HEADER MEMBRANE PROTEIN 15-MAY-15 4ZUD TITLE CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN RECEPTOR IN COMPLEX WITH TITLE 2 INVERSE AGONIST OLMESARTAN AT 2.8A RESOLUTION. COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHIMERA PROTEIN OF SOLUBLE CYTOCHROME B562 AND TYPE-1 COMPND 3 ANGIOTENSIN II RECEPTOR; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: CYTOCHROME B-562,AT1AR,AT1BR,ANGIOTENSIN II TYPE-1 RECEPTOR, COMPND 6 AT1,AT1AR,AT1BR,ANGIOTENSIN II TYPE-1 RECEPTOR,AT1; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI, HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 562, 9606; SOURCE 5 GENE: CYBC, AGTR1, AGTR1A, AGTR1B, AT2R1, AT2R1B; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF9; SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF9; SOURCE 10 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1711; SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PFASTBAC KEYWDS HUMAN ANGIOTENSIN RECEPTOR AT1R, BRIL, G PROTEIN-COUPLED RECEPTOR, KEYWDS 2 GPCR, GPCR NETWORK, LIPIDIC CUBIC PHASE, LCP, MEMBRANE PROTEIN, KEYWDS 3 STRUCTURAL GENOMICS, OLMESARTAN, ANGIOTENSIN RECEPTOR BLOCKER, ANTI- KEYWDS 4 HYPERTENSIVE DRUG, PSI-BIOLOGY, SIGNALING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR H.ZHANG,H.UNAL,R.DESNOYER,G.W.HAN,N.PATEL,V.KATRITCH,S.S.KARNIK, AUTHOR 2 V.CHEREZOV,R.C.STEVENS,GPCR NETWORK (GPCR) REVDAT 5 25-DEC-19 4ZUD 1 REMARK REVDAT 4 20-SEP-17 4ZUD 1 JRNL REMARK REVDAT 3 16-DEC-15 4ZUD 1 JRNL REVDAT 2 14-OCT-15 4ZUD 1 JRNL REVDAT 1 07-OCT-15 4ZUD 0 JRNL AUTH H.ZHANG,H.UNAL,R.DESNOYER,G.W.HAN,N.PATEL,V.KATRITCH, JRNL AUTH 2 S.S.KARNIK,V.CHEREZOV,R.C.STEVENS JRNL TITL STRUCTURAL BASIS FOR LIGAND RECOGNITION AND FUNCTIONAL JRNL TITL 2 SELECTIVITY AT ANGIOTENSIN RECEPTOR. JRNL REF J.BIOL.CHEM. V. 290 29127 2015 JRNL REFN ESSN 1083-351X JRNL PMID 26420482 JRNL DOI 10.1074/JBC.M115.689000 REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0103 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.68 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 94.0 REMARK 3 NUMBER OF REFLECTIONS : 10472 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) : 0.196 REMARK 3 R VALUE (WORKING SET) : 0.194 REMARK 3 FREE R VALUE : 0.235 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 555 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) : 2.80 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87 REMARK 3 REFLECTION IN BIN (WORKING SET) : 699 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.00 REMARK 3 BIN R VALUE (WORKING SET) : 0.2140 REMARK 3 BIN FREE R VALUE SET COUNT : 32 REMARK 3 BIN FREE R VALUE : 0.2750 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2918 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 33 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 84.96 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 28.35000 REMARK 3 B22 (A**2) : 28.35000 REMARK 3 B33 (A**2) : -56.69000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.077 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.210 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.583 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.904 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3021 ; 0.009 ; 0.020 REMARK 3 BOND LENGTHS OTHERS (A): 2941 ; 0.002 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4123 ; 1.133 ; 1.977 REMARK 3 BOND ANGLES OTHERS (DEGREES): 6718 ; 0.959 ; 3.002 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 372 ; 5.909 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 114 ;36.193 ;24.123 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 483 ;15.165 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;11.716 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 496 ; 0.059 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3342 ; 0.005 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): 687 ; 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): 1500 ; 1.525 ; 7.615 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1499 ; 1.525 ; 7.616 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1868 ; 2.658 ;11.416 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1869 ; 2.657 ;11.415 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1521 ; 1.087 ; 7.569 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1522 ; 1.087 ; 7.569 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2256 ; 1.895 ;11.333 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3512 ; 4.431 ;61.062 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3513 ; 4.430 ;61.065 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TWIN DETAILS REMARK 3 NUMBER OF TWIN DOMAINS : 2 REMARK 3 TWIN DOMAIN : 1 REMARK 3 TWIN OPERATOR : H, K, L REMARK 3 TWIN FRACTION : 0.575 REMARK 3 TWIN DOMAIN : 2 REMARK 3 TWIN OPERATOR : K, H, -L REMARK 3 TWIN FRACTION : 0.425 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 1002 A 1106 REMARK 3 ORIGIN FOR THE GROUP (A): -23.1608 72.6878 1.7663 REMARK 3 T TENSOR REMARK 3 T11: 0.0322 T22: 0.1081 REMARK 3 T33: 0.1438 T12: 0.0020 REMARK 3 T13: 0.0122 T23: 0.0147 REMARK 3 L TENSOR REMARK 3 L11: 0.0882 L22: 2.3768 REMARK 3 L33: 1.3014 L12: -0.2408 REMARK 3 L13: 0.3200 L23: -1.1785 REMARK 3 S TENSOR REMARK 3 S11: -0.0416 S12: 0.0249 S13: -0.0036 REMARK 3 S21: 0.0387 S22: -0.0445 S23: -0.1056 REMARK 3 S31: -0.1349 S32: 0.0366 S33: 0.0861 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 : A 12 A 304 REMARK 3 ORIGIN FOR THE GROUP (A): -40.6152 63.6571 36.7014 REMARK 3 T TENSOR REMARK 3 T11: 0.0391 T22: 0.1011 REMARK 3 T33: 0.1645 T12: 0.0157 REMARK 3 T13: 0.0372 T23: -0.0374 REMARK 3 L TENSOR REMARK 3 L11: 0.5899 L22: 0.0501 REMARK 3 L33: 1.3307 L12: 0.0982 REMARK 3 L13: -0.0189 L23: 0.1341 REMARK 3 S TENSOR REMARK 3 S11: 0.0267 S12: -0.0972 S13: 0.0322 REMARK 3 S21: -0.0021 S22: -0.0328 S23: -0.0151 REMARK 3 S31: 0.1226 S32: 0.1041 S33: 0.0061 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 4ZUD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAY-15. REMARK 100 THE DEPOSITION ID IS D_1000209879. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 31-DEC-14 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.0 REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0330 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11028 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 35.680 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0 REMARK 200 DATA REDUNDANCY : 2.360 REMARK 200 R MERGE (I) : 0.05400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.0500 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.87 REMARK 200 COMPLETENESS FOR SHELL (%) : 85.3 REMARK 200 DATA REDUNDANCY IN SHELL : 2.09 REMARK 200 R MERGE FOR SHELL (I) : 0.75800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.170 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 4YAY REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.54 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CITRATE, PH 5.0, 400 MM REMARK 280 KH2PO4, 25% (V/V) PEG400, AND 6% (V/V) DMSO, LIPIDIC CUBIC PHASE, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 167.44000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 83.72000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT IS UNKNOWN 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ALA A 1001 REMARK 465 MET A 134 REMARK 465 LYS A 135 REMARK 465 SER A 136 REMARK 465 ARG A 137 REMARK 465 LEU A 138 REMARK 465 ARG A 139 REMARK 465 ARG A 140 REMARK 465 SER A 186 REMARK 465 GLN A 187 REMARK 465 ASN A 188 REMARK 465 LYS A 223 REMARK 465 LYS A 224 REMARK 465 ALA A 225 REMARK 465 TYR A 226 REMARK 465 GLU A 227 REMARK 465 ILE A 228 REMARK 465 GLN A 229 REMARK 465 LYS A 230 REMARK 465 ASN A 231 REMARK 465 LYS A 232 REMARK 465 PRO A 233 REMARK 465 ARG A 234 REMARK 465 LEU A 305 REMARK 465 GLY A 306 REMARK 465 LYS A 307 REMARK 465 LYS A 308 REMARK 465 PHE A 309 REMARK 465 LYS A 310 REMARK 465 ARG A 311 REMARK 465 TYR A 312 REMARK 465 PHE A 313 REMARK 465 LEU A 314 REMARK 465 GLN A 315 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ILE A 53 CG1 CG2 CD1 REMARK 470 TYR A 54 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR A 56 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 MET A 57 CG SD CE REMARK 470 LYS A 58 CG CD CE NZ REMARK 470 LYS A 60 CG CD CE NZ REMARK 470 GLU A 173 CG CD OE1 OE2 REMARK 470 GLU A 185 CG CD OE1 OE2 REMARK 470 LEU A 202 CG CD1 CD2 REMARK 470 PHE A 204 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PHE A 206 CG CD1 CD2 CE1 CE2 CZ REMARK 470 TRP A 219 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 219 CZ3 CH2 REMARK 470 LYS A 220 CG CD CE NZ REMARK 470 ASN A 235 CG OD1 ND2 REMARK 470 ASP A 236 CG OD1 OD2 REMARK 470 LYS A 240 CG CD CE NZ REMARK 470 LEU A 268 CG CD1 CD2 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 ASP A1021 -60.12 -121.37 REMARK 500 LEU A1048 68.85 -114.19 REMARK 500 ASP A1050 45.63 -99.29 REMARK 500 PHE A 39 -74.15 -58.49 REMARK 500 PHE A 55 -76.24 -75.32 REMARK 500 TYR A 92 73.00 55.71 REMARK 500 ILE A 130 16.11 -140.57 REMARK 500 PHE A 204 -77.88 -81.05 REMARK 500 ASP A 273 119.03 -36.41 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLM A 1201 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: GPCR-11 RELATED DB: TARGETTRACK REMARK 900 AT1R IS A COMMUNITY TARGET. DBREF 4ZUD A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 4ZUD A 12 16 UNP P30556 AGTR1_HUMAN 2 6 DBREF 4ZUD A 17 315 UNP P30556 AGTR1_HUMAN 17 315 SEQADV 4ZUD TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 4ZUD ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 4ZUD LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQRES 1 A 410 ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN SEQRES 2 A 410 LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL SEQRES 3 A 410 LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP SEQRES 4 A 410 ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER SEQRES 5 A 410 PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE SEQRES 6 A 410 ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU SEQRES 7 A 410 ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA SEQRES 8 A 410 GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS SEQRES 9 A 410 TYR LEU ILE LEU ASN SER SER ASP CYS PRO LYS ALA GLY SEQRES 10 A 410 ARG HIS ASN TYR ILE PHE VAL MET ILE PRO THR LEU TYR SEQRES 11 A 410 SER ILE ILE PHE VAL VAL GLY ILE PHE GLY ASN SER LEU SEQRES 12 A 410 VAL VAL ILE VAL ILE TYR PHE TYR MET LYS LEU LYS THR SEQRES 13 A 410 VAL ALA SER VAL PHE LEU LEU ASN LEU ALA LEU ALA ASP SEQRES 14 A 410 LEU CYS PHE LEU LEU THR LEU PRO LEU TRP ALA VAL TYR SEQRES 15 A 410 THR ALA MET GLU TYR ARG TRP PRO PHE GLY ASN TYR LEU SEQRES 16 A 410 CYS LYS ILE ALA SER ALA SER VAL SER PHE ASN LEU TYR SEQRES 17 A 410 ALA SER VAL PHE LEU LEU THR CYS LEU SER ILE ASP ARG SEQRES 18 A 410 TYR LEU ALA ILE VAL HIS PRO MET LYS SER ARG LEU ARG SEQRES 19 A 410 ARG THR MET LEU VAL ALA LYS VAL THR CYS ILE ILE ILE SEQRES 20 A 410 TRP LEU LEU ALA GLY LEU ALA SER LEU PRO ALA ILE ILE SEQRES 21 A 410 HIS ARG ASN VAL PHE PHE ILE GLU ASN THR ASN ILE THR SEQRES 22 A 410 VAL CYS ALA PHE HIS TYR GLU SER GLN ASN SER THR LEU SEQRES 23 A 410 PRO ILE GLY LEU GLY LEU THR LYS ASN ILE LEU GLY PHE SEQRES 24 A 410 LEU PHE PRO PHE LEU ILE ILE LEU THR SER TYR THR LEU SEQRES 25 A 410 ILE TRP LYS ALA LEU LYS LYS ALA TYR GLU ILE GLN LYS SEQRES 26 A 410 ASN LYS PRO ARG ASN ASP ASP ILE PHE LYS ILE ILE MET SEQRES 27 A 410 ALA ILE VAL LEU PHE PHE PHE PHE SER TRP ILE PRO HIS SEQRES 28 A 410 GLN ILE PHE THR PHE LEU ASP VAL LEU ILE GLN LEU GLY SEQRES 29 A 410 ILE ILE ARG ASP CYS ARG ILE ALA ASP ILE VAL ASP THR SEQRES 30 A 410 ALA MET PRO ILE THR ILE CYS ILE ALA TYR PHE ASN ASN SEQRES 31 A 410 CYS LEU ASN PRO LEU PHE TYR GLY PHE LEU GLY LYS LYS SEQRES 32 A 410 PHE LYS ARG TYR PHE LEU GLN HET OLM A1201 33 HETNAM OLM OLMESARTAN FORMUL 2 OLM C24 H26 N6 O3 HELIX 1 AA1 ASP A 1002 LYS A 1019 1 18 HELIX 2 AA2 ASN A 1022 LYS A 1042 1 21 HELIX 3 AA3 SER A 1055 GLY A 1082 1 28 HELIX 4 AA4 LYS A 1083 ALA A 1091 1 9 HELIX 5 AA5 GLN A 1093 LEU A 1106 1 14 HELIX 6 AA6 TYR A 26 TYR A 56 1 31 HELIX 7 AA7 THR A 61 LEU A 81 1 21 HELIX 8 AA8 LEU A 81 MET A 90 1 10 HELIX 9 AA9 GLY A 97 HIS A 132 1 36 HELIX 10 AB1 MET A 142 SER A 160 1 19 HELIX 11 AB2 SER A 160 HIS A 166 1 7 HELIX 12 AB3 THR A 190 LEU A 195 1 6 HELIX 13 AB4 LEU A 197 PHE A 204 1 8 HELIX 14 AB5 PHE A 204 LEU A 222 1 19 HELIX 15 AB6 ASP A 236 LEU A 268 1 33 HELIX 16 AB7 ASP A 273 PHE A 293 1 21 HELIX 17 AB8 PHE A 293 PHE A 304 1 12 SHEET 1 AA1 3 ILE A 12 LEU A 13 0 SHEET 2 AA1 3 ARG A 167 ILE A 172 1 O PHE A 171 N LEU A 13 SHEET 3 AA1 3 THR A 178 PHE A 182 -1 O VAL A 179 N PHE A 170 SSBOND 1 CYS A 18 CYS A 274 1555 1555 2.04 SSBOND 2 CYS A 101 CYS A 180 1555 1555 2.04 SITE 1 AC1 8 TYR A 35 TRP A 84 SER A 105 VAL A 108 SITE 2 AC1 8 SER A 109 ARG A 167 PHE A 182 ILE A 288 CRYST1 41.200 41.200 251.160 90.00 90.00 120.00 P 32 3 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 0.024272 0.014013 0.000000 0.00000 SCALE2 0.000000 0.028027 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003982 0.00000 ATOM 1 N ASP A1002 -22.258 72.417 16.227 1.00106.94 N ANISOU 1 N ASP A1002 14045 13055 13531 96 -235 170 N ATOM 2 CA ASP A1002 -23.686 72.797 15.981 1.00106.79 C ANISOU 2 CA ASP A1002 14040 13067 13467 201 -86 150 C ATOM 3 C ASP A1002 -24.094 72.507 14.530 1.00104.08 C ANISOU 3 C ASP A1002 13468 12847 13229 196 -15 146 C ATOM 4 O ASP A1002 -23.865 73.325 13.638 1.00104.02 O ANISOU 4 O ASP A1002 13420 12856 13245 169 -50 147 O ATOM 5 CB ASP A1002 -23.917 74.278 16.323 1.00108.46 C ANISOU 5 CB ASP A1002 14460 13181 13567 242 -112 148 C ATOM 6 CG ASP A1002 -23.685 74.590 17.799 1.00110.68 C ANISOU 6 CG ASP A1002 15020 13318 13715 264 -174 151 C ATOM 7 OD1 ASP A1002 -23.153 73.722 18.526 1.00112.70 O ANISOU 7 OD1 ASP A1002 15297 13547 13974 227 -225 157 O ATOM 8 OD2 ASP A1002 -24.037 75.711 18.237 1.00109.58 O ANISOU 8 OD2 ASP A1002 15096 13081 13456 322 -174 148 O ATOM 9 N LEU A1003 -24.702 71.341 14.311 1.00101.69 N ANISOU 9 N LEU A1003 13033 12621 12983 218 74 143 N ATOM 10 CA LEU A1003 -25.056 70.873 12.961 1.00 99.52 C ANISOU 10 CA LEU A1003 12562 12448 12802 205 121 140 C ATOM 11 C LEU A1003 -26.316 71.538 12.390 1.00 98.22 C ANISOU 11 C LEU A1003 12375 12312 12629 273 210 144 C ATOM 12 O LEU A1003 -26.399 71.754 11.183 1.00 97.42 O ANISOU 12 O LEU A1003 12169 12263 12581 251 206 140 O ATOM 13 CB LEU A1003 -25.202 69.342 12.949 1.00 97.97 C ANISOU 13 CB LEU A1003 12252 12307 12665 193 161 141 C ATOM 14 CG LEU A1003 -25.424 68.616 11.611 1.00 96.58 C ANISOU 14 CG LEU A1003 11903 12216 12575 169 187 138 C ATOM 15 CD1 LEU A1003 -24.425 69.045 10.543 1.00 95.66 C ANISOU 15 CD1 LEU A1003 11730 12117 12498 115 123 135 C ATOM 16 CD2 LEU A1003 -25.368 67.107 11.818 1.00 95.67 C ANISOU 16 CD2 LEU A1003 11721 12128 12499 152 202 140 C ATOM 17 N GLU A1004 -27.292 71.850 13.245 1.00 99.30 N ANISOU 17 N GLU A1004 12613 12412 12704 360 294 158 N ATOM 18 CA GLU A1004 -28.504 72.568 12.813 1.00 98.11 C ANISOU 18 CA GLU A1004 12443 12281 12552 438 382 178 C ATOM 19 C GLU A1004 -28.188 73.996 12.357 1.00 98.37 C ANISOU 19 C GLU A1004 12560 12274 12540 437 328 164 C ATOM 20 O GLU A1004 -28.762 74.474 11.375 1.00 97.22 O ANISOU 20 O GLU A1004 12332 12171 12434 453 352 171 O ATOM 21 CB GLU A1004 -29.554 72.598 13.929 1.00 97.74 C ANISOU 21 CB GLU A1004 12493 12194 12447 549 504 213 C ATOM 22 CG GLU A1004 -30.929 73.076 13.477 1.00 97.41 C ANISOU 22 CG GLU A1004 12380 12189 12439 638 615 258 C ATOM 23 CD GLU A1004 -32.025 72.788 14.491 1.00 96.05 C ANISOU 23 CD GLU A1004 12248 11999 12246 750 763 317 C ATOM 24 OE1 GLU A1004 -31.829 73.081 15.687 1.00 94.89 O ANISOU 24 OE1 GLU A1004 12302 11764 11987 808 796 313 O ATOM 25 OE2 GLU A1004 -33.090 72.275 14.088 1.00 95.24 O ANISOU 25 OE2 GLU A1004 11980 11964 12240 779 845 376 O ATOM 26 N ASP A1005 -27.278 74.658 13.076 1.00100.41 N ANISOU 26 N ASP A1005 12990 12443 12717 413 243 150 N ATOM 27 CA ASP A1005 -26.828 76.021 12.747 1.00101.78 C ANISOU 27 CA ASP A1005 13268 12563 12841 396 167 141 C ATOM 28 C ASP A1005 -26.091 76.081 11.402 1.00100.55 C ANISOU 28 C ASP A1005 12961 12470 12773 303 93 134 C ATOM 29 O ASP A1005 -26.219 77.070 10.673 1.00100.35 O ANISOU 29 O ASP A1005 12945 12442 12739 306 78 132 O ATOM 30 CB ASP A1005 -25.932 76.577 13.871 1.00104.66 C ANISOU 30 CB ASP A1005 13856 12804 13103 370 62 137 C ATOM 31 CG ASP A1005 -25.654 78.084 13.742 1.00108.08 C ANISOU 31 CG ASP A1005 14446 13157 13463 366 -13 135 C ATOM 32 OD1 ASP A1005 -26.393 78.801 13.029 1.00110.64 O ANISOU 32 OD1 ASP A1005 14743 13507 13787 420 47 133 O ATOM 33 OD2 ASP A1005 -24.689 78.558 14.382 1.00107.25 O ANISOU 33 OD2 ASP A1005 14500 12951 13297 305 -147 139 O ATOM 34 N ASN A1006 -25.331 75.030 11.077 1.00 97.86 N ANISOU 34 N ASN A1006 12490 12180 12509 228 55 134 N ATOM 35 CA ASN A1006 -24.645 74.929 9.777 1.00 93.67 C ANISOU 35 CA ASN A1006 11818 11710 12062 157 14 136 C ATOM 36 C ASN A1006 -25.632 74.941 8.613 1.00 90.69 C ANISOU 36 C ASN A1006 11333 11401 11723 192 88 129 C ATOM 37 O ASN A1006 -25.458 75.701 7.664 1.00 92.26 O ANISOU 37 O ASN A1006 11511 11609 11932 170 62 129 O ATOM 38 CB ASN A1006 -23.787 73.658 9.691 1.00 93.35 C ANISOU 38 CB ASN A1006 11666 11709 12093 98 -10 144 C ATOM 39 CG ASN A1006 -22.637 73.644 10.686 1.00 94.40 C ANISOU 39 CG ASN A1006 11880 11775 12210 44 -110 164 C ATOM 40 OD1 ASN A1006 -22.346 72.611 11.287 1.00 95.61 O ANISOU 40 OD1 ASN A1006 12010 11932 12384 34 -113 168 O ATOM 41 ND2 ASN A1006 -21.971 74.782 10.858 1.00 94.30 N ANISOU 41 ND2 ASN A1006 11968 11696 12166 4 -206 183 N ATOM 42 N TRP A1007 -26.668 74.109 8.699 1.00 87.09 N ANISOU 42 N TRP A1007 10810 10986 11290 241 170 132 N ATOM 43 CA TRP A1007 -27.739 74.099 7.692 1.00 83.99 C ANISOU 43 CA TRP A1007 10321 10647 10941 272 223 139 C ATOM 44 C TRP A1007 -28.494 75.425 7.628 1.00 83.73 C ANISOU 44 C TRP A1007 10363 10584 10864 336 248 147 C ATOM 45 O TRP A1007 -28.878 75.856 6.543 1.00 83.67 O ANISOU 45 O TRP A1007 10298 10604 10885 333 243 149 O ATOM 46 CB TRP A1007 -28.707 72.931 7.921 1.00 81.99 C ANISOU 46 CB TRP A1007 9982 10435 10734 303 291 159 C ATOM 47 CG TRP A1007 -28.088 71.622 7.574 1.00 80.77 C ANISOU 47 CG TRP A1007 9742 10316 10629 240 263 149 C ATOM 48 CD1 TRP A1007 -27.728 70.631 8.436 1.00 80.73 C ANISOU 48 CD1 TRP A1007 9742 10305 10625 228 268 148 C ATOM 49 CD2 TRP A1007 -27.719 71.173 6.265 1.00 79.19 C ANISOU 49 CD2 TRP A1007 9460 10153 10475 189 229 137 C ATOM 50 NE1 TRP A1007 -27.171 69.582 7.745 1.00 80.71 N ANISOU 50 NE1 TRP A1007 9659 10336 10670 175 240 138 N ATOM 51 CE2 TRP A1007 -27.152 69.890 6.409 1.00 79.81 C ANISOU 51 CE2 TRP A1007 9497 10245 10579 154 221 132 C ATOM 52 CE3 TRP A1007 -27.817 71.730 4.981 1.00 79.77 C ANISOU 52 CE3 TRP A1007 9506 10241 10561 174 208 133 C ATOM 53 CZ2 TRP A1007 -26.685 69.147 5.314 1.00 78.80 C ANISOU 53 CZ2 TRP A1007 9314 10142 10484 116 201 123 C ATOM 54 CZ3 TRP A1007 -27.349 70.992 3.890 1.00 78.69 C ANISOU 54 CZ3 TRP A1007 9318 10126 10453 131 187 123 C ATOM 55 CH2 TRP A1007 -26.792 69.714 4.068 1.00 77.95 C ANISOU 55 CH2 TRP A1007 9195 10042 10379 107 188 118 C ATOM 56 N GLU A1008 -28.694 76.065 8.781 1.00 84.78 N ANISOU 56 N GLU A1008 10640 10652 10920 397 274 154 N ATOM 57 CA GLU A1008 -29.242 77.430 8.835 1.00 85.89 C ANISOU 57 CA GLU A1008 10891 10744 10998 467 295 160 C ATOM 58 C GLU A1008 -28.311 78.443 8.165 1.00 85.42 C ANISOU 58 C GLU A1008 10886 10654 10913 403 196 139 C ATOM 59 O GLU A1008 -28.775 79.313 7.442 1.00 86.42 O ANISOU 59 O GLU A1008 11016 10783 11036 429 201 141 O ATOM 60 CB GLU A1008 -29.529 77.868 10.282 1.00 88.74 C ANISOU 60 CB GLU A1008 11437 11020 11257 554 344 171 C ATOM 61 CG GLU A1008 -30.897 77.455 10.809 1.00 89.92 C ANISOU 61 CG GLU A1008 11551 11190 11423 666 486 216 C ATOM 62 CD GLU A1008 -31.995 78.444 10.445 1.00 91.76 C ANISOU 62 CD GLU A1008 11793 11419 11652 767 561 249 C ATOM 63 OE1 GLU A1008 -32.809 78.779 11.331 1.00 94.31 O ANISOU 63 OE1 GLU A1008 12215 11697 11921 891 675 288 O ATOM 64 OE2 GLU A1008 -32.043 78.898 9.280 1.00 92.34 O ANISOU 64 OE2 GLU A1008 11782 11530 11773 730 514 242 O ATOM 65 N THR A1009 -27.007 78.328 8.408 1.00 85.37 N ANISOU 65 N THR A1009 10918 10620 10899 317 103 128 N ATOM 66 CA THR A1009 -26.013 79.187 7.762 1.00 85.73 C ANISOU 66 CA THR A1009 10990 10641 10941 241 6 127 C ATOM 67 C THR A1009 -26.012 79.002 6.237 1.00 85.23 C ANISOU 67 C THR A1009 10772 10655 10955 203 15 125 C ATOM 68 O THR A1009 -25.973 79.989 5.494 1.00 83.32 O ANISOU 68 O THR A1009 10556 10400 10699 193 -13 126 O ATOM 69 CB THR A1009 -24.595 78.926 8.323 1.00 86.90 C ANISOU 69 CB THR A1009 11170 10750 11096 151 -96 140 C ATOM 70 OG1 THR A1009 -24.595 79.154 9.735 1.00 87.69 O ANISOU 70 OG1 THR A1009 11449 10760 11109 183 -122 140 O ATOM 71 CG2 THR A1009 -23.551 79.835 7.668 1.00 87.55 C ANISOU 71 CG2 THR A1009 11264 10807 11193 66 -197 161 C ATOM 72 N LEU A1010 -26.064 77.748 5.785 1.00 84.61 N ANISOU 72 N LEU A1010 10555 10645 10947 185 51 124 N ATOM 73 CA LEU A1010 -26.076 77.435 4.349 1.00 86.36 C ANISOU 73 CA LEU A1010 10661 10926 11226 155 61 122 C ATOM 74 C LEU A1010 -27.359 77.911 3.685 1.00 87.78 C ANISOU 74 C LEU A1010 10825 11122 11404 212 101 120 C ATOM 75 O LEU A1010 -27.308 78.671 2.718 1.00 88.40 O ANISOU 75 O LEU A1010 10909 11199 11478 197 77 118 O ATOM 76 CB LEU A1010 -25.908 75.933 4.104 1.00 85.17 C ANISOU 76 CB LEU A1010 10399 10826 11134 132 87 121 C ATOM 77 CG LEU A1010 -24.575 75.311 4.517 1.00 84.49 C ANISOU 77 CG LEU A1010 10295 10734 11072 76 51 132 C ATOM 78 CD1 LEU A1010 -24.655 73.795 4.423 1.00 84.57 C ANISOU 78 CD1 LEU A1010 10217 10787 11126 75 89 128 C ATOM 79 CD2 LEU A1010 -23.434 75.848 3.671 1.00 83.89 C ANISOU 79 CD2 LEU A1010 10198 10656 11019 19 10 154 C ATOM 80 N ASN A1011 -28.498 77.472 4.220 1.00 89.12 N ANISOU 80 N ASN A1011 10972 11304 11583 277 161 131 N ATOM 81 CA ASN A1011 -29.819 77.860 3.700 1.00 90.54 C ANISOU 81 CA ASN A1011 11116 11500 11783 338 199 151 C ATOM 82 C ASN A1011 -30.045 79.376 3.663 1.00 92.49 C ANISOU 82 C ASN A1011 11467 11700 11973 382 191 152 C ATOM 83 O ASN A1011 -30.698 79.876 2.749 1.00 93.44 O ANISOU 83 O ASN A1011 11554 11834 12115 400 186 162 O ATOM 84 CB ASN A1011 -30.944 77.196 4.509 1.00 90.78 C ANISOU 84 CB ASN A1011 11101 11547 11844 406 274 186 C ATOM 85 CG ASN A1011 -30.989 75.684 4.338 1.00 89.78 C ANISOU 85 CG ASN A1011 10862 11467 11782 361 275 193 C ATOM 86 OD1 ASN A1011 -30.209 75.099 3.583 1.00 89.66 O ANISOU 86 OD1 ASN A1011 10811 11470 11784 289 226 168 O ATOM 87 ND2 ASN A1011 -31.904 75.041 5.052 1.00 88.73 N ANISOU 87 ND2 ASN A1011 10679 11348 11683 409 338 233 N ATOM 88 N ASP A1012 -29.506 80.094 4.650 1.00 95.37 N ANISOU 88 N ASP A1012 11971 12003 12262 399 178 143 N ATOM 89 CA ASP A1012 -29.559 81.562 4.675 1.00 97.69 C ANISOU 89 CA ASP A1012 12397 12234 12485 435 156 140 C ATOM 90 C ASP A1012 -28.628 82.181 3.632 1.00 99.26 C ANISOU 90 C ASP A1012 12599 12429 12684 349 71 124 C ATOM 91 O ASP A1012 -29.033 83.091 2.912 1.00102.27 O ANISOU 91 O ASP A1012 13005 12800 13051 370 62 125 O ATOM 92 CB ASP A1012 -29.218 82.112 6.067 1.00 97.41 C ANISOU 92 CB ASP A1012 12545 12112 12353 473 150 137 C ATOM 93 CG ASP A1012 -30.287 81.802 7.107 1.00 98.36 C ANISOU 93 CG ASP A1012 12701 12218 12450 589 260 161 C ATOM 94 OD1 ASP A1012 -31.168 80.947 6.857 1.00 97.79 O ANISOU 94 OD1 ASP A1012 12481 12216 12459 621 333 188 O ATOM 95 OD2 ASP A1012 -30.233 82.412 8.195 1.00101.37 O ANISOU 95 OD2 ASP A1012 13270 12512 12731 648 272 161 O ATOM 96 N ASN A1013 -27.388 81.696 3.563 1.00101.09 N ANISOU 96 N ASN A1013 12803 12668 12937 257 17 119 N ATOM 97 CA ASN A1013 -26.424 82.175 2.559 1.00102.03 C ANISOU 97 CA ASN A1013 12905 12789 13071 175 -45 122 C ATOM 98 C ASN A1013 -26.869 81.847 1.136 1.00101.01 C ANISOU 98 C ASN A1013 12668 12718 12992 170 -18 118 C ATOM 99 O ASN A1013 -26.823 82.713 0.266 1.00101.88 O ANISOU 99 O ASN A1013 12807 12816 13087 155 -44 118 O ATOM 100 CB ASN A1013 -25.010 81.617 2.802 1.00101.74 C ANISOU 100 CB ASN A1013 12834 12753 13068 88 -95 139 C ATOM 101 CG ASN A1013 -24.235 82.400 3.851 1.00102.89 C ANISOU 101 CG ASN A1013 13116 12816 13162 54 -179 156 C ATOM 102 OD1 ASN A1013 -24.055 83.611 3.723 1.00102.07 O ANISOU 102 OD1 ASN A1013 13114 12657 13012 38 -236 164 O ATOM 103 ND2 ASN A1013 -23.751 81.708 4.883 1.00103.94 N ANISOU 103 ND2 ASN A1013 13262 12932 13299 36 -200 164 N ATOM 104 N LEU A1014 -27.325 80.614 0.917 1.00 99.94 N ANISOU 104 N LEU A1014 12428 12636 12907 179 25 115 N ATOM 105 CA LEU A1014 -27.836 80.175 -0.395 1.00 99.96 C ANISOU 105 CA LEU A1014 12355 12677 12948 173 35 113 C ATOM 106 C LEU A1014 -28.917 81.117 -0.950 1.00 99.92 C ANISOU 106 C LEU A1014 12377 12658 12927 222 31 117 C ATOM 107 O LEU A1014 -28.986 81.335 -2.159 1.00 99.40 O ANISOU 107 O LEU A1014 12303 12597 12867 199 7 114 O ATOM 108 CB LEU A1014 -28.361 78.731 -0.315 1.00 99.39 C ANISOU 108 CB LEU A1014 12191 12647 12925 181 68 115 C ATOM 109 CG LEU A1014 -28.585 77.965 -1.631 1.00 99.94 C ANISOU 109 CG LEU A1014 12206 12741 13026 153 58 113 C ATOM 110 CD1 LEU A1014 -28.289 76.482 -1.444 1.00100.16 C ANISOU 110 CD1 LEU A1014 12177 12793 13085 131 76 111 C ATOM 111 CD2 LEU A1014 -29.989 78.154 -2.191 1.00100.79 C ANISOU 111 CD2 LEU A1014 12289 12851 13157 189 44 129 C ATOM 112 N LYS A1015 -29.738 81.681 -0.064 1.00100.99 N ANISOU 112 N LYS A1015 12557 12771 13042 296 57 128 N ATOM 113 CA LYS A1015 -30.731 82.695 -0.445 1.00102.64 C ANISOU 113 CA LYS A1015 12798 12960 13238 357 59 142 C ATOM 114 C LYS A1015 -30.123 84.067 -0.804 1.00103.20 C ANISOU 114 C LYS A1015 12983 12982 13245 338 12 127 C ATOM 115 O LYS A1015 -30.720 84.816 -1.584 1.00103.15 O ANISOU 115 O LYS A1015 12992 12965 13235 363 -3 133 O ATOM 116 CB LYS A1015 -31.792 82.846 0.652 1.00102.86 C ANISOU 116 CB LYS A1015 12840 12975 13264 461 126 171 C ATOM 117 CG LYS A1015 -32.706 81.636 0.773 1.00102.60 C ANISOU 117 CG LYS A1015 12674 12994 13314 484 171 207 C ATOM 118 CD LYS A1015 -33.546 81.687 2.038 1.00103.81 C ANISOU 118 CD LYS A1015 12844 13134 13465 590 261 247 C ATOM 119 CE LYS A1015 -34.434 80.460 2.163 1.00104.03 C ANISOU 119 CE LYS A1015 12723 13213 13588 602 303 297 C ATOM 120 NZ LYS A1015 -35.076 80.374 3.503 1.00104.61 N ANISOU 120 NZ LYS A1015 12816 13274 13655 703 410 342 N ATOM 121 N VAL A1016 -28.959 84.395 -0.236 1.00102.41 N ANISOU 121 N VAL A1016 12961 12846 13101 290 -19 117 N ATOM 122 CA VAL A1016 -28.212 85.611 -0.616 1.00102.79 C ANISOU 122 CA VAL A1016 13110 12846 13099 247 -81 114 C ATOM 123 C VAL A1016 -27.658 85.499 -2.049 1.00104.30 C ANISOU 123 C VAL A1016 13238 13067 13322 175 -104 115 C ATOM 124 O VAL A1016 -27.550 86.511 -2.748 1.00105.64 O ANISOU 124 O VAL A1016 13470 13208 13461 160 -139 116 O ATOM 125 CB VAL A1016 -27.064 85.951 0.383 1.00102.18 C ANISOU 125 CB VAL A1016 13129 12715 12980 197 -133 120 C ATOM 126 CG1 VAL A1016 -26.305 87.207 -0.050 1.00101.78 C ANISOU 126 CG1 VAL A1016 13174 12608 12888 139 -210 131 C ATOM 127 CG2 VAL A1016 -27.607 86.131 1.798 1.00101.16 C ANISOU 127 CG2 VAL A1016 13107 12534 12793 276 -109 117 C ATOM 128 N ILE A1017 -27.316 84.281 -2.478 1.00105.19 N ANISOU 128 N ILE A1017 13247 13230 13487 138 -80 115 N ATOM 129 CA ILE A1017 -26.891 84.026 -3.867 1.00106.22 C ANISOU 129 CA ILE A1017 13338 13382 13637 91 -80 118 C ATOM 130 C ILE A1017 -28.056 84.261 -4.844 1.00107.55 C ANISOU 130 C ILE A1017 13508 13552 13802 130 -86 109 C ATOM 131 O ILE A1017 -27.864 84.870 -5.900 1.00109.10 O ANISOU 131 O ILE A1017 13746 13731 13976 106 -108 110 O ATOM 132 CB ILE A1017 -26.294 82.596 -4.050 1.00106.18 C ANISOU 132 CB ILE A1017 13246 13419 13678 59 -44 122 C ATOM 133 CG1 ILE A1017 -24.858 82.527 -3.502 1.00106.82 C ANISOU 133 CG1 ILE A1017 13315 13495 13774 3 -50 149 C ATOM 134 CG2 ILE A1017 -26.274 82.164 -5.519 1.00105.91 C ANISOU 134 CG2 ILE A1017 13198 13396 13646 43 -29 120 C ATOM 135 CD1 ILE A1017 -24.758 82.376 -2.003 1.00106.54 C ANISOU 135 CD1 ILE A1017 13292 13448 13740 12 -66 150 C ATOM 136 N GLU A1018 -29.247 83.778 -4.485 1.00106.22 N ANISOU 136 N GLU A1018 13293 13401 13663 187 -71 110 N ATOM 137 CA GLU A1018 -30.452 83.929 -5.320 1.00106.41 C ANISOU 137 CA GLU A1018 13300 13425 13706 222 -93 119 C ATOM 138 C GLU A1018 -30.777 85.392 -5.658 1.00108.52 C ANISOU 138 C GLU A1018 13649 13650 13931 250 -123 121 C ATOM 139 O GLU A1018 -31.195 85.686 -6.780 1.00109.04 O ANISOU 139 O GLU A1018 13730 13704 13995 243 -161 124 O ATOM 140 CB GLU A1018 -31.660 83.267 -4.644 1.00106.14 C ANISOU 140 CB GLU A1018 13183 13414 13728 280 -69 145 C ATOM 141 CG GLU A1018 -31.582 81.742 -4.604 1.00105.93 C ANISOU 141 CG GLU A1018 13074 13424 13748 246 -58 147 C ATOM 142 CD GLU A1018 -32.467 81.095 -3.546 1.00105.31 C ANISOU 142 CD GLU A1018 12917 13370 13723 297 -18 178 C ATOM 143 OE1 GLU A1018 -33.240 81.798 -2.860 1.00104.80 O ANISOU 143 OE1 GLU A1018 12856 13296 13665 372 14 206 O ATOM 144 OE2 GLU A1018 -32.386 79.858 -3.399 1.00105.52 O ANISOU 144 OE2 GLU A1018 12884 13423 13785 268 -11 181 O ATOM 145 N LYS A1019 -30.566 86.292 -4.693 1.00110.14 N ANISOU 145 N LYS A1019 13927 13825 14094 283 -113 120 N ATOM 146 CA LYS A1019 -30.816 87.733 -4.855 1.00111.38 C ANISOU 146 CA LYS A1019 14186 13931 14199 317 -141 121 C ATOM 147 C LYS A1019 -29.519 88.547 -5.048 1.00110.87 C ANISOU 147 C LYS A1019 14217 13829 14079 244 -180 111 C ATOM 148 O LYS A1019 -29.436 89.705 -4.620 1.00111.10 O ANISOU 148 O LYS A1019 14359 13803 14050 265 -206 111 O ATOM 149 CB LYS A1019 -31.581 88.265 -3.630 1.00113.29 C ANISOU 149 CB LYS A1019 14478 14146 14420 417 -102 135 C ATOM 150 CG LYS A1019 -32.888 87.546 -3.315 1.00114.07 C ANISOU 150 CG LYS A1019 14468 14282 14588 497 -48 169 C ATOM 151 CD LYS A1019 -33.938 87.794 -4.388 1.00114.53 C ANISOU 151 CD LYS A1019 14472 14348 14695 524 -78 197 C ATOM 152 CE LYS A1019 -35.282 87.200 -4.002 1.00114.24 C ANISOU 152 CE LYS A1019 14314 14343 14747 604 -32 257 C ATOM 153 NZ LYS A1019 -36.309 87.450 -5.047 1.00113.34 N ANISOU 153 NZ LYS A1019 14137 14229 14695 622 -83 300 N ATOM 154 N ALA A1020 -28.523 87.953 -5.710 1.00109.18 N ANISOU 154 N ALA A1020 13960 13639 13883 162 -184 111 N ATOM 155 CA ALA A1020 -27.205 88.576 -5.872 1.00109.11 C ANISOU 155 CA ALA A1020 14005 13602 13847 85 -214 125 C ATOM 156 C ALA A1020 -27.147 89.462 -7.109 1.00110.09 C ANISOU 156 C ALA A1020 14187 13700 13941 61 -242 129 C ATOM 157 O ALA A1020 -28.027 89.400 -7.973 1.00107.87 O ANISOU 157 O ALA A1020 13898 13425 13660 95 -242 117 O ATOM 158 CB ALA A1020 -26.123 87.512 -5.944 1.00108.70 C ANISOU 158 CB ALA A1020 13869 13589 13841 23 -184 141 C ATOM 159 N ASP A1021 -26.099 90.283 -7.174 1.00111.99 N ANISOU 159 N ASP A1021 14486 13905 14157 -2 -276 154 N ATOM 160 CA ASP A1021 -25.849 91.185 -8.305 1.00113.38 C ANISOU 160 CA ASP A1021 14724 14051 14301 -37 -301 167 C ATOM 161 C ASP A1021 -24.494 90.913 -8.960 1.00111.82 C ANISOU 161 C ASP A1021 14483 13868 14134 -120 -274 213 C ATOM 162 O ASP A1021 -24.436 90.583 -10.146 1.00111.25 O ANISOU 162 O ASP A1021 14398 13810 14060 -126 -232 218 O ATOM 163 CB ASP A1021 -25.909 92.650 -7.849 1.00115.98 C ANISOU 163 CB ASP A1021 15182 14311 14571 -34 -369 171 C ATOM 164 CG ASP A1021 -27.285 93.061 -7.330 1.00117.27 C ANISOU 164 CG ASP A1021 15402 14453 14701 69 -375 137 C ATOM 165 OD1 ASP A1021 -28.298 92.413 -7.680 1.00117.72 O ANISOU 165 OD1 ASP A1021 15391 14548 14788 131 -339 120 O ATOM 166 OD2 ASP A1021 -27.349 94.056 -6.574 1.00119.64 O ANISOU 166 OD2 ASP A1021 15820 14690 14945 93 -418 137 O ATOM 167 N ASN A1022 -23.417 91.051 -8.182 1.00111.20 N ANISOU 167 N ASN A1022 14388 13780 14084 -182 -298 257 N ATOM 168 CA ASN A1022 -22.038 90.936 -8.685 1.00111.83 C ANISOU 168 CA ASN A1022 14408 13870 14212 -262 -273 329 C ATOM 169 C ASN A1022 -21.256 89.786 -8.040 1.00112.92 C ANISOU 169 C ASN A1022 14430 14051 14423 -284 -235 362 C ATOM 170 O ASN A1022 -21.693 89.203 -7.044 1.00110.45 O ANISOU 170 O ASN A1022 14099 13751 14116 -250 -246 326 O ATOM 171 CB ASN A1022 -21.283 92.265 -8.504 1.00112.31 C ANISOU 171 CB ASN A1022 14541 13870 14261 -339 -356 385 C ATOM 172 CG ASN A1022 -21.116 92.660 -7.045 1.00112.07 C ANISOU 172 CG ASN A1022 14562 13795 14224 -363 -450 390 C ATOM 173 OD1 ASN A1022 -21.940 92.315 -6.198 1.00108.68 O ANISOU 173 OD1 ASN A1022 14160 13365 13765 -296 -453 333 O ATOM 174 ND2 ASN A1022 -20.049 93.397 -6.747 1.00113.59 N ANISOU 174 ND2 ASN A1022 14777 13940 14442 -460 -532 467 N ATOM 175 N ALA A1023 -20.093 89.486 -8.618 1.00115.90 N ANISOU 175 N ALA A1023 14728 14447 14858 -335 -183 437 N ATOM 176 CA ALA A1023 -19.259 88.343 -8.217 1.00116.81 C ANISOU 176 CA ALA A1023 14721 14606 15053 -348 -131 482 C ATOM 177 C ALA A1023 -18.701 88.421 -6.794 1.00117.21 C ANISOU 177 C ALA A1023 14745 14638 15149 -399 -219 515 C ATOM 178 O ALA A1023 -18.470 87.383 -6.170 1.00118.01 O ANISOU 178 O ALA A1023 14767 14772 15297 -387 -194 517 O ATOM 179 CB ALA A1023 -18.116 88.159 -9.207 1.00117.95 C ANISOU 179 CB ALA A1023 14791 14769 15255 -379 -43 576 C ATOM 180 N ALA A1024 -18.472 89.637 -6.295 1.00117.83 N ANISOU 180 N ALA A1024 14906 14655 15209 -459 -330 543 N ATOM 181 CA ALA A1024 -17.984 89.842 -4.926 1.00115.97 C ANISOU 181 CA ALA A1024 14691 14375 14995 -514 -443 574 C ATOM 182 C ALA A1024 -19.012 89.372 -3.899 1.00113.98 C ANISOU 182 C ALA A1024 14502 14119 14684 -440 -454 482 C ATOM 183 O ALA A1024 -18.679 88.609 -2.993 1.00114.17 O ANISOU 183 O ALA A1024 14478 14152 14747 -448 -469 493 O ATOM 184 CB ALA A1024 -17.636 91.305 -4.693 1.00116.98 C ANISOU 184 CB ALA A1024 14934 14419 15093 -592 -572 618 C ATOM 185 N GLN A1025 -20.256 89.822 -4.059 1.00111.71 N ANISOU 185 N GLN A1025 14316 13817 14310 -363 -441 402 N ATOM 186 CA GLN A1025 -21.367 89.394 -3.196 1.00110.88 C ANISOU 186 CA GLN A1025 14260 13712 14154 -276 -425 327 C ATOM 187 C GLN A1025 -21.608 87.880 -3.234 1.00109.38 C ANISOU 187 C GLN A1025 13945 13599 14014 -232 -333 303 C ATOM 188 O GLN A1025 -22.003 87.292 -2.226 1.00110.02 O ANISOU 188 O GLN A1025 14031 13682 14087 -194 -330 274 O ATOM 189 CB GLN A1025 -22.657 90.131 -3.567 1.00111.60 C ANISOU 189 CB GLN A1025 14451 13783 14166 -195 -412 267 C ATOM 190 CG GLN A1025 -22.659 91.604 -3.176 1.00113.74 C ANISOU 190 CG GLN A1025 14889 13962 14364 -212 -508 274 C ATOM 191 CD GLN A1025 -23.876 92.365 -3.688 1.00114.02 C ANISOU 191 CD GLN A1025 15012 13979 14331 -127 -487 227 C ATOM 192 OE1 GLN A1025 -24.517 91.963 -4.662 1.00114.73 O ANISOU 192 OE1 GLN A1025 15028 14123 14441 -86 -420 204 O ATOM 193 NE2 GLN A1025 -24.192 93.480 -3.036 1.00114.62 N ANISOU 193 NE2 GLN A1025 15258 13968 14324 -99 -553 217 N ATOM 194 N VAL A1026 -21.369 87.263 -4.392 1.00107.35 N ANISOU 194 N VAL A1026 13593 13397 13799 -235 -256 316 N ATOM 195 CA VAL A1026 -21.480 85.807 -4.546 1.00105.85 C ANISOU 195 CA VAL A1026 13299 13268 13651 -201 -175 300 C ATOM 196 C VAL A1026 -20.377 85.088 -3.763 1.00105.46 C ANISOU 196 C VAL A1026 13167 13230 13670 -248 -183 352 C ATOM 197 O VAL A1026 -20.671 84.193 -2.969 1.00104.36 O ANISOU 197 O VAL A1026 12999 13110 13541 -217 -170 324 O ATOM 198 CB VAL A1026 -21.458 85.389 -6.040 1.00105.24 C ANISOU 198 CB VAL A1026 13183 13223 13580 -187 -95 304 C ATOM 199 CG1 VAL A1026 -21.311 83.878 -6.210 1.00104.51 C ANISOU 199 CG1 VAL A1026 13002 13178 13526 -160 -17 300 C ATOM 200 CG2 VAL A1026 -22.728 85.868 -6.728 1.00105.52 C ANISOU 200 CG2 VAL A1026 13293 13245 13552 -135 -99 248 C ATOM 201 N LYS A1027 -19.123 85.485 -3.989 1.00104.80 N ANISOU 201 N LYS A1027 13040 13134 13642 -322 -207 436 N ATOM 202 CA LYS A1027 -17.967 84.868 -3.319 1.00105.28 C ANISOU 202 CA LYS A1027 13006 13205 13790 -375 -226 509 C ATOM 203 C LYS A1027 -18.018 85.020 -1.795 1.00106.66 C ANISOU 203 C LYS A1027 13245 13332 13948 -397 -333 497 C ATOM 204 O LYS A1027 -17.731 84.067 -1.070 1.00107.61 O ANISOU 204 O LYS A1027 13306 13470 14109 -394 -329 504 O ATOM 205 CB LYS A1027 -16.650 85.449 -3.856 1.00105.76 C ANISOU 205 CB LYS A1027 13000 13255 13928 -456 -242 626 C ATOM 206 CG LYS A1027 -15.395 84.737 -3.364 1.00105.07 C ANISOU 206 CG LYS A1027 12779 13184 13958 -506 -248 726 C ATOM 207 CD LYS A1027 -14.140 85.343 -3.966 1.00106.63 C ANISOU 207 CD LYS A1027 12889 13374 14250 -583 -254 864 C ATOM 208 CE LYS A1027 -12.887 84.773 -3.320 1.00108.54 C ANISOU 208 CE LYS A1027 12988 13624 14628 -642 -288 985 C ATOM 209 NZ LYS A1027 -11.642 85.344 -3.907 1.00109.68 N ANISOU 209 NZ LYS A1027 13019 13765 14890 -719 -287 1146 N ATOM 210 N ASP A1028 -18.383 86.214 -1.322 1.00108.91 N ANISOU 210 N ASP A1028 13668 13547 14163 -414 -428 479 N ATOM 211 CA ASP A1028 -18.520 86.487 0.119 1.00111.82 C ANISOU 211 CA ASP A1028 14153 13847 14485 -423 -530 463 C ATOM 212 C ASP A1028 -19.461 85.499 0.816 1.00111.44 C ANISOU 212 C ASP A1028 14112 13827 14400 -335 -467 387 C ATOM 213 O ASP A1028 -19.168 85.031 1.918 1.00113.14 O ANISOU 213 O ASP A1028 14347 14016 14622 -348 -514 396 O ATOM 214 CB ASP A1028 -19.014 87.924 0.363 1.00113.24 C ANISOU 214 CB ASP A1028 14517 13942 14567 -423 -615 440 C ATOM 215 CG ASP A1028 -17.950 88.977 0.074 1.00114.56 C ANISOU 215 CG ASP A1028 14707 14053 14768 -535 -724 529 C ATOM 216 OD1 ASP A1028 -16.979 88.688 -0.661 1.00116.07 O ANISOU 216 OD1 ASP A1028 14748 14290 15063 -598 -699 611 O ATOM 217 OD2 ASP A1028 -18.095 90.109 0.580 1.00115.57 O ANISOU 217 OD2 ASP A1028 15008 14086 14816 -557 -833 525 O ATOM 218 N ALA A1029 -20.581 85.191 0.164 1.00109.81 N ANISOU 218 N ALA A1029 13890 13669 14161 -250 -368 323 N ATOM 219 CA ALA A1029 -21.539 84.199 0.662 1.00108.43 C ANISOU 219 CA ALA A1029 13696 13529 13970 -170 -299 265 C ATOM 220 C ALA A1029 -21.037 82.760 0.492 1.00106.34 C ANISOU 220 C ALA A1029 13289 13331 13783 -180 -240 281 C ATOM 221 O ALA A1029 -21.261 81.924 1.363 1.00106.26 O ANISOU 221 O ALA A1029 13269 13329 13776 -153 -227 262 O ATOM 222 CB ALA A1029 -22.882 84.370 -0.032 1.00108.23 C ANISOU 222 CB ALA A1029 13688 13529 13903 -89 -233 212 C ATOM 223 N LEU A1030 -20.378 82.478 -0.631 1.00105.91 N ANISOU 223 N LEU A1030 13138 13316 13784 -209 -196 317 N ATOM 224 CA LEU A1030 -19.837 81.136 -0.913 1.00104.31 C ANISOU 224 CA LEU A1030 12814 13168 13649 -207 -129 337 C ATOM 225 C LEU A1030 -18.704 80.726 0.038 1.00102.66 C ANISOU 225 C LEU A1030 12553 12945 13504 -261 -181 398 C ATOM 226 O LEU A1030 -18.646 79.572 0.473 1.00 99.53 O ANISOU 226 O LEU A1030 12100 12578 13137 -239 -147 389 O ATOM 227 CB LEU A1030 -19.363 81.028 -2.374 1.00105.30 C ANISOU 227 CB LEU A1030 12878 13325 13804 -210 -56 370 C ATOM 228 CG LEU A1030 -20.335 80.462 -3.420 1.00105.99 C ANISOU 228 CG LEU A1030 12976 13443 13852 -147 22 313 C ATOM 229 CD1 LEU A1030 -20.356 78.942 -3.359 1.00106.71 C ANISOU 229 CD1 LEU A1030 13005 13570 13969 -113 84 299 C ATOM 230 CD2 LEU A1030 -21.747 81.009 -3.280 1.00106.47 C ANISOU 230 CD2 LEU A1030 13119 13487 13846 -107 -7 247 C ATOM 231 N THR A1031 -17.813 81.667 0.347 1.00101.36 N ANISOU 231 N THR A1031 12411 12733 13366 -336 -275 465 N ATOM 232 CA THR A1031 -16.685 81.420 1.257 1.00100.85 C ANISOU 232 CA THR A1031 12300 12642 13374 -404 -357 541 C ATOM 233 C THR A1031 -17.139 81.078 2.689 1.00100.82 C ANISOU 233 C THR A1031 12387 12599 13321 -388 -419 494 C ATOM 234 O THR A1031 -16.480 80.294 3.375 1.00100.04 O ANISOU 234 O THR A1031 12229 12500 13279 -413 -448 532 O ATOM 235 CB THR A1031 -15.718 82.629 1.288 1.00101.19 C ANISOU 235 CB THR A1031 12363 12626 13456 -503 -474 634 C ATOM 236 OG1 THR A1031 -15.428 83.054 -0.051 1.00100.28 O ANISOU 236 OG1 THR A1031 12184 12544 13373 -510 -405 675 O ATOM 237 CG2 THR A1031 -14.409 82.276 1.988 1.00101.93 C ANISOU 237 CG2 THR A1031 12367 12700 13661 -585 -561 743 C ATOM 238 N LYS A1032 -18.256 81.665 3.127 1.00100.59 N ANISOU 238 N LYS A1032 12502 12532 13186 -338 -430 419 N ATOM 239 CA LYS A1032 -18.869 81.337 4.426 1.00100.49 C ANISOU 239 CA LYS A1032 12593 12480 13108 -298 -454 372 C ATOM 240 C LYS A1032 -19.556 79.961 4.435 1.00 98.98 C ANISOU 240 C LYS A1032 12320 12357 12928 -227 -343 322 C ATOM 241 O LYS A1032 -19.535 79.261 5.453 1.00 99.95 O ANISOU 241 O LYS A1032 12465 12465 13045 -218 -359 314 O ATOM 242 CB LYS A1032 -19.887 82.408 4.828 1.00101.98 C ANISOU 242 CB LYS A1032 12962 12606 13180 -247 -474 320 C ATOM 243 CG LYS A1032 -19.290 83.779 5.096 1.00103.58 C ANISOU 243 CG LYS A1032 13297 12713 13346 -316 -607 361 C ATOM 244 CD LYS A1032 -20.383 84.817 5.291 1.00104.79 C ANISOU 244 CD LYS A1032 13629 12808 13377 -242 -599 307 C ATOM 245 CE LYS A1032 -19.815 86.224 5.361 1.00106.92 C ANISOU 245 CE LYS A1032 14040 12979 13603 -312 -732 346 C ATOM 246 NZ LYS A1032 -20.898 87.243 5.450 1.00107.95 N ANISOU 246 NZ LYS A1032 14349 13054 13614 -226 -710 294 N ATOM 247 N MET A1033 -20.183 79.597 3.316 1.00 95.93 N ANISOU 247 N MET A1033 11857 12038 12552 -181 -242 291 N ATOM 248 CA MET A1033 -20.825 78.278 3.162 1.00 93.75 C ANISOU 248 CA MET A1033 11506 11822 12292 -125 -151 253 C ATOM 249 C MET A1033 -19.827 77.124 3.107 1.00 90.34 C ANISOU 249 C MET A1033 10960 11424 11940 -155 -133 292 C ATOM 250 O MET A1033 -20.169 75.996 3.458 1.00 89.40 O ANISOU 250 O MET A1033 10806 11332 11828 -122 -90 267 O ATOM 251 CB MET A1033 -21.686 78.235 1.895 1.00 93.82 C ANISOU 251 CB MET A1033 11480 11875 12290 -82 -75 220 C ATOM 252 CG MET A1033 -22.939 79.086 1.970 1.00 93.67 C ANISOU 252 CG MET A1033 11550 11834 12204 -30 -72 181 C ATOM 253 SD MET A1033 -23.643 79.388 0.344 1.00 95.37 S ANISOU 253 SD MET A1033 11738 12082 12416 -8 -28 164 S ATOM 254 CE MET A1033 -24.071 77.728 -0.160 1.00 93.58 C ANISOU 254 CE MET A1033 11415 11911 12228 15 37 147 C ATOM 255 N ARG A1034 -18.611 77.404 2.642 1.00 87.72 N ANISOU 255 N ARG A1034 10564 11091 11672 -212 -161 363 N ATOM 256 CA ARG A1034 -17.551 76.398 2.590 1.00 86.40 C ANISOU 256 CA ARG A1034 10281 10952 11594 -231 -138 420 C ATOM 257 C ARG A1034 -17.057 76.046 3.999 1.00 88.17 C ANISOU 257 C ARG A1034 10522 11138 11838 -265 -224 444 C ATOM 258 O ARG A1034 -16.748 74.884 4.280 1.00 88.71 O ANISOU 258 O ARG A1034 10523 11233 11950 -250 -193 452 O ATOM 259 CB ARG A1034 -16.387 76.882 1.719 1.00 85.12 C ANISOU 259 CB ARG A1034 10034 10797 11508 -278 -133 512 C ATOM 260 CG ARG A1034 -15.518 75.753 1.205 1.00 85.13 C ANISOU 260 CG ARG A1034 9905 10842 11595 -258 -49 570 C ATOM 261 CD ARG A1034 -14.291 76.249 0.454 1.00 84.65 C ANISOU 261 CD ARG A1034 9748 10788 11627 -297 -31 687 C ATOM 262 NE ARG A1034 -13.523 75.119 -0.063 1.00 82.82 N ANISOU 262 NE ARG A1034 9400 10596 11471 -253 76 746 N ATOM 263 CZ ARG A1034 -12.736 74.321 0.664 1.00 84.23 C ANISOU 263 CZ ARG A1034 9491 10778 11734 -262 55 806 C ATOM 264 NH1 ARG A1034 -12.565 74.511 1.973 1.00 84.43 N ANISOU 264 NH1 ARG A1034 9537 10765 11778 -325 -83 816 N ATOM 265 NH2 ARG A1034 -12.099 73.316 0.070 1.00 85.95 N ANISOU 265 NH2 ARG A1034 9614 11030 12012 -202 175 861 N ATOM 266 N ALA A1035 -16.987 77.053 4.870 1.00 88.93 N ANISOU 266 N ALA A1035 10727 11164 11896 -310 -338 454 N ATOM 267 CA ALA A1035 -16.579 76.870 6.267 1.00 89.84 C ANISOU 267 CA ALA A1035 10906 11220 12009 -346 -443 473 C ATOM 268 C ALA A1035 -17.586 76.045 7.075 1.00 91.50 C ANISOU 268 C ALA A1035 11183 11433 12149 -277 -394 395 C ATOM 269 O ALA A1035 -17.192 75.179 7.865 1.00 93.85 O ANISOU 269 O ALA A1035 11461 11721 12473 -287 -420 409 O ATOM 270 CB ALA A1035 -16.367 78.223 6.931 1.00 89.51 C ANISOU 270 CB ALA A1035 11010 11082 11916 -405 -582 498 C ATOM 271 N ALA A1036 -18.875 76.325 6.881 1.00 91.44 N ANISOU 271 N ALA A1036 11247 11437 12059 -209 -323 324 N ATOM 272 CA ALA A1036 -19.952 75.632 7.599 1.00 89.74 C ANISOU 272 CA ALA A1036 11085 11226 11784 -140 -263 264 C ATOM 273 C ALA A1036 -20.044 74.143 7.234 1.00 90.38 C ANISOU 273 C ALA A1036 11038 11378 11921 -115 -180 252 C ATOM 274 O ALA A1036 -20.390 73.315 8.086 1.00 91.40 O ANISOU 274 O ALA A1036 11191 11504 12033 -89 -163 232 O ATOM 275 CB ALA A1036 -21.287 76.327 7.354 1.00 88.56 C ANISOU 275 CB ALA A1036 11012 11077 11560 -72 -203 215 C ATOM 276 N ALA A1037 -19.733 73.806 5.980 1.00 87.50 N ANISOU 276 N ALA A1037 10559 11071 11614 -119 -127 267 N ATOM 277 CA ALA A1037 -19.735 72.409 5.531 1.00 86.02 C ANISOU 277 CA ALA A1037 10276 10938 11469 -94 -54 258 C ATOM 278 C ALA A1037 -18.636 71.591 6.211 1.00 86.54 C ANISOU 278 C ALA A1037 10290 10994 11594 -124 -91 303 C ATOM 279 O ALA A1037 -18.872 70.449 6.611 1.00 86.42 O ANISOU 279 O ALA A1037 10257 10995 11582 -99 -59 282 O ATOM 280 CB ALA A1037 -19.589 72.337 4.020 1.00 85.95 C ANISOU 280 CB ALA A1037 10196 10972 11489 -84 10 267 C ATOM 281 N LEU A1038 -17.446 72.181 6.338 1.00 87.06 N ANISOU 281 N LEU A1038 10329 11032 11715 -183 -167 374 N ATOM 282 CA LEU A1038 -16.315 71.541 7.029 1.00 86.99 C ANISOU 282 CA LEU A1038 10262 11006 11781 -220 -225 437 C ATOM 283 C LEU A1038 -16.566 71.407 8.530 1.00 88.21 C ANISOU 283 C LEU A1038 10527 11103 11884 -232 -307 413 C ATOM 284 O LEU A1038 -16.246 70.374 9.129 1.00 89.65 O ANISOU 284 O LEU A1038 10680 11286 12096 -228 -313 422 O ATOM 285 CB LEU A1038 -15.024 72.327 6.800 1.00 86.66 C ANISOU 285 CB LEU A1038 10157 10943 11826 -290 -303 539 C ATOM 286 CG LEU A1038 -14.507 72.398 5.360 1.00 86.27 C ANISOU 286 CG LEU A1038 9989 10945 11841 -277 -212 589 C ATOM 287 CD1 LEU A1038 -13.469 73.503 5.242 1.00 87.95 C ANISOU 287 CD1 LEU A1038 10160 11126 12128 -356 -301 693 C ATOM 288 CD2 LEU A1038 -13.932 71.063 4.909 1.00 85.16 C ANISOU 288 CD2 LEU A1038 9730 10852 11773 -231 -117 623 C ATOM 289 N ASP A1039 -17.131 72.457 9.128 1.00 86.45 N ANISOU 289 N ASP A1039 10446 10821 11577 -240 -364 385 N ATOM 290 CA ASP A1039 -17.551 72.434 10.535 1.00 84.11 C ANISOU 290 CA ASP A1039 10300 10456 11201 -231 -421 355 C ATOM 291 C ASP A1039 -18.644 71.382 10.777 1.00 81.09 C ANISOU 291 C ASP A1039 9921 10112 10774 -157 -312 291 C ATOM 292 O ASP A1039 -18.655 70.735 11.824 1.00 82.01 O ANISOU 292 O ASP A1039 10097 10195 10866 -151 -336 284 O ATOM 293 CB ASP A1039 -18.041 73.830 10.964 1.00 84.07 C ANISOU 293 CB ASP A1039 10468 10376 11098 -232 -478 337 C ATOM 294 CG ASP A1039 -18.248 73.961 12.473 1.00 85.25 C ANISOU 294 CG ASP A1039 10812 10426 11153 -225 -552 322 C ATOM 295 OD1 ASP A1039 -17.646 73.196 13.263 1.00 86.12 O ANISOU 295 OD1 ASP A1039 10924 10507 11288 -255 -612 346 O ATOM 296 OD2 ASP A1039 -19.019 74.860 12.872 1.00 86.13 O ANISOU 296 OD2 ASP A1039 11090 10479 11157 -183 -547 288 O ATOM 297 N ALA A1040 -19.553 71.233 9.811 1.00 78.82 N ANISOU 297 N ALA A1040 9576 9890 10481 -107 -203 251 N ATOM 298 CA ALA A1040 -20.613 70.210 9.850 1.00 77.20 C ANISOU 298 CA ALA A1040 9349 9727 10255 -48 -107 207 C ATOM 299 C ALA A1040 -20.060 68.796 9.673 1.00 75.11 C ANISOU 299 C ALA A1040 8980 9502 10056 -56 -84 219 C ATOM 300 O ALA A1040 -20.512 67.863 10.334 1.00 73.74 O ANISOU 300 O ALA A1040 8823 9329 9865 -33 -57 199 O ATOM 301 CB ALA A1040 -21.657 70.491 8.774 1.00 77.31 C ANISOU 301 CB ALA A1040 9326 9789 10257 -8 -26 177 C ATOM 302 N GLN A1041 -19.084 68.655 8.778 1.00 74.84 N ANISOU 302 N GLN A1041 8845 9496 10095 -82 -88 257 N ATOM 303 CA GLN A1041 -18.429 67.372 8.477 1.00 74.52 C ANISOU 303 CA GLN A1041 8709 9487 10117 -77 -56 278 C ATOM 304 C GLN A1041 -17.721 66.738 9.684 1.00 75.57 C ANISOU 304 C GLN A1041 8855 9582 10273 -100 -124 306 C ATOM 305 O GLN A1041 -17.544 65.521 9.722 1.00 74.11 O ANISOU 305 O GLN A1041 8624 9418 10117 -80 -90 305 O ATOM 306 CB GLN A1041 -17.423 67.579 7.331 1.00 75.28 C ANISOU 306 CB GLN A1041 8707 9610 10286 -88 -36 333 C ATOM 307 CG GLN A1041 -16.710 66.327 6.844 1.00 74.98 C ANISOU 307 CG GLN A1041 8578 9599 10308 -61 20 364 C ATOM 308 CD GLN A1041 -15.858 66.588 5.622 1.00 75.50 C ANISOU 308 CD GLN A1041 8561 9689 10434 -51 74 423 C ATOM 309 OE1 GLN A1041 -15.161 67.603 5.541 1.00 76.22 O ANISOU 309 OE1 GLN A1041 8621 9768 10570 -93 27 483 O ATOM 310 NE2 GLN A1041 -15.890 65.663 4.669 1.00 74.92 N ANISOU 310 NE2 GLN A1041 8463 9642 10358 5 172 414 N ATOM 311 N LYS A1042 -17.303 67.562 10.648 1.00 76.55 N ANISOU 311 N LYS A1042 9059 9644 10382 -144 -228 332 N ATOM 312 CA LYS A1042 -16.749 67.074 11.921 1.00 77.98 C ANISOU 312 CA LYS A1042 9290 9771 10567 -171 -314 355 C ATOM 313 C LYS A1042 -17.822 66.502 12.853 1.00 77.65 C ANISOU 313 C LYS A1042 9356 9710 10437 -130 -277 294 C ATOM 314 O LYS A1042 -17.524 65.652 13.694 1.00 78.91 O ANISOU 314 O LYS A1042 9536 9843 10600 -135 -310 301 O ATOM 315 CB LYS A1042 -16.045 68.206 12.680 1.00 79.04 C ANISOU 315 CB LYS A1042 9514 9822 10695 -237 -459 403 C ATOM 316 CG LYS A1042 -14.875 68.863 11.964 1.00 79.78 C ANISOU 316 CG LYS A1042 9499 9921 10891 -295 -520 490 C ATOM 317 CD LYS A1042 -14.583 70.227 12.572 1.00 81.41 C ANISOU 317 CD LYS A1042 9831 10039 11061 -361 -662 521 C ATOM 318 CE LYS A1042 -13.684 71.060 11.679 1.00 82.87 C ANISOU 318 CE LYS A1042 9907 10237 11340 -417 -704 605 C ATOM 319 NZ LYS A1042 -13.485 72.412 12.263 1.00 84.38 N ANISOU 319 NZ LYS A1042 10244 10331 11484 -487 -854 633 N ATOM 320 N ALA A1043 -19.055 66.994 12.727 1.00 76.32 N ANISOU 320 N ALA A1043 9253 9550 10194 -87 -209 244 N ATOM 321 CA ALA A1043 -20.122 66.689 13.683 1.00 77.32 C ANISOU 321 CA ALA A1043 9489 9651 10238 -42 -164 206 C ATOM 322 C ALA A1043 -20.661 65.273 13.546 1.00 76.31 C ANISOU 322 C ALA A1043 9287 9575 10132 -13 -83 185 C ATOM 323 O ALA A1043 -20.246 64.515 12.669 1.00 80.30 O ANISOU 323 O ALA A1043 9674 10131 10704 -21 -61 193 O ATOM 324 CB ALA A1043 -21.258 67.702 13.551 1.00 77.44 C ANISOU 324 CB ALA A1043 9579 9661 10183 2 -106 179 C ATOM 325 N THR A1044 -21.574 64.931 14.450 1.00 75.60 N ANISOU 325 N THR A1044 9282 9462 9980 24 -38 166 N ATOM 326 CA THR A1044 -22.281 63.661 14.450 1.00 74.42 C ANISOU 326 CA THR A1044 9079 9351 9843 48 35 153 C ATOM 327 C THR A1044 -23.758 63.961 14.160 1.00 74.82 C ANISOU 327 C THR A1044 9126 9433 9868 96 131 144 C ATOM 328 O THR A1044 -24.344 64.837 14.813 1.00 73.05 O ANISOU 328 O THR A1044 9006 9170 9580 134 157 147 O ATOM 329 CB THR A1044 -22.142 62.967 15.823 1.00 75.12 C ANISOU 329 CB THR A1044 9264 9387 9892 50 12 157 C ATOM 330 OG1 THR A1044 -20.767 62.964 16.231 1.00 75.54 O ANISOU 330 OG1 THR A1044 9337 9395 9969 2 -100 179 O ATOM 331 CG2 THR A1044 -22.642 61.534 15.771 1.00 75.48 C ANISOU 331 CG2 THR A1044 9243 9471 9963 60 70 151 C ATOM 332 N PRO A1045 -24.371 63.241 13.192 1.00 73.57 N ANISOU 332 N PRO A1045 8858 9336 9759 97 181 141 N ATOM 333 CA PRO A1045 -25.766 63.506 12.858 1.00 74.06 C ANISOU 333 CA PRO A1045 8892 9426 9819 134 255 151 C ATOM 334 C PRO A1045 -26.727 62.911 13.891 1.00 73.60 C ANISOU 334 C PRO A1045 8868 9355 9739 169 321 174 C ATOM 335 O PRO A1045 -26.285 62.176 14.781 1.00 72.44 O ANISOU 335 O PRO A1045 8773 9179 9572 160 306 172 O ATOM 336 CB PRO A1045 -25.934 62.797 11.520 1.00 74.86 C ANISOU 336 CB PRO A1045 8882 9579 9980 107 253 147 C ATOM 337 CG PRO A1045 -25.059 61.605 11.654 1.00 74.18 C ANISOU 337 CG PRO A1045 8782 9488 9912 79 220 138 C ATOM 338 CD PRO A1045 -23.880 62.045 12.485 1.00 74.27 C ANISOU 338 CD PRO A1045 8859 9458 9902 69 167 137 C ATOM 339 N PRO A1046 -28.031 63.231 13.782 1.00 72.91 N ANISOU 339 N PRO A1046 8750 9289 9661 211 398 206 N ATOM 340 CA PRO A1046 -29.008 62.707 14.733 1.00 75.15 C ANISOU 340 CA PRO A1046 9051 9563 9936 252 482 249 C ATOM 341 C PRO A1046 -29.076 61.180 14.845 1.00 75.73 C ANISOU 341 C PRO A1046 9068 9655 10051 212 474 260 C ATOM 342 O PRO A1046 -28.947 60.657 15.952 1.00 78.01 O ANISOU 342 O PRO A1046 9430 9908 10301 225 495 266 O ATOM 343 CB PRO A1046 -30.327 63.286 14.216 1.00 75.50 C ANISOU 343 CB PRO A1046 9022 9643 10022 295 554 298 C ATOM 344 CG PRO A1046 -29.914 64.607 13.673 1.00 74.78 C ANISOU 344 CG PRO A1046 8970 9540 9900 307 521 267 C ATOM 345 CD PRO A1046 -28.619 64.312 12.966 1.00 72.77 C ANISOU 345 CD PRO A1046 8699 9292 9656 235 417 215 C ATOM 346 N LYS A1047 -29.242 60.467 13.733 1.00 73.00 N ANISOU 346 N LYS A1047 8612 9352 9772 164 436 261 N ATOM 347 CA LYS A1047 -29.490 59.009 13.808 1.00 71.89 C ANISOU 347 CA LYS A1047 8427 9220 9667 126 426 279 C ATOM 348 C LYS A1047 -28.262 58.105 14.070 1.00 69.59 C ANISOU 348 C LYS A1047 8182 8905 9353 93 366 235 C ATOM 349 O LYS A1047 -28.428 56.892 14.222 1.00 67.90 O ANISOU 349 O LYS A1047 7951 8690 9159 66 357 248 O ATOM 350 CB LYS A1047 -30.263 58.528 12.567 1.00 71.39 C ANISOU 350 CB LYS A1047 8257 9191 9675 85 397 307 C ATOM 351 CG LYS A1047 -31.757 58.805 12.652 1.00 71.08 C ANISOU 351 CG LYS A1047 8142 9173 9690 108 460 388 C ATOM 352 CD LYS A1047 -32.513 58.162 11.507 1.00 71.76 C ANISOU 352 CD LYS A1047 8130 9280 9854 48 399 428 C ATOM 353 CE LYS A1047 -34.010 58.119 11.773 1.00 72.25 C ANISOU 353 CE LYS A1047 8091 9361 9998 57 454 538 C ATOM 354 NZ LYS A1047 -34.731 57.610 10.578 1.00 72.66 N ANISOU 354 NZ LYS A1047 8055 9421 10131 -13 361 584 N ATOM 355 N LEU A1048 -27.057 58.680 14.146 1.00 68.02 N ANISOU 355 N LEU A1048 8037 8684 9120 95 321 195 N ATOM 356 CA LEU A1048 -25.823 57.902 14.313 1.00 67.72 C ANISOU 356 CA LEU A1048 8023 8626 9079 69 261 168 C ATOM 357 C LEU A1048 -25.164 58.185 15.666 1.00 69.27 C ANISOU 357 C LEU A1048 8325 8769 9223 82 242 164 C ATOM 358 O LEU A1048 -24.082 58.764 15.745 1.00 68.97 O ANISOU 358 O LEU A1048 8319 8707 9177 72 181 152 O ATOM 359 CB LEU A1048 -24.865 58.188 13.156 1.00 67.35 C ANISOU 359 CB LEU A1048 7932 8597 9060 52 214 145 C ATOM 360 CG LEU A1048 -25.415 58.026 11.730 1.00 67.75 C ANISOU 360 CG LEU A1048 7914 8682 9143 41 221 144 C ATOM 361 CD1 LEU A1048 -24.282 58.226 10.736 1.00 68.42 C ANISOU 361 CD1 LEU A1048 7980 8773 9242 38 192 127 C ATOM 362 CD2 LEU A1048 -26.078 56.675 11.485 1.00 67.98 C ANISOU 362 CD2 LEU A1048 7922 8714 9190 20 220 156 C ATOM 363 N GLU A1049 -25.827 57.733 16.725 1.00 71.53 N ANISOU 363 N GLU A1049 8668 9031 9476 101 289 184 N ATOM 364 CA GLU A1049 -25.434 58.023 18.109 1.00 73.84 C ANISOU 364 CA GLU A1049 9099 9256 9698 122 278 184 C ATOM 365 C GLU A1049 -24.530 56.938 18.698 1.00 75.79 C ANISOU 365 C GLU A1049 9380 9472 9945 92 214 174 C ATOM 366 O GLU A1049 -23.502 57.246 19.310 1.00 74.41 O ANISOU 366 O GLU A1049 9285 9243 9742 80 135 166 O ATOM 367 CB GLU A1049 -26.690 58.141 18.977 1.00 74.88 C ANISOU 367 CB GLU A1049 9293 9371 9786 175 385 221 C ATOM 368 CG GLU A1049 -27.662 59.235 18.533 1.00 74.06 C ANISOU 368 CG GLU A1049 9160 9292 9685 220 461 244 C ATOM 369 CD GLU A1049 -29.129 58.837 18.608 1.00 73.39 C ANISOU 369 CD GLU A1049 9006 9241 9635 254 575 306 C ATOM 370 OE1 GLU A1049 -29.985 59.703 18.323 1.00 73.86 O ANISOU 370 OE1 GLU A1049 9035 9320 9707 301 645 340 O ATOM 371 OE2 GLU A1049 -29.439 57.672 18.937 1.00 72.10 O ANISOU 371 OE2 GLU A1049 8811 9084 9497 233 593 331 O ATOM 372 N ASP A1050 -24.932 55.675 18.521 1.00 77.35 N ANISOU 372 N ASP A1050 9517 9695 10175 76 237 182 N ATOM 373 CA ASP A1050 -24.194 54.514 19.040 1.00 78.72 C ANISOU 373 CA ASP A1050 9719 9841 10351 54 185 175 C ATOM 374 C ASP A1050 -23.333 53.866 17.942 1.00 79.88 C ANISOU 374 C ASP A1050 9772 10019 10560 28 130 159 C ATOM 375 O ASP A1050 -23.314 52.639 17.783 1.00 82.23 O ANISOU 375 O ASP A1050 10045 10319 10876 15 124 158 O ATOM 376 CB ASP A1050 -25.174 53.496 19.646 1.00 78.85 C ANISOU 376 CB ASP A1050 9752 9853 10354 56 248 200 C ATOM 377 CG ASP A1050 -26.071 54.103 20.723 1.00 80.17 C ANISOU 377 CG ASP A1050 10014 9986 10457 101 333 230 C ATOM 378 OD1 ASP A1050 -25.795 55.233 21.179 1.00 81.74 O ANISOU 378 OD1 ASP A1050 10306 10148 10603 131 327 222 O ATOM 379 OD2 ASP A1050 -27.057 53.448 21.122 1.00 80.93 O ANISOU 379 OD2 ASP A1050 10102 10089 10556 110 409 270 O ATOM 380 N LYS A1051 -22.624 54.709 17.192 1.00 78.15 N ANISOU 380 N LYS A1051 9509 9815 10368 27 97 151 N ATOM 381 CA LYS A1051 -21.715 54.283 16.135 1.00 77.72 C ANISOU 381 CA LYS A1051 9375 9785 10369 20 66 146 C ATOM 382 C LYS A1051 -20.470 55.160 16.215 1.00 75.26 C ANISOU 382 C LYS A1051 9059 9455 10081 14 1 161 C ATOM 383 O LYS A1051 -20.550 56.339 16.569 1.00 72.07 O ANISOU 383 O LYS A1051 8697 9033 9650 10 -14 164 O ATOM 384 CB LYS A1051 -22.374 54.438 14.758 1.00 79.15 C ANISOU 384 CB LYS A1051 9486 10014 10571 24 110 138 C ATOM 385 CG LYS A1051 -23.560 53.507 14.519 1.00 79.08 C ANISOU 385 CG LYS A1051 9470 10018 10558 14 147 140 C ATOM 386 CD LYS A1051 -24.586 54.102 13.567 1.00 79.12 C ANISOU 386 CD LYS A1051 9429 10058 10575 9 178 146 C ATOM 387 CE LYS A1051 -25.959 53.477 13.772 1.00 80.82 C ANISOU 387 CE LYS A1051 9632 10278 10796 -9 207 174 C ATOM 388 NZ LYS A1051 -25.970 51.997 13.577 1.00 81.03 N ANISOU 388 NZ LYS A1051 9670 10286 10829 -34 177 176 N ATOM 389 N SER A1052 -19.327 54.577 15.871 1.00 74.09 N ANISOU 389 N SER A1052 8858 9305 9986 16 -35 179 N ATOM 390 CA SER A1052 -18.040 55.245 16.021 1.00 72.96 C ANISOU 390 CA SER A1052 8687 9141 9891 2 -109 217 C ATOM 391 C SER A1052 -17.841 56.299 14.939 1.00 72.30 C ANISOU 391 C SER A1052 8536 9094 9841 3 -89 229 C ATOM 392 O SER A1052 -18.446 56.190 13.868 1.00 73.21 O ANISOU 392 O SER A1052 8613 9251 9951 24 -18 206 O ATOM 393 CB SER A1052 -16.914 54.218 15.921 1.00 73.50 C ANISOU 393 CB SER A1052 8698 9203 10025 15 -136 251 C ATOM 394 OG SER A1052 -17.010 53.491 14.707 1.00 71.93 O ANISOU 394 OG SER A1052 8439 9043 9845 54 -60 241 O ATOM 395 N PRO A1053 -16.970 57.303 15.196 1.00 70.82 N ANISOU 395 N PRO A1053 8339 8881 9687 -24 -164 269 N ATOM 396 CA PRO A1053 -16.494 58.214 14.146 1.00 69.97 C ANISOU 396 CA PRO A1053 8151 8805 9628 -26 -153 297 C ATOM 397 C PRO A1053 -15.824 57.520 12.948 1.00 72.42 C ANISOU 397 C PRO A1053 8350 9157 10008 11 -90 326 C ATOM 398 O PRO A1053 -15.728 58.127 11.874 1.00 72.15 O ANISOU 398 O PRO A1053 8262 9154 9995 23 -44 337 O ATOM 399 CB PRO A1053 -15.464 59.084 14.873 1.00 69.91 C ANISOU 399 CB PRO A1053 8153 8747 9661 -76 -273 356 C ATOM 400 CG PRO A1053 -15.878 59.057 16.292 1.00 70.65 C ANISOU 400 CG PRO A1053 8387 8776 9680 -96 -337 332 C ATOM 401 CD PRO A1053 -16.459 57.694 16.523 1.00 71.03 C ANISOU 401 CD PRO A1053 8451 8838 9698 -62 -273 294 C ATOM 402 N ASP A1054 -15.346 56.285 13.136 1.00 72.81 N ANISOU 402 N ASP A1054 8379 9198 10086 37 -83 340 N ATOM 403 CA ASP A1054 -14.742 55.500 12.052 1.00 74.60 C ANISOU 403 CA ASP A1054 8531 9451 10362 94 -7 368 C ATOM 404 C ASP A1054 -15.690 54.448 11.435 1.00 72.71 C ANISOU 404 C ASP A1054 8348 9223 10055 133 70 306 C ATOM 405 O ASP A1054 -15.237 53.574 10.688 1.00 73.82 O ANISOU 405 O ASP A1054 8470 9365 10213 189 130 322 O ATOM 406 CB ASP A1054 -13.463 54.836 12.568 1.00 76.82 C ANISOU 406 CB ASP A1054 8749 9709 10729 107 -51 441 C ATOM 407 CG ASP A1054 -12.550 55.821 13.286 1.00 80.36 C ANISOU 407 CG ASP A1054 9148 10132 11251 50 -163 515 C ATOM 408 OD1 ASP A1054 -11.849 56.595 12.598 1.00 80.65 O ANISOU 408 OD1 ASP A1054 9092 10189 11362 48 -154 581 O ATOM 409 OD2 ASP A1054 -12.549 55.829 14.540 1.00 82.70 O ANISOU 409 OD2 ASP A1054 9511 10380 11528 3 -268 512 O ATOM 410 N SER A1055 -16.992 54.546 11.717 1.00 69.25 N ANISOU 410 N SER A1055 7982 8786 9543 105 69 246 N ATOM 411 CA SER A1055 -17.981 53.595 11.196 1.00 68.10 C ANISOU 411 CA SER A1055 7889 8643 9343 121 116 201 C ATOM 412 C SER A1055 -18.304 53.885 9.721 1.00 66.64 C ANISOU 412 C SER A1055 7698 8478 9141 145 174 189 C ATOM 413 O SER A1055 -18.195 55.030 9.280 1.00 65.56 O ANISOU 413 O SER A1055 7527 8362 9020 137 181 200 O ATOM 414 CB SER A1055 -19.271 53.682 12.021 1.00 68.79 C ANISOU 414 CB SER A1055 8033 8725 9377 81 97 165 C ATOM 415 OG SER A1055 -19.965 54.901 11.771 1.00 67.82 O ANISOU 415 OG SER A1055 7904 8624 9238 63 106 154 O ATOM 416 N PRO A1056 -18.735 52.858 8.959 1.00 65.06 N ANISOU 416 N PRO A1056 7552 8262 8903 171 207 166 N ATOM 417 CA PRO A1056 -19.115 53.103 7.558 1.00 64.61 C ANISOU 417 CA PRO A1056 7524 8208 8815 190 248 153 C ATOM 418 C PRO A1056 -20.303 54.072 7.412 1.00 64.44 C ANISOU 418 C PRO A1056 7503 8209 8772 142 226 129 C ATOM 419 O PRO A1056 -20.432 54.745 6.383 1.00 63.90 O ANISOU 419 O PRO A1056 7436 8148 8692 151 249 126 O ATOM 420 CB PRO A1056 -19.467 51.701 7.038 1.00 64.69 C ANISOU 420 CB PRO A1056 7628 8176 8775 214 256 132 C ATOM 421 CG PRO A1056 -19.827 50.918 8.254 1.00 64.66 C ANISOU 421 CG PRO A1056 7634 8161 8770 180 210 124 C ATOM 422 CD PRO A1056 -18.952 51.450 9.345 1.00 64.86 C ANISOU 422 CD PRO A1056 7586 8206 8852 177 195 152 C ATOM 423 N GLU A1057 -21.137 54.143 8.449 1.00 64.09 N ANISOU 423 N GLU A1057 7455 8170 8723 99 190 118 N ATOM 424 CA GLU A1057 -22.219 55.120 8.542 1.00 63.54 C ANISOU 424 CA GLU A1057 7372 8123 8645 66 181 111 C ATOM 425 C GLU A1057 -21.659 56.546 8.612 1.00 63.41 C ANISOU 425 C GLU A1057 7316 8125 8648 69 184 122 C ATOM 426 O GLU A1057 -22.105 57.419 7.874 1.00 62.20 O ANISOU 426 O GLU A1057 7154 7988 8488 66 194 117 O ATOM 427 CB GLU A1057 -23.090 54.850 9.780 1.00 63.97 C ANISOU 427 CB GLU A1057 7437 8175 8694 38 166 113 C ATOM 428 CG GLU A1057 -23.811 53.496 9.797 1.00 64.90 C ANISOU 428 CG GLU A1057 7587 8272 8799 20 152 113 C ATOM 429 CD GLU A1057 -23.009 52.354 10.415 1.00 64.26 C ANISOU 429 CD GLU A1057 7537 8163 8714 32 141 111 C ATOM 430 OE1 GLU A1057 -22.260 52.587 11.384 1.00 64.74 O ANISOU 430 OE1 GLU A1057 7589 8221 8786 42 136 117 O ATOM 431 OE2 GLU A1057 -23.137 51.209 9.935 1.00 63.08 O ANISOU 431 OE2 GLU A1057 7431 7986 8548 31 129 106 O ATOM 432 N MET A1058 -20.684 56.768 9.497 1.00 64.68 N ANISOU 432 N MET A1058 7461 8279 8835 70 163 142 N ATOM 433 CA MET A1058 -20.045 58.087 9.653 1.00 65.59 C ANISOU 433 CA MET A1058 7549 8399 8972 61 142 163 C ATOM 434 C MET A1058 -19.090 58.424 8.504 1.00 66.69 C ANISOU 434 C MET A1058 7639 8551 9148 83 169 191 C ATOM 435 O MET A1058 -18.951 59.593 8.143 1.00 69.10 O ANISOU 435 O MET A1058 7925 8867 9462 71 165 203 O ATOM 436 CB MET A1058 -19.307 58.196 10.993 1.00 66.41 C ANISOU 436 CB MET A1058 7665 8474 9092 42 84 186 C ATOM 437 CG MET A1058 -20.215 58.248 12.222 1.00 66.86 C ANISOU 437 CG MET A1058 7795 8509 9099 28 68 166 C ATOM 438 SD MET A1058 -21.158 59.776 12.429 1.00 67.52 S ANISOU 438 SD MET A1058 7926 8591 9137 24 76 154 S ATOM 439 CE MET A1058 -19.852 60.999 12.585 1.00 66.97 C ANISOU 439 CE MET A1058 7858 8493 9093 -1 0 188 C ATOM 440 N LYS A1059 -18.429 57.420 7.932 1.00 66.95 N ANISOU 440 N LYS A1059 7659 8579 9200 120 206 206 N ATOM 441 CA LYS A1059 -17.668 57.628 6.695 1.00 68.71 C ANISOU 441 CA LYS A1059 7850 8810 9446 160 263 238 C ATOM 442 C LYS A1059 -18.573 58.141 5.569 1.00 69.45 C ANISOU 442 C LYS A1059 7986 8911 9489 161 292 203 C ATOM 443 O LYS A1059 -18.169 59.005 4.798 1.00 71.87 O ANISOU 443 O LYS A1059 8268 9229 9809 170 320 226 O ATOM 444 CB LYS A1059 -16.927 56.353 6.265 1.00 70.11 C ANISOU 444 CB LYS A1059 8033 8969 9635 221 316 260 C ATOM 445 CG LYS A1059 -15.718 56.039 7.136 1.00 71.33 C ANISOU 445 CG LYS A1059 8116 9118 9867 229 294 320 C ATOM 446 CD LYS A1059 -14.793 55.002 6.515 1.00 72.59 C ANISOU 446 CD LYS A1059 8263 9263 10053 311 371 364 C ATOM 447 CE LYS A1059 -13.551 54.813 7.378 1.00 74.28 C ANISOU 447 CE LYS A1059 8380 9474 10368 317 339 443 C ATOM 448 NZ LYS A1059 -12.753 53.611 7.000 1.00 75.41 N ANISOU 448 NZ LYS A1059 8517 9598 10536 408 416 487 N ATOM 449 N ASP A1060 -19.797 57.621 5.491 1.00 69.56 N ANISOU 449 N ASP A1060 8061 8917 9451 146 277 158 N ATOM 450 CA ASP A1060 -20.785 58.106 4.519 1.00 70.12 C ANISOU 450 CA ASP A1060 8172 8989 9481 135 279 132 C ATOM 451 C ASP A1060 -21.323 59.515 4.848 1.00 69.79 C ANISOU 451 C ASP A1060 8098 8972 9447 102 252 129 C ATOM 452 O ASP A1060 -21.627 60.288 3.938 1.00 68.12 O ANISOU 452 O ASP A1060 7896 8764 9219 102 261 124 O ATOM 453 CB ASP A1060 -21.948 57.117 4.425 1.00 71.81 C ANISOU 453 CB ASP A1060 8445 9180 9656 117 249 104 C ATOM 454 CG ASP A1060 -22.887 57.419 3.269 1.00 73.92 C ANISOU 454 CG ASP A1060 8762 9435 9888 104 234 90 C ATOM 455 OD1 ASP A1060 -22.422 57.883 2.204 1.00 72.24 O ANISOU 455 OD1 ASP A1060 8578 9212 9655 132 266 93 O ATOM 456 OD2 ASP A1060 -24.100 57.182 3.434 1.00 76.38 O ANISOU 456 OD2 ASP A1060 9082 9742 10196 64 186 85 O ATOM 457 N PHE A1061 -21.458 59.830 6.138 1.00 69.33 N ANISOU 457 N PHE A1061 8019 8920 9404 78 220 131 N ATOM 458 CA PHE A1061 -21.839 61.176 6.580 1.00 70.92 C ANISOU 458 CA PHE A1061 8213 9130 9601 60 200 132 C ATOM 459 C PHE A1061 -20.864 62.219 6.061 1.00 72.65 C ANISOU 459 C PHE A1061 8406 9353 9842 60 201 157 C ATOM 460 O PHE A1061 -21.281 63.205 5.458 1.00 75.09 O ANISOU 460 O PHE A1061 8722 9670 10136 55 203 151 O ATOM 461 CB PHE A1061 -21.922 61.250 8.114 1.00 71.95 C ANISOU 461 CB PHE A1061 8361 9246 9727 47 170 135 C ATOM 462 CG PHE A1061 -22.131 62.647 8.658 1.00 72.72 C ANISOU 462 CG PHE A1061 8487 9336 9807 39 149 138 C ATOM 463 CD1 PHE A1061 -23.400 63.228 8.668 1.00 71.56 C ANISOU 463 CD1 PHE A1061 8362 9195 9630 50 171 126 C ATOM 464 CD2 PHE A1061 -21.058 63.377 9.188 1.00 74.42 C ANISOU 464 CD2 PHE A1061 8712 9527 10036 20 101 163 C ATOM 465 CE1 PHE A1061 -23.592 64.507 9.178 1.00 72.05 C ANISOU 465 CE1 PHE A1061 8471 9239 9663 57 159 129 C ATOM 466 CE2 PHE A1061 -21.246 64.658 9.699 1.00 73.76 C ANISOU 466 CE2 PHE A1061 8685 9418 9920 12 70 165 C ATOM 467 CZ PHE A1061 -22.516 65.224 9.693 1.00 73.80 C ANISOU 467 CZ PHE A1061 8728 9429 9882 37 106 143 C ATOM 468 N ARG A1062 -19.571 61.977 6.277 1.00 73.51 N ANISOU 468 N ARG A1062 8478 9457 9996 63 197 195 N ATOM 469 CA ARG A1062 -18.523 62.930 5.898 1.00 71.65 C ANISOU 469 CA ARG A1062 8196 9223 9803 54 192 243 C ATOM 470 C ARG A1062 -18.302 63.000 4.389 1.00 71.56 C ANISOU 470 C ARG A1062 8174 9224 9790 87 260 254 C ATOM 471 O ARG A1062 -17.965 64.067 3.865 1.00 72.76 O ANISOU 471 O ARG A1062 8307 9382 9956 75 262 279 O ATOM 472 CB ARG A1062 -17.209 62.603 6.613 1.00 72.14 C ANISOU 472 CB ARG A1062 8202 9273 9933 45 160 302 C ATOM 473 CG ARG A1062 -17.315 62.686 8.130 1.00 72.13 C ANISOU 473 CG ARG A1062 8238 9242 9923 8 77 296 C ATOM 474 CD ARG A1062 -15.948 62.628 8.802 1.00 73.90 C ANISOU 474 CD ARG A1062 8407 9445 10226 -16 13 370 C ATOM 475 NE ARG A1062 -15.390 61.272 8.782 1.00 72.77 N ANISOU 475 NE ARG A1062 8218 9306 10122 20 49 391 N ATOM 476 CZ ARG A1062 -15.635 60.317 9.680 1.00 72.51 C ANISOU 476 CZ ARG A1062 8226 9256 10068 23 26 365 C ATOM 477 NH1 ARG A1062 -16.445 60.527 10.722 1.00 73.32 N ANISOU 477 NH1 ARG A1062 8416 9332 10108 -4 -24 320 N ATOM 478 NH2 ARG A1062 -15.057 59.126 9.538 1.00 71.65 N ANISOU 478 NH2 ARG A1062 8077 9150 9997 62 62 388 N ATOM 479 N HIS A1063 -18.489 61.879 3.694 1.00 70.31 N ANISOU 479 N HIS A1063 8047 9061 9607 128 312 236 N ATOM 480 CA HIS A1063 -18.417 61.867 2.229 1.00 71.74 C ANISOU 480 CA HIS A1063 8261 9235 9759 167 380 239 C ATOM 481 C HIS A1063 -19.513 62.726 1.575 1.00 71.54 C ANISOU 481 C HIS A1063 8285 9211 9683 146 359 199 C ATOM 482 O HIS A1063 -19.276 63.348 0.532 1.00 71.42 O ANISOU 482 O HIS A1063 8287 9193 9655 162 397 213 O ATOM 483 CB HIS A1063 -18.483 60.440 1.686 1.00 72.22 C ANISOU 483 CB HIS A1063 8387 9270 9782 217 425 223 C ATOM 484 CG HIS A1063 -18.194 60.341 0.221 1.00 73.95 C ANISOU 484 CG HIS A1063 8671 9464 9960 273 504 235 C ATOM 485 ND1 HIS A1063 -16.917 60.194 -0.278 1.00 75.81 N ANISOU 485 ND1 HIS A1063 8876 9697 10232 336 597 300 N ATOM 486 CD2 HIS A1063 -19.016 60.379 -0.854 1.00 74.69 C ANISOU 486 CD2 HIS A1063 8870 9529 9978 279 506 198 C ATOM 487 CE1 HIS A1063 -16.966 60.133 -1.597 1.00 76.85 C ANISOU 487 CE1 HIS A1063 9105 9795 10299 388 666 297 C ATOM 488 NE2 HIS A1063 -18.228 60.244 -1.973 1.00 75.87 N ANISOU 488 NE2 HIS A1063 9073 9651 10102 350 603 231 N ATOM 489 N GLY A1064 -20.700 62.761 2.184 1.00 70.36 N ANISOU 489 N GLY A1064 8157 9065 9511 114 305 158 N ATOM 490 CA GLY A1064 -21.771 63.654 1.739 1.00 69.88 C ANISOU 490 CA GLY A1064 8122 9008 9419 94 279 134 C ATOM 491 C GLY A1064 -21.367 65.118 1.809 1.00 70.89 C ANISOU 491 C GLY A1064 8222 9147 9564 79 269 153 C ATOM 492 O GLY A1064 -21.725 65.912 0.932 1.00 72.30 O ANISOU 492 O GLY A1064 8425 9323 9719 78 272 147 O ATOM 493 N PHE A1065 -20.616 65.470 2.852 1.00 69.20 N ANISOU 493 N PHE A1065 7968 8937 9388 61 246 180 N ATOM 494 CA PHE A1065 -20.085 66.826 3.017 1.00 69.70 C ANISOU 494 CA PHE A1065 8016 8998 9468 35 217 208 C ATOM 495 C PHE A1065 -18.792 67.111 2.234 1.00 71.42 C ANISOU 495 C PHE A1065 8185 9218 9731 39 252 266 C ATOM 496 O PHE A1065 -18.371 68.261 2.169 1.00 71.40 O ANISOU 496 O PHE A1065 8170 9211 9746 10 224 298 O ATOM 497 CB PHE A1065 -19.912 67.155 4.511 1.00 69.88 C ANISOU 497 CB PHE A1065 8044 9004 9502 7 153 217 C ATOM 498 CG PHE A1065 -21.208 67.476 5.206 1.00 69.05 C ANISOU 498 CG PHE A1065 7998 8891 9347 12 135 175 C ATOM 499 CD1 PHE A1065 -21.694 68.779 5.226 1.00 70.13 C ANISOU 499 CD1 PHE A1065 8179 9015 9452 8 113 168 C ATOM 500 CD2 PHE A1065 -21.955 66.480 5.819 1.00 68.43 C ANISOU 500 CD2 PHE A1065 7930 8816 9255 28 149 151 C ATOM 501 CE1 PHE A1065 -22.895 69.085 5.858 1.00 70.59 C ANISOU 501 CE1 PHE A1065 8287 9064 9468 32 118 142 C ATOM 502 CE2 PHE A1065 -23.153 66.776 6.454 1.00 68.87 C ANISOU 502 CE2 PHE A1065 8025 8866 9275 44 153 132 C ATOM 503 CZ PHE A1065 -23.626 68.081 6.473 1.00 69.56 C ANISOU 503 CZ PHE A1065 8154 8942 9334 52 144 130 C ATOM 504 N ASP A1066 -18.154 66.081 1.670 1.00 74.43 N ANISOU 504 N ASP A1066 8544 9603 10133 77 315 290 N ATOM 505 CA ASP A1066 -17.151 66.270 0.602 1.00 76.36 C ANISOU 505 CA ASP A1066 8755 9849 10408 106 388 350 C ATOM 506 C ASP A1066 -17.817 66.574 -0.741 1.00 77.90 C ANISOU 506 C ASP A1066 9027 10035 10535 131 434 317 C ATOM 507 O ASP A1066 -17.312 67.401 -1.504 1.00 78.67 O ANISOU 507 O ASP A1066 9114 10133 10643 133 469 357 O ATOM 508 CB ASP A1066 -16.242 65.041 0.441 1.00 76.86 C ANISOU 508 CB ASP A1066 8783 9910 10509 160 461 395 C ATOM 509 CG ASP A1066 -15.165 64.954 1.504 1.00 79.30 C ANISOU 509 CG ASP A1066 8989 10225 10913 135 422 466 C ATOM 510 OD1 ASP A1066 -14.856 65.973 2.169 1.00 78.10 O ANISOU 510 OD1 ASP A1066 8795 10073 10806 73 341 499 O ATOM 511 OD2 ASP A1066 -14.614 63.847 1.669 1.00 82.64 O ANISOU 511 OD2 ASP A1066 9385 10647 11368 178 463 492 O ATOM 512 N ILE A1067 -18.926 65.889 -1.036 1.00 78.13 N ANISOU 512 N ILE A1067 9136 10051 10498 146 426 252 N ATOM 513 CA ILE A1067 -19.741 66.195 -2.220 1.00 79.55 C ANISOU 513 CA ILE A1067 9404 10210 10610 156 434 217 C ATOM 514 C ILE A1067 -20.287 67.630 -2.125 1.00 80.03 C ANISOU 514 C ILE A1067 9456 10282 10668 114 380 206 C ATOM 515 O ILE A1067 -20.378 68.328 -3.134 1.00 80.35 O ANISOU 515 O ILE A1067 9540 10310 10677 120 398 209 O ATOM 516 CB ILE A1067 -20.879 65.155 -2.429 1.00 80.11 C ANISOU 516 CB ILE A1067 9555 10256 10625 162 403 164 C ATOM 517 CG1 ILE A1067 -20.284 63.801 -2.850 1.00 81.22 C ANISOU 517 CG1 ILE A1067 9748 10367 10744 215 466 174 C ATOM 518 CG2 ILE A1067 -21.868 65.612 -3.498 1.00 79.53 C ANISOU 518 CG2 ILE A1067 9569 10155 10492 154 373 134 C ATOM 519 CD1 ILE A1067 -21.241 62.627 -2.744 1.00 80.31 C ANISOU 519 CD1 ILE A1067 9702 10222 10588 207 416 133 C ATOM 520 N LEU A1068 -20.625 68.065 -0.913 1.00 81.21 N ANISOU 520 N LEU A1068 9564 10448 10843 79 318 196 N ATOM 521 CA LEU A1068 -21.053 69.444 -0.667 1.00 82.16 C ANISOU 521 CA LEU A1068 9689 10569 10956 49 270 190 C ATOM 522 C LEU A1068 -19.928 70.450 -0.916 1.00 83.26 C ANISOU 522 C LEU A1068 9797 10707 11128 30 278 244 C ATOM 523 O LEU A1068 -20.109 71.410 -1.666 1.00 84.68 O ANISOU 523 O LEU A1068 10009 10881 11285 23 277 245 O ATOM 524 CB LEU A1068 -21.572 69.590 0.769 1.00 82.08 C ANISOU 524 CB LEU A1068 9669 10562 10953 31 215 174 C ATOM 525 CG LEU A1068 -22.169 70.939 1.190 1.00 84.01 C ANISOU 525 CG LEU A1068 9947 10797 11175 18 171 163 C ATOM 526 CD1 LEU A1068 -23.119 71.478 0.136 1.00 85.30 C ANISOU 526 CD1 LEU A1068 10145 10959 11304 31 176 141 C ATOM 527 CD2 LEU A1068 -22.880 70.829 2.532 1.00 84.88 C ANISOU 527 CD2 LEU A1068 10075 10900 11274 25 145 146 C ATOM 528 N VAL A1069 -18.774 70.218 -0.292 1.00 83.42 N ANISOU 528 N VAL A1069 9752 10733 11211 16 279 299 N ATOM 529 CA VAL A1069 -17.620 71.124 -0.399 1.00 84.10 C ANISOU 529 CA VAL A1069 9785 10815 11352 -15 271 375 C ATOM 530 C VAL A1069 -17.039 71.132 -1.826 1.00 84.48 C ANISOU 530 C VAL A1069 9825 10867 11406 19 368 417 C ATOM 531 O VAL A1069 -16.658 72.189 -2.327 1.00 85.97 O ANISOU 531 O VAL A1069 10007 11050 11607 -5 366 458 O ATOM 532 CB VAL A1069 -16.538 70.790 0.665 1.00 84.26 C ANISOU 532 CB VAL A1069 9726 10833 11455 -44 232 439 C ATOM 533 CG1 VAL A1069 -15.244 71.568 0.429 1.00 85.74 C ANISOU 533 CG1 VAL A1069 9833 11016 11726 -82 223 545 C ATOM 534 CG2 VAL A1069 -17.066 71.082 2.063 1.00 83.98 C ANISOU 534 CG2 VAL A1069 9734 10776 11397 -81 130 402 C ATOM 535 N GLY A1070 -16.984 69.964 -2.468 1.00 83.90 N ANISOU 535 N GLY A1070 9769 10794 11313 78 452 410 N ATOM 536 CA GLY A1070 -16.604 69.851 -3.879 1.00 83.25 C ANISOU 536 CA GLY A1070 9725 10700 11205 132 559 439 C ATOM 537 C GLY A1070 -17.505 70.627 -4.830 1.00 83.68 C ANISOU 537 C GLY A1070 9879 10736 11179 128 548 390 C ATOM 538 O GLY A1070 -17.030 71.181 -5.820 1.00 84.20 O ANISOU 538 O GLY A1070 9966 10790 11235 145 612 432 O ATOM 539 N GLN A1071 -18.804 70.660 -4.531 1.00 83.54 N ANISOU 539 N GLN A1071 9919 10713 11110 108 470 310 N ATOM 540 CA GLN A1071 -19.769 71.471 -5.288 1.00 83.60 C ANISOU 540 CA GLN A1071 10008 10702 11053 98 436 267 C ATOM 541 C GLN A1071 -19.609 72.975 -5.019 1.00 85.61 C ANISOU 541 C GLN A1071 10233 10964 11331 52 388 289 C ATOM 542 O GLN A1071 -19.786 73.791 -5.925 1.00 85.04 O ANISOU 542 O GLN A1071 10214 10874 11221 50 395 290 O ATOM 543 CB GLN A1071 -21.208 71.014 -4.999 1.00 81.84 C ANISOU 543 CB GLN A1071 9831 10473 10791 92 366 197 C ATOM 544 CG GLN A1071 -21.569 69.710 -5.702 1.00 82.03 C ANISOU 544 CG GLN A1071 9933 10468 10768 129 392 173 C ATOM 545 CD GLN A1071 -22.795 69.011 -5.136 1.00 82.95 C ANISOU 545 CD GLN A1071 10055 10582 10877 112 319 129 C ATOM 546 OE1 GLN A1071 -22.982 67.811 -5.344 1.00 81.76 O ANISOU 546 OE1 GLN A1071 9952 10408 10703 129 323 116 O ATOM 547 NE2 GLN A1071 -23.639 69.753 -4.422 1.00 84.13 N ANISOU 547 NE2 GLN A1071 10161 10753 11050 82 256 114 N ATOM 548 N ILE A1072 -19.281 73.326 -3.776 1.00 87.90 N ANISOU 548 N ILE A1072 10455 11268 11672 13 332 308 N ATOM 549 CA ILE A1072 -19.016 74.719 -3.379 1.00 90.40 C ANISOU 549 CA ILE A1072 10762 11576 12007 -35 270 335 C ATOM 550 C ILE A1072 -17.692 75.225 -3.974 1.00 91.99 C ANISOU 550 C ILE A1072 10911 11776 12262 -54 315 427 C ATOM 551 O ILE A1072 -17.545 76.425 -4.231 1.00 92.49 O ANISOU 551 O ILE A1072 10992 11826 12324 -90 282 452 O ATOM 552 CB ILE A1072 -19.034 74.873 -1.828 1.00 91.08 C ANISOU 552 CB ILE A1072 10827 11659 12120 -70 187 331 C ATOM 553 CG1 ILE A1072 -20.436 74.580 -1.275 1.00 90.67 C ANISOU 553 CG1 ILE A1072 10827 11607 12015 -44 159 255 C ATOM 554 CG2 ILE A1072 -18.617 76.274 -1.387 1.00 92.22 C ANISOU 554 CG2 ILE A1072 10987 11776 12275 -125 110 367 C ATOM 555 CD1 ILE A1072 -20.437 74.092 0.158 1.00 91.78 C ANISOU 555 CD1 ILE A1072 10953 11745 12173 -52 119 248 C ATOM 556 N ASP A1073 -16.738 74.316 -4.190 1.00 94.17 N ANISOU 556 N ASP A1073 11120 12066 12592 -26 395 486 N ATOM 557 CA ASP A1073 -15.482 74.650 -4.880 1.00 96.55 C ANISOU 557 CA ASP A1073 11355 12371 12958 -26 469 593 C ATOM 558 C ASP A1073 -15.717 75.161 -6.301 1.00 97.23 C ANISOU 558 C ASP A1073 11522 12440 12980 3 542 588 C ATOM 559 O ASP A1073 -15.362 76.296 -6.611 1.00 98.34 O ANISOU 559 O ASP A1073 11653 12573 13138 -37 524 637 O ATOM 560 CB ASP A1073 -14.529 73.441 -4.932 1.00 96.99 C ANISOU 560 CB ASP A1073 11331 12442 13077 24 568 660 C ATOM 561 CG ASP A1073 -13.874 73.133 -3.591 1.00 97.31 C ANISOU 561 CG ASP A1073 11264 12495 13213 -18 494 708 C ATOM 562 OD1 ASP A1073 -14.130 73.846 -2.597 1.00 96.31 O ANISOU 562 OD1 ASP A1073 11142 12357 13093 -89 365 688 O ATOM 563 OD2 ASP A1073 -13.087 72.162 -3.537 1.00 99.37 O ANISOU 563 OD2 ASP A1073 11450 12769 13537 24 566 768 O ATOM 564 N ASP A1074 -16.321 74.333 -7.154 1.00 98.11 N ANISOU 564 N ASP A1074 11727 12538 13010 71 612 532 N ATOM 565 CA ASP A1074 -16.497 74.690 -8.574 1.00100.60 C ANISOU 565 CA ASP A1074 12147 12824 13252 108 684 529 C ATOM 566 C ASP A1074 -17.400 75.921 -8.794 1.00 97.15 C ANISOU 566 C ASP A1074 11779 12370 12761 61 593 477 C ATOM 567 O ASP A1074 -17.234 76.638 -9.783 1.00 95.20 O ANISOU 567 O ASP A1074 11588 12101 12481 67 636 503 O ATOM 568 CB ASP A1074 -16.958 73.478 -9.412 1.00102.69 C ANISOU 568 CB ASP A1074 12530 13056 13430 186 758 481 C ATOM 569 CG ASP A1074 -18.431 73.152 -9.238 1.00103.19 C ANISOU 569 CG ASP A1074 12680 13103 13421 173 654 372 C ATOM 570 OD1 ASP A1074 -19.274 73.803 -9.892 1.00103.52 O ANISOU 570 OD1 ASP A1074 12815 13119 13399 159 606 328 O ATOM 571 OD2 ASP A1074 -18.744 72.218 -8.474 1.00105.74 O ANISOU 571 OD2 ASP A1074 12976 13440 13760 176 622 339 O ATOM 572 N ALA A1075 -18.340 76.154 -7.876 1.00 94.82 N ANISOU 572 N ALA A1075 11486 12084 12458 25 478 408 N ATOM 573 CA ALA A1075 -19.135 77.388 -7.868 1.00 93.81 C ANISOU 573 CA ALA A1075 11408 11941 12292 -11 391 370 C ATOM 574 C ALA A1075 -18.278 78.605 -7.506 1.00 93.50 C ANISOU 574 C ALA A1075 11316 11902 12308 -70 357 440 C ATOM 575 O ALA A1075 -18.456 79.677 -8.083 1.00 91.81 O ANISOU 575 O ALA A1075 11156 11667 12061 -90 335 442 O ATOM 576 CB ALA A1075 -20.306 77.264 -6.910 1.00 93.50 C ANISOU 576 CB ALA A1075 11378 11908 12236 -18 301 297 C ATOM 577 N LEU A1076 -17.366 78.434 -6.548 1.00 94.96 N ANISOU 577 N LEU A1076 11400 12104 12577 -104 339 500 N ATOM 578 CA LEU A1076 -16.361 79.464 -6.232 1.00 97.50 C ANISOU 578 CA LEU A1076 11662 12416 12967 -172 295 591 C ATOM 579 C LEU A1076 -15.425 79.744 -7.409 1.00 99.61 C ANISOU 579 C LEU A1076 11897 12682 13266 -165 398 685 C ATOM 580 O LEU A1076 -15.058 80.897 -7.636 1.00101.29 O ANISOU 580 O LEU A1076 12113 12877 13496 -219 360 738 O ATOM 581 CB LEU A1076 -15.523 79.087 -4.998 1.00 97.96 C ANISOU 581 CB LEU A1076 11617 12483 13118 -214 242 651 C ATOM 582 CG LEU A1076 -16.112 79.436 -3.634 1.00 98.44 C ANISOU 582 CG LEU A1076 11723 12523 13157 -252 110 596 C ATOM 583 CD1 LEU A1076 -15.431 78.618 -2.545 1.00100.05 C ANISOU 583 CD1 LEU A1076 11844 12734 13435 -271 77 636 C ATOM 584 CD2 LEU A1076 -15.982 80.928 -3.351 1.00 98.34 C ANISOU 584 CD2 LEU A1076 11762 12465 13136 -323 2 624 C ATOM 585 N LYS A1077 -15.042 78.697 -8.145 1.00100.19 N ANISOU 585 N LYS A1077 11953 12770 13343 -95 531 711 N ATOM 586 CA LYS A1077 -14.191 78.845 -9.339 1.00102.47 C ANISOU 586 CA LYS A1077 12230 13053 13650 -62 664 805 C ATOM 587 C LYS A1077 -14.800 79.815 -10.359 1.00103.67 C ANISOU 587 C LYS A1077 12506 13174 13711 -65 663 767 C ATOM 588 O LYS A1077 -14.077 80.581 -11.000 1.00103.84 O ANISOU 588 O LYS A1077 12505 13185 13763 -84 714 858 O ATOM 589 CB LYS A1077 -13.928 77.485 -10.004 1.00102.58 C ANISOU 589 CB LYS A1077 12260 13070 13643 38 815 815 C ATOM 590 CG LYS A1077 -12.783 77.496 -11.006 1.00103.45 C ANISOU 590 CG LYS A1077 12331 13177 13798 89 982 945 C ATOM 591 CD LYS A1077 -12.738 76.225 -11.840 1.00104.34 C ANISOU 591 CD LYS A1077 12530 13270 13843 210 1140 934 C ATOM 592 CE LYS A1077 -11.741 76.354 -12.983 1.00105.78 C ANISOU 592 CE LYS A1077 12713 13436 14041 280 1330 1061 C ATOM 593 NZ LYS A1077 -11.706 75.140 -13.844 1.00106.20 N ANISOU 593 NZ LYS A1077 12894 13451 14004 414 1493 1049 N ATOM 594 N LEU A1078 -16.126 79.773 -10.489 1.00105.05 N ANISOU 594 N LEU A1078 12801 13330 13782 -47 602 643 N ATOM 595 CA LEU A1078 -16.873 80.699 -11.345 1.00105.68 C ANISOU 595 CA LEU A1078 13004 13375 13774 -52 572 596 C ATOM 596 C LEU A1078 -16.902 82.118 -10.757 1.00107.44 C ANISOU 596 C LEU A1078 13208 13591 14022 -134 455 610 C ATOM 597 O LEU A1078 -16.719 83.097 -11.484 1.00109.73 O ANISOU 597 O LEU A1078 13544 13856 14290 -156 463 644 O ATOM 598 CB LEU A1078 -18.300 80.181 -11.574 1.00104.63 C ANISOU 598 CB LEU A1078 12985 13223 13544 -14 524 476 C ATOM 599 CG LEU A1078 -18.427 78.828 -12.296 1.00105.05 C ANISOU 599 CG LEU A1078 13107 13260 13545 60 616 453 C ATOM 600 CD1 LEU A1078 -19.783 78.183 -12.052 1.00103.85 C ANISOU 600 CD1 LEU A1078 13019 13099 13341 72 528 353 C ATOM 601 CD2 LEU A1078 -18.175 78.981 -13.789 1.00106.79 C ANISOU 601 CD2 LEU A1078 13452 13432 13689 106 716 481 C ATOM 602 N ALA A1079 -17.127 82.219 -9.446 1.00107.99 N ANISOU 602 N ALA A1079 13230 13673 14128 -174 348 584 N ATOM 603 CA ALA A1079 -17.136 83.512 -8.741 1.00109.31 C ANISOU 603 CA ALA A1079 13408 13817 14308 -247 226 595 C ATOM 604 C ALA A1079 -15.761 84.206 -8.663 1.00111.18 C ANISOU 604 C ALA A1079 13558 14046 14637 -320 218 727 C ATOM 605 O ALA A1079 -15.699 85.432 -8.531 1.00113.30 O ANISOU 605 O ALA A1079 13868 14280 14899 -383 129 750 O ATOM 606 CB ALA A1079 -17.716 83.343 -7.343 1.00108.34 C ANISOU 606 CB ALA A1079 13284 13695 14185 -257 126 537 C ATOM 607 N ASN A1080 -14.674 83.432 -8.729 1.00110.75 N ANISOU 607 N ASN A1080 13383 14021 14675 -314 305 823 N ATOM 608 CA ASN A1080 -13.312 83.988 -8.824 1.00110.98 C ANISOU 608 CA ASN A1080 13301 14047 14817 -380 317 979 C ATOM 609 C ASN A1080 -13.027 84.553 -10.218 1.00112.53 C ANISOU 609 C ASN A1080 13532 14233 14991 -362 424 1035 C ATOM 610 O ASN A1080 -12.392 85.603 -10.355 1.00111.80 O ANISOU 610 O ASN A1080 13410 14119 14949 -437 382 1130 O ATOM 611 CB ASN A1080 -12.257 82.927 -8.485 1.00110.02 C ANISOU 611 CB ASN A1080 13023 13961 14815 -363 391 1079 C ATOM 612 CG ASN A1080 -12.376 82.407 -7.062 1.00107.96 C ANISOU 612 CG ASN A1080 12726 13706 14587 -391 278 1042 C ATOM 613 OD1 ASN A1080 -12.865 83.100 -6.168 1.00107.31 O ANISOU 613 OD1 ASN A1080 12710 13590 14471 -451 127 989 O ATOM 614 ND2 ASN A1080 -11.930 81.175 -6.848 1.00105.36 N ANISOU 614 ND2 ASN A1080 12305 13410 14316 -341 356 1070 N ATOM 615 N GLU A1081 -13.490 83.837 -11.241 1.00112.71 N ANISOU 615 N GLU A1081 13631 14261 14932 -265 556 979 N ATOM 616 CA GLU A1081 -13.408 84.289 -12.634 1.00113.91 C ANISOU 616 CA GLU A1081 13863 14391 15027 -231 664 1010 C ATOM 617 C GLU A1081 -14.307 85.499 -12.936 1.00113.47 C ANISOU 617 C GLU A1081 13941 14295 14877 -270 560 933 C ATOM 618 O GLU A1081 -14.021 86.261 -13.858 1.00112.64 O ANISOU 618 O GLU A1081 13882 14165 14750 -280 609 987 O ATOM 619 CB GLU A1081 -13.761 83.137 -13.582 1.00115.20 C ANISOU 619 CB GLU A1081 14114 14549 15105 -115 811 959 C ATOM 620 CG GLU A1081 -12.739 82.004 -13.582 1.00116.65 C ANISOU 620 CG GLU A1081 14186 14762 15372 -54 956 1055 C ATOM 621 CD GLU A1081 -13.283 80.689 -14.122 1.00117.53 C ANISOU 621 CD GLU A1081 14407 14860 15386 55 1052 973 C ATOM 622 OE1 GLU A1081 -12.681 79.641 -13.818 1.00118.36 O ANISOU 622 OE1 GLU A1081 14430 14988 15550 106 1136 1020 O ATOM 623 OE2 GLU A1081 -14.300 80.688 -14.849 1.00119.26 O ANISOU 623 OE2 GLU A1081 14801 15039 15473 88 1036 868 O ATOM 624 N GLY A1082 -15.383 85.663 -12.165 1.00114.61 N ANISOU 624 N GLY A1082 14146 14431 14966 -284 427 815 N ATOM 625 CA GLY A1082 -16.323 86.781 -12.324 1.00114.38 C ANISOU 625 CA GLY A1082 14242 14364 14853 -308 324 741 C ATOM 626 C GLY A1082 -17.534 86.406 -13.160 1.00114.39 C ANISOU 626 C GLY A1082 14373 14349 14739 -233 350 631 C ATOM 627 O GLY A1082 -17.946 87.165 -14.039 1.00115.78 O ANISOU 627 O GLY A1082 14656 14489 14845 -230 344 612 O ATOM 628 N LYS A1083 -18.107 85.239 -12.864 1.00114.13 N ANISOU 628 N LYS A1083 14333 14337 14691 -179 366 564 N ATOM 629 CA LYS A1083 -19.235 84.681 -13.607 1.00113.03 C ANISOU 629 CA LYS A1083 14308 14178 14458 -117 374 474 C ATOM 630 C LYS A1083 -20.398 84.472 -12.633 1.00113.60 C ANISOU 630 C LYS A1083 14374 14263 14524 -112 265 386 C ATOM 631 O LYS A1083 -20.523 83.416 -12.007 1.00115.49 O ANISOU 631 O LYS A1083 14557 14531 14792 -90 276 364 O ATOM 632 CB LYS A1083 -18.822 83.366 -14.280 1.00113.26 C ANISOU 632 CB LYS A1083 14349 14210 14475 -54 502 492 C ATOM 633 CG LYS A1083 -17.551 83.472 -15.112 1.00114.29 C ANISOU 633 CG LYS A1083 14465 14331 14626 -40 642 601 C ATOM 634 CD LYS A1083 -17.277 82.208 -15.916 1.00114.68 C ANISOU 634 CD LYS A1083 14577 14365 14631 46 782 611 C ATOM 635 CE LYS A1083 -18.124 82.135 -17.177 1.00115.40 C ANISOU 635 CE LYS A1083 14874 14388 14585 93 790 546 C ATOM 636 NZ LYS A1083 -17.649 81.070 -18.105 1.00116.48 N ANISOU 636 NZ LYS A1083 15112 14485 14659 183 944 575 N ATOM 637 N VAL A1084 -21.242 85.496 -12.513 1.00112.17 N ANISOU 637 N VAL A1084 14253 14059 14306 -127 170 343 N ATOM 638 CA VAL A1084 -22.287 85.545 -11.486 1.00111.39 C ANISOU 638 CA VAL A1084 14141 13969 14210 -116 80 282 C ATOM 639 C VAL A1084 -23.433 84.603 -11.837 1.00111.14 C ANISOU 639 C VAL A1084 14139 13939 14148 -65 73 222 C ATOM 640 O VAL A1084 -23.732 83.678 -11.084 1.00112.63 O ANISOU 640 O VAL A1084 14266 14156 14369 -48 72 201 O ATOM 641 CB VAL A1084 -22.827 86.986 -11.297 1.00113.05 C ANISOU 641 CB VAL A1084 14418 14147 14389 -132 -6 267 C ATOM 642 CG1 VAL A1084 -23.983 87.027 -10.294 1.00111.66 C ANISOU 642 CG1 VAL A1084 14239 13976 14211 -96 -73 213 C ATOM 643 CG2 VAL A1084 -21.703 87.916 -10.857 1.00114.06 C ANISOU 643 CG2 VAL A1084 14527 14261 14548 -197 -26 333 C ATOM 644 N LYS A1085 -24.050 84.839 -12.992 1.00111.54 N ANISOU 644 N LYS A1085 14288 13952 14138 -48 60 201 N ATOM 645 CA LYS A1085 -25.225 84.073 -13.444 1.00110.02 C ANISOU 645 CA LYS A1085 14138 13744 13918 -15 19 155 C ATOM 646 C LYS A1085 -24.935 82.578 -13.613 1.00106.78 C ANISOU 646 C LYS A1085 13716 13342 13511 3 78 155 C ATOM 647 O LYS A1085 -25.825 81.742 -13.438 1.00102.91 O ANISOU 647 O LYS A1085 13217 12853 13030 18 32 125 O ATOM 648 CB LYS A1085 -25.770 84.657 -14.753 1.00111.50 C ANISOU 648 CB LYS A1085 14453 13874 14035 -10 -17 144 C ATOM 649 CG LYS A1085 -26.341 86.064 -14.610 1.00112.86 C ANISOU 649 CG LYS A1085 14647 14031 14201 -17 -91 138 C ATOM 650 CD LYS A1085 -26.293 86.830 -15.922 1.00115.34 C ANISOU 650 CD LYS A1085 15090 14288 14444 -25 -100 144 C ATOM 651 CE LYS A1085 -26.590 88.307 -15.725 1.00116.01 C ANISOU 651 CE LYS A1085 15199 14357 14521 -35 -160 145 C ATOM 652 NZ LYS A1085 -26.202 89.090 -16.930 1.00116.91 N ANISOU 652 NZ LYS A1085 15433 14420 14567 -52 -148 162 N ATOM 653 N GLU A1086 -23.684 82.259 -13.936 1.00106.03 N ANISOU 653 N GLU A1086 13619 13250 13415 3 180 197 N ATOM 654 CA GLU A1086 -23.221 80.878 -14.050 1.00106.19 C ANISOU 654 CA GLU A1086 13634 13275 13436 32 255 205 C ATOM 655 C GLU A1086 -23.045 80.250 -12.658 1.00104.45 C ANISOU 655 C GLU A1086 13278 13112 13295 24 251 205 C ATOM 656 O GLU A1086 -23.424 79.098 -12.444 1.00103.03 O ANISOU 656 O GLU A1086 13091 12936 13118 44 248 180 O ATOM 657 CB GLU A1086 -21.908 80.814 -14.845 1.00108.30 C ANISOU 657 CB GLU A1086 13937 13528 13684 52 386 267 C ATOM 658 CG GLU A1086 -22.036 81.165 -16.333 1.00110.25 C ANISOU 658 CG GLU A1086 14352 13705 13832 74 414 268 C ATOM 659 CD GLU A1086 -22.091 82.662 -16.647 1.00111.00 C ANISOU 659 CD GLU A1086 14472 13786 13914 38 373 281 C ATOM 660 