 303 -156 C ATOM 3783 O GLU D 29 -6.916 28.894 62.128 1.00 24.60 O ANISOU 3783 O GLU D 29 3120 2796 3430 -954 345 -161 O ATOM 3784 CB GLU D 29 -4.197 27.153 61.741 1.00 27.01 C ANISOU 3784 CB GLU D 29 2963 3133 4165 -1023 339 -101 C ATOM 3785 CG GLU D 29 -2.784 27.088 62.262 1.00 29.08 C ANISOU 3785 CG GLU D 29 3008 3341 4697 -1119 229 -84 C ATOM 3786 CD GLU D 29 -1.748 27.076 61.156 1.00 30.72 C ANISOU 3786 CD GLU D 29 3032 3496 5142 -1141 434 -22 C ATOM 3787 OE1 GLU D 29 -2.111 26.682 60.014 1.00 30.34 O ANISOU 3787 OE1 GLU D 29 3041 3475 5010 -1061 656 1 O ATOM 3788 OE2 GLU D 29 -0.574 27.458 61.426 1.00 32.85 O ANISOU 3788 OE2 GLU D 29 3110 3683 5687 -1243 375 5 O ATOM 3789 N LYS D 30 -7.299 26.702 61.865 1.00 23.03 N ANISOU 3789 N LYS D 30 2836 2751 3163 -825 345 -142 N ATOM 3790 CA LYS D 30 -8.454 26.885 61.023 1.00 22.04 C ANISOU 3790 CA LYS D 30 2837 2635 2900 -751 449 -116 C ATOM 3791 C LYS D 30 -9.779 26.583 61.709 1.00 20.67 C ANISOU 3791 C LYS D 30 2769 2499 2584 -677 380 -136 C ATOM 3792 O LYS D 30 -10.811 26.703 61.083 1.00 19.98 O ANISOU 3792 O LYS D 30 2764 2413 2414 -615 436 -103 O ATOM 3793 CB LYS D 30 -8.272 26.049 59.747 1.00 22.10 C ANISOU 3793 CB LYS D 30 2807 2679 2909 -707 574 -71 C ATOM 3794 CG LYS D 30 -7.126 26.563 58.842 1.00 23.66 C ANISOU 3794 CG LYS D 30 2938 2809 3243 -772 719 -38 C ATOM 3795 CD LYS D 30 -6.970 25.688 57.577 1.00 24.01 C ANISOU 3795 CD LYS D 30 2998 2867 3256 -724 876 -1 C ATOM 3796 CE LYS D 30 -6.072 26.347 56.528 1.00 25.74 C ANISOU 3796 CE LYS D 30 3213 2995 3570 -779 1076 40 C ATOM 3797 NZ LYS D 30 -6.083 25.584 55.231 1.00 26.15 N ANISOU 3797 NZ LYS D 30 3364 3038 3534 -731 1253 72 N ATOM 3798 N ALA D 31 -9.748 26.212 62.989 1.00 20.44 N ANISOU 3798 N ALA D 31 2741 2486 2536 -688 259 -181 N ATOM 3799 CA ALA D 31 -10.964 25.867 63.721 1.00 19.56 C ANISOU 3799 CA ALA D 31 2731 2397 2303 -618 229 -197 C ATOM 3800 C ALA D 31 -11.711 24.820 62.892 1.00 18.38 C ANISOU 3800 C ALA D 31 2550 2321 2112 -530 277 -154 C ATOM 3801 O ALA D 31 -11.099 23.850 62.460 1.00 18.39 O ANISOU 3801 O ALA D 31 2458 2376 2151 -525 273 -142 O ATOM 3802 CB ALA D 31 -11.817 27.125 63.977 1.00 19.76 C ANISOU 3802 CB ALA D 31 2892 2335 2280 -611 280 -208 C ATOM 3803 N PHE D 32 -13.002 25.004 62.624 1.00 17.72 N ANISOU 3803 N PHE D 32 2538 2224 1967 -464 320 -125 N ATOM 3804 CA PHE D 32 -13.707 24.092 61.707 1.00 16.85 C ANISOU 3804 CA PHE D 32 2408 2166 1827 -399 337 -77 C ATOM 3805 C PHE D 32 -14.188 24.804 60.454 1.00 16.87 C ANISOU 3805 C PHE D 32 2465 2122 1821 -387 392 -19 C ATOM 3806 O PHE D 32 -15.290 24.587 59.985 1.00 16.48 O ANISOU 3806 O PHE D 32 2444 2068 1746 -332 374 29 O ATOM 3807 CB PHE D 32 -14.820 23.358 62.445 1.00 16.32 C ANISOU 3807 CB PHE D 32 2353 2125 1723 -334 302 -74 C ATOM 3808 CG PHE D 32 -14.294 22.478 63.530 1.00 16.27 C ANISOU 3808 CG PHE D 32 2316 2163 1700 -346 242 -119 C ATOM 3809 CD1 PHE D 32 -13.840 21.191 63.233 1.00 15.98 C ANISOU 3809 CD1 PHE D 32 2205 2196 1670 -335 206 -114 C ATOM 3810 CD2 PHE D 32 -14.171 22.949 64.829 1.00 16.80 C ANISOU 3810 CD2 PHE D 32 2453 2189 1739 -374 215 -166 C ATOM 3811 CE1 PHE D 32 -13.292 20.357 64.236 1.00 16.01 C ANISOU 3811 CE1 PHE D 32 2178 2232 1669 -345 132 -144 C ATOM 3812 CE2 PHE D 32 -13.624 22.151 65.834 1.00 16.94 C ANISOU 3812 CE2 PHE D 32 2471 2237 1728 -395 130 -198 C ATOM 3813 CZ PHE D 32 -13.177 20.848 65.539 1.00 16.57 C ANISOU 3813 CZ PHE D 32 2324 2265 1705 -378 82 -182 C ATOM 3814 N SER D 33 -13.336 25.659 59.902 1.00 17.43 N ANISOU 3814 N SER D 33 2550 2148 1925 -446 448 -16 N ATOM 3815 CA SER D 33 -13.621 26.258 58.608 1.00 17.82 C ANISOU 3815 CA SER D 33 2677 2146 1946 -443 501 46 C ATOM 3816 C SER D 33 -13.678 25.146 57.548 1.00 17.48 C ANISOU 3816 C SER D 33 2656 2146 1836 -420 506 78 C ATOM 3817 O SER D 33 -13.144 24.073 57.759 1.00 16.89 O ANISOU 3817 O SER D 33 2515 2133 1769 -418 502 44 O ATOM 3818 CB SER D 33 -12.588 27.352 58.285 1.00 18.86 C ANISOU 3818 CB SER D 33 2822 2211 2131 -519 582 43 C ATOM 3819 OG SER D 33 -11.267 26.838 58.238 1.00 19.28 O ANISOU 3819 OG SER D 33 2785 2293 2247 -571 626 14 O ATOM 3820 N PRO D 34 -14.360 25.386 56.412 1.00 17.85 N ANISOU 3820 N PRO D 34 2817 2149 1814 -403 501 145 N ATOM 3821 CA PRO D 34 -14.542 24.309 55.418 1.00 17.94 C ANISOU 3821 CA PRO D 34 2901 2183 1732 -387 484 170 C ATOM 3822 C PRO D 34 -13.246 23.615 54.950 1.00 18.37 C ANISOU 3822 C PRO D 34 2950 2255 1775 -422 603 134 C ATOM 3823 O PRO D 34 -13.266 22.441 54.595 1.00 18.07 O ANISOU 3823 O PRO D 34 2934 2249 1681 -401 596 123 O ATOM 3824 CB PRO D 34 -15.235 25.003 54.236 1.00 18.80 C ANISOU 3824 CB PRO D 34 3172 2209 1760 -389 454 254 C ATOM 3825 CG PRO D 34 -15.488 26.405 54.650 1.00 19.08 C ANISOU 3825 CG PRO D 34 3193 2184 1870 -392 461 277 C ATOM 3826 CD PRO D 34 -15.077 26.623 56.060 1.00 18.43 C ANISOU 3826 CD PRO D 34 2971 2138 1891 -396 488 204 C ATOM 3827 N GLU D 35 -12.128 24.327 54.990 1.00 19.17 N ANISOU 3827 N GLU D 35 3008 2323 1951 -473 719 117 N ATOM 3828 CA GLU D 35 -10.827 23.767 54.600 1.00 20.02 C ANISOU 3828 CA GLU D 35 3069 2427 2109 -502 862 93 C ATOM 3829 C GLU D 35 -10.427 22.536 55.443 1.00 19.23 C ANISOU 3829 C GLU D 35 2817 2403 2084 -475 820 42 C ATOM 3830 O GLU D 35 -9.573 21.731 55.055 1.00 19.73 O ANISOU 3830 O GLU D 35 2842 2463 2191 -474 928 29 O ATOM 3831 CB GLU D 35 -9.760 24.854 54.720 1.00 21.24 C ANISOU 3831 CB GLU D 35 3154 2524 2391 -569 970 92 C ATOM 3832 CG GLU D 35 -9.965 26.066 53.756 1.00 22.50 C ANISOU 3832 CG GLU D 35 3478 2589 2480 -601 1048 150 C ATOM 3833 CD GLU D 35 -11.020 27.137 54.197 1.00 22.34 C ANISOU 3833 CD GLU D 35 3505 2547 2434 -590 921 174 C ATOM 3834 OE1 GLU D 35 -11.227 27.401 55.413 1.00 21.84 O ANISOU 3834 OE1 GLU D 35 3333 2514 2449 -585 826 133 O ATOM 3835 OE2 GLU D 35 -11.647 27.726 53.275 1.00 23.32 O ANISOU 3835 OE2 GLU D 35 3798 2606 2455 -585 925 238 O ATOM 3836 N VAL D 36 -11.065 22.392 56.593 1.00 18.01 N ANISOU 3836 N VAL D 36 2589 2305 1948 -449 675 19 N ATOM 3837 CA VAL D 36 -10.718 21.363 57.546 1.00 17.45 C ANISOU 3837 CA VAL D 36 2389 2298 1943 -429 612 -20 C ATOM 3838 C VAL D 36 -11.298 20.001 57.145 1.00 16.92 C ANISOU 3838 C VAL D 36 2368 2269 1791 -374 587 -18 C ATOM 3839 O VAL D 36 -10.728 18.978 57.469 1.00 16.75 O ANISOU 3839 O VAL D 36 2259 2279 1826 -357 592 -42 O ATOM 3840 CB VAL D 36 -11.130 21.816 58.966 1.00 16.87 C ANISOU 3840 CB VAL D 36 2263 2247 1898 -433 488 -46 C ATOM 3841 CG1 VAL D 36 -11.330 20.679 59.917 1.00 16.19 C ANISOU 3841 CG1 VAL D 36 2114 2224 1813 -396 393 -72 C ATOM 3842 CG2 VAL D 36 -10.090 22.782 59.498 1.00 17.71 C ANISOU 3842 CG2 VAL D 36 2296 2311 2119 -504 499 -65 C ATOM 3843 N ILE D 37 -12.388 20.001 56.391 1.00 16.74 N ANISOU 3843 N ILE D 37 2483 2229 1646 -353 551 15 N ATOM 3844 CA ILE D 37 -13.035 18.766 56.008 1.00 16.43 C ANISOU 3844 CA ILE D 37 2502 2212 1527 -315 499 19 C ATOM 3845 C ILE D 37 -12.115 17.935 55.106 1.00 17.29 C ANISOU 3845 C ILE D 37 2664 2291 1612 -319 633 1 C ATOM 3846 O ILE D 37 -11.770 16.829 55.488 1.00 17.03 O ANISOU 3846 O ILE D 37 2555 2290 1622 -291 635 -27 O ATOM 3847 CB ILE D 37 -14.405 19.035 55.368 1.00 16.51 C ANISOU 3847 CB ILE D 37 2644 2190 1438 -305 397 72 C ATOM 3848 CG1 ILE D 37 -15.289 19.792 56.376 1.00 15.96 C ANISOU 3848 CG1 ILE D 37 2492 2134 1436 -286 306 90 C ATOM 3849 CG2 ILE D 37 -15.058 17.717 54.898 1.00 16.39 C ANISOU 3849 CG2 ILE D 37 2699 2181 1344 -283 321 76 C ATOM 3850 CD1 ILE D 37 -16.684 20.119 55.877 1.00 16.24 C ANISOU 3850 CD1 ILE D 37 2601 2125 1442 -268 194 159 C ATOM 3851 N PRO D 38 -11.658 18.472 53.944 1.00 18.51 N ANISOU 3851 N PRO D 38 2956 2371 1704 -350 767 22 N ATOM 3852 CA PRO D 38 -10.726 17.667 53.130 1.00 19.63 C ANISOU 3852 CA PRO D 38 3161 2464 1834 -347 946 1 C ATOM 3853 C PRO D 38 -9.481 17.196 53.889 1.00 19.92 C ANISOU 3853 C PRO D 38 2973 2524 2071 -335 1037 -30 C ATOM 3854 O PRO D 38 -8.976 16.102 53.632 1.00 20.29 O ANISOU 3854 O PRO D 38 3012 2551 2144 -303 1130 -53 O ATOM 3855 CB PRO D 38 -10.301 18.631 52.006 1.00 20.95 C ANISOU 3855 CB PRO D 38 3490 2537 1931 -391 1106 33 C ATOM 3856 CG PRO D 38 -11.296 19.682 51.980 1.00 20.51 C ANISOU 3856 CG PRO D 38 3511 2480 1799 -410 964 78 C ATOM 3857 CD PRO D 38 -11.800 19.827 53.384 1.00 19.08 C ANISOU 3857 CD PRO D 38 3129 2387 1733 -388 798 63 C ATOM 3858 N MET D 39 -8.982 18.020 54.810 1.00 19.96 N ANISOU 3858 N MET D 39 2802 2555 2226 -361 999 -29 N ATOM 3859 CA MET D 39 -7.796 17.635 55.572 1.00 20.55 C ANISOU 3859 CA MET D 39 2652 2639 2515 -361 1035 -45 C ATOM 3860 C MET D 39 -8.098 16.405 56.421 1.00 19.35 C ANISOU 3860 C MET D 39 2420 2553 2379 -310 902 -67 C ATOM 3861 O MET D 39 -7.350 15.443 56.416 1.00 19.83 O ANISOU 3861 O MET D 39 2389 2598 2548 -279 974 -75 O ATOM 3862 CB MET D 39 -7.277 18.797 56.434 1.00 21.10 C ANISOU 3862 CB MET D 39 2578 2711 2726 -417 971 -39 C ATOM 3863 CG MET D 39 -6.337 19.738 55.694 1.00 22.94 C ANISOU 3863 CG MET D 39 2798 2858 3061 -471 1157 -13 C ATOM 3864 SD MET D 39 -4.714 18.951 55.571 1.00 25.41 S ANISOU 3864 SD MET D 39 2893 3111 3649 -463 1335 -2 S ATOM 3865 CE MET D 39 -3.774 20.137 54.616 1.00 27.27 C ANISOU 3865 CE MET D 39 3130 3228 4002 -531 1589 37 C ATOM 3866 N PHE D 40 -9.207 16.452 57.137 1.00 17.88 N ANISOU 3866 N PHE D 40 2268 2428 2096 -300 724 -72 N ATOM 3867 CA PHE D 40 -9.696 15.307 57.888 1.00 17.01 C ANISOU 3867 CA PHE D 40 2119 2373 1970 -255 605 -86 C ATOM 3868 C PHE D 40 -9.821 14.044 57.044 1.00 17.21 C ANISOU 3868 C PHE D 40 2232 2374 1930 -214 678 -94 C ATOM 3869 O PHE D 40 -9.391 12.988 57.484 1.00 17.18 O ANISOU 3869 O PHE D 40 2137 2381 2007 -178 670 -105 O ATOM 3870 CB PHE D 40 -11.046 15.609 58.549 1.00 15.77 C ANISOU 3870 CB PHE D 40 2020 2261 1710 -249 454 -80 C ATOM 3871 CG PHE D 40 -11.522 14.510 59.430 1.00 15.05 C ANISOU 3871 CG PHE D 40 1885 2215 1614 -211 349 -88 C ATOM 3872 CD1 PHE D 40 -11.025 14.371 60.715 1.00 14.97 C ANISOU 3872 CD1 PHE D 40 1765 2233 1688 -214 266 -98 C ATOM 3873 CD2 PHE D 40 -12.425 13.576 58.963 1.00 14.68 C ANISOU 3873 CD2 PHE D 40 1923 2173 1479 -179 322 -82 C ATOM 3874 CE1 PHE D 40 -11.448 13.350 61.531 1.00 14.50 C ANISOU 3874 CE1 PHE D 40 1689 2207 1613 -179 179 -98 C ATOM 3875 CE2 PHE D 40 -12.844 12.535 59.780 1.00 14.15 C ANISOU 3875 CE2 PHE D 40 1815 2139 1419 -146 239 -84 C ATOM 3876 CZ PHE D 40 -12.361 12.420 61.053 1.00 14.02 C ANISOU 3876 CZ PHE D 40 1698 2152 1476 -143 178 -91 C ATOM 3877 N SER D 41 -10.399 14.140 55.846 1.00 17.59 N ANISOU 3877 N SER D 41 2474 2379 1830 -221 739 -87 N ATOM 3878 CA SER D 41 -10.505 12.953 54.969 1.00 18.26 C ANISOU 3878 CA SER D 41 2693 2418 1825 -194 809 -104 C ATOM 3879 C SER D 41 -9.166 12.427 54.583 1.00 19.51 C ANISOU 3879 C SER D 41 2794 2515 2102 -173 1016 -120 C ATOM 3880 O SER D 41 -8.951 11.220 54.639 1.00 19.69 O ANISOU 3880 O SER D 41 2798 2523 2160 -129 1045 -141 O ATOM 3881 CB SER D 41 -11.224 13.243 53.666 1.00 18.87 C ANISOU 3881 CB SER D 41 3030 2432 1705 -222 830 -90 C ATOM 3882 OG SER D 41 -12.384 13.932 53.956 1.00 18.32 O ANISOU 3882 OG SER D 41 2982 2401 1575 -240 653 -58 O ATOM 3883 N ALA D 42 -8.277 13.323 54.144 1.00 20.63 N ANISOU 3883 N ALA D 42 2910 2606 2321 -202 1176 -107 N ATOM 3884 CA ALA D 42 -6.935 12.913 53.735 1.00 22.30 C ANISOU 3884 CA ALA D 42 3039 2737 2697 -180 1415 -111 C ATOM 3885 C ALA D 42 -6.190 12.289 54.914 1.00 22.41 C ANISOU 3885 C ALA D 42 2769 2790 2955 -145 1343 -107 C ATOM 3886 O ALA D 42 -5.529 11.267 54.765 1.00 23.60 O ANISOU 3886 O ALA D 42 2859 2887 3220 -94 1464 -113 O ATOM 3887 CB ALA D 42 -6.150 14.081 53.169 1.00 23.33 C ANISOU 3887 CB ALA D 42 3162 2802 2901 -226 1595 -85 C ATOM 3888 N LEU D 43 -6.309 12.877 56.097 1.00 21.73 N ANISOU 3888 N LEU D 43 2530 2783 2944 -172 1141 -93 N ATOM 3889 CA LEU D 43 -5.534 12.396 57.239 1.00 22.18 C ANISOU 3889 CA LEU D 43 2339 2861 3224 -154 1040 -78 C ATOM 3890 C LEU D 43 -6.124 11.111 57.854 1.00 21.54 C ANISOU 3890 C LEU D 43 2269 2827 3087 -99 905 -91 C ATOM 3891 O LEU D 43 -5.430 10.419 58.588 1.00 22.19 O ANISOU 3891 O LEU D 43 2178 2904 3348 -69 848 -72 O ATOM 3892 CB LEU D 43 -5.379 13.497 58.310 1.00 21.87 C ANISOU 3892 CB LEU D 43 2176 2868 3265 -215 865 -62 C ATOM 3893 CG LEU D 43 -4.581 14.789 57.988 1.00 22.97 C ANISOU 3893 CG LEU D 43 2243 2952 3530 -281 965 -42 C ATOM 3894 CD1 LEU D 43 -4.467 15.718 59.214 1.00 22.74 C ANISOU 3894 CD1 LEU D 43 2111 2959 3570 -347 750 -36 C ATOM 3895 CD2 LEU D 43 -3.198 14.516 57.415 1.00 24.93 C ANISOU 3895 CD2 LEU D 43 2326 3104 4042 -270 1181 -12 C ATOM 3896 N SER D 44 -7.378 10.781 57.544 1.00 20.64 N ANISOU 3896 N SER D 44 2349 2745 2745 -90 847 -113 N ATOM 3897 CA SER D 44 -8.029 9.592 58.111 1.00 20.05 C ANISOU 3897 CA SER D 44 2291 2707 2618 -47 724 -121 C ATOM 3898 C SER D 44 -8.181 8.408 57.131 1.00 20.67 C ANISOU 3898 C SER D 44 2509 2722 2623 -4 850 -146 C ATOM 3899 O SER D 44 -8.941 7.463 57.406 1.00 19.84 O ANISOU 3899 O SER D 44 2461 2637 2440 19 749 -155 O ATOM 3900 CB SER D 44 -9.398 9.986 58.633 1.00 18.67 C ANISOU 3900 CB SER D 44 2209 2604 2281 -72 550 -121 C ATOM 3901 OG SER D 44 -10.267 10.274 57.555 1.00 18.66 O ANISOU 3901 OG SER D 44 2400 2580 2110 -90 592 -129 O ATOM 3902 N GLU D 45 -7.477 8.446 55.995 1.00 22.13 N ANISOU 3902 N GLU D 45 2765 2814 2827 1 1080 -158 N ATOM 3903 CA GLU D 45 -7.612 7.374 55.012 1.00 22.99 C ANISOU 3903 CA GLU D 45 3060 2839 2836 36 1217 -191 C ATOM 3904 C GLU D 45 -7.249 6.024 55.659 1.00 22.74 C ANISOU 3904 C GLU D 45 2903 2793 2942 102 1193 -192 C ATOM 3905 O GLU D 45 -6.222 5.898 56.344 1.00 23.32 O ANISOU 3905 O GLU D 45 2738 2860 3261 136 1214 -162 O ATOM 3906 CB GLU D 45 -6.830 7.669 53.701 1.00 25.28 C ANISOU 3906 CB GLU D 45 3480 3008 3116 33 1513 -204 C ATOM 3907 CG GLU D 45 -7.707 8.535 52.736 1.00 25.62 C ANISOU 3907 CG GLU D 45 3800 3039 2894 -31 1501 -211 C ATOM 3908 CD GLU D 45 -7.073 8.909 51.395 1.00 27.97 C ANISOU 3908 CD GLU D 45 4298 3207 3120 -45 1793 -221 C ATOM 3909 OE1 GLU D 45 -6.433 8.046 50.742 1.00 30.01 O ANISOU 3909 OE1 GLU D 45 4649 3350 3403 -2 2029 -249 O ATOM 3910 OE2 GLU D 45 -7.238 10.086 50.969 1.00 28.60 O