HEADER OXYGEN TRANSPORT 24-MAY-07 2V1I TITLE CRYSTAL STRUCTURE OF RADIATION-INDUCED METMYOGLOBIN- AQUA TITLE 2 FERROUS MYOGLOBIN AT PH 6.8 COMPND MOL_ID: 1; COMPND 2 MOLECULE: MYOGLOBIN; COMPND 3 CHAIN: A; COMPND 4 OTHER_DETAILS: FE(II)-OH2 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: EQUUS CABALLUS; SOURCE 3 ORGANISM_COMMON: HORSE; SOURCE 4 ORGAN: HEART KEYWDS OXYGEN TRANSPORT, OXYGEN ACTIVATION, MONOOXYGENASE, METAL- KEYWDS 2 BINDING, MUSCLE PROTEIN, REACTION INTERMEDIATE, HAEM, IRON, KEYWDS 3 HEME, TRANSPORT, RADIATION EXPDTA X-RAY DIFFRACTION AUTHOR H.-P.HERSLETH,C.H.GORBITZ,K.K.ANDERSSON REVDAT 1 12-JUN-07 2V1I 0 JRNL AUTH H.-P.HERSLETH,T.UCHIDA,A.K.ROHR,T.TESCHNER, JRNL AUTH 2 V.SCHUNEMANN,T.KITAGAWA,A.X.TRAUTWEIN,C.H.GORBITZ, JRNL AUTH 3 K.K.ANDERSSON JRNL TITL CRYSTALLOGRAPHIC AND SPECTROSCOPICAL STUDIES OF JRNL TITL 2 PEROXIDE-DERIVED MYOGLOBIN COMPOUND II. OCCURRENCE JRNL TITL 3 OF PROTONATED FE(IV)O JRNL REF TO BE PUBLISHED JRNL REFN REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0019 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 21.95 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 94.3 REMARK 3 NUMBER OF REFLECTIONS : 34337 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) : 0.139 REMARK 3 R VALUE (WORKING SET) : 0.137 REMARK 3 FREE R VALUE : 0.168 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1825 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH : NULL REMARK 3 BIN RESOLUTION RANGE LOW : NULL REMARK 3 REFLECTION IN BIN (WORKING SET) : 2428 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.3640 REMARK 3 BIN FREE R VALUE SET COUNT : 112 REMARK 3 BIN FREE R VALUE : 0.4540 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 1550 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.51 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.14000 REMARK 3 B22 (A**2) : 0.34000 REMARK 3 B33 (A**2) : -0.14000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.11000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.047 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.044 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.978 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.968 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1386 ; 0.054 ; 0.054 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1853 ; 0.961 ; 2.019 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 173 ; 4.207 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 54 ;35.392 ;25.185 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 254 ;10.551 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 2 ;16.994 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 195 ; 0.082 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 997 ; 0.004 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 755 ; 0.235 ; 0.300 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 926 ; 0.321 ; 0.500 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 310 ; 0.199 ; 0.500 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): 88 ; 0.264 ; 0.300 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 79 ; 0.229 ; 0.500 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): 789 ; 1.534 ; 2.000 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1267 ; 2.168 ; 3.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 585 ; 2.030 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 575 ; 2.870 ; 3.000 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 : 0 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 0 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE REMARK 3 RIDING POSITIONS. REMARK 4 REMARK 4 2V1I COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.101 (2007-06-08) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI. REMARK 100 THE EBI ID CODE IS EBI-32659. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-APR-2001 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 6.80 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID14-3 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9312 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36225 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200 REMARK 200 RESOLUTION RANGE LOW (A) : 22.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0 REMARK 200 DATA REDUNDANCY : 2.700 REMARK 200 R MERGE (I) : 0.05000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 16.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.23 REMARK 200 COMPLETENESS FOR SHELL (%) : 86.6 REMARK 200 DATA REDUNDANCY IN SHELL : 2.00 REMARK 200 R MERGE FOR SHELL (I) : 0.34000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: PDB ENTRY 1GJN REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 31.94 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.41 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: BATCH METHOD: 6-12 MG/ML MYOGLOBIN, REMARK 280 80-85% OF THE CRYSTALLIZATION STOCK-SOLUTION (3.9 M AMMONIUM REMARK 280 SULPHATE, 0.1 M MOPS AND 5-10% OF GLYCEROL PH 6.8) REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,1/2+Y,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 14.38100 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 APPLY THE FOLLOWING TO CHAINS: A, Z 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 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI REMARK 500 OG1 THR A 51 O HOH Z 88 2.12 REMARK 500 O HOH Z 194 O HOH Z 195 2.13 REMARK 500 NZ LYS A 78 O HOH Z 111 2.14 REMARK 500 O HOH Z 172 O HOH Z 176 2.18 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH Z 132 O HOH Z 194 2645 2.09 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 GLY A 1 N GLY A 1 CA 0.040 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 PHE A 123 N - CA - C ANGL. DEV. = -6.5 DEGREES REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN A DBREF 2V1I A 1 153 UNP P68082 MYG_HORSE 1 153 SEQRES 1 A 153 GLY LEU SER ASP GLY GLU TRP GLN GLN VAL LEU ASN VAL SEQRES 2 A 153 TRP GLY LYS VAL GLU ALA ASP ILE ALA GLY HIS GLY GLN SEQRES 3 A 153 GLU VAL LEU ILE ARG LEU PHE THR GLY HIS PRO GLU THR SEQRES 4 A 153 LEU GLU LYS PHE ASP LYS PHE LYS HIS LEU LYS THR GLU SEQRES 5 A 153 ALA GLU MET LYS ALA SER GLU ASP LEU LYS LYS HIS GLY SEQRES 6 A 153 THR VAL VAL LEU THR ALA LEU GLY GLY ILE LEU LYS LYS SEQRES 7 A 153 LYS GLY HIS HIS GLU ALA GLU LEU LYS PRO LEU ALA GLN SEQRES 8 A 153 SER HIS ALA THR LYS HIS LYS ILE PRO ILE LYS TYR LEU SEQRES 9 A 153 GLU PHE ILE SER ASP ALA ILE ILE HIS VAL LEU HIS SER SEQRES 10 A 153 LYS HIS PRO GLY ASP PHE GLY ALA ASP ALA GLN GLY ALA SEQRES 11 A 153 MET THR LYS ALA LEU GLU LEU PHE ARG ASN ASP ILE ALA SEQRES 12 A 153 ALA LYS TYR LYS GLU LEU GLY PHE GLN GLY HET SO4 A1156 5 HET SO4 A1157 5 HET HEM A1154 43 HET GOL A1158 6 HET GOL A1159 6 HET GOL A1160 6 HET GOL A1161 6 HETNAM SO4 SULFATE ION HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETNAM GOL GLYCEROL HETSYN HEM HEME FORMUL 2 SO4 2(O4 S 2-) FORMUL 4 HEM C34 H32 FE N4 O4 FORMUL 5 GOL 4(C3 H8 O3) FORMUL 9 HOH *219(H2 O) HELIX 1 1 SER A 3 ASP A 20 1 18 HELIX 2 2 ASP A 20 HIS A 36 1 17 HELIX 3 3 PRO A 37 PHE A 43 5 7 HELIX 4 4 THR A 51 SER A 58 1 8 HELIX 5 5 SER A 58 LYS A 78 1 21 HELIX 6 6 HIS A 82 LYS A 96 1 15 HELIX 7 7 PRO A 100 HIS A 119 1 20 HELIX 8 8 GLY A 124 GLY A 150 1 27 LINK FE HEM A1154 O HOH A1155 LINK FE HEM A1154 NE2 HIS A 93 SITE 1 AC1 22 THR A 39 LYS A 42 PHE A 43 LYS A 45 SITE 2 AC1 22 HIS A 64 LEU A 89 SER A 92 HIS A 93 SITE 3 AC1 22 HIS A 97 ILE A 99 TYR A 103 LEU A 104 SITE 4 AC1 22 HIS A 113 HIS A 116 GLN A 128 HOH A1155 SITE 5 AC1 22 HOH Z 201 HOH Z 202 HOH Z 203 HOH Z 204 SITE 6 AC1 22 HOH Z 205 HOH Z 214 SITE 1 AC2 4 THR A 51 GLU A 52 HOH Z 88 HOH Z 207 SITE 1 AC3 4 GLY A 1 HOH Z 208 HOH Z 209 HOH Z 210 SITE 1 AC4 8 LYS A 45 LYS A 63 HIS A 64 HIS A 116 SITE 2 AC4 8 SER A 117 HOH Z 152 HOH Z 202 HOH Z 211 SITE 1 AC5 10 ARG A 31 LYS A 45 ASP A 60 HIS A 113 SITE 2 AC5 10 SER A 117 HOH Z 54 HOH Z 98 HOH Z 212 SITE 3 AC5 10 HOH Z 213 HOH Z 214 SITE 1 AC6 5 SER A 3 ASP A 4 GLY A 5 LYS A 98 SITE 2 AC6 5 HOH Z 216 SITE 1 AC7 9 ARG A 31 HIS A 36 LYS A 96 ASP A 109 SITE 2 AC7 9 ALA A 110 HOH Z 148 HOH Z 217 HOH Z 218 SITE 3 AC7 9 HOH Z 219 CRYST1 62.872 28.762 35.347 90.00 106.13 90.00 P 1 21 1 2 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.015905 0.000000 0.004600 0.00000 SCALE2 0.000000 0.034768 0.000000 0.00000 SCALE3 0.000000 0.000000 0.029450 0.00000 ATOM 1 N GLY A 1 27.084 -18.058 14.523 1.00 19.78 N ANISOU 1 N GLY A 1 1790 2862 2861 124 -239 -24 N ATOM 2 CA GLY A 1 25.700 -18.572 14.730 1.00 16.13 C ANISOU 2 CA GLY A 1 1408 2364 2357 306 -348 -29 C ATOM 3 C GLY A 1 24.679 -17.456 14.825 1.00 15.61 C ANISOU 3 C GLY A 1 1599 2038 2292 162 -223 21 C ATOM 4 O GLY A 1 25.014 -16.278 14.707 1.00 17.10 O ANISOU 4 O GLY A 1 1673 2133 2690 72 -65 129 O ATOM 5 N LEU A 2 23.425 -17.830 15.036 1.00 12.38 N ANISOU 5 N LEU A 2 1245 1732 1728 192 -242 -35 N ATOM 6 CA LEU A 2 22.360 -16.854 15.233 1.00 10.48 C ANISOU 6 CA LEU A 2 1024 1465 1492 5 -254 -28 C ATOM 7 C LEU A 2 22.093 -16.684 16.719 1.00 10.56 C ANISOU 7 C LEU A 2 1139 1424 1447 40 -187 -7 C ATOM 8 O LEU A 2 22.233 -17.632 17.498 1.00 12.44 O ANISOU 8 O LEU A 2 1697 1622 1406 -5 -503 188 O ATOM 9 CB LEU A 2 21.077 -17.324 14.558 1.00 10.67 C ANISOU 9 CB LEU A 2 1214 1543 1297 -77 -187 2 C ATOM 10 CG LEU A 2 20.977 -17.151 13.044 1.00 9.45 C ANISOU 10 CG LEU A 2 1082 1423 1087 -26 -245 151 C ATOM 11 CD1 LEU A 2 21.932 -18.078 12.304 1.00 10.53 C ANISOU 11 CD1 LEU A 2 1346 1345 1310 -80 -72 141 C ATOM 12 CD2 LEU A 2 19.546 -17.396 12.612 1.00 10.27 C ANISOU 12 CD2 LEU A 2 1110 1515 1275 -189 -130 81 C ATOM 13 N SER A 3 21.705 -15.478 17.111 1.00 10.02 N ANISOU 13 N SER A 3 1106 1474 1225 -188 -320 130 N ATOM 14 CA SER A 3 21.288 -15.232 18.482 1.00 11.44 C ANISOU 14 CA SER A 3 1484 1506 1356 -237 -262 31 C ATOM 15 C SER A 3 19.916 -15.857 18.711 1.00 10.61 C ANISOU 15 C SER A 3 1258 1679 1094 -167 -210 121 C ATOM 16 O SER A 3 19.200 -16.204 17.762 1.00 10.20 O ANISOU 16 O SER A 3 1205 1433 1236 -196 -291 103 O ATOM 17 CB SER A 3 21.199 -13.730 18.736 1.00 11.64 C ANISOU 17 CB SER A 3 1513 1458 1450 -207 -352 -23 C ATOM 18 OG SER A 3 20.123 -13.182 17.989 1.00 11.41 O ANISOU 18 OG SER A 3 1438 1520 1377 -259 -294 85 O ATOM 19 N ASP A 4 19.537 -15.984 19.977 1.00 12.44 N ANISOU 19 N ASP A 4 1615 1993 1119 -316 -140 257 N ATOM 20 CA ASP A 4 18.204 -16.453 20.308 1.00 12.58 C ANISOU 20 CA ASP A 4 1601 2145 1032 -257 -1 314 C