OE1 GLU A1086 -22.181 83.008 -17.845 1.00110.62 O ANISOU 660 OE1 GLU A1086 14567 13678 13782 54 393 283 O ATOM 661 OE2 GLU A1086 -22.053 83.500 -15.716 1.00112.18 O ANISOU 661 OE2 GLU A1086 14519 13976 14128 -4 317 289 O ATOM 662 N ALA A1087 -22.481 81.018 -11.722 1.00101.93 N ANISOU 662 N ALA A1087 12868 12826 13034 -8 240 234 N ATOM 663 CA ALA A1087 -22.278 80.568 -10.336 1.00 99.37 C ANISOU 663 CA ALA A1087 12434 12543 12776 -19 224 237 C ATOM 664 C ALA A1087 -23.581 80.414 -9.541 1.00 96.30 C ANISOU 664 C ALA A1087 12033 12164 12390 -9 143 181 C ATOM 665 O ALA A1087 -23.687 79.515 -8.703 1.00 96.18 O ANISOU 665 O ALA A1087 11957 12175 12410 0 145 170 O ATOM 666 CB ALA A1087 -21.333 81.517 -9.604 1.00100.44 C ANISOU 666 CB ALA A1087 12508 12691 12963 -66 212 290 C ATOM 667 N GLN A1088 -24.551 81.296 -9.790 1.00 93.19 N ANISOU 667 N GLN A1088 11691 11749 11966 -5 79 155 N ATOM 668 CA GLN A1088 -25.884 81.211 -9.162 1.00 92.41 C ANISOU 668 CA GLN A1088 11573 11658 11879 17 16 122 C ATOM 669 C GLN A1088 -26.606 79.886 -9.438 1.00 90.49 C ANISOU 669 C GLN A1088 11322 11417 11643 33 9 104 C ATOM 670 O GLN A1088 -27.394 79.433 -8.612 1.00 91.75 O ANISOU 670 O GLN A1088 11423 11597 11840 47 -17 96 O ATOM 671 CB GLN A1088 -26.781 82.375 -9.616 1.00 93.44 C ANISOU 671 CB GLN A1088 11762 11759 11980 27 -43 111 C ATOM 672 CG GLN A1088 -26.435 83.719 -8.992 1.00 95.01 C ANISOU 672 CG GLN A1088 11976 11949 12173 17 -60 123 C ATOM 673 CD GLN A1088 -27.202 84.880 -9.611 1.00 97.06 C ANISOU 673 CD GLN A1088 12309 12174 12396 32 -112 115 C ATOM 674 OE1 GLN A1088 -27.285 85.005 -10.835 1.00 97.87 O ANISOU 674 OE1 GLN A1088 12472 12250 12463 24 -120 113 O ATOM 675 NE2 GLN A1088 -27.758 85.745 -8.765 1.00 96.62 N ANISOU 675 NE2 GLN A1088 12263 12109 12340 61 -144 111 N ATOM 676 N ALA A1089 -26.347 79.287 -10.599 1.00 89.13 N ANISOU 676 N ALA A1089 11221 11213 11428 33 31 104 N ATOM 677 CA ALA A1089 -26.913 77.984 -10.960 1.00 89.22 C ANISOU 677 CA ALA A1089 11258 11208 11432 41 11 91 C ATOM 678 C ALA A1089 -26.253 76.829 -10.214 1.00 89.00 C ANISOU 678 C ALA A1089 11168 11212 11436 46 68 95 C ATOM 679 O ALA A1089 -26.936 75.897 -9.785 1.00 88.56 O ANISOU 679 O ALA A1089 11080 11163 11406 47 33 85 O ATOM 680 CB ALA A1089 -26.800 77.757 -12.460 1.00 90.47 C ANISOU 680 CB ALA A1089 11557 11303 11513 45 14 88 C ATOM 681 N ALA A1090 -24.927 76.886 -10.081 1.00 88.71 N ANISOU 681 N ALA A1090 11109 11191 11405 49 152 119 N ATOM 682 CA ALA A1090 -24.158 75.856 -9.374 1.00 87.91 C ANISOU 682 CA ALA A1090 10942 11117 11340 58 210 133 C ATOM 683 C ALA A1090 -24.506 75.754 -7.885 1.00 87.73 C ANISOU 683 C ALA A1090 10817 11137 11377 46 173 124 C ATOM 684 O ALA A1090 -24.436 74.668 -7.306 1.00 85.83 O ANISOU 684 O ALA A1090 10538 10912 11161 53 187 120 O ATOM 685 CB ALA A1090 -22.665 76.104 -9.545 1.00 88.73 C ANISOU 685 CB ALA A1090 11023 11230 11457 61 302 183 C ATOM 686 N ALA A1091 -24.872 76.882 -7.274 1.00 88.47 N ANISOU 686 N ALA A1091 10887 11242 11486 33 130 123 N ATOM 687 CA ALA A1091 -25.267 76.918 -5.859 1.00 86.68 C ANISOU 687 CA ALA A1091 10596 11040 11297 35 104 117 C ATOM 688 C ALA A1091 -26.599 76.209 -5.586 1.00 86.69 C ANISOU 688 C ALA A1091 10577 11047 11312 53 69 98 C ATOM 689 O ALA A1091 -26.844 75.773 -4.459 1.00 87.75 O ANISOU 689 O ALA A1091 10658 11202 11478 62 72 98 O ATOM 690 CB ALA A1091 -25.322 78.354 -5.359 1.00 85.68 C ANISOU 690 CB ALA A1091 10485 10905 11164 29 72 122 C ATOM 691 N GLU A1092 -27.454 76.096 -6.604 1.00 85.69 N ANISOU 691 N GLU A1092 10493 10896 11166 56 30 92 N ATOM 692 CA GLU A1092 -28.722 75.366 -6.470 1.00 86.19 C ANISOU 692 CA GLU A1092 10526 10961 11262 60 -17 95 C ATOM 693 C GLU A1092 -28.559 73.841 -6.395 1.00 85.99 C ANISOU 693 C GLU A1092 10491 10936 11245 49 -8 92 C ATOM 694 O GLU A1092 -29.511 73.146 -6.034 1.00 86.80 O ANISOU 694 O GLU A1092 10549 11043 11387 45 -47 106 O ATOM 695 CB GLU A1092 -29.696 75.740 -7.595 1.00 86.92 C ANISOU 695 CB GLU A1092 10669 11015 11339 54 -89 102 C ATOM 696 CG GLU A1092 -30.124 77.201 -7.566 1.00 87.77 C ANISOU 696 CG GLU A1092 10778 11123 11447 73 -106 109 C ATOM 697 CD GLU A1092 -31.631 77.371 -7.501 1.00 90.40 C ANISOU 697 CD GLU A1092 11060 11454 11833 90 -170 141 C ATOM 698 OE1 GLU A1092 -32.153 77.542 -6.378 1.00 90.07 O ANISOU 698 OE1 GLU A1092 10940 11442 11838 125 -143 162 O ATOM 699 OE2 GLU A1092 -32.294 77.321 -8.563 1.00 92.83 O ANISOU 699 OE2 GLU A1092 11408 11723 12137 71 -246 154 O ATOM 700 N GLN A1093 -27.369 73.326 -6.723 1.00 86.55 N ANISOU 700 N GLN A1093 10600 10999 11285 49 46 85 N ATOM 701 CA GLN A1093 -27.036 71.904 -6.508 1.00 86.43 C ANISOU 701 CA GLN A1093 10581 10982 11273 49 69 82 C ATOM 702 C GLN A1093 -27.025 71.474 -5.041 1.00 86.03 C ANISOU 702 C GLN A1093 10437 10975 11276 51 85 86 C ATOM 703 O GLN A1093 -27.097 70.285 -4.760 1.00 87.66 O ANISOU 703 O GLN A1093 10633 11179 11493 48 84 84 O ATOM 704 CB GLN A1093 -25.669 71.554 -7.106 1.00 86.53 C ANISOU 704 CB GLN A1093 10647 10980 11248 67 147 85 C ATOM 705 CG GLN A1093 -25.606 71.536 -8.621 1.00 86.21 C ANISOU 705 CG GLN A1093 10738 10882 11136 78 151 82 C ATOM 706 CD GLN A1093 -24.300 70.950 -9.127 1.00 89.07 C ANISOU 706 CD GLN A1093 11152 11226 11464 116 254 99 C ATOM 707 OE1 GLN A1093 -23.262 71.066 -8.471 1.00 89.96 O ANISOU 707 OE1 GLN A1093 11179 11378 11621 126 324 126 O ATOM 708 NE2 GLN A1093 -24.342 70.317 -10.300 1.00 89.49 N ANISOU 708 NE2 GLN A1093 11352 11211 11437 141 265 92 N ATOM 709 N LEU A1094 -26.912 72.424 -4.115 1.00 87.07 N ANISOU 709 N LEU A1094 10518 11133 11430 56 96 91 N ATOM 710 CA LEU A1094 -26.928 72.110 -2.682 1.00 88.29 C ANISOU 710 CA LEU A1094 10611 11314 11620 62 110 96 C ATOM 711 C LEU A1094 -28.336 71.812 -2.158 1.00 88.04 C ANISOU 711 C LEU A1094 10539 11291 11621 73 81 107 C ATOM 712 O LEU A1094 -28.479 71.275 -1.055 1.00 89.61 O ANISOU 712 O LEU A1094 10695 11506 11844 81 100 115 O ATOM 713 CB LEU A1094 -26.277 73.239 -1.870 1.00 90.36 C ANISOU 713 CB LEU A1094 10870 11581 11879 65 122 101 C ATOM 714 CG LEU A1094 -24.931 73.798 -2.376 1.00 91.76 C ANISOU 714 CG LEU A1094 11068 11751 12045 46 141 114 C ATOM 715 CD1 LEU A1094 -24.273 74.665 -1.312 1.00 93.52 C ANISOU 715 CD1 LEU A1094 11287 11968 12275 32 125 130 C ATOM 716 CD2 LEU A1094 -23.973 72.709 -2.854 1.00 92.69 C ANISOU 716 CD2 LEU A1094 11173 11870 12172 43 184 125 C ATOM 717 N LYS A1095 -29.363 72.150 -2.941 1.00 86.15 N ANISOU 717 N LYS A1095 10306 11037 11387 72 36 119 N ATOM 718 CA LYS A1095 -30.741 71.775 -2.620 1.00 86.56 C ANISOU 718 CA LYS A1095 10297 11096 11493 77 4 155 C ATOM 719 C LYS A1095 -30.972 70.266 -2.715 1.00 86.15 C ANISOU 719 C LYS A1095 10232 11037 11463 46 -24 164 C ATOM 720 O LYS A1095 -31.693 69.714 -1.886 1.00 88.65 O ANISOU 720 O LYS A1095 10478 11371 11830 49 -20 197 O ATOM 721 CB LYS A1095 -31.742 72.524 -3.509 1.00 87.41 C ANISOU 721 CB LYS A1095 10409 11186 11615 78 -52 180 C ATOM 722 CG LYS A1095 -31.696 74.036 -3.322 1.00 86.82 C ANISOU 722 CG LYS A1095 10350 11115 11521 116 -26 175 C ATOM 723 CD LYS A1095 -32.966 74.737 -3.780 1.00 86.41 C ANISOU 723 CD LYS A1095 10268 11054 11509 136 -72 218 C ATOM 724 CE LYS A1095 -32.932 76.205 -3.376 1.00 86.79 C ANISOU 724 CE LYS A1095 10342 11102 11532 187 -35 213 C ATOM 725 NZ LYS A1095 -34.205 76.924 -3.655 1.00 87.28 N ANISOU 725 NZ LYS A1095 10363 11157 11641 225 -64 265 N ATOM 726 N THR A1096 -30.373 69.603 -3.708 1.00 86.09 N ANISOU 726 N THR A1096 10301 10996 11411 20 -47 141 N ATOM 727 CA THR A1096 -30.485 68.129 -3.820 1.00 87.18 C ANISOU 727 CA THR A1096 10458 11112 11552 -7 -79 145 C ATOM 728 C THR A1096 -29.712 67.403 -2.709 1.00 85.83 C ANISOU 728 C THR A1096 10253 10969 11387 5 -14 132 C ATOM 729 O THR A1096 -30.150 66.348 -2.241 1.00 84.34 O ANISOU 729 O THR A1096 10036 10779 11227 -12 -35 149 O ATOM 730 CB THR A1096 -30.109 67.566 -5.223 1.00 88.01 C ANISOU 730 CB THR A1096 10694 11156 11590 -24 -119 125 C ATOM 731 OG1 THR A1096 -30.238 66.139 -5.217 1.00 89.96 O ANISOU 731 OG1 THR A1096 10975 11371 11832 -48 -155 129 O ATOM 732 CG2 THR A1096 -28.692 67.909 -5.649 1.00 88.43 C ANISOU 732 CG2 THR A1096 10813 11204 11580 7 -37 91 C ATOM 733 N THR A1097 -28.579 67.975 -2.299 1.00 84.50 N ANISOU 733 N THR A1097 10087 10822 11197 30 51 109 N ATOM 734 CA THR A1097 -27.827 67.516 -1.123 1.00 83.18 C ANISOU 734 CA THR A1097 9883 10679 11043 40 100 104 C ATOM 735 C THR A1097 -28.628 67.699 0.169 1.00 81.44 C ANISOU 735 C THR A1097 9596 10484 10863 51 107 125 C ATOM 736 O THR A1097 -28.618 66.829 1.043 1.00 78.61 O ANISOU 736 O THR A1097 9211 10133 10521 49 122 131 O ATOM 737 CB THR A1097 -26.502 68.297 -0.977 1.00 83.84 C ANISOU 737 CB THR A1097 9976 10771 11108 54 145 94 C ATOM 738 OG1 THR A1097 -25.733 68.170 -2.180 1.00 85.31 O ANISOU 738 OG1 THR A1097 10219 10934 11261 57 164 89 O ATOM 739 CG2 THR A1097 -25.679 67.792 0.210 1.00 83.92 C ANISOU 739 CG2 THR A1097 9952 10795 11137 57 174 97 C ATOM 740 N ARG A1098 -29.303 68.841 0.290 1.00 81.88 N ANISOU 740 N ARG A1098 9635 10547 10928 70 107 140 N ATOM 741 CA ARG A1098 -30.114 69.127 1.475 1.00 82.33 C ANISOU 741 CA ARG A1098 9646 10620 11014 102 136 169 C ATOM 742 C ARG A1098 -31.279 68.143 1.550 1.00 80.93 C ANISOU 742 C ARG A1098 9406 10449 10893 88 115 213 C ATOM 743 O ARG A1098 -31.514 67.551 2.605 1.00 83.43 O ANISOU 743 O ARG A1098 9689 10777 11231 100 151 233 O ATOM 744 CB ARG A1098 -30.632 70.573 1.478 1.00 83.82 C ANISOU 744 CB ARG A1098 9844 10808 11197 139 147 181 C ATOM 745 CG ARG A1098 -30.876 71.122 2.873 1.00 85.37 C ANISOU 745 CG ARG A1098 10047 11004 11383 193 205 197 C ATOM 746 CD ARG A1098 -32.029 72.117 2.930 1.00 87.86 C ANISOU 746 CD ARG A1098 10346 11319 11718 249 229 238 C ATOM 747 NE ARG A1098 -31.828 73.313 2.097 1.00 87.82 N ANISOU 747 NE ARG A1098 10386 11298 11681 251 199 219 N ATOM 748 CZ ARG A1098 -32.474 73.601 0.961 1.00 88.68 C ANISOU 748 CZ ARG A1098 10466 11407 11818 240 155 236 C ATOM 749 NH1 ARG A1098 -32.195 74.740 0.329 1.00 89.16 N ANISOU 749 NH1 ARG A1098 10583 11450 11841 245 134 215 N ATOM 750 NH2 ARG A1098 -33.384 72.780 0.432 1.00 89.37 N ANISOU 750 NH2 ARG A1098 10476 11506 11973 216 118 278 N ATOM 751 N ASN A1099 -31.984 67.970 0.427 1.00 76.76 N ANISOU 751 N ASN A1099 8868 9906 10389 58 49 234 N ATOM 752 CA ASN A1099 -33.064 66.978 0.311 1.00 74.44 C ANISOU 752 CA ASN A1099 8516 9607 10161 24 -2 290 C ATOM 753 C ASN A1099 -32.574 65.569 0.656 1.00 71.38 C ANISOU 753 C ASN A1099 8147 9211 9763 -6 -6 274 C ATOM 754 O ASN A1099 -33.170 64.883 1.493 1.00 71.95 O ANISOU 754 O ASN A1099 8157 9296 9884 -11 7 318 O ATOM 755 CB ASN A1099 -33.654 66.964 -1.108 1.00 75.62 C ANISOU 755 CB ASN A1099 8690 9720 10321 -19 -104 308 C ATOM 756 CG ASN A1099 -34.378 68.257 -1.474 1.00 76.24 C ANISOU 756 CG ASN A1099 8734 9804 10427 8 -115 340 C ATOM 757 OD1 ASN A1099 -35.092 68.850 -0.665 1.00 74.73 O ANISOU 757 OD1 ASN A1099 8460 9643 10289 54 -62 389 O ATOM 758 ND2 ASN A1099 -34.201 68.689 -2.717 1.00 77.88 N ANISOU 758 ND2 ASN A1099 9018 9978 10595 -12 -177 315 N ATOM 759 N ALA A1100 -31.482 65.160 0.011 1.00 68.09 N ANISOU 759 N ALA A1100 7818 8770 9282 -20 -17 219 N ATOM 760 CA ALA A1100 -30.820 63.873 0.278 1.00 66.38 C ANISOU 760 CA ALA A1100 7637 8539 9044 -36 -12 198 C ATOM 761 C ALA A1100 -30.498 63.687 1.751 1.00 66.00 C ANISOU 761 C ALA A1100 7543 8523 9010 -11 55 198 C ATOM 762 O ALA A1100 -30.687 62.603 2.298 1.00 66.98 O ANISOU 762 O ALA A1100 7652 8644 9153 -30 48 214 O ATOM 763 CB ALA A1100 -29.540 63.757 -0.534 1.00 65.46 C ANISOU 763 CB ALA A1100 7615 8396 8857 -26 2 147 C ATOM 764 N TYR A1101 -30.013 64.751 2.384 1.00 66.11 N ANISOU 764 N TYR A1101 7550 8558 9008 26 111 183 N ATOM 765 CA TYR A1101 -29.635 64.710 3.791 1.00 66.45 C ANISOU 765 CA TYR A1101 7582 8616 9049 51 165 181 C ATOM 766 C TYR A1101 -30.845 64.525 4.727 1.00 69.66 C ANISOU 766 C TYR A1101 7930 9036 9501 67 193 234 C ATOM 767 O TYR A1101 -30.798 63.660 5.613 1.00 70.13 O ANISOU 767 O TYR A1101 7983 9096 9567 64 214 244 O ATOM 768 CB TYR A1101 -28.830 65.959 4.172 1.00 65.68 C ANISOU 768 CB TYR A1101 7519 8519 8915 81 195 157 C ATOM 769 CG TYR A1101 -28.468 66.010 5.631 1.00 66.39 C ANISOU 769 CG TYR A1101 7630 8606 8989 104 231 157 C ATOM 770 CD1 TYR A1101 -27.364 65.309 6.122 1.00 66.03 C ANISOU 770 CD1 TYR A1101 7605 8550 8930 89 225 138 C ATOM 771 CD2 TYR A1101 -29.247 66.740 6.537 1.00 67.42 C ANISOU 771 CD2 TYR A1101 7769 8733 9114 148 274 183 C ATOM 772 CE1 TYR A1101 -27.039 65.344 7.473 1.00 66.80 C ANISOU 772 CE1 TYR A1101 7740 8632 9008 104 242 139 C ATOM 773 CE2 TYR A1101 -28.932 66.776 7.889 1.00 68.14 C ANISOU 773 CE2 TYR A1101 7914 8802 9171 174 305 182 C ATOM 774 CZ TYR A1101 -27.830 66.081 8.353 1.00 67.62 C ANISOU 774 CZ TYR A1101 7876 8724 9091 146 280 159 C ATOM 775 OH TYR A1101 -27.527 66.129 9.693 1.00 69.35 O ANISOU 775 OH TYR A1101 8166 8910 9271 166 295 160 O ATOM 776 N ILE A1102 -31.917 65.307 4.539 1.00 71.02 N ANISOU 776 N ILE A1102 8057 9219 9710 88 199 279 N ATOM 777 CA ILE A1102 -33.092 65.186 5.427 1.00 73.27 C ANISOU 777 CA ILE A1102 8270 9517 10049 118 249 351 C ATOM 778 C ILE A1102 -33.705 63.782 5.395 1.00 73.43 C ANISOU 778 C ILE A1102 8233 9537 10129 66 210 398 C ATOM 779 O ILE A1102 -34.077 63.248 6.440 1.00 72.75 O ANISOU 779 O ILE A1102 8115 9459 10066 82 264 438 O ATOM 780 CB ILE A1102 -34.196 66.276 5.218 1.00 74.84 C ANISOU 780 CB ILE A1102 8413 9727 10292 162 273 410 C ATOM 781 CG1 ILE A1102 -34.884 66.187 3.849 1.00 77.56 C ANISOU 781 CG1 ILE A1102 8707 10068 10694 111 179 442 C ATOM 782 CG2 ILE A1102 -33.624 67.675 5.419 1.00 75.26 C ANISOU 782 CG2 ILE A1102 8544 9772 10279 217 314 366 C ATOM 783 CD1 ILE A1102 -36.159 67.005 3.763 1.00 79.20 C ANISOU 783 CD1 ILE A1102 8826 10288 10976 153 199 528 C ATOM 784 N GLN A1103 -33.777 63.190 4.202 1.00 75.17 N ANISOU 784 N GLN A1103 8458 9739 10363 4 114 393 N ATOM 785 CA GLN A1103 -34.320 61.835 4.014 1.00 76.43 C ANISOU 785 CA GLN A1103 8588 9881 10570 -59 47 437 C ATOM 786 C GLN A1103 -33.563 60.785 4.814 1.00 75.06 C ANISOU 786 C GLN A1103 8458 9702 10360 -66 74 402 C ATOM 787 O GLN A1103 -34.175 59.887 5.399 1.00 74.83 O ANISOU 787 O GLN A1103 8380 9672 10379 -91 72 457 O ATOM 788 CB GLN A1103 -34.297 61.444 2.526 1.00 78.58 C ANISOU 788 CB GLN A1103 8917 10111 10828 -120 -71 420 C ATOM 789 CG GLN A1103 -35.402 62.081 1.694 1.00 80.01 C ANISOU 789 CG GLN A1103 9041 10285 11074 -141 -140 485 C ATOM 790 CD GLN A1103 -36.750 61.405 1.893 1.00 81.82 C ANISOU 790 CD GLN A1103 9156 10511 11418 -191 -198 602 C ATOM 791 OE1 GLN A1103 -36.848 60.179 1.846 1.00 83.27 O ANISOU 791 OE1 GLN A1103 9360 10663 11612 -253 -267 621 O ATOM 792 NE2 GLN A1103 -37.797 62.200 2.108 1.00 82.94 N ANISOU 792 NE2 GLN A1103 9177 10684 11652 -162 -171 691 N ATOM 793 N LYS A1104 -32.238 60.917 4.844 1.00 74.65 N ANISOU 793 N LYS A1104 8488 9643 10231 -44 98 321 N ATOM 794 CA LYS A1104 -31.352 59.905 5.432 1.00 74.85 C ANISOU 794 CA LYS A1104 8562 9656 10220 -50 111 285 C ATOM 795 C LYS A1104 -31.187 59.989 6.951 1.00 73.63 C ANISOU 795 C LYS A1104 8397 9519 10060 -11 189 291 C ATOM 796 O LYS A1104 -31.002 58.952 7.591 1.00 74.08 O ANISOU 796 O LYS A1104 8466 9565 10113 -26 192 293 O ATOM 797 CB LYS A1104 -29.975 59.994 4.777 1.00 75.85 C ANISOU 797 CB LYS A1104 8768 9768 10283 -39 104 215 C ATOM 798 CG LYS A1104 -29.078 58.792 5.022 1.00 75.94 C ANISOU 798 CG LYS A1104 8830 9758 10265 -46 100 186 C ATOM 799 CD LYS A1104 -27.865 58.839 4.103 1.00 75.79 C ANISOU 799 CD LYS A1104 8877 9719 10198 -28 101 141 C ATOM 800 CE LYS A1104 -27.169 57.493 4.008 1.00 75.47 C ANISOU 800 CE LYS A1104 8897 9647 10131 -28 92 124 C ATOM 801 NZ LYS A1104 -26.531 57.319 2.677 1.00 74.32 N ANISOU 801 NZ LYS A1104 8835 9464 9938 -10 86 101 N ATOM 802 N TYR A1105 -31.219 61.205 7.513 1.00 72.93 N ANISOU 802 N TYR A1105 8307 9445 9957 39 249 292 N ATOM 803 CA TYR A1105 -30.955 61.435 8.953 1.00 71.34 C ANISOU 803 CA TYR A1105 8140 9239 9724 84 319 291 C ATOM 804 C TYR A1105 -32.053 62.143 9.749 1.00 71.71 C ANISOU 804 C TYR A1105 8159 9295 9791 140 400 353 C ATOM 805 O TYR A1105 -32.055 62.061 10.978 1.00 72.28 O ANISOU 805 O TYR A1105 8275 9353 9835 178 464 366 O ATOM 806 CB TYR A1105 -29.683 62.266 9.135 1.00 70.76 C ANISOU 806 CB TYR A1105 8144 9151 9589 104 316 233 C ATOM 807 CG TYR A1105 -28.453 61.754 8.420 1.00 70.41 C ANISOU 807 CG TYR A1105 8122 9100 9530 69 262 185 C ATOM 808 CD1 TYR A1105 -27.614 60.817 9.014 1.00 70.31 C ANISOU 808 CD1 TYR A1105 8137 9072 9503 57 252 168 C ATOM 809 CD2 TYR A1105 -28.113 62.234 7.158 1.00 70.76 C ANISOU 809 CD2 TYR A1105 8163 9149 9573 57 231 165 C ATOM 810 CE1 TYR A1105 -26.479 60.357 8.363 1.00 70.97 C ANISOU 810 CE1 TYR A1105 8233 9148 9581 42 220 139 C ATOM 811 CE2 TYR A1105 -26.976 61.789 6.498 1.00 70.98 C ANISOU 811 CE2 TYR A1105 8213 9168 9588 43 206 136 C ATOM 812 CZ TYR A1105 -26.161 60.851 7.101 1.00 71.20 C ANISOU 812 CZ TYR A1105 8258 9184 9611 39 205 126 C ATOM 813 OH TYR A1105 -25.035 60.410 6.446 1.00 70.19 O ANISOU 813 OH TYR A1105 8144 9046 9477 40 197 111 O ATOM 814 N LEU A1106 -32.964 62.848 9.081 1.00 71.71 N ANISOU 814 N LEU A1106 8096 9311 9837 154 403 396 N ATOM 815 CA LEU A1106 -33.893 63.753 9.767 1.00 72.21 C ANISOU 815 CA LEU A1106 8141 9380 9915 231 498 458 C ATOM 816 C LEU A1106 -35.381 63.366 9.660 1.00 74.31 C ANISOU 816 C LEU A1106 8274 9671 10289 232 525 571 C ATOM 817 O LEU A1106 -36.244 64.159 10.047 1.00 75.81 O ANISOU 817 O LEU A1106 8428 9868 10507 306 612 639 O ATOM 818 CB LEU A1106 -33.650 65.192 9.280 1.00 71.24 C ANISOU 818 CB LEU A1106 8062 9252 9753 268 496 425 C ATOM 819 CG LEU A1106 -32.744 66.074 10.140 1.00 71.12 C ANISOU 819 CG LEU A1106 8182 9200 9638 317 531 370 C ATOM 820 CD1 LEU A1106 -31.395 65.426 10.406 1.00 70.86 C ANISOU 820 CD1 LEU A1106 8216 9148 9557 267 475 304 C ATOM 821 CD2 LEU A1106 -32.561 67.420 9.459 1.00 71.97 C ANISOU 821 CD2 LEU A1106 8325 9301 9718 338 509 344 C ATOM 822 N ILE A 12 -35.681 62.159 9.170 1.00 75.09 N ANISOU 822 N ILE A 12 8764 9899 9864 321 471 -284 N ATOM 823 CA ILE A 12 -37.062 61.650 9.122 1.00 77.24 C ANISOU 823 CA ILE A 12 9083 10110 10154 314 467 -293 C ATOM 824 C ILE A 12 -37.219 60.488 10.105 1.00 80.04 C ANISOU 824 C ILE A 12 9489 10403 10517 353 467 -329 C ATOM 825 O ILE A 12 -36.463 59.520 10.040 1.00 79.81 O ANISOU 825 O ILE A 12 9472 10389 10461 403 472 -362 O ATOM 826 CB ILE A 12 -37.471 61.222 7.690 1.00 76.53 C ANISOU 826 CB ILE A 12 8988 10060 10028 308 473 -305 C ATOM 827 CG1 ILE A 12 -37.581 62.462 6.795 1.00 76.11 C ANISOU 827 CG1 ILE A 12 8892 10056 9968 262 470 -259 C ATOM 828 CG2 ILE A 12 -38.795 60.454 7.701 1.00 76.77 C ANISOU 828 CG2 ILE A 12 9067 10036 10065 300 471 -327 C ATOM 829 CD1 ILE A 12 -37.904 62.179 5.345 1.00 76.51 C ANISOU 829 CD1 ILE A 12 8928 10163 9980 252 475 -265 C ATOM 830 N LEU A 13 -38.206 60.595 11.001 1.00 84.19 N ANISOU 830 N LEU A 13 10048 10862 11078 333 460 -322 N ATOM 831 CA LEU A 13 -38.528 59.540 11.971 1.00 88.87 C ANISOU 831 CA LEU A 13 10697 11391 11679 358 458 -350 C ATOM 832 C LEU A 13 -39.347 58.455 11.281 1.00 93.11 C ANISOU 832 C LEU A 13 11279 11906 12193 355 464 -381 C ATOM 833 O LEU A 13 -40.356 58.766 10.643 1.00 95.20 O ANISOU 833 O LEU A 13 11537 12178 12456 314 463 -373 O ATOM 834 CB LEU A 13 -39.321 60.117 13.151 1.00 90.47 C ANISOU 834 CB LEU A 13 10910 11542 11921 329 450 -331 C ATOM 835 CG LEU A 13 -39.474 59.258 14.423 1.00 91.94 C ANISOU 835 CG LEU A 13 11147 11668 12117 348 447 -350 C ATOM 836 CD1 LEU A 13 -39.781 60.139 15.629 1.00 91.06 C ANISOU 836 CD1 LEU A 13 11022 11533 12042 325 439 -328 C ATOM 837 CD2 LEU A 13 -40.529 58.161 14.282 1.00 91.98 C ANISOU 837 CD2 LEU A 13 11212 11627 12109 335 450 -375 C ATOM 838 N ASN A 14 -38.916 57.196 11.419 1.00 96.15 N ANISOU 838 N ASN A 14 11711 12263 12556 399 469 -417 N ATOM 839 CA ASN A 14 -39.583 56.053 10.769 1.00 96.38 C ANISOU 839 CA ASN A 14 11796 12264 12559 395 476 -454 C ATOM 840 C ASN A 14 -41.049 55.916 11.191 1.00 96.59 C ANISOU 840 C ASN A 14 11860 12240 12600 338 473 -453 C ATOM 841 O ASN A 14 -41.354 55.723 12.374 1.00 95.74 O ANISOU 841 O ASN A 14 11786 12077 12512 333 468 -449 O ATOM 842 CB ASN A 14 -38.841 54.738 11.055 1.00 97.00 C ANISOU 842 CB ASN A 14 11935 12303 12615 459 481 -491 C ATOM 843 CG ASN A 14 -37.553 54.604 10.259 1.00 97.05 C ANISOU 843 CG ASN A 14 11907 12377 12591 518 487 -507 C ATOM 844 OD1 ASN A 14 -37.560 54.678 9.029 1.00 97.28 O ANISOU 844 OD1 ASN A 14 11908 12459 12595 506 494 -519 O ATOM 845 ND2 ASN A 14 -36.443 54.389 10.957 1.00 96.87 N ANISOU 845 ND2 ASN A 14 11881 12359 12563 583 484 -509 N ATOM 846 N SER A 15 -41.939 56.018 10.205 1.00 95.77 N ANISOU 846 N SER A 15 11743 12164 12478 294 476 -458 N ATOM 847 CA SER A 15 -43.384 56.042 10.428 1.00 92.99 C ANISOU 847 CA SER A 15 11406 11792 12130 235 473 -457 C ATOM 848 C SER A 15 -43.898 54.791 11.143 1.00 90.97 C ANISOU 848 C SER A 15 11234 11464 11865 221 477 -490 C ATOM 849 O SER A 15 -43.608 53.665 10.720 1.00 90.95 O ANISOU 849 O SER A 15 11287 11433 11834 238 487 -527 O ATOM 850 CB SER A 15 -44.109 56.180 9.085 1.00 93.06 C ANISOU 850 CB SER A 15 11387 11860 12111 198 477 -464 C ATOM 851 OG SER A 15 -43.726 55.139 8.199 1.00 91.27 O ANISOU 851 OG SER A 15 11193 11637 11845 213 489 -505 O ATOM 852 N SER A 16 -44.655 55.002 12.221 1.00 86.75 N ANISOU 852 N SER A 16 10710 10897 11351 189 470 -476 N ATOM 853 CA SER A 16 -45.393 53.924 12.883 1.00 84.58 C ANISOU 853 CA SER A 16 10512 10561 11062 154 474 -501 C ATOM 854 C SER A 16 -46.560 53.483 12.014 1.00 81.77 C ANISOU 854 C SER A 16 10168 10229 10671 89 481 -528 C ATOM 855 O SER A 16 -46.944 54.176 11.070 1.00 82.83 O ANISOU 855 O SER A 16 10241 10433 10796 72 480 -519 O ATOM 856 CB SER A 16 -45.942 54.385 14.237 1.00 83.88 C ANISOU 856 CB SER A 16 10418 10450 11001 130 465 -479 C ATOM 857 OG SER A 16 -44.952 55.050 14.995 1.00 85.82 O ANISOU 857 OG SER A 16 10635 10692 11280 181 457 -452 O ATOM 858 N ASP A 17 -47.137 52.340 12.355 1.00 79.09 N ANISOU 858 N ASP A 17 9908 9835 10306 48 488 -558 N ATOM 859 CA ASP A 17 -48.345 51.864 11.686 1.00 78.94 C ANISOU 859 CA ASP A 17 9903 9842 10247 -28 496 -587 C ATOM 860 C ASP A 17 -49.546 52.748 12.035 1.00 78.12 C ANISOU 860 C ASP A 17 9736 9797 10148 -81 488 -566 C ATOM 861 O ASP A 17 -50.389 53.010 11.172 1.00 77.75 O ANISOU 861 O ASP A 17 9645 9821 10073 -123 489 -574 O ATOM 862 CB ASP A 17 -48.625 50.406 12.052 1.00 80.47 C ANISOU 862 CB ASP A 17 10208 9954 10410 -67 507 -625 C ATOM 863 CG ASP A 17 -47.511 49.480 11.615 1.00 80.83 C ANISOU 863 CG ASP A 17 10324 9941 10447 -6 516 -651 C ATOM 864 OD1 ASP A 17 -47.461 49.128 10.418 1.00 81.63 O ANISOU 864 OD1 ASP A 17 10427 10069 10519 -10 526 -683 O ATOM 865 OD2 ASP A 17 -46.677 49.118 12.468 1.00 81.01 O ANISOU 865 OD2 ASP A 17 10395 9895 10487 50 512 -641 O ATOM 866 N CYS A 18 -49.606 53.204 13.292 1.00 77.46 N ANISOU 866 N CYS A 18 9644 9690 10095 -75 478 -541 N ATOM 867 CA CYS A 18 -50.650 54.109 13.781 1.00 77.43 C ANISOU 867 CA CYS A 18 9579 9740 10099 -110 469 -522 C ATOM 868 C CYS A 18 -50.062 55.514 14.022 1.00 74.12 C ANISOU 868 C CYS A 18 9089 9346 9727 -50 456 -480 C ATOM 869 O CYS A 18 -49.721 55.852 15.155 1.00 74.81 O ANISOU 869 O CYS A 18 9178 9399 9845 -28 450 -463 O ATOM 870 CB CYS A 18 -51.269 53.555 15.081 1.00 81.14 C ANISOU 870 CB CYS A 18 10096 10168 10562 -157 468 -529 C ATOM 871 SG CYS A 18 -51.398 51.752 15.205 1.00 86.15 S ANISOU 871 SG CYS A 18 10856 10723 11154 -212 483 -569 S ATOM 872 N PRO A 19 -49.922 56.337 12.957 1.00 72.09 N ANISOU 872 N PRO A 19 8772 9147 9472 -26 454 -464 N ATOM 873 CA PRO A 19 -49.341 57.680 13.152 1.00 69.93 C ANISOU 873 CA PRO A 19 8441 8887 9239 22 443 -424 C ATOM 874 C PRO A 19 -50.229 58.655 13.929 1.00 68.42 C ANISOU 874 C PRO A 19 8208 8720 9067 11 432 -405 C ATOM 875 O PRO A 19 -49.762 59.276 14.880 1.00 67.51 O ANISOU 875 O PRO A 19 8086 8575 8990 38 426 -387 O ATOM 876 CB PRO A 19 -49.116 58.184 11.718 1.00 69.60 C ANISOU 876 CB PRO A 19 8357 8902 9184 37 444 -412 C ATOM 877 CG PRO A 19 -50.024 57.375 10.870 1.00 69.81 C ANISOU 877 CG PRO A 19 8395 8967 9161 -10 451 -444 C ATOM 878 CD PRO A 19 -50.117 56.036 11.527 1.00 71.19 C ANISOU 878 CD PRO A 19 8646 9080 9320 -42 461 -481 C ATOM 879 N LYS A 20 -51.499 58.764 13.540 1.00 69.10 N ANISOU 879 N LYS A 20 8265 8865 9123 -26 430 -414 N ATOM 880 CA LYS A 20 -52.415 59.758 14.116 1.00 68.59 C ANISOU 880 CA LYS A 20 8151 8838 9069 -25 418 -398 C ATOM 881 C LYS A 20 -52.875 59.440 15.545 1.00 69.17 C ANISOU 881 C LYS A 20 8247 8884 9149 -51 417 -413 C ATOM 882 O LYS A 20 -53.433 60.316 16.213 1.00 68.29 O ANISOU 882 O LYS A 20 8097 8796 9054 -39 407 -402 O ATOM 883 CB LYS A 20 -53.644 59.953 13.218 1.00 68.92 C ANISOU 883 CB LYS A 20 8148 8969 9069 -50 415 -404 C ATOM 884 CG LYS A 20 -53.343 60.438 11.801 1.00 69.53 C ANISOU 884 CG LYS A 20 8193 9087 9136 -24 414 -383 C ATOM 885 CD LYS A 20 -52.669 61.803 11.789 1.00 69.60 C ANISOU 885 CD LYS A 20 8174 9081 9190 35 403 -337 C ATOM 886 CE LYS A 20 -52.812 62.493 10.441 1.00 69.16 C ANISOU 886 CE LYS A 20 8076 9087 9114 55 398 -309 C ATOM 887 NZ LYS A 20 -52.348 61.648 9.311 1.00 69.27 N ANISOU 887 NZ LYS A 20 8104 9120 9096 35 409 -325 N ATOM 888 N ALA A 21 -52.662 58.201 16.003 1.00 69.77 N ANISOU 888 N ALA A 21 8387 8912 9210 -85 426 -438 N ATOM 889 CA ALA A 21 -52.974 57.793 17.379 1.00 70.12 C ANISOU 889 CA ALA A 21 8460 8925 9256 -114 426 -448 C ATOM 890 C ALA A 21 -52.525 58.846 18.383 1.00 69.74 C ANISOU 890 C ALA A 21 8382 8859 9255 -68 416 -424 C ATOM 891 O ALA A 21 -51.348 59.212 18.389 1.00 70.73 O ANISOU 891 O ALA A 21 8512 8945 9415 -19 415 -405 O ATOM 892 CB ALA A 21 -52.296 56.470 17.696 1.00 71.95 C ANISOU 892 CB ALA A 21 8777 9081 9477 -130 436 -463 C ATOM 893 N GLY A 22 -53.462 59.335 19.203 1.00 68.49 N ANISOU 893 N GLY A 22 8190 8737 9095 -86 409 -428 N ATOM 894 CA GLY A 22 -53.182 60.362 20.218 1.00 68.09 C ANISOU 894 CA GLY A 22 8110 8673 9086 -48 401 -413 C ATOM 895 C GLY A 22 -53.567 61.787 19.833 1.00 68.66 C ANISOU 895 C GLY A 22 8120 8790 9178 -6 391 -396 C ATOM 896 O GLY A 22 -53.741 62.641 20.707 1.00 64.97 O ANISOU 896 O GLY A 22 7626 8324 8734 15 383 -393 O ATOM 897 N ARG A 23 -53.695 62.050 18.531 1.00 71.42 N ANISOU 897 N ARG A 23 8448 9172 9514 6 390 -385 N ATOM 898 CA ARG A 23 -54.065 63.378 18.034 1.00 72.26 C ANISOU 898 CA ARG A 23 8504 9316 9634 51 380 -363 C ATOM 899 C ARG A 23 -55.550 63.655 18.244 1.00 73.34 C ANISOU 899 C ARG A 23 8595 9530 9739 39 373 -380 C ATOM 900 O ARG A 23 -56.381 63.280 17.414 1.00 75.81 O ANISOU 900 O ARG A 23 8886 9909 10006 15 373 -389 O ATOM 901 CB ARG A 23 -53.703 63.520 16.550 1.00 72.32 C ANISOU 901 CB ARG A 23 8504 9339 9632 67 381 -343 C ATOM 902 CG ARG A 23 -52.211 63.401 16.291 1.00 72.55 C ANISOU 902 CG ARG A 23 8566 9308 9689 85 387 -327 C ATOM 903 CD ARG A 23 -51.793 63.955 14.941 1.00 72.83 C ANISOU 903 CD ARG A 23 8584 9364 9722 110 385 -298 C ATOM 904 NE ARG A 23 -50.423 64.476 14.991 1.00 74.25 N ANISOU 904 NE ARG A 23 8776 9495 9938 137 387 -275 N ATOM 905 CZ ARG A 23 -50.058 65.654 15.506 1.00 74.02 C ANISOU 905 CZ ARG A 23 8738 9439 9947 165 380 -251 C ATOM 906 NH1 ARG A 23 -50.950 66.484 16.041 1.00 72.79 N ANISOU 906 NH1 ARG A 23 8563 9292 9802 180 371 -248 N ATOM 907 NH2 ARG A 23 -48.776 66.011 15.487 1.00 76.33 N ANISOU 907 NH2 ARG A 23 9041 9697 10263 177 384 -234 N ATOM 908 N HIS A 24 -55.869 64.289 19.372 1.00 73.61 N ANISOU 908 N HIS A 24 8612 9561 9792 57 366 -386 N ATOM 909 CA HIS A 24 -57.224 64.754 19.669 1.00 75.21 C ANISOU 909 CA HIS A 24 8763 9845 9967 62 358 -402 C ATOM 910 C HIS A 24 -57.177 66.217 20.082 1.00 77.12 C ANISOU 910 C HIS A 24 8981 10070 10249 133 347 -387 C ATOM 911 O HIS A 24 -56.231 66.651 20.749 1.00 75.77 O ANISOU 911 O HIS A 24 8837 9826 10126 152 348 -377 O ATOM 912 CB HIS A 24 -57.850 63.928 20.786 1.00 75.19 C ANISOU 912 CB HIS A 24 8764 9867 9936 4 363 -437 C ATOM 913 CG HIS A 24 -57.979 62.476 20.460 1.00 75.80 C ANISOU 913 CG HIS A 24 8877 9951 9969 -72 375 -454 C ATOM 914 ND1 HIS A 24 -58.528 62.024 19.280 1.00 77.01 N ANISOU 914 ND1 HIS A 24 9018 10163 10079 -98 378 -460 N ATOM 915 CD2 HIS A 24 -57.643 61.371 21.166 1.00 76.37 C ANISOU 915 CD2 HIS A 24 9002 9979 10033 -128 384 -468 C ATOM 916 CE1 HIS A 24 -58.517 60.703 19.268 1.00 77.77 C ANISOU 916 CE1 HIS A 24 9161 10242 10142 -171 390 -480 C ATOM 917 NE2 HIS A 24 -57.984 60.282 20.401 1.00 77.84 N ANISOU 917 NE2 HIS A 24 9215 10186 10173 -188 394 -483 N ATOM 918 N ASN A 25 -58.216 66.959 19.705 1.00 77.67 N ANISOU 918 N ASN A 25 9002 10211 10297 171 336 -386 N ATOM 919 CA ASN A 25 -58.231 68.419 19.845 1.00 77.46 C ANISOU 919 CA ASN A 25 8961 10163 10305 249 324 -368 C ATOM 920 C ASN A 25 -58.165 68.880 21.299 1.00 76.46 C ANISOU 920 C ASN A 25 8838 10004 10209 262 323 -390 C ATOM 921 O ASN A 25 -57.390 69.781 21.631 1.00 78.82 O ANISOU 921 O ASN A 25 9162 10229 10557 300 321 -374 O ATOM 922 CB ASN A 25 -59.456 69.014 19.147 1.00 78.31 C ANISOU 922 CB ASN A 25 9016 10364 10373 296 312 -365 C ATOM 923 CG ASN A 25 -59.452 68.759 17.645 1.00 80.54 C ANISOU 923 CG ASN A 25 9293 10679 10627 292 312 -338 C ATOM 924 OD1 ASN A 25 -58.632 69.317 16.905 1.00 79.41 O ANISOU 924 OD1 ASN A 25 9177 10479 10514 322 310 -299 O ATOM 925 ND2 ASN A 25 -60.370 67.912 17.186 1.00 82.15 N ANISOU 925 ND2 ASN A 25 9461 10981 10770 249 314 -360 N ATOM 926 N TYR A 26 -58.955 68.248 22.164 1.00 74.69 N ANISOU 926 N TYR A 26 8589 9837 9951 223 326 -427 N ATOM 927 CA TYR A 26 -58.945 68.570 23.598 1.00 73.57 C ANISOU 927 CA TYR A 26 8445 9677 9830 227 326 -452 C ATOM 928 C TYR A 26 -57.583 68.385 24.282 1.00 73.44 C ANISOU 928 C TYR A 26 8479 9562 9860 205 334 -443 C ATOM 929 O TYR A 26 -57.271 69.123 25.214 1.00 74.11 O ANISOU 929 O TYR A 26 8568 9610 9979 232 332 -453 O ATOM 930 CB TYR A 26 -60.033 67.804 24.363 1.00 73.39 C ANISOU 930 CB TYR A 26 8385 9745 9754 176 328 -492 C ATOM 931 CG TYR A 26 -59.922 66.294 24.347 1.00 72.68 C ANISOU 931 CG TYR A 26 8323 9661 9630 84 340 -499 C ATOM 932 CD1 TYR A 26 -59.089 65.622 25.241 1.00 72.96 C ANISOU 932 CD1 TYR A 26 8405 9631 9685 40 348 -501 C ATOM 933 CD2 TYR A 26 -60.681 65.534 23.459 1.00 72.43 C ANISOU 933 CD2 TYR A 26 8273 9703 9542 41 343 -505 C ATOM 934 CE1 TYR A 26 -59.006 64.235 25.236 1.00 73.53 C ANISOU 934 CE1 TYR A 26 8514 9699 9726 -37 359 -506 C ATOM 935 CE2 TYR A 26 -60.601 64.153 23.444 1.00 72.39 C ANISOU 935 CE2 TYR A 26 8306 9694 9505 -45 354 -514 C ATOM 936 CZ TYR A 26 -59.766 63.507 24.332 1.00 73.80 C ANISOU 936 CZ TYR A 26 8538 9795 9707 -82 362 -514 C ATOM 937 OH TYR A 26 -59.695 62.133 24.307 1.00 77.49 O ANISOU 937 OH TYR A 26 9053 10247 10140 -162 373 -521 O ATOM 938 N ILE A 27 -56.784 67.424 23.814 1.00 71.99 N ANISOU 938 N ILE A 27 8334 9341 9676 161 343 -428 N ATOM 939 CA ILE A 27 -55.405 67.225 24.300 1.00 71.55 C ANISOU 939 CA ILE A 27 8323 9202 9659 150 349 -416 C ATOM 940 C ILE A 27 -54.497 68.439 24.019 1.00 73.14 C ANISOU 940 C ILE A 27 8537 9342 9910 201 346 -391 C ATOM 941 O ILE A 27 -53.566 68.698 24.782 1.00 73.44 O ANISOU 941 O ILE A 27 8595 9326 9980 201 349 -390 O ATOM 942 CB ILE A 27 -54.781 65.912 23.724 1.00 70.98 C ANISOU 942 CB ILE A 27 8289 9109 9569 103 359 -407 C ATOM 943 CG1 ILE A 27 -55.477 64.669 24.307 1.00 70.36 C ANISOU 943 CG1 ILE A 27 8218 9067 9446 40 364 -433 C ATOM 944 CG2 ILE A 27 -53.273 65.817 23.961 1.00 70.99 C ANISOU 944 CG2 ILE A 27 8330 9035 9608 109 364 -390 C ATOM 945 CD1 ILE A 27 -55.286 64.446 25.799 1.00 70.17 C ANISOU 945 CD1 ILE A 27 8205 9026 9430 19 366 -449 C ATOM 946 N PHE A 28 -54.772 69.185 22.947 1.00 75.45 N ANISOU 946 N PHE A 28 8819 9645 10204 241 340 -368 N ATOM 947 CA PHE A 28 -53.970 70.367 22.587 1.00 76.12 C ANISOU 947 CA PHE A 28 8923 9668 10330 282 337 -340 C ATOM 948 C PHE A 28 -54.456 71.677 23.223 1.00 76.73 C ANISOU 948 C PHE A 28 8991 9732 10430 333 328 -349 C ATOM 949 O PHE A 28 -53.877 72.732 22.965 1.00 77.68 O ANISOU 949 O PHE A 28 9135 9795 10582 364 326 -326 O ATOM 950 CB PHE A 28 -53.897 70.516 21.060 1.00 76.21 C ANISOU 950 CB PHE A 28 8936 9688 10329 298 334 -304 C ATOM 951 CG PHE A 28 -53.480 69.255 20.335 1.00 76.62 C ANISOU 951 CG PHE A 28 8997 9756 10356 253 343 -299 C ATOM 952 CD1 PHE A 28 -52.424 68.466 20.801 1.00 76.06 C ANISOU 952 CD1 PHE A 28 8955 9647 10296 218 353 -306 C ATOM 953 CD2 PHE A 28 -54.138 68.858 19.169 1.00 77.12 C ANISOU 953 CD2 PHE A 28 9043 9877 10382 250 341 -291 C ATOM 954 CE1 PHE A 28 -52.045 67.314 20.123 1.00 77.34 C ANISOU 954 CE1 PHE A 28 9132 9819 10435 186 361 -305 C ATOM 955 CE2 PHE A 28 -53.760 67.706 18.487 1.00 76.28 C ANISOU 955 CE2 PHE A 28 8950 9781 10250 210 350 -292 C ATOM 956 CZ PHE A 28 -52.715 66.932 18.963 1.00 76.55 C ANISOU 956 CZ PHE A 28 9018 9769 10298 180 360 -300 C ATOM 957 N VAL A 29 -55.530 71.608 24.014 1.00 78.34 N ANISOU 957 N VAL A 29 9162 9991 10613 341 324 -384 N ATOM 958 CA VAL A 29 -56.028 72.735 24.835 1.00 77.56 C ANISOU 958 CA VAL A 29 9052 9884 10531 391 317 -406 C ATOM 959 C VAL A 29 -55.988 72.413 26.336 1.00 77.60 C ANISOU 959 C VAL A 29 9049 9894 10540 360 323 -446 C ATOM 960 O VAL A 29 -55.686 73.291 27.146 1.00 78.29 O ANISOU 960 O VAL A 29 9149 9939 10660 384 322 -461 O ATOM 961 CB VAL A 29 -57.470 73.124 24.422 1.00 78.50 C ANISOU 961 CB VAL A 29 9129 10082 10615 445 305 -415 C ATOM 962 CG1 VAL A 29 -58.003 74.288 25.261 1.00 79.09 C ANISOU 962 CG1 VAL A 29 9195 10148 10705 509 298 -442 C ATOM 963 CG2 VAL A 29 -57.521 73.461 22.932 1.00 78.81 C ANISOU 963 CG2 VAL A 29 9175 10121 10646 478 299 -372 C ATOM 964 N MET A 30 -56.304 71.167 26.700 1.00 78.01 N ANISOU 964 N MET A 30 9084 9999 10557 305 328 -463 N ATOM 965 CA MET A 30 -56.267 70.697 28.093 1.00 77.60 C ANISOU 965 CA MET A 30 9024 9959 10501 266 333 -495 C ATOM 966 C MET A 30 -54.851 70.630 28.654 1.00 75.83 C ANISOU 966 C MET A 30 8838 9659 10312 242 340 -485 C ATOM 967 O MET A 30 -54.596 71.118 29.750 1.00 74.61 O ANISOU 967 O MET A 30 8682 9488 10177 245 342 -507 O ATOM 968 CB MET A 30 -56.896 69.300 28.185 1.00 79.50 C ANISOU 968 CB MET A 30 9249 10266 10689 204 337 -507 C ATOM 969 CG MET A 30 -57.040 68.725 29.589 1.00 80.72 C ANISOU 969 CG MET A 30 9395 10446 10827 159 341 -536 C ATOM 970 SD MET A 30 -56.688 66.960 29.620 1.00 81.41 S ANISOU 970 SD MET A 30 9519 10531 10881 74 351 -525 S ATOM 971 CE MET A 30 -56.708 66.645 31.385 1.00 82.44 C ANISOU 971 CE MET A 30 9643 10679 11000 36 353 -552 C ATOM 972 N ILE A 31 -53.951 69.984 27.915 1.00 74.77 N ANISOU 972 N ILE A 31 8734 9490 10183 218 346 -455 N ATOM 973 CA ILE A 31 -52.575 69.755 28.372 1.00 73.01 C ANISOU 973 CA ILE A 31 8541 9213 9985 195 353 -444 C ATOM 974 C ILE A 31 -51.775 71.054 28.538 1.00 72.33 C ANISOU 974 C ILE A 31 8468 9071 9943 224 353 -439 C ATOM 975 O ILE A 31 -51.103 71.219 29.565 1.00 73.92 O ANISOU 975 O ILE A 31 8674 9252 10160 209 357 -454 O ATOM 976 CB ILE A 31 -51.818 68.752 27.454 1.00 74.53 C ANISOU 976 CB ILE A 31 8760 9389 10167 171 358 -416 C ATOM 977 CG1 ILE A 31 -52.510 67.370 27.459 1.00 74.04 C ANISOU 977 CG1 ILE A 31 8700 9369 10061 131 360 -426 C ATOM 978 CG2 ILE A 31 -50.343 68.621 27.853 1.00 74.99 C ANISOU 978 CG2 ILE A 31 8842 9402 10247 160 364 -405 C ATOM 979 CD1 ILE A 31 -52.574 66.667 28.807 1.00 73.95 C ANISOU 979 CD1 ILE A 31 8692 9371 10034 95 363 -447 C ATOM 980 N PRO A 32 -51.834 71.975 27.549 1.00 70.41 N ANISOU 980 N PRO A 32 8234 8803 9715 260 349 -418 N ATOM 981 CA PRO A 32 -51.084 73.222 27.755 1.00 70.59 C ANISOU 981 CA PRO A 32 8280 8765 9777 277 350 -413 C ATOM 982 C PRO A 32 -51.619 74.090 28.904 1.00 72.61 C ANISOU 982 C PRO A 32 8526 9016 10046 300 347 -452 C ATOM 983 O PRO A 32 -50.826 74.608 29.688 1.00 72.66 O ANISOU 983 O PRO A 32 8546 8984 10075 284 353 -466 O ATOM 984 CB PRO A 32 -51.197 73.949 26.407 1.00 71.17 C ANISOU 984 CB PRO A 32 8369 8813 9856 311 345 -378 C ATOM 985 CG PRO A 32 -52.264 73.258 25.647 1.00 71.30 C ANISOU 985 CG PRO A 32 8360 8890 9837 323 339 -373 C ATOM 986 CD PRO A 32 -52.332 71.857 26.167 1.00 71.38 C ANISOU 986 CD PRO A 32 8354 8944 9820 278 344 -391 C ATOM 987 N THR A 33 -52.940 74.237 29.017 1.00 74.63 N ANISOU 987 N THR A 33 8754 9317 10282 335 340 -473 N ATOM 988 CA THR A 33 -53.515 75.020 30.117 1.00 75.59 C ANISOU 988 CA THR A 33 8863 9444 10412 363 337 -516 C ATOM 989 C THR A 33 -53.249 74.391 31.496 1.00 76.76 C ANISOU 989 C THR A 33 8993 9620 10552 317 344 -549 C ATOM 990 O THR A 33 -53.175 75.104 32.498 1.00 78.91 O ANISOU 990 O THR A 33 9264 9877 10840 326 345 -583 O ATOM 991 CB THR A 33 -55.023 75.303 29.923 1.00 75.08 C ANISOU 991 CB THR A 33 8764 9439 10321 418 327 -535 C ATOM 992 OG1 THR A 33 -55.418 76.366 30.800 1.00 74.99 O ANISOU 992 OG1 THR A 33 8752 9414 10325 463 324 -574 O ATOM 993 CG2 THR A 33 -55.879 74.076 30.200 1.00 74.49 C ANISOU 993 CG2 THR A 33 8643 9459 10199 385 326 -552 C ATOM 994 N LEU A 34 -53.116 73.064 31.539 1.00 76.89 N ANISOU 994 N LEU A 34 8997 9674 10541 270 347 -539 N ATOM 995 CA LEU A 34 -52.668 72.368 32.750 1.00 78.13 C ANISOU 995 CA LEU A 34 9147 9850 10688 224 353 -558 C ATOM 996 C LEU A 34 -51.208 72.751 33.017 1.00 80.39 C ANISOU 996 C LEU A 34 9461 10077 11006 207 359 -547 C ATOM 997 O LEU A 34 -50.893 73.306 34.073 1.00 78.39 O ANISOU 997 O LEU A 34 9203 9816 10765 201 362 -576 O ATOM 998 CB LEU A 34 -52.841 70.844 32.613 1.00 77.08 C ANISOU 998 CB LEU A 34 9010 9758 10517 180 354 -543 C ATOM 999 CG LEU A 34 -54.212 70.207 32.927 1.00 77.67 C ANISOU 999 CG LEU A 34 9051 9912 10547 165 351 -566 C ATOM 1000 CD1 LEU A 34 -54.207 69.543 34.298 1.00 78.51 C ANISOU 1000 CD1 LEU A 34 9147 10052 10630 121 354 -588 C ATOM 1001 CD2 LEU A 34 -55.396 71.168 32.844 1.00 78.39 C ANISOU 1001 CD2 LEU A 34 9107 10043 10633 215 344 -593 C ATOM 1002 N TYR A 35 -50.348 72.512 32.022 1.00 81.74 N ANISOU 1002 N TYR A 35 9657 10214 11186 200 362 -509 N ATOM 1003 CA TYR A 35 -48.922 72.909 32.069 1.00 81.72 C ANISOU 1003 CA TYR A 35 9675 10166 11206 182 369 -496 C ATOM 1004 C TYR A 35 -48.702 74.387 32.465 1.00 79.78 C ANISOU 1004 C TYR A 35 9442 9876 10993 196 370 -516 C ATOM 1005 O TYR A 35 -47.713 74.713 33.132 1.00 80.01 O ANISOU 1005 O TYR A 35 9477 9889 11032 168 377 -526 O ATOM 1006 CB TYR A 35 -48.242 72.641 30.714 1.00 83.62 C ANISOU 1006 CB TYR A 35 9936 10385 11449 181 370 -453 C ATOM 1007 CG TYR A 35 -47.796 71.207 30.466 1.00 84.73 C ANISOU 1007 CG TYR A 35 10077 10552 11564 160 373 -435 C ATOM 1008 CD1 TYR A 35 -48.522 70.116 30.949 1.00 86.67 C ANISOU 1008 CD1 TYR A 35 10313 10836 11780 148 370 -446 C ATOM 1009 CD2 TYR A 35 -46.656 70.940 29.709 1.00 85.17 C ANISOU 1009 CD2 TYR A 35 10147 10594 11621 152 377 -407 C ATOM 1010 CE1 TYR A 35 -48.108 68.816 30.701 1.00 87.81 C ANISOU 1010 CE1 TYR A 35 10471 10991 11900 131 373 -429 C ATOM 1011 CE2 TYR A 35 -46.247 69.635 29.461 1.00 86.52 C ANISOU 1011 CE2 TYR A 35 10323 10783 11766 143 379 -393 C ATOM 1012 CZ TYR A 35 -46.979 68.580 29.961 1.00 86.42 C ANISOU 1012 CZ TYR A 35 10311 10795 11728 134 377 -404 C ATOM 1013 OH TYR A 35 -46.595 67.281 29.729 1.00 86.09 O ANISOU 1013 OH TYR A 35 10288 10760 11662 127 379 -392 O ATOM 1014 N SER A 36 -49.616 75.263 32.043 1.00 77.88 N ANISOU 1014 N SER A 36 9209 9617 10763 239 365 -522 N ATOM 1015 CA SER A 36 -49.601 76.679 32.435 1.00 77.77 C ANISOU 1015 CA SER A 36 9219 9551 10778 260 366 -546 C ATOM 1016 C SER A 36 -49.903 76.899 33.919 1.00 78.14 C ANISOU 1016 C SER A 36 9244 9621 10822 255 368 -600 C ATOM 1017 O SER A 36 -49.287 77.754 34.551 1.00 77.78 O ANISOU 1017 O SER A 36 9218 9536 10797 241 374 -623 O ATOM 1018 CB SER A 36 -50.606 77.474 31.602 1.00 77.39 C ANISOU 1018 CB SER A 36 9187 9481 10737 322 357 -538 C ATOM 1019 OG SER A 36 -50.321 77.358 30.221 1.00 77.84 O ANISOU 1019 OG SER A 36 9263 9517 10793 325 354 -488 O ATOM 1020 N ILE A 37 -50.863 76.148 34.460 1.00 78.41 N ANISOU 1020 N ILE A 37 9238 9724 10828 262 363 -620 N ATOM 1021 CA ILE A 37 -51.250 76.271 35.868 1.00 79.79 C ANISOU 1021 CA ILE A 37 9385 9937 10993 257 365 -672 C ATOM 1022 C ILE A 37 -50.135 75.713 36.752 1.00 80.98 C ANISOU 1022 C ILE A 37 9528 10099 11138 199 373 -674 C ATOM 1023 O ILE A 37 -49.658 76.403 37.659 1.00 81.77 O ANISOU 1023 O ILE A 37 9631 10185 11251 185 379 -708 O ATOM 1024 CB ILE A 37 -52.607 75.578 36.165 1.00 79.64 C ANISOU 1024 CB ILE A 37 9321 10000 10937 272 358 -691 C ATOM 1025 CG1 ILE A 37 -53.750 76.342 35.481 1.00 79.65 C ANISOU 1025 CG1 ILE A 37 9320 10002 10939 340 349 -699 C ATOM 1026 CG2 ILE A 37 -52.870 75.503 37.669 1.00 79.73 C ANISOU 1026 CG2 ILE A 37 9299 10064 10931 252 361 -740 C ATOM 1027 CD1 ILE A 37 -55.046 75.567 35.354 1.00 79.60 C ANISOU 1027 CD1 ILE A 37 9267 10087 10888 351 343 -706 C ATOM 1028 N ILE A 38 -49.722 74.475 36.477 1.00 81.88 N ANISOU 1028 N ILE A 38 9637 10242 11232 168 373 -641 N ATOM 1029 CA ILE A 38 -48.566 73.863 37.153 1.00 82.34 C ANISOU 1029 CA ILE A 38 9691 10313 11282 124 379 -633 C ATOM 1030 C ILE A 38 -47.354 74.806 37.146 1.00 81.21 C ANISOU 1030 C ILE A 38 9569 10121 11165 108 386 -635 C ATOM 1031 O ILE A 38 -46.668 74.935 38.163 1.00 80.67 O ANISOU 1031 O ILE A 38 9487 10070 11092 79 391 -657 O ATOM 1032 CB ILE A 38 -48.190 72.485 36.536 1.00 82.92 C ANISOU 1032 CB ILE A 38 9770 10402 11332 108 377 -590 C ATOM 1033 CG1 ILE A 38 -49.220 71.406 36.933 1.00 84.02 C ANISOU 1033 CG1 ILE A 38 9891 10596 11435 99 372 -595 C ATOM 1034 CG2 ILE A 38 -46.795 72.027 36.970 1.00 84.15 C ANISOU 1034 CG2 ILE A 38 9927 10563 11482 79 382 -576 C ATOM 1035 CD1 ILE A 38 -50.132 70.935 35.818 1.00 84.69 C ANISOU 1035 CD1 ILE A 38 9982 10687 11508 114 368 -575 C ATOM 1036 N PHE A 39 -47.108 75.462 36.010 1.00 79.82 N ANISOU 1036 N PHE A 39 9424 9891 11013 123 387 -610 N ATOM 1037 CA PHE A 39 -45.997 76.411 35.883 1.00 80.19 C ANISOU 1037 CA PHE A 39 9497 9890 11081 99 395 -609 C ATOM 1038 C PHE A 39 -46.089 77.552 36.894 1.00 80.30 C ANISOU 1038 C PHE A 39 9518 9881 11110 93 400 -660 C ATOM 1039 O PHE A 39 -45.355 77.555 37.879 1.00 79.93 O ANISOU 1039 O PHE A 39 9454 9860 11055 54 406 -684 O ATOM 1040 CB PHE A 39 -45.899 76.969 34.451 1.00 80.26 C ANISOU 1040 CB PHE A 39 9543 9843 11108 115 394 -572 C ATOM 1041 CG PHE A 39 -44.902 78.090 34.303 1.00 80.53 C ANISOU 1041 CG PHE A 39 9611 9823 11161 83 403 -572 C ATOM 1042 CD1 PHE A 39 -43.539 77.825 34.322 1.00 80.39 C ANISOU 1042 CD1 PHE A 39 9585 9826 11132 33 411 -558 C ATOM 1043 CD2 PHE A 39 -45.324 79.410 34.149 1.00 80.57 C ANISOU 1043 CD2 PHE A 39 9660 9758 11192 102 403 -587 C ATOM 1044 CE1 PHE A 39 -42.610 78.849 34.187 1.00 81.30 C ANISOU 1044 CE1 PHE A 39 9730 9901 11258 -9 421 -560 C ATOM 1045 CE2 PHE A 39 -44.402 80.440 34.015 1.00 81.20 C ANISOU 1045 CE2 PHE A 39 9782 9782 11287 61 413 -587 C ATOM 1046 CZ PHE A 39 -43.043 80.160 34.034 1.00 81.44 C ANISOU 1046 CZ PHE A 39 9799 9841 11303 -1 422 -574 C ATOM 1047 N VAL A 40 -47.010 78.490 36.664 1.00 81.64 N ANISOU 1047 N VAL A 40 9712 10007 11300 136 396 -678 N ATOM 1048 CA VAL A 40 -47.015 79.773 37.380 1.00 82.83 C ANISOU 1048 CA VAL A 40 9888 10111 11470 136 402 -726 C ATOM 1049 C VAL A 40 -47.305 79.639 38.879 1.00 82.25 C ANISOU 1049 C VAL A 40 9775 10092 11381 125 404 -781 C ATOM 1050 O VAL A 40 -46.761 80.403 39.678 1.00 84.05 O ANISOU 1050 O VAL A 40 10015 10301 11617 94 413 -820 O ATOM 1051 CB VAL A 40 -47.972 80.807 36.721 1.00 83.96 C ANISOU 1051 CB VAL A 40 10075 