ANISOU 3910 OE2 GLU D 45 4467 3288 3112 -100 1803 -198 O ATOM 3911 N GLY D 46 -8.144 5.046 55.498 1.00 21.72 N ANISOU 3911 N GLY D 46 2927 2656 2666 115 1117 -218 N ATOM 3912 CA GLY D 46 -7.978 3.722 56.097 1.00 21.32 C ANISOU 3912 CA GLY D 46 2792 2589 2719 175 1079 -217 C ATOM 3913 C GLY D 46 -8.242 3.636 57.592 1.00 19.70 C ANISOU 3913 C GLY D 46 2400 2485 2598 179 845 -177 C ATOM 3914 O GLY D 46 -7.958 2.613 58.196 1.00 19.92 O ANISOU 3914 O GLY D 46 2336 2495 2735 230 807 -162 O ATOM 3915 N ALA D 47 -8.768 4.693 58.205 1.00 18.08 N ANISOU 3915 N ALA D 47 2158 2372 2337 128 697 -158 N ATOM 3916 CA ALA D 47 -8.908 4.712 59.655 1.00 16.95 C ANISOU 3916 CA ALA D 47 1875 2306 2258 127 503 -122 C ATOM 3917 C ALA D 47 -9.900 3.643 60.100 1.00 15.90 C ANISOU 3917 C ALA D 47 1817 2188 2035 144 391 -120 C ATOM 3918 O ALA D 47 -10.879 3.357 59.415 1.00 15.51 O ANISOU 3918 O ALA D 47 1928 2124 1840 126 393 -144 O ATOM 3919 CB ALA D 47 -9.353 6.102 60.167 1.00 16.05 C ANISOU 3919 CB ALA D 47 1750 2265 2080 68 399 -111 C ATOM 3920 N THR D 48 -9.618 3.041 61.240 1.00 15.54 N ANISOU 3920 N THR D 48 1657 2159 2086 174 283 -86 N ATOM 3921 CA THR D 48 -10.610 2.255 61.938 1.00 14.66 C ANISOU 3921 CA THR D 48 1604 2072 1893 178 163 -71 C ATOM 3922 C THR D 48 -11.404 3.222 62.840 1.00 13.51 C ANISOU 3922 C THR D 48 1471 2004 1659 130 40 -53 C ATOM 3923 O THR D 48 -10.968 4.342 63.097 1.00 13.36 O ANISOU 3923 O THR D 48 1398 2013 1662 101 25 -51 O ATOM 3924 CB THR D 48 -9.958 1.164 62.831 1.00 15.22 C ANISOU 3924 CB THR D 48 1574 2113 2094 232 101 -32 C ATOM 3925 OG1 THR D 48 -9.275 1.801 63.909 1.00 15.45 O ANISOU 3925 OG1 THR D 48 1483 2176 2209 219 -14 7 O ATOM 3926 CG2 THR D 48 -8.981 0.280 62.036 1.00 16.48 C ANISOU 3926 CG2 THR D 48 1688 2177 2393 294 248 -44 C ATOM 3927 N PRO D 49 -12.550 2.770 63.361 1.00 12.83 N ANISOU 3927 N PRO D 49 1453 1935 1486 123 -33 -37 N ATOM 3928 CA PRO D 49 -13.252 3.583 64.369 1.00 12.27 C ANISOU 3928 CA PRO D 49 1398 1914 1350 90 -113 -15 C ATOM 3929 C PRO D 49 -12.382 4.052 65.538 1.00 12.69 C ANISOU 3929 C PRO D 49 1387 1984 1449 85 -195 5 C ATOM 3930 O PRO D 49 -12.471 5.200 65.919 1.00 12.33 O ANISOU 3930 O PRO D 49 1357 1964 1363 48 -217 0 O ATOM 3931 CB PRO D 49 -14.367 2.659 64.832 1.00 11.95 C ANISOU 3931 CB PRO D 49 1414 1861 1262 97 -150 9 C ATOM 3932 CG PRO D 49 -14.713 1.912 63.591 1.00 12.01 C ANISOU 3932 CG PRO D 49 1471 1826 1263 101 -99 -13 C ATOM 3933 CD PRO D 49 -13.383 1.653 62.899 1.00 12.71 C ANISOU 3933 CD PRO D 49 1522 1881 1426 132 -24 -42 C ATOM 3934 N GLN D 50 -11.550 3.166 66.087 1.00 13.60 N ANISOU 3934 N GLN D 50 1441 2071 1652 118 -253 33 N ATOM 3935 CA GLN D 50 -10.593 3.553 67.135 1.00 14.54 C ANISOU 3935 CA GLN D 50 1501 2189 1833 104 -376 63 C ATOM 3936 C GLN D 50 -9.654 4.693 66.682 1.00 15.04 C ANISOU 3936 C GLN D 50 1470 2254 1988 72 -354 44 C ATOM 3937 O GLN D 50 -9.388 5.621 67.450 1.00 15.33 O ANISOU 3937 O GLN D 50 1516 2302 2004 24 -452 50 O ATOM 3938 CB GLN D 50 -9.742 2.362 67.612 1.00 15.65 C ANISOU 3938 CB GLN D 50 1565 2281 2098 151 -455 111 C ATOM 3939 CG GLN D 50 -8.775 2.765 68.769 1.00 16.87 C ANISOU 3939 CG GLN D 50 1669 2420 2319 123 -641 157 C ATOM 3940 CD GLN D 50 -7.822 1.654 69.221 1.00 18.29 C ANISOU 3940 CD GLN D 50 1745 2538 2663 172 -750 222 C ATOM 3941 OE1 GLN D 50 -8.242 0.641 69.765 1.00 18.41 O ANISOU 3941 OE1 GLN D 50 1837 2533 2623 203 -797 257 O ATOM 3942 NE2 GLN D 50 -6.533 1.869 69.025 1.00 19.61 N ANISOU 3942 NE2 GLN D 50 1730 2666 3052 177 -794 249 N ATOM 3943 N ASP D 51 -9.150 4.615 65.447 1.00 15.33 N ANISOU 3943 N ASP D 51 1435 2268 2122 95 -218 22 N ATOM 3944 CA ASP D 51 -8.287 5.664 64.906 1.00 15.91 C ANISOU 3944 CA ASP D 51 1418 2331 2295 64 -160 10 C ATOM 3945 C ASP D 51 -9.027 6.990 64.805 1.00 15.03 C ANISOU 3945 C ASP D 51 1402 2262 2047 7 -147 -19 C ATOM 3946 O ASP D 51 -8.495 8.051 65.147 1.00 15.48 O ANISOU 3946 O ASP D 51 1415 2320 2146 -41 -195 -19 O ATOM 3947 CB ASP D 51 -7.776 5.277 63.515 1.00 16.55 C ANISOU 3947 CB ASP D 51 1456 2362 2470 102 35 -10 C ATOM 3948 CG ASP D 51 -6.920 4.035 63.536 1.00 17.86 C ANISOU 3948 CG ASP D 51 1509 2463 2814 168 59 20 C ATOM 3949 OD1 ASP D 51 -6.244 3.790 64.564 1.00 18.79 O ANISOU 3949 OD1 ASP D 51 1509 2569 3061 175 -93 71 O ATOM 3950 OD2 ASP D 51 -6.924 3.282 62.535 1.00 18.24 O ANISOU 3950 OD2 ASP D 51 1600 2458 2870 214 223 -4 O ATOM 3951 N LEU D 52 -10.267 6.922 64.348 1.00 14.00 N ANISOU 3951 N LEU D 52 1396 2154 1768 11 -92 -40 N ATOM 3952 CA LEU D 52 -11.099 8.110 64.178 1.00 13.26 C ANISOU 3952 CA LEU D 52 1387 2086 1564 -28 -73 -58 C ATOM 3953 C LEU D 52 -11.347 8.802 65.514 1.00 13.27 C ANISOU 3953 C LEU D 52 1426 2105 1510 -62 -183 -50 C ATOM 3954 O LEU D 52 -11.227 10.037 65.618 1.00 13.33 O ANISOU 3954 O LEU D 52 1447 2112 1504 -105 -185 -64 O ATOM 3955 CB LEU D 52 -12.408 7.714 63.498 1.00 12.44 C ANISOU 3955 CB LEU D 52 1386 1987 1354 -14 -27 -63 C ATOM 3956 CG LEU D 52 -12.268 7.331 62.023 1.00 12.60 C ANISOU 3956 CG LEU D 52 1442 1972 1373 -2 81 -82 C ATOM 3957 CD1 LEU D 52 -13.529 6.649 61.511 1.00 12.15 C ANISOU 3957 CD1 LEU D 52 1489 1903 1224 2 66 -79 C ATOM 3958 CD2 LEU D 52 -11.980 8.567 61.224 1.00 12.75 C ANISOU 3958 CD2 LEU D 52 1481 1982 1381 -37 156 -95 C ATOM 3959 N ASN D 53 -11.644 8.004 66.537 1.00 13.37 N ANISOU 3959 N ASN D 53 1476 2118 1484 -44 -267 -27 N ATOM 3960 CA ASN D 53 -11.803 8.513 67.889 1.00 13.79 C ANISOU 3960 CA ASN D 53 1613 2165 1458 -77 -365 -20 C ATOM 3961 C ASN D 53 -10.518 9.066 68.472 1.00 14.89 C ANISOU 3961 C ASN D 53 1698 2282 1675 -122 -486 -16 C ATOM 3962 O ASN D 53 -10.549 9.988 69.258 1.00 15.17 O ANISOU 3962 O ASN D 53 1824 2302 1638 -172 -551 -29 O ATOM 3963 CB ASN D 53 -12.344 7.444 68.836 1.00 13.88 C ANISOU 3963 CB ASN D 53 1704 2167 1402 -50 -417 11 C ATOM 3964 CG ASN D 53 -13.777 7.075 68.543 1.00 13.16 C ANISOU 3964 CG ASN D 53 1674 2082 1243 -24 -315 15 C ATOM 3965 OD1 ASN D 53 -14.600 7.906 68.091 1.00 12.70 O ANISOU 3965 OD1 ASN D 53 1641 2030 1153 -34 -233 0 O ATOM 3966 ND2 ASN D 53 -14.100 5.826 68.812 1.00 13.14 N ANISOU 3966 ND2 ASN D 53 1684 2067 1238 8 -326 45 N ATOM 3967 N THR D 54 -9.387 8.484 68.113 1.00 15.76 N ANISOU 3967 N THR D 54 1660 2377 1949 -105 -520 5 N ATOM 3968 CA THR D 54 -8.116 9.063 68.543 1.00 17.16 C ANISOU 3968 CA THR D 54 1741 2521 2258 -156 -647 21 C ATOM 3969 C THR D 54 -8.001 10.485 67.988 1.00 17.21 C ANISOU 3969 C THR D 54 1737 2527 2274 -210 -576 -14 C ATOM 3970 O THR D 54 -7.564 11.394 68.685 1.00 18.01 O ANISOU 3970 O THR D 54 1865 2600 2375 -279 -693 -19 O ATOM 3971 CB THR D 54 -6.926 8.239 68.068 1.00 18.11 C ANISOU 3971 CB THR D 54 1659 2607 2612 -119 -653 60 C ATOM 3972 OG1 THR D 54 -7.062 6.903 68.558 1.00 18.23 O ANISOU 3972 OG1 THR D 54 1690 2614 2622 -64 -717 97 O ATOM 3973 CG2 THR D 54 -5.611 8.825 68.573 1.00 19.69 C ANISOU 3973 CG2 THR D 54 1723 2758 2998 -179 -813 94 C ATOM 3974 N MET D 55 -8.419 10.670 66.735 1.00 16.57 N ANISOU 3974 N MET D 55 1641 2466 2189 -183 -393 -37 N ATOM 3975 CA MET D 55 -8.354 11.978 66.100 1.00 16.58 C ANISOU 3975 CA MET D 55 1644 2461 2195 -228 -311 -63 C ATOM 3976 C MET D 55 -9.296 12.991 66.762 1.00 16.07 C ANISOU 3976 C MET D 55 1738 2400 1964 -265 -341 -89 C ATOM 3977 O MET D 55 -8.895 14.103 67.044 1.00 16.52 O ANISOU 3977 O MET D 55 1808 2429 2039 -327 -383 -104 O ATOM 3978 CB MET D 55 -8.660 11.872 64.609 1.00 16.11 C ANISOU 3978 CB MET D 55 1579 2408 2135 -192 -121 -74 C ATOM 3979 CG MET D 55 -7.642 11.119 63.854 1.00 17.06 C ANISOU 3979 CG MET D 55 1563 2494 2422 -160 -34 -57 C ATOM 3980 SD MET D 55 -8.074 11.096 62.112 1.00 17.10 S ANISOU 3980 SD MET D 55 1651 2484 2361 -132 192 -78 S ATOM 3981 CE MET D 55 -7.232 12.555 61.497 1.00 17.67 C ANISOU 3981 CE MET D 55 1667 2514 2530 -194 293 -77 C ATOM 3982 N LEU D 56 -10.545 12.601 66.986 1.00 15.29 N ANISOU 3982 N LEU D 56 1757 2325 1726 -226 -307 -93 N ATOM 3983 CA LEU D 56 -11.526 13.480 67.613 1.00 15.17 C ANISOU 3983 CA LEU D 56 1888 2296 1579 -244 -293 -112 C ATOM 3984 C LEU D 56 -11.116 13.859 69.032 1.00 16.30 C ANISOU 3984 C LEU D 56 2130 2399 1664 -297 -430 -122 C ATOM 3985 O LEU D 56 -11.269 14.995 69.434 1.00 16.65 O ANISOU 3985 O LEU D 56 2273 2405 1647 -342 -429 -150 O ATOM 3986 CB LEU D 56 -12.906 12.814 67.652 1.00 14.36 C ANISOU 3986 CB LEU D 56 1859 2210 1388 -189 -224 -98 C ATOM 3987 CG LEU D 56 -13.549 12.433 66.316 1.00 13.59 C ANISOU 3987 CG LEU D 56 1710 2135 1318 -149 -126 -85 C ATOM 3988 CD1 LEU D 56 -14.929 11.858 66.532 1.00 13.09 C ANISOU 3988 CD1 LEU D 56 1701 2070 1200 -110 -89 -62 C ATOM 3989 CD2 LEU D 56 -13.581 13.623 65.402 1.00 13.56 C ANISOU 3989 CD2 LEU D 56 1702 2119 1330 -172 -58 -96 C ATOM 3990 N ASN D 57 -10.588 12.891 69.770 1.00 17.10 N ANISOU 3990 N ASN D 57 2222 2496 1776 -294 -556 -96 N ATOM 3991 CA ASN D 57 -10.160 13.095 71.150 1.00 18.63 C ANISOU 3991 CA ASN D 57 2546 2638 1891 -352 -726 -97 C ATOM 3992 C ASN D 57 -9.113 14.213 71.299 1.00 19.68 C ANISOU 3992 C ASN D 57 2649 2727 2101 -441 -842 -115 C ATOM 3993 O ASN D 57 -9.032 14.842 72.339 1.00 20.68 O ANISOU 3993 O ASN D 57 2948 2792 2114 -507 -958 -136 O ATOM 3994 CB ASN D 57 -9.618 11.771 71.705 1.00 19.37 C ANISOU 3994 CB ASN D 57 2602 2731 2023 -330 -865 -48 C ATOM 3995 CG ASN D 57 -9.302 11.833 73.187 1.00 21.03 C ANISOU 3995 CG ASN D 57 3000 2878 2112 -390 -1065 -38 C ATOM 3996 OD1 ASN D 57 -8.137 11.743 73.597 1.00 22.53 O ANISOU 3996 OD1 ASN D 57 3123 3031 2406 -441 -1278 -6 O ATOM 3997 ND2 ASN D 57 -10.333 11.983 73.998 1.00 21.19 N ANISOU 3997 ND2 ASN D 57 3263 2867 1918 -388 -1000 -57 N ATOM 3998 N THR D 58 -8.334 14.466 70.253 1.00 19.71 N ANISOU 3998 N THR D 58 2450 2746 2292 -448 -801 -107 N ATOM 3999 CA THR D 58 -7.344 15.550 70.283 1.00 20.96 C ANISOU 3999 CA THR D 58 2548 2853 2561 -538 -893 -118 C ATOM 4000 C THR D 58 -7.932 16.983 70.190 1.00 20.81 C ANISOU 4000 C THR D 58 2662 2805 2439 -580 -799 -169 C ATOM 4001 O THR D 58 -7.227 17.945 70.451 1.00 21.84 O ANISOU 4001 O THR D 58 2795 2876 2626 -668 -895 -184 O ATOM 4002 CB THR D 58 -6.334 15.410 69.140 1.00 21.27 C ANISOU 4002 CB THR D 58 2326 2900 2854 -530 -829 -87 C ATOM 4003 OG1 THR D 58 -6.986 15.713 67.896 1.00 19.98 O ANISOU 4003 OG1 THR D 58 2150 2774 2666 -482 -595 -106 O ATOM 4004 CG2 THR D 58 -5.715 13.996 69.094 1.00 21.57 C ANISOU 4004 CG2 THR D 58 2209 2951 3034 -474 -884 -33 C ATOM 4005 N VAL D 59 -9.198 17.137 69.805 1.00 19.65 N ANISOU 4005 N VAL D 59 2613 2686 2166 -519 -622 -189 N ATOM 4006 CA VAL D 59 -9.752 18.472 69.600 1.00 19.63 C ANISOU 4006 CA VAL D 59 2709 2645 2101 -544 -519 -226 C ATOM 4007 C VAL D 59 -10.010 19.192 70.909 1.00 20.80 C ANISOU 4007 C VAL D 59 3093 2714 2095 -601 -599 -268 C ATOM 4008 O VAL D 59 -10.796 18.736 71.751 1.00 20.78 O ANISOU 4008 O VAL D 59 3256 2698 1941 -567 -584 -274 O ATOM 4009 CB VAL D 59 -11.068 18.458 68.796 1.00 18.30 C ANISOU 4009 CB VAL D 59 2563 2513 1877 -460 -324 -221 C ATOM 4010 CG1 VAL D 59 -11.662 19.907 68.710 1.00 18.31 C ANISOU 4010 CG1 VAL D 59 2672 2454 1828 -481 -229 -250 C ATOM 4011 CG2 VAL D 59 -10.828 17.858 67.423 1.00 17.37 C ANISOU 4011 CG2 VAL D 59 2271 2453 1875 -418 -245 -188 C ATOM 4012 N GLY D 60 -9.336 20.330 71.053 1.00 21.99 N ANISOU 4012 N GLY D 60 3272 2797 2283 -691 -669 -297 N ATOM 4013 CA GLY D 60 -9.454 21.170 72.218 1.00 23.37 C ANISOU 4013 CA GLY D 60 3700 2871 2306 -762 -748 -347 C ATOM 4014 C GLY D 60 -10.342 22.350 71.908 1.00 23.16 C ANISOU 4014 C GLY D 60 3782 2796 2219 -744 -559 -385 C ATOM 4015 O GLY D 60 -10.201 23.000 70.847 1.00 22.75 O ANISOU 4015 O GLY D 60 3592 2758 2291 -743 -469 -375 O ATOM 4016 N GLY D 61 -11.241 22.643 72.850 1.00 23.64 N ANISOU 4016 N GLY D 61 4102 2784 2094 -729 -488 -423 N ATOM 4017 CA GLY D 61 -12.150 23.768 72.737 1.00 23.55 C ANISOU 4017 CA GLY D 61 4214 2698 2034 -702 -299 -457 C ATOM 4018 C GLY D 61 -13.248 23.471 71.733 1.00 21.90 C ANISOU 4018 C GLY D 61 3863 2558 1900 -582 -96 -410 C ATOM 4019 O GLY D 61 -13.504 22.311 71.399 1.00 20.88 O ANISOU 4019 O GLY D 61 3610 2518 1802 -521 -89 -365 O ATOM 4020 N HIS D 62 -13.889 24.539 71.256 1.00 21.75 N ANISOU 4020 N HIS D 62 3867 2482 1914 -556 52 -417 N ATOM 4021 CA HIS D 62 -15.000 24.464 70.320 1.00 20.49 C ANISOU 4021 CA HIS D 62 3591 2356 1838 -452 217 -363 C ATOM 4022 C HIS D 62 -16.091 23.550 70.856 1.00 20.24 C ANISOU 4022 C HIS D 62 3603 2333 1753 -369 314 -339 C ATOM 4023 O HIS D 62 -16.612 22.696 70.149 1.00 18.94 O ANISOU 4023 O HIS D 62 3283 2247 1663 -304 341 -282 O ATOM 4024 CB HIS D 62 -14.497 24.023 68.960 1.00 19.40 C ANISOU 4024 CB HIS D 62 3220 2323 1826 -446 168 -314 C ATOM 4025 CG HIS D 62 -13.396 24.884 68.429 1.00 19.88 C ANISOU 4025 CG HIS D 62 3228 2364 1958 -529 104 -329 C ATOM 4026 ND1 HIS D 62 -13.623 26.137 67.898 1.00 20.14 N ANISOU 4026 ND1 HIS D 62 3290 2327 2033 -537 191 -328 N ATOM 4027 CD2 HIS D 62 -12.059 24.679 68.358 1.00 20.28 C ANISOU 4027 CD2 HIS D 62 3188 2444 2071 -609 -30 -336 C ATOM 4028 CE1 HIS D 62 -12.475 26.662 67.511 1.00 20.69 C ANISOU 4028 CE1 HIS D 62 3297 2386 2175 -624 120 -337 C ATOM 4029 NE2 HIS D 62 -11.509 25.798 67.779 1.00 20.88 N ANISOU 4029 NE2 HIS D 62 3237 2468 2227 -668 -11 -341 N ATOM 4030 N GLN D 63 -16.438 23.763 72.118 1.00 21.57 N ANISOU 4030 N GLN D 63 4004 2403 1788 -377 374 -382 N ATOM 4031 CA GLN D 63 -17.352 22.884 72.815 1.00 21.96 C ANISOU 4031 CA GLN D 63 4127 2440 1777 -311 480 -360 C ATOM 4032 C GLN D 63 -18.722 22.894 72.133 1.00 21.09 C ANISOU 4032 C GLN D 63 3881 2321 1809 -204 671 -296 C ATOM 4033 O GLN D 63 -19.301 21.839 71.943 1.00 20.26 O ANISOU 4033 O GLN D 63 3664 2274 1756 -150 694 -243 O ATOM 4034 CB GLN D 63 -17.440 23.231 74.318 1.00 24.23 C ANISOU 4034 CB GLN D 63 4745 2593 1868 -347 537 -423 C ATOM 4035 CG GLN D 63 -17.894 22.067 75.244 1.00 25.12 C ANISOU 4035 CG GLN D 63 4975 2701 1865 -316 581 -405 C ATOM 4036 CD GLN D 63 -17.675 22.374 76.731 1.00 27.75 C ANISOU 4036 CD GLN D 63 5693 2896 1952 -380 585 -472 C ATOM 4037 OE1 GLN D 63 -16.542 22.667 77.158 1.00 29.32 O ANISOU 4037 OE1 GLN D 63 6020 3078 2042 -488 362 -520 O ATOM 4038 NE2 GLN D 63 -18.763 22.346 77.531 1.00 