ATOM 21 C ASP A 4 17.142 -15.560 19.652 1.00 11.88 C ANISOU 21 C ASP A 4 1509 1889 1115 -240 54 50 C ATOM 22 O ASP A 4 16.153 -16.058 19.108 1.00 11.22 O ANISOU 22 O ASP A 4 1339 1881 1041 -231 150 32 O ATOM 23 CB ASP A 4 18.019 -16.523 21.829 1.00 17.14 C ANISOU 23 CB ASP A 4 2072 3067 1373 -223 73 376 C ATOM 24 CG ASP A 4 18.844 -17.635 22.467 1.00 19.84 C ANISOU 24 CG ASP A 4 2481 3336 1720 -275 -64 438 C ATOM 25 OD1 ASP A 4 18.990 -18.705 21.836 1.00 21.20 O ANISOU 25 OD1 ASP A 4 2489 3189 2374 -37 -180 669 O ATOM 26 OD2 ASP A 4 19.337 -17.444 23.599 1.00 24.01 O ANISOU 26 OD2 ASP A 4 2821 4024 2278 -489 -83 407 O ATOM 27 N GLY A 5 17.360 -14.245 19.674 1.00 12.13 N ANISOU 27 N GLY A 5 1517 1966 1123 -237 120 -162 N ATOM 28 CA GLY A 5 16.427 -13.309 19.045 1.00 11.77 C ANISOU 28 CA GLY A 5 1416 1717 1338 -126 89 -424 C ATOM 29 C GLY A 5 16.307 -13.533 17.545 1.00 9.94 C ANISOU 29 C GLY A 5 1226 1268 1282 -170 139 -302 C ATOM 30 O GLY A 5 15.209 -13.501 16.976 1.00 10.22 O ANISOU 30 O GLY A 5 1112 1385 1386 -38 216 -212 O ATOM 31 N GLU A 6 17.442 -13.759 16.898 1.00 9.28 N ANISOU 31 N GLU A 6 1265 1131 1127 -126 85 -88 N ATOM 32 CA GLU A 6 17.446 -14.054 15.474 1.00 8.48 C ANISOU 32 CA GLU A 6 972 1073 1174 -104 101 -88 C ATOM 33 C GLU A 6 16.696 -15.345 15.156 1.00 7.51 C ANISOU 33 C GLU A 6 806 1014 1031 -13 50 20 C ATOM 34 O GLU A 6 15.890 -15.385 14.224 1.00 7.56 O ANISOU 34 O GLU A 6 727 1124 1020 -86 30 53 O ATOM 35 CB GLU A 6 18.878 -14.053 14.930 1.00 8.70 C ANISOU 35 CB GLU A 6 1022 1151 1130 -148 -33 109 C ATOM 36 CG GLU A 6 19.453 -12.641 14.858 1.00 9.87 C ANISOU 36 CG GLU A 6 1124 1193 1431 -311 -119 -24 C ATOM 37 CD GLU A 6 20.947 -12.595 14.619 1.00 9.47 C ANISOU 37 CD GLU A 6 1045 1235 1318 -226 -277 149 C ATOM 38 OE1 GLU A 6 21.644 -13.601 14.893 1.00 10.16 O ANISOU 38 OE1 GLU A 6 1075 1311 1473 -210 -116 152 O ATOM 39 OE2 GLU A 6 21.422 -11.533 14.166 1.00 10.95 O ANISOU 39 OE2 GLU A 6 1214 1288 1656 -298 -182 264 O ATOM 40 N TRP A 7 16.943 -16.404 15.927 1.00 7.94 N ANISOU 40 N TRP A 7 898 1007 1109 41 -19 15 N ATOM 41 CA TRP A 7 16.192 -17.637 15.707 1.00 7.80 C ANISOU 41 CA TRP A 7 976 902 1083 12 9 -45 C ATOM 42 C TRP A 7 14.691 -17.417 15.853 1.00 8.27 C ANISOU 42 C TRP A 7 1062 1002 1075 87 36 46 C ATOM 43 O TRP A 7 13.907 -17.963 15.088 1.00 7.70 O ANISOU 43 O TRP A 7 868 1040 1018 -65 28 -81 O ATOM 44 CB TRP A 7 16.659 -18.770 16.624 1.00 8.63 C ANISOU 44 CB TRP A 7 1190 952 1136 55 -10 113 C ATOM 45 CG TRP A 7 17.923 -19.432 16.163 1.00 8.38 C ANISOU 45 CG TRP A 7 1018 933 1233 51 61 49 C ATOM 46 CD1 TRP A 7 19.096 -19.523 16.852 1.00 8.58 C ANISOU 46 CD1 TRP A 7 1083 972 1204 -17 -40 132 C ATOM 47 CD2 TRP A 7 18.139 -20.107 14.913 1.00 8.47 C ANISOU 47 CD2 TRP A 7 1042 864 1313 113 -132 129 C ATOM 48 NE1 TRP A 7 20.032 -20.204 16.106 1.00 9.40 N ANISOU 48 NE1 TRP A 7 1123 989 1457 36 -86 130 N ATOM 49 CE2 TRP A 7 19.468 -20.577 14.915 1.00 8.77 C ANISOU 49 CE2 TRP A 7 1058 856 1417 145 -171 49 C ATOM 50 CE3 TRP A 7 17.334 -20.367 13.797 1.00 8.89 C ANISOU 50 CE3 TRP A 7 1122 1000 1255 170 17 41 C ATOM 51 CZ2 TRP A 7 20.017 -21.271 13.838 1.00 9.98 C ANISOU 51 CZ2 TRP A 7 1114 1094 1583 154 -73 -32 C ATOM 52 CZ3 TRP A 7 17.880 -21.061 12.727 1.00 9.47 C ANISOU 52 CZ3 TRP A 7 1135 1019 1441 144 -22 -102 C ATOM 53 CH2 TRP A 7 19.208 -21.507 12.757 1.00 9.60 C ANISOU 53 CH2 TRP A 7 1052 991 1602 214 -89 -233 C ATOM 54 N GLN A 8 14.283 -16.618 16.832 1.00 8.26 N ANISOU 54 N GLN A 8 951 1081 1106 12 88 31 N ATOM 55 CA GLN A 8 12.861 -16.358 17.018 1.00 9.46 C ANISOU 55 CA GLN A 8 1017 1335 1242 40 51 -69 C ATOM 56 C GLN A 8 12.289 -15.664 15.783 1.00 7.84 C ANISOU 56 C GLN A 8 950 906 1121 98 104 -56 C ATOM 57 O GLN A 8 11.189 -15.979 15.326 1.00 8.62 O ANISOU 57 O GLN A 8 885 1163 1226 -15 80 -32 O ATOM 58 CB GLN A 8 12.616 -15.521 18.274 1.00 10.83 C ANISOU 58 CB GLN A 8 1237 1596 1280 21 196 -341 C ATOM 59 CG GLN A 8 11.148 -15.391 18.616 1.00 12.34 C ANISOU 59 CG GLN A 8 1306 1841 1541 -140 198 -465 C ATOM 60 CD GLN A 8 10.920 -14.622 19.889 1.00 14.94 C ANISOU 60 CD GLN A 8 1739 2109 1826 -300 161 -707 C ATOM 61 OE1 GLN A 8 11.580 -13.616 20.148 1.00 17.01 O ANISOU 61 OE1 GLN A 8 1947 2311 2205 -451 297 -770 O ATOM 62 NE2 GLN A 8 9.975 -15.086 20.694 1.00 16.89 N ANISOU 62 NE2 GLN A 8 1942 2435 2040 -307 349 -493 N ATOM 63 N GLN A 9 13.041 -14.722 15.225 1.00 8.43 N ANISOU 63 N GLN A 9 921 957 1324 45 4 22 N ATOM 64 CA GLN A 9 12.611 -14.071 13.991 1.00 9.13 C ANISOU 64 CA GLN A 9 1065 990 1411 -9 -56 45 C ATOM 65 C GLN A 9 12.494 -15.063 12.829 1.00 7.62 C ANISOU 65 C GLN A 9 856 851 1186 22 14 204 C ATOM 66 O GLN A 9 11.519 -15.043 12.081 1.00 9.01 O ANISOU 66 O GLN A 9 1027 1150 1243 73 -97 87 O ATOM 67 CB GLN A 9 13.568 -12.936 13.623 1.00 11.58 C ANISOU 67 CB GLN A 9 1524 1212 1661 -110 -49 109 C ATOM 68 CG GLN A 9 13.428 -11.697 14.492 1.00 17.13 C ANISOU 68 CG GLN A 9 2269 1962 2279 16 -93 -149 C ATOM 69 CD GLN A 9 12.089 -11.008 14.301 1.00 22.19 C ANISOU 69 CD GLN A 9 2760 2679 2992 250 -105 -264 C ATOM 70 OE1 GLN A 9 11.342 -10.802 15.259 1.00 25.93 O ANISOU 70 OE1 GLN A 9 3014 3345 3491 286 77 -467 O ATOM 71 NE2 GLN A 9 11.773 -10.656 13.058 1.00 23.40 N ANISOU 71 NE2 GLN A 9 2823 3013 3053 163 -237 -92 N ATOM 72 N VAL A 10 13.486 -15.932 12.684 1.00 7.85 N ANISOU 72 N VAL A 10 958 956 1069 -60 63 22 N ATOM 73 CA VAL A 10 13.460 -16.949 11.638 1.00 7.71 C ANISOU 73 CA VAL A 10 888 918 1122 27 58 -36 C ATOM 74 C VAL A 10 12.200 -17.801 11.729 1.00 7.07 C ANISOU 74 C VAL A 10 746 943 994 41 -3 -62 C ATOM 75 O VAL A 10 11.501 -18.022 10.742 1.00 7.79 O ANISOU 75 O VAL A 10 756 1122 1081 76 -18 -39 O ATOM 76 CB VAL A 10 14.701 -17.868 11.708 1.00 7.36 C ANISOU 76 CB VAL A 10 801 963 1032 119 138 -9 C ATOM 77 CG1 VAL A 10 14.539 -19.058 10.758 1.00 8.93 C ANISOU 77 CG1 VAL A 10 887 1249 1256 174 172 -69 C ATOM 78 CG2 VAL A 10 15.965 -17.082 11.376 1.00 8.81 C ANISOU 78 CG2 VAL A 10 814 1333 1198 -24 238 5 C ATOM 79 N LEU A 11 11.896 -18.277 12.930 1.00 7.33 N ANISOU 79 N LEU A 11 770 925 1088 -58 112 -103 N ATOM 80 CA LEU A 11 10.772 -19.184 13.087 1.00 7.87 C ANISOU 80 CA LEU A 11 936 801 1252 6 13 60 C ATOM 81 C LEU A 11 9.430 -18.461 13.025 1.00 7.65 C ANISOU 81 C LEU A 11 779 960 1166 -39 258 0 C ATOM 82 O LEU A 11 8.416 -19.057 12.667 1.00 9.39 O ANISOU 82 O LEU A 11 743 1126 1696 -117 118 -89 O ATOM 83 CB LEU A 11 10.942 -20.043 14.340 1.00 8.97 C ANISOU 83 CB LEU A 11 1210 990 1206 62 116 81 C ATOM 84 CG LEU A 11 12.181 -20.946 14.271 1.00 9.59 C ANISOU 84 CG LEU A 11 1417 1109 1117 87 136 108 C ATOM 85 CD1 LEU A 11 12.250 -21.806 15.515 1.00 11.78 C ANISOU 85 CD1 LEU A 11 1845 1348 1281 310 47 321 C ATOM 86 CD2 LEU A 11 12.166 -21.832 13.025 1.00 11.24 C ANISOU 86 CD2 LEU A 11 1636 1305 1327 227 146 143 C ATOM 87 N ASN A 12 9.435 -17.162 13.303 1.00 8.19 N ANISOU 87 N ASN A 12 816 1054 1243 97 146 -56 N ATOM 88 CA ASN A 12 8.245 -16.361 13.085 1.00 9.54 C ANISOU 88 CA ASN A 12 1154 1064 1404 183 26 -227 C ATOM 89 C ASN A 12 7.964 -16.205 11.587 1.00 9.00 C ANISOU 89 C ASN A 12 935 992 1489 235 -87 -72 C ATOM 90 O ASN A 12 6.841 -16.398 11.132 1.00 9.87 O ANISOU 90 O ASN A 12 889 1311 1548 189 -176 -106 O ATOM 91 CB ASN A 12 8.404 -14.994 13.735 1.00 11.76 C ANISOU 91 CB ASN A 12 1244 1307 1915 259 -69 -325 C ATOM 92 CG ASN A 12 7.139 -14.186 13.665 1.00 16.07 C ANISOU 92 CG ASN A 12 1645 1865 2593 386 83 -431 C ATOM 93 OD1 ASN A 12 6.133 -14.540 14.276 1.00 20.64 O ANISOU 93 OD1 ASN A 12 1959 2663 3220 470 208 -437 O ATOM 94 ND2 ASN A 12 7.173 -13.103 12.906 1.00 18.76 N ANISOU 94 ND2 ASN A 12 2048 2025 3054 706 -51 -181 N ATOM 95 N VAL A 13 8.991 -15.858 10.819 1.00 9.22 N ANISOU 95 N VAL A 13 1191 1021 1290 9 -182 194 N ATOM 96 CA VAL A 13 8.872 -15.808 9.364 1.00 10.31 C ANISOU 96 CA VAL A 13 1273 1248 1395 -112 -222 336 C ATOM 97 C VAL A 13 8.402 -17.162 8.833 1.00 9.08 C ANISOU 97 C VAL A 13 875 1363 1211 -30 -162 149 C ATOM 98 O VAL A 13 7.543 -17.237 7.948 1.00 10.31 O ANISOU 98 O VAL A 13 1038 1672 1207 -233 -196 282 O ATOM 99 CB VAL A 13 10.218 -15.424 8.704 1.00 11.54 C ANISOU 99 CB VAL A 13 1502 1525 1355 -307 -267 251 C ATOM 100 CG1 VAL A 13 10.161 -15.604 7.192 1.00 13.14 C ANISOU 100 CG1 VAL A 13 1683 1979 1331 -434 -200 381 C ATOM 101 CG2 VAL A 13 10.609 -13.986 9.069 1.00 12.89 C ANISOU 101 CG2 VAL A 13 1635 1458 1801 -379 -231 315 C ATOM 102 N TRP A 14 8.948 -18.240 9.386 1.00 9.08 N ANISOU 102 N TRP A 14 1047 1217 1184 -32 -93 61 N ATOM 103 CA TRP A 14 8.617 -19.566 8.888 1.00 9.36 C ANISOU 103 CA TRP A 14 1060 1228 1266 11 -47 -140 C ATOM 104 C TRP A 14 7.132 -19.892 9.036 1.00 9.05 C ANISOU 104 C TRP A 14 1073 1140 1224 25 55 -127 C ATOM 105 O TRP A 14 6.573 -20.659 8.252 1.00 9.03 O ANISOU 105 O TRP A 14 945 1178 1306 109 -221 -354 O ATOM 106 CB TRP A 14 9.487 -20.641 9.539 1.00 10.48 C ANISOU 106 CB TRP A 14 1092 1464 1423 319 -134 -197 C ATOM 107 CG TRP A 14 9.447 -21.908 8.761 1.00 11.20 C ANISOU 107 CG TRP A 14 1004 1588 1662 324 -326 -244 C ATOM 108 CD1 TRP A 14 8.794 -23.055 9.099 1.00 12.56 C ANISOU 108 CD1 TRP A 14 1333 1510 1929 385 -323 -244 C ATOM 109 CD2 TRP A 14 10.031 -22.139 7.476 1.00 12.68 C ANISOU 109 CD2 TRP A 14 1107 1919 1788 418 -362 -347 C ATOM 110 NE1 TRP A 14 8.955 -24.000 8.113 1.00 14.01 N ANISOU 110 NE1 TRP A 14 1362 1791 2167 386 -538 -481 N ATOM 111 CE2 TRP A 14 9.707 -23.461 7.103 1.00 12.33 C ANISOU 111 CE2 TRP A 14 1099 1815 1770 571 -497 -577 C ATOM 112 CE3 TRP A 14 10.802 -21.361 6.607 1.00 12.42 C ANISOU 112 CE3 TRP A 14 1027 2225 1464 498 -256 -416 C ATOM 113 CZ2 TRP A 14 10.133 -24.023 5.902 1.00 14.58 C ANISOU 113 CZ2 TRP A 14 1224 2303 2011 705 -498 -698 C ATOM 114 CZ3 TRP A 14 11.228 -21.926 5.411 1.00 14.40 C ANISOU 114 CZ3 TRP A 14 1046 2683 1741 518 -288 -561 C ATOM 115 CH2 TRP A 14 10.886 -23.240 5.072 1.00 14.56 C ANISOU 115 CH2 TRP A 14 1062 2691 1778 632 -338 -797 C ATOM 116 N GLY A 15 6.480 -19.293 10.026 1.00 9.55 N ANISOU 116 N GLY A 15 1067 1257 1304 -72 170 -209 N ATOM 117 CA GLY A 15 5.032 -19.450 10.173 1.00 10.64 C ANISOU 117 CA GLY A 15 1099 1330 1612 -126 259 -236 C ATOM 118 C GLY A 15 4.271 -19.035 8.924 1.00 10.55 C ANISOU 118 C GLY A 15 1175 1047 1786 -15 187 -152 C ATOM 119 O GLY A 15 3.223 -19.605 8.610 1.00 11.40 O ANISOU 119 O GLY A 15 1035 1394 1901 -56 292 -111 O ATOM 120 N LYS A 16 4.787 -18.037 8.208 1.00 10.86 N ANISOU 120 N LYS A 16 1215 981 1930 23 179 -95 N ATOM 121 CA LYS A 16 4.168 -17.603 6.955 1.00 12.03 C ANISOU 121 CA LYS A 16 1279 1191 2099 -22 76 192 C ATOM 122 C LYS A 16 4.221 -18.725 5.935 1.00 10.62 C ANISOU 122 C LYS A 16 1050 1296 1686 114 20 296 C ATOM 123 O LYS A 16 3.236 -19.017 5.248 1.00 11.43 O ANISOU 123 O LYS A 16 963 1628 1750 169 80 257 O ATOM 124 CB LYS A 16 4.909 -16.400 6.378 1.00 14.12 C ANISOU 124 CB LYS A 16 1487 1285 2590 -228 0 368 C ATOM 125 CG LYS A 16 4.922 -15.188 7.268 1.00 17.81 C ANISOU 125 CG LYS A 16 2091 1431 3243 -141 -9 224 C ATOM 126 CD LYS A 16 5.760 -14.095 6.624 1.00 19.18 C ANISOU 126 CD LYS A 16 2204 1502 3580 -352 -329 406 C ATOM 127 CE LYS A 16 6.103 -13.000 7.612 1.00 22.90 C ANISOU 127 CE LYS A 16 2818 1869 4013 -109 -494 157 C ATOM 128 NZ LYS A 16 4.873 -12.369 8.144 1.00 23.72 N ANISOU 128 NZ LYS A 16 2763 1749 4498 57 -652 -168 N ATOM 129 N VAL A 17 5.389 -19.349 5.832 1.00 9.37 N ANISOU 129 N VAL A 17 871 1287 1401 193 30 298 N ATOM 130 CA VAL A 17 5.568 -20.456 4.911 1.00 9.92 C ANISOU 130 CA VAL A 17 780 1597 1391 125 -60 145 C ATOM 131 C VAL A 17 4.639 -21.622 5.260 1.00 10.11 C ANISOU 131 C VAL A 17 688 1602 1548 18 -182 -97 C ATOM 132 O VAL A 17 4.004 -22.207 4.381 1.00 10.86 O ANISOU 132 O VAL A 17 691 1889 1544 28 -95 -326 O ATOM 133 CB VAL A 17 7.034 -20.928 4.911 1.00 9.94 C ANISOU 133 CB VAL A 17 606 1866 1304 196 -12 83 C ATOM 134 CG1 VAL A 17 7.216 -22.118 3.980 1.00 11.97 C ANISOU 134 CG1 VAL A 17 800 2200 1548 258 36 -307 C ATOM 135 CG2 VAL A 17 7.967 -19.774 4.524 1.00 11.84 C ANISOU 135 CG2 VAL A 17 775 2339 1384 5 74 341 C ATOM 136 N GLU A 18 4.539 -21.942 6.548 1.00 9.17 N ANISOU 136 N GLU A 18 781 1185 1519 74 -148 17 N ATOM 137 CA GLU A 18 3.750 -23.085 6.987 1.00 10.84 C ANISOU 137 CA GLU A 18 1091 1361 1667 41 -237 -4 C ATOM 138 C GLU A 18 2.257 -22.953 6.726 1.00 10.81 C ANISOU 138 C GLU A 18 1063 1508 1535 -65 -149 -60 C ATOM 139 O GLU A 18 1.546 -23.955 6.663 1.00 12.29 O ANISOU 139 O GLU A 18 1167 1452 2047 -163 -148 49 O ATOM 140 CB GLU A 18 4.005 -23.373 8.458 1.00 12.66 C ANISOU 140 CB GLU A 18 1242 1773 1793 -29 -225 206 C ATOM 141 CG GLU A 18 5.414 -23.848 8.705 1.00 14.53 C ANISOU 141 CG GLU A 18 1577 1949 1994 145 -327 229 C ATOM 142 CD GLU A 18 5.631 -24.301 10.123 1.00 18.66 C ANISOU 142 CD GLU A 18 2189 2603 2298 68 -316 232 C ATOM 143 OE1 GLU A 18 4.852 -23.892 11.007 1.00 22.40 O ANISOU 143 OE1 GLU A 18 2652 3318 2539 5 -116 212 O ATOM 144 OE2 GLU A 18 6.583 -25.068 10.346 1.00 20.00 O ANISOU 144 OE2 GLU A 18 2428 2529 2639 248 -462 542 O ATOM 145 N ALA A 19 1.774 -21.723 6.580 1.00 9.35 N ANISOU 145 N ALA A 19 804 1480 1267 52 90 -91 N ATOM 146 CA ALA A 19 0.364 -21.510 6.260 1.00 10.38 C ANISOU 146 CA ALA A 19 840 1597 1504 167 23 -52 C ATOM 147 C ALA A 19 0.038 -21.964 4.839 1.00 10.05 C ANISOU 147 C ALA A 19 767 1622 1430 123 -60 39 C ATOM 148 O ALA A 19 -1.103 -22.295 4.535 1.00 12.37 O ANISOU 148 O ALA A 19 809 2133 1757 -38 -88 -140 O ATOM 149 CB ALA A 19 -0.010 -20.056 6.460 1.00 10.88 C ANISOU 149 CB ALA A 19 969 1458 1706 90 28 -58 C ATOM 150 N ASP A 20 1.039 -21.971 3.965 1.00 10.08 N ANISOU 150 N ASP A 20 786 1849 1192 -176 52 -168 N ATOM 151 CA ASP A 20 0.846 -22.414 2.588 1.00 11.20 C ANISOU 151 CA ASP A 20 858 2002 1392 -171 100 -244 C ATOM 152 C ASP A 20 2.161 -22.993 2.083 1.00 9.47 C ANISOU 152 C ASP A 20 749 1676 1174 -328 80 -288 C ATOM 153 O ASP A 20 2.852 -22.379 1.271 1.00 9.05 O ANISOU 153 O ASP A 20 825 1509 1102 -307 170 -99 O ATOM 154 CB ASP A 20 0.411 -21.237 1.714 1.00 13.45 C ANISOU 154 CB ASP A 20 929 2615 1565 23 19 -94 C ATOM 155 CG ASP A 20 0.202 -21.631 0.260 1.00 15.58 C ANISOU 155 CG ASP A 20 989 3146 1784 -39 -79 -37 C ATOM 156 OD1 ASP A 20 0.075 -22.839 -0.023 1.00 15.69 O ANISOU 156 OD1 ASP A 20 836 3445 1678 -508 -17 -350 O ATOM 157 OD2 ASP A 20 0.174 -20.728 -0.600 1.00 18.28 O ANISOU 157 OD2 ASP A 20 1271 3626 2046 43 -189 206 O ATOM 158 N ILE A 21 2.510 -24.177 2.574 1.00 10.06 N ANISOU 158 N ILE A 21 1031 1504 1288 -406 151 -346 N ATOM 159 CA AILE A 21 3.793 -24.800 2.250 0.50 11.57 C ANISOU 159 CA AILE A 21 1439 1384 1572 -320 377 -333 C ATOM 160 CA BILE A 21 3.797 -24.768 2.249 0.50 11.43 C ANISOU 160 CA BILE A 21 1444 1356 1540 -315 366 -254 C ATOM 161 C ILE A 21 3.922 -25.094 0.763 1.00 12.38 C ANISOU 161 C ILE A 21 1593 1436 1673 -455 446 -314 C ATOM 162 O ILE A 21 4.954 -24.824 0.150 1.00 11.23 O ANISOU 162 O ILE A 21 1575 1162 1529 -314 475 -163 O ATOM 163 CB AILE A 21 4.001 -26.112 3.037 0.50 13.72 C ANISOU 163 CB AILE A 21 1843 1588 1779 -199 613 -284 C ATOM 164 CB BILE A 21 4.085 -26.009 3.110 0.50 13.20 C ANISOU 164 CB BILE A 21 1833 1499 1681 -175 581 -156 C ATOM 165 CG1AILE A 21 4.345 -25.812 4.497 0.50 13.94 C ANISOU 165 CG1AILE A 21 1802 1560 1935 -126 562 -246 C ATOM 166 CG1BILE A 21 5.570 -26.363 3.051 0.50 14.14 C ANISOU 166 CG1BILE A 21 2005 1540 1827 67 613 57 C ATOM 167 CG2AILE A 21 5.102 -26.952 2.395 0.50 14.76 C ANISOU 167 CG2AILE A 21 2172 1553 1881 -20 684 -197 C ATOM 168 CG2BILE A 21 3.196 -27.171 2.699 0.50 15.30 C ANISOU 168 CG2BILE A 21 2301 1566 1945 -402 689 -184 C ATOM 169 CD1AILE A 21 5.717 -25.208 4.685 0.50 15.38 C ANISOU 169 CD1AILE A 21 1746 2037 2059 31 393 -149 C ATOM 170 CD1BILE A 21 6.450 -25.338 3.713 0.50 14.74 C ANISOU 170 CD1BILE A 21 1963 1769 1867 338 533 42 C ATOM 171 N ALA A 22 2.867 -25.655 0.182 1.00 14.42 N ANISOU 171 N ALA A 22 1879 1923 1676 -921 497 -491 N ATOM 172 CA ALA A 22 2.888 -26.007 -1.235 1.00 15.72 C ANISOU 172 CA ALA A 22 2098 2153 1718 -1055 518 -598 C ATOM 173 C ALA A 22 3.026 -24.781 -2.142 1.00 14.20 C ANISOU 173 C ALA A 22 1634 2268 1491 -932 325 -569 C ATOM 174 O ALA A 22 3.770 -24.809 -3.120 1.00 14.97 O ANISOU 174 O ALA A 22 1877 2335 1474 -969 495 -440 O ATOM 175 CB ALA A 22 1.657 -26.818 -1.606 1.00 19.11 C ANISOU 175 CB ALA A 22 2291 2918 2052 -1426 490 -911 C ATOM 176 N GLY A 23 2.302 -23.713 -1.818 1.00 13.84 N ANISOU 176 N GLY A 23 1303 2477 1476 -734 199 -571 N ATOM 177 CA GLY A 23 2.363 -22.479 -2.598 1.00 13.96 C ANISOU 177 CA GLY A 23 1134 2594 1576 -555 34 -384 C ATOM 178 C GLY A 23 3.724 -21.812 -2.522 1.00 11.27 C ANISOU 178 C GLY A 23 879 2051 1352 -223 165 -239 C ATOM 179 O GLY A 23 4.280 -21.379 -3.531 1.00 11.40 O ANISOU 179 O GLY A 23 893 2138 1299 -42 73 -38 O ATOM 180 N HIS A 24 4.278 -21.728 -1.319 1.00 9.64 N ANISOU 180 N HIS A 24 923 1587 1152 -157 101 -235 N ATOM 181 CA HIS A 24 5.622 -21.190 -1.156 1.00 8.58 C ANISOU 181 CA HIS A 24 705 1389 1164 -16 130 -88 C ATOM 182 C HIS A 24 6.649 -22.078 -1.861 1.00 8.00 C ANISOU 182 C HIS A 24 796 1193 1048 -50 17 9 C ATOM 183 O HIS A 24 7.547 -21.580 -2.538 1.00 8.12 O ANISOU 183 O HIS A 24 736 1244 1105 78 180 69 O ATOM 184 CB HIS A 24 5.982 -21.031 0.322 1.00 8.67 C ANISOU 184 CB HIS A 24 987 1190 1118 -57 109 -97 C ATOM 185 CG HIS A 24 5.344 -19.846 0.976 1.00 8.74 C ANISOU 185 CG HIS A 24 917 1184 1218 -66 139 -94 C ATOM 186 ND1 HIS A 24 4.047 -19.864 1.443 1.00 9.29 N ANISOU 186 ND1 HIS A 24 879 1377 1274 -52 17 -44 N ATOM 187 CD2 HIS A 24 5.831 -18.615 1.261 1.00 9.20 C ANISOU 187 CD2 HIS A 24 1149 1164 1183 15 73 -45 C ATOM 188 CE1 HIS A 24 3.760 -18.690 1.978 1.00 10.17 C ANISOU 188 CE1 HIS A 24 1120 1277 1467 82 140 58 C ATOM 189 NE2 HIS A 24 4.826 -17.917 1.886 1.00 9.89 N ANISOU 189 NE2 HIS A 24 1328 1030 1399 16 189 33 N ATOM 190 N GLY A 25 6.513 -23.392 -1.705 1.00 8.53 N ANISOU 190 N GLY A 25 1001 1137 1101 -66 151 14 N ATOM 191 CA GLY A 25 7.464 -24.322 -2.310 1.00 10.75 C ANISOU 191 CA GLY A 25 1580 1288 1215 -87 201 -20 C ATOM 192 C GLY A 25 7.440 -24.240 -3.823 1.00 9.80 C ANISOU 192 C GLY A 25 1360 1116 1244 -223 227 49 C ATOM 193 O GLY A 25 8.483 -24.224 -4.473 1.00 9.90 O ANISOU 193 O GLY A 25 1296 1191 1274 -40 220 103 O ATOM 194 N GLN A 26 6.239 -24.209 -4.386 1.00 12.00 N ANISOU 194 N GLN A 26 1498 1704 1357 -404 232 -127 N ATOM 195 CA GLN A 26 6.080 -24.061 -5.822 1.00 12.57 C ANISOU 195 CA GLN A 26 1424 2004 1347 -431 98 -193 C ATOM 196 C GLN A 26 6.755 -22.782 -6.316 1.00 10.41 C ANISOU 196 C GLN A 26 1046 1786 1121 -205 71 -133 C ATOM 197 O GLN A 26 7.517 -22.810 -7.284 1.00 11.05 O ANISOU 197 O GLN A 26 1173 1875 1148 -197 191 -53 O ATOM 198 CB GLN A 26 4.594 -24.028 -6.180 1.00 16.02 C ANISOU 198 CB GLN A 26 1542 2906 1640 -443 131 -255 C ATOM 199 CG GLN A 26 4.315 -23.769 -7.652 1.00 19.36 C ANISOU 199 CG GLN A 26 1711 3668 1974 -275 40 -277 C ATOM 200 CD GLN A 26 2.868 -23.397 -7.908 1.00 22.17 C ANISOU 200 CD GLN A 26 1805 4474 2144 75 32 -408 C ATOM 201 OE1 GLN A 26 2.349 -22.444 -7.323 1.00 25.84 O ANISOU 201 OE1 GLN A 26 2356 4832 2627 358 -14 -273 O ATOM 202 NE2 GLN A 26 2.210 -24.144 -8.784 1.00 26.13 N ANISOU 202 NE2 GLN A 26 2020 5396 2509 -104 19 -575 N ATOM 203 N GLU A 27 6.461 -21.661 -5.662 1.00 10.01 N ANISOU 203 N GLU A 27 871 1715 1215 63 -1 -33 N ATOM 204 CA GLU A 27 7.005 -20.378 -6.097 1.00 11.00 C ANISOU 204 CA GLU A 27 975 1738 1464 214 -82 65 C ATOM 205 C GLU A 27 8.521 -20.335 -5.981 1.00 9.47 C ANISOU 205 C GLU A 27 994 1407 1197 154 53 132 C ATOM 206 O GLU A 27 9.193 -19.766 -6.835 1.00 9.80 O ANISOU 206 O GLU A 27 1020 1433 1270 192 144 335 O ATOM 207 CB GLU A 27 6.354 -19.208 -5.350 1.00 11.97 C ANISOU 207 CB GLU A 27 1027 2003 1517 352 -85 -83 C ATOM 208 CG GLU A 27 4.921 -18.940 -5.800 1.00 15.21 C ANISOU 208 CG GLU A 27 1110 2650 2019 487 -13 43 C ATOM 209 CD GLU A 27 4.356 -17.631 -5.273 1.00 16.86 C ANISOU 209 CD GLU A 27 1412 2781 2210 641 103 132 C ATOM 210 OE1 GLU A 27 5.112 -16.639 -5.168 1.00 19.39 O ANISOU 210 OE1 GLU A 27 2055 2758 2553 771 104 202 O ATOM 211 OE2 GLU A 27 3.143 -17.595 -4.978 1.00 21.25 O ANISOU 211 OE2 GLU A 27 1715 3499 2861 641 120 84 O ATOM 212 N VAL A 28 9.064 -20.947 -4.935 1.00 8.42 N ANISOU 212 N VAL A 28 949 999 1247 74 -31 27 N ATOM 213 CA VAL A 28 10.510 -21.011 -4.788 1.00 8.71 C ANISOU 213 CA VAL A 28 912 1136 1259 123 -78 1 C ATOM 214 C VAL A 28 11.152 -21.778 -5.944 1.00 7.96 C ANISOU 214 C VAL A 28 756 1122 1144 141 6 140 C ATOM 215 O VAL A 28 12.118 -21.314 -6.550 1.00 8.23 O ANISOU 215 O VAL A 28 881 1077 1166 160 -17 236 O ATOM 216 CB VAL A 28 10.921 -21.626 -3.434 1.00 8.90 C ANISOU 216 CB VAL A 28 985 1174 1222 118 -21 57 C ATOM 217 CG1 VAL A 28 12.398 -21.999 -3.439 1.00 9.45 C ANISOU 217 CG1 VAL A 28 965 1288 1334 258 -97 69 C ATOM 218 CG2 VAL A 28 10.620 -20.650 -2.300 1.00 8.95 C ANISOU 218 CG2 VAL A 28 1009 1165 1226 -14 27 -32 C ATOM 219 N