10190 11637 199 396 -730 C ATOM 1052 CG1 VAL A 40 -49.440 80.470 36.980 1.00 84.22 C ANISOU 1052 CG1 VAL A 40 10071 10274 11654 260 385 -752 C ATOM 1053 CG2 VAL A 40 -47.645 82.221 37.191 1.00 84.84 C ANISOU 1053 CG2 VAL A 40 10237 10224 11773 191 404 -769 C ATOM 1054 N VAL A 41 -48.137 78.668 39.255 1.00 81.27 N ANISOU 1054 N VAL A 41 9606 10040 11231 142 397 -785 N ATOM 1055 CA VAL A 41 -48.380 78.362 40.673 1.00 80.63 C ANISOU 1055 CA VAL A 41 9482 10025 11127 124 399 -830 C ATOM 1056 C VAL A 41 -47.091 77.830 41.295 1.00 79.96 C ANISOU 1056 C VAL A 41 9380 9971 11027 63 406 -821 C ATOM 1057 O VAL A 41 -46.670 78.303 42.352 1.00 81.68 O ANISOU 1057 O VAL A 41 9587 10205 11242 34 413 -863 O ATOM 1058 CB VAL A 41 -49.521 77.332 40.872 1.00 80.79 C ANISOU 1058 CB VAL A 41 9459 10120 11115 144 390 -828 C ATOM 1059 CG1 VAL A 41 -49.631 76.910 42.338 1.00 81.19 C ANISOU 1059 CG1 VAL A 41 9466 10246 11136 114 392 -867 C ATOM 1060 CG2 VAL A 41 -50.850 77.896 40.377 1.00 80.91 C ANISOU 1060 CG2 VAL A 41 9478 10127 11136 209 383 -845 C ATOM 1061 N GLY A 42 -46.473 76.858 40.624 1.00 78.04 N ANISOU 1061 N GLY A 42 9136 9742 10773 47 404 -768 N ATOM 1062 CA GLY A 42 -45.196 76.295 41.045 1.00 77.21 C ANISOU 1062 CA GLY A 42 9014 9671 10649 2 409 -753 C ATOM 1063 C GLY A 42 -44.053 77.290 41.159 1.00 78.63 C ANISOU 1063 C GLY A 42 9211 9819 10844 -35 419 -769 C ATOM 1064 O GLY A 42 -43.183 77.124 42.022 1.00 77.29 O ANISOU 1064 O GLY A 42 9014 9697 10653 -75 425 -783 O ATOM 1065 N ILE A 43 -44.038 78.313 40.299 1.00 80.98 N ANISOU 1065 N ILE A 43 9553 10041 11172 -28 423 -766 N ATOM 1066 CA ILE A 43 -43.011 79.364 40.370 1.00 83.07 C ANISOU 1066 CA ILE A 43 9845 10269 11449 -75 435 -783 C ATOM 1067 C ILE A 43 -43.177 80.134 41.676 1.00 84.45 C ANISOU 1067 C ILE A 43 10012 10449 11623 -94 441 -849 C ATOM 1068 O ILE A 43 -42.287 80.104 42.515 1.00 84.96 O ANISOU 1068 O ILE A 43 10050 10562 11667 -145 449 -870 O ATOM 1069 CB ILE A 43 -43.045 80.334 39.155 1.00 84.08 C ANISOU 1069 CB ILE A 43 10034 10304 11608 -65 436 -762 C ATOM 1070 CG1 ILE A 43 -42.757 79.592 37.834 1.00 84.02 C ANISOU 1070 CG1 ILE A 43 10029 10298 11596 -53 431 -697 C ATOM 1071 CG2 ILE A 43 -42.049 81.482 39.335 1.00 84.99 C ANISOU 1071 CG2 ILE A 43 10184 10376 11731 -127 450 -785 C ATOM 1072 CD1 ILE A 43 -41.525 78.707 37.829 1.00 82.90 C ANISOU 1072 CD1 ILE A 43 9850 10222 11424 -93 435 -671 C ATOM 1073 N PHE A 44 -44.328 80.779 41.854 1.00 87.21 N ANISOU 1073 N PHE A 44 10382 10760 11992 -49 438 -884 N ATOM 1074 CA PHE A 44 -44.630 81.513 43.092 1.00 91.19 C ANISOU 1074 CA PHE A 44 10881 11271 12496 -58 444 -954 C ATOM 1075 C PHE A 44 -44.687 80.595 44.323 1.00 89.95 C ANISOU 1075 C PHE A 44 10656 11218 12302 -74 442 -975 C ATOM 1076 O PHE A 44 -44.423 81.040 45.439 1.00 89.02 O ANISOU 1076 O PHE A 44 10521 11129 12173 -107 450 -1028 O ATOM 1077 CB PHE A 44 -45.955 82.291 42.970 1.00 94.87 C ANISOU 1077 CB PHE A 44 11378 11683 12984 10 439 -987 C ATOM 1078 CG PHE A 44 -45.928 83.398 41.943 1.00 98.04 C ANISOU 1078 CG PHE A 44 11857 11972 13421 30 441 -973 C ATOM 1079 CD1 PHE A 44 -45.052 84.475 42.077 1.00100.26 C ANISOU 1079 CD1 PHE A 44 12190 12186 13717 -22 455 -998 C ATOM 1080 CD2 PHE A 44 -46.790 83.378 40.846 1.00 99.56 C ANISOU 1080 CD2 PHE A 44 12073 12127 13628 97 430 -936 C ATOM 1081 CE1 PHE A 44 -45.026 85.497 41.132 1.00101.54 C ANISOU 1081 CE1 PHE A 44 12434 12236 13908 -8 457 -981 C ATOM 1082 CE2 PHE A 44 -46.770 84.400 39.901 1.00100.34 C ANISOU 1082 CE2 PHE A 44 12248 12121 13756 118 431 -918 C ATOM 1083 CZ PHE A 44 -45.887 85.459 40.044 1.00100.72 C ANISOU 1083 CZ PHE A 44 12355 12094 13820 65 444 -939 C ATOM 1084 N GLY A 45 -45.039 79.325 44.113 1.00 88.17 N ANISOU 1084 N GLY A 45 10395 11048 12055 -54 432 -933 N ATOM 1085 CA GLY A 45 -45.076 78.328 45.182 1.00 86.14 C ANISOU 1085 CA GLY A 45 10083 10887 11759 -71 429 -939 C ATOM 1086 C GLY A 45 -43.697 77.983 45.711 1.00 83.06 C ANISOU 1086 C GLY A 45 9668 10544 11344 -126 434 -929 C ATOM 1087 O GLY A 45 -43.406 78.221 46.881 1.00 81.86 O ANISOU 1087 O GLY A 45 9487 10442 11173 -159 440 -972 O ATOM 1088 N ASN A 46 -42.853 77.422 44.847 1.00 82.93 N ANISOU 1088 N ASN A 46 9661 10522 11326 -134 433 -875 N ATOM 1089 CA ASN A 46 -41.477 77.057 45.221 1.00 82.59 C ANISOU 1089 CA ASN A 46 9590 10534 11253 -177 438 -861 C ATOM 1090 C ASN A 46 -40.552 78.261 45.437 1.00 82.37 C ANISOU 1090 C ASN A 46 9574 10489 11234 -231 451 -899 C ATOM 1091 O ASN A 46 -39.530 78.119 46.104 1.00 83.76 O ANISOU 1091 O ASN A 46 9714 10733 11378 -273 456 -907 O ATOM 1092 CB ASN A 46 -40.838 76.109 44.196 1.00 81.62 C ANISOU 1092 CB ASN A 46 9471 10416 11122 -163 432 -796 C ATOM 1093 CG ASN A 46 -41.481 74.731 44.171 1.00 81.37 C ANISOU 1093 CG ASN A 46 9430 10416 11071 -125 420 -759 C ATOM 1094 OD1 ASN A 46 -41.183 73.879 45.010 1.00 81.88 O ANISOU 1094 OD1 ASN A 46 9463 10548 11099 -130 416 -751 O ATOM 1095 ND2 ASN A 46 -42.341 74.492 43.187 1.00 80.16 N ANISOU 1095 ND2 ASN A 46 9305 10212 10938 -89 414 -735 N ATOM 1096 N SER A 47 -40.891 79.427 44.875 1.00 82.39 N ANISOU 1096 N SER A 47 9627 10402 11274 -230 458 -921 N ATOM 1097 CA SER A 47 -40.132 80.663 45.151 1.00 83.68 C ANISOU 1097 CA SER A 47 9814 10536 11444 -290 473 -963 C ATOM 1098 C SER A 47 -40.324 81.124 46.593 1.00 85.75 C ANISOU 1098 C SER A 47 10051 10838 11692 -315 479 -1033 C ATOM 1099 O SER A 47 -39.370 81.573 47.225 1.00 86.53 O ANISOU 1099 O SER A 47 10133 10973 11769 -379 490 -1065 O ATOM 1100 CB SER A 47 -40.503 81.799 44.189 1.00 82.59 C ANISOU 1100 CB SER A 47 9750 10279 11349 -280 477 -966 C ATOM 1101 OG SER A 47 -40.057 81.515 42.873 1.00 80.28 O ANISOU 1101 OG SER A 47 9479 9959 11064 -275 474 -905 O ATOM 1102 N LEU A 48 -41.556 81.017 47.097 1.00 87.69 N ANISOU 1102 N LEU A 48 10288 11083 11944 -266 472 -1059 N ATOM 1103 CA LEU A 48 -41.851 81.294 48.509 1.00 89.13 C ANISOU 1103 CA LEU A 48 10438 11320 12107 -283 477 -1125 C ATOM 1104 C LEU A 48 -41.152 80.321 49.461 1.00 90.95 C ANISOU 1104 C LEU A 48 10599 11671 12287 -317 474 -1115 C ATOM 1105 O LEU A 48 -40.708 80.729 50.531 1.00 91.98 O ANISOU 1105 O LEU A 48 10700 11852 12393 -363 483 -1166 O ATOM 1106 CB LEU A 48 -43.363 81.281 48.783 1.00 89.11 C ANISOU 1106 CB LEU A 48 10433 11308 12114 -220 469 -1152 C ATOM 1107 CG LEU A 48 -44.160 82.531 48.394 1.00 90.26 C ANISOU 1107 CG LEU A 48 10640 11351 12301 -182 472 -1193 C ATOM 1108 CD1 LEU A 48 -45.654 82.263 48.513 1.00 89.77 C ANISOU 1108 CD1 LEU A 48 10562 11306 12240 -109 462 -1207 C ATOM 1109 CD2 LEU A 48 -43.766 83.733 49.246 1.00 91.68 C ANISOU 1109 CD2 LEU A 48 10842 11508 12484 -226 488 -1271 C ATOM 1110 N VAL A 49 -41.049 79.050 49.075 1.00 92.66 N ANISOU 1110 N VAL A 49 10791 11930 12485 -292 462 -1050 N ATOM 1111 CA VAL A 49 -40.429 78.033 49.939 1.00 94.61 C ANISOU 1111 CA VAL A 49 10979 12286 12681 -310 458 -1032 C ATOM 1112 C VAL A 49 -38.927 78.276 50.152 1.00 97.21 C ANISOU 1112 C VAL A 49 11285 12665 12984 -368 467 -1034 C ATOM 1113 O VAL A 49 -38.452 78.177 51.285 1.00 97.74 O ANISOU 1113 O VAL A 49 11304 12820 13011 -402 469 -1062 O ATOM 1114 CB VAL A 49 -40.683 76.596 49.421 1.00 92.84 C ANISOU 1114 CB VAL A 49 10749 12083 12443 -266 443 -961 C ATOM 1115 CG1 VAL A 49 -39.868 75.568 50.199 1.00 92.54 C ANISOU 1115 CG1 VAL A 49 10662 12146 12352 -279 437 -933 C ATOM 1116 CG2 VAL A 49 -42.162 76.255 49.526 1.00 92.38 C ANISOU 1116 CG2 VAL A 49 10697 12011 12393 -225 435 -966 C ATOM 1117 N VAL A 50 -38.189 78.578 49.080 1.00 99.55 N ANISOU 1117 N VAL A 50 11611 12914 13297 -381 471 -1007 N ATOM 1118 CA VAL A 50 -36.736 78.833 49.192 1.00101.72 C ANISOU 1118 CA VAL A 50 11859 13246 13541 -441 481 -1010 C ATOM 1119 C VAL A 50 -36.402 80.040 50.075 1.00104.46 C ANISOU 1119 C VAL A 50 12203 13604 13882 -512 497 -1086 C ATOM 1120 O VAL A 50 -35.455 79.987 50.862 1.00106.11 O ANISOU 1120 O VAL A 50 12360 13911 14044 -561 502 -1104 O ATOM 1121 CB VAL A 50 -36.012 78.979 47.822 1.00102.27 C ANISOU 1121 CB VAL A 50 11960 13271 13625 -449 484 -968 C ATOM 1122 CG1 VAL A 50 -36.064 77.672 47.046 1.00102.83 C ANISOU 1122 CG1 VAL A 50 12023 13354 13690 -387 469 -897 C ATOM 1123 CG2 VAL A 50 -36.563 80.123 46.973 1.00102.74 C ANISOU 1123 CG2 VAL A 50 12092 13204 13738 -456 492 -985 C ATOM 1124 N ILE A 51 -37.184 81.112 49.948 1.00106.88 N ANISOU 1124 N ILE A 51 12565 13811 14231 -514 504 -1131 N ATOM 1125 CA ILE A 51 -36.942 82.346 50.711 1.00107.04 C ANISOU 1125 CA ILE A 51 12599 13819 14249 -580 521 -1209 C ATOM 1126 C ILE A 51 -37.294 82.219 52.196 1.00106.71 C ANISOU 1126 C ILE A 51 12505 13861 14177 -587 521 -1262 C ATOM 1127 O ILE A 51 -36.609 82.807 53.034 1.00108.48 O ANISOU 1127 O ILE A 51 12706 14137 14371 -656 534 -1316 O ATOM 1128 CB ILE A 51 -37.627 83.596 50.085 1.00108.26 C ANISOU 1128 CB ILE A 51 12843 13831 14459 -574 530 -1241 C ATOM 1129 CG1 ILE A 51 -39.163 83.489 50.092 1.00108.02 C ANISOU 1129 CG1 ILE A 51 12833 13747 14461 -488 519 -1249 C ATOM 1130 CG2 ILE A 51 -37.096 83.831 48.673 1.00107.63 C ANISOU 1130 CG2 ILE A 51 12814 13678 14401 -585 532 -1189 C ATOM 1131 CD1 ILE A 51 -39.869 84.739 49.612 1.00109.33 C ANISOU 1131 CD1 ILE A 51 13085 13780 14676 -469 525 -1286 C ATOM 1132 N VAL A 52 -38.345 81.459 52.518 1.00107.61 N ANISOU 1132 N VAL A 52 12600 13994 14293 -522 508 -1248 N ATOM 1133 CA VAL A 52 -38.694 81.182 53.927 1.00108.77 C ANISOU 1133 CA VAL A 52 12690 14235 14402 -528 506 -1290 C ATOM 1134 C VAL A 52 -37.727 80.195 54.602 1.00110.24 C ANISOU 1134 C VAL A 52 12803 14556 14527 -552 500 -1257 C ATOM 1135 O VAL A 52 -37.645 80.163 55.830 1.00110.49 O ANISOU 1135 O VAL A 52 12783 14678 14517 -581 503 -1297 O ATOM 1136 CB VAL A 52 -40.168 80.724 54.136 1.00107.65 C ANISOU 1136 CB VAL A 52 12547 14082 14273 -460 494 -1291 C ATOM 1137 CG1 VAL A 52 -41.142 81.770 53.601 1.00107.52 C ANISOU 1137 CG1 VAL A 52 12595 13947 14309 -426 499 -1331 C ATOM 1138 CG2 VAL A 52 -40.445 79.346 53.544 1.00108.45 C ANISOU 1138 CG2 VAL A 52 12635 14202 14366 -408 477 -1207 C ATOM 1139 N ILE A 53 -37.015 79.391 53.809 1.00112.11 N ANISOU 1139 N ILE A 53 13033 14807 14753 -536 492 -1186 N ATOM 1140 CA ILE A 53 -35.936 78.542 54.327 1.00114.90 C ANISOU 1140 CA ILE A 53 13323 15286 15047 -552 487 -1153 C ATOM 1141 C ILE A 53 -34.716 79.372 54.730 1.00117.67 C ANISOU 1141 C ILE A 53 13646 15696 15368 -635 503 -1198 C ATOM 1142 O ILE A 53 -34.065 79.067 55.731 1.00119.11 O ANISOU 1142 O ILE A 53 13763 16000 15492 -663 502 -1210 O ATOM 1143 CB ILE A 53 -35.498 77.483 53.300 1.00115.22 C ANISOU 1143 CB ILE A 53 13369 15324 15085 -504 475 -1068 C ATOM 1144 N TYR A 54 -34.407 80.408 53.947 1.00120.24 N ANISOU 1144 N TYR A 54 14021 15937 15726 -676 517 -1221 N ATOM 1145 CA TYR A 54 -33.356 81.377 54.296 1.00123.45 C ANISOU 1145 CA TYR A 54 14414 16385 16106 -771 535 -1274 C ATOM 1146 C TYR A 54 -33.746 82.243 55.501 1.00126.73 C ANISOU 1146 C TYR A 54 14824 16813 16514 -819 548 -1363 C ATOM 1147 O TYR A 54 -32.909 82.510 56.366 1.00129.14 O ANISOU 1147 O TYR A 54 15076 17221 16768 -888 557 -1405 O ATOM 1148 CB TYR A 54 -33.030 82.276 53.100 1.00123.05 C ANISOU 1148 CB TYR A 54 14432 16227 16094 -808 548 -1273 C ATOM 1149 N PHE A 55 -35.010 82.672 55.547 1.00128.45 N ANISOU 1149 N PHE A 55 15092 16933 16780 -779 547 -1395 N ATOM 1150 CA PHE A 55 -35.540 83.484 56.660 1.00129.30 C ANISOU 1150 CA PHE A 55 15199 17044 16884 -810 558 -1484 C ATOM 1151 C PHE A 55 -35.794 82.648 57.928 1.00130.24 C ANISOU 1151 C PHE A 55 15236 17294 16952 -792 548 -1490 C ATOM 1152 O PHE A 55 -35.002 82.702 58.871 1.00132.91 O ANISOU 1152 O PHE A 55 15515 17747 17236 -852 555 -1523 O ATOM 1153 CB PHE A 55 -36.834 84.221 56.247 1.00129.39 C ANISOU 1153 CB PHE A 55 15289 16912 16959 -760 560 -1517 C ATOM 1154 CG PHE A 55 -36.604 85.535 55.539 1.00130.15 C ANISOU 1154 CG PHE A 55 15473 16882 17096 -804 577 -1553 C ATOM 1155 CD1 PHE A 55 -35.722 85.630 54.460 1.00129.82 C ANISOU 1155 CD1 PHE A 55 15460 16801 17061 -838 580 -1504 C ATOM 1156 CD2 PHE A 55 -37.297 86.682 55.934 1.00130.62 C ANISOU 1156 CD2 PHE A 55 15590 16855 17184 -809 589 -1635 C ATOM 1157 CE1 PHE A 55 -35.524 86.840 53.808 1.00129.50 C ANISOU 1157 CE1 PHE A 55 15508 16640 17054 -885 596 -1532 C ATOM 1158 CE2 PHE A 55 -37.102 87.892 55.283 1.00131.04 C ANISOU 1158 CE2 PHE A 55 15737 16778 17273 -848 604 -1665 C ATOM 1159 CZ PHE A 55 -36.215 87.971 54.219 1.00130.80 C ANISOU 1159 CZ PHE A 55 15739 16710 17248 -890 607 -1611 C ATOM 1160 N TYR A 56 -36.883 81.872 57.935 1.00129.40 N ANISOU 1160 N TYR A 56 15128 17177 16861 -714 532 -1457 N ATOM 1161 CA TYR A 56 -37.399 81.234 59.161 1.00129.07 C ANISOU 1161 CA TYR A 56 15024 17241 16776 -699 524 -1471 C ATOM 1162 C TYR A 56 -36.568 80.043 59.644 1.00128.86 C ANISOU 1162 C TYR A 56 14924 17349 16685 -702 512 -1411 C ATOM 1163 O TYR A 56 -36.017 80.078 60.747 1.00130.32 O ANISOU 1163 O TYR A 56 15048 17650 16815 -749 516 -1445 O ATOM 1164 CB TYR A 56 -38.857 80.798 58.968 1.00127.62 C ANISOU 1164 CB TYR A 56 14861 17004 16622 -624 512 -1454 C ATOM 1165 N MET A 57 -36.494 78.994 58.824 1.00127.07 N ANISOU 1165 N MET A 57 14707 17108 16464 -648 496 -1323 N ATOM 1166 CA MET A 57 -35.728 77.787 59.158 1.00126.23 C ANISOU 1166 CA MET A 57 14546 17115 16299 -632 482 -1257 C ATOM 1167 C MET A 57 -34.233 78.080 59.289 1.00125.58 C ANISOU 1167 C MET A 57 14421 17116 16174 -688 491 -1266 C ATOM 1168 O MET A 57 -33.578 77.558 60.192 1.00126.59 O ANISOU 1168 O MET A 57 14482 17377 16236 -701 485 -1256 O ATOM 1169 CB MET A 57 -35.950 76.697 58.104 1.00126.39 C ANISOU 1169 CB MET A 57 14600 17081 16340 -561 466 -1167 C ATOM 1170 N LYS A 58 -33.714 78.912 58.383 1.00124.56 N ANISOU 1170 N LYS A 58 14331 16916 16079 -722 504 -1282 N ATOM 1171 CA LYS A 58 -32.315 79.363 58.393 1.00124.10 C ANISOU 1171 CA LYS A 58 14236 16933 15980 -791 515 -1299 C ATOM 1172 C LYS A 58 -31.291 78.224 58.240 1.00123.93 C ANISOU 1172 C LYS A 58 14159 17022 15904 -757 501 -1225 C ATOM 1173 O LYS A 58 -30.170 78.327 58.747 1.00125.86 O ANISOU 1173 O LYS A 58 14341 17392 16088 -806 506 -1241 O ATOM 1174 CB LYS A 58 -32.030 80.175 59.665 1.00123.22 C ANISOU 1174 CB LYS A 58 14081 16908 15829 -871 530 -1385 C ATOM 1175 N LEU A 59 -31.675 77.168 57.513 1.00121.93 N ANISOU 1175 N LEU A 59 13932 16724 15670 -672 484 -1148 N ATOM 1176 CA LEU A 59 -30.889 75.924 57.387 1.00119.88 C ANISOU 1176 CA LEU A 59 13632 16554 15360 -616 467 -1073 C ATOM 1177 C LEU A 59 -30.479 75.345 58.752 1.00117.39 C ANISOU 1177 C LEU A 59 13240 16391 14968 -616 458 -1072 C ATOM 1178 O LEU A 59 -29.316 75.001 58.982 1.00117.53 O ANISOU 1178 O LEU A 59 13197 16533 14923 -618 454 -1052 O ATOM 1179 CB LEU A 59 -29.673 76.124 56.461 1.00119.59 C ANISOU 1179 CB LEU A 59 13583 16543 15311 -636 473 -1056 C ATOM 1180 CG LEU A 59 -29.986 76.259 54.967 1.00119.72 C ANISOU 1180 CG LEU A 59 13672 16424 15392 -610 475 -1027 C ATOM 1181 CD1 LEU A 59 -28.762 76.746 54.199 1.00119.77 C ANISOU 1181 CD1 LEU A 59 13661 16467 15379 -657 486 -1029 C ATOM 1182 CD2 LEU A 59 -30.496 74.940 54.393 1.00118.91 C ANISOU 1182 CD2 LEU A 59 13597 16278 15302 -509 455 -949 C ATOM 1183 N LYS A 60 -31.460 75.241 59.646 1.00115.07 N ANISOU 1183 N LYS A 60 12949 16095 14677 -612 454 -1091 N ATOM 1184 CA LYS A 60 -31.236 74.752 61.008 1.00112.98 C ANISOU 1184 CA LYS A 60 12617 15970 14341 -617 446 -1093 C ATOM 1185 C LYS A 60 -31.053 73.236 61.044 1.00109.66 C ANISOU 1185 C LYS A 60 12188 15599 13879 -532 422 -999 C ATOM 1186 O LYS A 60 -30.078 72.746 61.618 1.00109.83 O ANISOU 1186 O LYS A 60 12147 15753 13829 -521 413 -975 O ATOM 1187 CB LYS A 60 -32.400 75.153 61.919 1.00113.60 C ANISOU 1187 CB LYS A 60 12700 16029 14432 -643 450 -1146 C ATOM 1188 N THR A 61 -31.989 72.507 60.430 1.00105.44 N ANISOU 1188 N THR A 61 11718 14958 13387 -472 411 -949 N ATOM 1189 CA THR A 61 -32.000 71.038 60.468 1.00102.06 C ANISOU 1189 CA THR A 61 11302 14551 12925 -392 388 -861 C ATOM 1190 C THR A 61 -31.364 70.397 59.235 1.00 98.64 C ANISOU 1190 C THR A 61 10901 14072 12504 -329 381 -800 C ATOM 1191 O THR A 61 -31.125 71.053 58.219 1.00 97.21 O ANISOU 1191 O THR A 61 10741 13826 12368 -346 393 -821 O ATOM 1192 CB THR A 61 -33.434 70.481 60.614 1.00101.41 C ANISOU 1192 CB THR A 61 11272 14388 12870 -370 380 -840 C ATOM 1193 OG1 THR A 61 -34.187 70.743 59.423 1.00101.77 O ANISOU 1193 OG1 THR A 61 11385 14291 12991 -358 386 -842 O ATOM 1194 CG2 THR A 61 -34.142 71.103 61.812 1.00101.93 C ANISOU 1194 CG2 THR A 61 11303 14501 12921 -429 388 -904 C ATOM 1195 N VAL A 62 -31.109 69.097 59.354 1.00 97.22 N ANISOU 1195 N VAL A 62 10729 13927 12281 -256 361 -725 N ATOM 1196 CA VAL A 62 -30.640 68.261 58.246 1.00 95.26 C ANISOU 1196 CA VAL A 62 10520 13632 12041 -180 351 -662 C ATOM 1197 C VAL A 62 -31.785 68.032 57.248 1.00 94.35 C ANISOU 1197 C VAL A 62 10491 13358 11997 -160 352 -644 C ATOM 1198 O VAL A 62 -31.539 67.885 56.054 1.00 94.72 O ANISOU 1198 O VAL A 62 10573 13339 12076 -127 353 -622 O ATOM 1199 CB VAL A 62 -30.101 66.897 58.758 1.00 95.45 C ANISOU 1199 CB VAL A 62 10538 13733 11995 -99 329 -587 C ATOM 1200 CG1 VAL A 62 -29.708 65.978 57.602 1.00 94.96 C ANISOU 1200 CG1 VAL A 62 10526 13611 11942 -11 319 -525 C ATOM 1201 CG2 VAL A 62 -28.919 67.100 59.700 1.00 96.99 C ANISOU 1201 CG2 VAL A 62 10639 14101 12112 -110 327 -601 C ATOM 1202 N ALA A 63 -33.024 67.988 57.744 1.00 92.15 N ANISOU 1202 N ALA A 63 10241 13030 11738 -183 351 -655 N ATOM 1203 CA ALA A 63 -34.212 67.900 56.890 1.00 90.24 C ANISOU 1203 CA ALA A 63 10072 12654 11561 -177 353 -649 C ATOM 1204 C ALA A 63 -34.422 69.170 56.070 1.00 89.08 C ANISOU 1204 C ALA A 63 9932 12434 11477 -219 371 -707 C ATOM 1205 O ALA A 63 -34.883 69.102 54.929 1.00 89.54 O ANISOU 1205 O ALA A 63 10044 12390 11585 -197 373 -691 O ATOM 1206 CB ALA A 63 -35.452 67.622 57.727 1.00 90.87 C ANISOU 1206 CB ALA A 63 10166 12724 11634 -198 349 -653 C ATOM 1207 N SER A 64 -34.099 70.320 56.662 1.00 87.51 N ANISOU 1207 N SER A 64 9684 12288 11275 -281 385 -774 N ATOM 1208 CA SER A 64 -34.290 71.615 56.010 1.00 85.36 C ANISOU 1208 CA SER A 64 9427 11944 11060 -327 403 -832 C ATOM 1209 C SER A 64 -33.490 71.769 54.722 1.00 84.98 C ANISOU 1209 C SER A 64 9397 11855 11035 -312 407 -812 C ATOM 1210 O SER A 64 -33.988 72.376 53.773 1.00 85.44 O ANISOU 1210 O SER A 64 9501 11810 11151 -320 415 -827 O ATOM 1211 CB SER A 64 -33.944 72.760 56.968 1.00 86.30 C ANISOU 1211 CB SER A 64 9494 12134 11161 -400 417 -909 C ATOM 1212 OG SER A 64 -34.072 74.023 56.337 1.00 86.57 O ANISOU 1212 OG SER A 64 9554 12089 11248 -444 434 -964 O ATOM 1213 N VAL A 65 -32.268 71.230 54.685 1.00 84.77 N ANISOU 1213 N VAL A 65 9333 11914 10959 -288 401 -778 N ATOM 1214 CA VAL A 65 -31.393 71.406 53.515 1.00 84.45 C ANISOU 1214 CA VAL A 65 9298 11858 10930 -279 406 -763 C ATOM 1215 C VAL A 65 -31.863 70.584 52.309 1.00 83.62 C ANISOU 1215 C VAL A 65 9257 11653 10861 -212 397 -707 C ATOM 1216 O VAL A 65 -31.840 71.084 51.182 1.00 83.84 O ANISOU 1216 O VAL A 65 9314 11608 10930 -221 405 -711 O ATOM 1217 CB VAL A 65 -29.891 71.163 53.846 1.00 85.82 C ANISOU 1217 CB VAL A 65 9401 12174 11032 -274 403 -752 C ATOM 1218 CG1 VAL A 65 -29.555 69.683 53.987 1.00 86.41 C ANISOU 1218 CG1 VAL A 65 9473 12299 11060 -182 383 -681 C ATOM 1219 CG2 VAL A 65 -28.998 71.807 52.793 1.00 85.61 C ANISOU 1219 CG2 VAL A 65 9366 12146 11015 -302 415 -763 C ATOM 1220 N PHE A 66 -32.307 69.345 52.545 1.00 83.15 N ANISOU 1220 N PHE A 66 9221 11586 10783 -151 381 -656 N ATOM 1221 CA PHE A 66 -32.879 68.502 51.477 1.00 80.77 C ANISOU 1221 CA PHE A 66 8988 11186 10514 -93 373 -607 C ATOM 1222 C PHE A 66 -34.159 69.110 50.895 1.00 80.45 C ANISOU 1222 C PHE A 66 8996 11029 10540 -121 381 -632 C ATOM 1223 O PHE A 66 -34.401 69.009 49.692 1.00 81.40 O ANISOU 1223 O PHE A 66 9160 11069 10698 -98 382 -613 O ATOM 1224 CB PHE A 66 -33.168 67.080 51.976 1.00 80.12 C ANISOU 1224 CB PHE A 66 8932 11115 10395 -34 355 -550 C ATOM 1225 CG PHE A 66 -31.932 66.267 52.269 1.00 80.29 C ANISOU 1225 CG PHE A 66 8921 11233 10352 22 344 -510 C ATOM 1226 CD1 PHE A 66 -31.081 65.874 51.240 1.00 80.34 C ANISOU 1226 CD1 PHE A 66 8933 11237 10352 75 342 -482 C ATOM 1227 CD2 PHE A 66 -31.631 65.868 53.570 1.00 81.17 C ANISOU 1227 CD2 PHE A 66 8994 11443 10404 27 334 -500 C ATOM 1228 CE1 PHE A 66 -29.944 65.119 51.502 1.00 81.54 C ANISOU 1228 CE1 PHE A 66 9053 11485 10441 139 330 -448 C ATOM 1229 CE2 PHE A 66 -30.498 65.111 53.842 1.00 82.02 C ANISOU 1229 CE2 PHE A 66 9071 11645 10447 90 322 -461 C ATOM 1230 CZ PHE A 66 -29.651 64.736 52.806 1.00 83.07 C ANISOU 1230 CZ PHE A 66 9211 11777 10576 150 320 -436 C ATOM 1231 N LEU A 67 -34.970 69.730 51.751 1.00 80.65 N ANISOU 1231 N LEU A 67 9011 11055 10575 -166 386 -676 N ATOM 1232 CA LEU A 67 -36.188 70.427 51.316 1.00 81.69 C ANISOU 1232 CA LEU A 67 9181 11091 10764 -187 393 -708 C ATOM 1233 C LEU A 67 -35.898 71.743 50.593 1.00 82.51 C ANISOU 1233 C LEU A 67 9289 11150 10910 -225 408 -750 C ATOM 1234 O LEU A 67 -36.698 72.174 49.764 1.00 84.24 O ANISOU 1234 O LEU A 67 9551 11276 11179 -221 412 -757 O ATOM 1235 CB LEU A 67 -37.120 70.684 52.506 1.00 83.58 C ANISOU 1235 CB LEU A 67 9404 11356 10995 -218 394 -747 C ATOM 1236 CG LEU A 67 -37.716 69.447 53.191 1.00 84.36 C ANISOU 1236 CG LEU A 67 9511 11485 11057 -192 380 -706 C ATOM 1237 CD1 LEU A 67 -38.312 69.812 54.544 1.00 85.46 C ANISOU 1237 CD1 LEU A 67 9612 11684 11172 -233 382 -750 C ATOM 1238 CD2 LEU A 67 -38.758 68.770 52.314 1.00 83.57 C ANISOU 1238 CD2 LEU A 67 9470 11295 10985 -162 374 -672 C ATOM 1239 N LEU A 68 -34.780 72.395 50.918 1.00 84.71 N ANISOU 1239 N LEU A 68 9525 11495 11165 -264 417 -777 N ATOM 1240 CA LEU A 68 -34.303 73.553 50.141 1.00 84.79 C ANISOU 1240 CA LEU A 68 9546 11464 11206 -307 432 -807 C ATOM 1241 C LEU A 68 -33.870 73.122 48.739 1.00 82.67 C ANISOU 1241 C LEU A 68 9304 11153 10951 -271 429 -758 C ATOM 1242 O LEU A 68 -34.184 73.795 47.757 1.00 83.33 O ANISOU 1242 O LEU A 68 9429 11151 11081 -282 436 -764 O ATOM 1243 CB LEU A 68 -33.143 74.268 50.852 1.00 86.37 C ANISOU 1243 CB LEU A 68 9690 11760 11366 -369 442 -847 C ATOM 1244 CG LEU A 68 -32.582 75.540 50.192 1.00 87.94 C ANISOU 1244 CG LEU A 68 9902 11921 11587 -433 460 -883 C ATOM 1245 CD1 LEU A 68 -33.625 76.648 50.137 1.00 88.28 C ANISOU 1245 CD1 LEU A 68 9998 11857 11688 -462 470 -932 C ATOM 1246 CD2 LEU A 68 -31.336 76.028 50.917 1.00 88.70 C ANISOU 1246 CD2 LEU A 68 9936 12135 11630 -498 470 -918 C ATOM 1247 N ASN A 69 -33.146 72.007 48.657 1.00 81.35 N ANISOU 1247 N ASN A 69 9116 11050 10743 -223 418 -710 N ATOM 1248 CA ASN A 69 -32.731 71.438 47.365 1.00 80.68 C ANISOU 1248 CA ASN A 69 9054 10934 10664 -179 414 -664 C ATOM 1249 C ASN A 69 -33.899 71.008 46.486 1.00 77.66 C ANISOU 1249 C ASN A 69 8736 10442 10330 -140 409 -638 C ATOM 1250 O ASN A 69 -33.887 71.258 45.281 1.00 77.93 O ANISOU 1250 O ASN A 69 8798 10416 10393 -135 413 -626 O ATOM 1251 CB ASN A 69 -31.789 70.247 47.568 1.00 81.38 C ANISOU 1251 CB ASN A 69 9110 11113 10694 -122 402 -621 C ATOM 1252 CG ASN A 69 -30.373 70.675 47.892 1.00 81.61 C ANISOU 1252 CG ASN A 69 9071 11260 10673 -154 409 -639 C ATOM 1253 OD1 ASN A 69 -29.600 71.006 46.994 1.00 81.77 O ANISOU 1253 OD1 ASN A 69 9081 11295 10692 -165 416 -637 O ATOM 1254 ND2 ASN A 69 -30.022 70.664 49.173 1.00 81.72 N ANISOU 1254 ND2 ASN A 69 9036 11371 10643 -171 406 -658 N ATOM 1255 N LEU A 70 -34.893 70.360 47.093 1.00 75.48 N ANISOU 1255 N LEU A 70 8478 10145 10053 -117 400 -629 N ATOM 1256 CA LEU A 70 -36.103 69.951 46.378 1.00 74.34 C ANISOU 1256 CA LEU A 70 8389 9909 9946 -89 395 -610 C ATOM 1257 C LEU A 70 -36.851 71.141 45.786 1.00 75.71 C ANISOU 1257 C LEU A 70 8587 10004 10173 -121 405 -645 C ATOM 1258 O LEU A 70 -37.404 71.041 44.697 1.00 77.00 O ANISOU 1258 O LEU A 70 8790 10097 10369 -99 404 -625 O ATOM 1259 CB LEU A 70 -37.043 69.159 47.294 1.00 73.48 C ANISOU 1259 CB LEU A 70 8290 9808 9820 -77 386 -601 C ATOM 1260 CG LEU A 70 -38.301 68.546 46.655 1.00 71.68 C ANISOU 1260 CG LEU A 70 8115 9503 9617 -54 380 -580 C ATOM 1261 CD1 LEU A 70 -37.975 67.725 45.413 1.00 70.09 C ANISOU 1261 CD1 LEU A 70 7951 9260 9420 -9 376 -533 C ATOM 1262 CD2 LEU A 70 -39.050 67.699 47.674 1.00 70.73 C ANISOU 1262 CD2 LEU A 70 7999 9409 9465 -54 372 -569 C ATOM 1263 N ALA A 71 -36.869 72.260 46.503 1.00 77.93 N ANISOU 1263 N ALA A 71 8847 10299 10463 -170 415 -697 N ATOM 1264 CA ALA A 71 -37.445 73.496 45.983 1.00 80.14 C ANISOU 1264 CA ALA A 71 9155 10501 10790 -195 424 -732 C ATOM 1265 C ALA A 71 -36.690 73.986 44.746 1.00 82.22 C ANISOU 1265 C ALA A 71 9437 10729 11071 -205 431 -715 C ATOM 1266 O ALA A 71 -37.311 74.363 43.758 1.00 84.39 O ANISOU 1266 O ALA A 71 9754 10923 11385 -193 432 -707 O ATOM 1267 CB ALA A 71 -37.457 74.569 47.058 1.00 81.63 C ANISOU 1267 CB ALA A 71 9322 10713 10978 -245 434 -794 C ATOM 1268 N LEU A 72 -35.357 73.961 44.802 1.00 84.55 N ANISOU 1268 N LEU A 72 9698 11094 11333 -228 436 -709 N ATOM 1269 CA LEU A 72 -34.516 74.351 43.658 1.00 85.15 C ANISOU 1269 CA LEU A 72 9783 11155 11414 -244 443 -692 C ATOM 1270 C LEU A 72 -34.673 73.403 42.468 1.00 83.88 C ANISOU 1270 C LEU A 72 9646 10962 11260 -186 434 -639 C ATOM 1271 O LEU A 72 -34.808 73.852 41.328 1.00 85.59 O ANISOU 1271 O LEU A 72 9896 11116 11506 -189 438 -627 O ATOM 1272 CB LEU A 72 -33.039 74.425 44.069 1.00 86.58 C ANISOU 1272 CB LEU A 72 9908 11442 11544 -281 448 -700 C ATOM 1273 CG LEU A 72 -32.687 75.544 45.055 1.00 87.22 C ANISOU 1273 CG LEU A 72 9965 11557 11614 -357 461 -758 C ATOM 1274 CD1 LEU A 72 -31.365 75.263 45.755 1.00 87.58 C ANISOU 1274 CD1 LEU A 72 9941 11739 11596 -381 463 -763 C ATOM 1275 CD2 LEU A 72 -32.656 76.896 44.354 1.00 86.86 C ANISOU 1275 CD2 LEU A 72 9962 11435 11603 -418 476 -782 C ATOM 1276 N ALA A 73 -34.654 72.100 42.738 1.00 81.99 N ANISOU 1276 N ALA A 73 9396 10764 10992 -134 422 -608 N ATOM 1277 CA ALA A 73 -34.885 71.089 41.702 1.00 82.72 C ANISOU 1277 CA ALA A 73 9518 10822 11089 -77 414 -562 C ATOM 1278 C ALA A 73 -36.259 71.241 41.025 1.00 83.22 C ANISOU 1278 C ALA A 73 9631 10787 11198 -66 412 -559 C ATOM 1279 O ALA A 73 -36.388 70.969 39.826 1.00 83.51 O ANISOU 1279 O ALA A 73 9696 10783 11251 -41 411 -532 O ATOM 1280 CB ALA A 73 -34.736 69.690 42.283 1.00 82.78 C ANISOU 1280 CB ALA A 73 9518 10878 11057 -26 402 -534 C ATOM 1281 N ASP A 74 -37.272 71.663 41.789 1.00 80.82 N ANISOU 1281 N ASP A 74 9334 10458 10913 -81 412 -589 N ATOM 1282 CA ASP A 74 -38.591 71.975 41.228 1.00 79.72 C ANISOU 1282 CA ASP A 74 9234 10242 10813 -70 411 -593 C ATOM 1283 C ASP A 74 -38.533 73.220 40.335 1.00 78.66 C ANISOU 1283 C ASP A 74 9121 10050 10714 -93 419 -605 C ATOM 1284 O ASP A 74 -39.142 73.239 39.268 1.00 77.88 O ANISOU 1284 O ASP A 74 9054 9895 10639 -71 417 -585 O ATOM 1285 CB ASP A 74 -39.651 72.156 42.330 1.00 80.73 C ANISOU 1285 CB ASP A 74 9355 10372 10944 -78 408 -628 C ATOM 1286 CG ASP A 74 -39.990 70.848 43.062 1.00 81.97 C ANISOU 1286 CG ASP A 74 9505 10572 11067 -57 398 -608 C ATOM 1287 OD1 ASP A 74 -39.886 69.755 42.458 1.00 80.81 O ANISOU 1287 OD1 ASP A 74 9377 10419 10905 -26 392 -566 O ATOM 1288 OD2 ASP A 74 -40.369 70.919 44.256 1.00 82.32 O ANISOU 1288 OD2 ASP A 74 9526 10653 11095 -74 397 -635 O ATOM 1289 N LEU A 75 -37.798 74.246 40.757 1.00 78.00 N ANISOU 1289 N LEU A 75 9024 9981 10631 -140 429 -635 N ATOM 1290 CA LEU A 75 -37.622 75.443 39.922 1.00 77.81 C ANISOU 1290 CA LEU A 75 9030 9897 10635 -170 439 -642 C ATOM 1291 C LEU A 75 -36.905 75.170 38.600 1.00 77.66 C ANISOU 1291 C LEU A 75 9019 9876 10611 -164 440 -599 C ATOM 1292 O LEU A 75 -37.285 75.742 37.579 1.00 81.66 O ANISOU 1292 O LEU A 75 9564 10315 11145 -162 441 -585 O ATOM 1293 CB LEU A 75 -36.895 76.576 40.671 1.00 77.88 C ANISOU 1293 CB LEU A 75 9028 9923 10639 -235 451 -685 C ATOM 1294 CG LEU A 75 -37.726 77.633 41.414 1.00 76.60 C ANISOU 1294 CG LEU A 75 8889 9709 10504 -252 455 -737 C ATOM 1295 CD1 LEU A 75 -38.990 78.052 40.666 1.00 75.43 C ANISOU 1295 CD1 LEU A 75 8791 9468 10398 -210 451 -732 C ATOM 1296 CD2 LEU A 75 -38.078 77.139 42.794 1.00 76.59 C ANISOU 1296 CD2 LEU A 75 8849 9769 10481 -244 451 -766 C ATOM 1297 N CYS A 76 -35.879 74.316 38.620 1.00 76.52 N ANISOU 1297 N CYS A 76 8838 9807 10428 -158 438 -579 N ATOM 1298 CA CYS A 76 -35.145 73.940 37.392 1.00 75.59 C ANISOU 1298 CA CYS A 76 8720 9702 10297 -146 439 -541 C ATOM 1299 C CYS A 76 -36.050 73.271 36.361 1.00 73.34 C ANISOU 1299 C CYS A 76 8470 9363 10033 -94 431 -509 C ATOM 1300 O CYS A 76 -35.919 73.513 35.158 1.00 74.07 O ANISOU 1300 O CYS A 76 8580 9426 10134 -95 434 -486 O ATOM 1301 CB CYS A 76 -33.986 72.987 37.710 1.00 76.07 C ANISOU 1301 CB CYS A 76 8733 9863 10307 -129 437 -528 C ATOM 1302 SG CYS A 76 -32.688 73.694 38.746 1.00 79.32 S ANISOU 1302 SG CYS A 76 9088 10368 10679 -195 447 -563 S ATOM 1303 N PHE A 77 -36.943 72.411 36.850 1.00 70.44 N ANISOU 1303 N PHE A 77 8109 8987 9667 -54 422 -507 N ATOM 1304 CA PHE A 77 -37.962 71.767 36.026 1.00 68.23 C ANISOU 1304 CA PHE A 77 7862 8660 9403 -14 414 -484 C ATOM 1305 C PHE A 77 -38.913 72.797 35.441 1.00 68.94 C ANISOU 1305 C PHE A 77 7983 8678 9532 -23 416 -492 C ATOM 1306 O PHE A 77 -39.104 72.849 34.225 1.00 68.19 O ANISOU 1306 O PHE A 77 7910 8550 9448 -10 416 -467 O ATOM 1307 CB PHE A 77 -38.757 70.756 36.861 1.00 66.64 C ANISOU 1307 CB PHE A 77 7661 8469 9189 12 406 -486 C ATOM 1308 CG PHE A 77 -39.928 70.157 36.141 1.00 65.53 C ANISOU 1308 CG PHE A 77 7553 8285 9061 41 400 -470 C ATOM 1309 CD1 PHE A 77 -41.185 70.756 36.203 1.00 64.92 C ANISOU 1309 CD1 PHE A 77 7489 8169 9009 37 398 -488 C ATOM 1310 CD2 PHE A 77 -39.780 68.991 35.399 1.00 66.23 C ANISOU 1310 CD2 PHE A 77 7657 8375 9130 73 396 -439 C ATOM 1311 CE1 PHE A 77 -42.271 70.196 35.541 1.00 65.04 C ANISOU 1311 CE1 PHE A 77 7525 8159 9027 59 393 -475 C ATOM 1312 CE2 PHE A 77 -40.863 68.429 34.729 1.00 65.83 C ANISOU 1312 CE2 PHE A 77 7636 8289 9086 90 391 -428 C ATOM 1313 CZ PHE A 77 -42.112 69.028 34.804 1.00 65.29 C ANISOU 1313 CZ PHE A 77 7573 8193 9039 80 390 -445 C ATOM 1314 N LEU A 78 -39.504 73.603 36.324 1.00 70.27 N ANISOU 1314 N LEU A 78 8154 8828 9718 -40 418 -527 N ATOM 1315 CA LEU A 78 -40.589 74.526 35.962 1.00 70.93 C ANISOU 1315 CA LEU A 78 8269 8845 9836 -32 417 -539 C ATOM 1316 C LEU A 78 -40.214 75.533 34.874 1.00 72.48 C ANISOU 1316 C LEU A 78 8495 8991 10052 -50 423 -523 C ATOM 1317 O LEU A 78 -41.045 75.839 34.019 1.00 73.68 O ANISOU 1317 O LEU A 78 8676 9093 10224 -23 418 -508 O ATOM 1318 CB LEU A 78 -41.112 75.259 37.201 1.00 71.03 C ANISOU 1318 CB LEU A 78 8276 8852 9859 -46 419 -586 C ATOM 1319 CG LEU A 78 -41.894 74.397 38.206 1.00 69.65 C ANISOU 1319 CG LEU A 78 8077 8718 9666 -27 412 -602 C ATOM 1320 CD1 LEU A 78 -41.893 75.030 39.592 1.00 68.10 C ANISOU 1320 CD1 LEU A 78 7862 8545 9468 -53 416 -651 C ATOM 1321 CD2 LEU A 78 -43.321 74.158 37.737 1.00 69.40 C ANISOU 1321 CD2 LEU A 78 8061 8661 9646 10 404 -597 C ATOM 1322 N LEU A 79 -38.976 76.030 34.894 1.00 73.83 N ANISOU 1322 N LEU A 79 8657 9181 10211 -96 432 -525 N ATOM 1323 CA LEU A 79 -38.489 76.950 33.845 1.00 75.04 C ANISOU 1323 CA LEU A 79 8841 9292 10375 -126 439 -505 C ATOM 1324 C LEU A 79 -38.719 76.424 32.419 1.00 74.48 C ANISOU 1324 C LEU A 79 8783 9209 10305 -93 433 -460 C ATOM 1325 O LEU A 79 -39.106 77.185 31.527 1.00 73.56 O ANISOU 1325 O LEU A 79 8706 9034 10209 -92 433 -442 O ATOM 1326 CB LEU A 79 -36.998 77.252 34.030 1.00 76.46 C ANISOU 1326 CB LEU A 79 8998 9523 10528 -187 450 -510 C ATOM 1327 CG LEU A 79 -36.577 78.153 35.195 1.00 77.93 C ANISOU 1327 CG LEU A 79 9181 9715 10713 -243 459 -556 C ATOM 1328 CD1 LEU A 79 -35.058 78.169 35.296 1.00 78.29 C ANISOU 1328 CD1 LEU A 79 9188 9839 10718 -302 469 -557 C ATOM 1329 CD2 LEU A 79 -37.120 79.567 35.041 1.00 78.19 C ANISOU 1329 CD2 LEU A 79 9275 9651 10781 -266 464 -572 C ATOM 1330 N THR A 80 -38.500 75.123 32.228 1.00 74.05 N ANISOU 1330 N THR A 80 8700 9207 10226 -64 429 -442 N ATOM 1331 CA THR A 80 -38.632 74.483 30.916 1.00 73.14 C ANISOU 1331 CA THR A 80 8592 9091 10105 -34 425 -405 C ATOM 1332 C THR A 80 -40.088 74.286 30.471 1.00 73.52 C ANISOU 1332 C THR A 80 8665 9096 10173 8 416 -397 C ATOM 1333 O THR A 80 -40.356 74.324 29.276 1.00 76.15 O ANISOU 1333 O THR A 80 9015 9408 10510 22 414 -369 O ATOM 1334 CB THR A 80 -37.911 73.111 30.859 1.00 72.64 C ANISOU 1334 CB THR A 80 8497 9094 10006 -13 423 -392 C ATOM 1335 OG1 THR A 80 -38.603 72.146 31.665 1.00 71.55 O ANISOU 1335 OG1 THR A 80 8355 8966 9863 19 416 -404 O ATOM 1336 CG2 THR A 80 -36.458 73.232 31.334 1.00 73.72 C ANISOU 1336 CG2 THR A 80 8599 9295 10114 -48 431 -401 C ATOM 1337 N LEU A 81 -41.013 74.066 31.412 1.00 73.15 N ANISOU 1337 N LEU A 81 8615 9045 10134 27 410 -423 N ATOM 1338 CA LEU A 81 -42.407 73.680 31.077 1.00 72.29 C ANISOU 1338 CA LEU A 81 8516 8918 10031 65 402 -420 C ATOM 1339 C LEU A 81 -43.048 74.437 29.911 1.00 72.05 C ANISOU 1339 C LEU A 81 8513 8841 10019 83 399 -399 C ATOM 1340 O LEU A 81 -43.590 73.793 29.010 1.00 72.66 O ANISOU 1340 O LEU A 81 8592 8927 10087 107 394 -377 O ATOM 1341 CB LEU A 81 -43.343 73.759 32.295 1.00 72.76 C ANISOU 1341 CB LEU A 81 8567 8981 10097 74 398 -456 C ATOM 1342 CG LEU A 81 -43.447 72.567 33.252 1.00 72.97 C ANISOU 1342 CG LEU A 81 8569 9055 10098 75 395 -468 C ATOM 1343 CD1 LEU A 81 -44.635 72.810 34.169 1.00 73.60 C ANISOU 1343 CD1 LEU A 81 8642 9139 10183 83 391 -501 C ATOM 1344 CD2 LEU A 81 -43.596 71.225 32.542 1.00 72.98 C ANISOU 1344 CD2 LEU A 81 8576 9075 10077 92 391 -440 C ATOM 1345 N PRO A 82 -42.974 75.793 29.905 1.00 70.57 N ANISOU 1345 N PRO A 82 8351 8605 9854 70 402 -404 N ATOM 1346 CA PRO A 82 -43.478 76.580 28.772 1.00 69.67 C ANISOU 1346 CA PRO A 82 8270 8443 9755 90 398 -378 C ATOM 1347 C PRO A 82 -43.128 76.048 27.375 1.00 70.92 C ANISOU 1347 C PRO A 82 8429 8619 9898 91 398 -334 C ATOM 1348 O PRO A 82 -43.848 76.330 26.415 1.00 74.04 O ANISOU 1348 O PRO A 82 8842 8993 10297 120 391 -310 O ATOM 1349 CB PRO A 82 -42.809 77.936 28.985 1.00 69.83 C ANISOU 1349 CB PRO A 82 8325 8412 9793 53 406 -384 C ATOM 1350 CG PRO A 82 -42.695 78.064 30.460 1.00 69.00 C ANISOU 1350 CG PRO A 82 8205 8318 9692 36 410 -431 C ATOM 1351 CD PRO A 82 -42.564 76.675 31.019 1.00 69.61 C ANISOU 1351 CD PRO A 82 8235 8467 9746 40 408 -439 C ATOM 1352 N LEU A 83 -42.028 75.304 27.271 1.00 69.23 N ANISOU 1352 N LEU A 83 8192 8449 9662 65 404 -326 N ATOM 1353 CA LEU A 83 -41.570 74.741 26.006 1.00 67.31 C ANISOU 1353 CA LEU A 83 7944 8231 9398 66 405 -291 C ATOM 1354 C LEU A 83 -42.361 73.498 25.620 1.00 65.20 C ANISOU 1354 C LEU A 83 7664 7993 9117 103 398 -288 C ATOM 1355 O LEU A 83 -42.470 73.181 24.440 1.00 64.88 O ANISOU 1355 O LEU A 83 7625 7961 9063 114 397 -262 O ATOM 1356 CB LEU A 83 -40.069 74.423 26.090 1.00 67.44 C ANISOU 1356 CB LEU A 83 7937 8293 9393 30 414 -289 C ATOM 1357 CG LEU A 83 -39.162 75.563 26.593 1.00 68.75 C ANISOU 1357 CG LEU A 83 8111 8445 9565 -22 423 -298 C ATOM 1358 CD1 LEU A 83 -37.698 75.153 26.508 1.00 69.88 C ANISOU 1358 CD1 LEU A 83 8220 8656 9675 -55 431 -295 C ATOM 1359 CD2 LEU A 83 -39.417 76.865 25.840 1.00 69.28 C ANISOU 1359 CD2 LEU A 83 8222 8449 9650 -40 423 -276 C ATOM 1360 N TRP A 84 -42.885 72.785 26.614 1.00 64.66 N ANISOU 1360 N TRP A 84 7583 7939 9045 115 395 -315 N ATOM 1361 CA TRP A 84 -43.739 71.610 26.384 1.00 63.83 C ANISOU 1361 CA TRP A 84 7472 7856 8922 139 390 -317 C ATOM 1362 C TRP A 84 -45.225 71.974 26.317 1.00 62.57 C ANISOU 1362 C TRP A 84 7317 7684 8771 163 382 -324 C ATOM 1363 O TRP A 84 -46.006 71.304 25.628 1.00 61.89 O ANISOU 1363 O TRP A 84 7228 7616 8668 177 378 -317 O ATOM 1364 CB TRP A 84 -43.523 70.574 27.480 1.00 63.37 C ANISOU 1364 CB TRP A 84 7403 7825 8849 135 391 -338 C ATOM 1365 CG TRP A 84 -42.113 70.091 27.608 1.00 64.31 C ANISOU 1365 CG TRP A 84 7513 7970 8952 126 397 -333 C ATOM 1366 CD1 TRP A 84 -41.252 70.352 28.627 1.00 66.04 C ANISOU 1366 CD1 TRP A 84 7717 8204 9171 108 400 -347 C ATOM 1367 CD2 TRP A 84 -41.411 69.244 26.695 1.00 66.20 C ANISOU 1367 CD2 TRP A 84 7752 8232 9168 137 400 -314 C ATOM 1368 NE1 TRP A 84 -40.051 69.724 28.408 1.00 67.42 N ANISOU 1368 NE1 TRP A 84 7879 8416 9321 111 404 -337 N ATOM 1369 CE2 TRP A 84 -40.122 69.035 27.226 1.00 67.55 C ANISOU 1369 CE2 TRP A 84 7905 8434 9323 131 404 -318 C ATOM 1370 CE3 TRP A 84 -41.744 68.644 25.470 1.00 67.74 C ANISOU 1370 CE3 TRP A 84 7958 8429 9350 152 399 -298 C ATOM 1371 CZ2 TRP A 84 -39.158 68.248 26.575 1.00 67.88 C ANISOU 1371 CZ2 TRP A 84 7940 8511 9338 149 407 -306 C ATOM 1372 CZ3 TRP A 84 -40.787 67.860 24.826 1.00 67.29 C ANISOU 1372 CZ3 TRP A 84 7898 8400 9268 165 403 -289 C ATOM 1373 CH2 TRP A 84 -39.511 67.673 25.380 1.00 67.17 C ANISOU 1373 CH2 TRP A 84 7865 8416 9238 166 407 -293 C ATOM 1374 N ALA A 85 -45.614 73.012 27.057 1.00 60.67 N ANISOU 1374 N ALA A 85 7080 7416 8552 167 380 -343 N ATOM 1375 CA ALA A 85 -46.945 73.588 26.950 1.00 59.32 C ANISOU 1375 CA ALA A 85 6912 7236 8389 199 372 -350 C ATOM 1376 C ALA A 85 -47.239 73.949 25.501 1.00 58.55 C ANISOU 1376 C ALA A 85 6827 7128 8289 220 368 -314 C ATOM 1377 O ALA A 85 -48.182 73.415 24.903 1.00 57.91 O ANISOU 1377 O ALA A 85 6734 7079 8189 241 362 -309 O ATOM 1378 CB ALA A 85 -47.061 74.819 27.832 1.00 60.10 C ANISOU 1378 CB ALA A 85 7023 7298 8515 205 372 -374 C ATOM 1379 N VAL A 86 -46.404 74.814 24.924 1.00 57.82 N ANISOU 1379 N VAL A 86 6759 6998 8211 208 371 -289 N ATOM 1380 CA VAL A 86 -46.635 75.285 23.547 1.00 58.02 C ANISOU 1380 CA VAL A 86 6800 7011 8232 227 367 -250 C ATOM 1381 C VAL A 86 -46.459 74.136 22.554 1.00 57.26 C ANISOU 1381 C VAL A 86 6686 6963 8107 219 369 -230 C ATOM 1382 O VAL A 86 -47.273 73.982 21.657 1.00 56.91 O ANISOU 1382 O VAL A 86 6635 6938 8047 244 362 -214 O ATOM 1383 CB VAL A 86 -45.779 76.519 23.132 1.00 58.25 C ANISOU 1383 CB VAL A 86 6867 6986 8279 206 371 -223 C ATOM 1384 CG1 VAL A 86 -45.951 77.674 24.118 1.00 57.48 C ANISOU 1384 CG1 VAL A 86 6798 6831 8209 212 371 -247 C ATOM 1385 CG2 VAL A 86 -44.312 76.159 22.960 1.00 59.25 C ANISOU 1385 CG2 VAL A 86 6987 7130 8395 155 382 -212 C ATOM 1386 N TYR A 87 -45.432 73.311 22.747 1.00 58.13 N ANISOU 1386 N TYR A 87 6785 7094 8206 189 377 -236 N ATOM 1387 CA TYR A 87 -45.233 72.093 21.945 1.00 58.87 C ANISOU 1387 CA TYR A 87 6866 7230 8271 186 379 -227 C ATOM 1388 C TYR A 87 -46.562 71.370 21.730 1.00 59.84 C ANISOU 1388 C TYR A 87 6978 7380 8376 207 373 -238 C ATOM 1389 O TYR A 87 -46.993 71.168 20.590 1.00 61.49 O ANISOU 1389 O TYR A 87 7184 7612 8567 217 370 -219 O ATOM 1390 CB TYR A 87 -44.230 71.172 22.647 1.00 58.63 C ANISOU 1390 CB TYR A 87 6826 7218 8231 167 387 -245 C ATOM 1391 CG TYR A 87 -43.900 69.896 21.920 1.00 58.79 C ANISOU 1391 CG TYR A 87 6842 7273 8222 170 390 -241 C ATOM 1392 CD1 TYR A 87 -43.500 69.924 20.590 1.00 60.00 C ANISOU 1392 CD1 TYR A 87 6993 7442 8360 169 393 -216 C ATOM 1393 CD2 TYR A 87 -43.941 68.659 22.571 1.00 58.04 C ANISOU 1393 CD2 TYR A 87 6749 7192 8112 172 392 -264 C ATOM 1394 CE1 TYR A 87 -43.180 68.757 19.905 1.00 59.45 C ANISOU 1394 CE1 TYR A 87 6921 7405 8262 175 397 -218 C ATOM 1395 CE2 TYR A 87 -43.625 67.486 21.897 1.00 57.68 C ANISOU 1395 CE2 TYR A 87 6708 7167 8038 179 395 -263 C ATOM 1396 CZ TYR A 87 -43.246 67.544 20.566 1.00 58.35 C ANISOU 1396 CZ TYR A 87 6790 7270 8110 182 398 -243 C ATOM 1397 OH TYR A 87 -42.919 66.398 19.893 1.00 57.65 O ANISOU 1397 OH TYR A 87 6708 7202 7992 192 403 -248 O ATOM 1398 N THR A 88 -47.225 71.041 22.835 1.00 60.27 N ANISOU 1398 N THR A 88 7025 7440 8433 209 371 -269 N ATOM 1399 CA THR A 88 -48.538 70.388 22.807 1.00 61.18 C ANISOU 1399 CA THR A 88 7127 7590 8526 218 365 -285 C ATOM 1400 C THR A 88 -49.643 71.309 22.262 1.00 63.25 C ANISOU 1400 C THR A 88 7380 7860 8789 252 356 -275 C ATOM 1401 O THR A 88 -50.553 70.843 21.576 1.00 62.61 O ANISOU 1401 O THR A 88 7284 7822 8680 259 352 -274 O ATOM 1402 CB THR A 88 -48.931 69.894 24.215 1.00 61.18 C ANISOU 1402 CB THR A 88 7120 7600 8524 206 366 -320 C ATOM 1403 OG1 THR A 88 -47.820 69.199 24.810 1.00 61.52 O ANISOU 1403 OG1 THR A 88 7174 7632 8567 184 373 -324 O ATOM 1404 CG2 THR A 88 -50.138 68.970 24.155 1.00 61.09 C ANISOU 1404 CG2 THR A 88 7096 7634 8479 197 363 -336 C ATOM 1405 N ALA A 89 -49.572 72.606 22.577 1.00 65.10 N ANISOU 1405 N ALA A 89 7627 8055 9053 273 352 -270 N ATOM 1406 CA ALA A 89 -50.502 73.603 22.008 1.00 65.89 C ANISOU 1406 CA ALA A 89 7728 8153 9154 319 342 -255 C ATOM 1407 C ALA A 89 -50.380 73.738 20.484 1.00 66.65 C ANISOU 1407 C ALA A 89 7830 8256 9235 328 339 -211 C ATOM 1408 O ALA A 89 -51.387 73.928 19.794 1.00 69.65 O ANISOU 1408 O ALA A 89 8196 8670 9596 363 330 -200 O ATOM 1409 CB ALA A 89 -50.315 74.961 22.669 1.00 66.79 C ANISOU 1409 CB ALA A 89 7868 8206 9303 340 340 -258 C ATOM 1410 N MET A 90 -49.157 73.607 19.965 1.00 65.63 N ANISOU 1410 N MET A 90 7717 8108 9111 296 348 -189 N ATOM 1411 CA MET A 90 -48.898 73.603 18.519 1.00 65.24 C ANISOU 1411 CA MET A 90 7669 8075 9042 295 347 -149 C ATOM 1412 C MET A 90 -49.186 72.240 17.851 1.00 64.36 C ANISOU 1412 C MET A 90 7533 8026 8894 281 350 -158 C ATOM 1413 O MET A 90 -48.724 71.985 16.733 1.00 65.37 O ANISOU 1413 O MET A 90 7660 8174 9003 270 353 -133 O ATOM 1414 CB MET A 90 -47.446 74.037 18.245 1.00 66.68 C ANISOU 1414 CB MET A 90 7875 8222 9238 262 356 -125 C ATOM 1415 CG MET A 90 -47.141 75.494 18.591 1.00 67.65 C ANISOU 1415 CG MET A 90 8033 8278 9391 266 354 -109 C ATOM 1416 SD MET A 90 -45.546 76.048 17.935 1.00 68.00 S ANISOU 1416 SD MET A 90 8102 8299 9436 215 364 -72 S ATOM 1417 CE MET A 90 -45.923 77.744 17.500 1.00 68.09 C ANISOU 1417 CE MET A 90 8167 8239 9464 237 355 -31 C ATOM 1418 N GLU A 91 -49.952 71.378 18.527 1.00 62.33 N ANISOU 1418 N GLU A 91 7258 7800 8624 276 350 -194 N ATOM 1419 CA GLU A 91 -50.348 70.064 18.020 1.00 60.87 C ANISOU 1419 CA GLU A 91 7058 7666 8401 256 353 -209 C ATOM 1420 C GLU A 91 -49.148 69.147 17.833 1.00 58.77 C ANISOU 1420 C GLU A 91 6807 7391 8131 226 365 -211 C ATOM 1421 O GLU A 91 -49.035 68.455 16.815 1.00 57.77 O ANISOU 1421 O GLU A 91 6678 7294 7977 215 369 -205 O ATOM 1422 CB GLU A 91 -51.166 70.200 16.729 1.00 62.49 C ANISOU 1422 CB GLU A 91 7245 7921 8577 274 347 -187 C ATOM 1423 CG GLU A 91 -52.336 71.168 16.848 1.00 63.05 C ANISOU 1423 CG GLU A 91 7299 8008 8647 318 334 -182 C ATOM 1424 CD GLU A 91 -53.216 71.190 15.611 1.00 64.75 C ANISOU 1424 CD GLU A 91 7489 8289 8824 339 326 -162 C ATOM 1425 OE1 GLU A 91 -52.951 70.410 14.657 1.00 61.66 O ANISOU 1425 OE1 GLU A 91 7092 7931 8404 311 332 -156 O ATOM 1426 OE2 GLU A 91 -54.177 72.003 15.599 1.00 65.92 O ANISOU 1426 OE2 GLU A 91 7621 8459 8965 387 314 -155 O ATOM 1427 N TYR A 92 -48.275 69.142 18.843 1.00 57.50 N ANISOU 1427 N TYR A 92 6660 7193 7994 215 370 -222 N ATOM 1428 CA TYR A 92 -46.975 68.457 18.800 1.00 57.10 C ANISOU 1428 CA TYR A 92 6619 7134 7939 199 379 -223 C ATOM 1429 C TYR A 92 -46.089 68.894 17.615 1.00 57.77 C ANISOU 1429 C TYR A 92 6703 7227 8020 198 383 -192 C ATOM 1430 O TYR A 92 -45.933 68.152 16.635 1.00 57.63 O ANISOU 1430 O TYR A 92 6682 7240 7974 195 387 -189 O ATOM 1431 CB TYR A 92 -47.143 66.921 18.803 1.00 55.79 C ANISOU 1431 CB TYR A 92 6464 6988 7745 185 385 -249 C ATOM 1432 CG TYR A 92 -47.933 66.343 19.967 1.00 55.35 C ANISOU 1432 CG TYR A 92 6414 6929 7686 174 383 -278 C ATOM 1433 CD1 TYR A 92 -47.782 66.832 21.272 1.00 54.74 C ANISOU 1433 CD1 TYR A 92 6335 6828 7634 175 381 -288 C ATOM 1434 CD2 TYR A 92 -48.807 