29.08 N ANISOU 4038 NE2 GLN D 63 6062 2949 2037 -318 842 -472 N ATOM 4039 N ALA D 64 -19.209 24.061 71.722 1.00 21.23 N ANISOU 4039 N ALA D 64 3895 2259 1910 -177 785 -293 N ATOM 4040 CA ALA D 64 -20.495 24.157 71.041 1.00 21.06 C ANISOU 4040 CA ALA D 64 3726 2212 2062 -78 933 -216 C ATOM 4041 C ALA D 64 -20.552 23.283 69.783 1.00 19.67 C ANISOU 4041 C ALA D 64 3302 2167 2003 -57 815 -144 C ATOM 4042 O ALA D 64 -21.505 22.536 69.596 1.00 19.23 O ANISOU 4042 O ALA D 64 3137 2123 2044 6 870 -79 O ATOM 4043 CB ALA D 64 -20.821 25.604 70.686 1.00 21.71 C ANISOU 4043 CB ALA D 64 3832 2186 2228 -59 1033 -217 C ATOM 4044 N ALA D 65 -19.522 23.384 68.946 1.00 19.09 N ANISOU 4044 N ALA D 65 3156 2175 1921 -116 662 -156 N ATOM 4045 CA ALA D 65 -19.389 22.574 67.732 1.00 18.23 C ANISOU 4045 CA ALA D 65 2867 2175 1882 -109 555 -102 C ATOM 4046 C ALA D 65 -19.164 21.069 67.990 1.00 17.87 C ANISOU 4046 C ALA D 65 2778 2218 1791 -110 480 -100 C ATOM 4047 O ALA D 65 -19.743 20.229 67.307 1.00 17.05 O ANISOU 4047 O ALA D 65 2558 2162 1758 -72 459 -44 O ATOM 4048 CB ALA D 65 -18.264 23.126 66.868 1.00 17.93 C ANISOU 4048 CB ALA D 65 2796 2176 1840 -173 460 -121 C ATOM 4049 N MET D 66 -18.317 20.730 68.961 1.00 18.63 N ANISOU 4049 N MET D 66 2977 2326 1772 -159 421 -155 N ATOM 4050 CA MET D 66 -18.094 19.316 69.321 1.00 18.63 C ANISOU 4050 CA MET D 66 2952 2395 1730 -156 350 -147 C ATOM 4051 C MET D 66 -19.354 18.625 69.843 1.00 19.17 C ANISOU 4051 C MET D 66 3034 2430 1816 -90 465 -105 C ATOM 4052 O MET D 66 -19.538 17.438 69.621 1.00 18.50 O ANISOU 4052 O MET D 66 2865 2404 1760 -70 425 -71 O ATOM 4053 CB MET D 66 -16.952 19.176 70.323 1.00 19.26 C ANISOU 4053 CB MET D 66 3151 2473 1691 -224 238 -201 C ATOM 4054 CG MET D 66 -15.605 19.517 69.712 1.00 19.22 C ANISOU 4054 CG MET D 66 3064 2510 1727 -290 106 -222 C ATOM 4055 SD MET D 66 -15.267 18.528 68.238 1.00 18.33 S ANISOU 4055 SD MET D 66 2730 2504 1730 -262 64 -177 S ATOM 4056 CE MET D 66 -14.961 16.953 69.090 1.00 18.19 C ANISOU 4056 CE MET D 66 2720 2528 1664 -252 -29 -168 C ATOM 4057 N GLN D 67 -20.229 19.377 70.494 1.00 20.58 N ANISOU 4057 N GLN D 67 3316 2504 2000 -57 626 -105 N ATOM 4058 CA GLN D 67 -21.519 18.843 70.930 1.00 21.85 C ANISOU 4058 CA GLN D 67 3462 2609 2229 9 779 -53 C ATOM 4059 C GLN D 67 -22.429 18.595 69.712 1.00 21.22 C ANISOU 4059 C GLN D 67 3159 2554 2349 58 775 29 C ATOM 4060 O GLN D 67 -23.185 17.623 69.687 1.00 20.66 O ANISOU 4060 O GLN D 67 2997 2490 2360 91 800 85 O ATOM 4061 CB GLN D 67 -22.169 19.773 71.978 1.00 23.91 C ANISOU 4061 CB GLN D 67 3905 2722 2454 36 991 -76 C ATOM 4062 CG GLN D 67 -23.607 19.441 72.326 1.00 25.53 C ANISOU 4062 CG GLN D 67 4064 2841 2795 116 1206 -8 C ATOM 4063 CD GLN D 67 -23.796 18.131 73.087 1.00 26.63 C ANISOU 4063 CD GLN D 67 4255 2995 2866 119 1236 9 C ATOM 4064 OE1 GLN D 67 -22.828 17.507 73.594 1.00 27.35 O ANISOU 4064 OE1 GLN D 67 4470 3146 2774 63 1102 -35 O ATOM 4065 NE2 GLN D 67 -25.072 17.721 73.225 1.00 27.85 N ANISOU 4065 NE2 GLN D 67 4314 3078 3188 185 1419 85 N ATOM 4066 N MET D 68 -22.324 19.459 68.699 1.00 21.27 N ANISOU 4066 N MET D 68 3089 2564 2426 53 724 41 N ATOM 4067 CA MET D 68 -23.088 19.286 67.465 1.00 21.35 C ANISOU 4067 CA MET D 68 2923 2589 2600 84 668 123 C ATOM 4068 C MET D 68 -22.607 18.004 66.751 1.00 19.64 C ANISOU 4068 C MET D 68 2630 2482 2348 54 511 131 C ATOM 4069 O MET D 68 -23.418 17.202 66.294 1.00 19.29 O ANISOU 4069 O MET D 68 2478 2441 2409 77 477 194 O ATOM 4070 CB MET D 68 -22.994 20.534 66.561 1.00 22.61 C ANISOU 4070 CB MET D 68 3061 2716 2811 80 640 137 C ATOM 4071 CG MET D 68 -24.075 20.626 65.432 1.00 23.86 C ANISOU 4071 CG MET D 68 3068 2839 3158 120 589 243 C ATOM 4072 SD MET D 68 -24.028 22.178 64.430 1.00 26.38 S ANISOU 4072 SD MET D 68 3392 3097 3533 119 558 275 S ATOM 4073 CE MET D 68 -23.511 23.323 65.697 1.00 26.20 C ANISOU 4073 CE MET D 68 3531 3000 3423 116 731 185 C ATOM 4074 N LEU D 69 -21.295 17.808 66.701 1.00 18.44 N ANISOU 4074 N LEU D 69 2535 2404 2064 2 421 67 N ATOM 4075 CA LEU D 69 -20.698 16.593 66.128 1.00 17.47 C ANISOU 4075 CA LEU D 69 2361 2370 1907 -19 305 64 C ATOM 4076 C LEU D 69 -21.148 15.346 66.877 1.00 17.18 C ANISOU 4076 C LEU D 69 2317 2341 1869 1 323 80 C ATOM 4077 O LEU D 69 -21.515 14.354 66.263 1.00 16.37 O ANISOU 4077 O LEU D 69 2135 2265 1817 8 263 116 O ATOM 4078 CB LEU D 69 -19.169 16.656 66.189 1.00 17.09 C ANISOU 4078 CB LEU D 69 2359 2375 1758 -70 237 0 C ATOM 4079 CG LEU D 69 -18.374 15.498 65.574 1.00 16.57 C ANISOU 4079 CG LEU D 69 2238 2381 1674 -86 146 -8 C ATOM 4080 CD1 LEU D 69 -18.691 15.361 64.082 1.00 16.19 C ANISOU 4080 CD1 LEU D 69 2137 2343 1670 -82 114 27 C ATOM 4081 CD2 LEU D 69 -16.887 15.768 65.774 1.00 16.59 C ANISOU 4081 CD2 LEU D 69 2257 2410 1636 -132 100 -59 C ATOM 4082 N LYS D 70 -21.079 15.413 68.201 1.00 17.69 N ANISOU 4082 N LYS D 70 2489 2370 1861 4 402 51 N ATOM 4083 CA LYS D 70 -21.496 14.311 69.042 1.00 18.23 C ANISOU 4083 CA LYS D 70 2585 2429 1911 22 441 71 C ATOM 4084 C LYS D 70 -22.958 13.962 68.767 1.00 18.36 C ANISOU 4084 C LYS D 70 2489 2394 2091 67 524 149 C ATOM 4085 O LYS D 70 -23.266 12.780 68.627 1.00 17.91 O ANISOU 4085 O LYS D 70 2368 2360 2075 70 484 183 O ATOM 4086 CB LYS D 70 -21.262 14.611 70.544 1.00 19.40 C ANISOU 4086 CB LYS D 70 2924 2519 1926 13 528 31 C ATOM 4087 CG LYS D 70 -21.829 13.567 71.489 1.00 20.27 C ANISOU 4087 CG LYS D 70 3097 2595 2007 34 607 62 C ATOM 4088 CD LYS D 70 -21.652 13.931 73.000 1.00 21.96 C ANISOU 4088 CD LYS D 70 3567 2726 2050 19 703 23 C ATOM 4089 CE LYS D 70 -20.197 13.702 73.458 1.00 22.13 C ANISOU 4089 CE LYS D 70 3704 2797 1905 -41 513 -28 C ATOM 4090 NZ LYS D 70 -20.047 13.640 74.946 1.00 23.70 N ANISOU 4090 NZ LYS D 70 4181 2912 1910 -66 553 -50 N ATOM 4091 N GLU D 71 -23.847 14.960 68.666 1.00 18.96 N ANISOU 4091 N GLU D 71 2528 2390 2283 99 631 185 N ATOM 4092 CA GLU D 71 -25.258 14.633 68.424 1.00 19.80 C ANISOU 4092 CA GLU D 71 2492 2431 2600 141 698 277 C ATOM 4093 C GLU D 71 -25.491 14.048 67.011 1.00 18.54 C ANISOU 4093 C GLU D 71 2183 2319 2541 121 514 326 C ATOM 4094 O GLU D 71 -26.300 13.156 66.846 1.00 18.56 O ANISOU 4094 O GLU D 71 2080 2298 2671 126 492 389 O ATOM 4095 CB GLU D 71 -26.232 15.793 68.773 1.00 21.82 C ANISOU 4095 CB GLU D 71 2726 2563 3001 193 880 317 C ATOM 4096 CG GLU D 71 -26.168 17.004 67.887 1.00 22.43 C ANISOU 4096 CG GLU D 71 2762 2625 3133 196 822 324 C ATOM 4097 CD GLU D 71 -27.337 17.976 68.098 1.00 24.70 C ANISOU 4097 CD GLU D 71 2977 2772 3634 263 996 392 C ATOM 4098 OE1 GLU D 71 -27.826 18.523 67.074 1.00 25.96 O ANISOU 4098 OE1 GLU D 71 3004 2903 3953 277 903 460 O ATOM 4099 OE2 GLU D 71 -27.765 18.201 69.266 1.00 26.21 O ANISOU 4099 OE2 GLU D 71 3254 2867 3836 302 1228 382 O ATOM 4100 N THR D 72 -24.749 14.519 66.016 1.00 17.35 N ANISOU 4100 N THR D 72 2048 2222 2321 91 385 297 N ATOM 4101 CA THR D 72 -24.813 13.953 64.670 1.00 16.68 C ANISOU 4101 CA THR D 72 1895 2172 2269 61 211 329 C ATOM 4102 C THR D 72 -24.376 12.481 64.680 1.00 15.87 C ANISOU 4102 C THR D 72 1808 2129 2093 37 142 304 C ATOM 4103 O THR D 72 -25.059 11.616 64.140 1.00 15.67 O ANISOU 4103 O THR D 72 1710 2085 2158 25 56 354 O ATOM 4104 CB THR D 72 -23.935 14.739 63.680 1.00 16.19 C ANISOU 4104 CB THR D 72 1895 2147 2108 32 127 293 C ATOM 4105 OG1 THR D 72 -24.420 16.095 63.564 1.00 16.67 O ANISOU 4105 OG1 THR D 72 1939 2139 2252 55 178 328 O ATOM 4106 CG2 THR D 72 -23.935 14.032 62.296 1.00 15.92 C ANISOU 4106 CG2 THR D 72 1854 2133 2060 -4 -39 318 C ATOM 4107 N ILE D 73 -23.252 12.197 65.332 1.00 15.26 N ANISOU 4107 N ILE D 73 1822 2109 1865 27 169 231 N ATOM 4108 CA ILE D 73 -22.814 10.813 65.470 1.00 14.91 C ANISOU 4108 CA ILE D 73 1790 2108 1766 15 117 213 C ATOM 4109 C ILE D 73 -23.881 9.989 66.177 1.00 15.44 C ANISOU 4109 C ILE D 73 1806 2125 1935 34 179 269 C ATOM 4110 O ILE D 73 -24.207 8.903 65.691 1.00 15.31 O ANISOU 4110 O ILE D 73 1741 2107 1967 19 100 296 O ATOM 4111 CB ILE D 73 -21.468 10.695 66.190 1.00 14.61 C ANISOU 4111 CB ILE D 73 1841 2122 1587 7 124 144 C ATOM 4112 CG1 ILE D 73 -20.353 11.316 65.314 1.00 14.20 C ANISOU 4112 CG1 ILE D 73 1806 2112 1475 -18 65 97 C ATOM 4113 CG2 ILE D 73 -21.134 9.228 66.499 1.00 14.33 C ANISOU 4113 CG2 ILE D 73 1811 2111 1521 7 82 140 C ATOM 4114 CD1 ILE D 73 -19.077 11.596 66.074 1.00 14.11 C ANISOU 4114 CD1 ILE D 73 1852 2130 1378 -33 64 43 C ATOM 4115 N ASN D 74 -24.436 10.502 67.287 1.00 16.04 N ANISOU 4115 N ASN D 74 1905 2144 2045 64 331 287 N ATOM 4116 CA ASN D 74 -25.498 9.803 68.011 1.00 16.99 C ANISOU 4116 CA ASN D 74 1977 2196 2282 84 438 350 C ATOM 4117 C ASN D 74 -26.730 9.515 67.155 1.00 17.62 C ANISOU 4117 C ASN D 74 1883 2220 2589 81 382 438 C ATOM 4118 O ASN D 74 -27.277 8.411 67.207 1.00 17.76 O ANISOU 4118 O ASN D 74 1838 2213 2696 68 363 483 O ATOM 4119 CB ASN D 74 -25.935 10.586 69.248 1.00 18.11 C ANISOU 4119 CB ASN D 74 2195 2259 2424 121 652 356 C ATOM 4120 CG ASN D 74 -24.945 10.491 70.397 1.00 18.19 C ANISOU 4120 CG ASN D 74 2408 2292 2211 112 697 288 C ATOM 4121 OD1 ASN D 74 -25.074 11.222 71.396 1.00 19.36 O ANISOU 4121 OD1 ASN D 74 2688 2372 2295 129 856 271 O ATOM 4122 ND2 ASN D 74 -23.964 9.614 70.275 1.00 17.22 N ANISOU 4122 ND2 ASN D 74 2322 2248 1970 83 555 252 N ATOM 4123 N GLU D 75 -27.141 10.510 66.364 1.00 17.94 N ANISOU 4123 N GLU D 75 1851 2233 2730 86 336 469 N ATOM 4124 CA GLU D 75 -28.284 10.387 65.471 1.00 18.87 C ANISOU 4124 CA GLU D 75 1805 2285 3078 75 231 565 C ATOM 4125 C GLU D 75 -28.069 9.367 64.357 1.00 18.36 C ANISOU 4125 C GLU D 75 1741 2261 2973 16 8 561 C ATOM 4126 O GLU D 75 -28.985 8.615 64.049 1.00 19.00 O ANISOU 4126 O GLU D 75 1709 2282 3225 -8 -72 634 O ATOM 4127 CB GLU D 75 -28.656 11.752 64.854 1.00 19.54 C ANISOU 4127 CB GLU D 75 1836 2325 3262 94 207 603 C ATOM 4128 CG GLU D 75 -29.231 12.717 65.879 1.00 20.66 C ANISOU 4128 CG GLU D 75 1949 2381 3518 158 445 629 C ATOM 4129 CD GLU D 75 -29.562 14.100 65.318 1.00 21.54 C ANISOU 4129 CD GLU D 75 2011 2436 3737 186 433 668 C ATOM 4130 OE1 GLU D 75 -29.074 14.463 64.196 1.00 21.18 O ANISOU 4130 OE1 GLU D 75 2002 2438 3608 151 244 655 O ATOM 4131 OE2 GLU D 75 -30.313 14.826 66.020 1.00 22.73 O ANISOU 4131 OE2 GLU D 75 2099 2481 4055 246 631 714 O ATOM 4132 N GLU D 76 -26.885 9.347 63.743 1.00 17.18 N ANISOU 4132 N GLU D 76 1721 2194 2612 -7 -82 479 N ATOM 4133 CA GLU D 76 -26.653 8.410 62.647 1.00 17.09 C ANISOU 4133 CA GLU D 76 1751 2198 2541 -60 -264 466 C ATOM 4134 C GLU D 76 -26.521 6.976 63.166 1.00 16.61 C ANISOU 4134 C GLU D 76 1702 2150 2458 -70 -248 449 C ATOM 4135 O GLU D 76 -26.904 6.041 62.486 1.00 16.92 O ANISOU 4135 O GLU D 76 1732 2155 2541 -114 -380 471 O ATOM 4136 CB GLU D 76 -25.425 8.789 61.813 1.00 16.50 C ANISOU 4136 CB GLU D 76 1815 2188 2265 -77 -319 389 C ATOM 4137 CG GLU D 76 -25.533 10.139 61.140 1.00 17.08 C ANISOU 4137 CG GLU D 76 1899 2241 2348 -76 -353 412 C ATOM 4138 CD GLU D 76 -26.668 10.258 60.136 1.00 18.35 C ANISOU 4138 CD GLU D 76 2003 2318 2649 -110 -527 505 C ATOM 4139 OE1 GLU D 76 -26.958 9.292 59.413 1.00 19.12 O ANISOU 4139 OE1 GLU D 76 2132 2386 2745 -160 -678 521 O ATOM 4140 OE2 GLU D 76 -27.254 11.353 60.039 1.00 19.25 O ANISOU 4140 OE2 GLU D 76 2051 2384 2877 -89 -527 565 O ATOM 4141 N ALA D 77 -25.960 6.820 64.359 1.00 15.89 N ANISOU 4141 N ALA D 77 1652 2095 2288 -35 -101 410 N ATOM 4142 CA ALA D 77 -25.886 5.514 65.010 1.00 15.78 C ANISOU 4142 CA ALA D 77 1654 2079 2260 -37 -71 407 C ATOM 4143 C ALA D 77 -27.301 5.025 65.347 1.00 16.80 C ANISOU 4143 C ALA D 77 1653 2118 2611 -45 -36 502 C ATOM 4144 O ALA D 77 -27.629 3.888 65.054 1.00 17.16 O ANISOU 4144 O ALA D 77 1672 2132 2714 -80 -119 525 O ATOM 4145 CB ALA D 77 -25.018 5.573 66.269 1.00 15.18 C ANISOU 4145 CB ALA D 77 1672 2047 2049 -1 57 359 C ATOM 4146 N ALA D 78 -28.123 5.888 65.941 1.00 17.37 N ANISOU 4146 N ALA D 78 1641 2134 2823 -13 95 559 N ATOM 4147 CA ALA D 78 -29.523 5.566 66.203 1.00 18.80 C ANISOU 4147 CA ALA D 78 1659 2209 3274 -17 152 665 C ATOM 4148 C ALA D 78 -30.237 5.229 64.890 1.00 19.51 C ANISOU 4148 C ALA D 78 1633 2252 3526 -76 -81 724 C ATOM 4149 O ALA D 78 -30.972 4.229 64.818 1.00 20.19 O ANISOU 4149 O ALA D 78 1626 2274 3772 -117 -139 784 O ATOM 4150 CB ALA D 78 -30.255 6.718 66.936 1.00 19.60 C ANISOU 4150 CB ALA D 78 1685 2238 3521 37 357 718 C ATOM 4151 N GLU D 79 -30.016 6.042 63.855 1.00 19.31 N ANISOU 4151 N GLU D 79 1631 2249 3455 -90 -228 710 N ATOM 4152 CA GLU D 79 -30.539 5.707 62.528 1.00 20.21 C ANISOU 4152 CA GLU D 79 1705 2315 3658 -160 -492 756 C ATOM 4153 C GLU D 79 -30.105 4.326 62.066 1.00 19.64 C ANISOU 4153 C GLU D 79 1738 2258 3464 -218 -619 707 C ATOM 4154 O GLU D 79 -30.898 3.550 61.591 1.00 20.53 O ANISOU 4154 O GLU D 79 1781 2292 3728 -280 -771 767 O ATOM 4155 CB GLU D 79 -30.104 6.694 61.460 1.00 20.27 C ANISOU 4155 CB GLU D 79 1802 2350 3550 -170 -627 732 C ATOM 4156 CG GLU D 79 -31.205 7.585 61.013 1.00 22.03 C ANISOU 4156 CG GLU D 79 1871 2480 4020 -171 -719 845 C ATOM 4157 CD GLU D 79 -32.373 6.820 60.426 1.00 24.00 C ANISOU 4157 CD GLU D 79 1981 2619 4516 -241 -934 951 C ATOM 4158 OE1 GLU D 79 -33.471 6.826 61.039 1.00 25.47 O ANISOU 4158 OE1 GLU D 79 1940 2715 5020 -221 -857 1057 O ATOM 4159 OE2 GLU D 79 -32.177 6.202 59.354 1.00 24.63 O ANISOU 4159 OE2 GLU D 79 2189 2691 4477 -320 -1175 929 O ATOM 4160 N TRP D 80 -28.830 4.036 62.200 1.00 18.15 N ANISOU 4160 N TRP D 80 1716 2160 3019 -199 -559 600 N ATOM 4161 CA TRP D 80 -28.336 2.725 61.813 1.00 17.86 C ANISOU 4161 CA TRP D 80 1788 2128 2871 -239 -645 548 C ATOM 4162 C TRP D 80 -29.079 1.625 62.563 1.00 18.59 C ANISOU 4162 C TRP D 80 1780 2158 3123 -254 -599 604 C ATOM 4163 O TRP D 80 -29.501 0.647 61.954 1.00 19.19 O ANISOU 4163 O TRP D 80 1862 2169 3258 -320 -750 622 O ATOM 4164 CB TRP D 80 -26.849 2.638 62.059 1.00 16.42 C ANISOU 4164 CB TRP D 80 1754 2039 2445 -198 -547 442 C ATOM 4165 CG TRP D 80 -26.278 1.320 61.774 1.00 16.29 C ANISOU 4165 CG TRP D 80 1840 2015 2332 -220 -594 390 C ATOM 4166 CD1 TRP D 80 -26.133 0.299 62.646 1.00 16.13 C ANISOU 4166 CD1 TRP D 80 1812 1991 2324 -202 -514 388 C ATOM 4167 CD2 