LEU A 29 10.613 -22.948 -6.261 1.00 8.39 N ANISOU 219 N LEU A 29 833 1231 1123 151 -26 63 N ATOM 220 CA LEU A 29 11.172 -23.739 -7.355 1.00 9.08 C ANISOU 220 CA LEU A 29 1146 1211 1090 117 -25 19 C ATOM 221 C LEU A 29 11.000 -23.041 -8.708 1.00 8.39 C ANISOU 221 C LEU A 29 863 1274 1047 73 -82 66 C ATOM 222 O LEU A 29 11.895 -23.068 -9.545 1.00 9.25 O ANISOU 222 O LEU A 29 1070 1439 1005 47 80 184 O ATOM 223 CB LEU A 29 10.569 -25.142 -7.379 1.00 8.84 C ANISOU 223 CB LEU A 29 1022 1255 1079 86 21 71 C ATOM 224 CG LEU A 29 10.962 -26.044 -6.208 1.00 9.59 C ANISOU 224 CG LEU A 29 1251 1184 1207 157 69 145 C ATOM 225 CD1 LEU A 29 10.182 -27.347 -6.244 1.00 12.17 C ANISOU 225 CD1 LEU A 29 1619 1345 1660 -87 182 72 C ATOM 226 CD2 LEU A 29 12.462 -26.315 -6.199 1.00 10.80 C ANISOU 226 CD2 LEU A 29 1269 1186 1645 150 193 93 C ATOM 227 N ILE A 30 9.855 -22.411 -8.927 1.00 9.50 N ANISOU 227 N ILE A 30 913 1529 1164 41 32 139 N ATOM 228 CA ILE A 30 9.641 -21.709 -10.186 1.00 10.53 C ANISOU 228 CA ILE A 30 955 1663 1382 68 -138 325 C ATOM 229 C ILE A 30 10.608 -20.534 -10.329 1.00 9.49 C ANISOU 229 C ILE A 30 890 1522 1192 171 -31 309 C ATOM 230 O ILE A 30 11.165 -20.303 -11.403 1.00 10.12 O ANISOU 230 O ILE A 30 1023 1679 1142 103 232 332 O ATOM 231 CB ILE A 30 8.177 -21.272 -10.354 1.00 12.10 C ANISOU 231 CB ILE A 30 1011 2132 1454 121 -94 416 C ATOM 232 CG1 ILE A 30 7.303 -22.512 -10.550 1.00 13.74 C ANISOU 232 CG1 ILE A 30 1054 2573 1593 -276 -65 178 C ATOM 233 CG2 ILE A 30 8.037 -20.301 -11.523 1.00 13.96 C ANISOU 233 CG2 ILE A 30 1177 2590 1536 184 51 710 C ATOM 234 CD1 ILE A 30 5.817 -22.226 -10.640 1.00 16.48 C ANISOU 234 CD1 ILE A 30 1119 3308 1835 -45 -130 274 C ATOM 235 N ARG A 31 10.828 -19.811 -9.236 1.00 9.47 N ANISOU 235 N ARG A 31 1196 1235 1164 256 43 340 N ATOM 236 CA ARG A 31 11.796 -18.719 -9.237 1.00 10.05 C ANISOU 236 CA ARG A 31 1261 1245 1310 220 94 423 C ATOM 237 C ARG A 31 13.185 -19.256 -9.582 1.00 10.05 C ANISOU 237 C ARG A 31 1253 1309 1254 157 55 399 C ATOM 238 O ARG A 31 13.901 -18.676 -10.392 1.00 10.63 O ANISOU 238 O ARG A 31 1229 1370 1439 77 147 397 O ATOM 239 CB ARG A 31 11.799 -18.004 -7.881 1.00 10.76 C ANISOU 239 CB ARG A 31 1436 1182 1471 89 99 466 C ATOM 240 CG ARG A 31 12.818 -16.885 -7.750 1.00 12.31 C ANISOU 240 CG ARG A 31 1564 1163 1950 176 129 412 C ATOM 241 CD ARG A 31 12.464 -15.710 -8.640 1.00 14.51 C ANISOU 241 CD ARG A 31 1889 1328 2293 369 212 612 C ATOM 242 NE ARG A 31 13.419 -14.620 -8.475 1.00 17.16 N ANISOU 242 NE ARG A 31 2439 1322 2757 262 557 535 N ATOM 243 CZ ARG A 31 13.233 -13.392 -8.944 1.00 20.16 C ANISOU 243 CZ ARG A 31 2965 1365 3327 391 869 693 C ATOM 244 NH1 ARG A 31 12.122 -13.097 -9.606 1.00 22.53 N ANISOU 244 NH1 ARG A 31 3258 1738 3563 705 946 977 N ATOM 245 NH2 ARG A 31 14.156 -12.462 -8.751 1.00 22.37 N ANISOU 245 NH2 ARG A 31 3275 1321 3903 265 1108 388 N ATOM 246 N LEU A 32 13.554 -20.379 -8.971 1.00 8.92 N ANISOU 246 N LEU A 32 1020 1203 1163 119 -38 270 N ATOM 247 CA LEU A 32 14.839 -21.016 -9.230 1.00 9.17 C ANISOU 247 CA LEU A 32 1047 1219 1218 49 -20 230 C ATOM 248 C LEU A 32 14.983 -21.404 -10.703 1.00 8.81 C ANISOU 248 C LEU A 32 958 1295 1093 94 69 261 C ATOM 249 O LEU A 32 15.982 -21.074 -11.354 1.00 8.96 O ANISOU 249 O LEU A 32 1107 1217 1079 128 60 213 O ATOM 250 CB LEU A 32 14.970 -22.265 -8.357 1.00 8.92 C ANISOU 250 CB LEU A 32 1057 1066 1265 60 40 246 C ATOM 251 CG LEU A 32 16.245 -23.086 -8.526 1.00 9.35 C ANISOU 251 CG LEU A 32 943 1262 1345 73 1 227 C ATOM 252 CD1 LEU A 32 17.453 -22.309 -8.025 1.00 10.26 C ANISOU 252 CD1 LEU A 32 1002 1469 1425 -5 -99 203 C ATOM 253 CD2 LEU A 32 16.101 -24.420 -7.792 1.00 11.06 C ANISOU 253 CD2 LEU A 32 1439 1379 1383 171 59 328 C ATOM 254 N PHE A 33 13.980 -22.107 -11.223 1.00 9.07 N ANISOU 254 N PHE A 33 994 1258 1191 93 4 42 N ATOM 255 CA PHE A 33 14.041 -22.670 -12.570 1.00 10.24 C ANISOU 255 CA PHE A 33 1243 1516 1131 80 -45 105 C ATOM 256 C PHE A 33 14.016 -21.592 -13.649 1.00 10.81 C ANISOU 256 C PHE A 33 1183 1603 1319 147 16 228 C ATOM 257 O PHE A 33 14.716 -21.698 -14.654 1.00 11.96 O ANISOU 257 O PHE A 33 1438 1891 1214 179 37 324 O ATOM 258 CB PHE A 33 12.872 -23.627 -12.810 1.00 10.56 C ANISOU 258 CB PHE A 33 1087 1665 1260 -182 -128 48 C ATOM 259 CG PHE A 33 12.909 -24.883 -11.977 1.00 10.39 C ANISOU 259 CG PHE A 33 1149 1543 1255 -116 -77 -65 C ATOM 260 CD1 PHE A 33 14.101 -25.387 -11.474 1.00 10.66 C ANISOU 260 CD1 PHE A 33 1374 1416 1259 -86 34 39 C ATOM 261 CD2 PHE A 33 11.736 -25.581 -11.733 1.00 11.74 C ANISOU 261 CD2 PHE A 33 1212 1799 1449 -291 59 -236 C ATOM 262 CE1 PHE A 33 14.107 -26.558 -10.720 1.00 11.27 C ANISOU 262 CE1 PHE A 33 1433 1406 1443 -201 116 32 C ATOM 263 CE2 PHE A 33 11.738 -26.745 -10.986 1.00 12.56 C ANISOU 263 CE2 PHE A 33 1359 1681 1730 -248 141 -255 C ATOM 264 CZ PHE A 33 12.925 -27.236 -10.480 1.00 11.97 C ANISOU 264 CZ PHE A 33 1521 1424 1601 -176 122 -188 C ATOM 265 N THR A 34 13.197 -20.564 -13.451 1.00 10.91 N ANISOU 265 N THR A 34 1156 1781 1206 224 156 483 N ATOM 266 CA THR A 34 13.086 -19.492 -14.435 1.00 12.03 C ANISOU 266 CA THR A 34 1225 1946 1398 304 54 693 C ATOM 267 C THR A 34 14.295 -18.556 -14.411 1.00 11.78 C ANISOU 267 C THR A 34 1270 1774 1430 284 -3 654 C ATOM 268 O THR A 34 14.752 -18.101 -15.456 1.00 13.10 O ANISOU 268 O THR A 34 1589 2028 1358 183 128 737 O ATOM 269 CB THR A 34 11.769 -18.700 -14.287 1.00 14.25 C ANISOU 269 CB THR A 34 1375 2445 1592 402 72 711 C ATOM 270 OG1 THR A 34 11.707 -18.078 -12.998 1.00 14.91 O ANISOU 270 OG1 THR A 34 1548 2308 1808 439 150 689 O ATOM 271 CG2 THR A 34 10.570 -19.619 -14.465 1.00 15.58 C ANISOU 271 CG2 THR A 34 1217 2862 1840 269 -93 742 C ATOM 272 N GLY A 35 14.830 -18.287 -13.225 1.00 11.52 N ANISOU 272 N GLY A 35 1326 1548 1500 152 84 504 N ATOM 273 CA GLY A 35 16.005 -17.430 -13.104 1.00 11.79 C ANISOU 273 CA GLY A 35 1429 1400 1651 182 127 363 C ATOM 274 C GLY A 35 17.288 -18.128 -13.514 1.00 10.63 C ANISOU 274 C GLY A 35 1324 1481 1234 131 195 438 C ATOM 275 O GLY A 35 18.241 -17.488 -13.959 1.00 10.97 O ANISOU 275 O GLY A 35 1490 1381 1295 55 235 432 O ATOM 276 N HIS A 36 17.302 -19.450 -13.377 1.00 9.97 N ANISOU 276 N HIS A 36 1214 1299 1273 206 43 353 N ATOM 277 CA HIS A 36 18.509 -20.245 -13.615 1.00 9.18 C ANISOU 277 CA HIS A 36 942 1302 1244 196 63 346 C ATOM 278 C HIS A 36 18.141 -21.557 -14.299 1.00 9.85 C ANISOU 278 C HIS A 36 1057 1357 1326 43 75 272 C ATOM 279 O HIS A 36 18.113 -22.607 -13.664 1.00 8.93 O ANISOU 279 O HIS A 36 984 1217 1190 107 202 339 O ATOM 280 CB HIS A 36 19.232 -20.521 -12.287 1.00 9.34 C ANISOU 280 CB HIS A 36 1131 1261 1153 179 77 278 C ATOM 281 CG HIS A 36 19.413 -19.298 -11.444 1.00 10.14 C ANISOU 281 CG HIS A 36 1235 1429 1187 227 -20 269 C ATOM 282 ND1 HIS A 36 20.476 -18.435 -11.601 1.00 11.15 N ANISOU 282 ND1 HIS A 36 1353 1457 1424 81 -124 223 N ATOM 283 CD2 HIS A 36 18.654 -18.781 -10.448 1.00 11.47 C ANISOU 283 CD2 HIS A 36 1558 1634 1163 349 -91 9 C ATOM 284 CE1 HIS A 36 20.370 -17.445 -10.733 1.00 12.68 C ANISOU 284 CE1 HIS A 36 1781 1524 1510 151 -273 203 C ATOM 285 NE2 HIS A 36 19.272 -17.631 -10.022 1.00 13.28 N ANISOU 285 NE2 HIS A 36 1770 1711 1561 262 -186 117 N ATOM 286 N PRO A 37 17.837 -21.501 -15.603 1.00 10.27 N ANISOU 286 N PRO A 37 1464 1240 1195 -75 -13 263 N ATOM 287 CA PRO A 37 17.350 -22.682 -16.312 1.00 10.63 C ANISOU 287 CA PRO A 37 1647 1258 1133 -142 -52 274 C ATOM 288 C PRO A 37 18.245 -23.911 -16.219 1.00 10.67 C ANISOU 288 C PRO A 37 1692 1306 1055 -163 95 218 C ATOM 289 O PRO A 37 17.765 -25.029 -16.404 1.00 11.96 O ANISOU 289 O PRO A 37 1916 1247 1379 -311 22 121 O ATOM 290 CB PRO A 37 17.234 -22.198 -17.761 1.00 13.08 C ANISOU 290 CB PRO A 37 2304 1547 1116 -307 -280 399 C ATOM 291 CG PRO A 37 17.018 -20.730 -17.635 1.00 13.68 C ANISOU 291 CG PRO A 37 2342 1460 1393 -306 -337 401 C ATOM 292 CD PRO A 37 17.883 -20.316 -16.477 1.00 11.80 C ANISOU 292 CD PRO A 37 1732 1430 1321 -109 -119 408 C ATOM 293 N GLU A 38 19.530 -23.721 -15.945 1.00 11.40 N ANISOU 293 N GLU A 38 1659 1286 1386 -53 334 140 N ATOM 294 CA GLU A 38 20.428 -24.859 -15.822 1.00 12.07 C ANISOU 294 CA GLU A 38 1624 1390 1569 -108 537 113 C ATOM 295 C GLU A 38 20.008 -25.755 -14.663 1.00 11.29 C ANISOU 295 C GLU A 38 1369 1334 1583 62 419 134 C ATOM 296 O GLU A 38 20.276 -26.953 -14.667 1.00 12.67 O ANISOU 296 O GLU A 38 1601 1355 1859 -32 522 74 O ATOM 297 CB GLU A 38 21.886 -24.407 -15.673 1.00 12.90 C ANISOU 297 CB GLU A 38 1524 1511 1863 -89 648 97 C ATOM 298 CG GLU A 38 22.230 -23.702 -14.367 1.00 11.17 C ANISOU 298 CG GLU A 38 1102 1366 1776 51 378 212 C ATOM 299 CD GLU A 38 22.035 -22.199 -14.412 1.00 10.39 C ANISOU 299 CD GLU A 38 1104 1421 1423 106 374 238 C ATOM 300 OE1 GLU A 38 21.124 -21.712 -15.121 1.00 10.70 O ANISOU 300 OE1 GLU A 38 1281 1463 1319 136 274 231 O ATOM 301 OE2 GLU A 38 22.800 -21.499 -13.720 1.00 10.58 O ANISOU 301 OE2 GLU A 38 1158 1394 1468 118 331 196 O ATOM 302 N THR A 39 19.328 -25.179 -13.679 1.00 10.14 N ANISOU 302 N THR A 39 1160 1358 1333 -75 297 196 N ATOM 303 CA THR A 39 18.927 -25.948 -12.510 1.00 9.83 C ANISOU 303 CA THR A 39 1015 1333 1384 87 207 236 C ATOM 304 C THR A 39 17.852 -26.971 -12.851 1.00 9.61 C ANISOU 304 C THR A 39 931 1307 1412 222 108 294 C ATOM 305 O THR A 39 17.793 -28.042 -12.245 1.00 10.13 O ANISOU 305 O THR A 39 1153 1481 1212 74 36 158 O ATOM 306 CB THR A 39 18.469 -25.048 -11.342 1.00 9.01 C ANISOU 306 CB THR A 39 999 1207 1215 98 75 259 C ATOM 307 OG1 THR A 39 17.300 -24.314 -11.714 1.00 9.46 O ANISOU 307 OG1 THR A 39 931 1462 1200 186 99 308 O ATOM 308 CG2 THR A 39 19.573 -24.086 -10.940 1.00 10.93 C ANISOU 308 CG2 THR A 39 1480 1187 1483 51 -58 230 C ATOM 309 N LEU A 40 17.000 -26.636 -13.818 1.00 10.66 N ANISOU 309 N LEU A 40 1072 1584 1392 4 35 348 N ATOM 310 CA LEU A 40 15.945 -27.540 -14.251 1.00 11.13 C ANISOU 310 CA LEU A 40 1045 1694 1488 75 -73 367 C ATOM 311 C LEU A 40 16.521 -28.860 -14.755 1.00 10.40 C ANISOU 311 C LEU A 40 1086 1640 1224 -63 -89 300 C ATOM 312 O LEU A 40 15.930 -29.925 -14.567 1.00 11.43 O ANISOU 312 O LEU A 40 1215 1657 1470 -133 -148 210 O ATOM 313 CB LEU A 40 15.108 -26.883 -15.348 1.00 13.47 C ANISOU 313 CB LEU A 40 1434 2038 1643 -22 -195 432 C ATOM 314 CG LEU A 40 13.793 -27.582 -15.679 1.00 15.01 C ANISOU 314 CG LEU A 40 1541 2361 1800 -218 -346 426 C ATOM 315 CD1 LEU A 40 12.799 -27.376 -14.550 1.00 15.82 C ANISOU 315 