65.271 19.769 1.00 55.26 C ANISOU 1434 CD2 TYR A 92 6410 6942 7642 154 384 -297 C ATOM 1435 CE1 TYR A 92 -48.504 66.296 22.326 1.00 54.51 C ANISOU 1435 CE1 TYR A 92 6309 6803 7597 160 379 -313 C ATOM 1436 CE2 TYR A 92 -49.518 64.715 20.825 1.00 55.07 C ANISOU 1436 CE2 TYR A 92 6394 6920 7610 133 383 -322 C ATOM 1437 CZ TYR A 92 -49.369 65.232 22.100 1.00 55.61 C ANISOU 1437 CZ TYR A 92 6457 6968 7702 138 380 -328 C ATOM 1438 OH TYR A 92 -50.084 64.688 23.152 1.00 55.74 O ANISOU 1438 OH TYR A 92 6478 6993 7705 114 380 -351 O ATOM 1439 N ARG A 93 -45.542 70.106 17.698 1.00 58.71 N ANISOU 1439 N ARG A 93 6825 7318 8161 198 381 -169 N ATOM 1440 CA ARG A 93 -44.395 70.491 16.865 1.00 61.59 C ANISOU 1440 CA ARG A 93 7189 7691 8520 183 387 -142 C ATOM 1441 C ARG A 93 -43.483 71.491 17.582 1.00 62.40 C ANISOU 1441 C ARG A 93 7302 7760 8648 164 390 -135 C ATOM 1442 O ARG A 93 -43.956 72.414 18.252 1.00 62.72 O ANISOU 1442 O ARG A 93 7355 7759 8714 169 385 -135 O ATOM 1443 CB ARG A 93 -44.813 70.977 15.465 1.00 63.94 C ANISOU 1443 CB ARG A 93 7484 8008 8800 190 383 -106 C ATOM 1444 CG ARG A 93 -45.402 72.379 15.338 1.00 66.41 C ANISOU 1444 CG ARG A 93 7813 8287 9132 203 373 -75 C ATOM 1445 CD ARG A 93 -45.180 72.928 13.929 1.00 69.34 C ANISOU 1445 CD ARG A 93 8186 8676 9483 198 372 -29 C ATOM 1446 NE ARG A 93 -43.771 73.255 13.699 1.00 72.36 N ANISOU 1446 NE ARG A 93 8573 9058 9863 161 381 -12 N ATOM 1447 CZ ARG A 93 -43.247 73.679 12.547 1.00 75.97 C ANISOU 1447 CZ ARG A 93 9029 9536 10297 142 383 26 C ATOM 1448 NH1 ARG A 93 -41.942 73.943 12.480 1.00 76.74 N ANISOU 1448 NH1 ARG A 93 9127 9643 10388 100 393 36 N ATOM 1449 NH2 ARG A 93 -44.005 73.841 11.459 1.00 78.12 N ANISOU 1449 NH2 ARG A 93 9299 9831 10548 161 375 57 N ATOM 1450 N TRP A 94 -42.176 71.284 17.426 1.00 63.21 N ANISOU 1450 N TRP A 94 7394 7884 8737 143 399 -132 N ATOM 1451 CA TRP A 94 -41.152 71.920 18.245 1.00 64.19 C ANISOU 1451 CA TRP A 94 7518 7994 8875 116 405 -136 C ATOM 1452 C TRP A 94 -40.415 73.001 17.447 1.00 65.30 C ANISOU 1452 C TRP A 94 7666 8134 9010 82 408 -100 C ATOM 1453 O TRP A 94 -39.620 72.675 16.560 1.00 64.89 O ANISOU 1453 O TRP A 94 7596 8131 8928 68 414 -87 O ATOM 1454 CB TRP A 94 -40.172 70.845 18.729 1.00 64.29 C ANISOU 1454 CB TRP A 94 7510 8048 8869 117 412 -162 C ATOM 1455 CG TRP A 94 -39.088 71.352 19.610 1.00 64.38 C ANISOU 1455 CG TRP A 94 7512 8064 8885 89 418 -170 C ATOM 1456 CD1 TRP A 94 -37.911 71.914 19.215 1.00 65.79 C ANISOU 1456 CD1 TRP A 94 7675 8273 9046 53 425 -155 C ATOM 1457 CD2 TRP A 94 -39.065 71.327 21.040 1.00 64.61 C ANISOU 1457 CD2 TRP A 94 7540 8076 8931 89 417 -198 C ATOM 1458 NE1 TRP A 94 -37.162 72.264 20.311 1.00 66.85 N ANISOU 1458 NE1 TRP A 94 7800 8414 9186 29 430 -174 N ATOM 1459 CE2 TRP A 94 -37.843 71.907 21.446 1.00 65.83 C ANISOU 1459 CE2 TRP A 94 7679 8254 9077 52 424 -199 C ATOM 1460 CE3 TRP A 94 -39.959 70.877 22.018 1.00 64.84 C ANISOU 1460 CE3 TRP A 94 7578 8080 8975 111 411 -221 C ATOM 1461 CZ2 TRP A 94 -37.487 72.047 22.790 1.00 65.33 C ANISOU 1461 CZ2 TRP A 94 7608 8191 9024 40 426 -225 C ATOM 1462 CZ3 TRP A 94 -39.605 71.016 23.361 1.00 65.79 C ANISOU 1462 CZ3 TRP A 94 7693 8198 9106 100 412 -245 C ATOM 1463 CH2 TRP A 94 -38.376 71.599 23.731 1.00 65.97 C ANISOU 1463 CH2 TRP A 94 7698 8244 9122 67 419 -246 C ATOM 1464 N PRO A 95 -40.664 74.290 17.763 1.00 67.57 N ANISOU 1464 N PRO A 95 7983 8367 9323 66 405 -85 N ATOM 1465 CA PRO A 95 -39.991 75.374 17.041 1.00 68.25 C ANISOU 1465 CA PRO A 95 8087 8441 9402 25 409 -47 C ATOM 1466 C PRO A 95 -38.609 75.742 17.596 1.00 69.34 C ANISOU 1466 C PRO A 95 8217 8596 9533 -30 421 -57 C ATOM 1467 O PRO A 95 -37.809 76.340 16.877 1.00 69.03 O ANISOU 1467 O PRO A 95 8182 8574 9473 -77 427 -28 O ATOM 1468 CB PRO A 95 -40.962 76.544 17.209 1.00 67.88 C ANISOU 1468 CB PRO A 95 8087 8318 9386 39 401 -31 C ATOM 1469 CG PRO A 95 -41.597 76.308 18.538 1.00 67.92 C ANISOU 1469 CG PRO A 95 8090 8298 9417 67 397 -74 C ATOM 1470 CD PRO A 95 -41.562 74.824 18.809 1.00 67.50 C ANISOU 1470 CD PRO A 95 7996 8303 9348 85 399 -104 C ATOM 1471 N PHE A 96 -38.317 75.352 18.838 1.00 72.15 N ANISOU 1471 N PHE A 96 8556 8958 9898 -29 424 -96 N ATOM 1472 CA PHE A 96 -37.189 75.916 19.596 1.00 73.17 C ANISOU 1472 CA PHE A 96 8679 9097 10022 -84 434 -110 C ATOM 1473 C PHE A 96 -35.804 75.340 19.278 1.00 74.01 C ANISOU 1473 C PHE A 96 8739 9294 10087 -112 444 -113 C ATOM 1474 O PHE A 96 -34.811 75.748 19.898 1.00 75.45 O ANISOU 1474 O PHE A 96 8907 9504 10257 -160 452 -126 O ATOM 1475 CB PHE A 96 -37.460 75.791 21.097 1.00 73.12 C ANISOU 1475 CB PHE A 96 8672 9069 10042 -70 432 -151 C ATOM 1476 CG PHE A 96 -38.730 76.453 21.537 1.00 73.70 C ANISOU 1476 CG PHE A 96 8785 9063 10153 -44 424 -155 C ATOM 1477 CD1 PHE A 96 -38.848 77.838 21.512 1.00 75.77 C ANISOU 1477 CD1 PHE A 96 9095 9258 10434 -73 425 -140 C ATOM 1478 CD2 PHE A 96 -39.811 75.694 21.976 1.00 74.45 C ANISOU 1478 CD2 PHE A 96 8873 9153 10260 10 415 -175 C ATOM 1479 CE1 PHE A 96 -40.024 78.463 21.917 1.00 77.23 C ANISOU 1479 CE1 PHE A 96 9317 9372 10651 -37 416 -147 C ATOM 1480 CE2 PHE A 96 -40.988 76.306 22.380 1.00 75.55 C ANISOU 1480 CE2 PHE A 96 9041 9234 10428 38 407 -182 C ATOM 1481 CZ PHE A 96 -41.097 77.696 22.353 1.00 76.68 C ANISOU 1481 CZ PHE A 96 9229 9312 10592 21 407 -170 C ATOM 1482 N GLY A 97 -35.723 74.410 18.326 1.00 74.18 N ANISOU 1482 N GLY A 97 8735 9368 10080 -82 443 -104 N ATOM 1483 CA GLY A 97 -34.438 73.869 17.880 1.00 75.23 C ANISOU 1483 CA GLY A 97 8821 9594 10168 -98 452 -107 C ATOM 1484 C GLY A 97 -33.982 72.634 18.633 1.00 75.23 C ANISOU 1484 C GLY A 97 8785 9646 10153 -54 452 -145 C ATOM 1485 O GLY A 97 -34.733 72.058 19.425 1.00 73.17 O ANISOU 1485 O GLY A 97 8538 9347 9917 -12 446 -165 O ATOM 1486 N ASN A 98 -32.732 72.246 18.380 1.00 76.80 N ANISOU 1486 N ASN A 98 8937 9936 10306 -64 460 -152 N ATOM 1487 CA ASN A 98 -32.183 70.943 18.789 1.00 76.22 C ANISOU 1487 CA ASN A 98 8829 9924 10207 -7 460 -182 C ATOM 1488 C ASN A 98 -31.438 70.972 20.133 1.00 77.43 C ANISOU 1488 C ASN A 98 8957 10109 10354 -16 462 -208 C ATOM 1489 O ASN A 98 -31.337 69.939 20.807 1.00 78.64 O ANISOU 1489 O ASN A 98 9099 10280 10499 40 458 -231 O ATOM 1490 CB ASN A 98 -31.257 70.414 17.676 1.00 76.36 C ANISOU 1490 CB ASN A 98 8805 10035 10172 2 466 -179 C ATOM 1491 CG ASN A 98 -31.269 68.898 17.558 1.00 75.19 C ANISOU 1491 CG ASN A 98 8650 9913 10006 85 463 -203 C ATOM 1492 OD1 ASN A 98 -31.384 68.185 18.547 1.00 77.05 O ANISOU 1492 OD1 ASN A 98 8892 10130 10250 129 458 -225 O ATOM 1493 ND2 ASN A 98 -31.141 68.403 16.335 1.00 74.21 N ANISOU 1493 ND2 ASN A 98 8514 9829 9853 105 466 -198 N ATOM 1494 N TYR A 99 -30.903 72.135 20.513 1.00 77.45 N ANISOU 1494 N TYR A 99 8953 10119 10355 -89 469 -204 N ATOM 1495 CA TYR A 99 -30.286 72.299 21.836 1.00 77.23 C ANISOU 1495 CA TYR A 99 8901 10121 10321 -107 471 -230 C ATOM 1496 C TYR A 99 -31.336 72.147 22.914 1.00 75.97 C ANISOU 1496 C TYR A 99 8777 9879 10208 -76 462 -244 C ATOM 1497 O TYR A 99 -31.219 71.287 23.783 1.00 76.50 O ANISOU 1497 O TYR A 99 8828 9970 10268 -30 458 -265 O ATOM 1498 CB TYR A 99 -29.583 73.660 21.985 1.00 79.46 C ANISOU 1498 CB TYR A 99 9177 10420 10592 -205 482 -225 C ATOM 1499 CG TYR A 99 -28.076 73.584 21.872 1.00 81.19 C ANISOU 1499 CG TYR A 99 9328 10772 10747 -238 492 -235 C ATOM 1500 CD1 TYR A 99 -27.442 73.668 20.628 1.00 82.01 C ANISOU 1500 CD1 TYR A 99 9407 10943 10810 -264 498 -216 C ATOM 1501 CD2 TYR A 99 -27.281 73.427 23.010 1.00 81.09 C ANISOU 1501 CD2 TYR A 99 9270 10830 10709 -243 494 -266 C ATOM 1502 CE1 TYR A 99 -26.058 73.597 20.520 1.00 83.11 C ANISOU 1502 CE1 TYR A 99 9475 11218 10882 -295 508 -228 C ATOM 1503 CE2 TYR A 99 -25.896 73.356 22.915 1.00 83.23 C ANISOU 1503 CE2 TYR A 99 9470 11239 10913 -271 503 -277 C ATOM 1504 CZ TYR A 99 -25.287 73.439 21.669 1.00 84.55 C ANISOU 1504 CZ TYR A 99 9610 11474 11039 -297 510 -260 C ATOM 1505 OH TYR A 99 -23.912 73.370 21.573 1.00 86.34 O ANISOU 1505 OH TYR A 99 9759 11853 11193 -325 519 -274 O ATOM 1506 N LEU A 100 -32.372 72.979 22.835 1.00 76.16 N ANISOU 1506 N LEU A 100 8850 9809 10275 -99 460 -231 N ATOM 1507 CA LEU A 100 -33.454 72.970 23.821 1.00 74.22 C ANISOU 1507 CA LEU A 100 8637 9490 10072 -75 452 -247 C ATOM 1508 C LEU A 100 -34.233 71.658 23.840 1.00 73.51 C ANISOU 1508 C LEU A 100 8554 9387 9987 -1 443 -252 C ATOM 1509 O LEU A 100 -34.760 71.277 24.882 1.00 73.91 O ANISOU 1509 O LEU A 100 8613 9414 10054 21 437 -272 O ATOM 1510 CB LEU A 100 -34.401 74.155 23.604 1.00 73.98 C ANISOU 1510 CB LEU A 100 8657 9369 10081 -105 450 -232 C ATOM 1511 CG LEU A 100 -33.782 75.533 23.874 1.00 74.60 C ANISOU 1511 CG LEU A 100 8748 9434 10162 -184 459 -232 C ATOM 1512 CD1 LEU A 100 -34.716 76.640 23.398 1.00 74.82 C ANISOU 1512 CD1 LEU A 100 8838 9365 10226 -199 457 -210 C ATOM 1513 CD2 LEU A 100 -33.429 75.705 25.345 1.00 74.10 C ANISOU 1513 CD2 LEU A 100 8669 9384 10101 -204 462 -269 C ATOM 1514 N CYS A 101 -34.306 70.963 22.706 1.00 73.16 N ANISOU 1514 N CYS A 101 8509 9360 9926 29 442 -237 N ATOM 1515 CA CYS A 101 -34.870 69.607 22.684 1.00 73.28 C ANISOU 1515 CA CYS A 101 8535 9369 9937 92 435 -246 C ATOM 1516 C CYS A 101 -34.188 68.707 23.720 1.00 73.45 C ANISOU 1516 C CYS A 101 8535 9433 9937 125 434 -268 C ATOM 1517 O CYS A 101 -34.867 67.970 24.435 1.00 73.69 O ANISOU 1517 O CYS A 101 8587 9430 9978 158 427 -279 O ATOM 1518 CB CYS A 101 -34.776 68.990 21.284 1.00 73.32 C ANISOU 1518 CB CYS A 101 8538 9400 9919 116 437 -232 C ATOM 1519 SG CYS A 101 -35.542 67.354 21.064 1.00 74.68 S ANISOU 1519 SG CYS A 101 8737 9552 10084 182 431 -245 S ATOM 1520 N LYS A 102 -32.863 68.816 23.830 1.00 73.41 N ANISOU 1520 N LYS A 102 8487 9506 9897 114 440 -273 N ATOM 1521 CA LYS A 102 -32.065 68.005 24.766 1.00 72.17 C ANISOU 1521 CA LYS A 102 8304 9406 9711 153 438 -291 C ATOM 1522 C LYS A 102 -32.128 68.471 26.222 1.00 72.57 C ANISOU 1522 C LYS A 102 8349 9447 9776 128 436 -306 C ATOM 1523 O LYS A 102 -32.379 67.660 27.116 1.00 72.57 O ANISOU 1523 O LYS A 102 8359 9438 9775 169 429 -315 O ATOM 1524 CB LYS A 102 -30.600 67.983 24.330 1.00 72.87 C ANISOU 1524 CB LYS A 102 8336 9601 9748 152 445 -293 C ATOM 1525 CG LYS A 102 -30.372 67.350 22.972 1.00 73.20 C ANISOU 1525 CG LYS A 102 8375 9672 9765 187 447 -285 C ATOM 1526 CD LYS A 102 -28.964 67.612 22.470 1.00 73.84 C ANISOU 1526 CD LYS A 102 8394 9868 9794 170 456 -288 C ATOM 1527 CE LYS A 102 -28.814 67.164 21.025 1.00 74.10 C ANISOU 1527 CE LYS A 102 8421 9929 9802 195 459 -280 C ATOM 1528 NZ LYS A 102 -29.164 65.729 20.838 1.00 73.88 N ANISOU 1528 NZ LYS A 102 8423 9878 9769 285 453 -291 N ATOM 1529 N ILE A 103 -31.876 69.757 26.472 1.00 73.38 N ANISOU 1529 N ILE A 103 8439 9552 9890 59 442 -309 N ATOM 1530 CA ILE A 103 -31.790 70.249 27.862 1.00 74.59 C ANISOU 1530 CA ILE A 103 8581 9709 10051 30 442 -329 C ATOM 1531 C ILE A 103 -33.156 70.291 28.554 1.00 75.78 C ANISOU 1531 C ILE A 103 8774 9772 10246 38 435 -336 C ATOM 1532 O ILE A 103 -33.239 70.070 29.765 1.00 80.67 O ANISOU 1532 O ILE A 103 9387 10399 10865 46 432 -353 O ATOM 1533 CB ILE A 103 -31.063 71.616 28.002 1.00 74.33 C ANISOU 1533 CB ILE A 103 8526 9704 10012 -53 453 -336 C ATOM 1534 CG1 ILE A 103 -31.862 72.780 27.397 1.00 74.51 C ANISOU 1534 CG1 ILE A 103 8596 9639 10076 -102 456 -324 C ATOM 1535 CG2 ILE A 103 -29.671 71.553 27.378 1.00 74.42 C ANISOU 1535 CG2 ILE A 103 8485 9821 9969 -68 461 -332 C ATOM 1536 CD1 ILE A 103 -31.427 74.141 27.912 1.00 75.27 C ANISOU 1536 CD1 ILE A 103 8693 9730 10175 -186 466 -338 C ATOM 1537 N ALA A 104 -34.211 70.566 27.788 1.00 73.80 N ANISOU 1537 N ALA A 104 8562 9448 10027 38 433 -322 N ATOM 1538 CA ALA A 104 -35.578 70.560 28.308 1.00 74.39 C ANISOU 1538 CA ALA A 104 8673 9454 10138 50 426 -330 C ATOM 1539 C ALA A 104 -36.112 69.143 28.545 1.00 74.38 C ANISOU 1539 C ALA A 104 8684 9449 10126 106 418 -330 C ATOM 1540 O ALA A 104 -37.078 68.967 29.288 1.00 76.08 O ANISOU 1540 O ALA A 104 8919 9629 10359 112 413 -341 O ATOM 1541 CB ALA A 104 -36.507 71.318 27.368 1.00 75.35 C ANISOU 1541 CB ALA A 104 8827 9511 10289 37 426 -314 C ATOM 1542 N SER A 105 -35.513 68.155 27.878 1.00 72.71 N ANISOU 1542 N SER A 105 8467 9273 9885 143 418 -319 N ATOM 1543 CA SER A 105 -35.831 66.738 28.070 1.00 71.07 C ANISOU 1543 CA SER A 105 8282 9059 9662 195 412 -319 C ATOM 1544 C SER A 105 -34.963 66.125 29.161 1.00 70.14 C ANISOU 1544 C SER A 105 8143 8991 9514 221 409 -327 C ATOM 1545 O SER A 105 -35.403 65.235 29.892 1.00 68.51 O ANISOU 1545 O SER A 105 7961 8766 9301 249 403 -329 O ATOM 1546 CB SER A 105 -35.627 65.981 26.762 1.00 72.51 C ANISOU 1546 CB SER A 105 8475 9248 9825 229 413 -307 C ATOM 1547 OG SER A 105 -36.394 66.578 25.729 1.00 73.52 O ANISOU 1547 OG SER A 105 8618 9340 9976 205 415 -297 O ATOM 1548 N ALA A 106 -33.721 66.595 29.249 1.00 70.45 N ANISOU 1548 N ALA A 106 8137 9100 9530 210 414 -331 N ATOM 1549 CA ALA A 106 -32.845 66.293 30.379 1.00 69.90 C ANISOU 1549 CA ALA A 106 8035 9094 9429 227 412 -340 C ATOM 1550 C ALA A 106 -33.346 66.884 31.709 1.00 69.38 C ANISOU 1550 C ALA A 106 7966 9011 9383 189 410 -355 C ATOM 1551 O ALA A 106 -33.059 66.328 32.769 1.00 67.48 O ANISOU 1551 O ALA A 106 7715 8803 9120 213 404 -359 O ATOM 1552 CB ALA A 106 -31.432 66.779 30.083 1.00 70.30 C ANISOU 1552 CB ALA A 106 8028 9236 9444 212 419 -344 C ATOM 1553 N SER A 107 -34.088 67.991 31.658 1.00 70.85 N ANISOU 1553 N SER A 107 8163 9148 9608 136 414 -364 N ATOM 1554 CA SER A 107 -34.585 68.653 32.880 1.00 73.69 C ANISOU 1554 CA SER A 107 8520 9492 9986 100 413 -385 C ATOM 1555 C SER A 107 -35.766 67.944 33.553 1.00 73.18 C ANISOU 1555 C SER A 107 8488 9383 9934 123 405 -386 C ATOM 1556 O SER A 107 -35.952 68.087 34.762 1.00 73.65 O ANISOU 1556 O SER A 107 8536 9455 9992 108 402 -403 O ATOM 1557 CB SER A 107 -34.967 70.113 32.596 1.00 75.15 C ANISOU 1557 CB SER A 107 8712 9635 10207 42 420 -396 C ATOM 1558 OG SER A 107 -35.251 70.811 33.801 1.00 76.17 O ANISOU 1558 OG SER A 107 8834 9758 10348 8 421 -423 O ATOM 1559 N VAL A 108 -36.565 67.198 32.788 1.00 73.53 N ANISOU 1559 N VAL A 108 8570 9381 9986 151 401 -371 N ATOM 1560 CA VAL A 108 -37.699 66.453 33.370 1.00 74.09 C ANISOU 1560 CA VAL A 108 8673 9416 10061 163 394 -372 C ATOM 1561 C VAL A 108 -37.293 65.052 33.857 1.00 73.36 C ANISOU 1561 C VAL A 108 8597 9345 9932 207 387 -359 C ATOM 1562 O VAL A 108 -37.869 64.538 34.818 1.00 76.54 O ANISOU 1562 O VAL A 108 9016 9739 10326 206 382 -361 O ATOM 1563 CB VAL A 108 -38.918 66.385 32.423 1.00 73.96 C ANISOU 1563 CB VAL A 108 8691 9343 10067 161 393 -366 C ATOM 1564 CG1 VAL A 108 -39.203 67.750 31.804 1.00 74.40 C ANISOU 1564 CG1 VAL A 108 8737 9376 10155 131 398 -373 C ATOM 1565 CG2 VAL A 108 -38.727 65.351 31.343 1.00 75.03 C ANISOU 1565 CG2 VAL A 108 8852 9469 10184 197 393 -347 C ATOM 1566 N SER A 109 -36.322 64.434 33.190 1.00 70.62 N ANISOU 1566 N SER A 109 8248 9024 9560 248 388 -345 N ATOM 1567 CA SER A 109 -35.674 63.236 33.724 1.00 69.72 C ANISOU 1567 CA SER A 109 8146 8937 9406 301 381 -332 C ATOM 1568 C SER A 109 -34.964 63.559 35.037 1.00 69.71 C ANISOU 1568 C SER A 109 8102 8999 9384 294 379 -340 C ATOM 1569 O SER A 109 -35.073 62.799 36.001 1.00 70.59 O ANISOU 1569 O SER A 109 8231 9114 9474 316 371 -331 O ATOM 1570 CB SER A 109 -34.679 62.668 32.716 1.00 69.56 C ANISOU 1570 CB SER A 109 8124 8944 9360 352 383 -322 C ATOM 1571 OG SER A 109 -35.351 62.285 31.529 1.00 70.20 O ANISOU 1571 OG SER A 109 8246 8970 9456 358 385 -317 O ATOM 1572 N PHE A 110 -34.257 64.695 35.060 1.00 68.29 N ANISOU 1572 N PHE A 110 7869 8869 9209 259 385 -355 N ATOM 1573 CA PHE A 110 -33.593 65.218 36.266 1.00 66.33 C ANISOU 1573 CA PHE A 110 7571 8688 8941 237 385 -370 C ATOM 1574 C PHE A 110 -34.564 65.252 37.447 1.00 64.49 C ANISOU 1574 C PHE A 110 7353 8428 8721 212 381 -380 C ATOM 1575 O PHE A 110 -34.315 64.639 38.482 1.00 63.43 O ANISOU 1575 O PHE A 110 7213 8331 8556 234 374 -373 O ATOM 1576 CB PHE A 110 -33.036 66.628 36.000 1.00 67.13 C ANISOU 1576 CB PHE A 110 7628 8822 9055 179 396 -391 C ATOM 1577 CG PHE A 110 -31.961 67.055 36.956 1.00 67.39 C ANISOU 1577 CG PHE A 110 7601 8948 9053 159 399 -407 C ATOM 1578 CD1 PHE A 110 -30.626 66.733 36.709 1.00 68.26 C ANISOU 1578 CD1 PHE A 110 7668 9149 9117 190 399 -400 C ATOM 1579 CD2 PHE A 110 -32.270 67.797 38.087 1.00 66.89 C ANISOU 1579 CD2 PHE A 110 7522 8892 9000 109 401 -432 C ATOM 1580 CE1 PHE A 110 -29.625 67.129 37.583 1.00 68.56 C ANISOU 1580 CE1 PHE A 110 7645 9289 9116 168 401 -416 C ATOM 1581 CE2 PHE A 110 -31.273 68.198 38.966 1.00 68.02 C ANISOU 1581 CE2 PHE A 110 7608 9129 9107 85 403 -450 C ATOM 1582 CZ PHE A 110 -29.950 67.863 38.716 1.00 68.71 C ANISOU 1582 CZ PHE A 110 7648 9311 9144 113 404 -441 C ATOM 1583 N ASN A 111 -35.694 65.928 37.263 1.00 63.16 N ANISOU 1583 N ASN A 111 7204 8199 8593 170 385 -393 N ATOM 1584 CA ASN A 111 -36.704 66.056 38.319 1.00 62.17 C ANISOU 1584 CA ASN A 111 7087 8055 8479 143 381 -408 C ATOM 1585 C ASN A 111 -37.140 64.708 38.917 1.00 61.11 C ANISOU 1585 C ASN A 111 6988 7911 8317 176 372 -387 C ATOM 1586 O ASN A 111 -37.386 64.619 40.126 1.00 61.75 O ANISOU 1586 O ASN A 111 7059 8018 8383 161 367 -394 O ATOM 1587 CB ASN A 111 -37.923 66.822 37.798 1.00 62.80 C ANISOU 1587 CB ASN A 111 7186 8071 8602 111 385 -423 C ATOM 1588 CG ASN A 111 -38.959 67.083 38.878 1.00 63.35 C ANISOU 1588 CG ASN A 111 7254 8134 8679 84 383 -446 C ATOM 1589 OD1 ASN A 111 -40.101 66.630 38.782 1.00 63.95 O ANISOU 1589 OD1 ASN A 111 7359 8175 8761 85 379 -443 O ATOM 1590 ND2 ASN A 111 -38.558 67.799 39.921 1.00 63.29 N ANISOU 1590 ND2 ASN A 111 7209 8169 8666 56 386 -472 N ATOM 1591 N LEU A 112 -37.216 63.671 38.084 1.00 57.65 N ANISOU 1591 N LEU A 112 6595 7438 7870 216 368 -361 N ATOM 1592 CA LEU A 112 -37.571 62.331 38.555 1.00 56.40 C ANISOU 1592 CA LEU A 112 6486 7259 7683 244 360 -338 C ATOM 1593 C LEU A 112 -36.473 61.717 39.420 1.00 57.88 C ANISOU 1593 C LEU A 112 6660 7505 7827 287 352 -321 C ATOM 1594 O LEU A 112 -36.755 61.223 40.522 1.00 58.57 O ANISOU 1594 O LEU A 112 6759 7602 7889 284 345 -311 O ATOM 1595 CB LEU A 112 -37.895 61.413 37.376 1.00 56.05 C ANISOU 1595 CB LEU A 112 6499 7155 7639 274 359 -320 C ATOM 1596 CG LEU A 112 -38.141 59.923 37.647 1.00 56.10 C ANISOU 1596 CG LEU A 112 6575 7125 7613 306 352 -293 C ATOM 1597 CD1 LEU A 112 -39.187 59.701 38.737 1.00 56.26 C ANISOU 1597 CD1 LEU A 112 6615 7134 7626 261 348 -293 C ATOM 1598 CD2 LEU A 112 -38.524 59.240 36.340 1.00 56.19 C ANISOU 1598 CD2 LEU A 112 6641 7075 7630 322 355 -286 C ATOM 1599 N TYR A 113 -35.230 61.748 38.933 1.00 58.28 N ANISOU 1599 N TYR A 113 6681 7601 7860 329 353 -317 N ATOM 1600 CA TYR A 113 -34.098 61.171 39.679 1.00 58.94 C ANISOU 1600 CA TYR A 113 6743 7755 7894 382 345 -301 C ATOM 1601 C TYR A 113 -33.739 62.019 40.890 1.00 59.39 C ANISOU 1601 C TYR A 113 6736 7888 7940 343 346 -320 C ATOM 1602 O TYR A 113 -33.607 61.491 41.994 1.00 61.27 O ANISOU 1602 O TYR A 113 6974 8160 8144 360 337 -306 O ATOM 1603 CB TYR A 113 -32.885 60.923 38.768 1.00 59.81 C ANISOU 1603 CB TYR A 113 6834 7906 7983 441 346 -294 C ATOM 1604 CG TYR A 113 -33.197 59.883 37.706 1.00 60.99 C ANISOU 1604 CG TYR A 113 7055 7982 8135 490 345 -276 C ATOM 1605 CD1 TYR A 113 -33.375 58.542 38.050 1.00 61.60 C ANISOU 1605 CD1 TYR A 113 7202 8018 8184 544 335 -249 C ATOM 1606 CD2 TYR A 113 -33.375 60.244 36.369 1.00 61.60 C ANISOU 1606 CD2 TYR A 113 7136 8028 8241 476 354 -287 C ATOM 1607 CE1 TYR A 113 -33.701 57.590 37.094 1.00 61.31 C ANISOU 1607 CE1 TYR A 113 7239 7907 8149 582 335 -237 C ATOM 1608 CE2 TYR A 113 -33.695 59.299 35.403 1.00 61.55 C ANISOU 1608 CE2 TYR A 113 7194 7957 8235 515 353 -276 C ATOM 1609 CZ TYR A 113 -33.858 57.973 35.774 1.00 61.60 C ANISOU 1609 CZ TYR A 113 7270 7919 8213 567 344 -253 C ATOM 1610 OH TYR A 113 -34.166 57.031 34.824 1.00 61.17 O ANISOU 1610 OH TYR A 113 7286 7797 8157 601 345 -247 O ATOM 1611 N ALA A 114 -33.621 63.330 40.700 1.00 59.29 N ANISOU 1611 N ALA A 114 6673 7898 7954 287 356 -352 N ATOM 1612 CA ALA A 114 -33.352 64.239 41.812 1.00 60.79 C ANISOU 1612 CA ALA A 114 6806 8154 8137 238 359 -378 C ATOM 1613 C ALA A 114 -34.372 64.062 42.940 1.00 63.49 C ANISOU 1613 C ALA A 114 7166 8474 8480 212 354 -382 C ATOM 1614 O ALA A 114 -33.984 63.794 44.080 1.00 65.21 O ANISOU 1614 O ALA A 114 7359 8756 8659 219 348 -377 O ATOM 1615 CB ALA A 114 -33.340 65.680 41.337 1.00 60.90 C ANISOU 1615 CB ALA A 114 6788 8164 8187 174 373 -413 C ATOM 1616 N SER A 115 -35.665 64.172 42.618 1.00 64.83 N ANISOU 1616 N SER A 115 7377 8566 8688 183 357 -388 N ATOM 1617 CA SER A 115 -36.717 64.083 43.640 1.00 66.55 C ANISOU 1617 CA SER A 115 7607 8773 8906 150 353 -396 C ATOM 1618 C SER A 115 -36.609 62.780 44.417 1.00 67.70 C ANISOU 1618 C SER A 115 7783 8936 9004 187 341 -359 C ATOM 1619 O SER A 115 -36.474 62.801 45.636 1.00 69.59 O ANISOU 1619 O SER A 115 7993 9233 9214 174 337 -363 O ATOM 1620 CB SER A 115 -38.124 64.196 43.039 1.00 67.24 C ANISOU 1620 CB SER A 115 7733 8781 9030 123 357 -405 C ATOM 1621 OG SER A 115 -38.375 65.495 42.519 1.00 67.87 O ANISOU 1621 OG SER A 115 7789 8843 9152 89 366 -439 O ATOM 1622 N VAL A 116 -36.631 61.654 43.710 1.00 68.33 N ANISOU 1622 N VAL A 116 7922 8964 9073 235 335 -324 N ATOM 1623 CA VAL A 116 -36.655 60.350 44.370 1.00 68.68 C ANISOU 1623 CA VAL A 116 8017 9004 9074 271 324 -284 C ATOM 1624 C VAL A 116 -35.422 60.135 45.262 1.00 69.48 C ANISOU 1624 C VAL A 116 8078 9193 9127 315 315 -269 C ATOM 1625 O VAL A 116 -35.564 59.655 46.390 1.00 70.72 O ANISOU 1625 O VAL A 116 8243 9378 9249 313 307 -250 O ATOM 1626 CB VAL A 116 -36.883 59.183 43.373 1.00 69.75 C ANISOU 1626 CB VAL A 116 8235 9058 9208 315 320 -253 C ATOM 1627 CG1 VAL A 116 -35.676 58.934 42.490 1.00 70.80 C ANISOU 1627 CG1 VAL A 116 8363 9206 9332 386 320 -243 C ATOM 1628 CG2 VAL A 116 -37.253 57.913 44.119 1.00 71.14 C ANISOU 1628 CG2 VAL A 116 8480 9204 9343 330 310 -214 C ATOM 1629 N PHE A 117 -34.240 60.535 44.787 1.00 67.90 N ANISOU 1629 N PHE A 117 7830 9047 8921 349 318 -277 N ATOM 1630 CA PHE A 117 -33.026 60.509 45.621 1.00 67.45 C ANISOU 1630 CA PHE A 117 7717 9096 8813 386 311 -270 C ATOM 1631 C PHE A 117 -33.107 61.467 46.809 1.00 68.33 C ANISOU 1631 C PHE A 117 7762 9279 8918 320 315 -301 C ATOM 1632 O PHE A 117 -32.622 61.140 47.894 1.00 69.88 O ANISOU 1632 O PHE A 117 7932 9550 9066 339 306 -287 O ATOM 1633 CB PHE A 117 -31.768 60.835 44.799 1.00 67.36 C ANISOU 1633 CB PHE A 117 7658 9142 8793 425 315 -279 C ATOM 1634 CG PHE A 117 -31.376 59.764 43.808 1.00 66.00 C ANISOU 1634 CG PHE A 117 7540 8928 8608 510 310 -248 C ATOM 1635 CD1 PHE A 117 -31.284 58.425 44.193 1.00 65.56 C ANISOU 1635 CD1 PHE A 117 7546 8851 8512 585 295 -204 C ATOM 1636 CD2 PHE A 117 -31.053 60.104 42.497 1.00 64.97 C ANISOU 1636 CD2 PHE A 117 7401 8782 8502 517 319 -262 C ATOM 1637 CE1 PHE A 117 -30.919 57.450 43.280 1.00 67.11 C ANISOU 1637 CE1 PHE A 117 7798 9003 8696 668 291 -181 C ATOM 1638 CE2 PHE A 117 -30.681 59.135 41.582 1.00 66.28 C ANISOU 1638 CE2 PHE A 117 7614 8914 8653 597 315 -240 C ATOM 1639 CZ PHE A 117 -30.611 57.803 41.972 1.00 67.06 C ANISOU 1639 CZ PHE A 117 7777 8986 8715 675 301 -202 C ATOM 1640 N LEU A 118 -33.698 62.646 46.598 1.00 68.76 N ANISOU 1640 N LEU A 118 7791 9312 9020 248 328 -345 N ATOM 1641 CA LEU A 118 -33.943 63.610 47.691 1.00 69.35 C ANISOU 1641 CA LEU A 118 7813 9441 9095 181 333 -384 C ATOM 1642 C LEU A 118 -34.959 63.100 48.723 1.00 70.29 C ANISOU 1642 C LEU A 118 7960 9546 9201 160 326 -373 C ATOM 1643 O LEU A 118 -34.755 63.270 49.926 1.00 71.79 O ANISOU 1643 O LEU A 118 8106 9812 9355 140 323 -383 O ATOM 1644 CB LEU A 118 -34.383 64.982 47.146 1.00 69.34 C ANISOU 1644 CB LEU A 118 7791 9404 9148 117 348 -434 C ATOM 1645 CG LEU A 118 -33.315 66.077 46.968 1.00 69.15 C ANISOU 1645 CG LEU A 118 7704 9443 9123 88 359 -467 C ATOM 1646 CD1 LEU A 118 -32.045 65.601 46.283 1.00 69.09 C ANISOU 1646 CD1 LEU A 118 7680 9485 9085 143 356 -442 C ATOM 1647 CD2 LEU A 118 -33.905 67.248 46.197 1.00 68.32 C ANISOU 1647 CD2 LEU A 118 7610 9270 9077 36 373 -504 C ATOM 1648 N LEU A 119 -36.041 62.479 48.254 1.00 71.64 N ANISOU 1648 N LEU A 119 8198 9628 9392 160 324 -355 N ATOM 1649 CA LEU A 119 -37.052 61.881 49.145 1.00 72.75 C ANISOU 1649 CA LEU A 119 8370 9755 9513 134 317 -341 C ATOM 1650 C LEU A 119 -36.529 60.653 49.888 1.00 73.52 C ANISOU 1650 C LEU A 119 8497 9884 9550 184 303 -287 C ATOM 1651 O LEU A 119 -36.925 60.415 51.025 1.00 73.84 O ANISOU 1651 O LEU A 119 8534 9964 9559 157 297 -279 O ATOM 1652 CB LEU A 119 -38.320 61.511 48.371 1.00 72.80 C ANISOU 1652 CB LEU A 119 8440 9666 9551 115 320 -336 C ATOM 1653 CG LEU A 119 -39.079 62.661 47.701 1.00 73.59 C ANISOU 1653 CG LEU A 119 8520 9732 9708 71 333 -384 C ATOM 1654 CD1 LEU A 119 -40.101 62.114 46.718 1.00 73.34 C ANISOU 1654 CD1 LEU A 119 8551 9615 9698 68 334 -370 C ATOM 1655 CD2 LEU A 119 -39.756 63.563 48.721 1.00 75.00 C ANISOU 1655 CD2 LEU A 119 8651 9955 9890 13 338 -428 C ATOM 1656 N THR A 120 -35.652 59.879 49.244 1.00 74.33 N ANISOU 1656 N THR A 120 8631 9974 9636 258 296 -251 N ATOM 1657 CA THR A 120 -34.942 58.772 49.908 1.00 74.55 C ANISOU 1657 CA THR A 120 8684 10036 9602 324 280 -199 C ATOM 1658 C THR A 120 -34.128 59.282 51.096 1.00 75.00 C ANISOU 1658 C THR A 120 8658 10219 9618 320 276 -210 C ATOM 1659 O THR A 120 -34.134 58.671 52.166 1.00 74.22 O ANISOU 1659 O THR A 120 8569 10159 9469 330 265 -178 O ATOM 1660 CB THR A 120 -33.993 58.023 48.939 1.00 73.94 C ANISOU 1660 CB THR A 120 8643 9935 9515 417 275 -169 C ATOM 1661 OG1 THR A 120 -34.649 57.801 47.687 1.00 73.29 O ANISOU 1661 OG1 THR A 120 8621 9747 9476 412 282 -172 O ATOM 1662 CG2 THR A 120 -33.570 56.675 49.511 1.00 74.32 C ANISOU 1662 CG2 THR A 120 8751 9983 9503 493 257 -108 C ATOM 1663 N CYS A 121 -33.439 60.407 50.891 1.00 77.23 N ANISOU 1663 N CYS A 121 8860 10565 9916 300 286 -255 N ATOM 1664 CA CYS A 121 -32.656 61.067 51.948 1.00 77.42 C ANISOU 1664 CA CYS A 121 8796 10717 9902 281 286 -278 C ATOM 1665 C CYS A 121 -33.522 61.642 53.063 1.00 76.65 C ANISOU 1665 C CYS A 121 8672 10645 9806 202 290 -308 C ATOM 1666 O CYS A 121 -33.161 61.536 54.231 1.00 77.94 O ANISOU 1666 O CYS A 121 8795 10900 9917 200 283 -301 O ATOM 1667 CB CYS A 121 -31.785 62.184 51.370 1.00 77.12 C ANISOU 1667 CB CYS A 121 8687 10732 9883 262 299 -324 C ATOM 1668 SG CYS A 121 -30.404 61.586 50.386 1.00 78.66 S ANISOU 1668 SG CYS A 121 8877 10960 10050 359 293 -294 S ATOM 1669 N LEU A 122 -34.642 62.268 52.702 1.00 75.70 N ANISOU 1669 N LEU A 122 8569 10451 9739 141 302 -344 N ATOM 1670 CA LEU A 122 -35.624 62.735 53.698 1.00 76.64 C ANISOU 1670 CA LEU A 122 8670 10590 9860 71 305 -375 C ATOM 1671 C LEU A 122 -36.159 61.580 54.560 1.00 77.40 C ANISOU 1671 C LEU A 122 8810 10689 9908 81 291 -325 C ATOM 1672 O LEU A 122 -36.378 61.754 55.755 1.00 78.44 O ANISOU 1672 O LEU A 122 8904 10892 10005 43 289 -337 O ATOM 1673 CB LEU A 122 -36.788 63.472 53.021 1.00 75.32 C ANISOU 1673 CB LEU A 122 8521 10340 9757 21 318 -417 C ATOM 1674 CG LEU A 122 -36.427 64.831 52.398 1.00 74.99 C ANISOU 1674 CG LEU A 122 8436 10296 9761 -5 333 -474 C ATOM 1675 CD1 LEU A 122 -37.313 65.173 51.206 1.00 74.20 C ANISOU 1675 CD1 LEU A 122 8379 10091 9722 -15 341 -488 C ATOM 1676 CD2 LEU A 122 -36.491 65.935 53.444 1.00 75.44 C ANISOU 1676 CD2 LEU A 122 8428 10423 9812 -65 342 -533 C ATOM 1677 N SER A 123 -36.354 60.412 53.948 1.00 78.24 N ANISOU 1677 N SER A 123 9000 10717 10010 128 283 -270 N ATOM 1678 CA SER A 123 -36.806 59.215 54.663 1.00 79.58 C ANISOU 1678 CA SER A 123 9231 10874 10131 137 269 -214 C ATOM 1679 C SER A 123 -35.719 58.673 55.581 1.00 82.21 C ANISOU 1679 C SER A 123 9541 11297 10397 191 254 -173 C ATOM 1680 O SER A 123 -35.953 58.449 56.772 1.00 83.31 O ANISOU 1680 O SER A 123 9668 11496 10489 164 247 -157 O ATOM 1681 CB SER A 123 -37.225 58.119 53.678 1.00 78.84 C ANISOU 1681 CB SER A 123 9241 10662 10049 172 265 -169 C ATOM 1682 OG SER A 123 -38.072 58.632 52.672 1.00 78.01 O ANISOU 1682 OG SER A 123 9151 10484 10005 133 278 -206 O ATOM 1683 N ILE A 124 -34.533 58.464 55.015 1.00 84.06 N ANISOU 1683 N ILE A 124 9768 11549 10621 269 250 -156 N ATOM 1684 CA ILE A 124 -33.374 57.985 55.777 1.00 86.24 C ANISOU 1684 CA ILE A 124 10014 11923 10829 336 235 -118 C ATOM 1685 C ILE A 124 -33.039 58.953 56.925 1.00 86.74 C ANISOU 1685 C ILE A 124 9970 12120 10864 284 238 -160 C ATOM 1686 O ILE A 124 -32.670 58.513 58.014 1.00 86.58 O ANISOU 1686 O ILE A 124 9932 12184 10781 304 225 -127 O ATOM 1687 CB ILE A 124 -32.158 57.734 54.846 1.00 87.08 C ANISOU 1687 CB ILE A 124 10116 12038 10932 430 231 -104 C ATOM 1688 CG1 ILE A 124 -32.437 56.519 53.945 1.00 88.14 C ANISOU 1688 CG1 ILE A 124 10367 12045 11075 494 224 -54 C ATOM 1689 CG2 ILE A 124 -30.877 57.494 55.642 1.00 88.37 C ANISOU 1689 CG2 ILE A 124 10221 12334 11022 498 217 -79 C ATOM 1690 CD1 ILE A 124 -31.568 56.445 52.706 1.00 88.75 C ANISOU 1690 CD1 ILE A 124 10445 12104 11169 568 226 -58 C ATOM 1691 N ASP A 125 -33.196 60.255 56.675 1.00 87.11 N ANISOU 1691 N ASP A 125 9954 12184 10959 217 256 -232 N ATOM 1692 CA ASP A 125 -33.033 61.289 57.697 1.00 89.25 C ANISOU 1692 CA ASP A 125 10131 12566 11211 152 264 -285 C ATOM 1693 C ASP A 125 -34.012 61.098 58.852 1.00 91.94 C ANISOU 1693 C ASP A 125 10479 12925 11527 99 260 -281 C ATOM 1694 O ASP A 125 -33.593 60.955 60.001 1.00 92.74 O ANISOU 1694 O ASP A 125 10536 13133 11566 99 251 -267 O ATOM 1695 CB ASP A 125 -33.225 62.683 57.085 1.00 89.76 C ANISOU 1695 CB ASP A 125 10154 12609 11340 88 285 -362 C ATOM 1696 CG ASP A 125 -33.189 63.788 58.122 1.00 90.64 C ANISOU 1696 CG ASP A 125 10182 12818 11438 14 295 -425 C ATOM 1697 OD1 ASP A 125 -32.132 63.950 58.765 1.00 91.93 O ANISOU 1697 OD1 ASP A 125 10278 13102 11549 24 291 -430 O ATOM 1698 OD2 ASP A 125 -34.213 64.486 58.292 1.00 90.11 O ANISOU 1698 OD2 ASP A 125 10115 12712 11408 -50 306 -473 O ATOM 1699 N ARG A 126 -35.308 61.089 58.539 1.00 93.19 N ANISOU 1699 N ARG A 126 10690 12989 11728 53 267 -291 N ATOM 1700 CA ARG A 126 -36.355 60.932 59.555 1.00 93.58 C ANISOU 1700 CA ARG A 126 10745 13058 11753 -5 265 -292 C ATOM 1701 C ARG A 126 -36.346 59.570 60.247 1.00 96.26 C ANISOU 1701 C ARG A 126 11141 13408 12026 29 246 -210 C ATOM 1702 O ARG A 126 -36.841 59.458 61.364 1.00 95.47 O ANISOU 1702 O ARG A 126 11022 13367 11882 -16 242 -206 O ATOM 1703 CB ARG A 126 -37.741 61.204 58.965 1.00 94.29 C ANISOU 1703 CB ARG A 126 10874 13053 11899 -58 276 -323 C ATOM 1704 CG ARG A 126 -37.995 62.654 58.570 1.00 95.41 C ANISOU 1704 CG ARG A 126 10960 13190 12099 -103 294 -407 C ATOM 1705 CD ARG A 126 -38.139 63.580 59.776 1.00 97.01 C ANISOU 1705 CD ARG A 126 11082 13494 12280 -163 302 -467 C ATOM 1706 NE ARG A 126 -36.854 64.091 60.263 1.00 99.17 N ANISOU 1706 NE ARG A 126 11286 13866 12525 -152 302 -485 N ATOM 1707 CZ ARG A 126 -36.680 64.816 61.370 1.00100.67 C ANISOU 1707 CZ ARG A 126 11403 14163 12685 -198 307 -534 C ATOM 1708 NH1 ARG A 126 -37.711 65.143 62.148 1.00103.08 N ANISOU 1708 NH1 ARG A 126 11690 14491 12984 -255 312 -571 N ATOM 1709 NH2 ARG A 126 -35.459 65.225 61.707 1.00100.84 N ANISOU 1709 NH2 ARG A 126 11361 14275 12675 -190 308 -548 N ATOM 1710 N TYR A 127 -35.800 58.541 59.594 1.00 99.58 N ANISOU 1710 N TYR A 127 11632 13768 12435 109 234 -147 N ATOM 1711 CA TYR A 127 -35.563 57.253 60.256 1.00103.05 C ANISOU 1711 CA TYR A 127 12131 14217 12805 159 214 -64 C ATOM 1712 C TYR A 127 -34.484 57.415 61.316 1.00107.65 C ANISOU 1712 C TYR A 127 12634 14945 13323 190 204 -56 C ATOM 1713 O TYR A 127 -34.720 57.144 62.492 1.00109.95 O ANISOU 1713 O TYR A 127 12912 15304 13557 161 195 -32 O ATOM 1714 CB TYR A 127 -35.158 56.175 59.250 1.00104.79 C ANISOU 1714 CB TYR A 127 12449 14335 13031 248 204 -6 C ATOM 1715 CG TYR A 127 -34.716 54.872 59.882 1.00106.48 C ANISOU 1715 CG TYR A 127 12731 14554 13172 318 182 80 C ATOM 1716 CD1 TYR A 127 -35.555 54.181 60.752 1.00106.27 C ANISOU 1716 CD1 TYR A 127 12762 14513 13103 271 174 124 C ATOM 1717 CD2 TYR A 127 -33.460 54.324 59.605 1.00109.00 C ANISOU 1717 CD2 TYR A 127 13059 14895 13460 434 168 120 C ATOM 1718 CE1 TYR A 127 -35.157 52.986 61.335 1.00108.16 C ANISOU 1718 CE1 TYR A 127 13074 14748 13273 336 153 209 C ATOM 1719 CE2 TYR A 127 -33.052 53.128 60.182 1.00109.45 C ANISOU 1719 CE2 TYR A 127 13186 14951 13448 510 147 203 C ATOM 1720 CZ TYR A 127 -33.902 52.462 61.047 1.00109.30 C ANISOU 1720 CZ TYR A 127 13232 14906 13390 460 139 249 C ATOM 1721 OH TYR A 127 -33.503 51.277 61.624 1.00109.70 O ANISOU 1721 OH TYR A 127 13362 14948 13370 536 117 336 O ATOM 1722 N LEU A 128 -33.309 57.874 60.891 1.00110.74 N ANISOU 1722 N LEU A 128 12966 15392 13718 243 205 -76 N ATOM 1723 CA LEU A 128 -32.182 58.111 61.807 1.00113.00 C ANISOU 1723 CA LEU A 128 13163 15833 13939 272 197 -76 C ATOM 1724 C LEU A 128 -32.487 59.157 62.887 1.00113.37 C ANISOU 1724 C LEU A 128 13114 15986 13972 177 207 -138 C ATOM 1725 O LEU A 128 -32.080 58.989 64.033 1.00114.40 O ANISOU 1725 O LEU A 128 13198 16234 14032 180 196 -118 O ATOM 1726 CB LEU A 128 -30.910 58.515 61.035 1.00114.69 C ANISOU 1726 CB LEU A 128 13323 16092 14160 333 200 -97 C ATOM 1727 CG LEU A 128 -29.957 57.392 60.603 1.00116.45 C ANISOU 1727 CG LEU A 128 13594 16309 14342 462 181 -26 C ATOM 1728 CD1 LEU A 128 -29.159 56.864 61.789 1.00118.00 C ANISOU 1728 CD1 LEU A 128 13751 16640 14444 519 161 21 C ATOM 1729 CD2 LEU A 128 -30.695 56.256 59.911 1.00116.88 C ANISOU 1729 CD2 LEU A 128 13785 16202 14421 502 173 30 C ATOM 1730 N ALA A 129 -33.207 60.217 62.520 1.00113.35 N ANISOU 1730 N ALA A 129 13087 15944 14035 96 228 -214 N ATOM 1731 CA ALA A 129 -33.468 61.344 63.428 1.00114.27 C ANISOU 1731 CA ALA A 129 13115 16153 14147 9 241 -287 C ATOM 1732 C ALA A 129 -34.330 61.003 64.648 1.00116.20 C ANISOU 1732 C ALA A 129 13362 16441 14347 -40 235 -272 C ATOM 1733 O ALA A 129 -34.201 61.662 65.684 1.00119.90 O ANISOU 1733 O ALA A 129 13749 17027 14779 -90 239 -315 O ATOM 1734 CB ALA A 129 -34.094 62.505 62.668 1.00113.73 C ANISOU 1734 CB ALA A 129 13035 16014 14161 -52 263 -368 C ATOM 1735 N ILE A 130 -35.204 60.000 64.527 1.00116.22 N ANISOU 1735 N ILE A 130 13456 16353 14346 -34 226 -214 N ATOM 1736 CA ILE A 130 -36.102 59.603 65.633 1.00115.61 C ANISOU 1736 CA ILE A 130 13390 16315 14223 -89 220 -194 C ATOM 1737 C ILE A 130 -36.330 58.082 65.822 1.00115.21 C ANISOU 1737 C ILE A 130 13440 16211 14121 -49 200 -90 C ATOM 1738 O ILE A 130 -37.267 57.685 66.514 1.00114.83 O ANISOU 1738 O ILE A 130 13419 16167 14042 -106 198 -70 O ATOM 1739 CB ILE A 130 -37.453 60.385 65.555 1.00114.93 C ANISOU 1739 CB ILE A 130 13293 16188 14187 -180 239 -265 C ATOM 1740 CG1 ILE A 130 -37.884 60.601 64.100 1.00113.43 C ANISOU 1740 CG1 ILE A 130 13155 15860 14080 -169 249 -286 C ATOM 1741 CG2 ILE A 130 -37.335 61.742 66.241 1.00115.69 C ANISOU 1741 CG2 ILE A 130 13279 16389 14286 -237 253 -358 C ATOM 1742 CD1 ILE A 130 -39.287 61.142 63.928 1.00111.94 C ANISOU 1742 CD1 ILE A 130 12971 15624 13935 -241 264 -341 C ATOM 1743 N VAL A 131 -35.480 57.239 65.224 1.00116.64 N ANISOU 1743 N VAL A 131 13680 16346 14292 47 186 -26 N ATOM 1744 CA VAL A 131 -35.342 55.818 65.629 1.00117.33 C ANISOU 1744 CA VAL A 131 13857 16407 14313 104 164 76 C ATOM 1745 C VAL A 131 -33.969 55.550 66.272 1.00119.18 C ANISOU 1745 C VAL A 131 14043 16760 14477 189 146 117 C ATOM 1746 O VAL A 131 -33.870 54.723 67.182 1.00122.28 O ANISOU 1746 O VAL A 131 14468 17197 14795 212 128 188 O ATOM 1747 CB VAL A 131 -35.579 54.832 64.454 1.00116.13 C ANISOU 1747 CB VAL A 131 13835 16092 14196 157 160 128 C ATOM 1748 CG1 VAL A 131 -35.489 53.380 64.924 1.00116.80 C ANISOU 1748 CG1 VAL A 131 14027 16139 14211 211 137 233 C ATOM 1749 CG2 VAL A 131 -36.935 55.087 63.811 1.00115.04 C ANISOU 1749 CG2 VAL A 131 13737 15851 14120 71 177 88 C ATOM 1750 N HIS A 132 -32.922 56.227 65.791 1.00118.05 N ANISOU 1750 N HIS A 132 13826 16673 14353 236 151 75 N ATOM 1751 CA HIS A 132 -31.604 56.207 66.430 1.00118.17 C ANISOU 1751 CA HIS A 132 13767 16833 14299 305 138 95 C ATOM 1752 C HIS A 132 -31.064 57.630 66.635 1.00117.55 C ANISOU 1752 C HIS A 132 13550 16879 14233 252 155 1 C ATOM 1753 O HIS A 132 -30.082 58.022 65.994 1.00116.32 O ANISOU 1753 O HIS A 132 13347 16757 14089 299 158 -23 O ATOM 1754 CB HIS A 132 -30.630 55.366 65.601 1.00118.10 C ANISOU 1754 CB HIS A 132 13813 16779 14279 438 123 153 C ATOM 1755 CG HIS A 132 -30.927 53.901 65.637 1.00118.92 C ANISOU 1755 CG HIS A 132 14052 16782 14348 504 103 253 C ATOM 1756 ND1 HIS A 132 -30.688 53.124 66.749 1.00120.29 N ANISOU 1756 ND1 HIS A 132 14243 17025 14433 542 81 327 N ATOM 1757 CD2 HIS A 132 -31.446 53.072 64.702 1.00118.19 C ANISOU 1757 CD2 HIS A 132 14088 16522 14295 535 101 291 C ATOM 1758 CE1 HIS A 132 -31.046 51.878 66.498 1.00120.94 C ANISOU 1758 CE1 HIS A 132 14468 16979 14504 593 67 408 C ATOM 1759 NE2 HIS A 132 -31.509 51.819 65.262 1.00119.47 N ANISOU 1759 NE2 HIS A 132 14350 16648 14394 588 80 386 N ATOM 1760 N PRO A 133 -31.705 58.412 67.533 1.00116.61 N ANISOU 1760 N PRO A 133 13368 16828 14108 149 166 -54 N ATOM 1761 CA PRO A 133 -31.226 59.768 67.830 1.00116.16 C ANISOU 1761 CA PRO A 133 13189 16887 14059 89 183 -147 C ATOM 1762 C PRO A 133 -29.961 59.786 68.693 1.00117.21 C ANISOU 1762 C PRO A 133 13229 17199 14104 130 172 -134 C ATOM 1763 O PRO A 133 -29.499 58.737 69.154 1.00117.88 O ANISOU 1763 O PRO A 133 13343 17327 14119 209 148 -49 O ATOM 1764 CB PRO A 133 -32.404 60.398 68.583 1.00115.99 C ANISOU 1764 CB PRO A 133 13144 16875 14051 -22 197 -202 C ATOM 1765 CG PRO A 133 -33.093 59.251 69.231 1.00116.26 C ANISOU 1765 CG PRO A 133 13251 16885 14036 -14 179 -120 C ATOM 1766 CD PRO A 133 -32.919 58.079 68.306 1.00116.58 C ANISOU 1766 CD PRO A 133 13404 16801 14088 79 165 -36 C ATOM 1767 N THR A 141 -25.020 65.988 61.364 1.00100.54 N ANISOU 1767 N THR A 141 10855 15051 12292 16 294 -535 N ATOM 1768 CA THR A 141 -24.364 65.751 60.080 1.00101.24 C ANISOU 1768 CA THR A 141 10961 15106 12398 74 294 -514 C ATOM 1769 C THR A 141 -24.843 66.754 59.020 1.00101.43 C ANISOU 1769 C THR A 141 11022 15007 12510 0 317 -567 C ATOM 1770 O THR A 141 -25.394 66.369 57.984 1.00 99.57 O ANISOU 1770 O THR A 141 10865 14631 12334 38 315 -539 O ATOM 1771 CB THR A 141 -24.590 64.296 59.592 1.00100.25 C ANISOU 1771 CB THR A 141 10919 14897 12273 201 271 -426 C ATOM 1772 OG1 THR A 141 -25.991 64.047 59.417 1.00 97.24 O ANISOU 1772 OG1 THR A 141 10635 14350 11961 184 272 -412 O ATOM 1773 CG2 THR A 141 -24.017 63.294 60.586 1.00100.37 C ANISOU 1773 CG2 THR A 141 10905 15033 12195 286 247 -366 C ATOM 1774 N MET A 142 -24.632 68.041 59.300 1.00102.92 N ANISOU 1774 N MET A 142 11155 15246 12703 -110 337 -644 N ATOM 1775 CA MET A 142 -25.006 69.120 58.366 1.00104.01 C ANISOU 1775 CA MET A 142 11326 15272 12918 -188 360 -697 C ATOM 1776 C MET A 142 -24.073 69.185 57.158 1.00104.24 C ANISOU 1776 C MET A 142 11344 15315 12945 -166 364 -688 C ATOM 1777 O MET A 142 -24.521 69.447 56.038 1.00103.80 O ANISOU 1777 O MET A 142 11350 15129 12959 -173 373 -690 O ATOM 1778 CB MET A 142 -25.030 70.486 59.069 1.00105.59 C ANISOU 1778 CB MET A 142 11481 15518 13119 -313 381 -784 C ATOM 1779 CG MET A 142 -26.312 70.774 59.841 1.00106.44 C ANISOU 1779 CG MET A 142 11626 15549 13266 -353 384 -813 C ATOM 1780 SD MET A 142 -27.743 71.119 58.791 1.00105.75 S ANISOU 1780 SD MET A 142 11649 15237 13293 -361 393 -821 S ATOM 1781 CE MET A 142 -27.317 72.713 58.091 1.00104.32 C ANISOU 1781 CE MET A 142 11463 15023 13151 -465 421 -899 C ATOM 1782 N LEU A 143 -22.781 68.962 57.396 1.00105.27 N ANISOU 1782 N LEU A 143 11389 15613 12992 -139 359 -680 N ATOM 1783 CA LEU A 143 -21.773 68.919 56.328 1.00105.06 C ANISOU 1783 CA LEU A 143 11336 15633 12946 -111 362 -670 C ATOM 1784 C LEU A 143 -22.050 67.761 55.359 1.00104.24 C ANISOU 1784 C LEU A 143 11306 15427 12872 9 345 -600 C ATOM 1785 O LEU A 143 -22.073 67.957 54.140 1.00103.39 O ANISOU 1785 O LEU A 143 11237 15236 12811 8 354 -601 O ATOM 1786 CB LEU A 143 -20.361 68.795 56.935 1.00105.72 C ANISOU 1786 CB LEU A 143 11305 15943 12921 -96 356 -674 C ATOM 1787 CG LEU A 143 -19.092 68.995 56.085 1.00106.39 C ANISOU 1787 CG LEU A 143 11324 16138 12959 -94 363 -683 C ATOM 1788 CD1 LEU A 143 -18.738 67.775 55.242 1.00106.10 C ANISOU 1788 CD1 LEU A 143 11312 16091 12909 50 344 -615 C ATOM 1789 CD2 LEU A 143 -19.197 70.244 55.215 1.00106.07 C ANISOU 1789 CD2 LEU A 143 11306 16019 12977 -216 390 -739 C ATOM 1790 N VAL A 144 -22.290 66.573 55.916 1.00103.84 N ANISOU 1790 N VAL A 144 11281 15377 12793 109 323 -542 N ATOM 1791 CA VAL A 144 -22.526 65.354 55.127 1.00104.68 C ANISOU 1791 CA VAL A 144 11464 15389 12917 230 306 -474 C ATOM 1792 C VAL A 144 -23.830 65.439 54.315 1.00104.10 C ANISOU 1792 C VAL A 144 11496 15111 12944 205 314 -473 C ATOM 1793 O VAL A 144 -23.909 64.886 53.216 1.00105.34 O ANISOU 1793 O VAL A 144 11709 15182 13131 267 310 -442 O ATOM 1794 CB VAL A 144 -22.517 64.085 56.025 1.00105.88 C ANISOU 1794 CB VAL A 144 11631 15584 13012 334 280 -410 C ATOM 1795 CG1 VAL A 144 -22.857 62.826 55.227 1.00105.53 C ANISOU 1795 CG1 VAL A 144 11684 15420 12990 451 265 -344 C ATOM 1796 CG2 VAL A 144 -21.162 63.925 56.716 1.00106.57 C ANISOU 1796 CG2 VAL A 144 11611 15885 12995 378 271 -406 C ATOM 1797 N ALA A 145 -24.835 66.134 54.851 1.00103.55 N ANISOU 1797 N ALA A 145 11450 14974 12921 118 324 -509 N ATOM 1798 CA ALA A 145 -26.091 66.379 54.132 1.00102.74 C ANISOU 1798 CA ALA A 145 11434 14694 12908 86 332 -516 C ATOM 1799 C ALA A 145 -25.880 67.223 52.875 1.00102.70 C ANISOU 1799 C ALA A 145 11434 14635 12950 42 350 -548 C ATOM 1800 O ALA A 145 -26.451 66.922 51.826 1.00103.06 O ANISOU 1800 O ALA A 145 11549 14559 13050 72 350 -526 O ATOM 1801 CB ALA A 145 -27.105 67.052 55.044 1.00102.67 C ANISOU 1801 CB ALA A 145 11432 14649 12928 4 340 -557 C ATOM 1802 N LYS A 146 -25.069 68.275 52.993 1.00103.27 N ANISOU 1802 N LYS A 146 11435 14803 13000 -34 365 -600 N ATOM 1803 CA LYS A 146 -24.705 69.126 51.847 1.00102.37 C ANISOU 1803 CA LYS A 146 11321 14655 12917 -86 382 -628 C ATOM 1804 C LYS A 146 -23.841 68.383 50.821 1.00100.04 C ANISOU 1804 C LYS A 146 11017 14397 12594 -4 374 -587 C ATOM 1805 O LYS A 146 -24.041 68.541 49.613 1.00 97.26 O ANISOU 1805 O LYS A 146 10710 13955 12290 -5 381 -582 O ATOM 1806 CB LYS A 146 -23.993 70.400 52.316 1.00104.54 C ANISOU 1806 CB LYS A 146 11524 15030 13163 -199 400 -693 C ATOM 1807 CG LYS A 146 -24.899 71.348 53.086 1.00105.71 C ANISOU 1807 CG LYS A 146 11694 15118 13353 -288 412 -746 C ATOM 1808 CD LYS A 146 -24.198 72.649 53.438 1.00107.06 C ANISOU 1808 CD LYS A 146 11808 15369 13498 -407 433 -815 C ATOM 1809 CE LYS A 146 -25.167 73.624 54.089 1.00108.81 C ANISOU 1809 CE LYS A 146 12065 15510 13768 -488 446 -872 C ATOM 1810 NZ LYS A 146 -24.544 74.944 54.386 1.00110.35 N ANISOU 1810 NZ LYS A 146 12222 15762 13943 -612 469 -944 N ATOM 1811 N VAL A 147 -22.896 67.577 51.308 1.00 97.78 N ANISOU 1811 N VAL A 147 10674 14249 12229 70 360 -559 N ATOM 1812 CA VAL A 147 -22.089 66.693 50.448 1.00 96.52 C ANISOU 1812 CA VAL A 147 10504 14132 12034 172 350 -518 C ATOM 1813 C VAL A 147 -22.985 65.731 49.654 1.00 93.87 C ANISOU 1813 C VAL A 147 10273 13638 11754 255 339 -470 C ATOM 1814 O VAL A 147 -22.726 65.476 48.475 1.00 92.37 O ANISOU 1814 O VAL A 147 10105 13414 11578 295 341 -457 O ATOM 1815 CB VAL A 147 -21.026 