TRP D 80 -25.748 0.876 60.530 1.00 16.40 C ANISOU 4167 CD2 TRP D 80 2005 2010 2216 -261 -717 332 C ATOM 4168 NE1 TRP D 80 -25.555 -0.770 62.019 1.00 16.27 N ANISOU 4168 NE1 TRP D 80 1945 1988 2248 -225 -584 334 N ATOM 4169 CE2 TRP D 80 -25.292 -0.432 60.719 1.00 16.43 C ANISOU 4169 CE2 TRP D 80 2073 1996 2174 -261 -695 293 C ATOM 4170 CE3 TRP D 80 -25.598 1.467 59.279 1.00 16.73 C ANISOU 4170 CE3 TRP D 80 2158 2035 2163 -297 -827 309 C ATOM 4171 CZ2 TRP D 80 -24.703 -1.176 59.696 1.00 16.78 C ANISOU 4171 CZ2 TRP D 80 2286 1999 2090 -291 -765 226 C ATOM 4172 CZ3 TRP D 80 -25.013 0.734 58.267 1.00 17.16 C ANISOU 4172 CZ3 TRP D 80 2400 2048 2068 -333 -894 244 C ATOM 4173 CH2 TRP D 80 -24.580 -0.577 58.479 1.00 17.15 C ANISOU 4173 CH2 TRP D 80 2457 2024 2034 -328 -855 199 C ATOM 4174 N ASP D 81 -29.240 1.789 63.873 1.00 18.62 N ANISOU 4174 N ASP D 81 1715 2170 3188 -200 -389 631 N ATOM 4175 CA ASP D 81 -29.942 0.790 64.674 1.00 19.67 C ANISOU 4175 CA ASP D 81 1765 2234 3472 -211 -305 691 C ATOM 4176 C ASP D 81 -31.418 0.637 64.277 1.00 21.42 C ANISOU 4176 C ASP D 81 1788 2336 4012 -267 -402 808 C ATOM 4177 O ASP D 81 -31.973 -0.440 64.388 1.00 22.21 O ANISOU 4177 O ASP D 81 1830 2364 4243 -314 -434 854 O ATOM 4178 CB ASP D 81 -29.838 1.102 66.174 1.00 19.64 C ANISOU 4178 CB ASP D 81 1771 2244 3444 -143 -39 701 C ATOM 4179 CG ASP D 81 -28.417 0.874 66.740 1.00 18.47 C ANISOU 4179 CG ASP D 81 1811 2191 3015 -104 18 604 C ATOM 4180 OD1 ASP D 81 -27.572 0.171 66.133 1.00 17.85 O ANISOU 4180 OD1 ASP D 81 1826 2154 2802 -122 -105 541 O ATOM 4181 OD2 ASP D 81 -28.135 1.424 67.815 1.00 18.50 O ANISOU 4181 OD2 ASP D 81 1875 2213 2939 -55 188 595 O ATOM 4182 N ARG D 82 -32.033 1.713 63.801 1.00 22.14 N ANISOU 4182 N ARG D 82 1769 2396 4246 -264 -460 864 N ATOM 4183 CA ARG D 82 -33.431 1.693 63.408 1.00 24.15 C ANISOU 4183 CA ARG D 82 1801 2524 4847 -315 -575 992 C ATOM 4184 C ARG D 82 -33.621 0.994 62.065 1.00 24.98 C ANISOU 4184 C ARG D 82 1950 2582 4956 -420 -911 996 C ATOM 4185 O ARG D 82 -34.633 0.342 61.862 1.00 26.75 O ANISOU 4185 O ARG D 82 2023 2693 5445 -490 -1036 1089 O ATOM 4186 CB ARG D 82 -33.983 3.122 63.333 1.00 24.78 C ANISOU 4186 CB ARG D 82 1750 2574 5090 -269 -537 1058 C ATOM 4187 CG ARG D 82 -35.500 3.231 63.264 1.00 27.09 C ANISOU 4187 CG ARG D 82 1752 2718 5823 -295 -585 1217 C ATOM 4188 CD ARG D 82 -35.919 4.675 63.165 1.00 27.72 C ANISOU 4188 CD ARG D 82 1716 2764 6050 -236 -541 1278 C ATOM 4189 NE ARG D 82 -35.561 5.229 61.860 1.00 27.42 N ANISOU 4189 NE ARG D 82 1782 2759 5874 -276 -834 1253 N ATOM 4190 CZ ARG D 82 -36.312 5.135 60.756 1.00 29.04 C ANISOU 4190 CZ ARG D 82 1894 2873 6266 -358 -1162 1344 C ATOM 4191 NH1 ARG D 82 -37.492 4.519 60.760 1.00 31.12 N ANISOU 4191 NH1 ARG D 82 1917 3003 6903 -413 -1262 1473 N ATOM 4192 NH2 ARG D 82 -35.882 5.679 59.628 1.00 28.79 N ANISOU 4192 NH2 ARG D 82 2017 2870 6049 -392 -1402 1314 N ATOM 4193 N THR D 83 -32.665 1.130 61.149 1.00 24.05 N ANISOU 4193 N THR D 83 2048 2535 4552 -437 -1052 897 N ATOM 4194 CA THR D 83 -32.858 0.641 59.781 1.00 25.13 C ANISOU 4194 CA THR D 83 2284 2607 4655 -540 -1372 897 C ATOM 4195 C THR D 83 -32.034 -0.599 59.458 1.00 24.56 C ANISOU 4195 C THR D 83 2430 2553 4347 -579 -1416 792 C ATOM 4196 O THR D 83 -32.346 -1.309 58.507 1.00 25.70 O ANISOU 4196 O THR D 83 2666 2611 4488 -677 -1660 795 O ATOM 4197 CB THR D 83 -32.530 1.737 58.741 1.00 25.10 C ANISOU 4197 CB THR D 83 2398 2628 4510 -545 -1518 877 C ATOM 4198 OG1 THR D 83 -31.141 2.056 58.819 1.00 23.35 O ANISOU 4198 OG1 THR D 83 2374 2527 3967 -483 -1364 752 O ATOM 4199 CG2 THR D 83 -33.352 3.011 58.999 1.00 25.88 C ANISOU 4199 CG2 THR D 83 2280 2694 4858 -500 -1484 987 C ATOM 4200 N HIS D 84 -30.984 -0.857 60.232 1.00 23.02 N ANISOU 4200 N HIS D 84 2329 2455 3962 -505 -1192 704 N ATOM 4201 CA HIS D 84 -30.216 -2.096 60.114 1.00 22.72 C ANISOU 4201 CA HIS D 84 2462 2420 3748 -522 -1192 617 C ATOM 4202 C HIS D 84 -30.170 -2.781 61.467 1.00 22.11 C ANISOU 4202 C HIS D 84 2301 2359 3739 -472 -981 632 C ATOM 4203 O HIS D 84 -29.097 -3.138 61.934 1.00 20.91 O ANISOU 4203 O HIS D 84 2265 2277 3402 -415 -851 555 O ATOM 4204 CB HIS D 84 -28.787 -1.813 59.606 1.00 21.68 C ANISOU 4204 CB HIS D 84 2553 2377 3308 -479 -1144 496 C ATOM 4205 CG HIS D 84 -28.751 -1.106 58.281 1.00 22.47 C ANISOU 4205 CG HIS D 84 2781 2454 3303 -526 -1321 479 C ATOM 4206 ND1 HIS D 84 -28.814 -1.777 57.073 1.00 23.87 N ANISOU 4206 ND1 HIS D 84 3150 2538 3379 -616 -1527 446 N ATOM 4207 CD2 HIS D 84 -28.705 0.215 57.975 1.00 22.35 C ANISOU 4207 CD2 HIS D 84 2751 2479 3260 -502 -1327 496 C ATOM 4208 CE1 HIS D 84 -28.797 -0.897 56.082 1.00 24.39 C ANISOU 4208 CE1 HIS D 84 3329 2591 3346 -645 -1653 447 C ATOM 4209 NE2 HIS D 84 -28.730 0.319 56.603 1.00 23.43 N ANISOU 4209 NE2 HIS D 84 3073 2552 3276 -575 -1535 480 N ATOM 4210 N PRO D 85 -31.341 -2.987 62.095 1.00 23.10 N ANISOU 4210 N PRO D 85 2225 2407 4144 -495 -946 742 N ATOM 4211 CA PRO D 85 -31.303 -3.522 63.450 1.00 22.79 C ANISOU 4211 CA PRO D 85 2136 2375 4146 -444 -713 764 C ATOM 4212 C PRO D 85 -30.692 -4.933 63.445 1.00 22.52 C ANISOU 4212 C PRO D 85 2243 2323 3987 -466 -737 705 C ATOM 4213 O PRO D 85 -31.067 -5.764 62.624 1.00 23.57 O ANISOU 4213 O PRO D 85 2409 2370 4175 -552 -925 706 O ATOM 4214 CB PRO D 85 -32.774 -3.563 63.841 1.00 24.55 C ANISOU 4214 CB PRO D 85 2118 2484 4726 -484 -689 900 C ATOM 4215 CG PRO D 85 -33.492 -3.880 62.526 1.00 25.98 C ANISOU 4215 CG PRO D 85 2257 2568 5044 -597 -1007 937 C ATOM 4216 CD PRO D 85 -32.653 -3.191 61.455 1.00 25.03 C ANISOU 4216 CD PRO D 85 2322 2523 4664 -593 -1156 844 C ATOM 4217 N PRO D 86 -29.739 -5.203 64.337 1.00 21.27 N ANISOU 4217 N PRO D 86 2183 2235 3662 -391 -564 655 N ATOM 4218 CA PRO D 86 -29.181 -6.556 64.348 1.00 21.09 C ANISOU 4218 CA PRO D 86 2282 2181 3550 -403 -585 611 C ATOM 4219 C PRO D 86 -30.147 -7.524 65.016 1.00 22.01 C ANISOU 4219 C PRO D 86 2295 2190 3876 -447 -534 703 C ATOM 4220 O PRO D 86 -30.903 -7.129 65.902 1.00 22.49 O ANISOU 4220 O PRO D 86 2220 2229 4096 -431 -386 790 O ATOM 4221 CB PRO D 86 -27.909 -6.388 65.185 1.00 19.98 C ANISOU 4221 CB PRO D 86 2246 2140 3202 -305 -430 553 C ATOM 4222 CG PRO D 86 -28.280 -5.271 66.172 1.00 19.84 C ANISOU 4222 CG PRO D 86 2136 2166 3235 -258 -269 608 C ATOM 4223 CD PRO D 86 -29.401 -4.464 65.568 1.00 20.58 C ANISOU 4223 CD PRO D 86 2080 2218 3518 -305 -340 666 C ATOM 4224 N ALA D 87 -30.176 -8.763 64.534 1.00 22.25 N ANISOU 4224 N ALA D 87 2395 2136 3920 -508 -648 685 N ATOM 4225 CA ALA D 87 -30.822 -9.821 65.245 1.00 23.03 C ANISOU 4225 CA ALA D 87 2433 2137 4180 -542 -579 760 C ATOM 4226 C ALA D 87 -29.882 -10.198 66.389 1.00 21.93 C ANISOU 4226 C ALA D 87 2403 2054 3876 -449 -385 740 C ATOM 4227 O ALA D 87 -28.659 -10.201 66.230 1.00 20.69 O ANISOU 4227 O ALA D 87 2389 1971 3498 -388 -394 651 O ATOM 4228 CB ALA D 87 -31.074 -11.015 64.322 1.00 24.09 C ANISOU 4228 CB ALA D 87 2634 2153 4364 -641 -777 737 C ATOM 4229 N MET D 88 -30.446 -10.491 67.551 1.00 22.41 N ANISOU 4229 N MET D 88 2397 2065 4051 -439 -210 830 N ATOM 4230 CA MET D 88 -29.639 -10.894 68.687 1.00 21.86 C ANISOU 4230 CA MET D 88 2457 2027 3821 -362 -52 829 C ATOM 4231 C MET D 88 -29.024 -12.292 68.539 1.00 21.87 C ANISOU 4231 C MET D 88 2582 1973 3752 -368 -121 796 C ATOM 4232 O MET D 88 -29.692 -13.243 68.106 1.00 22.84 O ANISOU 4232 O MET D 88 2669 1982 4027 -448 -200 824 O ATOM 4233 CB MET D 88 -30.465 -10.830 69.967 1.00 22.98 C ANISOU 4233 CB MET D 88 2535 2110 4086 -355 175 940 C ATOM 4234 CG MET D 88 -30.533 -9.445 70.553 1.00 22.64 C ANISOU 4234 CG MET D 88 2466 2135 3998 -299 319 951 C ATOM 4235 SD MET D 88 -31.217 -9.521 72.192 1.00 24.30 S ANISOU 4235 SD MET D 88 2706 2258 4268 -275 639 1064 S ATOM 4236 CE MET D 88 -31.387 -7.745 72.474 1.00 23.85 C ANISOU 4236 CE MET D 88 2608 2265 4185 -221 771 1053 C ATOM 4237 N GLY D 89 -27.740 -12.386 68.901 1.00 20.84 N ANISOU 4237 N GLY D 89 2593 1914 3410 -284 -98 740 N ATOM 4238 CA GLY D 89 -27.021 -13.661 69.034 1.00 20.99 C ANISOU 4238 CA GLY D 89 2733 1877 3364 -261 -122 723 C ATOM 4239 C GLY D 89 -27.507 -14.396 70.267 1.00 21.94 C ANISOU 4239 C GLY D 89 2874 1914 3546 -263 16 828 C ATOM 4240 O GLY D 89 -28.530 -14.041 70.831 1.00 22.65 O ANISOU 4240 O GLY D 89 2876 1970 3760 -299 134 910 O ATOM 4241 N PRO D 90 -26.752 -15.391 70.749 1.00 22.15 N ANISOU 4241 N PRO D 90 3025 1899 3489 -218 23 836 N ATOM 4242 CA PRO D 90 -25.341 -15.755 70.566 1.00 21.51 C ANISOU 4242 CA PRO D 90 3054 1855 3263 -139 -52 769 C ATOM 4243 C PRO D 90 -24.938 -16.304 69.200 1.00 21.38 C ANISOU 4243 C PRO D 90 3055 1801 3266 -155 -181 673 C ATOM 4244 O PRO D 90 -25.731 -16.950 68.511 1.00 22.09 O ANISOU 4244 O PRO D 90 3124 1792 3475 -240 -238 669 O ATOM 4245 CB PRO D 90 -25.134 -16.848 71.617 1.00 22.45 C ANISOU 4245 CB PRO D 90 3277 1886 3367 -109 10 851 C ATOM 4246 CG PRO D 90 -26.421 -17.503 71.696 1.00 23.64 C ANISOU 4246 CG PRO D 90 3374 1919 3688 -199 70 921 C ATOM 4247 CD PRO D 90 -27.454 -16.410 71.544 1.00 23.51 C ANISOU 4247 CD PRO D 90 3219 1946 3766 -255 122 937 C ATOM 4248 N LEU D 91 -23.677 -16.079 68.859 1.00 20.69 N ANISOU 4248 N LEU D 91 3019 1776 3064 -76 -218 601 N ATOM 4249 CA LEU D 91 -23.120 -16.541 67.596 1.00 20.81 C ANISOU 4249 CA LEU D 91 3088 1747 3070 -74 -293 502 C ATOM 4250 C LEU D 91 -22.306 -17.800 67.750 1.00 21.64 C ANISOU 4250 C LEU D 91 3284 1754 3183 -13 -283 502 C ATOM 4251 O LEU D 91 -21.717 -18.015 68.791 1.00 21.73 O ANISOU 4251 O LEU D 91 3308 1777 3169 58 -245 566 O ATOM 4252 CB LEU D 91 -22.279 -15.440 66.992 1.00 19.76 C ANISOU 4252 CB LEU D 91 2941 1727 2840 -27 -308 424 C ATOM 4253 CG LEU D 91 -23.227 -14.448 66.318 1.00 19.35 C ANISOU 4253 CG LEU D 91 2825 1721 2804 -109 -354 404 C ATOM 4254 CD1 LEU D 91 -23.043 -13.108 66.928 1.00 18.34 C ANISOU 4254 CD1 LEU D 91 2624 1726 2617 -72 -307 424 C ATOM 4255 CD2 LEU D 91 -23.005 -14.459 64.817 1.00 19.46 C ANISOU 4255 CD2 LEU D 91 2919 1699 2776 -141 -429 301 C ATOM 4256 N PRO D 92 -22.279 -18.642 66.703 1.00 22.52 N ANISOU 4256 N PRO D 92 3475 1753 3326 -42 -322 432 N ATOM 4257 CA PRO D 92 -21.413 -19.817 66.698 1.00 23.46 C ANISOU 4257 CA PRO D 92 3684 1762 3466 29 -295 419 C ATOM 4258 C PRO D 92 -19.923 -19.442 66.847 1.00 23.16 C ANISOU 4258 C PRO D 92 3629 1791 3381 159 -255 397 C ATOM 4259 O PRO D 92 -19.566 -18.287 66.711 1.00 22.04 O ANISOU 4259 O PRO D 92 3424 1772 3177 178 -255 368 O ATOM 4260 CB PRO D 92 -21.691 -20.472 65.324 1.00 24.26 C ANISOU 4260 CB PRO D 92 3902 1736 3579 -38 -338 320 C ATOM 4261 CG PRO D 92 -22.941 -19.852 64.829 1.00 24.08 C ANISOU 4261 CG PRO D 92 3839 1739 3570 -167 -425 316 C ATOM 4262 CD PRO D 92 -23.008 -18.489 65.427 1.00 22.77 C ANISOU 4262 CD PRO D 92 3539 1742 3367 -144 -403 359 C ATOM 4263 N PRO D 93 -19.057 -20.431 67.119 1.00 24.39 N ANISOU 4263 N PRO D 93 3826 1850 3590 247 -225 417 N ATOM 4264 CA PRO D 93 -17.619 -20.174 67.247 1.00 24.63 C ANISOU 4264 CA PRO D 93 3806 1916 3635 372 -198 412 C ATOM 4265 C PRO D 93 -17.045 -19.459 66.024 1.00 24.53 C ANISOU 4265 C PRO D 93 3791 1940 3589 387 -150 297 C ATOM 4266 O PRO D 93 -17.394 -19.791 64.885 1.00 25.03 O ANISOU 4266 O PRO D 93 3962 1918 3628 336 -121 206 O ATOM 4267 CB PRO D 93 -17.014 -21.576 67.361 1.00 26.01 C ANISOU 4267 CB PRO D 93 4039 1927 3913 448 -168 438 C ATOM 4268 CG PRO D 93 -18.148 -22.457 67.784 1.00 26.50 C ANISOU 4268 CG PRO D 93 4175 1900 3991 364 -192 494 C ATOM 4269 CD PRO D 93 -19.366 -21.868 67.152 1.00 25.72 C ANISOU 4269 CD PRO D 93 4086 1850 3836 232 -218 441 C ATOM 4270 N GLY D 94 -16.205 -18.458 66.258 1.00 24.26 N ANISOU 4270 N GLY D 94 3653 2019 3542 446 -146 303 N ATOM 4271 CA GLY D 94 -15.505 -17.792 65.164 1.00 24.39 C ANISOU 4271 CA GLY D 94 3664 2059 3544 473 -72 207 C ATOM 4272 C GLY D 94 -16.177 -16.535 64.673 1.00 23.50 C ANISOU 4272 C GLY D 94 3544 2067 3315 387 -100 160 C ATOM 4273 O GLY D 94 -15.489 -15.613 64.244 1.00 23.35 O ANISOU 4273 O GLY D 94 3475 2117 3277 417 -56 119 O ATOM 4274 N GLN D 95 -17.510 -16.484 64.739 1.00 23.33 N ANISOU 4274 N GLN D 95 3561 2060 3240 281 -169 174 N ATOM 4275 CA GLN D 95 -18.270 -15.467 64.034 1.00 22.68 C ANISOU 4275 CA GLN D 95 3490 2052 3074 193 -204 128 C ATOM 4276 C GLN D 95 -18.455 -14.227 64.878 1.00 21.60 C ANISOU 4276 C GLN D 95 3231 2066 2907 188 -235 183 C ATOM 4277 O GLN D 95 -18.497 -14.293 66.103 1.00 21.38 O ANISOU 4277 O GLN D 95 3147 2072 2903 212 -249 267 O ATOM 4278 CB GLN D 95 -19.644 -15.991 63.621 1.00 23.30 C ANISOU 4278 CB GLN D 95 3645 2053 3155 77 -280 126 C ATOM 4279 CG GLN D 95 -19.594 -17.214 62.768 1.00 24.80 C ANISOU 4279 CG GLN D 95 3993 2074 3354 60 -268 63 C ATOM 4280 CD GLN D 95 -20.920 -17.531 62.085 1.00 25.65 C ANISOU 4280 CD GLN D 95 4189 2098 3456 -79 -383 45 C ATOM 4281 OE1 GLN D 95 -20.974 -18.426 61.252 1.00 27.21 O ANISOU 4281 OE1 GLN D 95 4555 2148 3634 -117 -396 -19 O ATOM 4282 NE2 GLN D 95 -21.981 -16.813 62.432 1.00 25.12 N ANISOU 4282 NE2 GLN D 95 4013 2110 3420 -157 -469 106 N ATOM 4283 N ILE D 96 -18.577 -13.090 64.207 1.00 20.86 N ANISOU 4283 N ILE D 96 3125 2052 2749 154 -241 135 N ATOM 4284 CA ILE D 96 -18.776 -11.850 64.885 1.00 19.94 C ANISOU 4284 CA ILE D 96 2911 2064 2601 146 -258 175 C ATOM 4285 C ILE D 96 -20.149 -11.352 64.492 1.00 19.55 C ANISOU 4285 C ILE D 96 2860 2027 2541 46 -314 181 C ATOM 4286 O ILE D 96 -20.617 -11.590 63.389 1.00 19.90 O ANISOU 4286 O ILE D 96 2983 2005 2572 -13 -358 131 O ATOM 4287 CB ILE D 96 -17.685 -10.813 64.516 1.00 19.70 C ANISOU 4287 CB ILE D 96 2839 2112 2532 196 -217 129 C ATOM 4288 CG1 ILE D 96 -16.297 -11.450 64.641 1.00 20.51 C ANISOU 4288 CG1 ILE D 96 2923 2166 2703 294 -163 124 C ATOM 4289 CG2 ILE D 96 -17.801 -9.585 65.401 1.00 18.78 C ANISOU 4289 CG2 ILE D 96 2635 2116 2383 192 -239 173 C ATOM 4290 CD1 ILE D 96 -15.133 -10.435 64.687 1.00 20.46 C ANISOU 4290 CD1 ILE D 96 2823 2237 2714 348 -131 112 C ATOM 4291 N ARG D 97 -20.809 -10.707 65.439 1.00 19.00 N ANISOU 4291 N ARG D 97 2709 2023 2487 28 -314 249 N ATOM 4292 CA ARG D 97 -22.118 -10.118 65.220 1.00 18.96 C ANISOU 4292 CA ARG D 97 2656 2026 2522 -53 -353 276 C ATOM 4293 