CD1 LEU A 40 1284 2748 1977 -340 -108 331 C ATOM 316 CD2 LEU A 40 13.234 -27.040 -16.973 1.00 18.22 C ANISOU 316 CD2 LEU A 40 2114 2614 2193 -56 -750 501 C ATOM 317 N GLU A 41 17.690 -28.785 -15.380 1.00 10.96 N ANISOU 317 N GLU A 41 1103 1822 1236 -37 -8 94 N ATOM 318 CA GLU A 41 18.307 -29.950 -16.000 1.00 12.57 C ANISOU 318 CA GLU A 41 1426 1952 1396 -2 1 8 C ATOM 319 C GLU A 41 18.751 -30.999 -14.992 1.00 11.52 C ANISOU 319 C GLU A 41 1269 1682 1426 -11 -35 -34 C ATOM 320 O GLU A 41 18.969 -32.155 -15.348 1.00 13.77 O ANISOU 320 O GLU A 41 1668 1936 1625 94 31 -170 O ATOM 321 CB GLU A 41 19.476 -29.523 -16.882 1.00 13.95 C ANISOU 321 CB GLU A 41 1686 2166 1445 -116 98 -67 C ATOM 322 CG GLU A 41 19.063 -28.604 -18.011 1.00 16.48 C ANISOU 322 CG GLU A 41 2208 2333 1721 -208 65 13 C ATOM 323 CD GLU A 41 17.947 -29.188 -18.858 1.00 17.98 C ANISOU 323 CD GLU A 41 2658 2424 1749 -178 -168 -42 C ATOM 324 OE1 GLU A 41 18.099 -30.331 -19.329 1.00 18.32 O ANISOU 324 OE1 GLU A 41 2861 2406 1692 -277 -89 -183 O ATOM 325 OE2 GLU A 41 16.920 -28.504 -19.057 1.00 20.46 O ANISOU 325 OE2 GLU A 41 2960 2604 2210 -103 -486 -127 O ATOM 326 N LYS A 42 18.870 -30.599 -13.730 1.00 10.85 N ANISOU 326 N LYS A 42 928 2101 1093 55 -80 -15 N ATOM 327 CA LYS A 42 19.232 -31.542 -12.679 1.00 11.54 C ANISOU 327 CA LYS A 42 1141 1974 1269 -11 -112 26 C ATOM 328 C LYS A 42 18.049 -32.415 -12.281 1.00 10.84 C ANISOU 328 C LYS A 42 1091 1861 1167 69 -146 29 C ATOM 329 O LYS A 42 18.227 -33.422 -11.596 1.00 11.32 O ANISOU 329 O LYS A 42 1091 1772 1436 83 -114 56 O ATOM 330 CB LYS A 42 19.777 -30.813 -11.449 1.00 10.93 C ANISOU 330 CB LYS A 42 940 1890 1319 11 -70 -93 C ATOM 331 CG LYS A 42 21.108 -30.126 -11.673 1.00 11.32 C ANISOU 331 CG LYS A 42 1082 1807 1412 115 15 25 C ATOM 332 CD LYS A 42 22.238 -31.131 -11.842 1.00 11.72 C ANISOU 332 CD LYS A 42 1043 1829 1581 197 -71 44 C ATOM 333 CE LYS A 42 23.554 -30.406 -12.062 1.00 12.26 C ANISOU 333 CE LYS A 42 1100 1925 1631 192 39 344 C ATOM 334 NZ LYS A 42 24.710 -31.341 -12.121 1.00 13.62 N ANISOU 334 NZ LYS A 42 1412 2180 1582 253 167 112 N ATOM 335 N PHE A 43 16.851 -32.027 -12.722 1.00 10.21 N ANISOU 335 N PHE A 43 829 1956 1093 5 -122 -15 N ATOM 336 CA PHE A 43 15.627 -32.737 -12.363 1.00 11.69 C ANISOU 336 CA PHE A 43 1107 1864 1469 -25 -87 -101 C ATOM 337 C PHE A 43 15.089 -33.474 -13.580 1.00 13.83 C ANISOU 337 C PHE A 43 1405 2190 1657 -54 -249 -115 C ATOM 338 O PHE A 43 14.408 -32.889 -14.426 1.00 12.98 O ANISOU 338 O PHE A 43 1355 2169 1407 -236 -138 -126 O ATOM 339 CB PHE A 43 14.540 -31.765 -11.900 1.00 10.50 C ANISOU 339 CB PHE A 43 789 1778 1420 80 -159 -48 C ATOM 340 CG PHE A 43 14.766 -31.175 -10.533 1.00 11.02 C ANISOU 340 CG PHE A 43 909 1867 1409 82 -96 57 C ATOM 341 CD1 PHE A 43 15.428 -29.968 -10.382 1.00 10.57 C ANISOU 341 CD1 PHE A 43 971 1767 1277 158 -227 196 C ATOM 342 CD2 PHE A 43 14.267 -31.800 -9.406 1.00 10.56 C ANISOU 342 CD2 PHE A 43 778 1905 1329 114 -26 -55 C ATOM 343 CE1 PHE A 43 15.611 -29.410 -9.124 1.00 12.30 C ANISOU 343 CE1 PHE A 43 1077 1937 1656 301 -363 19 C ATOM 344 CE2 PHE A 43 14.446 -31.245 -8.153 1.00 11.14 C ANISOU 344 CE2 PHE A 43 997 1852 1383 299 -54 38 C ATOM 345 CZ PHE A 43 15.115 -30.050 -8.015 1.00 11.67 C ANISOU 345 CZ PHE A 43 1011 1817 1604 389 -251 -6 C ATOM 346 N ASP A 44 15.371 -34.765 -13.663 1.00 16.94 N ANISOU 346 N ASP A 44 1884 2391 2160 43 -227 -385 N ATOM 347 CA ASP A 44 14.848 -35.554 -14.762 1.00 20.25 C ANISOU 347 CA ASP A 44 2338 2894 2460 -26 -323 -373 C ATOM 348 C ASP A 44 13.334 -35.424 -14.847 1.00 20.87 C ANISOU 348 C ASP A 44 2342 3054 2531 -80 -326 -351 C ATOM 349 O ASP A 44 12.763 -35.459 -15.934 1.00 22.10 O ANISOU 349 O ASP A 44 2389 3454 2553 -269 -511 -451 O ATOM 350 CB ASP A 44 15.258 -37.018 -14.617 1.00 23.88 C ANISOU 350 CB ASP A 44 2831 3132 3107 123 -205 -380 C ATOM 351 CG ASP A 44 16.706 -37.248 -14.985 1.00 26.19 C ANISOU 351 CG ASP A 44 3105 3424 3419 200 -116 -301 C ATOM 352 OD1 ASP A 44 17.222 -36.498 -15.842 1.00 28.12 O ANISOU 352 OD1 ASP A 44 3350 3718 3616 261 4 -251 O ATOM 353 OD2 ASP A 44 17.327 -38.172 -14.419 1.00 28.66 O ANISOU 353 OD2 ASP A 44 3459 3647 3781 223 -165 -285 O ATOM 354 N LYS A 45 12.682 -35.255 -13.702 1.00 19.10 N ANISOU 354 N LYS A 45 2009 2856 2391 -196 -339 -194 N ATOM 355 CA LYS A 45 11.226 -35.198 -13.684 1.00 20.49 C ANISOU 355 CA LYS A 45 2091 3104 2588 -78 -135 -101 C ATOM 356 C LYS A 45 10.628 -33.806 -13.907 1.00 18.36 C ANISOU 356 C LYS A 45 1708 2918 2351 -108 -203 -58 C ATOM 357 O LYS A 45 9.407 -33.657 -13.953 1.00 17.55 O ANISOU 357 O LYS A 45 1335 3111 2220 -206 -142 -204 O ATOM 358 CB LYS A 45 10.671 -35.830 -12.411 1.00 21.45 C ANISOU 358 CB LYS A 45 2389 3221 2537 -94 -74 -158 C ATOM 359 CG LYS A 45 10.890 -35.004 -11.162 1.00 21.67 C ANISOU 359 CG LYS A 45 2370 3297 2565 -49 -127 -214 C ATOM 360 CD LYS A 45 10.357 -35.738 -9.951 1.00 23.17 C ANISOU 360 CD LYS A 45 2650 3345 2807 76 -24 -58 C ATOM 361 CE LYS A 45 10.479 -34.899 -8.698 1.00 23.68 C ANISOU 361 CE LYS A 45 2889 3250 2859 128 108 -78 C ATOM 362 NZ LYS A 45 10.108 -35.678 -7.486 1.00 25.50 N ANISOU 362 NZ LYS A 45 3105 3464 3119 254 195 42 N ATOM 363 N PHE A 46 11.475 -32.791 -14.047 1.00 14.47 N ANISOU 363 N PHE A 46 1290 2636 1572 -95 -194 33 N ATOM 364 CA PHE A 46 10.980 -31.453 -14.370 1.00 14.56 C ANISOU 364 CA PHE A 46 1417 2501 1613 -44 -107 42 C ATOM 365 C PHE A 46 11.526 -30.899 -15.684 1.00 15.27 C ANISOU 365 C PHE A 46 1648 2567 1587 -87 -46 22 C ATOM 366 O PHE A 46 11.094 -29.840 -16.143 1.00 15.59 O ANISOU 366 O PHE A 46 1766 2484 1674 15 -188 132 O ATOM 367 CB PHE A 46 11.209 -30.469 -13.217 1.00 14.43 C ANISOU 367 CB PHE A 46 1405 2397 1679 24 -146 111 C ATOM 368 CG PHE A 46 10.505 -30.855 -11.948 1.00 13.79 C ANISOU 368 CG PHE A 46 1240 2431 1568 68 -223 60 C ATOM 369 CD1 PHE A 46 9.165 -31.210 -11.961 1.00 14.26 C ANISOU 369 CD1 PHE A 46 1277 2430 1708 72 -175 132 C ATOM 370 CD2 PHE A 46 11.179 -30.859 -10.738 1.00 13.43 C ANISOU 370 CD2 PHE A 46 1221 2293 1587 291 -284 150 C ATOM 371 CE1 PHE A 46 8.516 -31.569 -10.788 1.00 14.99 C ANISOU 371 CE1 PHE A 46 1483 2392 1819 98 -94 34 C ATOM 372 CE2 PHE A 46 10.533 -31.216 -9.568 1.00 14.00 C ANISOU 372 CE2 PHE A 46 1323 2250 1746 305 -12 30 C ATOM 373 CZ PHE A 46 9.203 -31.571 -9.592 1.00 14.88 C ANISOU 373 CZ PHE A 46 1456 2383 1813 190 -45 60 C ATOM 374 N LYS A 47 12.459 -31.627 -16.294 1.00 17.28 N ANISOU 374 N LYS A 47 2048 2683 1835 -59 288 20 N ATOM 375 CA LYS A 47 13.047 -31.242 -17.582 1.00 20.64 C ANISOU 375 CA LYS A 47 2585 3174 2081 91 392 98 C ATOM 376 C LYS A 47 12.018 -30.963 -18.673 1.00 21.06 C ANISOU 376 C LYS A 47 2710 3350 1941 111 321 92 C ATOM 377 O LYS A 47 12.269 -30.165 -19.581 1.00 22.54 O ANISOU 377 O LYS A 47 2995 3506 2060 192 460 215 O ATOM 378 CB LYS A 47 13.991 -32.337 -18.084 1.00 23.47 C ANISOU 378 CB LYS A 47 2876 3526 2514 179 423 92 C ATOM 379 CG LYS A 47 15.393 -32.267 -17.536 1.00 25.03 C ANISOU 379 CG LYS A 47 3038 3624 2846 168 324 16 C ATOM 380 CD LYS A 47 16.239 -33.388 -18.124 1.00 26.35 C ANISOU 380 CD LYS A 47 3147 3744 3121 359 281 -63 C ATOM 381 CE LYS A 47 17.699 -33.256 -17.731 1.00 27.89 C ANISOU 381 CE LYS A 47 3311 3895 3389 371 177 45 C ATOM 382 NZ LYS A 47 18.509 -34.401 -18.236 1.00 29.28 N ANISOU 382 NZ LYS A 47 3505 4012 3608 433 173 68 N ATOM 383 N HIS A 48 10.876 -31.640 -18.601 1.00 20.88 N ANISOU 383 N HIS A 48 2655 3395 1882 141 103 -64 N ATOM 384 CA HIS A 48 9.852 -31.540 -19.641 1.00 22.13 C ANISOU 384 CA HIS A 48 2735 3668 2006 169 -125 -62 C ATOM 385 C HIS A 48 9.101 -30.219 -19.566 1.00 22.62 C ANISOU 385 C HIS A 48 2785 3709 2097 188 -222 57 C ATOM 386 O HIS A 48 8.374 -29.858 -20.492 1.00 24.89 O ANISOU 386 O HIS A 48 3043 4144 2267 206 -383 213 O ATOM 387 CB HIS A 48 8.844 -32.680 -19.503 1.00 22.57 C ANISOU 387 CB HIS A 48 2668 3681 2223 166 -185 -324 C ATOM 388 CG HIS A 48 7.968 -32.557 -18.297 1.00 21.96 C ANISOU 388 CG HIS A 48 2500 3604 2238 195 -320 -395 C ATOM 389 ND1 HIS A 48 8.356 -32.996 -17.050 1.00 21.00 N ANISOU 389 ND1 HIS A 48 2281 3476 2220 159 -518 -366 N ATOM 390 CD2 HIS A 48 6.732 -32.026 -18.141 1.00 21.93 C ANISOU 390 CD2 HIS A 48 2387 3627 2315 135 -461 -449 C ATOM 391 CE1 HIS A 48 7.394 -32.750 -16.180 1.00 21.46 C ANISOU 391 CE1 HIS A 48 2392 3462 2296 154 -475 -449 C ATOM 392 NE2 HIS A 48 6.397 -32.162 -16.816 1.00 21.59 N ANISOU 392 NE2 HIS A 48 2268 3543 2391 117 -477 -474 N ATOM 393 N LEU A 49 9.257 -29.509 -18.455 1.00 20.49 N ANISOU 393 N LEU A 49 2370 3434 1979 116 -74 113 N ATOM 394 CA LEU A 49 8.566 -28.241 -18.272 1.00 20.82 C ANISOU 394 CA LEU A 49 2408 3381 2118 182 -145 211 C ATOM 395 C LEU A 49 9.229 -27.169 -19.119 1.00 21.83 C ANISOU 395 C LEU A 49 2539 3363 2392 162 -170 271 C ATOM 396 O LEU A 49 10.309 -26.682 -18.795 1.00 22.84 O ANISOU 396 O LEU A 49 2539 3534 2602 103 -271 522 O ATOM 397 CB LEU A 49 8.534 -27.843 -16.796 1.00 19.27 C ANISOU 397 CB LEU A 49 2114 3180 2027 196 -243 205 C ATOM 398 CG LEU A 49 7.721 -28.789 -15.907 1.00 18.73 C ANISOU 398 CG LEU A 49 1845 3120 2149 146 -255 92 C ATOM 399 CD1 LEU A 49 7.914 -28.455 -14.439 1.00 18.76 C ANISOU 399 CD1 LEU A 49 2062 3005 2060 162 -219 221 C ATOM 400 CD2 LEU A 49 6.242 -28.770 -16.280 1.00 19.52 C ANISOU 400 CD2 LEU A 49 1833 3291 2291 161 -287 40 C ATOM 401 N LYS A 50 8.569 -26.811 -20.214 1.00 22.30 N ANISOU 401 N LYS A 50 2646 3519 2307 253 -161 249 N ATOM 402 CA LYS A 50 9.155 -25.928 -21.213 1.00 23.37 C ANISOU 402 CA LYS A 50 2849 3521 2508 293 17 257 C ATOM 403 C LYS A 50 8.762 -24.469 -21.016 1.00 22.01 C ANISOU 403 C LYS A 50 2606 3362 2393 312 -17 258 C ATOM 404 O LYS A 50 9.366 -23.573 -21.603 1.00 23.36 O ANISOU 404 O LYS A 50 2932 3371 2572 289 143 373 O ATOM 405 CB LYS A 50 8.754 -26.382 -22.617 1.00 25.95 C ANISOU 405 CB LYS A 50 3196 3940 2721 348 4 100 C ATOM 406 CG LYS A 50 9.069 -27.841 -22.909 1.00 27.87 C ANISOU 406 CG LYS A 50 3372 4093 3122 427 34 58 C ATOM 407 CD LYS A 50 10.549 -28.129 -22.731 1.00 29.24 C ANISOU 407 CD LYS A 50 3500 4256 3351 468 61 80 C ATOM 408 CE LYS A 50 10.878 -29.567 -23.095 1.00 30.15 C ANISOU 408 CE LYS A 50 3624 4372 3457 476 72 6 C ATOM 409 NZ LYS A 50 12.323 -29.865 -22.887 1.00 31.17 N ANISOU 409 NZ LYS A 50 3627 4581 3633 401 82 1 N ATOM 410 N THR A 51 7.743 -24.238 -20.197 1.00 20.15 N ANISOU 410 N THR A 51 2322 3625 1708 219 66 831 N ATOM 411 CA ATHR A 51 7.248 -22.889 -19.944 