65.908 51.268 1.00 97.81 C ANISOU 1815 CB VAL A 147 10594 14470 12099 256 332 -493 C ATOM 1816 CG1 VAL A 147 -20.390 64.778 50.459 1.00 97.83 C ANISOU 1816 CG1 VAL A 147 10607 14495 12068 390 318 -445 C ATOM 1817 CG2 VAL A 147 -19.941 66.854 51.769 1.00 99.11 C ANISOU 1817 CG2 VAL A 147 10644 14814 12198 173 345 -543 C ATOM 1818 N THR A 148 -24.033 65.212 50.297 1.00 91.03 N ANISOU 1818 N THR A 148 9977 13189 11422 273 329 -447 N ATOM 1819 CA THR A 148 -25.015 64.359 49.618 1.00 88.19 C ANISOU 1819 CA THR A 148 9720 12673 11115 331 322 -408 C ATOM 1820 C THR A 148 -25.757 65.131 48.524 1.00 85.81 C ANISOU 1820 C THR A 148 9463 12246 10892 265 338 -434 C ATOM 1821 O THR A 148 -25.741 64.718 47.366 1.00 85.72 O ANISOU 1821 O THR A 148 9491 12173 10902 311 338 -414 O ATOM 1822 CB THR A 148 -26.047 63.754 50.597 1.00 87.60 C ANISOU 1822 CB THR A 148 9698 12536 11048 341 310 -382 C ATOM 1823 OG1 THR A 148 -25.376 63.186 51.729 1.00 86.59 O ANISOU 1823 OG1 THR A 148 9524 12530 10843 390 295 -359 O ATOM 1824 CG2 THR A 148 -26.872 62.669 49.912 1.00 87.62 C ANISOU 1824 CG2 THR A 148 9805 12399 11086 409 301 -336 C ATOM 1825 N CYS A 149 -26.372 66.258 48.892 1.00 83.09 N ANISOU 1825 N CYS A 149 9113 11869 10588 162 352 -479 N ATOM 1826 CA CYS A 149 -27.184 67.064 47.959 1.00 82.21 C ANISOU 1826 CA CYS A 149 9049 11634 10552 101 366 -503 C ATOM 1827 C CYS A 149 -26.483 67.414 46.636 1.00 82.05 C ANISOU 1827 C CYS A 149 9018 11617 10539 98 376 -506 C ATOM 1828 O CYS A 149 -27.085 67.286 45.577 1.00 82.29 O ANISOU 1828 O CYS A 149 9107 11539 10618 113 378 -492 O ATOM 1829 CB CYS A 149 -27.677 68.346 48.638 1.00 82.76 C ANISOU 1829 CB CYS A 149 9102 11693 10650 -3 380 -558 C ATOM 1830 SG CYS A 149 -28.904 68.067 49.940 1.00 84.90 S ANISOU 1830 SG CYS A 149 9400 11924 10931 -11 372 -560 S ATOM 1831 N ILE A 150 -25.224 67.847 46.700 1.00 82.91 N ANISOU 1831 N ILE A 150 9049 11859 10595 75 382 -525 N ATOM 1832 CA ILE A 150 -24.427 68.105 45.481 1.00 82.69 C ANISOU 1832 CA ILE A 150 8999 11859 10558 72 390 -527 C ATOM 1833 C ILE A 150 -24.059 66.827 44.705 1.00 81.26 C ANISOU 1833 C ILE A 150 8837 11683 10354 191 377 -480 C ATOM 1834 O ILE A 150 -23.918 66.873 43.480 1.00 78.63 O ANISOU 1834 O ILE A 150 8521 11314 10039 199 383 -475 O ATOM 1835 CB ILE A 150 -23.156 68.965 45.749 1.00 84.60 C ANISOU 1835 CB ILE A 150 9147 12255 10741 1 402 -564 C ATOM 1836 CG1 ILE A 150 -22.146 68.248 46.669 1.00 86.12 C ANISOU 1836 CG1 ILE A 150 9261 12613 10844 64 390 -553 C ATOM 1837 CG2 ILE A 150 -23.553 70.325 46.312 1.00 84.92 C ANISOU 1837 CG2 ILE A 150 9186 12267 10812 -124 419 -616 C ATOM 1838 CD1 ILE A 150 -20.870 69.030 46.913 1.00 86.72 C ANISOU 1838 CD1 ILE A 150 9237 12860 10853 -6 401 -591 C ATOM 1839 N ILE A 151 -23.902 65.707 45.413 1.00 80.51 N ANISOU 1839 N ILE A 151 8742 11630 10217 283 359 -448 N ATOM 1840 CA ILE A 151 -23.758 64.383 44.774 1.00 81.62 C ANISOU 1840 CA ILE A 151 8923 11744 10341 406 345 -403 C ATOM 1841 C ILE A 151 -25.074 63.907 44.126 1.00 83.56 C ANISOU 1841 C ILE A 151 9276 11813 10659 422 343 -381 C ATOM 1842 O ILE A 151 -25.033 63.232 43.092 1.00 83.54 O ANISOU 1842 O ILE A 151 9314 11763 10664 487 340 -360 O ATOM 1843 CB ILE A 151 -23.197 63.325 45.766 1.00 81.38 C ANISOU 1843 CB ILE A 151 8872 11805 10242 505 325 -371 C ATOM 1844 CG1 ILE A 151 -21.726 63.631 46.074 1.00 81.27 C ANISOU 1844 CG1 ILE A 151 8746 11987 10146 512 326 -389 C ATOM 1845 CG2 ILE A 151 -23.326 61.902 45.223 1.00 81.02 C ANISOU 1845 CG2 ILE A 151 8900 11691 10190 632 309 -323 C ATOM 1846 CD1 ILE A 151 -21.192 62.950 47.315 1.00 81.99 C ANISOU 1846 CD1 ILE A 151 8796 12189 10164 581 308 -367 C ATOM 1847 N ILE A 152 -26.227 64.250 44.715 1.00 85.82 N ANISOU 1847 N ILE A 152 9605 12011 10992 363 345 -389 N ATOM 1848 CA ILE A 152 -27.535 63.905 44.109 1.00 87.30 C ANISOU 1848 CA ILE A 152 9884 12042 11243 365 344 -374 C ATOM 1849 C ILE A 152 -27.719 64.594 42.742 1.00 86.31 C ANISOU 1849 C ILE A 152 9773 11855 11165 324 358 -391 C ATOM 1850 O ILE A 152 -28.211 63.969 41.797 1.00 83.46 O ANISOU 1850 O ILE A 152 9472 11407 10831 366 356 -370 O ATOM 1851 CB ILE A 152 -28.767 64.255 45.002 1.00 87.88 C ANISOU 1851 CB ILE A 152 9988 12047 11352 304 345 -387 C ATOM 1852 CG1 ILE A 152 -28.663 63.674 46.426 1.00 89.20 C ANISOU 1852 CG1 ILE A 152 10140 12280 11472 329 332 -371 C ATOM 1853 CG2 ILE A 152 -30.059 63.773 44.335 1.00 87.71 C ANISOU 1853 CG2 ILE A 152 10055 11885 11384 311 344 -369 C ATOM 1854 CD1 ILE A 152 -28.258 62.216 46.505 1.00 91.22 C ANISOU 1854 CD1 ILE A 152 10429 12547 11681 439 315 -319 C ATOM 1855 N TRP A 153 -27.336 65.871 42.653 1.00 84.99 N ANISOU 1855 N TRP A 153 9554 11730 11005 240 372 -428 N ATOM 1856 CA TRP A 153 -27.359 66.611 41.377 1.00 85.24 C ANISOU 1856 CA TRP A 153 9595 11716 11074 197 385 -440 C ATOM 1857 C TRP A 153 -26.467 65.971 40.306 1.00 84.00 C ANISOU 1857 C TRP A 153 9425 11606 10885 264 384 -420 C ATOM 1858 O TRP A 153 -26.832 65.961 39.134 1.00 83.46 O ANISOU 1858 O TRP A 153 9395 11465 10850 267 388 -412 O ATOM 1859 CB TRP A 153 -26.962 68.084 41.576 1.00 86.01 C ANISOU 1859 CB TRP A 153 9644 11859 11175 92 401 -481 C ATOM 1860 CG TRP A 153 -28.081 68.959 42.105 1.00 86.21 C ANISOU 1860 CG TRP A 153 9704 11795 11254 20 408 -507 C ATOM 1861 CD1 TRP A 153 -28.715 68.847 43.309 1.00 86.07 C ANISOU 1861 CD1 TRP A 153 9692 11769 11240 15 402 -517 C ATOM 1862 CD2 TRP A 153 -28.676 70.084 41.445 1.00 86.16 C ANISOU 1862 CD2 TRP A 153 9731 11702 11302 -49 420 -528 C ATOM 1863 NE1 TRP A 153 -29.674 69.821 43.437 1.00 86.18 N ANISOU 1863 NE1 TRP A 153 9738 11700 11307 -49 410 -547 N ATOM 1864 CE2 TRP A 153 -29.670 70.597 42.308 1.00 85.51 C ANISOU 1864 CE2 TRP A 153 9672 11562 11254 -87 421 -553 C ATOM 1865 CE3 TRP A 153 -28.470 70.706 40.202 1.00 86.64 C ANISOU 1865 CE3 TRP A 153 9804 11730 11383 -82 430 -527 C ATOM 1866 CZ2 TRP A 153 -30.458 71.702 41.972 1.00 85.42 C ANISOU 1866 CZ2 TRP A 153 9700 11458 11297 -146 432 -577 C ATOM 1867 CZ3 TRP A 153 -29.256 71.807 39.867 1.00 86.39 C ANISOU 1867 CZ3 TRP A 153 9815 11601 11405 -145 440 -546 C ATOM 1868 CH2 TRP A 153 -30.239 72.291 40.753 1.00 85.40 C ANISOU 1868 CH2 TRP A 153 9715 11416 11314 -172 440 -571 C ATOM 1869 N LEU A 154 -25.313 65.443 40.717 1.00 84.14 N ANISOU 1869 N LEU A 154 9383 11750 10833 319 377 -414 N ATOM 1870 CA LEU A 154 -24.387 64.748 39.814 1.00 83.40 C ANISOU 1870 CA LEU A 154 9269 11720 10698 397 373 -398 C ATOM 1871 C LEU A 154 -25.009 63.478 39.222 1.00 82.71 C ANISOU 1871 C LEU A 154 9263 11531 10629 493 362 -365 C ATOM 1872 O LEU A 154 -24.993 63.286 38.002 1.00 82.47 O ANISOU 1872 O LEU A 154 9255 11465 10612 515 367 -360 O ATOM 1873 CB LEU A 154 -23.093 64.400 40.557 1.00 84.59 C ANISOU 1873 CB LEU A 154 9338 12037 10766 448 366 -399 C ATOM 1874 CG LEU A 154 -21.959 63.698 39.805 1.00 86.12 C ANISOU 1874 CG LEU A 154 9490 12330 10898 540 361 -390 C ATOM 1875 CD1 LEU A 154 -21.454 64.536 38.637 1.00 85.37 C ANISOU 1875 CD1 LEU A 154 9356 12273 10805 476 378 -412 C ATOM 1876 CD2 LEU A 154 -20.830 63.392 40.779 1.00 86.81 C ANISOU 1876 CD2 LEU A 154 9496 12586 10902 592 352 -391 C ATOM 1877 N LEU A 155 -25.557 62.627 40.090 1.00 79.92 N ANISOU 1877 N LEU A 155 8956 11133 10274 543 349 -342 N ATOM 1878 CA LEU A 155 -26.212 61.381 39.667 1.00 77.94 C ANISOU 1878 CA LEU A 155 8795 10778 10038 623 339 -311 C ATOM 1879 C LEU A 155 -27.493 61.608 38.847 1.00 76.16 C ANISOU 1879 C LEU A 155 8640 10412 9883 572 347 -314 C ATOM 1880 O LEU A 155 -27.785 60.837 37.931 1.00 77.00 O ANISOU 1880 O LEU A 155 8805 10450 10002 622 345 -299 O ATOM 1881 CB LEU A 155 -26.534 60.504 40.882 1.00 78.87 C ANISOU 1881 CB LEU A 155 8951 10881 10133 671 323 -285 C ATOM 1882 CG LEU A 155 -25.344 59.961 41.684 1.00 80.06 C ANISOU 1882 CG LEU A 155 9048 11162 10207 752 311 -271 C ATOM 1883 CD1 LEU A 155 -25.772 59.563 43.090 1.00 80.07 C ANISOU 1883 CD1 LEU A 155 9071 11158 10192 757 299 -250 C ATOM 1884 CD2 LEU A 155 -24.702 58.780 40.966 1.00 80.79 C ANISOU 1884 CD2 LEU A 155 9172 11260 10262 879 301 -247 C ATOM 1885 N ALA A 156 -28.259 62.647 39.180 1.00 73.15 N ANISOU 1885 N ALA A 156 8255 9992 9547 475 355 -334 N ATOM 1886 CA ALA A 156 -29.480 62.983 38.433 1.00 71.11 C ANISOU 1886 CA ALA A 156 8051 9614 9350 427 362 -338 C ATOM 1887 C ALA A 156 -29.154 63.577 37.057 1.00 69.52 C ANISOU 1887 C ALA A 156 7835 9413 9166 405 373 -348 C ATOM 1888 O ALA A 156 -29.893 63.363 36.093 1.00 68.12 O ANISOU 1888 O ALA A 156 7709 9150 9022 408 375 -341 O ATOM 1889 CB ALA A 156 -30.362 63.940 39.233 1.00 70.28 C ANISOU 1889 CB ALA A 156 7944 9476 9283 341 367 -359 C ATOM 1890 N GLY A 157 -28.061 64.336 36.979 1.00 69.30 N ANISOU 1890 N GLY A 157 7733 9486 9109 377 381 -365 N ATOM 1891 CA GLY A 157 -27.527 64.815 35.701 1.00 69.63 C ANISOU 1891 CA GLY A 157 7753 9552 9151 359 391 -371 C ATOM 1892 C GLY A 157 -27.031 63.666 34.841 1.00 69.87 C ANISOU 1892 C GLY A 157 7797 9597 9150 455 385 -353 C ATOM 1893 O GLY A 157 -27.419 63.542 33.679 1.00 70.97 O ANISOU 1893 O GLY A 157 7971 9678 9313 460 389 -348 O ATOM 1894 N LEU A 158 -26.200 62.809 35.428 1.00 70.38 N ANISOU 1894 N LEU A 158 7838 9742 9160 535 375 -345 N ATOM 1895 CA LEU A 158 -25.712 61.606 34.746 1.00 71.74 C ANISOU 1895 CA LEU A 158 8032 9927 9298 644 368 -331 C ATOM 1896 C LEU A 158 -26.819 60.600 34.384 1.00 71.08 C ANISOU 1896 C LEU A 158 8051 9706 9250 687 362 -312 C ATOM 1897 O LEU A 158 -26.718 59.921 33.363 1.00 71.78 O ANISOU 1897 O LEU A 158 8170 9769 9331 744 362 -309 O ATOM 1898 CB LEU A 158 -24.613 60.922 35.576 1.00 72.55 C ANISOU 1898 CB LEU A 158 8089 10144 9330 730 356 -325 C ATOM 1899 CG LEU A 158 -23.306 61.725 35.690 1.00 72.80 C ANISOU 1899 CG LEU A 158 8010 10341 9309 701 363 -346 C ATOM 1900 CD1 LEU A 158 -22.415 61.188 36.801 1.00 73.56 C ANISOU 1900 CD1 LEU A 158 8056 10553 9337 773 350 -340 C ATOM 1901 CD2 LEU A 158 -22.555 61.739 34.367 1.00 73.29 C ANISOU 1901 CD2 LEU A 158 8036 10464 9346 723 371 -357 C ATOM 1902 N ALA A 159 -27.867 60.507 35.201 1.00 70.39 N ANISOU 1902 N ALA A 159 8015 9535 9195 656 357 -303 N ATOM 1903 CA ALA A 159 -29.026 59.656 34.880 1.00 70.07 C ANISOU 1903 CA ALA A 159 8070 9365 9185 674 353 -288 C ATOM 1904 C ALA A 159 -29.905 60.247 33.765 1.00 69.47 C ANISOU 1904 C ALA A 159 8017 9215 9161 610 364 -298 C ATOM 1905 O ALA A 159 -30.621 59.499 33.093 1.00 69.25 O ANISOU 1905 O ALA A 159 8058 9102 9149 632 364 -291 O ATOM 1906 CB ALA A 159 -29.861 59.390 36.124 1.00 70.22 C ANISOU 1906 CB ALA A 159 8130 9335 9216 653 345 -275 C ATOM 1907 N SER A 160 -29.854 61.577 33.593 1.00 68.33 N ANISOU 1907 N SER A 160 7819 9102 9040 531 374 -315 N ATOM 1908 CA SER A 160 -30.542 62.291 32.499 1.00 67.18 C ANISOU 1908 CA SER A 160 7686 8901 8938 473 384 -321 C ATOM 1909 C SER A 160 -29.686 62.446 31.226 1.00 66.78 C ANISOU 1909 C SER A 160 7601 8903 8867 489 391 -325 C ATOM 1910 O SER A 160 -30.094 63.124 30.268 1.00 64.64 O ANISOU 1910 O SER A 160 7333 8600 8625 441 399 -328 O ATOM 1911 CB SER A 160 -30.982 63.682 32.974 1.00 67.28 C ANISOU 1911 CB SER A 160 7670 8906 8985 381 390 -336 C ATOM 1912 OG SER A 160 -31.848 63.602 34.095 1.00 68.11 O ANISOU 1912 OG SER A 160 7801 8967 9108 363 384 -336 O ATOM 1913 N LEU A 161 -28.516 61.807 31.211 1.00 66.78 N ANISOU 1913 N LEU A 161 7569 8989 8815 560 388 -325 N ATOM 1914 CA LEU A 161 -27.581 61.875 30.081 1.00 66.38 C ANISOU 1914 CA LEU A 161 7476 9012 8734 582 394 -332 C ATOM 1915 C LEU A 161 -28.101 61.182 28.803 1.00 66.68 C ANISOU 1915 C LEU A 161 7568 8981 8784 617 396 -329 C ATOM 1916 O LEU A 161 -27.656 61.535 27.705 1.00 68.49 O ANISOU 1916 O LEU A 161 7766 9252 9003 604 405 -335 O ATOM 1917 CB LEU A 161 -26.217 61.302 30.499 1.00 66.54 C ANISOU 1917 CB LEU A 161 7442 9152 8686 661 389 -336 C ATOM 1918 CG LEU A 161 -24.963 61.662 29.703 1.00 66.90 C ANISOU 1918 CG LEU A 161 7409 9326 8684 667 397 -350 C ATOM 1919 CD1 LEU A 161 -24.624 63.140 29.807 1.00 66.50 C ANISOU 1919 CD1 LEU A 161 7293 9336 8637 554 408 -360 C ATOM 1920 CD2 LEU A 161 -23.799 60.818 30.207 1.00 67.62 C ANISOU 1920 CD2 LEU A 161 7458 9528 8705 771 387 -353 C ATOM 1921 N PRO A 162 -29.027 60.198 28.932 1.00 64.89 N ANISOU 1921 N PRO A 162 7424 8654 8577 654 390 -320 N ATOM 1922 CA PRO A 162 -29.737 59.673 27.753 1.00 63.74 C ANISOU 1922 CA PRO A 162 7334 8434 8449 665 393 -320 C ATOM 1923 C PRO A 162 -30.680 60.654 27.053 1.00 62.74 C ANISOU 1923 C PRO A 162 7210 8258 8370 576 401 -320 C ATOM 1924 O PRO A 162 -30.950 60.479 25.864 1.00 63.98 O ANISOU 1924 O PRO A 162 7386 8392 8531 578 406 -322 O ATOM 1925 CB PRO A 162 -30.527 58.495 28.326 1.00 64.13 C ANISOU 1925 CB PRO A 162 7470 8391 8504 706 385 -311 C ATOM 1926 CG PRO A 162 -29.674 58.012 29.441 1.00 64.45 C ANISOU 1926 CG PRO A 162 7495 8487 8506 768 375 -305 C ATOM 1927 CD PRO A 162 -29.196 59.287 30.079 1.00 64.77 C ANISOU 1927 CD PRO A 162 7451 8608 8548 706 378 -309 C ATOM 1928 N ALA A 163 -31.184 61.655 27.776 1.00 62.33 N ANISOU 1928 N ALA A 163 7142 8190 8349 505 402 -317 N ATOM 1929 CA ALA A 163 -31.941 62.757 27.163 1.00 62.07 C ANISOU 1929 CA ALA A 163 7105 8120 8357 428 408 -316 C ATOM 1930 C ALA A 163 -31.059 63.640 26.271 1.00 63.80 C ANISOU 1930 C ALA A 163 7268 8410 8561 397 417 -317 C ATOM 1931 O ALA A 163 -31.519 64.126 25.251 1.00 63.17 O ANISOU 1931 O ALA A 163 7196 8304 8501 363 423 -310 O ATOM 1932 CB ALA A 163 -32.608 63.609 28.227 1.00 61.70 C ANISOU 1932 CB ALA A 163 7056 8042 8343 369 407 -317 C ATOM 1933 N ILE A 164 -29.796 63.838 26.656 1.00 65.67 N ANISOU 1933 N ILE A 164 7446 8745 8759 407 419 -323 N ATOM 1934 CA ILE A 164 -28.860 64.661 25.880 1.00 66.36 C ANISOU 1934 CA ILE A 164 7475 8915 8823 368 429 -325 C ATOM 1935 C ILE A 164 -28.336 63.927 24.633 1.00 67.08 C ANISOU 1935 C ILE A 164 7559 9049 8880 423 432 -327 C ATOM 1936 O ILE A 164 -28.014 64.566 23.629 1.00 66.22 O ANISOU 1936 O ILE A 164 7422 8978 8762 381 440 -323 O ATOM 1937 CB ILE A 164 -27.675 65.152 26.749 1.00 68.24 C ANISOU 1937 CB ILE A 164 7645 9260 9023 350 431 -336 C ATOM 1938 CG1 ILE A 164 -28.185 65.975 27.946 1.00 67.72 C ANISOU 1938 CG1 ILE A 164 7585 9153 8989 288 430 -340 C ATOM 1939 CG2 ILE A 164 -26.698 65.996 25.921 1.00 68.55 C ANISOU 1939 CG2 ILE A 164 7623 9391 9029 297 442 -338 C ATOM 1940 CD1 ILE A 164 -27.225 66.018 29.115 1.00 68.26 C ANISOU 1940 CD1 ILE A 164 7599 9316 9018 293 428 -353 C ATOM 1941 N ILE A 165 -28.268 62.596 24.688 1.00 67.99 N ANISOU 1941 N ILE A 165 7703 9154 8973 514 425 -332 N ATOM 1942 CA ILE A 165 -27.677 61.794 23.600 1.00 67.73 C ANISOU 1942 CA ILE A 165 7663 9167 8902 579 427 -342 C ATOM 1943 C ILE A 165 -28.675 61.506 22.478 1.00 66.06 C ANISOU 1943 C ILE A 165 7507 8873 8718 571 430 -338 C ATOM 1944 O ILE A 165 -28.389 61.763 21.311 1.00 66.95 O ANISOU 1944 O ILE A 165 7594 9027 8816 557 438 -340 O ATOM 1945 CB ILE A 165 -27.094 60.465 24.140 1.00 68.37 C ANISOU 1945 CB ILE A 165 7761 9273 8944 690 419 -352 C ATOM 1946 CG1 ILE A 165 -25.921 60.744 25.091 1.00 68.51 C ANISOU 1946 CG1 ILE A 165 7707 9404 8919 706 416 -356 C ATOM 1947 CG2 ILE A 165 -26.629 59.558 23.004 1.00 69.41 C ANISOU 1947 CG2 ILE A 165 7899 9434 9039 767 421 -366 C ATOM 1948 CD1 ILE A 165 -25.665 59.628 26.084 1.00 69.73 C ANISOU 1948 CD1 ILE A 165 7890 9555 9049 803 404 -356 C ATOM 1949 N HIS A 166 -29.840 60.976 22.840 1.00 65.90 N ANISOU 1949 N HIS A 166 7558 8745 8734 576 425 -334 N ATOM 1950 CA HIS A 166 -30.804 60.433 21.864 1.00 65.42 C ANISOU 1950 CA HIS A 166 7554 8611 8690 579 427 -335 C ATOM 1951 C HIS A 166 -31.909 61.386 21.377 1.00 66.72 C ANISOU 1951 C HIS A 166 7729 8722 8899 497 430 -322 C ATOM 1952 O HIS A 166 -32.538 61.108 20.350 1.00 68.36 O ANISOU 1952 O HIS A 166 7963 8898 9111 493 433 -323 O ATOM 1953 CB HIS A 166 -31.459 59.190 22.456 1.00 65.31 C ANISOU 1953 CB HIS A 166 7618 8515 8682 630 420 -340 C ATOM 1954 CG HIS A 166 -30.489 58.100 22.792 1.00 64.59 C ANISOU 1954 CG HIS A 166 7535 8458 8545 727 415 -352 C ATOM 1955 ND1 HIS A 166 -29.958 57.259 21.839 1.00 63.88 N ANISOU 1955 ND1 HIS A 166 7457 8392 8421 795 419 -369 N ATOM 1956 CD2 HIS A 166 -29.958 57.713 23.974 1.00 64.18 C ANISOU 1956 CD2 HIS A 166 7484 8425 8476 773 407 -348 C ATOM 1957 CE1 HIS A 166 -29.139 56.402 22.419 1.00 64.57 C ANISOU 1957 CE1 HIS A 166 7554 8507 8471 886 412 -376 C ATOM 1958 NE2 HIS A 166 -29.120 56.656 23.714 1.00 64.65 N ANISOU 1958 NE2 HIS A 166 7557 8517 8491 874 405 -361 N ATOM 1959 N ARG A 167 -32.168 62.473 22.110 1.00 67.90 N ANISOU 1959 N ARG A 167 7858 8863 9078 436 429 -310 N ATOM 1960 CA ARG A 167 -33.208 63.439 21.734 1.00 69.23 C ANISOU 1960 CA ARG A 167 8038 8980 9286 369 430 -296 C ATOM 1961 C ARG A 167 -32.763 64.309 20.571 1.00 71.83 C ANISOU 1961 C ARG A 167 8329 9357 9606 331 437 -285 C ATOM 1962 O ARG A 167 -31.728 64.971 20.656 1.00 75.57 O ANISOU 1962 O ARG A 167 8753 9899 10058 308 442 -283 O ATOM 1963 CB ARG A 167 -33.550 64.363 22.901 1.00 69.83 C ANISOU 1963 CB ARG A 167 8107 9030 9393 322 427 -292 C ATOM 1964 CG ARG A 167 -34.420 63.726 23.970 1.00 70.34 C ANISOU 1964 CG ARG A 167 8215 9034 9477 338 419 -298 C ATOM 1965 CD ARG A 167 -35.883 63.912 23.620 1.00 71.13 C ANISOU 1965 CD ARG A 167 8352 9064 9609 308 417 -294 C ATOM 1966 NE ARG A 167 -36.772 63.072 24.416 1.00 72.50 N ANISOU 1966 NE ARG A 167 8569 9185 9789 321 412 -301 N ATOM 1967 CZ ARG A 167 -38.090 63.243 24.530 1.00 72.38 C ANISOU 1967 CZ ARG A 167 8579 9121 9798 292 409 -301 C ATOM 1968 NH1 ARG A 167 -38.716 64.241 23.906 1.00 71.63 N ANISOU 1968 NH1 ARG A 167 8472 9016 9726 257 410 -294 N ATOM 1969 NH2 ARG A 167 -38.793 62.405 25.286 1.00 73.25 N ANISOU 1969 NH2 ARG A 167 8728 9196 9906 298 404 -308 N ATOM 1970 N ASN A 168 -33.549 64.320 19.498 1.00 72.25 N ANISOU 1970 N ASN A 168 8405 9378 9669 318 439 -276 N ATOM 1971 CA ASN A 168 -33.310 65.220 18.369 1.00 72.09 C ANISOU 1971 CA ASN A 168 8356 9393 9641 275 445 -258 C ATOM 1972 C ASN A 168 -34.613 65.712 17.774 1.00 70.33 C ANISOU 1972 C ASN A 168 8164 9108 9449 243 442 -240 C ATOM 1973 O ASN A 168 -35.638 65.029 17.841 1.00 69.39 O ANISOU 1973 O ASN A 168 8083 8935 9344 263 437 -249 O ATOM 1974 CB ASN A 168 -32.501 64.526 17.267 1.00 73.27 C ANISOU 1974 CB ASN A 168 8481 9613 9744 311 451 -268 C ATOM 1975 CG ASN A 168 -31.050 64.294 17.645 1.00 74.77 C ANISOU 1975 CG ASN A 168 8623 9893 9892 341 454 -282 C ATOM 1976 OD1 ASN A 168 -30.616 63.148 17.788 1.00 76.10 O ANISOU 1976 OD1 ASN A 168 8798 10082 10034 412 453 -305 O ATOM 1977 ND2 ASN A 168 -30.284 65.373 17.784 1.00 74.97 N ANISOU 1977 ND2 ASN A 168 8602 9975 9908 286 459 -270 N ATOM 1978 N VAL A 169 -34.556 66.906 17.193 1.00 69.73 N ANISOU 1978 N VAL A 169 8072 9041 9379 192 444 -215 N ATOM 1979 CA VAL A 169 -35.648 67.440 16.397 1.00 69.08 C ANISOU 1979 CA VAL A 169 8013 8917 9317 169 441 -193 C ATOM 1980 C VAL A 169 -35.652 66.672 15.084 1.00 69.84 C ANISOU 1980 C VAL A 169 8104 9050 9381 192 445 -195 C ATOM 1981 O VAL A 169 -34.666 66.708 14.347 1.00 68.88 O ANISOU 1981 O VAL A 169 7949 8997 9224 187 451 -192 O ATOM 1982 CB VAL A 169 -35.483 68.956 16.131 1.00 68.60 C ANISOU 1982 CB VAL A 169 7944 8852 9267 110 443 -161 C ATOM 1983 CG1 VAL A 169 -36.519 69.460 15.133 1.00 69.23 C ANISOU 1983 CG1 VAL A 169 8045 8899 9358 99 438 -132 C ATOM 1984 CG2 VAL A 169 -35.596 69.733 17.431 1.00 68.86 C ANISOU 1984 CG2 VAL A 169 7989 8840 9334 86 440 -164 C ATOM 1985 N PHE A 170 -36.753 65.971 14.814 1.00 71.34 N ANISOU 1985 N PHE A 170 8325 9201 9579 214 441 -204 N ATOM 1986 CA PHE A 170 -36.937 65.203 13.579 1.00 72.61 C ANISOU 1986 CA PHE A 170 8487 9391 9710 232 444 -211 C ATOM 1987 C PHE A 170 -38.202 65.661 12.863 1.00 75.67 C ANISOU 1987 C PHE A 170 8888 9752 10109 209 439 -191 C ATOM 1988 O PHE A 170 -39.186 66.015 13.513 1.00 74.70 O ANISOU 1988 O PHE A 170 8787 9578 10018 200 432 -186 O ATOM 1989 CB PHE A 170 -37.102 63.712 13.888 1.00 70.99 C ANISOU 1989 CB PHE A 170 8312 9167 9493 279 445 -249 C ATOM 1990 CG PHE A 170 -35.860 63.034 14.402 1.00 69.81 C ANISOU 1990 CG PHE A 170 8152 9052 9321 321 449 -271 C ATOM 1991 CD1 PHE A 170 -34.797 62.766 13.555 1.00 70.16 C ANISOU 1991 CD1 PHE A 170 8163 9170 9324 342 456 -279 C ATOM 1992 CD2 PHE A 170 -35.777 62.611 15.723 1.00 70.11 C ANISOU 1992 CD2 PHE A 170 8210 9055 9373 343 445 -284 C ATOM 1993 CE1 PHE A 170 -33.662 62.117 14.023 1.00 70.18 C ANISOU 1993 CE1 PHE A 170 8150 9213 9300 392 459 -301 C ATOM 1994 CE2 PHE A 170 -34.646 61.958 16.193 1.00 69.12 C ANISOU 1994 CE2 PHE A 170 8074 8966 9222 392 447 -302 C ATOM 1995 CZ PHE A 170 -33.589 61.710 15.343 1.00 68.47 C ANISOU 1995 CZ PHE A 170 7956 8959 9098 420 453 -311 C ATOM 1996 N PHE A 171 -38.174 65.633 11.529 1.00 81.80 N ANISOU 1996 N PHE A 171 9649 10573 10857 203 443 -180 N ATOM 1997 CA PHE A 171 -39.390 65.725 10.711 1.00 86.08 C ANISOU 1997 CA PHE A 171 10201 11106 11397 193 438 -168 C ATOM 1998 C PHE A 171 -40.082 64.362 10.746 1.00 89.87 C ANISOU 1998 C PHE A 171 10710 11570 11867 217 439 -207 C ATOM 1999 O PHE A 171 -39.476 63.369 11.155 1.00 90.06 O ANISOU 1999 O PHE A 171 10747 11592 11880 245 445 -239 O ATOM 2000 CB PHE A 171 -39.066 66.078 9.254 1.00 88.74 C ANISOU 2000 CB PHE A 171 10511 11506 11700 177 442 -144 C ATOM 2001 CG PHE A 171 -38.397 67.418 9.074 1.00 92.52 C ANISOU 2001 CG PHE A 171 10971 12001 12182 142 441 -101 C ATOM 2002 CD1 PHE A 171 -39.152 68.587 8.990 1.00 93.43 C ANISOU 2002 CD1 PHE A 171 11098 12079 12319 119 432 -59 C ATOM 2003 CD2 PHE A 171 -37.009 67.512 8.958 1.00 93.25 C ANISOU 2003 CD2 PHE A 171 11033 12147 12249 131 450 -102 C ATOM 2004 CE1 PHE A 171 -38.536 69.822 8.814 1.00 94.59 C ANISOU 2004 CE1 PHE A 171 11242 12230 12468 81 433 -18 C ATOM 2005 CE2 PHE A 171 -36.390 68.743 8.782 1.00 94.08 C ANISOU 2005 CE2 PHE A 171 11124 12268 12352 85 451 -62 C ATOM 2006 CZ PHE A 171 -37.153 69.899 8.710 1.00 94.76 C ANISOU 2006 CZ PHE A 171 11236 12304 12464 57 443 -19 C ATOM 2007 N ILE A 172 -41.342 64.313 10.313 1.00 94.78 N ANISOU 2007 N ILE A 172 11342 12183 12487 206 435 -204 N ATOM 2008 CA ILE A 172 -42.095 63.053 10.225 1.00 97.81 C ANISOU 2008 CA ILE A 172 11754 12555 12853 213 438 -242 C ATOM 2009 C ILE A 172 -42.794 62.927 8.869 1.00101.02 C ANISOU 2009 C ILE A 172 12147 13007 13227 198 439 -240 C ATOM 2010 O ILE A 172 -43.355 63.893 8.375 1.00102.73 O ANISOU 2010 O ILE A 172 12342 13244 13447 183 432 -204 O ATOM 2011 CB ILE A 172 -43.109 62.899 11.387 1.00 98.98 C ANISOU 2011 CB ILE A 172 11930 12650 13028 205 431 -253 C ATOM 2012 CG1 ILE A 172 -44.053 64.106 11.489 1.00100.40 C ANISOU 2012 CG1 ILE A 172 12092 12826 13229 189 421 -221 C ATOM 2013 CG2 ILE A 172 -42.365 62.719 12.703 1.00 99.95 C ANISOU 2013 CG2 ILE A 172 12069 12733 13173 223 432 -263 C ATOM 2014 CD1 ILE A 172 -45.178 63.931 12.490 1.00100.44 C ANISOU 2014 CD1 ILE A 172 12115 12797 13251 181 415 -236 C ATOM 2015 N GLU A 173 -42.717 61.743 8.256 1.00103.62 N ANISOU 2015 N GLU A 173 12492 13354 13522 205 448 -277 N ATOM 2016 CA GLU A 173 -43.425 61.436 6.999 1.00105.54 C ANISOU 2016 CA GLU A 173 12725 13645 13728 187 451 -285 C ATOM 2017 C GLU A 173 -43.284 62.492 5.886 1.00106.03 C ANISOU 2017 C GLU A 173 12740 13769 13775 176 447 -241 C ATOM 2018 O GLU A 173 -44.207 62.691 5.092 1.00105.26 O ANISOU 2018 O GLU A 173 12627 13710 13657 157 443 -230 O ATOM 2019 CB GLU A 173 -44.910 61.188 7.297 1.00107.11 C ANISOU 2019 CB GLU A 173 12941 13827 13928 161 446 -296 C ATOM 2020 N ASN A 174 -42.119 63.143 5.832 1.00109.32 N ANISOU 2020 N ASN A 174 13135 14203 14198 184 448 -217 N ATOM 2021 CA ASN A 174 -41.841 64.258 4.911 1.00110.21 C ANISOU 2021 CA ASN A 174 13210 14365 14297 167 445 -168 C ATOM 2022 C ASN A 174 -42.894 65.381 4.977 1.00110.09 C ANISOU 2022 C ASN A 174 13192 14332 14303 154 432 -122 C ATOM 2023 O ASN A 174 -43.676 65.588 4.040 1.00111.54 O ANISOU 2023 O ASN A 174 13361 14558 14461 145 427 -103 O ATOM 2024 CB ASN A 174 -41.647 63.737 3.475 1.00110.94 C ANISOU 2024 CB ASN A 174 13278 14535 14336 163 453 -180 C ATOM 2025 CG ASN A 174 -40.936 64.737 2.566 1.00111.11 C ANISOU 2025 CG ASN A 174 13262 14617 14337 144 453 -132 C ATOM 2026 OD1 ASN A 174 -40.264 65.662 3.032 1.00109.32 O ANISOU 2026 OD1 ASN A 174 13030 14374 14132 135 450 -98 O ATOM 2027 ND2 ASN A 174 -41.075 64.543 1.255 1.00110.51 N ANISOU 2027 ND2 ASN A 174 13160 14613 14215 133 456 -131 N ATOM 2028 N THR A 175 -42.899 66.086 6.108 1.00106.85 N ANISOU 2028 N THR A 175 12798 13863 13936 157 425 -105 N ATOM 2029 CA THR A 175 -43.822 67.196 6.359 1.00105.26 C ANISOU 2029 CA THR A 175 12601 13633 13759 156 412 -66 C ATOM 2030 C THR A 175 -43.048 68.416 6.843 1.00104.90 C ANISOU 2030 C THR A 175 12561 13553 13743 147 409 -27 C ATOM 2031 O THR A 175 -41.832 68.356 7.032 1.00108.74 O ANISOU 2031 O THR A 175 13043 14046 14228 136 418 -33 O ATOM 2032 CB THR A 175 -44.899 66.816 7.404 1.00104.70 C ANISOU 2032 CB THR A 175 12549 13518 13712 167 407 -94 C ATOM 2033 OG1 THR A 175 -45.906 67.836 7.460 1.00103.42 O ANISOU 2033 OG1 THR A 175 12384 13345 13563 175 393 -60 O ATOM 2034 CG2 THR A 175 -44.297 66.648 8.791 1.00105.56 C ANISOU 2034 CG2 THR A 175 12679 13570 13856 172 410 -116 C ATOM 2035 N ASN A 176 -43.769 69.516 7.045 1.00102.48 N ANISOU 2035 N ASN A 176 12267 13212 13458 151 398 9 N ATOM 2036 CA ASN A 176 -43.196 70.738 7.608 1.00101.00 C ANISOU 2036 CA ASN A 176 12098 12976 13301 139 395 43 C ATOM 2037 C ASN A 176 -42.973 70.618 9.122 1.00 97.80 C ANISOU 2037 C ASN A 176 11710 12514 12936 143 397 10 C ATOM 2038 O ASN A 176 -41.940 71.058 9.629 1.00 98.03 O ANISOU 2038 O ASN A 176 11743 12524 12977 122 403 14 O ATOM 2039 CB ASN A 176 -44.108 71.938 7.296 1.00102.06 C ANISOU 2039 CB ASN A 176 12248 13083 13443 152 381 92 C ATOM 2040 CG ASN A 176 -43.431 73.286 7.521 1.00102.40 C ANISOU 2040 CG ASN A 176 12321 13076 13508 130 380 135 C ATOM 2041 OD1 ASN A 176 -42.223 73.371 7.760 1.00102.43 O ANISOU 2041 OD1 ASN A 176 12325 13080 13513 95 390 132 O ATOM 2042 ND2 ASN A 176 -44.217 74.355 7.432 1.00101.91 N ANISOU 2042 ND2 ASN A 176 12288 12974 13459 150 367 176 N ATOM 2043 N ILE A 177 -43.939 70.027 9.831 1.00 94.48 N ANISOU 2043 N ILE A 177 11295 12074 12529 165 393 -22 N ATOM 2044 CA ILE A 177 -43.900 69.947 11.306 1.00 90.98 C ANISOU 2044 CA ILE A 177 10866 11579 12120 170 393 -51 C ATOM 2045 C ILE A 177 -42.747 69.072 11.846 1.00 86.47 C ANISOU 2045 C ILE A 177 10292 11016 11546 162 404 -83 C ATOM 2046 O ILE A 177 -42.479 67.981 11.331 1.00 81.65 O ANISOU 2046 O ILE A 177 9672 10443 10907 168 411 -106 O ATOM 2047 CB ILE A 177 -45.276 69.544 11.926 1.00 91.26 C ANISOU 2047 CB ILE A 177 10907 11602 12165 191 386 -76 C ATOM 2048 CG1 ILE A 177 -45.627 68.067 11.691 1.00 91.66 C ANISOU 2048 CG1 ILE A 177 10951 11687 12186 189 391 -115 C ATOM 2049 CG2 ILE A 177 -46.392 70.439 11.385 1.00 92.81 C ANISOU 2049 CG2 ILE A 177 11100 11803 12359 210 373 -44 C ATOM 2050 CD1 ILE A 177 -46.981 67.665 12.240 1.00 92.75 C ANISOU 2050 CD1 ILE A 177 11090 11824 12323 196 385 -139 C ATOM 2051 N THR A 178 -42.088 69.585 12.887 1.00 81.82 N ANISOU 2051 N THR A 178 9710 10392 10983 153 406 -86 N ATOM 2052 CA THR A 178 -40.869 69.022 13.453 1.00 78.81 C ANISOU 2052 CA THR A 178 9320 10026 10597 149 415 -109 C ATOM 2053 C THR A 178 -41.075 68.590 14.905 1.00 76.41 C ANISOU 2053 C THR A 178 9029 9685 10317 161 413 -141 C ATOM 2054 O THR A 178 -41.413 69.410 15.756 1.00 74.14 O ANISOU 2054 O THR A 178 8751 9356 10059 154 408 -137 O ATOM 2055 CB THR A 178 -39.752 70.077 13.450 1.00 81.09 C ANISOU 2055 CB THR A 178 9600 10321 10887 116 419 -84 C ATOM 2056 OG1 THR A 178 -40.214 71.271 14.101 1.00 81.62 O ANISOU 2056 OG1 THR A 178 9689 10331 10989 103 413 -66 O ATOM 2057 CG2 THR A 178 -39.325 70.405 12.031 1.00 82.29 C ANISOU 2057 CG2 THR A 178 9737 10521 11008 97 422 -52 C ATOM 2058 N VAL A 179 -40.804 67.318 15.184 1.00 74.04 N ANISOU 2058 N VAL A 179 8730 9398 10001 180 418 -173 N ATOM 2059 CA VAL A 179 -41.079 66.688 16.474 1.00 72.10 C ANISOU 2059 CA VAL A 179 8502 9121 9770 193 416 -201 C ATOM 2060 C VAL A 179 -39.764 66.528 17.258 1.00 70.31 C ANISOU 2060 C VAL A 179 8264 8908 9541 198 421 -212 C ATOM 2061 O VAL A 179 -38.724 66.288 16.651 1.00 68.92 O ANISOU 2061 O VAL A 179 8069 8776 9338 205 427 -211 O ATOM 2062 CB VAL A 179 -41.753 65.315 16.228 1.00 74.00 C ANISOU 2062 CB VAL A 179 8763 9362 9989 209 417 -226 C ATOM 2063 CG1 VAL A 179 -42.365 64.750 17.497 1.00 74.55 C ANISOU 2063 CG1 VAL A 179 8857 9395 10072 211 413 -249 C ATOM 2064 CG2 VAL A 179 -42.841 65.427 15.159 1.00 74.02 C ANISOU 2064 CG2 VAL A 179 8764 9378 9981 200 414 -216 C ATOM 2065 N CYS A 180 -39.816 66.673 18.589 1.00 69.55 N ANISOU 2065 N CYS A 180 8175 8784 9466 197 418 -224 N ATOM 2066 CA CYS A 180 -38.647 66.486 19.494 1.00 69.23 C ANISOU 2066 CA CYS A 180 8121 8764 9420 204 421 -236 C ATOM 2067 C CYS A 180 -38.730 65.122 20.199 1.00 67.76 C ANISOU 2067 C CYS A 180 7957 8567 9221 238 420 -260 C ATOM 2068 O CYS A 180 -39.178 65.023 21.344 1.00 66.66 O ANISOU 2068 O CYS A 180 7831 8398 9097 236 415 -270 O ATOM 2069 CB CYS A 180 -38.567 67.632 20.522 1.00 70.38 C ANISOU 2069 CB CYS A 180 8258 8889 9594 175 419 -232 C ATOM 2070 SG CYS A 180 -37.393 67.461 21.914 1.00 73.06 S ANISOU 2070 SG CYS A 180 8577 9256 9925 179 422 -251 S ATOM 2071 N ALA A 181 -38.279 64.080 19.507 1.00 66.71 N ANISOU 2071 N ALA A 181 7832 8456 9058 269 423 -269 N ATOM 2072 CA ALA A 181 -38.490 62.700 19.936 1.00 67.79 C ANISOU 2072 CA ALA A 181 8008 8569 9179 302 422 -289 C ATOM 2073 C ALA A 181 -37.192 61.977 20.278 1.00 69.11 C ANISOU 2073 C ALA A 181 8169 8768 9319 349 425 -300 C ATOM 2074 O ALA A 181 -36.103 62.361 19.833 1.00 71.90 O ANISOU 2074 O ALA A 181 8482 9179 9655 358 429 -296 O ATOM 2075 CB ALA A 181 -39.233 61.936 18.851 1.00 68.43 C ANISOU 2075 CB ALA A 181 8117 8637 9244 305 425 -297 C ATOM 2076 N PHE A 182 -37.341 60.911 21.060 1.00 68.51 N ANISOU 2076 N PHE A 182 8135 8659 9234 379 421 -313 N ATOM 2077 CA PHE A 182 -36.240 60.028 21.438 1.00 68.80 C ANISOU 2077 CA PHE A 182 8179 8718 9241 439 421 -322 C ATOM 2078 C PHE A 182 -35.921 59.100 20.270 1.00 71.37 C ANISOU 2078 C PHE A 182 8526 9053 9535 481 427 -337 C ATOM 2079 O PHE A 182 -36.836 58.610 19.603 1.00 72.70 O ANISOU 2079 O PHE A 182 8734 9182 9705 465 429 -345 O ATOM 2080 CB PHE A 182 -36.652 59.197 22.660 1.00 67.50 C ANISOU 2080 CB PHE A 182 8065 8503 9078 455 415 -326 C ATOM 2081 CG PHE A 182 -35.501 58.574 23.396 1.00 67.49 C ANISOU 2081 CG PHE A 182 8063 8530 9050 517 412 -328 C ATOM 2082 CD1 PHE A 182 -35.036 57.310 23.055 1.00 67.93 C ANISOU 2082 CD1 PHE A 182 8164 8573 9072 585 412 -340 C ATOM 2083 CD2 PHE A 182 -34.891 59.243 24.445 1.00 67.69 C ANISOU 2083 CD2 PHE A 182 8044 8595 9078 512 408 -321 C ATOM 2084 CE1 PHE A 182 -33.978 56.731 23.735 1.00 66.96 C ANISOU 2084 CE1 PHE A 182 8040 8479 8919 655 407 -340 C ATOM 2085 CE2 PHE A 182 -33.837 58.668 25.137 1.00 68.39 C ANISOU 2085 CE2 PHE A 182 8126 8721 9135 574 403 -321 C ATOM 2086 CZ PHE A 182 -33.376 57.411 24.776 1.00 68.10 C ANISOU 2086 CZ PHE A 182 8133 8674 9065 650 402 -329 C ATOM 2087 N HIS A 183 -34.638 58.868 20.004 1.00 73.73 N ANISOU 2087 N HIS A 183 8795 9413 9804 532 429 -344 N ATOM 2088 CA HIS A 183 -34.242 57.833 19.047 1.00 75.98 C ANISOU 2088 CA HIS A 183 9106 9708 10055 588 434 -365 C ATOM 2089 C HIS A 183 -33.838 56.566 19.790 1.00 79.62 C ANISOU 2089 C HIS A 183 9622 10136 10493 662 430 -378 C ATOM 2090 O HIS A 183 -32.935 56.595 20.627 1.00 77.97 O ANISOU 2090 O HIS A 183 9387 9967 10271 702 425 -373 O ATOM 2091 CB HIS A 183 -33.097 58.292 18.149 1.00 75.21 C ANISOU 2091 CB HIS A 183 8941 9706 9928 606 440 -368 C ATOM 2092 CG HIS A 183 -32.834 57.354 17.014 1.00 74.20 C ANISOU 2092 CG HIS A 183 8835 9591 9766 655 446 -393 C ATOM 2093 ND1 HIS A 183 -31.721 56.545 16.958 1.00 75.51 N ANISOU 2093 ND1 HIS A 183 8997 9803 9890 741 447 -415 N ATOM 2094 CD2 HIS A 183 -33.566 57.064 15.911 1.00 73.70 C ANISOU 2094 CD2 HIS A 183 8798 9502 9701 635 452 -404 C ATOM 2095 CE1 HIS A 183 -31.765 55.814 15.858 1.00 75.82 C ANISOU 2095 CE1 HIS A 183 9061 9840 9905 772 454 -440 C ATOM 2096 NE2 HIS A 183 -32.876 56.108 15.207 1.00 74.93 N ANISOU 2096 NE2 HIS A 183 8967 9685 9816 704 457 -434 N ATOM 2097 N TYR A 184 -34.502 55.458 19.462 1.00 85.57 N ANISOU 2097 N TYR A 184 10453 10818 11238 679 431 -394 N ATOM 2098 CA TYR A 184 -34.286 54.175 20.134 1.00 88.93 C ANISOU 2098 CA TYR A 184 10955 11191 11644 746 427 -403 C ATOM 2099 C TYR A 184 -33.291 53.302 19.377 1.00 93.46 C ANISOU 2099 C TYR A 184 11542 11793 12175 837 431 -428 C ATOM 2100 O TYR A 184 -32.328 52.800 19.971 1.00 96.71 O ANISOU 2100 O TYR A 184 11957 12227 12560 919 425 -429 O ATOM 2101 CB TYR A 184 -35.619 53.439 20.303 1.00 89.03 C ANISOU 2101 CB TYR A 184 11057 11101 11668 703 428 -407 C ATOM 2102 CG TYR A 184 -36.569 54.126 21.267 1.00 89.29 C ANISOU 2102 CG TYR A 184 11081 11108 11734 628 422 -385 C ATOM 2103 CD1 TYR A 184 -37.458 55.115 20.829 1.00 88.70 C ANISOU 2103 CD1 TYR A 184 10965 11048 11688 550 425 -379 C ATOM 2104 CD2 TYR A 184 -36.577 53.790 22.623 1.00 89.43 C ANISOU 2104 CD2 TYR A 184 11132 11093 11753 639 414 -370 C ATOM 2105 CE1 TYR A 184 -38.326 55.746 21.714 1.00 87.73 C ANISOU 2105 CE1 TYR A 184 10832 10908 11593 490 420 -364 C ATOM 2106 CE2 TYR A 184 -37.443 54.412 23.514 1.00 88.29 C ANISOU 2106 CE2 TYR A 184 10975 10933 11636 572 410 -355 C ATOM 2107 CZ TYR A 184 -38.314 55.387 23.061 1.00 87.63 C ANISOU 2107 CZ TYR A 184 10849 10865 11580 500 413 -354 C ATOM 2108 OH TYR A 184 -39.166 55.996 23.956 1.00 86.86 O ANISOU 2108 OH TYR A 184 10738 10756 11506 442 409 -343 O ATOM 2109 N GLU A 185 -33.528 53.133 18.073 1.00 95.14 N ANISOU 2109 N GLU A 185 11759 12011 12378 826 440 -450 N ATOM 2110 CA GLU A 185 -32.723 52.255 17.199 1.00 97.28 C ANISOU 2110 CA GLU A 185 12048 12306 12607 910 445 -482 C ATOM 2111 C GLU A 185 -32.965 50.777 17.509 1.00 98.01 C ANISOU 2111 C GLU A 185 12258 12296 12682 969 444 -501 C ATOM 2112 O GLU A 185 -33.513 50.042 16.681 1.00 97.98 O ANISOU 2112 O GLU A 185 12318 12238 12668 962 452 -529 O ATOM 2113 CB GLU A 185 -31.223 52.576 17.282 1.00 95.80 C ANISOU 2113 CB GLU A 185 11781 12230 12389 983 443 -484 C ATOM 2114 N SER A 189 -30.567 43.167 19.134 1.00126.31 N ANISOU 2114 N SER A 189 16459 15447 16084 1576 422 -588 N ATOM 2115 CA SER A 189 -30.160 43.463 20.503 1.00126.73 C ANISOU 2115 CA SER A 189 16483 15527 16140 1605 406 -540 C ATOM 2116 C SER A 189 -31.359 43.776 21.397 1.00126.58 C ANISOU 2116 C SER A 189 16498 15436 16160 1475 404 -501 C ATOM 2117 O SER A 189 -31.556 43.125 22.428 1.00125.69 O ANISOU 2117 O SER A 189 16478 15237 16041 1495 394 -471 O ATOM 2118 CB SER A 189 -29.183 44.639 20.519 1.00126.12 C ANISOU 2118 CB SER A 189 16238 15623 16059 1624 402 -531 C ATOM 2119 OG SER A 189 -28.004 44.326 19.800 1.00127.07 O ANISOU 2119 OG SER A 189 16319 15826 16133 1750 403 -566 O ATOM 2120 N THR A 190 -32.142 44.779 20.988 1.00126.50 N ANISOU 2120 N THR A 190 16411 15466 16185 1347 412 -500 N ATOM 2121 CA THR A 190 -33.293 45.313 21.754 1.00126.61 C ANISOU 2121 CA THR A 190 16426 15441 16236 1219 411 -468 C ATOM 2122 C THR A 190 -32.992 45.571 23.244 1.00125.37 C ANISOU 2122 C THR A 190 16250 15301 16082 1237 396 -423 C ATOM 2123 O THR A 190 -33.842 45.348 24.111 1.00123.55 O ANISOU 2123 O THR A 190 16083 14995 15863 1172 392 -397 O ATOM 2124 CB THR A 190 -34.561 44.432 21.611 1.00127.04 C ANISOU 2124 CB THR A 190 16614 15360 16294 1142 419 -478 C ATOM 2125 OG1 THR A 190 -34.399 43.212 22.346 1.00128.73 O ANISOU 2125 OG1 THR A 190 16962 15466 16481 1210 412 -466 O ATOM 2126 CG2 THR A 190 -34.847 44.122 20.143 1.00127.07 C ANISOU 2126 CG2 THR A 190 16639 15351 16290 1124 434 -526 C ATOM 2127 N LEU A 191 -31.778 46.051 23.514 1.00125.45 N ANISOU 2127 N LEU A 191 16168 15421 16077 1320 388 -415 N ATOM 2128 CA LEU A 191 -31.358 46.444 24.858 1.00124.53 C ANISOU 2128 CA LEU A 191 16008 15348 15958 1338 374 -377 C ATOM 2129 C LEU A 191 -31.912 47.806 25.317 1.00122.50 C ANISOU 2129 C LEU A 191 15651 15152 15741 1219 375 -358 C ATOM 2130 O LEU A 191 -31.848 48.093 26.513 1.00120.15 O ANISOU 2130 O LEU A 191 15333 14872 15446 1209 365 -328 O ATOM 2131 CB LEU A 191 -29.826 46.427 24.968 1.00124.46 C ANISOU 2131 CB LEU A 191 15933 15446 15908 1471 365 -380 C ATOM 2132 CG LEU A 191 -29.172 45.050 24.773 1.00125.03 C ANISOU 2132 CG LEU A 191 16108 15461 15934 1615 360 -394 C ATOM 2133 CD1 LEU A 191 -27.710 45.184 24.369 1.00124.87 C ANISOU 2133 CD1 LEU A 191 15996 15576 15872 1739 357 -414 C ATOM 2134 CD2 LEU A 191 -29.308 44.194 26.025 1.00124.36 C ANISOU 2134 CD2 LEU A 191 16131 15285 15834 1660 346 -355 C ATOM 2135 N PRO A 192 -32.436 48.654 24.387 1.00122.95 N ANISOU 2135 N PRO A 192 15645 15241 15826 1132 386 -376 N ATOM 2136 CA PRO A 192 -33.195 49.846 24.824 1.00122.02 C ANISOU 2136 CA PRO A 192 15460 15153 15750 1017 387 -359 C ATOM 2137 C PRO A 192 -34.422 49.596 25.716 1.00121.51 C ANISOU 2137 C PRO A 192 15465 14998 15703 939 384 -339 C ATOM 2138 O PRO A 192 -34.844 50.510 26.424 1.00121.44 O ANISOU 2138 O PRO A 192 15399 15021 15720 870 382 -323 O ATOM 2139 CB PRO A 192 -33.625 50.481 23.500 1.00121.78 C ANISOU 2139 CB PRO A 192 15383 15148 15738 956 400 -383 C ATOM 2140 CG PRO A 192 -32.498 50.169 22.586 1.00122.30 C ANISOU 2140 CG PRO A 192 15423 15272 15771 1048 403 -407 C ATOM 2141 CD PRO A 192 -32.064 48.777 22.959 1.00123.03 C ANISOU 2141 CD PRO A 192 15618 15299 15829 1152 397 -411 C ATOM 2142 N ILE A 193 -34.992 48.390 25.658 1.00121.21 N ANISOU 2142 N ILE A 193 15550 14853 15650 945 386 -343 N ATOM 2143 CA ILE A 193 -36.004 47.937 26.623 1.00118.21 C ANISOU 2143 CA ILE A 193 15249 14391 15274 881 382 -322 C ATOM 2144 C ILE A 193 -35.316 47.241 27.805 1.00117.91 C ANISOU 2144 C ILE A 193 15263 14330 15207 962 369 -292 C ATOM 2145 O ILE A 193 -35.732 47.422 28.951 1.00116.72 O ANISOU 2145 O ILE A 193 15113 14173 15060 917 361 -264 O ATOM 2146 CB ILE A 193 -37.049 46.999 25.967 1.00117.55 C ANISOU 2146 CB ILE A 193 15279 14201 15183 827 392 -341 C ATOM 2147 CG1 ILE A 193 -37.897 47.770 24.934 1.00116.82 C ANISOU 2147 CG1 ILE A 193 15127 14141 15117 735 404 -365 C ATOM 2148 CG2 ILE A 193 -37.957 46.361 27.021 1.00117.33 C ANISOU 2148 CG2 ILE A 193 15343 14088 15146 766 388 -316 C ATOM 2149 CD1 ILE A 193 -37.227 48.017 23.597 1.00115.56 C ANISOU 2149 CD1 ILE A 193 14916 14035 14956 783 411 -394 C ATOM 2150 N GLY A 194 -34.278 46.448 27.520 1.00117.48 N ANISOU 2150 N GLY A 194 15249 14268 15119 1084 365 -298 N ATOM 2151 CA GLY A 194 -33.476 45.774 28.549 1.00116.92 C ANISOU 2151 CA GLY A 194 15223 14187 15014 1184 350 -268 C ATOM 2152 C GLY A 194 -32.837 46.702 29.570 1.00115.51 C ANISOU 2152 C GLY A 194 14933 14119 14837 1195 339 -244 C ATOM 2153 O GLY A 194 -32.804 46.385 30.760 1.00114.45 O ANISOU 2153 O GLY A 194 14833 13966 14686 1211 328 -209 O ATOM 2154 N LEU A 195 -32.323 47.837 29.097 1.00115.30 N ANISOU 2154 N LEU A 195 14775 14206 14827 1182 344 -261 N ATOM 2155 CA LEU A 195 -31.778 48.901 29.958 1.00115.75 C ANISOU 2155 CA LEU A 195 14716 14375 14888 1169 337 -246 C ATOM 2156 C LEU A 195 -32.693 50.142 30.042 1.00114.70 C ANISOU 2156 C LEU A 195 14512 14265 14801 1035 345 -250 C ATOM 2157 O LEU A 195 -32.387 51.091 30.764 1.00112.78 O ANISOU 2157 O LEU A 195 14181 14104 14566 1007 341 -241 O ATOM 2158 CB LEU A 195 -30.354 49.275 29.508 1.00115.46 C ANISOU 2158 CB LEU A 195 14583 14461 14823 1259 336 -262 C ATOM 2159 CG LEU A 195 -29.212 48.416 30.085 1.00115.70 C ANISOU 2159 CG LEU A 195 14638 14522 14799 1401 322 -247 C ATOM 2160 CD1 LEU A 195 -28.921 48.783 31.535 1.00115.07 C ANISOU 2160 CD1 LEU A 195 14513 14500 14706 1399 310 -214 C ATOM 2161 CD2 LEU A 195 -29.478 46.920 29.965 1.00114.66 C ANISOU 2161 CD2 LEU A 195 14659 14259 14646 1474 318 -241 C ATOM 2162 N GLY A 196 -33.806 50.131 29.308 1.00115.29 N ANISOU 2162 N GLY A 196 14627 14272 14904 955 355 -264 N ATOM 2163 CA GLY A 196 -34.927 51.037 29.569 1.00115.92 C ANISOU 2163 CA GLY A 196 14671 14349 15022 836 360 -263 C ATOM 2164 C GLY A 196 -35.795 50.616 30.747 1.00115.72 C ANISOU 2164 C GLY A 196 14709 14263 14995 786 354 -240 C ATOM 2165 O GLY A 196 -36.695 51.358 31.136 1.00116.58 O ANISOU 2165 O GLY A 196 14783 14380 15130 695 356 -240 O ATOM 2166 N LEU A 197 -35.554 49.420 31.292 1.00116.52 N ANISOU 2166 N LEU A 197 14906 14303 15062 847 346 -220 N ATOM 2167 CA LEU A 197 -36.216 48.956 32.517 1.00117.54 C ANISOU 2167 CA LEU A 197 15097 14382 15179 807 338 -191 C ATOM 2168 C LEU A 197 -35.337 49.164 33.764 1.00116.97 C ANISOU 2168 C LEU A 197 14979 14378 15085 862 325 -163 C ATOM 2169 O LEU A 197 -35.858 49.130 34.880 1.00117.66 O ANISOU 2169 O LEU A 197 15083 14454 15166 815 319 -140 O ATOM 2170 CB LEU A 197 -36.627 47.475 32.380 1.00118.93 C ANISOU 2170 CB LEU A 197 15424 14436 15326 826 338 -181 C ATOM 2171 CG LEU A 197 -38.048 47.055 32.792 1.00118.73 C ANISOU 2171 CG LEU A 197 15478 14332 15301 714 342 -172 C ATOM 2172 CD1 LEU A 197 -38.289 47.246 34.282 1.00118.94 C ANISOU 2172 CD1 LEU A 197 15492 14382 15317 678 332 -138 C ATOM 2173 CD2 LEU A 197 -39.111 47.783 31.975 1.00117.55 C ANISOU 2173 CD2 LEU A 197 15280 14197 15185 609 356 -204 C ATOM 2174 N THR A 198 -34.027 49.388 33.588 1.00116.06 N ANISOU 2174 N THR A 198 14800 14341 14954 956 320 -167 N ATOM 2175 CA THR A 198 -33.133 49.683 34.728 1.00116.40 C ANISOU 2175 CA THR A 198 14783 14471 14973 1006 308 -145 C ATOM 2176 C THR A 198 -33.402 51.058 35.387 1.00115.39 C ANISOU 2176 C THR A 198 14544 14424 14872 916 310 -152 C ATOM 2177 O THR A 198 -32.970 51.308 36.518 1.00116.31 O ANISOU 2177 O THR A 198 14619 14602 14969 928 301 -134 O ATOM 2178 CB THR A 198 -31.629 49.542 34.376 1.00117.44 C ANISOU 2178 CB THR A 198 14868 14683 15069 1131 303 -150 C ATOM 2179 OG1 THR A 198 -30.884 49.272 35.571 1.00116.75 O ANISOU 2179 OG1 THR A 198 14770 14648 14942 1199 287 -120 O ATOM 2180 CG2 THR A 198 -31.068 50.806 33.714 1.00117.82 C ANISOU 2180 CG2 THR A 198 14785 14841 15137 1106 312 -181 C ATOM 2181 N LYS A 199 -34.073 51.949 34.656 1.00112.04 N ANISOU 2181 N LYS A 199 14075 14004 14492 833 323 -179 N ATOM 2182 CA LYS A 199 -34.595 53.204 35.223 1.00109.80 C ANISOU 2182 CA LYS A 199 13709 13769 14238 740 326 -188 C ATOM 2183 C LYS A 199 -35.769 52.998 36.188 1.00107.38 C ANISOU 2183 C LYS A 199 13450 13412 13936 667 324 -174 C ATOM 2184 O LYS A 199 -35.887 53.725 37.175 1.00109.76 O ANISOU 2184 O LYS A 199 13694 13765 14242 625 321 -172 O ATOM 2185 CB LYS A 199 -34.983 54.222 34.131 1.00110.34 C ANISOU 2185 CB LYS A 199 13722 13851 14349 681 339 -218 C ATOM 2186 CG LYS A 199 -35.744 53.709 32.915 1.00110.43 C ANISOU 2186 CG LYS A 199 13797 13784 14374 663 347 -230 C ATOM 2187 CD LYS A 199 -36.233 54.862 32.039 1.00110.71 C ANISOU 2187 CD LYS A 199 13771 13843 14451 598 358 -253 C ATOM 2188 CE LYS A 199 -35.894 54.669 30.564 1.00111.24 C ANISOU 2188 CE LYS A 199 13843 13904 14518 630 365 -269 C ATOM 2189 NZ LYS A 199 -34.461 54.969 30.274 1.00110.81 N ANISOU 2189 NZ LYS A 199 13725 13931 14445 698 365 -272 N ATOM 2190 N ASN A 200 -36.634 52.026 35.893 1.00103.79 N ANISOU 2190 N ASN A 200 13097 12860 13476 647 325 -166 N ATOM 2191 CA ASN A 200 -37.751 51.664 36.782 1.00100.62 C ANISOU 2191 CA ASN A 200 12750 12413 13067 574 323 -150 C ATOM 2192 C ASN A 200 -37.291 50.966 38.076 1.00 97.92 C ANISOU 2192 C ASN A 200 12447 12074 12683 617 309 -112 C ATOM 2193 O ASN A 200 -37.792 51.295 39.151 1.00 94.35 O ANISOU 2193 O ASN A 200 11971 11649 12226 560 306 -103 O ATOM 2194 CB ASN A 200 -38.788 50.810 36.028 1.00101.98 C ANISOU 2194 CB ASN A 200 13021 12486 13239 530 330 -155 C ATOM 2195 CG ASN A 200 -39.766 50.103 36.955 1.00104.45 C ANISOU 2195 CG ASN A 200 13411 12746 13527 465 327 -132 C ATOM 2196 OD1 ASN A 200 -39.654 48.898 37.184 1.00104.75 O ANISOU 2196 OD1 ASN A 200 13557 12712 13530 498 322 -106 O ATOM 2197 ND2 ASN A 200 -40.718 50.852 37.504 1.00106.56 N ANISOU 2197 ND2 ASN A 200 13626 13050 13809 374 330 -143 N ATOM 2198 N ILE A 201 -36.367 50.004 37.976 1.00 95.61 N ANISOU 2198 N ILE A 201 12214 11755 12356 720 301 -91 N ATOM 2199 CA ILE A 201 -35.786 49.341 39.180 1.00 93.99 C ANISOU 2199 CA ILE A 201 12045 11560 12106 779 286 -50 C ATOM 2200 C ILE A 201 -35.059 50.324 40.099 1.00 97.09 C ANISOU 2200 C ILE A 201 12318 12076 12493 789 280 -50 C ATOM 2201 O ILE A 201 -35.304 50.331 41.310 1.00 99.69 O ANISOU 2201 O ILE A 201 12645 12429 12803 758 272 -27 O ATOM 2202 CB ILE A 201 -34.840 48.139 38.854 1.00 90.90 C ANISOU 2202 CB ILE A 201 11741 11122 11676 909 277 -27 C ATOM 2203 CG1 ILE A 201 -34.243 47.516 40.133 1.00 89.96 C ANISOU 2203 CG1 ILE A 201 11654 11019 11505 976 260 19 C ATOM 2204 CG2 ILE A 201 -33.689 48.541 37.953 1.00 90.75 C ANISOU 2204 CG2 ILE A 201 11647 11172 11660 995 280 -54 C ATOM 2205 CD1 ILE A 201 -33.267 46.379 39.877 1.00 89.62 C ANISOU 2205 CD1 ILE A 201 11695 10935 11420 1119 249 42 C ATOM 2206 N LEU A 202 -34.174 51.144 39.532 1.00 98.33 N ANISOU 2206 N LEU A 202 12380 12316 12665 826 284 -76 N ATOM 2207 CA LEU A 202 -33.352 52.063 40.325 1.00 99.92 C ANISOU 2207 CA LEU A 202 12468 12640 12855 835 279 -81 C ATOM 2208 C LEU A 202 -34.170 53.264 40.790 1.00101.75 C ANISOU 2208 C LEU A 202 12629 12907 13124 720 288 -105 C ATOM 2209 O LEU A 202 -33.903 53.817 41.853 1.00102.46 O ANISOU 2209 O LEU A 202 12656 13074 13200 702 283 -103 O ATOM 2210 CB LEU A 202 -32.135 52.536 39.527 1.00100.67 C ANISOU 2210 CB LEU A 202 12485 12816 12947 902 282 -103 C ATOM 2211 N GLY A 203 -35.151 53.668 39.983 1.00103.81 N ANISOU 2211 N GLY A 203 12899 13113 13428 648 300 -130 N ATOM 2212 CA GLY A 203 -36.084 54.725 40.354 1.00104.27 C ANISOU 2212 CA GLY A 203 12905 13191 13522 547 307 -154 C ATOM 2213 C GLY A 203 -37.059 54.252 41.413 1.00106.25 C ANISOU 2213 C GLY A 203 13205 13410 13756 493 302 -134 C ATOM 2214 O GLY A 203 -37.132 54.832 42.492 1.00107.10 O ANISOU 2214 O GLY A 203 13259 13578 13856 457 299 -138 O ATOM 2215 N PHE A 204 -37.802 53.192 41.102 1.00108.67 N ANISOU 2215 N PHE A 204 13613 13624 14050 482 302 -116 N ATOM 2216 CA PHE A 204 -38.803 52.645 42.020 1.00111.74 C ANISOU 2216 CA PHE A 204 14059 13979 14418 420 298 -96 C ATOM 2217 C PHE A 204 -38.171 51.742 43.084 1.00115.32 C ANISOU 2217 C PHE A 204 14561 14437 14819 476 284 -50 C ATOM 2218 O PHE A 204 -37.958 52.183 44.214 1.00116.37 O ANISOU 2218 O PHE A 204 14637 14643 14934 464 277 -43 O ATOM 2219 CB PHE A 204 -39.902 51.889 41.258 1.00112.83 C ANISOU 2219 CB PHE A 204 14289 14020 14560 370 305 -97 C ATOM 2220 N LEU A 205 -37.834 50.507 42.706 1.00116.76 N ANISOU 2220 N LEU A 205 14847 14541 14973 541 278 -19 N ATOM 2221 CA LEU A 205 -37.533 49.428 43.670 1.00116.70 C ANISOU 2221 CA LEU A 205 14922 14506 14911 586 264 32 C ATOM 2222 C LEU A 205 -36.470 49.758 44.724 1.00117.41 C ANISOU 2222 C LEU A 205 14939 14698 14970 649 251 51 C ATOM 2223 O LEU A 205 -36.632 49.390 45.889 1.00117.23 O ANISOU 2223 O LEU A 205 14942 14690 14910 633 241 87 O ATOM 2224 CB LEU A 205 -37.149 48.123 42.946 1.00117.63 C ANISOU 2224 CB LEU A 205 15165 14521 15007 669 260 57 C ATOM 2225 CG LEU A 205 -38.279 47.173 42.529 1.00117.57 C ANISOU 2225 CG LEU A 205 15287 14388 14994 602 267 65 C ATOM 2226 CD1 LEU A 205 -38.833 46.427 43.735 1.00118.49 C ANISOU 2226 CD1 LEU A 205 15485 14470 15065 556 258 113 C ATOM 2227 CD2 LEU A 205 -39.394 47.892 41.780 1.00117.10 C ANISOU 2227 CD2 LEU A 205 15184 14327 14978 494 283 19 C ATOM 2228 N PHE A 206 -35.402 50.449 44.325 1.00118.54 N ANISOU 2228 N PHE A 206 14992 14921 15126 712 251 28 N ATOM 2229 CA PHE A 206 -34.306 50.761 45.252 1.00119.75 C ANISOU 2229 CA PHE A 206 15068 15185 15243 773 240 42 C ATOM 2230 C PHE A 206 -34.727 51.785 46.323 1.00118.78 C ANISOU 2230 C PHE A 206 14855 15149 15127 684 242 25 C ATOM 2231 O PHE A 206 -34.549 51.522 47.510 1.00117.30 O ANISOU 2231 O PHE A 206 14666 15006 14896 692 230 57 O ATOM 2232 CB PHE A 206 -33.044 51.201 44.498 1.00120.23 C ANISOU 2232 CB PHE A 206 15055 15318 15308 858 241 19 C ATOM 2233 N PRO A 207 -35.280 52.948 45.914 1.00118.51 N ANISOU 2233 N PRO A 207 14747 15137 15143 601 257 -23 N ATOM 2234 CA PRO A 207 -35.909 53.864 46.875 1.00118.02 C ANISOU 2234 CA PRO A 207 14616 15136 15090 510 260 -45 C ATOM 2235 C PRO A 207 -37.185 53.356 47.561 1.00117.77 C ANISOU 2235 C PRO A 207 14648 15053 15046 434 259 -27 C ATOM 2236 O PRO A 207 -37.269 53.434 48.780 1.00119.54 O ANISOU 2236 O PRO A 207 14846 15335 15238 407 253 -13 O ATOM 2237 CB PRO A 207 -36.222 55.097 46.023 1.00117.11 C ANISOU 2237 CB PRO A 207 14430 15030 15033 457 276 -100 C ATOM 2238 CG PRO A 207 -35.139 55.101 45.013 1.00117.05 C ANISOU 2238 CG PRO A 207 14407 15034 15033 535 277 -106 C ATOM 2239 CD PRO A 207 -34.953 53.653 44.662 1.00117.96 C ANISOU 2239 CD PRO A 207 14629 15071 15117 610 268 -63 C ATOM 2240 N PHE A 208 -38.152 52.843 46.798 1.00118.22 N ANISOU 2240 N PHE A 208 14783 15012 15122 395 266 -27 N ATOM 2241 CA PHE A 208 -39.473 52.454 47.344 1.00118.76 C ANISOU 2241 CA PHE A 208 14904 15042 15176 304 268 -17 C ATOM 2242 C PHE A 208 -39.363 51.512 48.542 1.00118.77 C ANISOU 2242 C PHE A 208 14965 15045 15116 315 254 37 C ATOM 2243 O PHE A 208 -40.017 51.734 49.565 1.00120.55 O ANISOU 2243 O PHE A 208 15166 15316 15321 244 253 38 O ATOM 2244 CB PHE A 208 -40.361 51.790 46.278 1.00120.86 C ANISOU 2244 CB PHE A 208 15260 15201 15458 270 276 -19 C ATOM 2245 CG PHE A 208 -41.156 52.759 45.436 1.00122.16 C ANISOU 2245 CG PHE A 208 15367 15371 15675 209 290 -72 C ATOM 2246 CD1 PHE A 208 -40.563 53.893 44.880 1.00122.92 C ANISOU 2246 CD1 PHE A 208 15371 15517 15813 237 296 -109 C ATOM 2247 CD2 PHE A 208 -42.505 52.519 45.172 1.00123.73 C ANISOU 2247 CD2 PHE A 208 15608 15527 15876 122 298 -83 C ATOM 2248 CE1 PHE A 208 -41.301 54.768 44.093 1.00123.79 C ANISOU 2248 CE1 PHE A 208 15437 15626 15969 187 308 -153 C ATOM 2249 CE2 PHE A 208 -43.247 53.394 44.387 1.00124.75 C ANISOU 2249 CE2 PHE A 208 15683 15666 16048 76 310 -129 C ATOM 2250 CZ PHE A 208 -42.643 54.519 43.845 1.00123.98 C ANISOU 2250 CZ PHE A 208 15500 15611 15995 112 314 -162 C ATOM 2251 N LEU A 209 -38.543 50.468 48.406 1.00115.93 N ANISOU 2251 N LEU A 209 14685 14636 14724 407 243 82 N ATOM 2252 CA LEU A 209 -38.322 49.504 49.496 1.00115.33 C ANISOU 2252 CA LEU A 209 14679 14555 14585 435 227 144 C ATOM 2253 C LEU A 209 -37.592 50.132 50.681 1.00115.06 C ANISOU 2253 C LEU A 209 14545 14648 14523 457 218 148 C ATOM 2254 O LEU A 209 -37.952 49.881 51.830 1.00115.95 O ANISOU 2254 O LEU A 209 14669 14791 14593 415 210 178 O ATOM 2255 CB LEU A 209 -37.564 48.255 49.014 1.00114.53 C ANISOU 2255 CB LEU A 209 14692 14366 14455 545 216 190 C ATOM 2256 CG LEU A 209 -38.408 47.097 48.466 1.00114.02 C ANISOU 2256 CG LEU A 209 14780 14159 14383 511 220 214 C ATOM 2257 CD1 LEU A 209 -39.175 46.391 49.580 1.00112.60 C ANISOU 2257 CD1 LEU A 209 14678 13951 14152 439 213 262 C ATOM 2258 CD2 LEU A 209 -39.356 47.568 47.372 1.00113.62 C ANISOU 2258 CD2 LEU A 209 14715 14068 14385 428 239 161 C ATOM 2259 N ILE A 210 -36.573 50.940 50.391 1.00114.14 N ANISOU 2259 N ILE A 210 14330 14610 14425 517 219 118 N ATOM 2260 CA ILE A 210 -35.837 51.683 51.422 1.00113.71 C ANISOU 2260 CA ILE A 210 14167 14690 14347 529 212 111 C ATOM 2261 C ILE A 210 -36.755 52.698 52.120 1.00111.40 C ANISOU 2261 C ILE A 210 13796 14455 14072 412 222 69 C ATOM 2262 O ILE A 210 -36.723 52.820 53.341 1.00113.33 O ANISOU 2262 O ILE A 210 14004 14779 14278 389 215 82 O ATOM 2263 CB ILE A 210 -34.582 52.389 50.830 1.00115.04 C ANISOU 2263 CB ILE A 210 14245 14932 14531 603 214 79 C ATOM 2264 CG1 ILE A 210 -33.533 51.353 50.379 1.00115.75 C ANISOU 2264 CG1 ILE A 210 14398 14994 14587 736 201 122 C ATOM 2265 CG2 ILE A 210 -33.958 53.374 51.822 1.00115.37 C ANISOU 2265 CG2 ILE A 210 14161 15119 14553 588 213 56 C ATOM 2266 CD1 ILE A 210 -32.735 50.706 51.494 1.00117.60 C ANISOU 2266 CD1 ILE A 210 14640 15293 14748 813 181 176 C ATOM 2267 N ILE A 211 -37.573 53.399 51.339 1.00108.75 N ANISOU 2267 N ILE A 211 13440 14085 13794 345 238 20 N ATOM 2268 CA ILE A 211 -38.468 54.447 51.849 1.00106.27 C ANISOU 2268 CA ILE A 211 13051 13822 13502 245 249 -28 C ATOM 2269 C ILE A 211 -39.669 53.872 52.617 1.00105.87 C ANISOU 2269 C ILE A 211 13054 13748 13420 166 247 -6 C ATOM 2270 O ILE A 211 -40.091 54.452 53.617 1.00104.73 O ANISOU 2270 O ILE A 211 12848 13682 13261 106 249 -26 O ATOM 2271 CB ILE A 211 -38.922 55.392 50.705 1.00103.99 C ANISOU 2271 CB ILE A 211 12724 13503 13281 212 265 -85 C ATOM 2272 CG1 ILE A 211 -37.728 56.220 50.216 1.00103.60 C ANISOU 2272 CG1 ILE A 211 12600 13507 13256 267 268 -113 C ATOM 2273 CG2 ILE A 211 -40.028 56.334 51.165 1.00104.68 C ANISOU 2273 CG2 ILE A 211 12755 13627 13390 116 275 -133 C ATOM 2274 CD1 ILE A 211 -37.941 56.914 48.890 1.00103.01 C ANISOU 2274 CD1 ILE A 211 12509 13386 13241 256 281 -153 C ATOM 2275 N LEU A 212 -40.218 52.751 52.149 1.00107.14 N ANISOU 2275 N LEU A 212 13331 13808 13569 161 245 32 N ATOM 2276 CA LEU A 212 -41.292 52.055 52.871 1.00107.35 C ANISOU 2276 CA LEU A 212 13420 13812 13554 81 243 60 C ATOM 2277 C LEU A 212 -40.764 51.547 54.211 1.00108.07 C ANISOU 2277 C LEU A 212 13520 13960 13580 103 228 112 C ATOM 2278 O LEU A 212 -41.318 51.871 55.260 1.00109.97 O ANISOU 2278 O LEU A 212 13716 14275 13793 33 228 105 O ATOM 2279 CB LEU A 212 -41.852 50.891 52.040 1.00108.00 C ANISOU 2279 CB LEU A 212 13635 13766 13631 72 245 93 C ATOM 2280 CG LEU A 212 -42.999 50.052 52.625 1.00108.65 C ANISOU 2280 CG LEU A 212 13801 13813 13667 -22 244 125 C ATOM 2281 CD1 LEU A 212 -44.241 50.896 52.875 1.00108.04 C ANISOU 2281 CD1 LEU A 212 13647 13798 13603 -134 257 72 C ATOM 2282 CD2 LEU A 212 -43.325 48.887 51.700 1.00108.82 C ANISOU 2282 CD2 LEU A 212 13961 13700 13683 -21 246 154 C ATOM 2283 N THR A 213 -39.677 50.776 54.160 1.00108.68 N ANISOU 2283 N THR A 213 13652 14010 13630 206 214 162 N ATOM 2284 CA THR A 213 -39.030 50.222 55.359 1.00109.97 C ANISOU 2284 CA THR A 213 13828 14227 13726 249 196 219 C ATOM 2285 C THR A 213 -38.480 51.307 56.308 1.00111.00 C ANISOU 2285 C THR A 213 13819 14507 13847 246 195 187 C ATOM 2286 O THR A 213 -38.334 51.067 57.510 1.00113.54 O ANISOU 2286 O THR A 213 14130 14897 14111 239 184 223 O ATOM 2287 CB THR A 213 -37.897 49.235 54.979 1.00110.93 C ANISOU 2287 CB THR A 213 14032 14294 13823 381 182 274 C ATOM 2288 OG1 THR A 213 -38.352 48.350 53.946 1.00111.10 O ANISOU 2288 OG1 THR A 213 14178 14172 13862 386 186 290 O ATOM 2289 CG2 THR A 213 -37.447 48.398 56.184 1.00111.61 C ANISOU 2289 CG2 THR A 213 14166 14409 13831 424 161 348 C ATOM 2290 N SER A 214 -38.173 52.487 55.766 1.00110.65 N ANISOU 2290 N SER A 214 13673 14512 13856 247 207 121 N ATOM 2291 CA SER A 214 -37.839 53.658 56.579 1.00109.28 C ANISOU 2291 CA SER A 214 13368 14470 13681 219 210 75 C ATOM 2292 C SER A 214 -39.044 54.122 57.404 1.00107.63 C ANISOU 2292 C SER A 214 13126 14301 13465 105 218 46 C ATOM 2293 O SER A 214 -38.971 54.156 58.632 1.00108.06 O ANISOU 2293 O SER A 214 13142 14445 13469 82 211 60 O ATOM 2294 CB SER A 214 -37.325 54.804 55.694 1.00109.25 C ANISOU 2294 CB SER A 214 13281 14489 13737 236 223 10 C ATOM 2295 OG SER A 214 -37.106 55.986 56.440 1.00109.74 O ANISOU 2295 OG SER A 214 13227 14667 13801 195 229 -41 O ATOM 2296 N TYR A 215 -40.147 54.454 56.731 1.00105.92 N ANISOU 2296 N TYR A 215 12922 14027 13295 37 232 7 N ATOM 2297 CA TYR A 215 -41.321 55.040 57.399 1.00105.67 C ANISOU 2297 CA TYR A 215 12843 14045 13261 -65 241 -32 C ATOM 2298 C TYR A 215 -42.189 54.070 58.183 1.00104.69 C ANISOU 2298 C TYR A 215 12789 13910 13077 -126 234 15 C ATOM 2299 O TYR A 215 -42.723 54.450 59.221 1.00104.71 O ANISOU 2299 O TYR A 215 12736 13999 13048 -192 236 -2 O ATOM 2300 CB TYR A 215 -42.215 55.788 56.407 1.00105.94 C ANISOU 2300 CB TYR A 215 12857 14033 13359 -110 257 -94 C ATOM 2301 CG TYR A 215 -41.558 56.980 55.767 1.00106.24 C ANISOU 2301 CG TYR A 215 12817 14092 13455 -74 266 -151 C ATOM 2302 CD1 TYR A 215 -40.887 57.936 56.533 1.00107.34 C ANISOU 2302 CD1 TYR A 215 12859 14333 13589 -70 268 -187 C ATOM 2303 CD2 TYR A 215 -41.627 57.172 54.394 1.00107.55 C ANISOU 2303 CD2 TYR A 215 13006 14178 13677 -51 274 -169 C ATOM 2304 CE1 TYR A 215 -40.290 59.034 55.944 1.00107.63 C ANISOU 2304 CE1 TYR A 215 12833 14385 13676 -49 277 -239 C ATOM 2305 CE2 TYR A 215 -41.038 58.271 53.801 1.00108.30 C ANISOU 2305 CE2 TYR A 215 13035 14290 13821 -26 283 -218 C ATOM 2306 CZ TYR A 215 -40.375 59.195 54.577 1.00108.94 C ANISOU 2306 CZ TYR A 215 13028 14466 13897 -27 284 -252 C ATOM 2307 OH TYR A 215 -39.783 60.263 53.957 1.00111.71 O ANISOU 2307 OH TYR A 215 13323 14826 14293 -11 294 -297 O ATOM 2308 N THR A 216 -42.354 52.842 57.691 1.00104.02 N ANISOU 2308 N THR A 216 12826 13720 12974 -111 228 74 N ATOM 2309 CA THR A 216 -43.167 51.829 58.387 1.00104.42 C ANISOU 2309 CA THR A 216 12960 13749 12963 -179 223 127 C ATOM 2310 C THR A 216 -42.699 51.624 59.835 1.00104.78 C ANISOU 2310 C THR A 216 12981 13890 12940 -174 209 168 C ATOM 2311 O THR A 216 -43.516 51.364 60.721 1.00106.50 O ANISOU 2311 O THR A 216 13207 14149 13108 -260 208 184 O ATOM 2312 CB THR A 216 -43.176 50.478 57.630 1.00104.46 C ANISOU 2312 CB THR A 216 13116 13616 12956 -149 217 189 C ATOM 2313 OG1 THR A 216 -43.618 50.687 56.285 1.00102.87 O ANISOU 2313 OG1 THR A 216 12932 13338 12816 -157 230 148 O ATOM 2314 CG2 THR A 216 -44.110 49.462 58.301 1.00105.99 C ANISOU 2314 CG2 THR A 216 13405 13780 13085 -238 214 242 C ATOM 2315 N LEU A 217 -41.391 51.753 60.062 1.00104.16 N ANISOU 2315 N LEU A 217 12866 13855 12854 -78 198 185 N ATOM 2316 CA LEU A 217 -40.835 51.782 61.413 1.00105.57 C ANISOU 2316 CA LEU A 217 12994 14147 12970 -67 185 213 C ATOM 2317 C LEU A 217 -41.226 53.067 62.148 1.00104.15 C ANISOU 2317 C LEU A 217 12678 14095 12799 -139 197 138 C ATOM 2318 O LEU A 217 -41.951 53.011 63.144 1.00106.25 O ANISOU 2318 O LEU A 217 12927 14424 13017 -218 196 143 O ATOM 2319 CB LEU A 217 -39.305 51.644 61.379 1.00106.26 C ANISOU 2319 CB LEU A 217 13067 14261 13045 58 172 243 C ATOM 2320 CG LEU A 217 -38.755 50.307 60.872 1.00107.22 C ANISOU 2320 CG LEU A 217 13323 14272 13144 150 157 323 C ATOM 2321 CD1 LEU A 217 -37.262 50.407 60.592 1.00107.42 C ANISOU 2321 CD1 LEU A 217 13309 14335 13168 281 147 330 C ATOM 2322 CD2 LEU A 217 -39.040 49.181 61.860 1.00107.83 C ANISOU 2322 CD2 LEU A 217 13495 14333 13140 132 141 407 C ATOM 2323 N ILE A 218 -40.763 54.214 61.648 1.00101.16 N ANISOU 2323 N ILE A 218 12206 13750 12477 -113 207 67 N ATOM 2324 CA ILE A 218 -40.892 55.489 62.379 1.00100.12 C ANISOU 2324 CA ILE A 218 11947 13740 12353 -164 217 -6 C ATOM 2325 C ILE A 218 -42.330 56.031 62.464 1.00 97.54 C ANISOU 2325 C ILE A 218 11594 13420 12045 -267 232 -62 C ATOM 2326 O ILE A 218 -42.652 56.764 63.394 1.00 96.51 O ANISOU 2326 O ILE A 218 11379 13395 11895 -320 237 -108 O ATOM 2327 CB ILE A 218 -39.891 56.571 61.862 1.00100.76 C ANISOU 2327 CB ILE A 218 11944 13855 12485 -111 224 -63 C ATOM 2328 CG1 ILE A 218 -39.875 57.831 62.760 1.00101.61 C ANISOU 2328 CG1 ILE A 218 11928 14089 12589 -161 234 -137 C ATOM 2329 CG2 ILE A 218 -40.165 56.957 60.409 1.00 99.74 C ANISOU 2329 CG2 ILE A 218 11838 13624 12434 -100 237 -101 C ATOM 2330 CD1 ILE A 218 -39.604 57.592 64.239 1.00101.63 C ANISOU 2330 CD1 ILE A 218 11891 14212 12511 -178 222 -110 C ATOM 2331 N TRP A 219 -43.187 55.673 61.510 1.00 96.75 N ANISOU 2331 N TRP A 219 11562 13219 11978 -292 239 -62 N ATOM 2332 CA TRP A 219 -44.623 55.944 61.630 1.00 95.47 C ANISOU 2332 CA TRP A 219 11385 13071 11817 -388 250 -102 C ATOM 2333 C TRP A 219 -45.176 55.162 62.817 1.00 96.15 C ANISOU 2333 C TRP A 219 11499 13213 11820 -454 242 -54 C ATOM 2334 O TRP A 219 -45.819 55.733 63.701 1.00 95.21 O ANISOU 2334 O TRP A 219 11305 13196 11674 -521 247 -97 O ATOM 2335 CB TRP A 219 -45.372 55.554 60.356 1.00 94.76 C ANISOU 2335 CB TRP A 219 11370 12867 11768 -402 257 -102 C ATOM 2336 N LYS A 220 -44.892 53.859 62.835 1.00 95.88 N ANISOU 2336 N LYS A 220 11575 13112 11743 -433 229 33 N ATOM 2337 CA LYS A 220 -45.300 52.971 63.928 1.00 95.53 C ANISOU 2337 CA LYS A 220 11577 13106 11613 -492 219 95 C ATOM 2338 C LYS A 220 -44.697 53.370 65.281 1.00 95.80 C ANISOU 2338 C LYS A 220 11526 13276 11596 -485 210 96 C ATOM 2339 O LYS A 220 -45.361 53.240 66.309 1.00 97.93 O ANISOU 2339 O LYS A 220 11774 13627 11805 -565 209 104 O ATOM 2340 CB LYS A 220 -44.929 51.519 63.607 1.00 94.08 C ANISOU 2340 CB LYS A 220 11541 12807 11398 -452 205 193 C ATOM 2341 N ALA A 221 -43.454 53.855 65.272 1.00 94.89 N ANISOU 2341 N ALA A 221 11358 13194 11503 -396 205 86 N ATOM 2342 CA ALA A 221 -42.752 54.251 66.503 1.00 94.97 C ANISOU 2342 CA ALA A 221 11281 13338 11462 -384 197 85 C ATOM 2343 C ALA A 221 -43.261 55.583 67.066 1.00 94.03 C ANISOU 2343 C ALA A 221 11033 13335 11358 -449 212 -12 C ATOM 2344 O ALA A 221 -43.654 55.654 68.229 1.00 93.29 O ANISOU 2344 O ALA A 221 10892 13347 11204 -510 211 -16 O ATOM 2345 CB ALA A 221 -41.249 54.320 66.258 1.00 94.54 C ANISOU 2345 CB ALA A 221 11211 13290 11419 -271 187 104 C ATOM 2346 N LEU A 222 -43.251 56.624 66.233 1.00 93.07 N ANISOU 2346 N LEU A 222 10857 13188 11314 -434 227 -92 N ATOM 2347 CA LEU A 222 -43.681 57.971 66.629 1.00 92.27 C ANISOU 2347 CA LEU A 222 10643 13176 11237 -482 243 -192 C ATOM 2348 C LEU A 222 -45.190 58.044 66.873 1.00 92.14 C ANISOU 2348 C LEU A 222 10620 13180 11208 -575 252 -226 C ATOM 2349 O LEU A 222 -45.966 57.262 66.319 1.00 92.41 O ANISOU 2349 O LEU A 222 10735 13134 11240 -604 252 -188 O ATOM 2350 CB LEU A 222 -43.277 58.991 65.552 1.00 92.73 C ANISOU 2350 CB LEU A 222 10667 13181 11383 -438 255 -259 C ATOM 2351 CG LEU A 222 -43.526 60.486 65.790 1.00 93.10 C ANISOU 2351 CG LEU A 222 10609 13296 11466 -469 272 -366 C ATOM 2352 CD1 LEU A 222 -42.802 60.986 67.029 1.00 94.45 C ANISOU 2352 CD1 LEU A 222 10695 13602 11589 -477 269 -390 C ATOM 2353 CD2 LEU A 222 -43.100 61.282 64.569 1.00 92.08 C ANISOU 2353 CD2 LEU A 222 10477 13088 11421 -423 282 -411 C ATOM 2354 N ASN A 235 -39.293 66.700 64.669 1.00102.34 N ANISOU 2354 N ASN A 235 11471 14569 12844 -400 331 -716 N ATOM 2355 CA ASN A 235 -39.772 65.324 64.789 1.00102.02 C ANISOU 2355 CA ASN A 235 11485 14510 12764 -381 314 -631 C ATOM 2356 C ASN A 235 -41.104 65.102 64.071 1.00100.55 C ANISOU 2356 C ASN A 235 11357 14225 12620 -393 318 -630 C ATOM 2357 O ASN A 235 -41.129 64.517 62.991 1.00 98.86 O ANISOU 2357 O ASN A 235 11210 13911 12438 -354 313 -584 O ATOM 2358 CB ASN A 235 -39.886 64.920 66.263 1.00103.66 C ANISOU 2358 CB ASN A 235 11651 14842 12891 -416 306 -617 C ATOM 2359 N ASP A 236 -42.192 65.601 64.661 1.00100.14 N ANISOU 2359 N ASP A 236 11274 14209 12564 -445 326 -686 N ATOM 2360 CA ASP A 236 -43.553 65.352 64.175 1.00 98.08 C ANISOU 2360 CA ASP A 236 11054 13886 12325 -463 328 -687 C ATOM 2361 C ASP A 236 -43.972 66.265 63.018 1.00 97.95 C ANISOU 2361 C ASP A 236 11051 13776 12389 -447 341 -742 C ATOM 2362 O ASP A 236 -44.659 65.814 62.099 1.00 97.88 O ANISOU 2362 O ASP A 236 11097 13684 12407 -435 339 -715 O ATOM 2363 CB ASP A 236 -44.556 65.500 65.323 1.00 98.49 C ANISOU 2363 CB ASP A 236 11059 14033 12329 -523 331 -726 C ATOM 2364 N ASP A 237 -43.558 67.533 63.063 1.00 99.11 N ANISOU 2364 N ASP A 237 11151 13935 12570 -449 353 -817 N ATOM 2365 CA ASP A 237 -44.006 68.547 62.082 1.00 99.63 C ANISOU 2365 CA ASP A 237 11229 13916 12709 -435 365 -874 C ATOM 2366 C ASP A 237 -43.411 68.300 60.698 1.00 99.27 C ANISOU 2366 C ASP A 237 11241 13765 12712 -389 363 -828 C ATOM 2367 O ASP A 237 -44.117 68.353 59.686 1.00 98.64 O ANISOU 2367 O ASP A 237 11201 13599 12676 -372 365 -828 O ATOM 2368 CB ASP A 237 -43.626 69.971 62.524 1.00100.23 C ANISOU 2368 CB ASP A 237 11253 14025 12805 -453 380 -965 C ATOM 2369 CG ASP A 237 -44.011 70.270 63.961 1.00100.27 C ANISOU 2369 CG ASP A 237 11193 14146 12757 -498 383 -1017 C ATOM 2370 OD1 ASP A 237 -43.414 69.652 64.867 1.00 97.49 O ANISOU 2370 OD1 ASP A 237 10813 13884 12344 -515 375 -981 O ATOM 2371 OD2 ASP A 237 -44.892 71.127 64.181 1.00101.98 O ANISOU 2371 OD2 ASP A 237 11387 14368 12990 -511 393 -1093 O ATOM 2372 N ILE A 238 -42.109 68.022 60.678 1.00 98.56 N ANISOU 2372 N ILE A 238 11149 13692 12607 -369 358 -791 N ATOM 2373 CA ILE A 238 -41.357 67.799 59.446 1.00 98.60 C ANISOU 2373 CA ILE A 238 11198 13615 12649 -325 356 -751 C ATOM 2374 C ILE A 238 -41.671 66.406 58.873 1.00 97.12 C ANISOU 2374 C ILE A 238 11077 13374 12450 -294 343 -668 C ATOM 2375 O ILE A 238 -41.606 66.205 57.661 1.00 97.55 O ANISOU 2375 O ILE A 238 11179 13340 12544 -260 343 -643 O ATOM 2376 CB ILE A 238 -39.829 67.997 59.678 1.00100.87 C ANISOU 2376 CB ILE A 238 11450 13959 12916 -313 356 -745 C ATOM 2377 CG1 ILE A 238 -39.531 69.437 60.164 1.00101.73 C ANISOU 2377 CG1 ILE A 238 11502 14110 13038 -356 372 -833 C ATOM 2378 CG2 ILE A 238 -39.027 67.677 58.418 1.00100.38 C ANISOU 2378 CG2 ILE A 238 11428 13826 12883 -265 353 -701 C ATOM 2379 CD1 ILE A 238 -39.480 69.619 61.673 1.00102.26 C ANISOU 2379 CD1 ILE A 238 11505 14298 13047 -397 372 -867 C ATOM 2380 N PHE A 239 -42.014 65.455 59.744 1.00 96.23 N ANISOU 2380 N PHE A 239 10970 13313 12277 -309 333 -627 N ATOM 2381 CA PHE A 239 -42.488 64.131 59.320 1.00 95.95 C ANISOU 2381 CA PHE A 239 11007 13222 12224 -294 322 -554 C ATOM 2382 C PHE A 239 -43.818 64.210 58.568 1.00 94.28 C ANISOU 2382 C PHE A 239 10829 12943 12050 -313 328 -574 C ATOM 2383 O PHE A 239 -44.029 63.452 57.625 1.00 94.40 O ANISOU 2383 O PHE A 239 10909 12877 12080 -292 324 -529 O ATOM 2384 CB PHE A 239 -42.621 63.196 60.534 1.00 98.09 C ANISOU 2384 CB PHE A 239 11280 13569 12420 -317 310 -509 C ATOM 2385 CG PHE A 239 -43.054 61.794 60.192 1.00 99.79 C ANISOU 2385 CG PHE A 239 11582 13723 12610 -309 299 -431 C ATOM 2386 CD1 PHE A 239 -42.119 60.834 59.823 1.00101.02 C ANISOU 2386 CD1 PHE A 239 11794 13838 12749 -251 287 -360 C ATOM 2387 CD2 PHE A 239 -44.398 61.425 60.256 1.00100.68 C ANISOU 2387 CD2 PHE A 239 11721 13822 12709 -361 301 -432 C ATOM 2388 CE1 PHE A 239 -42.513 59.540 59.514 1.00101.34 C ANISOU 2388 CE1 PHE A 239 11926 13812 12765 -245 278 -290 C ATOM 2389 CE2 PHE A 239 -44.798 60.133 59.948 1.00100.76 C ANISOU 2389 CE2 PHE A 239 11817 13772 12692 -366 293 -362 C ATOM 2390 CZ PHE A 239 -43.853 59.187 59.577 1.00101.51 C ANISOU 2390 CZ PHE A 239 11979 13813 12776 -308 281 -291 C ATOM 2391 N LYS A 240 -44.702 65.120 58.983 1.00 91.68 N ANISOU 2391 N LYS A 240 10452 12650 11731 -351 337 -643 N ATOM 2392 CA LYS A 240 -46.025 65.262 58.361 1.00 90.96 C ANISOU 2392 CA LYS A 240 10377 12515 11666 -367 343 -668 C ATOM 2393 C LYS A 240 -45.957 65.753 56.910 1.00 89.71 C ANISOU 2393 C LYS A 240 10250 12258 11577 -328 348 -678 C ATOM 2394 O LYS A 240 -46.689 65.249 56.054 1.00 88.43 O ANISOU 2394 O LYS A 240 10133 12038 11428 -325 347 -655 O ATOM 2395 CB LYS A 240 -46.919 66.195 59.188 1.00 90.13 C ANISOU 2395 CB LYS A 240 10207 12483 11552 -405 351 -746 C ATOM 2396 N ILE A 241 -45.085 66.726 56.642 1.00 89.18 N ANISOU 2396 N ILE A 241 10159 12176 11549 -304 355 -712 N ATOM 2397 CA ILE A 241 -44.898 67.247 55.275 1.00 88.87 C ANISOU 2397 CA ILE A 241 10149 12045 11572 -269 360 -718 C ATOM 2398 C ILE A 241 -44.186 66.241 54.355 1.00 87.18 C ANISOU 2398 C ILE A 241 9991 11771 11360 -233 353 -646 C ATOM 2399 O ILE A 241 -44.584 66.069 53.204 1.00 84.30 O ANISOU 2399 O ILE A 241 9668 11332 11029 -214 353 -631 O ATOM 2400 CB ILE A 241 -44.181 68.632 55.239 1.00 90.00 C ANISOU 2400 CB ILE A 241 10256 12186 11753 -265 371 -776 C ATOM 2401 CG1 ILE A 241 -42.708 68.557 55.684 1.00 91.85 C ANISOU 2401 CG1 ILE A 241 10468 12464 11963 -261 369 -757 C ATOM 2402 CG2 ILE A 241 -44.935 69.647 56.094 1.00 90.16 C ANISOU 2402 CG2 ILE A 241 10228 12254 11772 -294 379 -853 C ATOM 2403 CD1 ILE A 241 -41.940 69.845 55.477 1.00 94.37 C ANISOU 2403 CD1 ILE A 241 10762 12774 12317 -267 381 -809 C ATOM 2404 N ILE A 242 -43.149 65.578 54.869 1.00 85.64 N ANISOU 2404 N ILE A 242 9797 11614 11128 -220 345 -604 N ATOM 2405 CA ILE A 242 -42.340 64.654 54.067 1.00 85.47 C ANISOU 2405 CA ILE A 242 9826 11543 11105 -174 337 -541 C ATOM 2406 C ILE A 242 -43.161 63.421 53.682 1.00 85.27 C ANISOU 2406 C ILE A 242 9869 11467 11062 -175 330 -490 C ATOM 2407 O ILE A 242 -43.095 62.960 52.541 1.00 84.76 O ANISOU 2407 O ILE A 242 9855 11326 11021 -145 329 -462 O ATOM 2408 CB ILE A 242 -41.049 64.227 54.806 1.00 85.66 C ANISOU 2408 CB ILE A 242 9831 11633 11084 -151 330 -508 C ATOM 2409 CG1 ILE A 242 -40.098 65.417 54.970 1.00 84.52 C ANISOU 2409 CG1 ILE A 242 9622 11535 10955 -155 338 -557 C ATOM 2410 CG2 ILE A 242 -40.322 63.134 54.041 1.00 85.92 C ANISOU 2410 CG2 ILE A 242 9921 11617 11107 -94 320 -442 C ATOM 2411 CD1 ILE A 242 -39.017 65.192 56.008 1.00 83.80 C ANISOU 2411 CD1 ILE A 242 9488 11543 10808 -147 332 -542 C ATOM 2412 N MET A 243 -43.907 62.893 54.651 1.00 83.98 N ANISOU 2412 N MET A 243 9706 11350 10853 -215 326 -481 N ATOM 2413 CA MET A 243 -44.869 61.814 54.428 1.00 83.63 C ANISOU 2413 CA MET A 243 9724 11267 10785 -239 321 -442 C ATOM 2414 C MET A 243 -45.842 62.170 53.301 1.00 80.39 C ANISOU 2414 C MET A 243 9329 10796 10419 -248 329 -470 C ATOM 2415 O MET A 243 -46.060 61.369 52.393 1.00 80.89 O ANISOU 2415 O MET A 243 9456 10789 10487 -237 327 -433 O ATOM 2416 CB MET A 243 -45.641 61.539 55.727 1.00 87.29 C ANISOU 2416 CB MET A 243 10165 11807 11191 -297 319 -445 C ATOM 2417 CG MET A 243 -46.552 60.322 55.727 1.00 91.50 C ANISOU 2417 CG MET A 243 10766 12315 11683 -338 314 -399 C ATOM 2418 SD MET A 243 -45.640 58.769 55.807 1.00 98.54 S ANISOU 2418 SD MET A 243 11750 13159 12531 -302 300 -304 S ATOM 2419 CE MET A 243 -46.958 57.632 56.237 1.00 99.93 C ANISOU 2419 CE MET A 243 11989 13331 12645 -385 297 -268 C ATOM 2420 N ALA A 244 -46.396 63.379 53.354 1.00 76.97 N ANISOU 2420 N ALA A 244 8838 10390 10016 -263 338 -536 N ATOM 2421 CA ALA A 244 -47.412 63.819 52.390 1.00 76.52 C ANISOU 2421 CA ALA A 244 8786 10292 9996 -267 345 -566 C ATOM 2422 C ALA A 244 -46.837 64.028 50.993 1.00 75.18 C ANISOU 2422 C ALA A 244 8646 10038 9878 -219 347 -554 C ATOM 2423 O ALA A 244 -47.499 63.739 49.998 1.00 75.09 O ANISOU 2423 O ALA A 244 8669 9977 9882 -217 348 -545 O ATOM 2424 CB ALA A 244 -48.098 65.090 52.877 1.00 77.47 C ANISOU 2424 CB ALA A 244 8839 10463 10132 -282 352 -639 C ATOM 2425 N ILE A 245 -45.607 64.536 50.936 1.00 75.00 N ANISOU 2425 N ILE A 245 8607 10010 9876 -186 348 -556 N ATOM 2426 CA ILE A 245 -44.862 64.674 49.685 1.00 73.60 C ANISOU 2426 CA ILE A 245 8456 9766 9740 -143 350 -540 C ATOM 2427 C ILE A 245 -44.543 63.301 49.107 1.00 73.19 C ANISOU 2427 C ILE A 245 8470 9669 9668 -120 342 -477 C ATOM 2428 O ILE A 245 -44.777 63.056 47.922 1.00 71.56 O ANISOU 2428 O ILE A 245 8302 9399 9485 -104 344 -463 O ATOM 2429 CB ILE A 245 -43.548 65.473 49.890 1.00 74.89 C ANISOU 2429 CB ILE A 245 8582 9954 9919 -123 353 -556 C ATOM 2430 CG1 ILE A 245 -43.859 66.942 50.213 1.00 76.43 C ANISOU 2430 CG1 ILE A 245 8727 10169 10143 -144 362 -623 C ATOM 2431 CG2 ILE A 245 -42.671 65.431 48.641 1.00 74.52 C ANISOU 2431 CG2 ILE A 245 8562 9850 9901 -82 354 -531 C ATOM 2432 CD1 ILE A 245 -42.710 67.695 50.853 1.00 76.93 C ANISOU 2432 CD1 ILE A 245 8747 10279 10204 -149 367 -648 C ATOM 2433 N VAL A 246 -43.999 62.421 49.949 1.00 74.03 N ANISOU 2433 N VAL A 246 8592 9806 9727 -117 334 -439 N ATOM 2434 CA VAL A 246 -43.591 61.078 49.528 1.00 74.26 C ANISOU 2434 CA VAL A 246 8694 9788 9731 -87 326 -378 C ATOM 2435 C VAL A 246 -44.766 60.235 49.039 1.00 75.84 C ANISOU 2435 C VAL A 246 8955 9938 9921 -119 327 -360 C ATOM 2436 O VAL A 246 -44.671 59.618 47.980 1.00 74.57 O ANISOU 2436 O VAL A 246 8850 9709 9772 -94 326 -335 O ATOM 2437 CB VAL A 246 -42.826 60.334 50.649 1.00 74.52 C ANISOU 2437 CB VAL A 246 8734 9868 9710 -72 316 -339 C ATOM 2438 CG1 VAL A 246 -42.747 58.831 50.387 1.00 75.28 C ANISOU 2438 CG1 VAL A 246 8922 9907 9774 -49 307 -275 C ATOM 2439 CG2 VAL A 246 -41.423 60.906 50.781 1.00 74.55 C ANISOU 2439 CG2 VAL A 246 8689 9915 9720 -27 315 -345 C ATOM 2440 N LEU A 247 -45.856 60.198 49.806 1.00 77.84 N ANISOU 2440 N LEU A 247 9195 10232 10147 -178 327 -375 N ATOM 2441 CA LEU A 247 -47.000 59.347 49.447 1.00 79.03 C ANISOU 2441 CA LEU A 247 9401 10349 10275 -223 328 -359 C ATOM 2442 C LEU A 247 -47.656 59.788 48.148 1.00 80.58 C ANISOU 2442 C LEU A 247 9597 10503 10514 -222 336 -386 C ATOM 2443 O LEU A 247 -47.953 58.944 47.298 1.00 80.44 O ANISOU 2443 O LEU A 247 9643 10426 10491 -227 336 -360 O ATOM 2444 CB LEU A 247 -48.045 59.255 50.569 1.00 78.84 C ANISOU 2444 CB LEU A 247 9353 10396 10206 -294 328 -372 C ATOM 2445 CG LEU A 247 -47.875 58.045 51.492 1.00 78.73 C ANISOU 2445 CG LEU A 247 9394 10389 10129 -319 319 -317 C ATOM 2446 CD1 LEU A 247 -46.721 58.268 52.458 1.00 79.65 C ANISOU 2446 CD1 LEU A 247 9477 10552 10232 -281 312 -305 C ATOM 2447 CD2 LEU A 247 -49.162 57.759 52.251 1.00 79.17 C ANISOU 2447 CD2 LEU A 247 9443 10502 10135 -405 321 -326 C ATOM 2448 N PHE A 248 -47.865 61.098 47.996 1.00 82.47 N ANISOU 2448 N PHE A 248 9769 10771 10794 -214 341 -438 N ATOM 2449 CA PHE A 248 -48.432 61.656 46.761 1.00 82.77 C ANISOU 2449 CA PHE A 248 9802 10773 10872 -203 347 -462 C ATOM 2450 C PHE A 248 -47.549 61.364 45.550 1.00 82.14 C ANISOU 2450 C PHE A 248 9764 10620 10822 -153 347 -434 C ATOM 2451 O PHE A 248 -48.044 60.882 44.528 1.00 82.23 O ANISOU 2451 O PHE A 248 9817 10588 10839 -157 349 -423 O ATOM 2452 CB PHE A 248 -48.650 63.172 46.871 1.00 83.91 C ANISOU 2452 CB PHE A 248 9874 10952 11054 -191 352 -519 C ATOM 2453 CG PHE A 248 -49.157 63.798 45.597 1.00 85.86 C ANISOU 2453 CG PHE A 248 10118 11161 11342 -170 357 -538 C ATOM 2454 CD1 PHE A 248 -50.505 63.723 45.262 1.00 86.10 C ANISOU 2454 CD1 PHE A 248 10143 11211 11359 -198 358 -556 C ATOM 2455 CD2 PHE A 248 -48.284 64.439 44.716 1.00 85.71 C ANISOU 2455 CD2 PHE A 248 10101 11094 11369 -124 359 -537 C ATOM 2456 CE1 PHE A 248 -50.976 64.281 44.082 1.00 87.03 C ANISOU 2456 CE1 PHE A 248 10256 11300 11509 -174 361 -570 C ATOM 2457 CE2 PHE A 248 -48.751 65.001 43.536 1.00 86.21 C ANISOU 2457 CE2 PHE A 248 10164 11123 11466 -105 362 -549 C ATOM 2458 CZ PHE A 248 -50.098 64.917 43.216 1.00 86.78 C ANISOU 2458 CZ PHE A 248 10231 11214 11525 -126 362 -565 C ATOM 2459 N PHE A 249 -46.254 61.661 45.682 1.00 82.03 N ANISOU 2459 N PHE A 249 9738 10604 10823 -110 346 -425 N ATOM 2460 CA PHE A 249 -45.284 61.532 44.585 1.00 81.99 C ANISOU 2460 CA PHE A 249 9759 10547 10844 -59 346 -403 C ATOM 2461 C PHE A 249 -45.318 60.142 43.955 1.00 82.51 C ANISOU 2461 C PHE A 249 9905 10556 10886 -50 343 -361 C ATOM 2462 O PHE A 249 -45.392 60.018 42.734 1.00 81.14 O ANISOU 2462 O PHE A 249 9758 10336 10734 -33 346 -357 O ATOM 2463 CB PHE A 249 -43.868 61.862 45.081 1.00 82.92 C ANISOU 2463 CB PHE A 249 9848 10693 10962 -21 344 -398 C ATOM 2464 CG PHE A 249 -42.824 61.900 43.994 1.00 83.67 C ANISOU 2464 CG PHE A 249 9955 10755 11080 28 345 -383 C ATOM 2465 CD1 PHE A 249 -42.911 62.825 42.958 1.00 84.23 C ANISOU 2465 CD1 PHE A 249 10006 10801 11195 33 352 -407 C ATOM 2466 CD2 PHE A 249 -41.740 61.031 44.018 1.00 84.23 C ANISOU 2466 CD2 PHE A 249 10054 10823 11125 74 339 -346 C ATOM 2467 CE1 PHE A 249 -41.951 62.868 41.955 1.00 84.42 C ANISOU 2467 CE1 PHE A 249 10037 10802 11235 73 354 -394 C ATOM 2468 CE2 PHE A 249 -40.771 61.072 43.024 1.00 85.44 C ANISOU 2468 CE2 PHE A 249 10210 10959 11294 121 341 -337 C ATOM 2469 CZ PHE A 249 -40.878 61.991 41.989 1.00 85.41 C ANISOU 2469 CZ PHE A 249 10184 10934 11332 116 349 -361 C ATOM 2470 N PHE A 250 -45.308 59.111 44.796 1.00 83.99 N ANISOU 2470 N PHE A 250 10134 10749 11028 -64 337 -329 N ATOM 2471 CA PHE A 250 -45.317 57.726 44.333 1.00 86.64 C ANISOU 2471 CA PHE A 250 10561 11022 11336 -57 333 -287 C ATOM 2472 C PHE A 250 -46.685 57.257 43.843 1.00 87.92 C ANISOU 2472 C PHE A 250 10760 11158 11486 -118 338 -294 C ATOM 2473 O PHE A 250 -46.753 56.458 42.906 1.00 89.12 O ANISOU 2473 O PHE A 250 10978 11247 11635 -111 340 -277 O ATOM 2474 CB PHE A 250 -44.806 56.784 45.428 1.00 90.57 C ANISOU 2474 CB PHE A 250 11100 11528 11785 -49 324 -246 C ATOM 2475 CG PHE A 250 -43.385 57.056 45.879 1.00 93.29 C ANISOU 2475 CG PHE A 250 11411 11906 12129 16 318 -234 C ATOM 2476 CD1 PHE A 250 -42.436 57.645 45.032 1.00 95.03 C ANISOU 2476 CD1 PHE A 250 11598 12122 12384 72 321 -247 C ATOM 2477 CD2 PHE A 250 -42.981 56.677 47.156 1.00 95.64 C ANISOU 2477 CD2 PHE A 250 11707 12248 12384 18 309 -209 C ATOM 2478 CE1 PHE A 250 -41.136 57.863 45.463 1.00 97.56 C ANISOU 2478 CE1 PHE A 250 11882 12488 12696 125 316 -238 C ATOM 2479 CE2 PHE A 250 -41.680 56.894 47.588 1.00 97.56 C ANISOU 2479 CE2 PHE A 250 11914 12536 12619 78 303 -199 C ATOM 2480 CZ PHE A 250 -40.758 57.492 46.742 1.00 98.02 C ANISOU 2480 CZ PHE A 250 11935 12595 12710 130 307 -215 C ATOM 2481 N PHE A 251 -47.763 57.727 44.472 1.00 88.36 N ANISOU 2481 N PHE A 251 10773 11269 11531 -178 341 -322 N ATOM 2482 CA PHE A 251 -49.124 57.461 43.970 1.00 88.45 C ANISOU 2482 CA PHE A 251 10800 11279 11528 -240 346 -337 C ATOM 2483 C PHE A 251 -49.362 58.101 42.595 1.00 87.36 C ANISOU 2483 C PHE A 251 10640 11118 11432 -216 352 -362 C ATOM 2484 O PHE A 251 -50.091 57.544 41.770 1.00 87.04 O ANISOU 2484 O PHE A 251 10637 11051 11380 -247 356 -361 O ATOM 2485 CB PHE A 251 -50.210 57.936 44.957 1.00 89.91 C ANISOU 2485 CB PHE A 251 10928 11546 11686 -302 348 -367 C ATOM 2486 CG PHE A 251 -50.681 56.874 45.920 1.00 91.64 C ANISOU 2486 CG PHE A 251 11195 11781 11843 -367 345 -339 C ATOM 2487 CD1 PHE A 251 -51.237 55.684 45.450 1.00 94.24 C ANISOU 2487 CD1 PHE A 251 11608 12062 12135 -416 347 -313 C ATOM 2488 CD2 PHE A 251 -50.614 57.075 47.295 1.00 92.76 C ANISOU 2488 CD2 PHE A 251 11299 11987 11956 -387 341 -340 C ATOM 2489 CE1 PHE A 251 -51.685 54.707 46.331 1.00 95.45 C ANISOU 2489 CE1 PHE A 251 11814 12225 12227 -485 345 -283 C ATOM 2490 CE2 PHE A 251 -51.063 56.104 48.180 1.00 94.52 C ANISOU 2490 CE2 PHE A 251 11568 12227 12117 -451 338 -310 C ATOM 2491 CZ PHE A 251 -51.600 54.918 47.698 1.00 95.24 C ANISOU 2491 CZ PHE A 251 11749 12264 12173 -502 340 -280 C ATOM 2492 N SER A 252 -48.754 59.264 42.362 1.00 84.18 N ANISOU 2492 N SER A 252 10178 10728 11076 -167 353 -384 N ATOM 2493 CA SER A 252 -48.844 59.956 41.069 1.00 82.54 C ANISOU 2493 CA SER A 252 9951 10499 10910 -140 357 -402 C ATOM 2494 C SER A 252 -48.183 59.199 39.904 1.00 79.31 C ANISOU 2494 C SER A 252 9602 10022 10508 -106 358 -374 C ATOM 2495 O SER A 252 -48.635 59.306 38.761 1.00 78.06 O ANISOU 2495 O SER A 252 9449 9845 10365 -105 362 -383 O ATOM 2496 CB SER A 252 -48.222 61.354 41.176 1.00 82.40 C ANISOU 2496 CB SER A 252 9869 10503 10936 -100 358 -427 C ATOM 2497 OG SER A 252 -48.773 62.070 42.267 1.00 83.58 O ANISOU 2497 OG SER A 252 9964 10711 11078 -126 358 -459 O ATOM 2498 N TRP A 253 -47.120 58.450 40.196 1.00 75.94 N ANISOU 2498 N TRP A 253 9219 9565 10068 -73 354 -342 N ATOM 2499 CA TRP A 253 -46.370 57.715 39.161 1.00 75.12 C ANISOU 2499 CA TRP A 253 9172 9402 9968 -29 355 -319 C ATOM 2500 C TRP A 253 -46.948 56.342 38.791 1.00 73.96 C ANISOU 2500 C TRP A 253 9113 9201 9784 -60 357 -299 C ATOM 2501 O TRP A 253 -46.498 55.734 37.816 1.00 72.72 O ANISOU 2501 O TRP A 253 9006 8992 9630 -27 359 -288 O ATOM 2502 CB TRP A 253 -44.887 57.588 39.556 1.00 74.70 C ANISOU 2502 CB TRP A 253 9120 9347 9914 34 350 -297 C ATOM 2503 CG TRP A 253 -44.069 58.735 39.069 1.00 73.22 C ANISOU 2503 CG TRP A 253 8868 9183 9767 74 352 -314 C ATOM 2504 CD1 TRP A 253 -43.844 59.919 39.707 1.00 72.56 C ANISOU 2504 CD1 TRP A 253 8713 9151 9703 69 353 -336 C ATOM 2505 CD2 TRP A 253 -43.384 58.816 37.818 1.00 72.49 C ANISOU 2505 CD2 TRP A 253 8781 9065 9695 118 356 -311 C ATOM 2506 NE1 TRP A 253 -43.051 60.732 38.932 1.00 72.13 N ANISOU 2506 NE1 TRP A 253 8625 9100 9681 102 356 -345 N ATOM 2507 CE2 TRP A 253 -42.749 60.076 37.769 1.00 71.49 C ANISOU 2507 CE2 TRP A 253 8586 8977 9600 133 358 -329 C ATOM 2508 CE3 TRP A 253 -43.237 57.939 36.734 1.00 72.51 C ANISOU 2508 CE3 TRP A 253 8841 9018 9690 143 358 -297 C ATOM 2509 CZ2 TRP A 253 -41.980 60.485 36.676 1.00 72.06 C ANISOU 2509 CZ2 TRP A 253 8642 9043 9692 168 362 -330 C ATOM 2510 CZ3 TRP A 253 -42.467 58.345 35.647 1.00 71.75 C ANISOU 2510 CZ3 TRP A 253 8724 8919 9616 185 361 -301 C ATOM 2511 CH2 TRP A 253 -41.851 59.607 35.627 1.00 71.62 C ANISOU 2511 CH2 TRP A 253 8636 8946 9628 195 363 -315 C ATOM 2512 N ILE A 254 -47.934 55.860 39.552 1.00 74.25 N ANISOU 2512 N ILE A 254 9171 9254 9785 -128 356 -298 N ATOM 2513 CA ILE A 254 -48.593 54.583 39.253 1.00 74.53 C ANISOU 2513 CA ILE A 254 9296 9240 9780 -177 360 -282 C ATOM 2514 C ILE A 254 -49.398 54.659 37.942 1.00 75.38 C ANISOU 2514 C ILE A 254 9403 9339 9897 -204 368 -306 C ATOM 2515 O ILE A 254 -49.192 53.808 37.069 1.00 77.12 O ANISOU 2515 O ILE A 254 9695 9497 10110 -194 371 -296 O ATOM 2516 CB ILE A 254 -49.457 54.061 40.435 1.00 74.20 C ANISOU 2516 CB ILE A 254 9275 9226 9688 -256 358 -274 C ATOM 2517 CG1 ILE A 254 -48.566 53.705 41.631 1.00 74.31 C ANISOU 2517 CG1 ILE A 254 9311 9238 9684 -224 349 -240 C ATOM 2518 CG2 ILE A 254 -50.263 52.828 40.020 1.00 75.58 C ANISOU 2518 CG2 ILE A 254 9543 9351 9819 -324 364 -263 C ATOM 2519 CD1 ILE A 254 -49.310 53.583 42.944 1.00 74.37 C ANISOU 2519 CD1 ILE A 254 9308 9299 9649 -296 347 -236 C ATOM 2520 N PRO A 255 -50.302 55.664 37.791 1.00 73.74 N ANISOU 2520 N PRO A 255 9116 9195 9704 -234 370 -340 N ATOM 2521 CA PRO A 255 -51.013 55.821 36.515 1.00 73.45 C ANISOU 2521 CA PRO A 255 9070 9162 9676 -250 377 -361 C ATOM 2522 C PRO A 255 -50.106 55.802 35.285 1.00 73.02 C ANISOU 2522 C PRO A 255 9035 9054 9652 -186 379 -353 C ATOM 2523 O PRO A 255 -50.381 55.074 34.339 1.00 71.38 O ANISOU 2523 O PRO A 255 8879 8812 9430 -204 384 -354 O ATOM 2524 CB PRO A 255 -51.687 57.188 36.661 1.00 72.51 C ANISOU 2524 CB PRO A 255 8852 9119 9579 -252 376 -393 C ATOM 2525 CG PRO A 255 -51.968 57.302 38.106 1.00 71.98 C ANISOU 2525 CG PRO A 255 8760 9097 9489 -284 372 -396 C ATOM 2526 CD PRO A 255 -50.851 56.578 38.814 1.00 73.42 C ANISOU 2526 CD PRO A 255 8998 9231 9664 -258 368 -361 C ATOM 2527 N HIS A 256 -49.024 56.579 35.328 1.00 74.96 N ANISOU 2527 N HIS A 256 9242 9302 9937 -117 375 -349 N ATOM 2528 CA HIS A 256 -48.106 56.706 34.193 1.00 74.69 C ANISOU 2528 CA HIS A 256 9212 9235 9931 -57 377 -344 C ATOM 2529 C HIS A 256 -47.280 55.452 33.944 1.00 76.23 C ANISOU 2529 C HIS A 256 9493 9364 10106 -25 377 -320 C ATOM 2530 O HIS A 256 -47.146 55.031 32.794 1.00 76.76 O ANISOU 2530 O HIS A 256 9592 9397 10173 -9 382 -323 O ATOM 2531 CB HIS A 256 -47.174 57.907 34.380 1.00 73.66 C ANISOU 2531 CB HIS A 256 9014 9131 9840 -3 373 -346 C ATOM 2532 CG HIS A 256 -46.421 58.282 33.143 1.00 73.27 C ANISOU 2532 CG HIS A 256 8953 9067 9818 44 376 -345 C ATOM 2533 ND1 HIS A 256 -45.060 58.491 33.135 1.00 74.15 N ANISOU 2533 ND1 HIS A 256 9052 9176 9943 101 375 -333 N ATOM 2534 CD2 HIS A 256 -46.836 58.467 31.869 1.00 73.06 C ANISOU 2534 CD2 HIS A 256 8922 9036 9802 41 381 -354 C ATOM 2535 CE1 HIS A 256 -44.669 58.800 31.913 1.00 73.08 C ANISOU 2535 CE1 HIS A 256 8905 9034 9825 128 378 -335 C ATOM 2536 NE2 HIS A 256 -45.726 58.784 31.124 1.00 73.42 N ANISOU 2536 NE2 HIS A 256 8954 9073 9866 94 382 -346 N ATOM 2537 N GLN A 257 -46.729 54.861 35.005 1.00 78.15 N ANISOU 2537 N GLN A 257 9772 9591 10328 -11 371 -298 N ATOM 2538 CA GLN A 257 -45.926 53.641 34.863 1.00 82.38 C ANISOU 2538 CA GLN A 257 10397 10062 10841 30 370 -274 C ATOM 2539 C GLN A 257 -46.739 52.509 34.210 1.00 82.53 C ANISOU 2539 C GLN A 257 10506 10023 10829 -19 377 -276 C ATOM 2540 O GLN A 257 -46.188 51.707 33.454 1.00 83.06 O ANISOU 2540 O GLN A 257 10639 10031 10888 20 379 -271 O ATOM 2541 CB GLN A 257 -45.332 53.194 36.208 1.00 85.90 C ANISOU 2541 CB GLN A 257 10869 10505 11264 51 361 -245 C ATOM 2542 CG GLN A 257 -44.291 52.073 36.115 1.00 89.81 C ANISOU 2542 CG GLN A 257 11448 10936 11736 122 357 -218 C ATOM 2543 CD GLN A 257 -43.026 52.473 35.350 1.00 92.22 C ANISOU 2543 CD GLN A 257 11716 11256 12067 213 356 -222 C ATOM 2544 OE1 GLN A 257 -42.343 53.435 35.717 1.00 93.15 O ANISOU 2544 OE1 GLN A 257 11751 11435 12205 244 352 -226 O ATOM 2545 NE2 GLN A 257 -42.703 51.729 34.287 1.00 92.47 N ANISOU 2545 NE2 GLN A 257 11807 11232 12091 251 360 -225 N ATOM 2546 N ILE A 258 -48.043 52.472 34.489 1.00 81.14 N ANISOU 2546 N ILE A 258 10327 9869 10631 -108 380 -288 N ATOM 2547 CA ILE A 258 -48.963 51.538 33.836 1.00 80.70 C ANISOU 2547 CA ILE A 258 10344 9775 10543 -176 389 -298 C ATOM 2548 C ILE A 258 -49.022 51.800 32.324 1.00 81.19 C ANISOU 2548 C ILE A 258 10385 9836 10625 -159 396 -321 C ATOM 2549 O ILE A 258 -48.870 50.870 31.531 1.00 84.14 O ANISOU 2549 O ILE A 258 10838 10148 10982 -155 402 -323 O ATOM 2550 CB ILE A 258 -50.381 51.600 34.470 1.00 80.06 C ANISOU 2550 CB ILE A 258 10243 9745 10429 -281 391 -310 C ATOM 2551 CG1 ILE A 258 -50.343 51.065 35.908 1.00 80.27 C ANISOU 2551 CG1 ILE A 258 10311 9762 10424 -308 386 -283 C ATOM 2552 CG2 ILE A 258 -51.398 50.796 33.662 1.00 79.95 C ANISOU 2552 CG2 ILE A 258 10287 9711 10379 -362 402 -327 C ATOM 2553 CD1 ILE A 258 -51.463 51.585 36.787 1.00 81.22 C ANISOU 2553 CD1 ILE A 258 10368 9966 10522 -387 385 -297 C ATOM 2554 N PHE A 259 -49.220 53.056 31.924 1.00 79.54 N ANISOU 2554 N PHE A 259 10076 9693 10450 -147 395 -339 N ATOM 2555 CA PHE A 259 -49.365 53.384 30.494 1.00 78.79 C ANISOU 2555 CA PHE A 259 9956 9608 10370 -136 401 -358 C ATOM 2556 C PHE A 259 -48.052 53.418 29.707 1.00 81.54 C ANISOU 2556 C PHE A 259 10311 9925 10745 -49 401 -351 C ATOM 2557 O PHE A 259 -48.058 53.149 28.505 1.00 82.99 O ANISOU 2557 O PHE A 259 10513 10094 10926 -43 407 -363 O ATOM 2558 CB PHE A 259 -50.185 54.665 30.292 1.00 76.27 C ANISOU 2558 CB PHE A 259 9538 9369 10072 -157 400 -377 C ATOM 2559 CG PHE A 259 -51.662 54.447 30.460 1.00 74.65 C ANISOU 2559 CG PHE A 259 9328 9206 9829 -246 404 -395 C ATOM 2560 CD1 PHE A 259 -52.390 53.771 29.480 1.00 73.50 C ANISOU 2560 CD1 PHE A 259 9218 9057 9651 -297 412 -411 C ATOM 2561 CD2 PHE A 259 -52.323 54.875 31.605 1.00 72.82 C ANISOU 2561 CD2 PHE A 259 9054 9026 9586 -283 400 -400 C ATOM 2562 CE1 PHE A 259 -53.749 53.542 29.635 1.00 72.24 C ANISOU 2562 CE1 PHE A 259 9048 8949 9448 -386 416 -430 C ATOM 2563 CE2 PHE A 259 -53.683 54.653 31.765 1.00 73.01 C ANISOU 2563 CE2 PHE A 259 9067 9104 9567 -368 403 -419 C ATOM 2564 CZ PHE A 259 -54.395 53.983 30.779 1.00 73.92 C ANISOU 2564 CZ PHE A 259 9216 9221 9650 -421 412 -433 C ATOM 2565 N THR A 260 -46.941 53.750 30.365 1.00 84.15 N ANISOU 2565 N THR A 260 10622 10255 11095 14 394 -333 N ATOM 2566 CA THR A 260 -45.624 53.686 29.719 1.00 86.82 C ANISOU 2566 CA THR A 260 10965 10574 11448 96 394 -327 C ATOM 2567 C THR A 260 -45.135 52.238 29.585 1.00 88.29 C ANISOU 2567 C THR A 260 11257 10685 11601 125 395 -318 C ATOM 2568 O THR