C ARG D 97 -22.067 -9.051 64.129 1.00 18.58 C ANISOU 4293 C ARG D 97 2615 2026 2417 -78 -394 216 C ATOM 4294 O ARG D 97 -21.019 -8.472 63.855 1.00 18.04 O ANISOU 4294 O ARG D 97 2566 2015 2272 -26 -357 165 O ATOM 4295 CB ARG D 97 -22.601 -9.484 66.520 1.00 18.57 C ANISOU 4295 CB ARG D 97 2529 2033 2494 -42 -292 355 C ATOM 4296 CG ARG D 97 -21.767 -8.261 66.938 1.00 17.64 C ANISOU 4296 CG ARG D 97 2392 2025 2284 10 -256 336 C ATOM 4297 CD ARG D 97 -22.158 -7.795 68.296 1.00 17.63 C ANISOU 4297 CD ARG D 97 2375 2050 2270 21 -183 406 C ATOM 4298 NE ARG D 97 -21.358 -6.644 68.700 1.00 17.00 N ANISOU 4298 NE ARG D 97 2302 2060 2097 60 -170 382 N ATOM 4299 CZ ARG D 97 -20.097 -6.717 69.143 1.00 17.02 C ANISOU 4299 CZ ARG D 97 2341 2090 2033 113 -200 369 C ATOM 4300 NH1 ARG D 97 -19.475 -7.889 69.241 1.00 17.51 N ANISOU 4300 NH1 ARG D 97 2435 2099 2118 148 -232 380 N ATOM 4301 NH2 ARG D 97 -19.441 -5.609 69.484 1.00 16.58 N ANISOU 4301 NH2 ARG D 97 2285 2106 1909 131 -207 349 N ATOM 4302 N GLU D 98 -23.205 -8.780 63.514 1.00 19.13 N ANISOU 4302 N GLU D 98 2664 2062 2540 -160 -475 232 N ATOM 4303 CA GLU D 98 -23.313 -7.585 62.702 1.00 18.91 C ANISOU 4303 CA GLU D 98 2634 2085 2464 -185 -521 203 C ATOM 4304 C GLU D 98 -23.196 -6.366 63.621 1.00 17.61 C ANISOU 4304 C GLU D 98 2366 2029 2296 -138 -441 238 C ATOM 4305 O GLU D 98 -23.769 -6.347 64.704 1.00 17.49 O ANISOU 4305 O GLU D 98 2271 2019 2354 -132 -385 307 O ATOM 4306 CB GLU D 98 -24.632 -7.554 61.955 1.00 20.33 C ANISOU 4306 CB GLU D 98 2798 2194 2732 -285 -659 236 C ATOM 4307 CG GLU D 98 -24.797 -8.716 60.996 1.00 21.96 C ANISOU 4307 CG GLU D 98 3144 2276 2923 -351 -766 195 C ATOM 4308 CD GLU D 98 -25.999 -8.534 60.122 1.00 23.71 C ANISOU 4308 CD GLU D 98 3365 2420 3220 -463 -955 227 C ATOM 4309 OE1 GLU D 98 -26.905 -7.731 60.506 1.00 24.33 O ANISOU 4309 OE1 GLU D 98 3277 2531 3435 -485 -985 308 O ATOM 4310 OE2 GLU D 98 -26.040 -9.166 59.036 1.00 25.31 O ANISOU 4310 OE2 GLU D 98 3744 2520 3351 -532 -1078 173 O ATOM 4311 N PRO D 99 -22.444 -5.344 63.191 1.00 16.58 N ANISOU 4311 N PRO D 99 2254 1968 2074 -110 -421 190 N ATOM 4312 CA PRO D 99 -22.214 -4.236 64.101 1.00 15.61 C ANISOU 4312 CA PRO D 99 2058 1934 1936 -69 -349 214 C ATOM 4313 C PRO D 99 -23.469 -3.407 64.334 1.00 15.36 C ANISOU 4313 C PRO D 99 1936 1904 1994 -106 -354 275 C ATOM 4314 O PRO D 99 -24.252 -3.209 63.429 1.00 15.83 O ANISOU 4314 O PRO D 99 1981 1924 2109 -162 -446 286 O ATOM 4315 CB PRO D 99 -21.122 -3.425 63.395 1.00 15.24 C ANISOU 4315 CB PRO D 99 2055 1943 1792 -42 -334 146 C ATOM 4316 CG PRO D 99 -21.370 -3.657 61.917 1.00 15.85 C ANISOU 4316 CG PRO D 99 2226 1958 1837 -93 -409 104 C ATOM 4317 CD PRO D 99 -21.935 -5.073 61.831 1.00 16.70 C ANISOU 4317 CD PRO D 99 2375 1970 1998 -127 -462 118 C ATOM 4318 N THR D 100 -23.665 -2.982 65.570 1.00 14.86 N ANISOU 4318 N THR D 100 1823 1869 1952 -76 -257 321 N ATOM 4319 CA THR D 100 -24.640 -1.954 65.921 1.00 14.77 C ANISOU 4319 CA THR D 100 1726 1859 2025 -88 -207 374 C ATOM 4320 C THR D 100 -24.080 -0.556 65.648 1.00 13.91 C ANISOU 4320 C THR D 100 1627 1822 1836 -66 -197 332 C ATOM 4321 O THR D 100 -22.923 -0.417 65.296 1.00 13.24 O ANISOU 4321 O THR D 100 1606 1786 1637 -45 -219 268 O ATOM 4322 CB THR D 100 -24.953 -2.028 67.408 1.00 15.03 C ANISOU 4322 CB THR D 100 1756 1877 2078 -59 -67 428 C ATOM 4323 OG1 THR D 100 -23.788 -1.633 68.150 1.00 14.32 O ANISOU 4323 OG1 THR D 100 1757 1850 1832 -12 -25 387 O ATOM 4324 CG2 THR D 100 -25.371 -3.450 67.795 1.00 15.72 C ANISOU 4324 CG2 THR D 100 1849 1889 2234 -77 -57 474 C ATOM 4325 N GLY D 101 -24.896 0.479 65.862 1.00 14.03 N ANISOU 4325 N GLY D 101 1570 1829 1931 -69 -147 374 N ATOM 4326 CA GLY D 101 -24.453 1.871 65.713 1.00 13.42 C ANISOU 4326 CA GLY D 101 1504 1806 1786 -49 -125 341 C ATOM 4327 C GLY D 101 -23.300 2.240 66.637 1.00 12.83 C ANISOU 4327 C GLY D 101 1511 1790 1571 -9 -53 296 C ATOM 4328 O GLY D 101 -22.323 2.859 66.229 1.00 12.15 O ANISOU 4328 O GLY D 101 1462 1758 1397 -1 -84 241 O ATOM 4329 N SER D 102 -23.409 1.860 67.898 1.00 13.12 N ANISOU 4329 N SER D 102 1586 1806 1590 10 36 325 N ATOM 4330 CA SER D 102 -22.321 2.122 68.837 1.00 12.92 C ANISOU 4330 CA SER D 102 1663 1820 1426 35 60 290 C ATOM 4331 C SER D 102 -21.060 1.291 68.471 1.00 12.52 C ANISOU 4331 C SER D 102 1636 1804 1315 45 -41 249 C ATOM 4332 O SER D 102 -19.937 1.681 68.793 1.00 12.23 O ANISOU 4332 O SER D 102 1640 1807 1200 58 -74 215 O ATOM 4333 CB SER D 102 -22.791 1.867 70.269 1.00 13.65 C ANISOU 4333 CB SER D 102 1837 1861 1488 47 176 338 C ATOM 4334 OG SER D 102 -22.945 0.477 70.486 1.00 14.04 O ANISOU 4334 OG SER D 102 1894 1873 1566 45 161 374 O ATOM 4335 N ASP D 103 -21.247 0.156 67.794 1.00 12.62 N ANISOU 4335 N ASP D 103 1620 1789 1386 36 -89 255 N ATOM 4336 CA ASP D 103 -20.106 -0.645 67.326 1.00 12.61 C ANISOU 4336 CA ASP D 103 1636 1797 1356 55 -155 216 C ATOM 4337 C ASP D 103 -19.328 0.108 66.261 1.00 12.22 C ANISOU 4337 C ASP D 103 1570 1787 1283 54 -181 158 C ATOM 4338 O ASP D 103 -18.108 0.060 66.234 1.00 12.08 O ANISOU 4338 O ASP D 103 1552 1791 1244 80 -195 127 O ATOM 4339 CB ASP D 103 -20.530 -2.010 66.739 1.00 13.01 C ANISOU 4339 CB ASP D 103 1687 1788 1468 43 -187 227 C ATOM 4340 CG ASP D 103 -20.921 -3.051 67.806 1.00 13.62 C ANISOU 4340 CG ASP D 103 1791 1814 1567 52 -160 285 C ATOM 4341 OD1 ASP D 103 -20.466 -2.987 68.966 1.00 13.83 O ANISOU 4341 OD1 ASP D 103 1867 1852 1533 78 -136 310 O ATOM 4342 OD2 ASP D 103 -21.688 -3.980 67.454 1.00 14.00 O ANISOU 4342 OD2 ASP D 103 1827 1800 1690 24 -173 310 O ATOM 4343 N ILE D 104 -20.062 0.765 65.361 1.00 12.25 N ANISOU 4343 N ILE D 104 1557 1789 1309 22 -187 152 N ATOM 4344 CA ILE D 104 -19.469 1.501 64.246 1.00 12.10 C ANISOU 4344 CA ILE D 104 1550 1792 1253 13 -199 104 C ATOM 4345 C ILE D 104 -18.719 2.718 64.777 1.00 11.89 C ANISOU 4345 C ILE D 104 1508 1820 1190 26 -165 87 C ATOM 4346 O ILE D 104 -17.625 3.037 64.306 1.00 11.83 O ANISOU 4346 O ILE D 104 1499 1832 1162 35 -155 47 O ATOM 4347 CB ILE D 104 -20.541 1.909 63.219 1.00 12.26 C ANISOU 4347 CB ILE D 104 1576 1781 1299 -30 -245 119 C ATOM 4348 CG1 ILE D 104 -21.041 0.655 62.487 1.00 12.82 C ANISOU 4348 CG1 ILE D 104 1691 1784 1394 -59 -312 122 C ATOM 4349 CG2 ILE D 104 -19.973 2.936 62.249 1.00 12.13 C ANISOU 4349 CG2 ILE D 104 1597 1786 1223 -40 -242 81 C ATOM 4350 CD1 ILE D 104 -22.345 0.824 61.713 1.00 13.36 C ANISOU 4350 CD1 ILE D 104 1753 1799 1522 -117 -411 163 C ATOM 4351 N ALA D 105 -19.279 3.343 65.805 1.00 11.94 N ANISOU 4351 N ALA D 105 1508 1834 1194 26 -135 118 N ATOM 4352 CA ALA D 105 -18.674 4.510 66.447 1.00 11.99 C ANISOU 4352 CA ALA D 105 1528 1873 1153 28 -112 100 C ATOM 4353 C ALA D 105 -17.466 4.165 67.341 1.00 12.42 C ANISOU 4353 C ALA D 105 1603 1941 1171 44 -150 90 C ATOM 4354 O ALA D 105 -16.798 5.056 67.846 1.00 12.43 O ANISOU 4354 O ALA D 105 1623 1961 1138 33 -166 72 O ATOM 4355 CB ALA D 105 -19.743 5.263 67.263 1.00 12.14 C ANISOU 4355 CB ALA D 105 1566 1869 1175 24 -45 134 C ATOM 4356 N GLY D 106 -17.183 2.876 67.509 1.00 12.89 N ANISOU 4356 N GLY D 106 1661 1982 1252 65 -183 105 N ATOM 4357 CA GLY D 106 -16.062 2.427 68.306 1.00 13.61 C ANISOU 4357 CA GLY D 106 1760 2072 1338 83 -248 113 C ATOM 4358 C GLY D 106 -16.301 2.343 69.793 1.00 14.37 C ANISOU 4358 C GLY D 106 1954 2146 1356 79 -272 152 C ATOM 4359 O GLY D 106 -15.388 1.968 70.533 1.00 15.26 O ANISOU 4359 O GLY D 106 2093 2248 1458 87 -365 171 O ATOM 4360 N THR D 107 -17.516 2.669 70.233 1.00 14.45 N ANISOU 4360 N THR D 107 2028 2137 1323 66 -188 172 N ATOM 4361 CA THR D 107 -17.854 2.724 71.660 1.00 15.33 C ANISOU 4361 CA THR D 107 2281 2209 1334 59 -162 206 C ATOM 4362 C THR D 107 -18.033 1.351 72.289 1.00 15.85 C ANISOU 4362 C THR D 107 2401 2230 1390 77 -174 259 C ATOM 4363 O THR D 107 -17.635 1.120 73.426 1.00 16.78 O ANISOU 4363 O THR D 107 2652 2314 1409 73 -224 288 O ATOM 4364 CB THR D 107 -19.189 3.493 71.853 1.00 15.48 C ANISOU 4364 CB THR D 107 2336 2198 1347 50 -14 216 C ATOM 4365 OG1 THR D 107 -19.023 4.815 71.357 1.00 15.21 O ANISOU 4365 OG1 THR D 107 2268 2193 1316 36 -5 173 O ATOM 4366 CG2 THR D 107 -19.596 3.557 73.328 1.00 16.62 C ANISOU 4366 CG2 THR D 107 2666 2277 1371 45 65 248 C ATOM 4367 N THR D 108 -18.671 0.448 71.566 1.00 15.49 N ANISOU 4367 N THR D 108 2273 2172 1439 88 -136 275 N ATOM 4368 CA THR D 108 -18.968 -0.884 72.111 1.00 16.13 C ANISOU 4368 CA THR D 108 2403 2199 1526 101 -131 330 C ATOM 4369 C THR D 108 -18.277 -2.010 71.328 1.00 16.12 C ANISOU 4369 C THR D 108 2319 2197 1607 126 -215 321 C ATOM 4370 O THR D 108 -18.640 -3.169 71.455 1.00 16.68 O ANISOU 4370 O THR D 108 2405 2217 1713 135 -205 360 O ATOM 4371 CB THR D 108 -20.478 -1.112 72.129 1.00 16.18 C ANISOU 4371 CB THR D 108 2397 2157 1591 87 2 369 C ATOM 4372 OG1 THR D 108 -21.008 -0.920 70.801 1.00 15.33 O ANISOU 4372 OG1 THR D 108 2153 2070 1600 73 2 343 O ATOM 4373 CG2 THR D 108 -21.141 -0.135 73.105 1.00 16.71 C ANISOU 4373 CG2 THR D 108 2569 2194 1585 76 130 387 C ATOM 4374 N SER D 109 -17.291 -1.676 70.505 1.00 15.81 N ANISOU 4374 N SER D 109 2198 2199 1608 138 -277 272 N ATOM 4375 CA SER D 109 -16.585 -2.688 69.740 1.00 15.90 C ANISOU 4375 CA SER D 109 2144 2190 1705 171 -317 259 C ATOM 4376 C SER D 109 -15.102 -2.595 70.040 1.00 16.55 C ANISOU 4376 C SER D 109 2189 2280 1817 201 -410 260 C ATOM 4377 O SER D 109 -14.595 -1.525 70.351 1.00 16.51 O ANISOU 4377 O SER D 109 2179 2312 1779 182 -449 247 O ATOM 4378 CB SER D 109 -16.810 -2.484 68.236 1.00 15.28 C ANISOU 4378 CB SER D 109 2002 2124 1678 159 -271 203 C ATOM 4379 OG SER D 109 -16.343 -1.207 67.814 1.00 14.84 O ANISOU 4379 OG SER D 109 1910 2121 1606 147 -264 162 O ATOM 4380 N THR D 110 -14.401 -3.717 69.901 1.00 17.36 N ANISOU 4380 N THR D 110 2253 2336 2007 245 -448 280 N ATOM 4381 CA THR D 110 -12.952 -3.757 70.107 1.00 18.30 C ANISOU 4381 CA THR D 110 2292 2442 2219 282 -542 297 C ATOM 4382 C THR D 110 -12.262 -3.568 68.745 1.00 18.26 C ANISOU 4382 C THR D 110 2168 2439 2331 305 -463 239 C ATOM 4383 O THR D 110 -12.898 -3.671 67.697 1.00 17.58 O ANISOU 4383 O THR D 110 2102 2351 2226 295 -357 189 O ATOM 4384 CB THR D 110 -12.502 -5.097 70.730 1.00 19.30 C ANISOU 4384 CB THR D 110 2429 2493 2409 330 -618 365 C ATOM 4385 OG1 THR D 110 -12.538 -6.107 69.719 1.00 19.16 O ANISOU 4385 OG1 THR D 110 2366 2425 2489 371 -527 339 O ATOM 4386 CG2 THR D 110 -13.407 -5.504 71.922 1.00 19.46 C ANISOU 4386 CG2 THR D 110 2608 2490 2293 306 -649 424 C ATOM 4387 N LEU D 111 -10.962 -3.290 68.781 1.00 19.31 N ANISOU 4387 N LEU D 111 2187 2561 2586 330 -517 251 N ATOM 4388 CA LEU D 111 -10.145 -3.107 67.556 1.00 19.73 C ANISOU 4388 CA LEU D 111 2125 2596 2774 358 -408 206 C ATOM 4389 C LEU D 111 -10.169 -4.350 66.666 1.00 20.14 C ANISOU 4389 C LEU D 111 2186 2570 2894 413 -291 184 C ATOM 4390 O LEU D 111 -10.322 -4.250 65.447 1.00 19.75 O ANISOU 4390 O LEU D 111 2165 2505 2830 410 -151 120 O ATOM 4391 CB LEU D 111 -8.691 -2.774 67.949 1.00 21.01 C ANISOU 4391 CB LEU D 111 2130 2735 3116 381 -498 249 C ATOM 4392 CG LEU D 111 -7.683 -2.366 66.872 1.00 21.61 C ANISOU 4392 CG LEU D 111 2061 2782 3366 405 -369 217 C ATOM 4393 CD1 LEU D 111 -8.193 -1.124 66.103 1.00 20.49 C ANISOU 4393 CD1 LEU D 111 1976 2706 3102 346 -268 148 C ATOM 4394 CD2 LEU D 111 -6.296 -2.103 67.512 1.00 23.12 C ANISOU 4394 CD2 LEU D 111 2066 2937 3781 419 -502 286 C ATOM 4395 N GLN D 112 -10.059 -5.520 67.286 1.00 21.16 N ANISOU 4395 N GLN D 112 2321 2639 3079 457 -353 238 N ATOM 4396 CA GLN D 112 -10.067 -6.805 66.559 1.00 21.87 C ANISOU 4396 CA GLN D 112 2436 2633 3237 511 -247 220 C ATOM 4397 C GLN D 112 -11.415 -7.049 65.871 1.00 20.73 C ANISOU 4397 C GLN D 112 2444 2494 2939 461 -175 164 C ATOM 4398 O GLN D 112 -11.480 -7.593 64.746 1.00 20.92 O ANISOU 4398 O GLN D 112 2526 2449 2972 475 -53 106 O ATOM 4399 CB GLN D 112 -9.725 -7.972 67.502 1.00 23.29 C ANISOU 4399 CB GLN D 112 2598 2742 3508 565 -349 303 C ATOM 4400 CG GLN D 112 -8.308 -7.937 68.105 1.00 24.96 C ANISOU 4400 CG GLN D 112 2641 2916 3925 621 -454 377 C ATOM 4401 CD GLN D 112 -8.095 -6.825 69.168 1.00 25.25 C ANISOU 4401 CD GLN D 112 2658 3033 3903 564 -637 422 C ATOM 4402 OE1 GLN D 112 -9.051 -6.281 69.742 1.00 24.42 O ANISOU 4402 OE1 GLN D 112 2688 2998 3589 496 -688 413 O ATOM 4403 NE2 GLN D 112 -6.824 -6.484 69.416 1.00 26.99 N ANISOU 4403 NE2 GLN D 112 2707 3224 4321 589 -732 472 N ATOM 4404 N GLU D 113 -12.493 -6.611 66.529 1.00 19.62 N ANISOU 4404 N GLU D 113 2373 2420 2661 399 -248 182 N ATOM 4405 CA GLU D 113 -13.831 -6.704 65.933 1.00 18.67 C ANISOU 4405 CA GLU D 113 2358 2301 2434 342 -208 145 C ATOM 4406 C GLU D 113 -13.960 -5.726 64.766 1.00 17.86 C ANISOU 4406 C GLU D 113 2271 2232 2280 305 -138 76 C ATOM 4407 O GLU D 113 -14.588 -6.041 63.741 1.00 17.69 O ANISOU 4407 O GLU D 113 2342 2167 2211 274 -93 30 O ATOM 4408 CB GLU D 113 -14.914 -6.438 66.982 1.00 18.25 C ANISOU 4408 CB GLU D 113 2348 2293 2292 294 -274 195 C ATOM 4409 CG GLU D 113 -14.937 -7.488 68.092 1.00 19.06 C ANISOU 4409 CG GLU D 113 2482 2344 2415 321 -330 269 C ATOM 4410 CD GLU D 113 -15.929 -7.163 69.219 1.00 18.98 C ANISOU 4410 CD GLU D 113 2538 2362 2309 277 -355 323 C ATOM 4411 OE1 GLU D 113 -16.103 -5.970 69.552 1.00 18.53 O ANISOU 4411 OE1 GLU D 113 2482 2373 2183 248 -357 316 O ATOM 4412 OE2 GLU D 113 -16.547 -8.112 69.759 1.00 19.64 O ANISOU 4412 OE2 GLU D 113 2682 2388 2391 273 -351 373 O ATOM 4413 N GLN D 114 -13.353 -4.548 64.914 1.00 17.21 N ANISOU 4413 N GLN D 114 2118 2216 2202 302 -142 73 N ATOM 4414 CA GLN D 114 -13.375 -3.548 63.842 1.00 16.69 C ANISOU 4414 CA GLN D 114 2072 2177 2089 269 -72 17 C ATOM 4415 C GLN D 114 -12.636 -4.061 62.610 1.00 17.45 C ANISOU 4415 C GLN D 114 2202 2191 2234 304 56 -34 C ATOM 4416 O GLN D 114 -13.165 -4.001 61.494 1.00 17.29 O ANISOU 4416 O GLN D 114 2306 2139 2124 268 112 -85 O ATOM 4417 CB GLN D 114 -12.810 -2.199 64.309 1.00 16.27 C ANISOU 4417 CB GLN D 114 1936 2200 2046 256 -99 27 C ATOM 4418 CG GLN D 114 -13.685 -1.490 65.340 1.00 15.46 C ANISOU 4418 CG GLN D 114 1854 2163 1857 213 -186 61 C ATOM 4419 CD GLN D 114 -12.945 -0.435 66.134 1.00 