0.50 18.61 C ANISOU 411 CA ATHR A 51 1997 3473 1598 105 -106 930 C ATOM 412 CA BTHR A 51 7.276 -22.885 -19.932 0.50 20.23 C ANISOU 412 CA BTHR A 51 2226 3594 1865 93 -20 834 C ATOM 413 C THR A 51 6.880 -22.721 -18.476 1.00 17.95 C ANISOU 413 C THR A 51 1831 3212 1777 118 -137 798 C ATOM 414 O THR A 51 6.639 -23.704 -17.771 1.00 16.86 O ANISOU 414 O THR A 51 1702 3082 1620 -31 -174 655 O ATOM 415 CB ATHR A 51 5.978 -22.602 -20.761 0.50 18.64 C ANISOU 415 CB ATHR A 51 1995 3632 1454 69 -245 1130 C ATOM 416 CB BTHR A 51 6.060 -22.529 -20.797 0.50 22.20 C ANISOU 416 CB BTHR A 51 2432 3937 2065 51 -130 937 C ATOM 417 OG1ATHR A 51 4.897 -23.386 -20.239 0.50 17.02 O ANISOU 417 OG1ATHR A 51 1660 3578 1227 -37 -490 1028 O ATOM 418 OG1BTHR A 51 5.577 -21.235 -20.419 0.50 23.94 O ANISOU 418 OG1BTHR A 51 2491 4007 2598 23 -62 952 O ATOM 419 CG2ATHR A 51 6.193 -22.928 -22.239 0.50 20.10 C ANISOU 419 CG2ATHR A 51 2302 4019 1315 77 -284 1143 C ATOM 420 CG2BTHR A 51 4.952 -23.549 -20.591 0.50 22.96 C ANISOU 420 CG2BTHR A 51 2525 4026 2172 -101 -270 781 C ATOM 421 N GLU A 52 6.813 -21.473 -18.024 1.00 17.65 N ANISOU 421 N GLU A 52 1870 3000 1836 131 -205 905 N ATOM 422 CA GLU A 52 6.405 -21.208 -16.654 1.00 16.94 C ANISOU 422 CA GLU A 52 1789 2900 1746 106 -199 857 C ATOM 423 C GLU A 52 4.957 -21.619 -16.411 1.00 16.96 C ANISOU 423 C GLU A 52 1619 3085 1737 262 -377 914 C ATOM 424 O GLU A 52 4.611 -22.068 -15.319 1.00 17.14 O ANISOU 424 O GLU A 52 1597 3211 1704 264 -195 973 O ATOM 425 CB GLU A 52 6.629 -19.747 -16.273 1.00 17.25 C ANISOU 425 CB GLU A 52 1987 2732 1832 155 -281 885 C ATOM 426 CG GLU A 52 6.183 -19.426 -14.857 1.00 18.47 C ANISOU 426 CG GLU A 52 2273 2805 1938 140 -194 708 C ATOM 427 CD GLU A 52 6.601 -18.044 -14.413 1.00 21.02 C ANISOU 427 CD GLU A 52 2893 2771 2323 100 -255 616 C ATOM 428 OE1 GLU A 52 7.443 -17.426 -15.098 1.00 23.15 O ANISOU 428 OE1 GLU A 52 3050 2973 2771 -186 -405 727 O ATOM 429 OE2 GLU A 52 6.086 -17.580 -13.375 1.00 24.90 O ANISOU 429 OE2 GLU A 52 3524 3079 2859 86 -120 261 O ATOM 430 N ALA A 53 4.111 -21.475 -17.428 1.00 18.46 N ANISOU 430 N ALA A 53 1694 3474 1847 227 -390 1060 N ATOM 431 CA ALA A 53 2.729 -21.919 -17.315 1.00 19.49 C ANISOU 431 CA ALA A 53 1663 3685 2057 177 -374 1168 C ATOM 432 C ALA A 53 2.698 -23.409 -17.008 1.00 18.60 C ANISOU 432 C ALA A 53 1473 3757 1835 -69 -532 1096 C ATOM 433 O ALA A 53 1.938 -23.859 -16.154 1.00 20.05 O ANISOU 433 O ALA A 53 1498 3962 2157 -277 -448 1336 O ATOM 434 CB ALA A 53 1.954 -21.621 -18.596 1.00 21.18 C ANISOU 434 CB ALA A 53 1774 4049 2223 145 -468 1473 C ATOM 435 N GLU A 54 3.531 -24.176 -17.703 1.00 17.84 N ANISOU 435 N GLU A 54 1772 3540 1467 -254 -609 855 N ATOM 436 CA GLU A 54 3.602 -25.606 -17.449 1.00 18.91 C ANISOU 436 CA GLU A 54 1817 3646 1719 -387 -650 650 C ATOM 437 C GLU A 54 4.105 -25.865 -16.030 1.00 16.37 C ANISOU 437 C GLU A 54 1286 3359 1575 -370 -522 602 C ATOM 438 O GLU A 54 3.600 -26.748 -15.338 1.00 17.73 O ANISOU 438 O GLU A 54 1467 3499 1769 -535 -407 634 O ATOM 439 CB GLU A 54 4.481 -26.305 -18.491 1.00 20.09 C ANISOU 439 CB GLU A 54 2337 3666 1629 -455 -716 324 C ATOM 440 CG GLU A 54 3.862 -26.338 -19.884 1.00 24.63 C ANISOU 440 CG GLU A 54 3028 4455 1876 -519 -947 228 C ATOM 441 CD GLU A 54 4.812 -26.861 -20.943 1.00 27.54 C ANISOU 441 CD GLU A 54 3729 4713 2020 -362 -793 59 C ATOM 442 OE1 GLU A 54 6.041 -26.806 -20.728 1.00 29.18 O ANISOU 442 OE1 GLU A 54 3812 4938 2336 -23 -541 38 O ATOM 443 OE2 GLU A 54 4.327 -27.316 -22.002 1.00 32.02 O ANISOU 443 OE2 GLU A 54 4495 5394 2275 -481 -1047 -161 O ATOM 444 N MET A 55 5.099 -25.094 -15.596 1.00 15.66 N ANISOU 444 N MET A 55 1197 3228 1523 -99 -265 479 N ATOM 445 CA MET A 55 5.600 -25.215 -14.228 1.00 14.40 C ANISOU 445 CA MET A 55 942 3129 1400 -82 -226 541 C ATOM 446 C MET A 55 4.491 -24.960 -13.218 1.00 14.84 C ANISOU 446 C MET A 55 904 3336 1397 -26 -264 642 C ATOM 447 O MET A 55 4.323 -25.719 -12.270 1.00 14.98 O ANISOU 447 O MET A 55 988 3380 1323 -119 -162 723 O ATOM 448 CB MET A 55 6.746 -24.237 -13.975 1.00 14.25 C ANISOU 448 CB MET A 55 1042 2974 1395 -7 -122 478 C ATOM 449 CG MET A 55 7.991 -24.499 -14.792 1.00 14.97 C ANISOU 449 CG MET A 55 1176 2988 1522 -109 -17 563 C ATOM 450 SD MET A 55 9.227 -23.243 -14.443 1.00 15.39 S ANISOU 450 SD MET A 55 1204 2921 1721 -132 -81 832 S ATOM 451 CE MET A 55 10.399 -23.563 -15.760 1.00 17.21 C ANISOU 451 CE MET A 55 1317 3460 1761 -55 4 903 C ATOM 452 N LYS A 56 3.723 -23.897 -13.438 1.00 15.71 N ANISOU 452 N LYS A 56 1055 3339 1575 111 -145 845 N ATOM 453 CA ALYS A 56 2.646 -23.522 -12.526 0.50 17.49 C ANISOU 453 CA ALYS A 56 1183 3733 1728 120 39 802 C ATOM 454 CA BLYS A 56 2.654 -23.528 -12.520 0.50 17.34 C ANISOU 454 CA BLYS A 56 1184 3711 1693 142 41 815 C ATOM 455 C LYS A 56 1.554 -24.587 -12.477 1.00 18.18 C ANISOU 455 C LYS A 56 903 4111 1892 72 -60 1029 C ATOM 456 O LYS A 56 0.940 -24.814 -11.433 1.00 19.85 O ANISOU 456 O LYS A 56 1012 4581 1947 -17 75 1060 O ATOM 457 CB ALYS A 56 2.042 -22.173 -12.927 0.50 19.61 C ANISOU 457 CB ALYS A 56 1429 3895 2125 313 169 856 C ATOM 458 CB BLYS A 56 2.068 -22.169 -12.898 0.50 19.24 C ANISOU 458 CB BLYS A 56 1433 3859 2017 380 181 889 C ATOM 459 CG ALYS A 56 2.962 -20.976 -12.724 0.50 20.17 C ANISOU 459 CG ALYS A 56 1784 3647 2232 359 217 617 C ATOM 460 CG BLYS A 56 1.185 -21.554 -11.825 0.50 21.85 C ANISOU 460 CG BLYS A 56 1729 4265 2305 717 394 913 C ATOM 461 CD ALYS A 56 3.116 -20.623 -11.253 0.50 22.42 C ANISOU 461 CD ALYS A 56 2314 3806 2397 352 347 352 C ATOM 462 CD BLYS A 56 1.999 -21.145 -10.608 0.50 22.85 C ANISOU 462 CD BLYS A 56 2261 4209 2210 736 476 631 C ATOM 463 CE ALYS A 56 4.013 -19.406 -11.074 0.50 24.61 C ANISOU 463 CE ALYS A 56 3010 3713 2628 294 337 119 C ATOM 464 CE BLYS A 56 1.135 -20.430 -9.583 0.50 27.23 C ANISOU 464 CE BLYS A 56 2934 4803 2607 1093 788 587 C ATOM 465 NZ ALYS A 56 4.374 -19.180 -9.646 0.50 26.78 N ANISOU 465 NZ ALYS A 56 3681 3926 2566 192 388 -124 N ATOM 466 NZ BLYS A 56 1.940 -19.903 -8.447 0.50 29.26 N ANISOU 466 NZ BLYS A 56 3653 4838 2626 1022 831 263 N ATOM 467 N ALA A 57 1.320 -25.240 -13.611 1.00 18.01 N ANISOU 467 N ALA A 57 886 3992 1963 -79 -339 1045 N ATOM 468 CA ALA A 57 0.276 -26.256 -13.723 1.00 19.82 C ANISOU 468 CA ALA A 57 1019 4447 2062 -328 -540 1255 C ATOM 469 C ALA A 57 0.723 -27.629 -13.233 1.00 18.81 C ANISOU 469 C ALA A 57 792 4250 2105 -522 -608 1247 C ATOM 470 O ALA A 57 -0.088 -28.550 -13.123 1.00 21.30 O ANISOU 470 O ALA A 57 1057 4536 2499 -712 -816 1485 O ATOM 471 CB ALA A 57 -0.216 -26.348 -15.163 1.00 21.57 C ANISOU 471 CB ALA A 57 1339 4658 2198 -403 -936 1355 C ATOM 472 N SER A 58 2.007 -27.767 -12.918 1.00 15.15 N ANISOU 472 N SER A 58 1296 2677 1781 -310 -228 527 N ATOM 473 CA SER A 58 2.542 -29.062 -12.515 1.00 13.89 C ANISOU 473 CA SER A 58 1146 2568 1561 -449 -123 365 C ATOM 474 C SER A 58 2.239 -29.391 -11.055 1.00 12.03 C ANISOU 474 C SER A 58 802 2281 1486 -503 -4 327 C ATOM 475 O SER A 58 2.747 -28.743 -10.141 1.00 13.38 O ANISOU 475 O SER A 58 1233 2419 1431 -631 -183 257 O ATOM 476 CB SER A 58 4.048 -29.118 -12.764 1.00 13.74 C ANISOU 476 CB SER A 58 1133 2583 1505 -443 -146 359 C ATOM 477 OG SER A 58 4.587 -30.320 -12.249 1.00 13.40 O ANISOU 477 OG SER A 58 1275 2419 1395 -389 -167 134 O ATOM 478 N GLU A 59 1.429 -30.416 -10.831 1.00 12.82 N ANISOU 478 N GLU A 59 872 2384 1614 -435 -231 386 N ATOM 479 CA GLU A 59 1.115 -30.813 -9.468 1.00 12.19 C ANISOU 479 CA GLU A 59 780 2234 1616 -175 -137 292 C ATOM 480 C GLU A 59 2.314 -31.504 -8.819 1.00 10.88 C ANISOU 480 C GLU A 59 750 2039 1341 -234 -106 146 C ATOM 481 O GLU A 59 2.514 -31.418 -7.605 1.00 11.07 O ANISOU 481 O GLU A 59 819 2047 1337 -80 -147 38 O ATOM 482 CB GLU A 59 -0.140 -31.691 -9.428 1.00 13.31 C ANISOU 482 CB GLU A 59 685 2472 1900 -268 -310 439 C ATOM 483 CG GLU A 59 -1.414 -30.984 -9.910 1.00 16.76 C ANISOU 483 CG GLU A 59 1058 2795 2514 52 -375 539 C ATOM 484 CD GLU A 59 -1.724 -29.719 -9.120 1.00 18.04 C ANISOU 484 CD GLU A 59 1030 2994 2829 501 -248 569 C ATOM 485 OE1 GLU A 59 -1.393 -29.657 -7.922 1.00 20.12 O ANISOU 485 OE1 GLU A 59 1540 2932 3172 442 -291 595 O ATOM 486 OE2 GLU A 59 -2.318 -28.783 -9.697 1.00 22.76 O ANISOU 486 OE2 GLU A 59 2116 3209 3322 808 -227 690 O ATOM 487 N ASP A 60 3.128 -32.170 -9.632 1.00 10.69 N ANISOU 487 N ASP A 60 739 2028 1292 -277 -202 66 N ATOM 488 CA ASP A 60 4.306 -32.826 -9.105 1.00 11.58 C ANISOU 488 CA ASP A 60 909 1971 1519 -206 -74 59 C ATOM 489 C ASP A 60 5.361 -31.826 -8.654 1.00 10.76 C ANISOU 489 C ASP A 60 829 1814 1445 -183 -111 75 C ATOM 490 O ASP A 60 6.116 -32.095 -7.719 1.00 10.43 O ANISOU 490 O ASP A 60 983 1778 1202 -151 -241 96 O ATOM 491 CB ASP A 60 4.905 -33.803 -10.106 1.00 13.16 C ANISOU 491 CB ASP A 60 980 2244 1774 -94 -222 3 C ATOM 492 CG ASP A 60 5.834 -34.780 -9.444 1.00 15.24 C ANISOU 492 CG ASP A 60 1287 2289 2214 8 -49 34 C ATOM 493 OD1 ASP A 60 5.399 -35.413 -8.459 1.00 16.41 O ANISOU 493 OD1 ASP A 60 1595 2312 2324 129 16 151 O ATOM 494 OD2 ASP A 60 6.993 -34.904 -9.889 1.00 18.93 O ANISOU 494 OD2 ASP A 60 1524 2915 2750 227 129 -74 O ATOM 495 N LEU A 61 5.429 -30.676 -9.322 1.00 10.31 N ANISOU 495 N LEU A 61 812 1751 1350 -390 -229 124 N ATOM 496 CA ALEU A 61 6.356 -29.629 -8.922 0.50 10.80 C ANISOU 496 CA ALEU A 61 959 1826 1318 -413 -235 269 C ATOM 497 CA BLEU A 61 6.359 -29.628 -8.916 0.50 10.97 C ANISOU 497 CA BLEU A 61 1020 1832 1313 -379 -218 235 C ATOM 498 C LEU A 61 5.946 -29.071 -7.560 1.00 10.43 C ANISOU 498 C LEU A 61 1002 1626 1332 -267 -215 289 C ATOM 499 O LEU A 61 6.783 -28.872 -6.681 1.00 10.28 O ANISOU 499 O LEU A 61 958 1738 1209 -463 -409 342 O ATOM 500 CB ALEU A 61 6.418 -28.530 -9.988 0.50 11.33 C ANISOU 500 CB ALEU A 61 971 1891 1441 -472 -309 361 C ATOM 501 CB BLEU A 61 6.440 -28.513 -9.967 0.50 11.36 C ANISOU 501 CB BLEU A 61 1079 1895 1341 -411 -306 293 C ATOM 502 CG ALEU A 61 7.507 -27.467 -9.839 0.50 12.15 C ANISOU 502 CG ALEU A 61 1152 1953 1510 -525 -297 435 C ATOM 503 CG BLEU A 61 7.452 -27.403 -9.662 0.50 11.80 C ANISOU 503 CG BLEU A 61 1320 1901 1261 -421 -333 294 C ATOM 504 CD1ALEU A 61 7.878 -26.914 -11.207 0.50 12.81 C ANISOU 504 CD1ALEU A 61 1174 2070 1620 -817 -261 536 C ATOM 505 CD1BLEU A 61 8.824 -27.988 -9.362 0.50 11.24 C ANISOU 505 CD1BLEU A 61 1231 1942 1097 -508 -359 139 C ATOM 506 CD2ALEU A 61 7.043 -26.363 -8.903 0.50 13.10 C ANISOU 506 CD2ALEU A 61 1374 1867 