A 260 -44.365 51.927 28.679 1.00 89.52 O ANISOU 2568 O THR A 260 11432 10821 11759 182 398 -323 O ATOM 2569 CB THR A 260 -44.571 54.571 30.430 1.00 88.48 C ANISOU 2569 CB THR A 260 11111 10824 11684 152 386 -314 C ATOM 2570 OG1 THR A 260 -43.478 54.822 29.536 1.00 91.32 O ANISOU 2570 OG1 THR A 260 11447 11192 12057 217 388 -315 O ATOM 2571 CG2 THR A 260 -44.045 53.925 31.698 1.00 88.65 C ANISOU 2571 CG2 THR A 260 11173 10826 11684 173 379 -292 C ATOM 2572 N PHE A 261 -45.572 51.361 30.487 1.00 90.38 N ANISOU 2572 N PHE A 261 11593 10908 11835 88 393 -305 N ATOM 2573 CA PHE A 261 -45.387 49.930 30.293 1.00 93.17 C ANISOU 2573 CA PHE A 261 12068 11177 12155 100 396 -299 C ATOM 2574 C PHE A 261 -46.162 49.514 29.042 1.00 92.12 C ANISOU 2574 C PHE A 261 11969 11021 12010 50 408 -327 C ATOM 2575 O PHE A 261 -45.580 48.962 28.106 1.00 92.17 O ANISOU 2575 O PHE A 261 12020 10987 12012 99 413 -338 O ATOM 2576 CB PHE A 261 -45.851 49.135 31.517 1.00 96.47 C ANISOU 2576 CB PHE A 261 12560 11554 12538 53 392 -276 C ATOM 2577 CG PHE A 261 -45.677 47.648 31.375 1.00102.22 C ANISOU 2577 CG PHE A 261 13429 12180 13230 63 395 -266 C ATOM 2578 CD1 PHE A 261 -44.409 47.072 31.459 1.00105.04 C ANISOU 2578 CD1 PHE A 261 13838 12490 13582 171 389 -248 C ATOM 2579 CD2 PHE A 261 -46.776 46.818 31.152 1.00105.35 C ANISOU 2579 CD2 PHE A 261 13909 12528 13592 -32 405 -277 C ATOM 2580 CE1 PHE A 261 -44.240 45.698 31.327 1.00107.67 C ANISOU 2580 CE1 PHE A 261 14310 12718 13881 191 391 -240 C ATOM 2581 CE2 PHE A 261 -46.613 45.442 31.022 1.00108.30 C ANISOU 2581 CE2 PHE A 261 14424 12793 13929 -25 408 -270 C ATOM 2582 CZ PHE A 261 -45.343 44.882 31.107 1.00109.08 C ANISOU 2582 CZ PHE A 261 14581 12835 14028 90 401 -250 C ATOM 2583 N LEU A 262 -47.462 49.816 29.023 1.00 88.31 N ANISOU 2583 N LEU A 262 11458 10575 11519 -44 413 -342 N ATOM 2584 CA LEU A 262 -48.316 49.542 27.854 1.00 86.46 C ANISOU 2584 CA LEU A 262 11240 10341 11269 -102 424 -371 C ATOM 2585 C LEU A 262 -47.756 50.085 26.535 1.00 86.93 C ANISOU 2585 C LEU A 262 11248 10427 11355 -45 427 -387 C ATOM 2586 O LEU A 262 -47.888 49.435 25.499 1.00 86.59 O ANISOU 2586 O LEU A 262 11253 10353 11293 -56 436 -408 O ATOM 2587 CB LEU A 262 -49.741 50.074 28.064 1.00 84.51 C ANISOU 2587 CB LEU A 262 10937 10163 11009 -201 426 -385 C ATOM 2588 CG LEU A 262 -50.806 49.071 28.503 1.00 83.40 C ANISOU 2588 CG LEU A 262 10876 9994 10816 -306 433 -390 C ATOM 2589 CD1 LEU A 262 -50.417 48.300 29.757 1.00 84.11 C ANISOU 2589 CD1 LEU A 262 11048 10022 10887 -304 427 -359 C ATOM 2590 CD2 LEU A 262 -52.119 49.812 28.704 1.00 82.49 C ANISOU 2590 CD2 LEU A 262 10676 9975 10689 -388 434 -406 C ATOM 2591 N ASP A 263 -47.143 51.269 26.579 1.00 87.83 N ANISOU 2591 N ASP A 263 11266 10597 11508 8 420 -378 N ATOM 2592 CA ASP A 263 -46.518 51.870 25.388 1.00 87.82 C ANISOU 2592 CA ASP A 263 11211 10626 11528 61 423 -388 C ATOM 2593 C ASP A 263 -45.332 51.041 24.882 1.00 88.92 C ANISOU 2593 C ASP A 263 11412 10714 11660 139 425 -389 C ATOM 2594 O ASP A 263 -45.112 50.946 23.675 1.00 89.29 O ANISOU 2594 O ASP A 263 11455 10765 11703 159 432 -406 O ATOM 2595 CB ASP A 263 -46.071 53.317 25.673 1.00 86.30 C ANISOU 2595 CB ASP A 263 10913 10498 11376 95 415 -375 C ATOM 2596 CG ASP A 263 -45.733 54.105 24.404 1.00 85.48 C ANISOU 2596 CG ASP A 263 10748 10436 11292 124 418 -383 C ATOM 2597 OD1 ASP A 263 -46.229 53.749 23.311 1.00 87.14 O ANISOU 2597 OD1 ASP A 263 10975 10645 11486 100 426 -400 O ATOM 2598 OD2 ASP A 263 -44.977 55.098 24.502 1.00 82.80 O ANISOU 2598 OD2 ASP A 263 10343 10133 10981 165 414 -371 O ATOM 2599 N VAL A 264 -44.577 50.447 25.807 1.00 90.69 N ANISOU 2599 N VAL A 264 11687 10894 11875 187 419 -370 N ATOM 2600 CA VAL A 264 -43.453 49.564 25.463 1.00 92.48 C ANISOU 2600 CA VAL A 264 11978 11071 12087 273 420 -371 C ATOM 2601 C VAL A 264 -43.926 48.246 24.805 1.00 95.77 C ANISOU 2601 C VAL A 264 12510 11408 12469 246 429 -392 C ATOM 2602 O VAL A 264 -43.207 47.679 23.977 1.00 97.88 O ANISOU 2602 O VAL A 264 12817 11647 12726 309 434 -409 O ATOM 2603 CB VAL A 264 -42.525 49.337 26.693 1.00 92.20 C ANISOU 2603 CB VAL A 264 11962 11021 12048 339 409 -342 C ATOM 2604 CG1 VAL A 264 -41.498 48.231 26.451 1.00 93.57 C ANISOU 2604 CG1 VAL A 264 12220 11134 12196 432 408 -342 C ATOM 2605 CG2 VAL A 264 -41.812 50.639 27.051 1.00 89.83 C ANISOU 2605 CG2 VAL A 264 11544 10805 11779 374 402 -330 C ATOM 2606 N LEU A 265 -45.128 47.777 25.149 1.00 98.25 N ANISOU 2606 N LEU A 265 12878 11690 12762 149 434 -396 N ATOM 2607 CA LEU A 265 -45.767 46.667 24.415 1.00 99.53 C ANISOU 2607 CA LEU A 265 13141 11785 12889 97 446 -423 C ATOM 2608 C LEU A 265 -46.139 47.085 22.978 1.00101.45 C ANISOU 2608 C LEU A 265 13330 12079 13136 72 456 -456 C ATOM 2609 O LEU A 265 -45.994 46.293 22.043 1.00104.10 O ANISOU 2609 O LEU A 265 13731 12370 13451 84 465 -484 O ATOM 2610 CB LEU A 265 -47.009 46.130 25.151 1.00 98.97 C ANISOU 2610 CB LEU A 265 13132 11683 12788 -17 449 -419 C ATOM 2611 CG LEU A 265 -46.788 45.177 26.333 1.00 99.03 C ANISOU 2611 CG LEU A 265 13249 11606 12771 -11 444 -391 C ATOM 2612 CD1 LEU A 265 -46.125 45.868 27.510 1.00 98.83 C ANISOU 2612 CD1 LEU A 265 13160 11619 12770 46 429 -354 C ATOM 2613 CD2 LEU A 265 -48.107 44.562 26.778 1.00 98.98 C ANISOU 2613 CD2 LEU A 265 13309 11571 12725 -143 451 -394 C ATOM 2614 N ILE A 266 -46.613 48.322 22.815 1.00102.11 N ANISOU 2614 N ILE A 266 13296 12255 13244 42 453 -453 N ATOM 2615 CA ILE A 266 -46.947 48.880 21.490 1.00104.66 C ANISOU 2615 CA ILE A 266 13555 12639 13572 25 459 -477 C ATOM 2616 C ILE A 266 -45.696 49.077 20.624 1.00106.67 C ANISOU 2616 C ILE A 266 13782 12905 13841 122 460 -482 C ATOM 2617 O ILE A 266 -45.708 48.718 19.444 1.00110.74 O ANISOU 2617 O ILE A 266 14312 13421 14340 122 469 -509 O ATOM 2618 CB ILE A 266 -47.747 50.212 21.598 1.00103.59 C ANISOU 2618 CB ILE A 266 13305 12595 13458 -19 454 -468 C ATOM 2619 CG1 ILE A 266 -49.124 49.966 22.238 1.00103.02 C ANISOU 2619 CG1 ILE A 266 13253 12530 13360 -121 456 -473 C ATOM 2620 CG2 ILE A 266 -47.925 50.871 20.229 1.00103.18 C ANISOU 2620 CG2 ILE A 266 13185 12608 13411 -18 458 -483 C ATOM 2621 CD1 ILE A 266 -49.741 51.193 22.878 1.00102.10 C ANISOU 2621 CD1 ILE A 266 13037 12490 13265 -144 447 -459 C ATOM 2622 N GLN A 267 -44.636 49.648 21.198 1.00107.51 N ANISOU 2622 N GLN A 267 13843 13030 13974 199 450 -457 N ATOM 2623 CA GLN A 267 -43.372 49.858 20.468 1.00110.12 C ANISOU 2623 CA GLN A 267 14139 13387 14313 289 450 -461 C ATOM 2624 C GLN A 267 -42.708 48.549 20.025 1.00111.42 C ANISOU 2624 C GLN A 267 14403 13482 14447 348 456 -483 C ATOM 2625 O GLN A 267 -42.146 48.480 18.930 1.00113.02 O ANISOU 2625 O GLN A 267 14590 13708 14642 391 462 -505 O ATOM 2626 CB GLN A 267 -42.375 50.671 21.303 1.00112.12 C ANISOU 2626 CB GLN A 267 14327 13679 14592 351 439 -432 C ATOM 2627 CG GLN A 267 -42.735 52.140 21.461 1.00112.93 C ANISOU 2627 CG GLN A 267 14324 13856 14728 313 435 -416 C ATOM 2628 CD GLN A 267 -41.739 52.897 22.325 1.00114.36 C ANISOU 2628 CD GLN A 267 14447 14072 14930 364 426 -392 C ATOM 2629 OE1 GLN A 267 -40.530 52.674 22.237 1.00114.68 O ANISOU 2629 OE1 GLN A 267 14486 14123 14963 440 424 -391 O ATOM 2630 NE2 GLN A 267 -42.242 53.802 23.162 1.00115.51 N ANISOU 2630 NE2 GLN A 267 14544 14244 15099 323 420 -376 N ATOM 2631 N LEU A 268 -42.776 47.523 20.874 1.00111.01 N ANISOU 2631 N LEU A 268 14455 13346 14377 351 455 -478 N ATOM 2632 CA LEU A 268 -42.174 46.217 20.576 1.00110.29 C ANISOU 2632 CA LEU A 268 14476 13172 14256 414 460 -498 C ATOM 2633 C LEU A 268 -42.873 45.444 19.444 1.00109.55 C ANISOU 2633 C LEU A 268 14451 13038 14135 360 475 -540 C ATOM 2634 O LEU A 268 -42.249 44.594 18.803 1.00109.87 O ANISOU 2634 O LEU A 268 14559 13031 14153 424 481 -568 O ATOM 2635 CB LEU A 268 -42.135 45.351 21.841 1.00110.63 C ANISOU 2635 CB LEU A 268 14622 13127 14284 426 453 -474 C ATOM 2636 N GLY A 269 -44.151 45.741 19.202 1.00108.03 N ANISOU 2636 N GLY A 269 14236 12871 13939 247 481 -549 N ATOM 2637 CA GLY A 269 -44.966 45.016 18.223 1.00107.12 C ANISOU 2637 CA GLY A 269 14182 12727 13792 176 495 -590 C ATOM 2638 C GLY A 269 -45.781 43.887 18.835 1.00108.49 C ANISOU 2638 C GLY A 269 14486 12801 13932 99 501 -596 C ATOM 2639 O GLY A 269 -46.368 43.086 18.104 1.00109.35 O ANISOU 2639 O GLY A 269 14670 12869 14008 39 515 -635 O ATOM 2640 N ILE A 270 -45.830 43.830 20.170 1.00108.73 N ANISOU 2640 N ILE A 270 14545 12798 13969 92 492 -560 N ATOM 2641 CA ILE A 270 -46.588 42.805 20.900 1.00108.67 C ANISOU 2641 CA ILE A 270 14662 12698 13927 12 496 -557 C ATOM 2642 C ILE A 270 -48.087 43.021 20.690 1.00108.74 C ANISOU 2642 C ILE A 270 14641 12757 13915 -133 505 -574 C ATOM 2643 O ILE A 270 -48.822 42.065 20.435 1.00109.87 O ANISOU 2643 O ILE A 270 14886 12841 14017 -220 518 -600 O ATOM 2644 CB ILE A 270 -46.251 42.806 22.419 1.00108.48 C ANISOU 2644 CB ILE A 270 14660 12643 13913 41 482 -508 C ATOM 2645 CG1 ILE A 270 -44.787 42.396 22.639 1.00109.13 C ANISOU 2645 CG1 ILE A 270 14787 12673 14004 188 473 -494 C ATOM 2646 CG2 ILE A 270 -47.173 41.861 23.194 1.00108.63 C ANISOU 2646 CG2 ILE A 270 14800 12580 13893 -61 487 -500 C ATOM 2647 CD1 ILE A 270 -44.227 42.763 23.997 1.00109.25 C ANISOU 2647 CD1 ILE A 270 14774 12699 14034 240 457 -445 C ATOM 2648 N ILE A 271 -48.519 44.278 20.795 1.00107.78 N ANISOU 2648 N ILE A 271 14382 12748 13819 -157 498 -559 N ATOM 2649 CA ILE A 271 -49.921 44.661 20.624 1.00108.21 C ANISOU 2649 CA ILE A 271 14384 12876 13854 -280 504 -573 C ATOM 2650 C ILE A 271 -50.042 45.563 19.386 1.00107.94 C ANISOU 2650 C ILE A 271 14237 12941 13834 -268 506 -593 C ATOM 2651 O ILE A 271 -49.272 46.513 19.227 1.00108.28 O ANISOU 2651 O ILE A 271 14190 13033 13916 -183 497 -575 O ATOM 2652 CB ILE A 271 -50.474 45.312 21.922 1.00109.57 C ANISOU 2652 CB ILE A 271 14500 13093 14036 -321 493 -540 C ATOM 2653 CG1 ILE A 271 -52.006 45.300 21.948 1.00110.39 C ANISOU 2653 CG1 ILE A 271 14586 13255 14100 -459 500 -558 C ATOM 2654 CG2 ILE A 271 -49.937 46.722 22.141 1.00109.03 C ANISOU 2654 CG2 ILE A 271 14299 13107 14019 -245 480 -515 C ATOM 2655 CD1 ILE A 271 -52.569 45.514 23.339 1.00109.84 C ANISOU 2655 CD1 ILE A 271 14504 13205 14025 -511 493 -530 C ATOM 2656 N ARG A 272 -50.986 45.235 18.503 1.00108.30 N ANISOU 2656 N ARG A 272 14291 13016 13841 -356 518 -630 N ATOM 2657 CA ARG A 272 -51.131 45.896 17.196 1.00106.82 C ANISOU 2657 CA ARG A 272 14013 12917 13656 -349 522 -651 C ATOM 2658 C ARG A 272 -52.194 46.990 17.205 1.00103.64 C ANISOU 2658 C ARG A 272 13489 12634 13253 -407 516 -642 C ATOM 2659 O ARG A 272 -51.915 48.130 16.824 1.00104.03 O ANISOU 2659 O ARG A 272 13432 12757 13336 -351 508 -625 O ATOM 2660 CB ARG A 272 -51.480 44.858 16.119 1.00108.83 C ANISOU 2660 CB ARG A 272 14347 13139 13863 -405 540 -701 C ATOM 2661 CG ARG A 272 -51.665 45.411 14.702 1.00110.73 C ANISOU 2661 CG ARG A 272 14502 13475 14096 -405 544 -725 C ATOM 2662 CD ARG A 272 -53.127 45.694 14.355 1.00110.92 C ANISOU 2662 CD ARG A 272 14466 13597 14080 -521 549 -742 C ATOM 2663 NE ARG A 272 -53.298 46.163 12.980 1.00111.23 N ANISOU 2663 NE ARG A 272 14428 13728 14107 -518 553 -764 N ATOM 2664 CZ ARG A 272 -54.453 46.571 12.448 1.00112.14 C ANISOU 2664 CZ ARG A 272 14468 13952 14186 -597 555 -777 C ATOM 2665 NH1 ARG A 272 -55.581 46.581 13.165 1.00111.61 N ANISOU 2665 NH1 ARG A 272 14389 13926 14092 -689 554 -776 N ATOM 2666 NH2 ARG A 272 -54.484 46.976 11.179 1.00111.95 N ANISOU 2666 NH2 ARG A 272 14377 14007 14149 -584 558 -792 N ATOM 2667 N ASP A 273 -53.407 46.609 17.611 1.00 98.61 N ANISOU 2667 N ASP A 273 12874 12017 12574 -520 522 -655 N ATOM 2668 CA ASP A 273 -54.625 47.427 17.470 1.00 95.99 C ANISOU 2668 CA ASP A 273 12437 11810 12224 -588 519 -659 C ATOM 2669 C ASP A 273 -54.372 48.925 17.670 1.00 93.13 C ANISOU 2669 C ASP A 273 11949 11522 11912 -511 503 -624 C ATOM 2670 O ASP A 273 -53.912 49.339 18.732 1.00 93.15 O ANISOU 2670 O ASP A 273 11942 11498 11950 -466 493 -594 O ATOM 2671 CB ASP A 273 -55.702 46.932 18.456 1.00 95.80 C ANISOU 2671 CB ASP A 273 12449 11791 12157 -699 522 -663 C ATOM 2672 CG ASP A 273 -57.101 47.443 18.127 1.00 96.10 C ANISOU 2672 CG ASP A 273 12395 11964 12154 -787 524 -682 C ATOM 2673 OD1 ASP A 273 -57.450 47.567 16.929 1.00 96.23 O ANISOU 2673 OD1 ASP A 273 12369 12045 12147 -802 530 -707 O ATOM 2674 OD2 ASP A 273 -57.864 47.697 19.083 1.00 94.58 O ANISOU 2674 OD2 ASP A 273 12170 11819 11946 -839 519 -672 O ATOM 2675 N CYS A 274 -54.645 49.722 16.638 1.00 90.22 N ANISOU 2675 N CYS A 274 11490 11243 11544 -495 501 -629 N ATOM 2676 CA CYS A 274 -54.397 51.169 16.690 1.00 87.96 C ANISOU 2676 CA CYS A 274 11095 11019 11304 -422 486 -597 C ATOM 2677 C CYS A 274 -55.366 51.913 17.603 1.00 86.35 C ANISOU 2677 C CYS A 274 10825 10883 11098 -455 477 -585 C ATOM 2678 O CYS A 274 -55.039 52.998 18.095 1.00 85.52 O ANISOU 2678 O CYS A 274 10657 10797 11038 -393 465 -556 O ATOM 2679 CB CYS A 274 -54.439 51.789 15.290 1.00 88.49 C ANISOU 2679 CB CYS A 274 11092 11160 11367 -396 486 -601 C ATOM 2680 SG CYS A 274 -53.099 51.269 14.196 1.00 91.27 S ANISOU 2680 SG CYS A 274 11493 11453 11731 -330 494 -611 S ATOM 2681 N ARG A 275 -56.555 51.349 17.815 1.00 85.42 N ANISOU 2681 N ARG A 275 10720 10807 10926 -556 484 -609 N ATOM 2682 CA ARG A 275 -57.488 51.877 18.808 1.00 83.78 C ANISOU 2682 CA ARG A 275 10457 10665 10707 -594 476 -604 C ATOM 2683 C ARG A 275 -56.894 51.769 20.221 1.00 80.62 C ANISOU 2683 C ARG A 275 10102 10190 10340 -571 471 -581 C ATOM 2684 O ARG A 275 -57.081 52.667 21.038 1.00 78.84 O ANISOU 2684 O ARG A 275 9812 10005 10138 -544 460 -564 O ATOM 2685 CB ARG A 275 -58.851 51.171 18.705 1.00 86.00 C ANISOU 2685 CB ARG A 275 10747 11017 10913 -718 486 -639 C ATOM 2686 CG ARG A 275 -59.922 51.625 19.701 1.00 89.09 C ANISOU 2686 CG ARG A 275 11074 11494 11278 -766 480 -640 C ATOM 2687 CD ARG A 275 -60.160 53.136 19.710 1.00 89.20 C ANISOU 2687 CD ARG A 275 10968 11598 11325 -688 464 -622 C ATOM 2688 NE ARG A 275 -61.049 53.541 20.801 1.00 90.14 N ANISOU 2688 NE ARG A 275 11034 11790 11424 -721 458 -625 N ATOM 2689 CZ ARG A 275 -61.227 54.796 21.231 1.00 91.20 C ANISOU 2689 CZ ARG A 275 11080 11983 11589 -651 444 -611 C ATOM 2690 NH1 ARG A 275 -60.584 55.824 20.669 1.00 90.62 N ANISOU 2690 NH1 ARG A 275 10964 11898 11569 -548 434 -588 N ATOM 2691 NH2 ARG A 275 -62.062 55.030 22.243 1.00 90.95 N ANISOU 2691 NH2 ARG A 275 11005 12021 11531 -687 441 -621 N ATOM 2692 N ILE A 276 -56.165 50.685 20.489 1.00 79.22 N ANISOU 2692 N ILE A 276 10034 9904 10162 -576 478 -581 N ATOM 2693 CA ILE A 276 -55.416 50.525 21.744 1.00 77.82 C ANISOU 2693 CA ILE A 276 9904 9650 10014 -541 473 -554 C ATOM 2694 C ILE A 276 -54.244 51.510 21.812 1.00 76.34 C ANISOU 2694 C ILE A 276 9666 9446 9891 -424 461 -526 C ATOM 2695 O ILE A 276 -54.027 52.139 22.850 1.00 73.63 O ANISOU 2695 O ILE A 276 9289 9108 9577 -393 452 -505 O ATOM 2696 CB ILE A 276 -54.932 49.064 21.944 1.00 78.87 C ANISOU 2696 CB ILE A 276 10176 9667 10124 -568 482 -560 C ATOM 2697 CG1 ILE A 276 -56.143 48.153 22.185 1.00 79.81 C ANISOU 2697 CG1 ILE A 276 10350 9799 10176 -702 493 -583 C ATOM 2698 CG2 ILE A 276 -53.950 48.955 23.110 1.00 79.74 C ANISOU 2698 CG2 ILE A 276 10331 9699 10267 -507 474 -527 C ATOM 2699 CD1 ILE A 276 -55.834 46.673 22.157 1.00 81.60 C ANISOU 2699 CD1 ILE A 276 10726 9907 10370 -743 505 -594 C ATOM 2700 N ALA A 277 -53.497 51.639 20.715 1.00 76.19 N ANISOU 2700 N ALA A 277 9642 9414 9892 -365 463 -527 N ATOM 2701 CA ALA A 277 -52.437 52.648 20.623 1.00 76.01 C ANISOU 2701 CA ALA A 277 9563 9392 9923 -266 454 -502 C ATOM 2702 C ALA A 277 -52.989 54.036 20.945 1.00 76.63 C ANISOU 2702 C ALA A 277 9538 9551 10025 -255 443 -489 C ATOM 2703 O ALA A 277 -52.471 54.718 21.828 1.00 75.46 O ANISOU 2703 O ALA A 277 9363 9394 9914 -211 435 -468 O ATOM 2704 CB ALA A 277 -51.792 52.636 19.246 1.00 75.72 C ANISOU 2704 CB ALA A 277 9522 9355 9891 -222 459 -510 C ATOM 2705 N ASP A 278 -54.065 54.418 20.252 1.00 78.49 N ANISOU 2705 N ASP A 278 9719 9867 10234 -294 444 -503 N ATOM 2706 CA ASP A 278 -54.765 55.702 20.472 1.00 77.58 C ANISOU 2706 CA ASP A 278 9509 9833 10132 -281 434 -495 C ATOM 2707 C ASP A 278 -55.081 55.988 21.940 1.00 76.69 C ANISOU 2707 C ASP A 278 9383 9724 10028 -293 427 -490 C ATOM 2708 O ASP A 278 -54.905 57.116 22.402 1.00 75.24 O ANISOU 2708 O ASP A 278 9144 9561 9883 -243 418 -475 O ATOM 2709 CB ASP A 278 -56.075 55.738 19.678 1.00 78.71 C ANISOU 2709 CB ASP A 278 9607 10069 10227 -336 436 -516 C ATOM 2710 CG ASP A 278 -56.721 57.113 19.677 1.00 80.01 C ANISOU 2710 CG ASP A 278 9675 10318 10405 -300 424 -506 C ATOM 2711 OD1 ASP A 278 -56.055 58.075 19.238 1.00 80.62 O ANISOU 2711 OD1 ASP A 278 9718 10386 10524 -226 417 -482 O ATOM 2712 OD2 ASP A 278 -57.895 57.237 20.105 1.00 79.12 O ANISOU 2712 OD2 ASP A 278 9522 10281 10257 -344 422 -522 O ATOM 2713 N ILE A 279 -55.558 54.966 22.651 1.00 76.76 N ANISOU 2713 N ILE A 279 9449 9715 10000 -365 434 -504 N ATOM 2714 CA ILE A 279 -55.891 55.073 24.083 1.00 75.68 C ANISOU 2714 CA ILE A 279 9306 9587 9861 -389 429 -500 C ATOM 2715 C ILE A 279 -54.651 55.355 24.939 1.00 73.94 C ANISOU 2715 C ILE A 279 9105 9298 9691 -322 423 -475 C ATOM 2716 O ILE A 279 -54.685 56.214 25.814 1.00 73.62 O ANISOU 2716 O ILE A 279 9014 9284 9674 -297 415 -468 O ATOM 2717 CB ILE A 279 -56.625 53.800 24.584 1.00 76.09 C ANISOU 2717 CB ILE A 279 9425 9629 9854 -491 438 -517 C ATOM 2718 CG1 ILE A 279 -58.039 53.752 23.991 1.00 76.56 C ANISOU 2718 CG1 ILE A 279 9440 9790 9858 -568 443 -546 C ATOM 2719 CG2 ILE A 279 -56.709 53.757 26.112 1.00 76.76 C ANISOU 2719 CG2 ILE A 279 9520 9707 9938 -513 434 -507 C ATOM 2720 CD1 ILE A 279 -58.669 52.375 23.994 1.00 77.87 C ANISOU 2720 CD1 ILE A 279 9686 9942 9959 -680 456 -567 C ATOM 2721 N VAL A 280 -53.577 54.614 24.684 1.00 73.64 N ANISOU 2721 N VAL A 280 9138 9177 9663 -292 427 -464 N ATOM 2722 CA VAL A 280 -52.295 54.791 25.376 1.00 70.44 C ANISOU 2722 CA VAL A 280 8749 8716 9298 -223 422 -441 C ATOM 2723 C VAL A 280 -51.691 56.156 25.051 1.00 70.27 C ANISOU 2723 C VAL A 280 8650 8722 9325 -152 415 -429 C ATOM 2724 O VAL A 280 -51.292 56.886 25.957 1.00 70.53 O ANISOU 2724 O VAL A 280 8650 8759 9387 -121 408 -418 O ATOM 2725 CB VAL A 280 -51.300 53.661 25.004 1.00 69.84 C ANISOU 2725 CB VAL A 280 8764 8556 9216 -197 428 -436 C ATOM 2726 CG1 VAL A 280 -49.881 53.970 25.480 1.00 69.66 C ANISOU 2726 CG1 VAL A 280 8740 8496 9231 -113 421 -413 C ATOM 2727 CG2 VAL A 280 -51.785 52.333 25.578 1.00 69.95 C ANISOU 2727 CG2 VAL A 280 8870 8521 9183 -266 434 -442 C ATOM 2728 N ASP A 281 -51.643 56.498 23.764 1.00 69.63 N ANISOU 2728 N ASP A 281 8544 8662 9250 -131 417 -432 N ATOM 2729 CA ASP A 281 -51.012 57.745 23.302 1.00 67.66 C ANISOU 2729 CA ASP A 281 8234 8432 9042 -69 411 -417 C ATOM 2730 C ASP A 281 -51.732 59.000 23.783 1.00 68.26 C ANISOU 2730 C ASP A 281 8238 8560 9135 -66 403 -416 C ATOM 2731 O ASP A 281 -51.081 60.011 24.063 1.00 69.44 O ANISOU 2731 O ASP A 281 8354 8706 9324 -20 398 -402 O ATOM 2732 CB ASP A 281 -50.925 57.778 21.777 1.00 67.92 C ANISOU 2732 CB ASP A 281 8257 8481 9068 -56 415 -418 C ATOM 2733 CG ASP A 281 -50.055 56.668 21.209 1.00 69.32 C ANISOU 2733 CG ASP A 281 8500 8605 9231 -42 424 -423 C ATOM 2734 OD1 ASP A 281 -49.485 55.881 22.000 1.00 68.09 O ANISOU 2734 OD1 ASP A 281 8401 8395 9073 -36 425 -421 O ATOM 2735 OD2 ASP A 281 -49.954 56.581 19.960 1.00 70.95 O ANISOU 2735 OD2 ASP A 281 8702 8826 9427 -34 428 -428 O ATOM 2736 N THR A 282 -53.064 58.947 23.848 1.00 68.17 N ANISOU 2736 N THR A 282 8204 8603 9091 -115 403 -433 N ATOM 2737 CA THR A 282 -53.858 60.041 24.420 1.00 67.81 C ANISOU 2737 CA THR A 282 8094 8614 9056 -108 395 -438 C ATOM 2738 C THR A 282 -53.767 60.079 25.958 1.00 65.63 C ANISOU 2738 C THR A 282 7822 8326 8789 -117 392 -442 C ATOM 2739 O THR A 282 -53.755 61.161 26.552 1.00 63.21 O ANISOU 2739 O THR A 282 7470 8035 8510 -83 385 -441 O ATOM 2740 CB THR A 282 -55.338 60.010 23.950 1.00 69.82 C ANISOU 2740 CB THR A 282 8311 8951 9265 -151 395 -459 C ATOM 2741 OG1 THR A 282 -55.963 61.257 24.276 1.00 73.62 O ANISOU 2741 OG1 THR A 282 8724 9485 9760 -117 385 -462 O ATOM 2742 CG2 THR A 282 -56.135 58.895 24.606 1.00 71.53 C ANISOU 2742 CG2 THR A 282 8559 9186 9431 -232 401 -480 C ATOM 2743 N ALA A 283 -53.692 58.905 26.590 1.00 64.95 N ANISOU 2743 N ALA A 283 7793 8208 8675 -162 397 -445 N ATOM 2744 CA ALA A 283 -53.544 58.807 28.052 1.00 64.92 C ANISOU 2744 CA ALA A 283 7798 8194 8673 -174 394 -444 C ATOM 2745 C ALA A 283 -52.214 59.369 28.541 1.00 65.29 C ANISOU 2745 C ALA A 283 7844 8197 8767 -113 391 -426 C ATOM 2746 O ALA A 283 -52.158 59.954 29.620 1.00 67.97 O ANISOU 2746 O ALA A 283 8154 8549 9119 -105 386 -429 O ATOM 2747 CB ALA A 283 -53.687 57.361 28.517 1.00 63.65 C ANISOU 2747 CB ALA A 283 7711 8000 8469 -236 401 -444 C ATOM 2748 N MET A 284 -51.160 59.175 27.746 1.00 65.13 N ANISOU 2748 N MET A 284 7850 8130 8764 -73 393 -410 N ATOM 2749 CA MET A 284 -49.784 59.512 28.129 1.00 65.91 C ANISOU 2749 CA MET A 284 7951 8194 8896 -20 391 -394 C ATOM 2750 C MET A 284 -49.613 60.953 28.643 1.00 64.63 C ANISOU 2750 C MET A 284 7727 8057 8771 7 385 -395 C ATOM 2751 O MET A 284 -49.210 61.127 29.797 1.00 65.17 O ANISOU 2751 O MET A 284 7790 8123 8847 11 383 -395 O ATOM 2752 CB MET A 284 -48.797 59.185 26.984 1.00 68.87 C ANISOU 2752 CB MET A 284 8352 8537 9278 17 395 -382 C ATOM 2753 CG MET A 284 -48.428 57.710 26.885 1.00 71.18 C ANISOU 2753 CG MET A 284 8721 8782 9540 10 400 -380 C ATOM 2754 SD MET A 284 -46.922 57.285 27.775 1.00 75.96 S ANISOU 2754 SD MET A 284 9359 9348 10153 63 397 -362 S ATOM 2755 CE MET A 284 -45.683 57.756 26.565 1.00 75.46 C ANISOU 2755 CE MET A 284 9270 9289 10112 126 399 -355 C ATOM 2756 N PRO A 285 -49.936 61.983 27.820 1.00 61.30 N ANISOU 2756 N PRO A 285 7263 7657 8369 26 384 -397 N ATOM 2757 CA PRO A 285 -49.865 63.377 28.299 1.00 59.44 C ANISOU 2757 CA PRO A 285 6981 7435 8167 51 379 -400 C ATOM 2758 C PRO A 285 -50.508 63.609 29.657 1.00 59.31 C ANISOU 2758 C PRO A 285 6943 7445 8145 31 376 -420 C ATOM 2759 O PRO A 285 -49.942 64.323 30.490 1.00 59.77 O ANISOU 2759 O PRO A 285 6984 7496 8227 47 374 -423 O ATOM 2760 CB PRO A 285 -50.653 64.156 27.244 1.00 59.68 C ANISOU 2760 CB PRO A 285 6981 7492 8202 64 377 -401 C ATOM 2761 CG PRO A 285 -50.571 63.340 26.012 1.00 60.05 C ANISOU 2761 CG PRO A 285 7054 7533 8228 57 381 -390 C ATOM 2762 CD PRO A 285 -50.303 61.917 26.394 1.00 60.12 C ANISOU 2762 CD PRO A 285 7113 7519 8210 28 386 -393 C ATOM 2763 N ILE A 286 -51.682 63.014 29.865 1.00 59.83 N ANISOU 2763 N ILE A 286 7010 7547 8175 -9 376 -435 N ATOM 2764 CA ILE A 286 -52.460 63.219 31.089 1.00 60.71 C ANISOU 2764 CA ILE A 286 7094 7700 8273 -33 373 -457 C ATOM 2765 C ILE A 286 -51.743 62.586 32.274 1.00 61.77 C ANISOU 2765 C ILE A 286 7256 7812 8400 -49 374 -451 C ATOM 2766 O ILE A 286 -51.605 63.207 33.325 1.00 64.03 O ANISOU 2766 O ILE A 286 7516 8114 8699 -43 371 -462 O ATOM 2767 CB ILE A 286 -53.895 62.651 30.971 1.00 60.57 C ANISOU 2767 CB ILE A 286 7066 7740 8207 -82 374 -475 C ATOM 2768 CG1 ILE A 286 -54.671 63.395 29.872 1.00 61.44 C ANISOU 2768 CG1 ILE A 286 7137 7888 8319 -57 371 -481 C ATOM 2769 CG2 ILE A 286 -54.631 62.764 32.306 1.00 60.39 C ANISOU 2769 CG2 ILE A 286 7014 7769 8163 -112 372 -498 C ATOM 2770 CD1 ILE A 286 -55.955 62.715 29.440 1.00 61.87 C ANISOU 2770 CD1 ILE A 286 7180 8006 8319 -107 373 -497 C ATOM 2771 N THR A 287 -51.292 61.352 32.095 1.00 62.54 N ANISOU 2771 N THR A 287 7411 7875 8477 -68 377 -433 N ATOM 2772 CA THR A 287 -50.530 60.648 33.125 1.00 64.31 C ANISOU 2772 CA THR A 287 7670 8073 8690 -74 377 -420 C ATOM 2773 C THR A 287 -49.193 61.334 33.455 1.00 64.34 C ANISOU 2773 C THR A 287 7658 8057 8730 -23 375 -410 C ATOM 2774 O THR A 287 -48.717 61.251 34.585 1.00 65.63 O ANISOU 2774 O THR A 287 7821 8227 8889 -24 373 -407 O ATOM 2775 CB THR A 287 -50.299 59.166 32.725 1.00 65.29 C ANISOU 2775 CB THR A 287 7871 8153 8783 -93 381 -402 C ATOM 2776 OG1 THR A 287 -50.278 59.038 31.299 1.00 65.62 O ANISOU 2776 OG1 THR A 287 7926 8176 8830 -79 384 -400 O ATOM 2777 CG2 THR A 287 -51.407 58.276 33.252 1.00 65.57 C ANISOU 2777 CG2 THR A 287 7936 8208 8770 -165 382 -409 C ATOM 2778 N ILE A 288 -48.605 62.010 32.469 1.00 66.82 N ANISOU 2778 N ILE A 288 7956 8356 9074 14 376 -405 N ATOM 2779 CA ILE A 288 -47.380 62.805 32.655 1.00 68.41 C ANISOU 2779 CA ILE A 288 8135 8548 9306 52 376 -399 C ATOM 2780 C ILE A 288 -47.638 64.065 33.483 1.00 70.20 C ANISOU 2780 C ILE A 288 8314 8803 9556 50 374 -421 C ATOM 2781 O ILE A 288 -46.793 64.434 34.298 1.00 69.95 O ANISOU 2781 O ILE A 288 8267 8775 9534 59 373 -422 O ATOM 2782 CB ILE A 288 -46.732 63.175 31.296 1.00 68.80 C ANISOU 2782 CB ILE A 288 8184 8579 9377 83 379 -386 C ATOM 2783 CG1 ILE A 288 -46.241 61.910 30.583 1.00 68.95 C ANISOU 2783 CG1 ILE A 288 8252 8571 9372 94 381 -370 C ATOM 2784 CG2 ILE A 288 -45.551 64.130 31.471 1.00 69.83 C ANISOU 2784 CG2 ILE A 288 8286 8710 9534 109 379 -383 C ATOM 2785 CD1 ILE A 288 -46.202 62.029 29.078 1.00 69.47 C ANISOU 2785 CD1 ILE A 288 8320 8630 9446 108 385 -363 C ATOM 2786 N CYS A 289 -48.784 64.723 33.278 1.00 73.94 N ANISOU 2786 N CYS A 289 8761 9297 10035 42 372 -439 N ATOM 2787 CA CYS A 289 -49.175 65.884 34.107 1.00 76.24 C ANISOU 2787 CA CYS A 289 9011 9611 10344 45 370 -466 C ATOM 2788 C CYS A 289 -49.232 65.513 35.577 1.00 76.55 C ANISOU 2788 C CYS A 289 9043 9679 10362 19 369 -480 C ATOM 2789 O CYS A 289 -48.706 66.237 36.423 1.00 75.25 O ANISOU 2789 O CYS A 289 8855 9521 10213 25 370 -494 O ATOM 2790 CB CYS A 289 -50.547 66.430 33.710 1.00 78.82 C ANISOU 2790 CB CYS A 289 9312 9966 10667 46 368 -486 C ATOM 2791 SG CYS A 289 -50.668 67.045 32.019 1.00 86.02 S ANISOU 2791 SG CYS A 289 10226 10855 11600 80 367 -469 S ATOM 2792 N ILE A 290 -49.864 64.371 35.853 1.00 77.75 N ANISOU 2792 N ILE A 290 9217 9849 10476 -15 369 -474 N ATOM 2793 CA ILE A 290 -50.066 63.865 37.215 1.00 78.67 C ANISOU 2793 CA ILE A 290 9332 9997 10562 -48 367 -482 C ATOM 2794 C ILE A 290 -48.713 63.618 37.892 1.00 78.61 C ANISOU 2794 C ILE A 290 9338 9971 10557 -33 367 -464 C ATOM 2795 O ILE A 290 -48.496 64.041 39.035 1.00 79.19 O ANISOU 2795 O ILE A 290 9383 10073 10629 -39 365 -479 O ATOM 2796 CB ILE A 290 -50.930 62.573 37.213 1.00 79.42 C ANISOU 2796 CB ILE A 290 9461 10104 10609 -96 368 -472 C ATOM 2797 CG1 ILE A 290 -52.351 62.874 36.705 1.00 80.88 C ANISOU 2797 CG1 ILE A 290 9617 10333 10780 -117 368 -496 C ATOM 2798 CG2 ILE A 290 -51.017 61.957 38.606 1.00 79.93 C ANISOU 2798 CG2 ILE A 290 9533 10197 10638 -135 366 -471 C ATOM 2799 CD1 ILE A 290 -53.118 61.654 36.237 1.00 81.84 C ANISOU 2799 CD1 ILE A 290 9777 10460 10857 -168 371 -487 C ATOM 2800 N ALA A 291 -47.811 62.961 37.165 1.00 77.48 N ANISOU 2800 N ALA A 291 9234 9787 10417 -10 367 -435 N ATOM 2801 CA ALA A 291 -46.455 62.658 37.646 1.00 77.43 C ANISOU 2801 CA ALA A 291 9239 9771 10407 14 366 -415 C ATOM 2802 C ALA A 291 -45.620 63.898 38.006 1.00 76.39 C ANISOU 2802 C ALA A 291 9060 9657 10306 33 367 -431 C ATOM 2803 O ALA A 291 -44.787 63.848 38.914 1.00 76.24 O ANISOU 2803 O ALA A 291 9030 9661 10276 39 366 -428 O ATOM 2804 CB ALA A 291 -45.721 61.816 36.609 1.00 77.90 C ANISOU 2804 CB ALA A 291 9345 9790 10463 44 367 -387 C ATOM 2805 N TYR A 292 -45.852 64.994 37.287 1.00 76.46 N ANISOU 2805 N TYR A 292 9045 9657 10349 41 371 -448 N ATOM 2806 CA TYR A 292 -45.152 66.260 37.504 1.00 75.68 C ANISOU 2806 CA TYR A 292 8911 9563 10278 50 374 -465 C ATOM 2807 C TYR A 292 -46.050 67.374 38.082 1.00 77.14 C ANISOU 2807 C TYR A 292 9064 9764 10480 36 374 -503 C ATOM 2808 O TYR A 292 -45.625 68.525 38.177 1.00 78.52 O ANISOU 2808 O TYR A 292 9220 9932 10682 40 378 -522 O ATOM 2809 CB TYR A 292 -44.480 66.670 36.188 1.00 74.92 C ANISOU 2809 CB TYR A 292 8823 9437 10206 73 377 -450 C ATOM 2810 CG TYR A 292 -43.335 65.731 35.834 1.00 73.74 C ANISOU 2810 CG TYR A 292 8694 9286 10038 93 377 -421 C ATOM 2811 CD1 TYR A 292 -42.092 65.864 36.445 1.00 73.06 C ANISOU 2811 CD1 TYR A 292 8587 9228 9943 101 378 -419 C ATOM 2812 CD2 TYR A 292 -43.503 64.694 34.921 1.00 72.46 C ANISOU 2812 CD2 TYR A 292 8569 9101 9861 108 376 -399 C ATOM 2813 CE1 TYR A 292 -41.042 65.009 36.145 1.00 72.67 C ANISOU 2813 CE1 TYR A 292 8550 9187 9870 131 377 -394 C ATOM 2814 CE2 TYR A 292 -42.458 63.828 34.616 1.00 72.41 C ANISOU 2814 CE2 TYR A 292 8583 9092 9835 137 376 -376 C ATOM 2815 CZ TYR A 292 -41.230 63.990 35.234 1.00 71.94 C ANISOU 2815 CZ TYR A 292 8501 9066 9767 153 376 -374 C ATOM 2816 OH TYR A 292 -40.186 63.143 34.944 1.00 71.03 O ANISOU 2816 OH TYR A 292 8400 8959 9627 193 375 -354 O ATOM 2817 N PHE A 293 -47.270 67.020 38.505 1.00 78.27 N ANISOU 2817 N PHE A 293 9203 9931 10604 19 371 -517 N ATOM 2818 CA PHE A 293 -48.160 67.944 39.236 1.00 78.79 C ANISOU 2818 CA PHE A 293 9234 10025 10676 12 371 -558 C ATOM 2819 C PHE A 293 -47.615 68.215 40.642 1.00 77.18 C ANISOU 2819 C PHE A 293 9005 9854 10463 -3 372 -579 C ATOM 2820 O PHE A 293 -47.937 69.243 41.246 1.00 75.30 O ANISOU 2820 O PHE A 293 8738 9631 10238 -3 374 -618 O ATOM 2821 CB PHE A 293 -49.593 67.380 39.340 1.00 80.50 C ANISOU 2821 CB PHE A 293 9445 10277 10863 -6 368 -568 C ATOM 2822 CG PHE A 293 -50.671 68.434 39.364 1.00 81.95 C ANISOU 2822 CG PHE A 293 9595 10483 11058 8 367 -607 C ATOM 2823 CD1 PHE A 293 -50.982 69.109 40.536 1.00 83.79 C ANISOU 2823 CD1 PHE A 293 9792 10754 11287 3 368 -648 C ATOM 2824 CD2 PHE A 293 -51.396 68.735 38.212 1.00 84.23 C ANISOU 2824 CD2 PHE A 293 9886 10760 11357 32 366 -604 C ATOM 2825 CE1 PHE A 293 -51.976 70.079 40.564 1.00 84.70 C ANISOU 2825 CE1 PHE A 293 9879 10892 11411 29 367 -687 C ATOM 2826 CE2 PHE A 293 -52.395 69.704 38.231 1.00 85.62 C ANISOU 2826 CE2 PHE A 293 10032 10959 11540 59 363 -639 C ATOM 2827 CZ PHE A 293 -52.685 70.378 39.411 1.00 85.56 C ANISOU 2827 CZ PHE A 293 9991 10985 11529 60 364 -682 C ATOM 2828 N ASN A 294 -46.799 67.288 41.159 1.00 75.81 N ANISOU 2828 N ASN A 294 8845 9694 10265 -14 371 -553 N ATOM 2829 CA ASN A 294 -46.142 67.455 42.460 1.00 75.63 C ANISOU 2829 CA ASN A 294 8796 9712 10228 -29 371 -568 C ATOM 2830 C ASN A 294 -45.223 68.674 42.544 1.00 76.30 C ANISOU 2830 C ASN A 294 8858 9789 10342 -22 377 -590 C ATOM 2831 O ASN A 294 -45.011 69.203 43.629 1.00 78.82 O ANISOU 2831 O ASN A 294 9147 10145 10654 -39 379 -621 O ATOM 2832 CB ASN A 294 -45.371 66.183 42.876 1.00 75.87 C ANISOU 2832 CB ASN A 294 8849 9756 10222 -30 367 -528 C ATOM 2833 CG ASN A 294 -43.964 66.111 42.290 1.00 75.20 C ANISOU 2833 CG ASN A 294 8773 9652 10145 -1 368 -503 C ATOM 2834 OD1 ASN A 294 -42.996 66.481 42.947 1.00 76.92 O ANISOU 2834 OD1 ASN A 294 8964 9902 10358 -1 369 -510 O ATOM 2835 ND2 ASN A 294 -43.846 65.622 41.063 1.00 75.50 N ANISOU 2835 ND2 ASN A 294 8845 9646 10192 20 368 -476 N ATOM 2836 N ASN A 295 -44.688 69.123 41.409 1.00 75.88 N ANISOU 2836 N ASN A 295 8820 9691 10317 -3 380 -577 N ATOM 2837 CA ASN A 295 -43.775 70.266 41.393 1.00 77.28 C ANISOU 2837 CA ASN A 295 8984 9858 10519 -9 387 -596 C ATOM 2838 C ASN A 295 -44.423 71.595 41.761 1.00 80.10 C ANISOU 2838 C ASN A 295 9329 10202 10902 -16 391 -644 C ATOM 2839 O ASN A 295 -43.714 72.518 42.155 1.00 84.67 O ANISOU 2839 O ASN A 295 9896 10779 11492 -34 398 -669 O ATOM 2840 CB ASN A 295 -43.097 70.408 40.029 1.00 77.34 C ANISOU 2840 CB ASN A 295 9013 9823 10546 6 390 -568 C ATOM 2841 CG ASN A 295 -42.327 69.164 39.624 1.00 76.90 C ANISOU 2841 CG ASN A 295 8971 9782 10465 22 386 -526 C ATOM 2842 OD1 ASN A 295 -41.668 68.518 40.443 1.00 76.23 O ANISOU 2842 OD1 ASN A 295 8873 9739 10350 21 384 -518 O ATOM 2843 ND2 ASN A 295 -42.416 68.818 38.355 1.00 76.53 N ANISOU 2843 ND2 ASN A 295 8950 9699 10427 42 386 -499 N ATOM 2844 N CYS A 296 -45.746 71.701 41.620 1.00 81.86 N ANISOU 2844 N CYS A 296 9554 10416 11130 -2 388 -659 N ATOM 2845 CA CYS A 296 -46.485 72.907 42.014 1.00 83.76 C ANISOU 2845 CA CYS A 296 9785 10647 11392 4 391 -708 C ATOM 2846 C CYS A 296 -47.224 72.779 43.352 1.00 86.80 C ANISOU 2846 C CYS A 296 10135 11093 11749 -9 389 -747 C ATOM 2847 O CYS A 296 -47.488 73.797 44.003 1.00 88.37 O ANISOU 2847 O CYS A 296 10320 11295 11960 -8 393 -796 O ATOM 2848 CB CYS A 296 -47.481 73.301 40.922 1.00 83.79 C ANISOU 2848 CB CYS A 296 9808 10611 11417 40 387 -704 C ATOM 2849 SG CYS A 296 -49.102 72.521 41.073 1.00 82.99 S ANISOU 2849 SG CYS A 296 9685 10560 11284 51 380 -712 S ATOM 2850 N LEU A 297 -47.581 71.553 43.744 1.00 87.84 N ANISOU 2850 N LEU A 297 10258 11273 11844 -23 384 -725 N ATOM 2851 CA LEU A 297 -48.322 71.320 44.990 1.00 88.10 C ANISOU 2851 CA LEU A 297 10257 11373 11843 -43 382 -756 C ATOM 2852 C LEU A 297 -47.441 70.859 46.155 1.00 87.75 C ANISOU 2852 C LEU A 297 10194 11376 11769 -75 383 -753 C ATOM 2853 O LEU A 297 -47.914 70.840 47.291 1.00 90.82 O ANISOU 2853 O LEU A 297 10551 11825 12130 -96 383 -783 O ATOM 2854 CB LEU A 297 -49.504 70.363 44.750 1.00 89.92 C ANISOU 2854 CB LEU A 297 10489 11633 12044 -48 376 -740 C ATOM 2855 CG LEU A 297 -49.370 68.830 44.846 1.00 89.95 C ANISOU 2855 CG LEU A 297 10512 11656 12008 -76 372 -692 C ATOM 2856 CD1 LEU A 297 -49.579 68.329 46.271 1.00 90.24 C ANISOU 2856 CD1 LEU A 297 10523 11763 11999 -114 370 -704 C ATOM 2857 CD2 LEU A 297 -50.351 68.129 43.907 1.00 89.61 C ANISOU 2857 CD2 LEU A 297 10490 11604 11953 -76 369 -671 C ATOM 2858 N ASN A 298 -46.178 70.504 45.899 1.00 87.19 N ANISOU 2858 N ASN A 298 10138 11288 11700 -77 383 -718 N ATOM 2859 CA ASN A 298 -45.211 70.270 46.990 1.00 85.58 C ANISOU 2859 CA ASN A 298 9911 11136 11468 -99 384 -718 C ATOM 2860 C ASN A 298 -45.098 71.470 47.946 1.00 83.76 C ANISOU 2860 C ASN A 298 9645 10935 11244 -119 391 -778 C ATOM 2861 O ASN A 298 -45.141 71.273 49.150 1.00 83.61 O ANISOU 2861 O ASN A 298 9594 10980 11191 -142 390 -797 O ATOM 2862 CB ASN A 298 -43.816 69.869 46.462 1.00 86.42 C ANISOU 2862 CB ASN A 298 10033 11229 11574 -89 384 -676 C ATOM 2863 CG ASN A 298 -43.707 68.395 46.088 1.00 87.38 C ANISOU 2863 CG ASN A 298 10185 11346 11668 -74 375 -619 C ATOM 2864 OD1 ASN A 298 -44.550 67.566 46.446 1.00 88.49 O ANISOU 2864 OD1 ASN A 298 10337 11503 11782 -83 370 -606 O ATOM 2865 ND2 ASN A 298 -42.648 68.064 45.352 1.00 88.00 N ANISOU 2865 ND2 ASN A 298 10280 11405 11750 -51 375 -585 N ATOM 2866 N PRO A 299 -44.962 72.708 47.414 1.00 83.83 N ANISOU 2866 N PRO A 299 9664 10892 11295 -111 399 -810 N ATOM 2867 CA PRO A 299 -45.056 73.926 48.238 1.00 84.00 C ANISOU 2867 CA PRO A 299 9664 10924 11327 -126 407 -876 C ATOM 2868 C PRO A 299 -46.296 74.046 49.133 1.00 84.08 C ANISOU 2868 C PRO A 299 9647 10981 11319 -125 405 -921 C ATOM 2869 O PRO A 299 -46.205 74.598 50.227 1.00 82.79 O ANISOU 2869 O PRO A 299 9453 10861 11142 -147 411 -971 O ATOM 2870 CB PRO A 299 -45.082 75.035 47.196 1.00 84.28 C ANISOU 2870 CB PRO A 299 9736 10874 11411 -107 412 -889 C ATOM 2871 CG PRO A 299 -44.215 74.513 46.123 1.00 84.01 C ANISOU 2871 CG PRO A 299 9726 10807 11384 -102 411 -832 C ATOM 2872 CD PRO A 299 -44.478 73.036 46.057 1.00 83.12 C ANISOU 2872 CD PRO A 299 9609 10730 11240 -92 401 -784 C ATOM 2873 N LEU A 300 -47.438 73.552 48.659 1.00 83.74 N ANISOU 2873 N LEU A 300 9610 10934 11272 -102 399 -907 N ATOM 2874 CA LEU A 300 -48.684 73.596 49.432 1.00 83.61 C ANISOU 2874 CA LEU A 300 9560 10975 11231 -100 397 -948 C ATOM 2875 C LEU A 300 -48.610 72.689 50.665 1.00 83.21 C ANISOU 2875 C LEU A 300 9475 11014 11127 -141 394 -941 C ATOM 2876 O LEU A 300 -49.177 73.016 51.703 1.00 81.04 O ANISOU 2876 O LEU A 300 9161 10803 10828 -154 396 -991 O ATOM 2877 CB LEU A 300 -49.896 73.232 48.559 1.00 82.87 C ANISOU 2877 CB LEU A 300 9477 10870 11139 -71 391 -932 C ATOM 2878 CG LEU A 300 -50.101 74.040 47.264 1.00 83.55 C ANISOU 2878 CG LEU A 300 9597 10873 11272 -25 391 -931 C ATOM 2879 CD1 LEU A 300 -51.294 73.506 46.480 1.00 83.45 C ANISOU 2879 CD1 LEU A 300 9586 10872 11248 -2 384 -913 C ATOM 2880 CD2 LEU A 300 -50.267 75.529 47.539 1.00 83.95 C ANISOU 2880 CD2 LEU A 300 9649 10895 11353 1 398 -995 C ATOM 2881 N PHE A 301 -47.905 71.561 50.543 1.00 85.70 N ANISOU 2881 N PHE A 301 9806 11335 11421 -157 389 -880 N ATOM 2882 CA PHE A 301 -47.650 70.667 51.681 1.00 87.31 C ANISOU 2882 CA PHE A 301 9987 11614 11571 -192 385 -862 C ATOM 2883 C PHE A 301 -46.787 71.297 52.784 1.00 89.50 C ANISOU 2883 C PHE A 301 10227 11940 11836 -214 390 -898 C ATOM 2884 O PHE A 301 -46.888 70.892 53.937 1.00 87.89 O ANISOU 2884 O PHE A 301 9991 11815 11586 -243 388 -905 O ATOM 2885 CB PHE A 301 -46.994 69.349 51.229 1.00 87.74 C ANISOU 2885 CB PHE A 301 10078 11652 11607 -192 377 -786 C ATOM 2886 CG PHE A 301 -47.951 68.346 50.633 1.00 87.57 C ANISOU 2886 CG PHE A 301 10088 11615 11570 -193 371 -749 C ATOM 2887 CD1 PHE A 301 -49.091 67.940 51.327 1.00 88.15 C ANISOU 2887 CD1 PHE A 301 10140 11748 11601 -225 369 -763 C ATOM 2888 CD2 PHE A 301 -47.681 67.755 49.399 1.00 87.70 C ANISOU 2888 CD2 PHE A 301 10153 11564 11605 -170 368 -701 C ATOM 2889 CE1 PHE A 301 -49.962 67.004 50.784 1.00 87.93 C ANISOU 2889 CE1 PHE A 301 10142 11712 11553 -239 365 -731 C ATOM 2890 CE2 PHE A 301 -48.543 66.807 48.861 1.00 87.80 C ANISOU 2890 CE2 PHE A 301 10197 11563 11598 -180 364 -671 C ATOM 2891 CZ PHE A 301 -49.687 66.436 49.551 1.00 87.81 C ANISOU 2891 CZ PHE A 301 10179 11624 11559 -217 363 -685 C ATOM 2892 N TYR A 302 -45.938 72.266 52.438 1.00 94.85 N ANISOU 2892 N TYR A 302 10911 12575 12551 -207 398 -921 N ATOM 2893 CA TYR A 302 -45.157 73.000 53.447 1.00 98.34 C ANISOU 2893 CA TYR A 302 11319 13064 12982 -235 405 -967 C ATOM 2894 C TYR A 302 -46.085 73.795 54.363 1.00100.23 C ANISOU 2894 C TYR A 302 11523 13344 13213 -245 411 -1041 C ATOM 2895 O TYR A 302 -45.895 73.786 55.579 1.00103.82 O ANISOU 2895 O TYR A 302 11936 13880 13629 -277 412 -1069 O ATOM 2896 CB TYR A 302 -44.135 73.958 52.819 1.00 99.11 C ANISOU 2896 CB TYR A 302 11434 13103 13118 -236 414 -981 C ATOM 2897 CG TYR A 302 -42.929 73.295 52.195 1.00101.37 C ANISOU 2897 CG TYR A 302 11736 13379 13400 -233 411 -919 C ATOM 2898 CD1 TYR A 302 -43.007 72.733 50.928 1.00102.27 C ANISOU 2898 CD1 TYR A 302 11891 13429 13535 -200 405 -867 C ATOM 2899 CD2 TYR A 302 -41.699 73.252 52.858 1.00103.25 C ANISOU 2899 CD2 TYR A 302 11942 13679 13606 -260 413 -918 C ATOM 2900 CE1 TYR A 302 -41.911 72.130 50.329 1.00103.29 C ANISOU 2900 CE1 TYR A 302 12032 13554 13658 -191 402 -815 C ATOM 2901 CE2 TYR A 302 -40.589 72.649 52.269 1.00104.85 C ANISOU 2901 CE2 TYR A 302 12153 13884 13799 -248 409 -864 C ATOM 2902 CZ TYR A 302 -40.703 72.087 51.002 1.00103.97 C ANISOU 2902 CZ TYR A 302 12085 13705 13711 -212 404 -814 C ATOM 2903 OH TYR A 302 -39.624 71.489 50.393 1.00104.16 O ANISOU 2903 OH TYR A 302 12116 13735 13725 -194 400 -766 O ATOM 2904 N GLY A 303 -47.072 74.475 53.770 1.00101.02 N ANISOU 2904 N GLY A 303 11641 13393 13348 -214 413 -1074 N ATOM 2905 CA GLY A 303 -48.054 75.281 54.508 1.00102.67 C ANISOU 2905 CA GLY A 303 11820 13637 13552 -208 418 -1150 C ATOM 2906 C GLY A 303 -48.569 74.569 55.743 1.00103.81 C ANISOU 2906 C GLY A 303 11913 13893 13635 -239 414 -1159 C ATOM 2907 O GLY A 303 -48.185 74.912 56.861 1.00106.16 O ANISOU 2907 O GLY A 303 12173 14254 13907 -270 419 -1201 O ATOM 2908 N PHE A 304 -49.434 73.580 55.518 1.00102.29 N ANISOU 2908 N PHE A 304 11720 13728 13417 -237 405 -1119 N ATOM 2909 CA PHE A 304 -49.802 72.564 56.518 1.00101.35 C ANISOU 2909 CA PHE A 304 11565 13709 13233 -277 399 -1100 C ATOM 2910 C PHE A 304 -50.417 73.126 57.807 1.00101.45 C ANISOU 2910 C PHE A 304 11518 13817 13210 -296 405 -1174 C ATOM 2911 O PHE A 304 -49.716 73.575 58.716 1.00100.48 O ANISOU 2911 O PHE A 304 11368 13735 13075 -320 410 -1208 O ATOM 2912 CB PHE A 304 -48.592 71.659 56.827 1.00100.28 C ANISOU 2912 CB PHE A 304 11440 13588 13072 -305 394 -1036 C ATOM 2913 CG PHE A 304 -48.935 70.193 56.912 1.00100.19 C ANISOU 2913 CG PHE A 304 11444 13610 13014 -327 384 -967 C ATOM 2914 CD1 PHE A 304 -49.144 69.443 55.751 1.00 99.79 C ANISOU 2914 CD1 PHE A 304 11445 13490 12980 -309 378 -910 C ATOM 2915 CD2 PHE A 304 -49.045 69.555 58.145 1.00100.60 C ANISOU 2915 CD2 PHE A 304 11462 13758 13001 -370 380 -959 C ATOM 2916 CE1 PHE A 304 -49.460 68.090 55.819 1.00 98.67 C ANISOU 2916 CE1 PHE A 304 11328 13367 12793 -335 370 -849 C ATOM 2917 CE2 PHE A 304 -49.360 68.201 58.219 1.00101.30 C ANISOU 2917 CE2 PHE A 304 11578 13867 13045 -396 371 -892 C ATOM 2918 CZ PHE A 304 -49.566 67.468 57.055 1.00 99.98 C ANISOU 2918 CZ PHE A 304 11469 13622 12896 -379 366 -838 C TER 2919 PHE A 304 HETATM 2920 C4 OLM A1201 -38.457 63.365 29.082 1.00 75.53 C HETATM 2921 C3 OLM A1201 -39.090 64.377 28.362 1.00 76.86 C HETATM 2922 O3 OLM A1201 -46.837 65.303 26.157 1.00 83.69 O HETATM 2923 C2 OLM A1201 -40.480 64.412 28.223 1.00 78.75 C HETATM 2924 O2 OLM A1201 -42.661 63.038 25.258 1.00 86.70 O HETATM 2925 C1 OLM A1201 -40.992 65.501 27.482 1.00 82.24 C HETATM 2926 O1 OLM A1201 -41.944 64.919 24.460 1.00 84.34 O HETATM 2927 C20 OLM A1201 -42.758 66.654 31.824 1.00 80.61 C HETATM 2928 C19 OLM A1201 -42.366 66.102 30.471 1.00 81.31 C HETATM 2929 C18 OLM A1201 -43.248 66.847 29.497 1.00 82.00 C HETATM 2930 C15 OLM A1201 -43.398 66.051 28.173 1.00 83.08 C HETATM 2931 N6 OLM A1201 -44.607 65.823 27.667 1.00 83.66 N HETATM 2932 C16 OLM A1201 -44.446 65.136 26.546 1.00 83.19 C HETATM 2933 C22 OLM A1201 -45.637 64.676 25.668 1.00 83.54 C HETATM 2934 C23 OLM A1201 -45.441 65.138 24.215 1.00 81.77 C HETATM 2935 C24 OLM A1201 -45.801 63.138 25.749 1.00 82.94 C HETATM 2936 C17 OLM A1201 -43.136 64.940 26.359 1.00 84.36 C HETATM 2937 C21 OLM A1201 -42.571 64.284 25.337 1.00 85.70 C HETATM 2938 N1 OLM A1201 -42.461 65.501 27.376 1.00 83.85 N HETATM 2939 C7 OLM A1201 -41.235 63.386 28.813 1.00 78.13 C HETATM 2940 C6 OLM A1201 -40.598 62.367 29.534 1.00 76.82 C HETATM 2941 C5 OLM A1201 -39.204 62.344 29.672 1.00 74.92 C HETATM 2942 C8 OLM A1201 -38.569 61.328 30.405 1.00 74.15 C HETATM 2943 C9 OLM A1201 -38.978 61.134 31.733 1.00 72.93 C HETATM 2944 C10 OLM A1201 -38.395 60.151 32.530 1.00 70.74 C HETATM 2945 C11 OLM A1201 -37.384 59.349 32.008 1.00 72.84 C HETATM 2946 C12 OLM A1201 -36.959 59.530 30.691 1.00 74.04 C HETATM 2947 C13 OLM A1201 -37.543 60.510 29.881 1.00 74.05 C HETATM 2948 C14 OLM A1201 -37.093 60.646 28.632 1.00 74.27 C HETATM 2949 N5 OLM A1201 -37.752 60.367 27.521 1.00 74.18 N HETATM 2950 N4 OLM A1201 -37.002 60.651 26.635 1.00 74.62 N HETATM 2951 N3 OLM A1201 -35.872 61.115 27.122 1.00 74.33 N HETATM 2952 N2 OLM A1201 -35.908 61.125 28.297 1.00 74.01 N CONECT 871 2680 CONECT 1519 2070 CONECT 2070 1519 CONECT 2680 871 CONECT 2920 2921 2941 CONECT 2921 2920 2923 CONECT 2922 2933 CONECT 2923 2921 2925 2939 CONECT 2924 2937 CONECT 2925 2923 2938 CONECT 2926 2937 CONECT 2927 2928 CONECT 2928 2927 2929 CONECT 2929 2928 2930 CONECT 2930 2929 2931 2938 CONECT 2931 2930 2932 CONECT 2932 2931 2933 2936 CONECT 2933 2922 2932 2934 2935 CONECT 2934 2933 CONECT 2935 2933 CONECT 2936 2932 2937 2938 CONECT 2937 2924 2926 2936 CONECT 2938 2925 2930 2936 CONECT 2939 2923 2940 CONECT 2940 2939 2941 CONECT 2941 2920 2940 2942 CONECT 2942 2941 2943 2947 CONECT 2943 2942 2944 CONECT 2944 2943 2945 CONECT 2945 2944 2946 CONECT 2946 2945 2947 CONECT 2947 2942 2946 2948 CONECT 2948 2947 2949 2952 CONECT 2949 2948 2950 CONECT 2950 2949 2951 CONECT 2951 2950 2952 CONECT 2952 2948 2951 MASTER 378 0 1 17 3 0 2 6 2951 1 37 32 END