15.45 C ANISOU 4419 CD GLN D 114 1790 2210 1871 204 -242 77 C ATOM 4420 OE1 GLN D 114 -11.950 0.120 65.673 1.00 15.60 O ANISOU 4420 OE1 GLN D 114 1731 2229 1964 212 -211 58 O ATOM 4421 NE2 GLN D 114 -13.449 -0.131 67.336 1.00 15.36 N ANISOU 4421 NE2 GLN D 114 1824 2224 1786 182 -317 114 N ATOM 4422 N ILE D 115 -11.438 -4.603 62.806 1.00 18.43 N ANISOU 4422 N ILE D 115 2232 2264 2505 374 104 -17 N ATOM 4423 CA ILE D 115 -10.657 -5.133 61.677 1.00 19.65 C ANISOU 4423 CA ILE D 115 2419 2314 2731 421 276 -65 C ATOM 4424 C ILE D 115 -11.338 -6.346 61.051 1.00 20.03 C ANISOU 4424 C ILE D 115 2632 2267 2708 419 315 -103 C ATOM 4425 O ILE D 115 -11.260 -6.537 59.834 1.00 20.67 O ANISOU 4425 O ILE D 115 2853 2264 2733 415 452 -168 O ATOM 4426 CB ILE D 115 -9.224 -5.520 62.062 1.00 21.01 C ANISOU 4426 CB ILE D 115 2419 2429 3132 507 328 -24 C ATOM 4427 CG1 ILE D 115 -8.471 -4.350 62.704 1.00 21.00 C ANISOU 4427 CG1 ILE D 115 2248 2505 3225 496 259 18 C ATOM 4428 CG2 ILE D 115 -8.435 -5.997 60.832 1.00 22.43 C ANISOU 4428 CG2 ILE D 115 2640 2481 3400 563 564 -75 C ATOM 4429 CD1 ILE D 115 -7.637 -4.824 63.914 1.00 21.98 C ANISOU 4429 CD1 ILE D 115 2202 2610 3536 548 124 105 C ATOM 4430 N GLY D 116 -11.992 -7.161 61.882 1.00 19.73 N ANISOU 4430 N GLY D 116 2600 2228 2666 416 198 -61 N ATOM 4431 CA GLY D 116 -12.765 -8.295 61.408 1.00 20.17 C ANISOU 4431 CA GLY D 116 2808 2193 2662 396 203 -90 C ATOM 4432 C GLY D 116 -13.898 -7.887 60.487 1.00 19.82 C ANISOU 4432 C GLY D 116 2923 2154 2453 303 173 -140 C ATOM 4433 O GLY D 116 -14.079 -8.459 59.433 1.00 20.71 O ANISOU 4433 O GLY D 116 3207 2163 2498 282 236 -200 O ATOM 4434 N TRP D 117 -14.662 -6.880 60.875 1.00 18.90 N ANISOU 4434 N TRP D 117 2762 2144 2274 245 71 -111 N ATOM 4435 CA TRP D 117 -15.689 -6.315 59.979 1.00 18.74 C ANISOU 4435 CA TRP D 117 2864 2126 2127 158 20 -142 C ATOM 4436 C TRP D 117 -15.101 -5.746 58.690 1.00 19.60 C ANISOU 4436 C TRP D 117 3092 2196 2157 153 133 -208 C ATOM 4437 O TRP D 117 -15.626 -5.974 57.595 1.00 20.15 O ANISOU 4437 O TRP D 117 3359 2185 2112 96 123 -254 O ATOM 4438 CB TRP D 117 -16.492 -5.240 60.706 1.00 17.48 C ANISOU 4438 CB TRP D 117 2606 2080 1955 115 -81 -90 C ATOM 4439 CG TRP D 117 -17.407 -5.804 61.749 1.00 17.11 C ANISOU 4439 CG TRP D 117 2501 2043 1955 98 -170 -27 C ATOM 4440 CD1 TRP D 117 -18.178 -6.910 61.629 1.00 17.64 C ANISOU 4440 CD1 TRP D 117 2635 2028 2039 65 -220 -19 C ATOM 4441 CD2 TRP D 117 -17.649 -5.289 63.064 1.00 16.43 C ANISOU 4441 CD2 TRP D 117 2301 2036 1902 108 -203 35 C ATOM 4442 NE1 TRP D 117 -18.878 -7.126 62.777 1.00 17.35 N ANISOU 4442 NE1 TRP D 117 2515 2016 2058 57 -266 51 N ATOM 4443 CE2 TRP D 117 -18.567 -6.152 63.683 1.00 16.58 C ANISOU 4443 CE2 TRP D 117 2323 2016 1961 86 -248 84 C ATOM 4444 CE3 TRP D 117 -17.172 -4.186 63.782 1.00 15.79 C ANISOU 4444 CE3 TRP D 117 2139 2043 1816 129 -193 53 C ATOM 4445 CZ2 TRP D 117 -19.024 -5.955 64.975 1.00 16.26 C ANISOU 4445 CZ2 TRP D 117 2220 2014 1941 88 -258 151 C ATOM 4446 CZ3 TRP D 117 -17.634 -3.986 65.065 1.00 15.50 C ANISOU 4446 CZ3 TRP D 117 2058 2044 1785 127 -222 112 C ATOM 4447 CH2 TRP D 117 -18.538 -4.875 65.658 1.00 15.81 C ANISOU 4447 CH2 TRP D 117 2116 2038 1852 111 -242 161 C ATOM 4448 N MET D 118 -14.001 -5.010 58.828 1.00 19.93 N ANISOU 4448 N MET D 118 3028 2283 2261 205 236 -207 N ATOM 4449 CA MET D 118 -13.440 -4.235 57.721 1.00 20.74 C ANISOU 4449 CA MET D 118 3224 2358 2296 196 364 -255 C ATOM 4450 C MET D 118 -12.794 -5.121 56.658 1.00 22.64 C ANISOU 4450 C MET D 118 3637 2449 2513 229 542 -320 C ATOM 4451 O MET D 118 -12.765 -4.746 55.488 1.00 23.29 O ANISOU 4451 O MET D 118 3914 2468 2465 194 635 -371 O ATOM 4452 CB MET D 118 -12.437 -3.208 58.266 1.00 20.49 C ANISOU 4452 CB MET D 118 3002 2407 2373 236 423 -226 C ATOM 4453 CG MET D 118 -13.124 -2.032 58.965 1.00 19.24 C ANISOU 4453 CG MET D 118 2757 2374 2179 187 283 -184 C ATOM 4454 SD MET D 118 -12.058 -0.851 59.832 1.00 18.99 S ANISOU 4454 SD MET D 118 2513 2430 2271 214 297 -148 S ATOM 4455 CE MET D 118 -11.026 -0.213 58.491 1.00 19.92 C ANISOU 4455 CE MET D 118 2686 2483 2396 221 510 -194 C ATOM 4456 N THR D 119 -12.317 -6.305 57.073 1.00 23.74 N ANISOU 4456 N THR D 119 3728 2517 2771 296 594 -316 N ATOM 4457 CA THR D 119 -11.609 -7.255 56.187 1.00 25.90 C ANISOU 4457 CA THR D 119 4155 2626 3058 348 799 -377 C ATOM 4458 C THR D 119 -12.397 -8.519 55.869 1.00 27.13 C ANISOU 4458 C THR D 119 4507 2671 3127 315 739 -413 C ATOM 4459 O THR D 119 -11.859 -9.460 55.312 1.00 28.63 O ANISOU 4459 O THR D 119 4826 2711 3338 365 903 -462 O ATOM 4460 CB THR D 119 -10.277 -7.712 56.804 1.00 26.54 C ANISOU 4460 CB THR D 119 4023 2671 3388 465 936 -341 C ATOM 4461 OG1 THR D 119 -10.524 -8.414 58.036 1.00 25.79 O ANISOU 4461 OG1 THR D 119 3777 2619 3401 492 775 -277 O ATOM 4462 CG2 THR D 119 -9.366 -6.513 57.041 1.00 26.31 C ANISOU 4462 CG2 THR D 119 3795 2723 3477 491 1000 -306 C ATOM 4463 N HIS D 120 -13.666 -8.538 56.240 1.00 27.00 N ANISOU 4463 N HIS D 120 4507 2716 3032 233 513 -385 N ATOM 4464 CA HIS D 120 -14.545 -9.631 55.923 1.00 28.37 C ANISOU 4464 CA HIS D 120 4860 2785 3132 177 421 -413 C ATOM 4465 C HIS D 120 -14.837 -9.663 54.408 1.00 30.27 C ANISOU 4465 C HIS D 120 5441 2896 3164 103 462 -499 C ATOM 4466 O HIS D 120 -14.717 -8.644 53.709 1.00 30.44 O ANISOU 4466 O HIS D 120 5547 2943 3073 73 503 -519 O ATOM 4467 CB HIS D 120 -15.840 -9.454 56.716 1.00 27.60 C ANISOU 4467 CB HIS D 120 4657 2787 3042 101 178 -346 C ATOM 4468 CG HIS D 120 -16.650 -10.696 56.818 1.00 28.61 C ANISOU 4468 CG HIS D 120 4871 2819 3178 57 75 -344 C ATOM 4469 ND1 HIS D 120 -17.708 -10.966 55.974 1.00 29.57 N ANISOU 4469 ND1 HIS D 120 5198 2854 3180 -56 -62 -375 N ATOM 4470 CD2 HIS D 120 -16.546 -11.757 57.654 1.00 29.06 C ANISOU 4470 CD2 HIS D 120 4842 2840 3358 105 78 -310 C ATOM 4471 CE1 HIS D 120 -18.219 -12.144 56.286 1.00 30.37 C ANISOU 4471 CE1 HIS D 120 5328 2871 3341 -80 -132 -365 C ATOM 4472 NE2 HIS D 120 -17.531 -12.646 57.301 1.00 29.98 N ANISOU 4472 NE2 HIS D 120 5108 2850 3433 20 -37 -325 N ATOM 4473 N ASN D 121 -15.204 -10.838 53.906 1.00 31.88 N ANISOU 4473 N ASN D 121 5861 2946 3303 70 448 -549 N ATOM 4474 CA ASN D 121 -15.649 -10.997 52.525 1.00 33.84 C ANISOU 4474 CA ASN D 121 6486 3049 3323 -22 432 -631 C ATOM 4475 C ASN D 121 -17.079 -11.557 52.540 1.00 33.93 C ANISOU 4475 C ASN D 121 6581 3025 3284 -147 143 -612 C ATOM 4476 O ASN D 121 -17.277 -12.738 52.812 1.00 34.46 O ANISOU 4476 O ASN D 121 6679 2999 3415 -146 119 -623 O ATOM 4477 CB ASN D 121 -14.706 -11.954 51.777 1.00 36.16 C ANISOU 4477 CB ASN D 121 7017 3144 3578 43 702 -721 C ATOM 4478 CG ASN D 121 -14.746 -11.768 50.275 1.00 38.31 C ANISOU 4478 CG ASN D 121 7711 3264 3579 -30 780 -813 C ATOM 4479 OD1 ASN D 121 -15.039 -12.710 49.522 1.00 40.50 O ANISOU 4479 OD1 ASN D 121 8320 3353 3713 -85 779 -889 O ATOM 4480 ND2 ASN D 121 -14.426 -10.555 49.819 1.00 38.25 N ANISOU 4480 ND2 ASN D 121 7723 3323 3486 -36 852 -807 N ATOM 4481 N PRO D 122 -18.089 -10.704 52.291 1.00 33.43 N ANISOU 4481 N PRO D 122 6531 3029 3140 -253 -81 -574 N ATOM 4482 CA PRO D 122 -18.011 -9.275 51.995 1.00 32.67 C ANISOU 4482 CA PRO D 122 6400 3039 2974 -265 -85 -551 C ATOM 4483 C PRO D 122 -17.799 -8.408 53.251 1.00 30.22 C ANISOU 4483 C PRO D 122 5706 2930 2847 -191 -71 -467 C ATOM 4484 O PRO D 122 -18.226 -8.776 54.347 1.00 28.99 O ANISOU 4484 O PRO D 122 5326 2842 2846 -175 -158 -406 O ATOM 4485 CB PRO D 122 -19.374 -8.980 51.375 1.00 33.28 C ANISOU 4485 CB PRO D 122 6622 3080 2940 -412 -385 -526 C ATOM 4486 CG PRO D 122 -20.308 -9.936 52.080 1.00 33.20 C ANISOU 4486 CG PRO D 122 6489 3051 3075 -459 -566 -481 C ATOM 4487 CD PRO D 122 -19.484 -11.135 52.510 1.00 33.56 C ANISOU 4487 CD PRO D 122 6527 3027 3194 -367 -370 -526 C ATOM 4488 N PRO D 123 -17.157 -7.244 53.075 1.00 29.56 N ANISOU 4488 N PRO D 123 5572 2925 2732 -155 38 -464 N ATOM 4489 CA PRO D 123 -16.810 -6.385 54.190 1.00 27.66 C ANISOU 4489 CA PRO D 123 5013 2853 2643 -90 64 -398 C ATOM 4490 C PRO D 123 -17.968 -5.549 54.702 1.00 26.16 C ANISOU 4490 C PRO D 123 4681 2773 2485 -154 -150 -323 C ATOM 4491 O PRO D 123 -18.859 -5.172 53.938 1.00 26.56 O ANISOU 4491 O PRO D 123 4874 2786 2431 -247 -305 -316 O ATOM 4492 CB PRO D 123 -15.753 -5.468 53.594 1.00 28.02 C ANISOU 4492 CB PRO D 123 5105 2907 2632 -48 260 -430 C ATOM 4493 CG PRO D 123 -16.167 -5.315 52.199 1.00 29.45 C ANISOU 4493 CG PRO D 123 5622 2975 2592 -133 229 -480 C ATOM 4494 CD PRO D 123 -16.714 -6.663 51.793 1.00 30.82 C ANISOU 4494 CD PRO D 123 6004 3005 2700 -181 150 -523 C ATOM 4495 N ILE D 124 -17.933 -5.302 56.008 1.00 24.49 N ANISOU 4495 N ILE D 124 4199 2679 2424 -103 -157 -262 N ATOM 4496 CA ILE D 124 -18.742 -4.301 56.668 1.00 22.92 C ANISOU 4496 CA ILE D 124 3834 2592 2281 -132 -278 -191 C ATOM 4497 C ILE D 124 -17.733 -3.194 56.991 1.00 21.49 C ANISOU 4497 C ILE D 124 3541 2506 2116 -70 -149 -192 C ATOM 4498 O ILE D 124 -16.967 -3.300 57.952 1.00 20.73 O ANISOU 4498 O ILE D 124 3292 2465 2119 0 -69 -178 O ATOM 4499 CB ILE D 124 -19.405 -4.842 57.961 1.00 22.59 C ANISOU 4499 CB ILE D 124 3611 2592 2379 -123 -350 -126 C ATOM 4500 CG1 ILE D 124 -20.097 -6.188 57.707 1.00 23.74 C ANISOU 4500 CG1 ILE D 124 3857 2622 2539 -173 -438 -131 C ATOM 4501 CG2 ILE D 124 -20.412 -3.818 58.494 1.00 21.91 C ANISOU 4501 CG2 ILE D 124 3387 2585 2351 -159 -451 -55 C ATOM 4502 CD1 ILE D 124 -19.179 -7.440 57.881 1.00 24.35 C ANISOU 4502 CD1 ILE D 124 3984 2630 2637 -107 -317 -174 C ATOM 4503 N PRO D 125 -17.685 -2.148 56.152 1.00 20.92 N ANISOU 4503 N PRO D 125 3560 2441 1947 -102 -139 -206 N ATOM 4504 CA PRO D 125 -16.604 -1.187 56.257 1.00 20.11 C ANISOU 4504 CA PRO D 125 3380 2400 1860 -52 2 -216 C ATOM 4505 C PRO D 125 -16.925 -0.152 57.317 1.00 18.31 C ANISOU 4505 C PRO D 125 2951 2291 1714 -46 -60 -158 C ATOM 4506 O PRO D 125 -17.323 0.951 57.001 1.00 17.83 O ANISOU 4506 O PRO D 125 2902 2261 1609 -81 -103 -139 O ATOM 4507 CB PRO D 125 -16.578 -0.579 54.858 1.00 21.15 C ANISOU 4507 CB PRO D 125 3734 2466 1835 -101 34 -251 C ATOM 4508 CG PRO D 125 -18.003 -0.600 54.447 1.00 21.48 C ANISOU 4508 CG PRO D 125 3874 2475 1812 -187 -181 -219 C ATOM 4509 CD PRO D 125 -18.621 -1.793 55.071 1.00 21.50 C ANISOU 4509 CD PRO D 125 3815 2454 1899 -192 -274 -204 C ATOM 4510 N VAL D 126 -16.759 -0.528 58.580 1.00 17.28 N ANISOU 4510 N VAL D 126 2658 2213 1692 -2 -65 -129 N ATOM 4511 CA VAL D 126 -17.187 0.324 59.691 1.00 16.07 C ANISOU 4511 CA VAL D 126 2358 2150 1595 -1 -120 -77 C ATOM 4512 C VAL D 126 -16.354 1.591 59.807 1.00 15.46 C ANISOU 4512 C VAL D 126 2220 2132 1521 13 -53 -85 C ATOM 4513 O VAL D 126 -16.845 2.605 60.305 1.00 14.82 O ANISOU 4513 O VAL D 126 2079 2104 1444 -3 -93 -55 O ATOM 4514 CB VAL D 126 -17.191 -0.416 61.042 1.00 15.66 C ANISOU 4514 CB VAL D 126 2201 2122 1626 34 -141 -42 C ATOM 4515 CG1 VAL D 126 -18.249 -1.463 61.013 1.00 15.99 C ANISOU 4515 CG1 VAL D 126 2285 2107 1682 4 -214 -21 C ATOM 4516 CG2 VAL D 126 -15.790 -1.019 61.384 1.00 15.97 C ANISOU 4516 CG2 VAL D 126 2193 2149 1722 98 -62 -61 C ATOM 4517 N GLY D 127 -15.101 1.518 59.367 1.00 15.72 N ANISOU 4517 N GLY D 127 2260 2141 1569 46 61 -122 N ATOM 4518 CA GLY D 127 -14.241 2.684 59.337 1.00 15.69 C ANISOU 4518 CA GLY D 127 2196 2174 1589 50 133 -128 C ATOM 4519 C GLY D 127 -14.862 3.727 58.442 1.00 15.58 C ANISOU 4519 C GLY D 127 2285 2158 1476 0 120 -130 C ATOM 4520 O GLY D 127 -15.059 4.856 58.876 1.00 15.11 O ANISOU 4520 O GLY D 127 2162 2152 1424 -16 88 -107 O ATOM 4521 N GLU D 128 -15.210 3.327 57.222 1.00 16.24 N ANISOU 4521 N GLU D 128 2546 2167 1457 -28 133 -154 N ATOM 4522 CA GLU D 128 -15.784 4.227 56.210 1.00 16.61 C ANISOU 4522 CA GLU D 128 2731 2187 1389 -82 99 -148 C ATOM 4523 C GLU D 128 -17.206 4.726 56.621 1.00 15.48 C ANISOU 4523 C GLU D 128 2541 2081 1259 -118 -74 -91 C ATOM 4524 O GLU D 128 -17.534 5.888 56.397 1.00 15.27 O ANISOU 4524 O GLU D 128 2519 2071 1211 -142 -104 -64 O ATOM 4525 CB GLU D 128 -15.747 3.553 54.807 1.00 18.45 C ANISOU 4525 CB GLU D 128 3216 2307 1484 -110 145 -189 C ATOM 4526 CG GLU D 128 -16.779 4.067 53.775 1.00 19.52 C ANISOU 4526 CG GLU D 128 3547 2390 1477 -185 11 -166 C ATOM 4527 CD GLU D 128 -16.624 3.513 52.324 1.00 21.58 C ANISOU 4527 CD GLU D 128 4129 2518 1552 -225 60 -214 C ATOM 4528 OE1 GLU D 128 -17.008 2.336 52.061 1.00 22.68 O ANISOU 4528 OE1 GLU D 128 4385 2584 1647 -244 -2 -240 O ATOM 4529 OE2 GLU D 128 -16.165 4.271 51.414 1.00 22.78 O ANISOU 4529 OE2 GLU D 128 4446 2622 1585 -245 160 -224 O ATOM 4530 N ILE D 129 -18.017 3.878 57.263 1.00 14.60 N ANISOU 4530 N ILE D 129 2369 1972 1207 -118 -171 -67 N ATOM 4531 CA ILE D 129 -19.337 4.310 57.722 1.00 13.88 C ANISOU 4531 CA ILE D 129 2198 1898 1177 -144 -299 -4 C ATOM 4532 C ILE D 129 -19.253 5.375 58.834 1.00 12.76 C ANISOU 4532 C ILE D 129 1906 1832 1108 -113 -254 20 C ATOM 4533 O ILE D 129 -19.950 6.396 58.778 1.00 12.58 O ANISOU 4533 O ILE D 129 1857 1812 1109 -129 -297 61 O ATOM 4534 CB ILE D 129 -20.233 3.121 58.168 1.00 13.97 C ANISOU 4534 CB ILE D 129 2171 1878 1259 -155 -389 23 C ATOM 4535 CG1 ILE D 129 -20.482 2.173 56.991 1.00 14.94 C ANISOU 4535 CG1 ILE D 129 2472 1905 1299 -204 -467 -1 C ATOM 4536 CG2 ILE D 129 -21.556 3.651 58.729 1.00 13.83 C ANISOU 4536 CG2 ILE D 129 2033 1867 1355 -173 -479 100 C ATOM 4537 CD1 ILE D 129 -20.911 0.783 57.376 1.00 15.19 C ANISOU 4537 CD1 ILE D 129 2487 1893 1389 -211 -515 2 C ATOM 4538 N TYR D 130 -18.378 5.160 59.818 1.00 11.99 N ANISOU 4538 N TYR D 130 1728 1782 1046 -71 -174 -1 N ATOM 4539 CA TYR D 130 -18.177 6.128 60.890 1.00 11.36 C ANISOU 4539 CA TYR D 130 1553 1757 1005 -52 -139 11 C ATOM 4540 C TYR D 130 -17.599 7.452 60.387 1.00 11.36 C ANISOU 4540 C TYR D 130 1573 1770 973 -66 -92 -4 C ATOM 4541 O TYR D 130 -18.030 8.530 60.808 1.00 11.09 O ANISOU 4541 O TYR D 130 1505 1750 957 -71 -95 18 O ATOM 4542 CB TYR D 130 -17.267 5.534 61.984 1.00 11.11 C ANISOU 4542 CB TYR D 130 1460 1756 1005 -17 -105 -4 C ATOM 4543 CG TYR D 130 -17.150 6.343 63.267 1.00 10.76 C ANISOU 4543 CG TYR D 130 1363 1748 976 -10 -98 8 C ATOM 4544 CD1 TYR D 130 -18.178 7.168 63.703 1.00 10.60 C