1735 -549 -401 391 C ATOM 507 CD2BLEU A 61 7.526 -26.413 -10.813 0.50 14.15 C ANISOU 507 CD2BLEU A 61 1648 2164 1563 -626 -308 439 C ATOM 508 N LYS A 62 4.650 -28.833 -7.379 1.00 10.08 N ANISOU 508 N LYS A 62 940 1492 1395 -139 -396 240 N ATOM 509 CA ALYS A 62 4.136 -28.370 -6.090 0.50 10.92 C ANISOU 509 CA ALYS A 62 1038 1532 1577 -43 -294 182 C ATOM 510 CA BLYS A 62 4.145 -28.372 -6.092 0.50 10.44 C ANISOU 510 CA BLYS A 62 947 1493 1525 44 -408 221 C ATOM 511 C LYS A 62 4.449 -29.404 -5.009 1.00 9.30 C ANISOU 511 C LYS A 62 823 1274 1434 -31 -225 83 C ATOM 512 O LYS A 62 4.873 -29.058 -3.908 1.00 9.40 O ANISOU 512 O LYS A 62 968 1187 1415 -14 -279 64 O ATOM 513 CB ALYS A 62 2.622 -28.108 -6.157 0.50 11.66 C ANISOU 513 CB ALYS A 62 994 1675 1762 33 -423 156 C ATOM 514 CB BLYS A 62 2.640 -28.096 -6.172 0.50 10.96 C ANISOU 514 CB BLYS A 62 919 1557 1685 194 -613 246 C ATOM 515 CG ALYS A 62 2.201 -26.917 -7.021 0.50 12.98 C ANISOU 515 CG ALYS A 62 1296 1712 1922 35 -299 87 C ATOM 516 CG BLYS A 62 1.992 -27.856 -4.824 0.50 12.29 C ANISOU 516 CG BLYS A 62 1134 1687 1847 344 -450 142 C ATOM 517 CD ALYS A 62 0.679 -26.819 -7.121 0.50 14.47 C ANISOU 517 CD ALYS A 62 1393 2034 2070 165 -253 3 C ATOM 518 CD BLYS A 62 0.483 -27.704 -4.944 0.50 13.69 C ANISOU 518 CD BLYS A 62 1237 2060 1901 298 -470 17 C ATOM 519 CE ALYS A 62 0.249 -25.935 -8.283 0.50 16.95 C ANISOU 519 CE ALYS A 62 1870 2194 2374 161 -244 -16 C ATOM 520 CE BLYS A 62 0.116 -26.427 -5.671 0.50 15.89 C ANISOU 520 CE BLYS A 62 1487 2222 2327 545 -464 38 C ATOM 521 NZ ALYS A 62 -1.227 -25.958 -8.485 0.50 19.62 N ANISOU 521 NZ ALYS A 62 2016 2790 2646 226 -226 -177 N ATOM 522 NZ BLYS A 62 -1.339 -26.139 -5.565 0.50 16.57 N ANISOU 522 NZ BLYS A 62 1431 2515 2347 706 -325 -51 N ATOM 523 N LYS A 63 4.236 -30.674 -5.334 1.00 8.40 N ANISOU 523 N LYS A 63 697 1155 1339 -22 -139 127 N ATOM 524 CA LYS A 63 4.553 -31.765 -4.422 1.00 9.06 C ANISOU 524 CA LYS A 63 748 1253 1438 -149 -241 5 C ATOM 525 C LYS A 63 6.023 -31.717 -4.001 1.00 7.90 C ANISOU 525 C LYS A 63 846 921 1235 -146 -182 24 C ATOM 526 O LYS A 63 6.353 -31.810 -2.813 1.00 8.17 O ANISOU 526 O LYS A 63 841 997 1265 -132 -98 16 O ATOM 527 CB LYS A 63 4.234 -33.096 -5.099 1.00 8.96 C ANISOU 527 CB LYS A 63 768 1101 1535 -155 -220 69 C ATOM 528 CG LYS A 63 4.464 -34.319 -4.244 1.00 9.60 C ANISOU 528 CG LYS A 63 944 1155 1546 -183 -187 19 C ATOM 529 CD LYS A 63 4.140 -35.563 -5.067 1.00 10.72 C ANISOU 529 CD LYS A 63 1136 1310 1627 -306 -284 141 C ATOM 530 CE LYS A 63 4.375 -36.844 -4.300 1.00 11.97 C ANISOU 530 CE LYS A 63 1645 1195 1708 -248 -400 137 C ATOM 531 NZ LYS A 63 3.927 -38.019 -5.100 1.00 14.29 N ANISOU 531 NZ LYS A 63 2189 1356 1882 -554 -557 234 N ATOM 532 N HIS A 64 6.917 -31.579 -4.972 1.00 7.47 N ANISOU 532 N HIS A 64 637 1032 1168 -85 -229 -49 N ATOM 533 CA HIS A 64 8.323 -31.488 -4.623 1.00 7.87 C ANISOU 533 CA HIS A 64 699 1089 1203 -142 -149 20 C ATOM 534 C HIS A 64 8.628 -30.239 -3.792 1.00 7.61 C ANISOU 534 C HIS A 64 756 1075 1060 -29 -142 -24 C ATOM 535 O HIS A 64 9.447 -30.280 -2.878 1.00 7.82 O ANISOU 535 O HIS A 64 814 1167 989 -104 -181 116 O ATOM 536 CB HIS A 64 9.236 -31.571 -5.844 1.00 8.15 C ANISOU 536 CB HIS A 64 725 1173 1198 -66 -100 -73 C ATOM 537 CG HIS A 64 10.675 -31.751 -5.478 1.00 8.11 C ANISOU 537 CG HIS A 64 811 1142 1126 93 -251 -72 C ATOM 538 ND1 HIS A 64 11.148 -32.902 -4.885 1.00 8.55 N ANISOU 538 ND1 HIS A 64 792 1035 1419 29 -202 -1 N ATOM 539 CD2 HIS A 64 11.737 -30.916 -5.574 1.00 8.13 C ANISOU 539 CD2 HIS A 64 685 1340 1063 -18 -119 -40 C ATOM 540 CE1 HIS A 64 12.441 -32.772 -4.643 1.00 8.69 C ANISOU 540 CE1 HIS A 64 728 1202 1369 21 -215 -6 C ATOM 541 NE2 HIS A 64 12.824 -31.574 -5.048 1.00 8.44 N ANISOU 541 NE2 HIS A 64 690 1361 1154 -75 -169 -111 N ATOM 542 N GLY A 65 7.958 -29.134 -4.100 1.00 7.59 N ANISOU 542 N GLY A 65 762 975 1146 -206 -182 91 N ATOM 543 CA GLY A 65 8.100 -27.926 -3.297 1.00 8.63 C ANISOU 543 CA GLY A 65 882 1187 1209 -33 -286 -103 C ATOM 544 C GLY A 65 7.768 -28.183 -1.836 1.00 8.17 C ANISOU 544 C GLY A 65 802 1106 1192 16 -82 19 C ATOM 545 O GLY A 65 8.449 -27.691 -0.941 1.00 7.92 O ANISOU 545 O GLY A 65 885 956 1166 129 -197 -99 O ATOM 546 N THR A 66 6.712 -28.953 -1.593 1.00 8.24 N ANISOU 546 N THR A 66 808 1105 1216 56 -211 11 N ATOM 547 CA THR A 66 6.344 -29.341 -0.237 1.00 8.42 C ANISOU 547 CA THR A 66 672 1248 1277 -76 -78 -62 C ATOM 548 C THR A 66 7.445 -30.173 0.427 1.00 7.30 C ANISOU 548 C THR A 66 616 1158 997 -36 47 23 C ATOM 549 O THR A 66 7.792 -29.949 1.584 1.00 7.70 O ANISOU 549 O THR A 66 753 1142 1029 -112 -93 -30 O ATOM 550 CB THR A 66 5.024 -30.120 -0.234 1.00 10.08 C ANISOU 550 CB THR A 66 663 1667 1498 -70 -75 -96 C ATOM 551 OG1 THR A 66 3.975 -29.250 -0.677 1.00 12.55 O ANISOU 551 OG1 THR A 66 836 2083 1847 115 -206 -133 O ATOM 552 CG2 THR A 66 4.702 -30.628 1.164 1.00 11.73 C ANISOU 552 CG2 THR A 66 903 1919 1633 -234 115 0 C ATOM 553 N VAL A 67 7.996 -31.128 -0.312 1.00 7.18 N ANISOU 553 N VAL A 67 665 1039 1021 -20 -112 111 N ATOM 554 CA VAL A 67 9.077 -31.952 0.209 1.00 7.35 C ANISOU 554 CA VAL A 67 752 858 1181 -70 -64 96 C ATOM 555 C VAL A 67 10.279 -31.083 0.594 1.00 6.90 C ANISOU 555 C VAL A 67 783 783 1053 -22 -27 16 C ATOM 556 O VAL A 67 10.856 -31.231 1.678 1.00 7.08 O ANISOU 556 O VAL A 67 788 809 1090 -56 -204 74 O ATOM 557 CB VAL A 67 9.473 -33.051 -0.810 1.00 8.07 C ANISOU 557 CB VAL A 67 844 963 1258 -206 -95 -97 C ATOM 558 CG1 VAL A 67 10.786 -33.726 -0.414 1.00 8.96 C ANISOU 558 CG1 VAL A 67 1015 858 1531 3 -188 -73 C ATOM 559 CG2 VAL A 67 8.347 -34.079 -0.946 1.00 9.39 C ANISOU 559 CG2 VAL A 67 1184 963 1417 -425 -229 14 C ATOM 560 N VAL A 68 10.652 -30.173 -0.297 1.00 5.95 N ANISOU 560 N VAL A 68 604 694 963 -76 84 21 N ATOM 561 CA VAL A 68 11.805 -29.315 -0.069 1.00 6.45 C ANISOU 561 CA VAL A 68 714 846 891 -38 -54 -83 C ATOM 562 C VAL A 68 11.617 -28.428 1.160 1.00 6.27 C ANISOU 562 C VAL A 68 705 726 950 24 9 163 C ATOM 563 O VAL A 68 12.466 -28.395 2.055 1.00 6.97 O ANISOU 563 O VAL A 68 829 855 962 -39 -77 27 O ATOM 564 CB VAL A 68 12.086 -28.454 -1.313 1.00 7.09 C ANISOU 564 CB VAL A 68 714 997 982 -89 -168 -19 C ATOM 565 CG1 VAL A 68 13.106 -27.376 -1.007 1.00 7.44 C ANISOU 565 CG1 VAL A 68 893 1026 907 -114 -9 -67 C ATOM 566 CG2 VAL A 68 12.542 -29.339 -2.476 1.00 8.23 C ANISOU 566 CG2 VAL A 68 738 1238 1148 47 -40 -185 C ATOM 567 N LEU A 69 10.505 -27.705 1.215 1.00 7.00 N ANISOU 567 N LEU A 69 861 755 1042 25 -123 118 N ATOM 568 CA LEU A 69 10.303 -26.786 2.328 1.00 7.02 C ANISOU 568 CA LEU A 69 819 822 1026 86 19 -25 C ATOM 569 C LEU A 69 10.032 -27.500 3.648 1.00 7.14 C ANISOU 569 C LEU A 69 779 776 1154 95 -51 25 C ATOM 570 O LEU A 69 10.371 -26.984 4.707 1.00 7.71 O ANISOU 570 O LEU A 69 1044 805 1080 -72 -179 -12 O ATOM 571 CB LEU A 69 9.247 -25.723 2.011 1.00 8.42 C ANISOU 571 CB LEU A 69 1077 860 1261 163 -12 93 C ATOM 572 CG LEU A 69 9.622 -24.740 0.894 1.00 8.86 C ANISOU 572 CG LEU A 69 1183 891 1292 159 -31 112 C ATOM 573 CD1 LEU A 69 8.618 -23.594 0.826 1.00 10.67 C ANISOU 573 CD1 LEU A 69 1465 906 1681 530 -10 66 C ATOM 574 CD2 LEU A 69 11.031 -24.179 1.068 1.00 10.50 C ANISOU 574 CD2 LEU A 69 1478 1115 1397 -72 -81 103 C ATOM 575 N THR A 70 9.463 -28.699 3.593 1.00 7.14 N ANISOU 575 N THR A 70 819 934 959 36 -14 2 N ATOM 576 CA THR A 70 9.272 -29.476 4.816 1.00 7.81 C ANISOU 576 CA THR A 70 835 1037 1096 -214 -35 23 C ATOM 577 C THR A 70 10.635 -29.865 5.394 1.00 7.01 C ANISOU 577 C THR A 70 904 764 995 -176 2 156 C ATOM 578 O THR A 70 10.873 -29.771 6.602 1.00 7.05 O ANISOU 578 O THR A 70 929 854 894 -84 -34 30 O ATOM 579 CB THR A 70 8.436 -30.735 4.543 1.00 8.91 C ANISOU 579 CB THR A 70 977 1247 1159 -312 -192 105 C ATOM 580 OG1 THR A 70 7.118 -30.341 4.144 1.00 9.45 O ANISOU 580 OG1 THR A 70 818 1488 1283 -267 -55 -103 O ATOM 581 CG2 THR A 70 8.353 -31.611 5.781 1.00 11.09 C ANISOU 581 CG2 THR A 70 1397 1647 1167 -423 -95 142 C ATOM 582 N ALA A 71 11.548 -30.282 4.519 1.00 6.85 N ANISOU 582 N ALA A 71 907 680 1012 -61 -31 86 N ATOM 583 CA ALA A 71 12.897 -30.650 4.961 1.00 7.32 C ANISOU 583 CA ALA A 71 788 814 1178 -6 -171 -27 C ATOM 584 C ALA A 71 13.619 -29.428 5.540 1.00 7.84 C ANISOU 584 C ALA A 71 1038 826 1114 -73 -99 22 C ATOM 585 O ALA A 71 14.227 -29.493 6.619 1.00 7.68 O ANISOU 585 O ALA A 71 994 858 1064 -24 -114 48 O ATOM 586 CB ALA A 71 13.689 -31.247 3.809 1.00 8.00 C ANISOU 586 CB ALA A 71 1028 841 1170 -38 -165 25 C ATOM 587 N LEU A 72 13.559 -28.310 4.824 1.00 6.88 N ANISOU 587 N LEU A 72 805 734 1075 -29 -124 10 N ATOM 588 CA LEU A 72 14.208 -27.094 5.295 1.00 7.36 C ANISOU 588 CA LEU A 72 908 781 1106 -74 -91 90 C ATOM 589 C LEU A 72 13.630 -26.627 6.629 1.00 7.32 C ANISOU 589 C LEU A 72 905 818 1057 -93 -72 8 C ATOM 590 O LEU A 72 14.371 -26.220 7.528 1.00 7.37 O ANISOU 590 O LEU A 72 1028 829 942 -292 -204 107 O ATOM 591 CB LEU A 72 14.107 -25.985 4.247 1.00 7.16 C ANISOU 591 CB LEU A 72 939 849 931 -125 -108 172 C ATOM 592 CG LEU A 72 14.746 -24.653 4.650 1.00 7.98 C ANISOU 592 CG LEU A 72 1087 827 1114 -123 -127 86 C ATOM 593 CD1 LEU A 72 16.214 -24.810 5.057 1.00 8.99 C ANISOU 593 CD1 LEU A 72 1119 998 1297 -266 -199 48 C ATOM 594 CD2 LEU A 72 14.606 -23.630 3.524 1.00 8.89 C ANISOU 594 CD2 LEU A 72 1277 953 1147 -104 -145 187 C ATOM 595 N GLY A 73 12.311 -26.693 6.762 1.00 7.41 N ANISOU 595 N GLY A 73 1006 775 1033 -112 -75 84 N ATOM 596 CA GLY A 73 11.647 -26.289 7.998 1.00 8.17 C ANISOU 596 CA GLY A 73 942 1135 1024 -105 -35 21 C ATOM 597 C GLY A 73 12.083 -27.120 9.191 1.00 8.94 C ANISOU 597 C GLY A 73 1023 1166 1206 -318 -83 54 C ATOM 598 O GLY A 73 12.290 -26.594 10.283 1.00 9.44 O ANISOU 598 O GLY A 73 1019 1462 1104 -303 -14 -7 O ATOM 599 N GLY A 74 12.215 -28.427 8.986 1.00 9.02 N ANISOU 599 N GLY A 74 1230 1083 1115 -413 -239 54 N ATOM 600 CA GLY A 74 12.702 -29.311 10.046 1.00 9.87 C ANISOU 600 CA GLY A 74 1270 1314 1165 -489 -260 189 C ATOM 601 C GLY A 74 14.098 -28.911 10.475 1.00 9.27 C ANISOU 601 C GLY A 74 1294 1073 1153 -283 -272 141 C ATOM 602 O GLY A 74 14.413 -28.884 11.661 1.00 11.02 O ANISOU 602 O GLY A 74 1406 1530 1252 -379 -368 181 O ATOM 603 N ILE A 75 14.939 -28.585 9.499 1.00 8.35 N ANISOU 603 N ILE A 75 1040 1040 1090 -160 -176 57 N ATOM 604 CA ILE A 75 16.291 -28.119 9.789 1.00 8.36 C ANISOU 604 CA ILE A 75 1101 917 1158 6 -176 49 C ATOM 605 C ILE A 75 16.276 -26.799 10.567 1.00 7.79 C