ANISOU 4544 CD1 TYR D 130 1340 1726 961 -20 -97 38 C ATOM 4545 CD2 TYR D 130 -16.042 6.208 64.077 1.00 10.84 C ANISOU 4545 CD2 TYR D 130 1337 1778 1001 5 -98 -6 C ATOM 4546 CE1 TYR D 130 -18.065 7.884 64.857 1.00 10.58 C ANISOU 4546 CE1 TYR D 130 1336 1736 947 -16 -72 39 C ATOM 4547 CE2 TYR D 130 -15.923 6.900 65.230 1.00 10.87 C ANISOU 4547 CE2 TYR D 130 1340 1798 990 0 -115 0 C ATOM 4548 CZ TYR D 130 -16.933 7.753 65.630 1.00 10.72 C ANISOU 4548 CZ TYR D 130 1354 1773 944 -12 -90 17 C ATOM 4549 OH TYR D 130 -16.820 8.435 66.810 1.00 10.83 O ANISOU 4549 OH TYR D 130 1412 1784 919 -21 -89 15 O ATOM 4550 N LYS D 131 -16.598 7.360 59.518 1.00 11.72 N ANISOU 4550 N LYS D 131 1676 1797 979 -68 -27 -41 N ATOM 4551 CA LYS D 131 -15.976 8.532 58.925 1.00 12.01 C ANISOU 4551 CA LYS D 131 1742 1831 989 -86 38 -53 C ATOM 4552 C LYS D 131 -17.034 9.380 58.208 1.00 12.03 C ANISOU 4552 C LYS D 131 1822 1806 940 -119 -25 -16 C ATOM 4553 O LYS D 131 -17.033 10.582 58.334 1.00 11.82 O ANISOU 4553 O LYS D 131 1773 1790 925 -128 -9 -2 O ATOM 4554 CB LYS D 131 -14.895 8.115 57.914 1.00 12.90 C ANISOU 4554 CB LYS D 131 1931 1898 1070 -84 151 -91 C ATOM 4555 CG LYS D 131 -14.111 9.275 57.349 1.00 13.45 C ANISOU 4555 CG LYS D 131 2022 1956 1133 -103 252 -98 C ATOM 4556 CD LYS D 131 -13.194 8.864 56.202 1.00 14.66 C ANISOU 4556 CD LYS D 131 2282 2037 1249 -101 406 -129 C ATOM 4557 CE LYS D 131 -12.241 7.739 56.594 1.00 15.11 C ANISOU 4557 CE LYS D 131 2245 2081 1412 -53 486 -154 C ATOM 4558 NZ LYS D 131 -11.251 7.384 55.483 1.00 16.59 N ANISOU 4558 NZ LYS D 131 2531 2176 1594 -40 694 -184 N ATOM 4559 N ARG D 132 -17.889 8.713 57.440 1.00 12.37 N ANISOU 4559 N ARG D 132 1961 1801 936 -140 -110 1 N ATOM 4560 CA ARG D 132 -19.033 9.310 56.805 1.00 12.78 C ANISOU 4560 CA ARG D 132 2072 1813 971 -174 -225 55 C ATOM 4561 C ARG D 132 -19.932 10.051 57.796 1.00 12.02 C ANISOU 4561 C ARG D 132 1833 1742 991 -156 -266 107 C ATOM 4562 O ARG D 132 -20.398 11.143 57.499 1.00 12.26 O ANISOU 4562 O ARG D 132 1869 1750 1037 -166 -296 147 O ATOM 4563 CB ARG D 132 -19.851 8.242 56.075 1.00 13.77 C ANISOU 4563 CB ARG D 132 2298 1874 1059 -207 -351 71 C ATOM 4564 CG ARG D 132 -20.890 8.820 55.189 1.00 14.91 C ANISOU 4564 CG ARG D 132 2528 1954 1182 -254 -505 135 C ATOM 4565 CD ARG D 132 -21.582 7.736 54.378 1.00 16.19 C ANISOU 4565 CD ARG D 132 2822 2036 1292 -306 -659 146 C ATOM 4566 NE ARG D 132 -22.432 6.887 55.220 1.00 16.14 N ANISOU 4566 NE ARG D 132 2661 2036 1433 -300 -735 177 N ATOM 4567 CZ ARG D 132 -22.528 5.561 55.084 1.00 16.75 C ANISOU 4567 CZ ARG D 132 2797 2075 1491 -322 -781 150 C ATOM 4568 NH1 ARG D 132 -21.817 4.906 54.162 1.00 17.53 N ANISOU 4568 NH1 ARG D 132 3114 2121 1424 -346 -748 84 N ATOM 4569 NH2 ARG D 132 -23.315 4.865 55.894 1.00 16.73 N ANISOU 4569 NH2 ARG D 132 2644 2073 1637 -318 -835 187 N ATOM 4570 N TRP D 133 -20.192 9.472 58.960 1.00 11.22 N ANISOU 4570 N TRP D 133 1619 1672 971 -128 -252 109 N ATOM 4571 CA TRP D 133 -20.989 10.200 59.960 1.00 10.87 C ANISOU 4571 CA TRP D 133 1466 1633 1030 -105 -238 152 C ATOM 4572 C TRP D 133 -20.245 11.440 60.467 1.00 10.40 C ANISOU 4572 C TRP D 133 1397 1604 951 -93 -146 125 C ATOM 4573 O TRP D 133 -20.845 12.489 60.600 1.00 10.48 O ANISOU 4573 O TRP D 133 1381 1587 1012 -87 -137 160 O ATOM 4574 CB TRP D 133 -21.409 9.327 61.131 1.00 10.58 C ANISOU 4574 CB TRP D 133 1348 1607 1061 -81 -216 162 C ATOM 4575 CG TRP D 133 -22.198 8.138 60.742 1.00 10.96 C ANISOU 4575 CG TRP D 133 1391 1616 1155 -99 -306 194 C ATOM 4576 CD1 TRP D 133 -22.836 7.903 59.549 1.00 11.64 C ANISOU 4576 CD1 TRP D 133 1530 1646 1245 -141 -435 226 C ATOM 4577 CD2 TRP D 133 -22.407 6.979 61.539 1.00 10.87 C ANISOU 4577 CD2 TRP D 133 1336 1605 1186 -87 -291 199 C ATOM 4578 NE1 TRP D 133 -23.431 6.662 59.567 1.00 11.94 N ANISOU 4578 NE1 TRP D 133 1551 1649 1336 -160 -506 246 N ATOM 4579 CE2 TRP D 133 -23.198 6.082 60.782 1.00 11.48 C ANISOU 4579 CE2 TRP D 133 1426 1626 1309 -124 -407 231 C ATOM 4580 CE3 TRP D 133 -22.040 6.626 62.839 1.00 10.50 C ANISOU 4580 CE3 TRP D 133 1259 1590 1138 -54 -202 184 C ATOM 4581 CZ2 TRP D 133 -23.600 4.848 61.275 1.00 11.65 C ANISOU 4581 CZ2 TRP D 133 1412 1625 1390 -127 -419 247 C ATOM 4582 CZ3 TRP D 133 -22.457 5.405 63.326 1.00 10.72 C ANISOU 4582 CZ3 TRP D 133 1264 1595 1211 -52 -209 206 C ATOM 4583 CH2 TRP D 133 -23.232 4.530 62.539 1.00 11.20 C ANISOU 4583 CH2 TRP D 133 1319 1602 1334 -87 -309 236 C ATOM 4584 N ILE D 134 -18.941 11.308 60.699 1.00 10.02 N ANISOU 4584 N ILE D 134 1364 1595 847 -92 -84 67 N ATOM 4585 CA ILE D 134 -18.122 12.423 61.210 1.00 9.87 C ANISOU 4585 CA ILE D 134 1333 1595 821 -96 -18 38 C ATOM 4586 C ILE D 134 -18.073 13.577 60.197 1.00 10.15 C ANISOU 4586 C ILE D 134 1423 1599 832 -120 -6 51 C ATOM 4587 O ILE D 134 -18.217 14.725 60.576 1.00 10.21 O ANISOU 4587 O ILE D 134 1420 1593 864 -122 21 60 O ATOM 4588 CB ILE D 134 -16.690 11.961 61.605 1.00 9.81 C ANISOU 4588 CB ILE D 134 1301 1622 802 -98 16 -10 C ATOM 4589 CG1 ILE D 134 -16.729 10.951 62.762 1.00 9.60 C ANISOU 4589 CG1 ILE D 134 1236 1617 794 -74 -10 -13 C ATOM 4590 CG2 ILE D 134 -15.862 13.101 62.071 1.00 9.99 C ANISOU 4590 CG2 ILE D 134 1306 1649 837 -119 52 -34 C ATOM 4591 CD1 ILE D 134 -15.380 10.183 62.969 1.00 9.79 C ANISOU 4591 CD1 ILE D 134 1220 1659 838 -69 -9 -43 C ATOM 4592 N ILE D 135 -17.905 13.252 58.920 1.00 10.47 N ANISOU 4592 N ILE D 135 1547 1616 813 -140 -22 55 N ATOM 4593 CA ILE D 135 -17.864 14.238 57.834 1.00 10.98 C ANISOU 4593 CA ILE D 135 1705 1638 827 -168 -13 76 C ATOM 4594 C ILE D 135 -19.177 14.992 57.692 1.00 11.19 C ANISOU 4594 C ILE D 135 1729 1622 900 -164 -100 145 C ATOM 4595 O ILE D 135 -19.174 16.186 57.352 1.00 11.45 O ANISOU 4595 O ILE D 135 1797 1622 931 -174 -82 169 O ATOM 4596 CB ILE D 135 -17.546 13.585 56.453 1.00 11.69 C ANISOU 4596 CB ILE D 135 1943 1687 810 -193 -13 68 C ATOM 4597 CG1 ILE D 135 -16.116 13.051 56.400 1.00 11.84 C ANISOU 4597 CG1 ILE D 135 1960 1723 815 -190 119 8 C ATOM 4598 CG2 ILE D 135 -17.781 14.566 55.287 1.00 12.46 C ANISOU 4598 CG2 ILE D 135 2182 1721 829 -227 -32 109 C ATOM 4599 CD1 ILE D 135 -15.118 14.005 56.838 1.00 11.84 C ANISOU 4599 CD1 ILE D 135 1885 1741 873 -196 218 -10 C ATOM 4600 N LEU D 136 -20.282 14.274 57.906 1.00 11.22 N ANISOU 4600 N LEU D 136 1684 1613 966 -150 -193 185 N ATOM 4601 CA LEU D 136 -21.598 14.870 57.973 1.00 11.73 C ANISOU 4601 CA LEU D 136 1688 1624 1142 -136 -270 264 C ATOM 4602 C LEU D 136 -21.653 15.842 59.125 1.00 11.47 C ANISOU 4602 C LEU D 136 1569 1598 1191 -101 -164 259 C ATOM 4603 O LEU D 136 -22.113 16.973 58.953 1.00 11.97 O ANISOU 4603 O LEU D 136 1627 1609 1311 -91 -164 304 O ATOM 4604 CB LEU D 136 -22.683 13.810 58.147 1.00 11.98 C ANISOU 4604 CB LEU D 136 1648 1635 1267 -131 -368 309 C ATOM 4605 CG LEU D 136 -24.106 14.373 58.276 1.00 12.78 C ANISOU 4605 CG LEU D 136 1638 1665 1550 -111 -439 408 C ATOM 4606 CD1 LEU D 136 -24.534 15.067 56.968 1.00 13.77 C ANISOU 4606 CD1 LEU D 136 1847 1719 1663 -143 -586 478 C ATOM 4607 CD2 LEU D 136 -25.149 13.312 58.696 1.00 13.10 C ANISOU 4607 CD2 LEU D 136 1563 1679 1734 -106 -502 457 C ATOM 4608 N GLY D 137 -21.199 15.402 60.303 1.00 10.94 N ANISOU 4608 N GLY D 137 1455 1577 1122 -83 -80 206 N ATOM 4609 CA GLY D 137 -21.084 16.290 61.465 1.00 10.90 C ANISOU 4609 CA GLY D 137 1426 1566 1149 -61 24 183 C ATOM 4610 C GLY D 137 -20.293 17.546 61.105 1.00 11.11 C ANISOU 4610 C GLY D 137 1511 1581 1128 -84 63 158 C ATOM 4611 O GLY D 137 -20.768 18.657 61.322 1.00 11.50 O ANISOU 4611 O GLY D 137 1559 1575 1235 -68 105 183 O ATOM 4612 N LEU D 138 -19.117 17.375 60.491 1.00 10.99 N ANISOU 4612 N LEU D 138 1544 1603 1027 -121 62 116 N ATOM 4613 CA LEU D 138 -18.291 18.529 60.130 1.00 11.37 C ANISOU 4613 CA LEU D 138 1639 1633 1047 -153 112 96 C ATOM 4614 C LEU D 138 -18.994 19.464 59.134 1.00 12.16 C ANISOU 4614 C LEU D 138 1791 1667 1161 -153 83 162 C ATOM 4615 O LEU D 138 -18.832 20.687 59.219 1.00 12.41 O ANISOU 4615 O LEU D 138 1845 1657 1212 -162 132 164 O ATOM 4616 CB LEU D 138 -16.922 18.113 59.575 1.00 11.28 C ANISOU 4616 CB LEU D 138 1651 1655 977 -189 145 53 C ATOM 4617 CG LEU D 138 -16.012 17.311 60.502 1.00 10.93 C ANISOU 4617 CG LEU D 138 1542 1663 946 -191 157 0 C ATOM 4618 CD1 LEU D 138 -14.796 16.855 59.748 1.00 11.21 C ANISOU 4618 CD1 LEU D 138 1576 1708 973 -215 206 -23 C ATOM 4619 CD2 LEU D 138 -15.620 18.064 61.739 1.00 10.98 C ANISOU 4619 CD2 LEU D 138 1525 1666 982 -207 169 -33 C ATOM 4620 N ASN D 139 -19.752 18.901 58.190 1.00 12.72 N ANISOU 4620 N ASN D 139 1893 1716 1222 -150 -12 218 N ATOM 4621 CA ASN D 139 -20.392 19.747 57.186 1.00 13.81 C ANISOU 4621 CA ASN D 139 2098 1781 1368 -157 -79 294 C ATOM 4622 C ASN D 139 -21.458 20.601 57.857 1.00 14.36 C ANISOU 4622 C ASN D 139 2078 1792 1585 -111 -78 348 C ATOM 4623 O ASN D 139 -21.666 21.749 57.484 1.00 15.06 O ANISOU 4623 O ASN D 139 2200 1816 1706 -107 -76 393 O ATOM 4624 CB ASN D 139 -20.963 18.937 56.013 1.00 14.40 C ANISOU 4624 CB ASN D 139 2256 1827 1386 -178 -221 346 C ATOM 4625 CG ASN D 139 -19.927 18.689 54.910 1.00 14.74 C ANISOU 4625 CG ASN D 139 2470 1870 1260 -227 -187 311 C ATOM 4626 OD1 ASN D 139 -19.808 19.467 53.973 1.00 15.60 O ANISOU 4626 OD1 ASN D 139 2709 1920 1297 -254 -196 350 O ATOM 4627 ND2 ASN D 139 -19.184 17.597 55.025 1.00 14.35 N ANISOU 4627 ND2 ASN D 139 2425 1872 1152 -234 -130 244 N ATOM 4628 N LYS D 140 -22.114 20.036 58.860 1.00 14.41 N ANISOU 4628 N LYS D 140 1977 1811 1687 -72 -59 347 N ATOM 4629 CA LYS D 140 -23.057 20.803 59.650 1.00 15.21 C ANISOU 4629 CA LYS D 140 1993 1843 1942 -19 2 389 C ATOM 4630 C LYS D 140 -22.362 21.953 60.376 1.00 15.11 C ANISOU 4630 C LYS D 140 2028 1813 1898 -19 137 329 C ATOM 4631 O LYS D 140 -22.822 23.068 60.325 1.00 15.96 O ANISOU 4631 O LYS D 140 2136 1837 2088 5 172 371 O ATOM 4632 CB LYS D 140 -23.827 19.910 60.608 1.00 15.41 C ANISOU 4632 CB LYS D 140 1914 1873 2066 17 36 397 C ATOM 4633 CG LYS D 140 -25.267 20.332 60.738 1.00 16.76 C ANISOU 4633 CG LYS D 140 1967 1941 2460 73 38 499 C ATOM 4634 CD LYS D 140 -25.981 19.569 61.872 1.00 17.08 C ANISOU 4634 CD LYS D 140 1908 1969 2613 113 139 505 C ATOM 4635 CE LYS D 140 -27.162 20.372 62.432 1.00 18.52 C ANISOU 4635 CE LYS D 140 1981 2024 3032 185 260 582 C ATOM 4636 NZ LYS D 140 -27.590 19.852 63.809 1.00 18.97 N ANISOU 4636 NZ LYS D 140 2002 2056 3150 225 450 560 N ATOM 4637 N ILE D 141 -21.206 21.684 60.960 1.00 14.40 N ANISOU 4637 N ILE D 141 1984 1790 1695 -54 192 236 N ATOM 4638 CA ILE D 141 -20.470 22.631 61.811 1.00 14.37 C ANISOU 4638 CA ILE D 141 2036 1767 1657 -72 292 170 C ATOM 4639 C ILE D 141 -19.786 23.786 61.083 1.00 14.60 C ANISOU 4639 C ILE D 141 2129 1761 1657 -112 302 168 C ATOM 4640 O ILE D 141 -19.728 24.883 61.623 1.00 15.04 O ANISOU 4640 O ILE D 141 2225 1750 1738 -113 376 148 O ATOM 4641 CB ILE D 141 -19.393 21.868 62.603 1.00 13.85 C ANISOU 4641 CB ILE D 141 1985 1777 1497 -110 298 85 C ATOM 4642 CG1 ILE D 141 -20.035 21.128 63.764 1.00 13.87 C ANISOU 4642 CG1 ILE D 141 1969 1782 1517 -71 335 76 C ATOM 4643 CG2 ILE D 141 -18.321 22.772 63.133 1.00 14.07 C ANISOU 4643 CG2 ILE D 141 2078 1788 1479 -161 337 20 C ATOM 4644 CD1 ILE D 141 -19.093 20.039 64.300 1.00 13.47 C ANISOU 4644 CD1 ILE D 141 1924 1811 1381 -102 291 20 C ATOM 4645 N VAL D 142 -19.264 23.548 59.877 1.00 14.39 N ANISOU 4645 N VAL D 142 2132 1764 1571 -148 243 189 N ATOM 4646 CA VAL D 142 -18.509 24.571 59.131 1.00 14.74 C ANISOU 4646 CA VAL D 142 2249 1770 1580 -194 274 192 C ATOM 4647 C VAL D 142 -19.312 25.861 58.908 1.00 15.41 C ANISOU 4647 C VAL D 142 2364 1751 1741 -165 287 256 C ATOM 4648 O VAL D 142 -18.748 26.931 58.764 1.00 15.80 O ANISOU 4648 O VAL D 142 2470 1749 1783 -198 342 245 O ATOM 4649 CB VAL D 142 -17.985 24.058 57.752 1.00 14.93 C ANISOU 4649 CB VAL D 142 2338 1818 1515 -230 237 217 C ATOM 4650 CG1 VAL D 142 -16.899 22.974 57.945 1.00 14.37 C ANISOU 4650 CG1 VAL D 142 2235 1829 1393 -259 266 148 C ATOM 4651 CG2 VAL D 142 -19.133 23.605 56.871 1.00 15.25 C ANISOU 4651 CG2 VAL D 142 2408 1831 1554 -200 121 302 C ATOM 4652 N ARG D 143 -20.633 25.744 58.924 1.00 15.63 N ANISOU 4652 N ARG D 143 2337 1734 1865 -102 238 327 N ATOM 4653 CA ARG D 143 -21.530 26.891 58.906 1.00 16.52 C ANISOU 4653 CA ARG D 143 2441 1732 2101 -55 258 397 C ATOM 4654 C ARG D 143 -21.260 27.869 60.086 1.00 16.56 C ANISOU 4654 C ARG D 143 2472 1681 2139 -47 403 329 C ATOM 4655 O ARG D 143 -21.513 29.083 59.980 1.00 17.33 O ANISOU 4655 O ARG D 143 2606 1674 2304 -30 451 362 O ATOM 4656 CB ARG D 143 -22.952 26.316 58.876 1.00 17.04 C ANISOU 4656 CB ARG D 143 2398 1765 2310 10 182 486 C ATOM 4657 CG ARG D 143 -23.958 26.892 59.761 1.00 17.89 C ANISOU 4657 CG ARG D 143 2422 1776 2599 86 279 519 C ATOM 4658 CD ARG D 143 -25.023 25.867 60.202 1.00 18.08 C ANISOU 4658 CD ARG D 143 2308 1803 2756 137 259 564 C ATOM 4659 NE ARG D 143 -25.237 24.777 59.233 1.00 17.95 N ANISOU 4659 NE ARG D 143 2262 1846 2710 105 70 616 N ATOM 4660 CZ ARG D 143 -26.206 23.866 59.326 1.00 18.27 C ANISOU 4660 CZ ARG D 143 2176 1878 2885 133 3 677 C ATOM 4661 NH1 ARG D 143 -27.113 23.923 60.301 1.00 18.95 N ANISOU 4661 NH1 ARG D 143 2136 1896 3167 201 129 706 N ATOM 4662 NH2 ARG D 143 -26.302 22.927 58.405 1.00 18.18 N ANISOU 4662 NH2 ARG D 143 2174 1909 2821 89 -181 714 N ATOM 4663 N MET D 144 -20.730 27.347 61.196 1.00 15.76 N ANISOU 4663 N MET D 144 2373 1635 1979 -66 463 235 N ATOM 4664 CA MET D 144 -20.340 28.180 62.329 1.00 16.08 C ANISOU 4664 CA MET D 144 2488 1616 2004 -80 575 156 C ATOM 4665 C MET D 144 -19.007 28.943 62.122 1.00 16.07 C ANISOU 4665 C MET D 144 2566 1614 1926 -169 574 99 C ATOM 4666 O MET D 144 -18.744 29.934 62.813 1.00 16.67 O ANISOU 4666 O MET D 144 2724 1606 2002 -192 645 49 O ATOM 4667 CB MET D 144 -20.284 27.337 63.606 1.00 15.77 C ANISOU 4667 CB MET D 144 2457 1619 1912 -76 613 86 C ATOM 4668 CG MET D 144 -21.665 26.851 64.077 1.00 16.13 C ANISOU 4668 CG MET D 144 2437 1623 2067 12 676 139 C ATOM 4669 SD MET D 144 -21.595 25.563 65.375 1.00 15.80 S ANISOU 4669 SD MET D 144 2418 1645 1939 12 711 74 S ATOM 4670 CE MET D 144 -20.896 26.410 66.786 1.00 16.53 C ANISOU 4670 CE MET D 144 2712 1660 1909 -32 814 -37 C ATOM 4671 N TYR D 145 -18.182 28.486 61.177 1.00 15.50 N ANISOU 4671 N TYR D 145 2473 1618 1797 -221 505 109 N ATOM 4672 CA TYR D 145 -16.815 28.994 61.012 1.00 15.68 C ANISOU 4672 CA TYR D 145 2532 1644 1778 -311 517 60 C ATOM 4673 C TYR D 145 -16.496 29.438 59.578 1.00 16.05 C ANISOU 4673 C TYR D 145 2608 1670 1818 -339 517 124 C ATOM 4674 O TYR D 145 -15.338 29.742 59.259 1.00 16.42 O ANISOU 4674 O TYR D 145 2666 1718 1852 -414 549 99 O ATOM 4675 CB TYR D 145 -15.812 27.910 61.449 1.00 15.04 C ANISOU 4675 CB TYR D 145 2398 1664 1649 -358 474 -2 C ATOM 4676 CG TYR D 145 -15.891 27.539 62.917 1.00 14.91 C ANISOU 4676 CG TYR D 145 2398 1658 1610 -353 462 -69 C ATOM 4677 CD1 TYR D 145 -15.159 28.234 63.883 1.00 15.61 C ANISOU 4677 CD1 TYR D 145 2554 1692 1682 -420 460 -140 C ATOM 4678 CD2 TYR D 145 -16.702 26.502 63.342 1.00 14.37 C ANISOU 4678 CD2 TYR D 145 2296 1636 1525 -290 447 -58 C ATOM 4679 CE1 TYR D 145 -15.242 27.874 65.259 1.00 15.78 C ANISOU 4679 CE1 TYR D 145 2645 1706 1644 -422 438 -200 C ATOM 4680 CE2 TYR D 145 -16.795 26.148 64.710 1.00 14.49 C ANISOU 4680 CE2 TYR D 145 2362 1646 1496 -286 452 -114 C ATOM 4681 CZ TYR D 145 -16.078 26.831 65.654 1.00 15.20 C ANISOU 4681 CZ TYR D 145 2552 1680 1542 -351 447 -184 C ATOM 4682 OH TYR D 145 -16.192 26.437 66.983 1.00 15.52 O ANISOU 4682 OH TYR D 145 2690 1703 1504 -352 443 -236 O ATOM 4683 OXT TYR D 145 -17.353 29.508 58.694 1.00 16.21 O ANISOU 4683 OXT TYR D 145 2648 1660 1848 -292 485 210 O TER 4684 TYR D 145 HETATM 4685 O HOH A 201 -2.299 -6.725 18.402 1.00 9.20 O HETATM 4686 O HOH A 202 -11.963 -11.012 21.717 1.00 5.65 O HETATM 4687 O HOH A 203 1.012 -9.875 22.401 1.00 11.33 O HETATM 4688 O HOH A 204 -13.158 -7.521 27.547 1.00 6.20 O HETATM 4689 O HOH A 205 -1.344 -11.921 39.156 1.00 5.87 O HETATM 4690 O HOH A 206 -20.043 -7.108 26.474 1.00 18.07 O HETATM 4691 O HOH A 207 -18.589 -27.522 36.612 1.00 24.28 O HETATM 4692 O HOH A 208 0.931 -4.284 24.879 1.00 9.16 O HETATM 4693 O HOH A 209 -5.565 1.698 18.363 1.00 23.54 O HETATM 4694 O HOH A 210 1.905 0.337 20.320 1.00 14.85 O HETATM 4695 O HOH A 211 -4.604 -9.935 41.904 1.00 11.15 O HETATM 4696 O HOH A 212 -18.211 -9.865 20.849 1.00 6.45 O HETATM 4697 O HOH A 213 -0.941 -26.282 42.400 1.00 13.53 O HETATM 4698 O HOH A 214 -10.757 -5.160 28.232 1.00 17.47 O HETATM 4699 O HOH A 215 -18.966 -10.386 26.629 1.00 15.20 O HETATM 4700 O HOH A 216 -5.541 -24.020 13.936 1.00 24.91 O HETATM 4701 O HOH A 217 -21.228 -11.391 34.479 1.00 15.74 O HETATM 4702 O HOH A 218 -10.828 -28.242 23.432 1.00 25.62 O HETATM 4703 O HOH A 219 3.618 -26.645 29.399 1.00 17.70 O HETATM 4704 O HOH A 220 -18.012 -22.946 31.494 1.00 23.18 O HETATM 4705 O HOH A 221 6.057 -20.142 30.576 1.00 18.63 O HETATM 4706 O HOH A 222 -11.719 -7.591 37.089 1.00 16.15 O HETATM 4707 O HOH A 223 -20.547 -17.308 20.706 1.00 18.35 O HETATM 4708 O HOH A 224 12.003 -14.874 38.022 1.00 26.48 O HETATM 4709 O HOH A 225 -13.706 -1.998 26.675 1.00 31.63 O HETATM 4710 O HOH A 226 -23.705 -23.529 30.051 1.00 18.82 O HETATM 4711 O HOH A 227 2.669 -15.704 16.258 1.00 17.83 O HETATM 4712 O HOH A 228 -5.158 -8.522 33.623 1.00 17.26 O HETATM 4713 O HOH A 229 -22.919 -16.834 26.314 1.00 12.74 O HETATM 4714 O HOH A 230 -21.381 -17.060 23.529 1.00 13.39 O HETATM 4715 O HOH A 231 1.703 -27.386 25.164 1.00 27.09 O HETATM 4716 O HOH A 232 -26.769 -15.185 19.856 1.00 21.84 O HETATM 4717 O HOH A 233 3.589 -29.861 24.355 1.00 31.86 O HETATM 4718 O HOH A 234 7.696 -18.638 41.014 1.00 25.26 O HETATM 4719 O HOH A 235 -7.064 -8.063 11.887 1.00 21.29 O HETATM 4720 O HOH A 236 -3.345 -11.367 31.143 1.00 23.51 O HETATM 4721 O HOH A 237 -23.449 -8.747 27.380 1.00 14.52 O HETATM 4722 O HOH A 238 5.277 -13.831 36.448 1.00 15.55 O HETATM 4723 O HOH A 239 -6.417 -2.324 14.705 1.00 16.36 O HETATM 4724 O HOH A 240 2.948 -11.512 21.258 1.00 24.98 O HETATM 4725 O HOH A 241 -2.258 -30.855 27.917 1.00 18.16 O HETATM 4726 O HOH A 242 -9.585 -4.768 39.537 1.00 23.42 O HETATM 4727 O HOH A 243 -12.963 -19.954 45.201 1.00 22.56 O HETATM 4728 O HOH A 244 2.132 -14.353 14.027 1.00 25.85 O HETATM 4729 O HOH A 245 -9.472 -6.920 11.418 1.00 28.23 O HETATM 4730 O HOH A 246 1.030 -27.356 27.921 1.00 18.42 O HETATM 4731 O HOH A 247 1.926 -7.381 22.418 1.00 22.46 O HETATM 4732 O HOH A 248 -5.623 -29.492 28.102 1.00 22.01 O HETATM 4733 O HOH A 249 2.998 -5.960 20.074 1.00 28.89 O HETATM 4734 O HOH A 250 7.810 -18.502 29.820 1.00 16.55 O HETATM 4735 O HOH A 251 -7.278 -5.814 41.155 1.00 20.07 O HETATM 4736 O HOH A 252 9.446 -19.536 27.781 1.00 37.88 O HETATM 4737 O HOH A 253 2.616 -6.561 24.608 1.00 24.82 O HETATM 4738 O HOH A 254 -2.320 -4.648 11.179 1.00 16.22 O HETATM 4739 O HOH A 255 -0.754 -26.635 16.730 1.00 24.57 O HETATM 4740 O HOH A 256 6.719 -12.565 32.785 1.00 19.92 O HETATM 4741 O HOH A 257 0.387 -24.693 41.052 1.00 15.65 O HETATM 4742 O HOH A 258 -26.852 -21.109 37.226 1.00 25.49 O HETATM 4743 O HOH A 259 3.115 -25.416 21.435 1.00 22.10 O HETATM 4744 O HOH A 260 -15.008 -28.791 29.353 1.00 20.98 O HETATM 4745 O HOH A 261 -2.439 -27.190 20.928 1.00 20.18 O HETATM 4746 O HOH A 262 12.829 -21.311 41.642 1.00 31.67 O HETATM 4747 O HOH A 263 -17.228 -24.653 16.394 1.00 32.26 O HETATM 4748 O HOH A 264 -6.495 0.493 28.927 1.00 28.54 O HETATM 4749 O HOH A 265 -12.031 -1.783 31.347 1.00 23.87 O HETATM 4750 O HOH A 266 -18.427 -30.326 31.906 1.00 27.54 O HETATM 4751 O HOH A 267 -9.247 3.642 19.440 1.00 22.66 O HETATM 4752 O HOH A 268 -9.187 -15.064 13.410 1.00 20.52 O HETATM 4753 O HOH A 269 -3.364 -25.762 41.552 1.00 25.60 O HETATM 4754 O HOH A 270 -18.039 -22.153 39.537 1.00 20.93 O HETATM 4755 O HOH A 271 1.468 -7.772 34.132 1.00 31.86 O HETATM 4756 O HOH A 272 -28.201 -21.528 29.059 1.00 27.45 O HETATM 4757 O HOH A 273 0.592 -25.798 22.781 1.00 38.54 O HETATM 4758 O HOH A 274 -6.631 -3.438 12.404 1.00 19.95 O HETATM 4759 O HOH A 275 -8.088 -16.401 11.407 1.00 22.15 O HETATM 4760 O HOH A 276 0.122 -5.064 10.965 1.00 26.43 O HETATM 4761 O HOH B 201 -25.370 -7.247 76.567 1.00 11.73 O HETATM 4762 O HOH B 202 -32.048 -14.234 66.689 1.00 11.04 O HETATM 4763 O HOH B 203 -32.779 -11.293 82.274 1.00 11.37 O HETATM 4764 O HOH B 204 -27.076 -8.415 82.702 1.00 8.93 O HETATM 4765 O HOH B 205 -17.607 -9.935 85.929 1.00 18.01 O HETATM 4766 O HOH B 206 -27.561 -27.274 63.981 1.00 14.42 O HETATM 4767 O HOH B 207 -23.117 -23.694 78.052 1.00 18.22 O HETATM 4768 O HOH B 208 -23.086 -14.414 85.745 1.00 9.15 O HETATM 4769 O HOH B 209 -38.495 -15.008 70.696 1.00 11.54 O HETATM 4770 O HOH B 210 -28.203 -1.228 83.271 1.00 23.05 O HETATM 4771 O HOH B 211 -34.649 -8.448 73.795 1.00 13.05 O HETATM 4772 O HOH B 212 -31.694 -9.907 75.643 1.00 3.66 O HETATM 4773 O HOH B 213 -17.685 -22.423 80.064 1.00 16.25 O HETATM 4774 O HOH B 214 -20.397 -5.328 78.870 1.00 17.12 O HETATM 4775 O HOH B 215 -39.925 -17.040 73.631 1.00 21.97 O HETATM 4776 O HOH B 216 -25.501 -10.643 78.198 1.00 13.50 O HETATM 4777 O HOH B 217 -22.134 -14.034 70.722 1.00 16.05 O HETATM 4778 O HOH B 218 -35.407 -30.235 62.495 1.00 14.80 O HETATM 4779 O HOH B 219 -30.748 -0.437 84.079 1.00 24.66 O HETATM 4780 O HOH B 220 -22.019 -14.835 83.137 1.00 10.08 O HETATM 4781 O HOH B 221 -30.086 -26.164 70.556 1.00 38.47 O HETATM 4782 O HOH B 222 -40.616 -21.480 66.705 1.00 11.55 O HETATM 4783 O HOH B 223 -21.434 -8.361 76.415 1.00 13.12 O HETATM 4784 O HOH B 224 -20.432 -15.282 80.580 1.00 10.21 O HETATM 4785 O HOH B 225 -37.035 -8.174 62.202 1.00 17.76 O HETATM 4786 O HOH B 226 -37.567 -29.979 61.278 1.00 26.09 O HETATM 4787 O HOH B 227 -33.548 -6.914 70.058 1.00 23.74 O HETATM 4788 O HOH B 228 -33.548 -5.440 89.966 1.00 22.96 O HETATM 4789 O HOH B 229 -34.430 -13.012 63.384 1.00 29.01 O HETATM 4790 O HOH B 230 -38.105 -20.019 63.549 1.00 17.07 O HETATM 4791 O HOH B 231 -31.436 -15.617 96.019 1.00 16.28 O HETATM 4792 O HOH B 232 -25.418 -7.017 67.007 1.00 24.48 O HETATM 4793 O HOH B 233 -29.108 -18.157 63.404 1.00 21.23 O HETATM 4794 O HOH B 234 -24.811 -10.921 69.445 1.00 26.00 O HETATM 4795 O HOH B 235 -22.037 -11.488 70.007 1.00 20.59 O HETATM 4796 O HOH B 236 -22.260 -25.531 70.299 1.00 26.65 O HETATM 4797 O HOH B 237 -25.703 -7.204 91.045 1.00 31.08 O HETATM 4798 O HOH B 238 -14.846 -14.807 80.966 1.00 37.06 O HETATM 4799 O HOH B 239 -33.446 -10.755 91.839 1.00 19.09 O HETATM 4800 O HOH B 240 -36.395 -26.670 60.722 1.00 27.71 O HETATM 4801 O HOH B 241 -20.362 -8.590 74.026 1.00 18.80 O HETATM 4802 O HOH B 242 -15.749 -9.783 79.445 1.00 23.82 O HETATM 4803 O HOH B 243 -33.842 -17.406 63.300 1.00 31.91 O HETATM 4804 O HOH B 244 -24.483 -2.535 85.536 1.00 32.19 O HETATM 4805 O HOH B 245 -19.756 -14.934 70.286 1.00 23.30 O HETATM 4806 O HOH B 246 -35.550 -12.293 91.402 1.00 27.32 O HETATM 4807 O HOH B 247 -23.792 -2.270 72.063 1.00 26.35 O HETATM 4808 O HOH B 248 -17.593 -19.172 88.414 1.00 24.53 O HETATM 4809 O HOH B 249 -22.159 -10.432 72.575 1.00 19.31 O HETATM 4810 O HOH C 201 -19.755 8.025 36.956 1.00 11.54 O HETATM 4811 O HOH C 202 -25.026 13.363 54.041 1.00 10.24 O HETATM 4812 O HOH C 203 -31.895 3.797 48.384 1.00 18.28 O HETATM 4813 O HOH C 204 -27.580 12.611 55.509 1.00 18.92 O HETATM 4814 O HOH C 205 -12.299 11.968 43.494 1.00 32.79 O HETATM 4815 O HOH C 206 -26.977 4.405 31.217 1.00 22.44 O HETATM 4816 O HOH C 207 -29.707 -2.834 38.487 1.00 20.58 O HETATM 4817 O HOH C 208 -23.478 3.418 33.512 1.00 24.27 O HETATM 4818 O HOH C 209 -17.389 14.100 51.856 1.00 18.01 O HETATM 4819 O HOH C 210 -31.701 -10.486 44.371 1.00 22.38 O HETATM 4820 O HOH C 211 -19.914 10.841 36.872 1.00 24.96 O HETATM 4821 O HOH C 212 -18.718 9.666 47.542 1.00 17.03 O HETATM 4822 O HOH C 213 -29.349 -12.353 44.128 1.00 34.81 O HETATM 4823 O HOH C 214 -27.514 17.704 57.785 1.00 14.11 O HETATM 4824 O HOH C 215 -17.492 3.678 38.699 1.00 23.64 O HETATM 4825 O HOH C 216 -19.599 11.129 50.884 1.00 20.90 O HETATM 4826 O HOH C 217 -26.535 29.295 58.492 1.00 39.95 O HETATM 4827 O HOH C 218 -22.304 10.531 51.866 1.00 17.78 O HETATM 4828 O HOH C 219 -33.009 9.406 37.458 1.00 25.16 O HETATM 4829 O HOH C 220 -23.347 8.546 50.532 1.00 31.27 O HETATM 4830 O HOH C 221 -29.762 30.578 44.621 1.00 24.60 O HETATM 4831 O HOH C 222 -26.662 -10.959 45.184 1.00 29.90 O HETATM 4832 O HOH C 223 -29.611 8.414 53.016 1.00 20.44 O HETATM 4833 O HOH C 224 -33.998 5.001 49.671 1.00 27.21 O HETATM 4834 O HOH C 225 -23.970 12.638 36.990 1.00 33.69 O HETATM 4835 O HOH C 226 -25.355 2.970 32.197 1.00 33.12 O HETATM 4836 O HOH C 227 -13.738 14.283 44.270 1.00 26.01 O HETATM 4837 O HOH C 228 -13.714 15.999 41.936 1.00 20.83 O HETATM 4838 O HOH D 201 -23.699 23.772 57.458 1.00 26.29 O HETATM 4839 O HOH D 202 -15.101 25.220 74.346 1.00 22.51 O HETATM 4840 O HOH D 203 -0.253 -4.876 64.565 1.00 18.53 O HETATM 4841 O HOH D 204 -20.486 12.457 54.925 1.00 18.02 O HETATM 4842 O HOH D 205 0.145 -7.794 64.336 1.00 24.88 O HETATM 4843 O HOH D 206 -13.938 0.818 56.575 1.00 16.94 O HETATM 4844 O HOH D 207 -14.269 -2.718 54.551 1.00 32.77 O HETATM 4845 O HOH D 208 -22.914 -3.787 70.110 1.00 21.12 O HETATM 4846 O HOH D 209 -26.153 -9.619 67.219 1.00 14.06 O HETATM 4847 O HOH D 210 -25.536 -10.113 64.382 1.00 14.47 O HETATM 4848 O HOH D 211 -19.423 5.098 53.313 1.00 30.08 O HETATM 4849 O HOH D 212 -20.496 22.201 54.696 1.00 24.81 O HETATM 4850 O HOH D 213 -17.819 26.024 68.940 1.00 17.84 O HETATM 4851 O HOH D 214 -20.001 -10.570 68.334 1.00 14.58 O HETATM 4852 O HOH D 215 -9.046 26.229 66.835 1.00 21.38 O HETATM 4853 O HOH D 216 -13.569 -11.213 59.305 1.00 37.83 O HETATM 4854 O HOH D 217 -19.458 30.932 59.284 1.00 12.22 O HETATM 4855 O HOH D 218 -12.730 1.577 69.523 1.00 16.61 O HETATM 4856 O HOH D 219 -27.165 6.190 59.757 1.00 19.35 O HETATM 4857 O HOH D 220 -17.307 26.984 75.055 1.00 23.20 O HETATM 4858 O HOH D 221 -8.273 23.704 69.320 1.00 27.34 O HETATM 4859 O HOH D 222 -9.197 17.136 73.636 1.00 27.16 O HETATM 4860 O HOH D 223 -17.632 16.894 52.523 1.00 10.83 O HETATM 4861 O HOH D 224 -21.900 5.262 70.692 1.00 25.87 O HETATM 4862 O HOH D 225 -6.289 -11.607 58.449 1.00 27.80 O HETATM 4863 O HOH D 226 -12.198 -8.668 70.283 1.00 26.33 O HETATM 4864 O HOH D 227 -32.690 3.566 66.694 1.00 16.20 O HETATM 4865 O HOH D 228 -11.185 8.671 73.347 1.00 27.38 O HETATM 4866 O HOH D 229 -25.949 1.038 68.883 1.00 20.27 O HETATM 4867 O HOH D 230 -0.796 -6.474 51.021 1.00 33.56 O HETATM 4868 O HOH D 231 -17.899 26.615 72.193 1.00 31.86 O HETATM 4869 O HOH D 232 -15.563 28.059 72.095 1.00 26.51 O HETATM 4870 O HOH D 233 -9.416 8.175 71.941 1.00 30.30 O HETATM 4871 O HOH D 234 -10.004 -2.789 71.548 1.00 27.65 O HETATM 4872 O HOH D 235 -12.164 4.319 70.082 1.00 28.74 O HETATM 4873 O HOH D 236 -7.789 18.372 66.820 1.00 43.09 O HETATM 4874 O HOH D 237 -16.236 7.362 54.226 1.00 16.73 O HETATM 4875 O HOH D 238 -9.721 5.314 70.408 1.00 26.06 O HETATM 4876 O HOH D 239 -24.209 30.380 59.118 1.00 27.22 O HETATM 4877 O HOH D 240 -1.499 -1.210 67.220 1.00 22.69 O HETATM 4878 O HOH D 241 -12.782 27.249 71.303 1.00 25.70 O HETATM 4879 O HOH D 242 -4.285 -15.968 60.610 1.00 28.63 O HETATM 4880 O HOH D 243 -13.599 19.536 72.547 1.00 24.65 O HETATM 4881 O HOH D 244 -12.545 -14.865 64.179 1.00 32.04 O HETATM 4882 O HOH D 245 2.135 -0.106 63.888 1.00 31.68 O HETATM 4883 O HOH D 246 -25.796 -1.173 71.121 1.00 23.85 O HETATM 4884 O HOH D 247 -11.580 29.142 70.033 1.00 22.29 O CONECT 389 532 CONECT 532 389 CONECT 1643 1786 CONECT 1786 1643 MASTER 403 0 0 21 18 0 0 6 4880 4 4 50 END
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Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
4dge
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
TRIMCyp
Ligand Name
capsid protein
EC.Number
E.C.5.2.1.8
Resolution
2.2(Å)
Affinity (Kd/Ki/IC50)
Kd=38.5uM
Release Year
2012
Protein/NA Sequence
Check fasta file
Primary Reference
(2012) Nat.Struct.Mol.Biol. Vol. 19: pp. 411-416
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
P62940
P12497
Entrez Gene ID
NCBI Entrez Gene ID:
574102
ASD
Information of known allosteric effects of PDB entries
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