ANISOU 605 C ILE A 75 869 1062 1026 24 -100 52 C ATOM 606 O ILE A 75 16.948 -26.667 11.596 1.00 8.29 O ANISOU 606 O ILE A 75 875 1264 1011 -24 -182 -11 O ATOM 607 CB ILE A 75 17.132 -28.033 8.498 1.00 8.60 C ANISOU 607 CB ILE A 75 1259 867 1141 114 -236 -48 C ATOM 608 CG1 ILE A 75 17.476 -29.446 8.015 1.00 10.73 C ANISOU 608 CG1 ILE A 75 1416 1156 1506 193 -179 -261 C ATOM 609 CG2 ILE A 75 18.384 -27.185 8.710 1.00 9.78 C ANISOU 609 CG2 ILE A 75 1151 1133 1430 -100 -115 -40 C ATOM 610 CD1 ILE A 75 17.980 -29.513 6.590 1.00 12.71 C ANISOU 610 CD1 ILE A 75 1707 1445 1674 297 -23 -483 C ATOM 611 N LEU A 76 15.492 -25.833 10.098 1.00 7.24 N ANISOU 611 N LEU A 76 853 815 1083 -130 -106 8 N ATOM 612 CA LEU A 76 15.452 -24.529 10.754 1.00 7.91 C ANISOU 612 CA LEU A 76 1001 918 1085 -118 -32 -60 C ATOM 613 C LEU A 76 14.981 -24.628 12.196 1.00 7.95 C ANISOU 613 C LEU A 76 786 933 1301 -109 -59 -28 C ATOM 614 O LEU A 76 15.487 -23.920 13.069 1.00 8.30 O ANISOU 614 O LEU A 76 988 1026 1137 64 -187 -83 O ATOM 615 CB LEU A 76 14.572 -23.556 9.978 1.00 8.45 C ANISOU 615 CB LEU A 76 1050 954 1203 -138 -136 -54 C ATOM 616 CG LEU A 76 15.078 -23.139 8.596 1.00 9.16 C ANISOU 616 CG LEU A 76 1262 1048 1168 -173 -94 -13 C ATOM 617 CD1 LEU A 76 14.035 -22.288 7.894 1.00 11.05 C ANISOU 617 CD1 LEU A 76 1644 1131 1420 80 -123 134 C ATOM 618 CD2 LEU A 76 16.399 -22.383 8.703 1.00 11.05 C ANISOU 618 CD2 LEU A 76 1442 1283 1473 -426 -85 111 C ATOM 619 N LYS A 77 14.025 -25.512 12.456 1.00 8.51 N ANISOU 619 N LYS A 77 976 1065 1190 -22 59 15 N ATOM 620 CA LYS A 77 13.516 -25.671 13.810 1.00 9.36 C ANISOU 620 CA LYS A 77 953 1318 1282 -15 -11 113 C ATOM 621 C LYS A 77 14.530 -26.257 14.786 1.00 9.04 C ANISOU 621 C LYS A 77 1006 1187 1238 -93 -90 -92 C ATOM 622 O LYS A 77 14.334 -26.179 15.994 1.00 10.08 O ANISOU 622 O LYS A 77 1207 1521 1100 94 -6 17 O ATOM 623 CB LYS A 77 12.190 -26.425 13.808 1.00 11.08 C ANISOU 623 CB LYS A 77 910 1774 1523 -49 -79 226 C ATOM 624 CG LYS A 77 11.080 -25.611 13.152 1.00 12.86 C ANISOU 624 CG LYS A 77 1176 2197 1514 -36 -253 284 C ATOM 625 CD LYS A 77 9.747 -26.312 13.160 1.00 14.57 C ANISOU 625 CD LYS A 77 1297 2519 1720 -124 -243 426 C ATOM 626 CE LYS A 77 8.724 -25.482 12.411 1.00 14.96 C ANISOU 626 CE LYS A 77 1412 2548 1724 -30 -252 352 C ATOM 627 NZ LYS A 77 7.376 -26.085 12.489 1.00 17.21 N ANISOU 627 NZ LYS A 77 1467 3061 2011 -261 -80 319 N ATOM 628 N LYS A 78 15.617 -26.822 14.261 1.00 7.97 N ANISOU 628 N LYS A 78 763 1022 1240 31 -61 2 N ATOM 629 CA LYS A 78 16.724 -27.274 15.110 1.00 8.69 C ANISOU 629 CA LYS A 78 972 1106 1221 87 -24 -10 C ATOM 630 C LYS A 78 17.644 -26.133 15.543 1.00 8.97 C ANISOU 630 C LYS A 78 950 1191 1266 77 -51 27 C ATOM 631 O LYS A 78 18.532 -26.329 16.372 1.00 9.46 O ANISOU 631 O LYS A 78 930 1422 1242 75 -146 -49 O ATOM 632 CB LYS A 78 17.527 -28.375 14.421 1.00 10.13 C ANISOU 632 CB LYS A 78 1273 1148 1428 157 -53 -29 C ATOM 633 CG LYS A 78 16.807 -29.728 14.385 1.00 13.54 C ANISOU 633 CG LYS A 78 1654 1463 2027 191 -176 -99 C ATOM 634 CD LYS A 78 16.581 -30.255 15.805 1.00 18.62 C ANISOU 634 CD LYS A 78 2464 2061 2546 -152 244 88 C ATOM 635 CE LYS A 78 16.535 -31.776 15.863 1.00 23.12 C ANISOU 635 CE LYS A 78 3079 2687 3016 -64 78 118 C ATOM 636 NZ LYS A 78 15.355 -32.341 15.154 1.00 24.93 N ANISOU 636 NZ LYS A 78 3180 3156 3133 -88 19 31 N ATOM 637 N LYS A 79 17.449 -24.951 14.966 1.00 8.15 N ANISOU 637 N LYS A 79 858 1014 1222 -18 -7 -77 N ATOM 638 CA ALYS A 79 18.191 -23.766 15.380 0.50 9.00 C ANISOU 638 CA ALYS A 79 796 1285 1335 48 -32 -76 C ATOM 639 CA BLYS A 79 18.194 -23.764 15.370 0.50 8.82 C ANISOU 639 CA BLYS A 79 792 1264 1293 93 -65 -18 C ATOM 640 C LYS A 79 19.696 -24.025 15.384 1.00 9.13 C ANISOU 640 C LYS A 79 808 1310 1350 78 -101 5 C ATOM 641 O LYS A 79 20.397 -23.712 16.353 1.00 9.55 O ANISOU 641 O LYS A 79 1004 1303 1319 143 -117 -175 O ATOM 642 CB ALYS A 79 17.711 -23.283 16.754 0.50 9.60 C ANISOU 642 CB ALYS A 79 851 1369 1427 -48 7 -42 C ATOM 643 CB BLYS A 79 17.706 -23.249 16.728 0.50 9.02 C ANISOU 643 CB BLYS A 79 834 1293 1300 103 -78 127 C ATOM 644 CG ALYS A 79 16.258 -22.812 16.757 0.50 9.68 C ANISOU 644 CG ALYS A 79 864 1295 1518 -10 105 -200 C ATOM 645 CG BLYS A 79 16.219 -22.907 16.743 0.50 8.87 C ANISOU 645 CG BLYS A 79 843 1210 1316 237 -66 94 C ATOM 646 CD ALYS A 79 15.694 -22.691 18.169 0.50 9.91 C ANISOU 646 CD ALYS A 79 882 1376 1506 -55 232 -98 C ATOM 647 CD BLYS A 79 15.823 -22.129 17.989 0.50 8.02 C ANISOU 647 CD BLYS A 79 792 1160 1096 356 -18 351 C ATOM 648 CE ALYS A 79 16.371 -21.577 18.953 0.50 10.62 C ANISOU 648 CE ALYS A 79 938 1508 1589 -54 326 -116 C ATOM 649 CE BLYS A 79 16.104 -22.919 19.254 0.50 8.96 C ANISOU 649 CE BLYS A 79 929 1268 1205 273 141 412 C ATOM 650 NZ ALYS A 79 15.861 -21.492 20.355 0.50 10.81 N ANISOU 650 NZ ALYS A 79 1121 1486 1500 91 313 4 N ATOM 651 NZ BLYS A 79 15.656 -22.167 20.461 0.50 8.11 N ANISOU 651 NZ BLYS A 79 863 1148 1069 205 114 410 N ATOM 652 N GLY A 80 20.190 -24.595 14.289 1.00 9.28 N ANISOU 652 N GLY A 80 971 1103 1449 132 -12 -188 N ATOM 653 CA GLY A 80 21.622 -24.811 14.133 1.00 10.59 C ANISOU 653 CA GLY A 80 1026 1324 1674 197 -103 -155 C ATOM 654 C GLY A 80 22.104 -26.182 14.565 1.00 10.99 C ANISOU 654 C GLY A 80 1242 1408 1523 294 -135 -118 C ATOM 655 O GLY A 80 23.167 -26.623 14.139 1.00 11.67 O ANISOU 655 O GLY A 80 1053 1646 1735 338 91 -140 O ATOM 656 N HIS A 81 21.333 -26.854 15.415 1.00 10.35 N ANISOU 656 N HIS A 81 1269 1399 1262 344 -25 -129 N ATOM 657 CA HIS A 81 21.696 -28.187 15.898 1.00 10.94 C ANISOU 657 CA HIS A 81 1462 1466 1229 263 -50 -83 C ATOM 658 C HIS A 81 21.157 -29.244 14.957 1.00 9.32 C ANISOU 658 C HIS A 81 1073 1140 1328 284 -189 101 C ATOM 659 O HIS A 81 20.329 -30.069 15.342 1.00 11.36 O ANISOU 659 O HIS A 81 1355 1533 1426 340 36 234 O ATOM 660 CB HIS A 81 21.123 -28.416 17.292 1.00 14.14 C ANISOU 660 CB HIS A 81 1942 1940 1490 288 -48 26 C ATOM 661 CG HIS A 81 21.607 -27.432 18.304 1.00 17.26 C ANISOU 661 CG HIS A 81 2193 2498 1865 199 -358 -114 C ATOM 662 ND1 HIS A 81 22.822 -27.558 18.940 1.00 20.86 N ANISOU 662 ND1 HIS A 81 2522 2987 2413 139 -473 -236 N ATOM 663 CD2 HIS A 81 21.045 -26.299 18.785 1.00 18.41 C ANISOU 663 CD2 HIS A 81 2318 2634 2042 166 -366 -333 C ATOM 664 CE1 HIS A 81 22.985 -26.549 19.776 1.00 20.81 C ANISOU 664 CE1 HIS A 81 2598 2989 2320 123 -505 -382 C ATOM 665 NE2 HIS A 81 21.921 -25.770 19.701 1.00 20.35 N ANISOU 665 NE2 HIS A 81 2392 3043 2295 11 -529 -356 N ATOM 666 N HIS A 82 21.641 -29.211 13.722 1.00 9.28 N ANISOU 666 N HIS A 82 1108 1194 1225 35 12 -89 N ATOM 667 CA HIS A 82 20.990 -29.911 12.629 1.00 9.11 C ANISOU 667 CA HIS A 82 1099 1132 1230 72 13 -74 C ATOM 668 C HIS A 82 21.898 -30.904 11.919 1.00 8.53 C ANISOU 668 C HIS A 82 937 1062 1241 43 67 8 C ATOM 669 O HIS A 82 21.616 -31.295 10.794 1.00 8.61 O ANISOU 669 O HIS A 82 1161 965 1143 58 -30 -78 O ATOM 670 CB HIS A 82 20.427 -28.909 11.615 1.00 9.51 C ANISOU 670 CB HIS A 82 967 1207 1439 31 27 -13 C ATOM 671 CG HIS A 82 21.437 -27.925 11.111 1.00 8.47 C ANISOU 671 CG HIS A 82 931 999 1288 19 79 -51 C ATOM 672 ND1 HIS A 82 21.139 -26.594 10.909 1.00 9.51 N ANISOU 672 ND1 HIS A 82 1101 1153 1360 27 251 -213 N ATOM 673 CD2 HIS A 82 22.738 -28.077 10.768 1.00 8.92 C ANISOU 673 CD2 HIS A 82 1020 1097 1269 -131 73 -9 C ATOM 674 CE1 HIS A 82 22.215 -25.968 10.462 1.00 9.05 C ANISOU 674 CE1 HIS A 82 1049 944 1442 -136 259 -131 C ATOM 675 NE2 HIS A 82 23.201 -26.844 10.372 1.00 9.28 N ANISOU 675 NE2 HIS A 82 1250 1012 1262 -134 186 -183 N ATOM 676 N GLU A 83 22.978 -31.323 12.568 1.00 8.31 N ANISOU 676 N GLU A 83 902 1185 1067 75 18 -16 N ATOM 677 CA GLU A 83 23.910 -32.240 11.918 1.00 9.38 C ANISOU 677 CA GLU A 83 1091 1321 1150 177 -89 2 C ATOM 678 C GLU A 83 23.228 -33.483 11.340 1.00 9.35 C ANISOU 678 C GLU A 83 1268 1159 1123 215 22 103 C ATOM 679 O GLU A 83 23.470 -33.851 10.192 1.00 9.98 O ANISOU 679 O GLU A 83 1572 1090 1126 223 -17 79 O ATOM 680 CB GLU A 83 25.039 -32.634 12.874 1.00 11.12 C ANISOU 680 CB GLU A 83 1185 1721 1317 361 -117 164 C ATOM 681 CG GLU A 83 25.873 -33.818 12.402 1.00 12.57 C ANISOU 681 CG GLU A 83 1410 1819 1547 399 -11 240 C ATOM 682 CD GLU A 83 26.782 -33.493 11.226 1.00 12.83 C ANISOU 682 CD GLU A 83 1486 1869 1521 341 43 308 C ATOM 683 OE1 GLU A 83 27.011 -32.301 10.940 1.00 13.93 O ANISOU 683 OE1 GLU A 83 1474 1982 1834 155 167 255 O ATOM 684 OE2 GLU A 83 27.285 -34.443 10.596 1.00 14.57 O ANISOU 684 OE2 GLU A 83 1679 2047 1808 323 226 195 O ATOM 685 N ALA A 84 22.374 -34.127 12.130 1.00 10.06 N ANISOU 685 N ALA A 84 1418 1102 1303 189 31 100 N ATOM 686 CA ALA A 84 21.751 -35.381 11.711 1.00 9.96 C ANISOU 686 CA ALA A 84 1645 977 1160 17 13 211 C ATOM 687 C ALA A 84 20.799 -35.176 10.533 1.00 9.87 C ANISOU 687 C ALA A 84 1555 1018 1177 -126 22 132 C ATOM 688 O ALA A 84 20.650 -36.047 9.672 1.00 10.40 O ANISOU 688 O ALA A 84 1811 898 1241 15 -63 56 O ATOM 689 CB ALA A 84 21.022 -36.036 12.883 1.00 13.69 C ANISOU 689 CB ALA A 84 2320 1431 1448 -90 96 258 C ATOM 690 N GLU A 85 20.157 -34.016 10.495 1.00 8.97 N ANISOU 690 N GLU A 85 1105 1001 1301 -97 55 87 N ATOM 691 CA GLU A 85 19.201 -33.682 9.443 1.00 10.12 C ANISOU 691 CA GLU A 85 1152 1251 1439 -166 -36 -4 C ATOM 692 C GLU A 85 19.928 -33.236 8.177 1.00 9.82 C ANISOU 692 C GLU A 85 1203 1061 1465 -253 -71 19 C ATOM 693 O GLU A 85 19.510 -33.546 7.062 1.00 11.46 O ANISOU 693 O GLU A 85 1648 1219 1485 -400 -171 128 O ATOM 694 CB GLU A 85 18.282 -32.542 9.908 1.00 11.34 C ANISOU 694 CB GLU A 85 1282 1450 1574 -85 -43 -137 C ATOM 695 CG GLU A 85 17.263 -32.901 10.980 1.00 13.10 C ANISOU 695 CG GLU A 85 1372 1716 1885 -254 181 -22 C ATOM 696 CD GLU A 85 17.822 -32.912 12.397 1.00 13.39 C ANISOU 696 CD GLU A 85 1462 1656 1969 -235 300 -21 C ATOM 697 OE1 GLU A 85 18.989 -32.515 12.618 1.00 11.83 O ANISOU 697 OE1 GLU A 85 1419 1565 1507 -38 299 -146 O ATOM 698 OE2 GLU A 85 17.065 -33.308 13.308 1.00 16.68 O ANISOU 698 OE2 GLU A 85 1931 2327 2078 -299 422 125 O ATOM 699 N LEU A 86 21.006 -32.487 8.359 1.00 9.53 N ANISOU 699 N LEU A 86 1257 1034 1327 -113 -49 98 N ATOM 700 CA LEU A 86 21.649 -31.817 7.253 1.00 9.34 C ANISOU 700 CA LEU A 86 1353 1068 1127 -106 165 53 C ATOM 701 C LEU A 86 22.653 -32.722 6.540 1.00 8.93 C ANISOU 701 C LEU A 86 1265 1010 1116 -63 39 167 C ATOM 702 O LEU A 86 22.742 -32.706 5.312 1.00 10.59 O ANISOU 702 O LEU A 86 1628 1372 1022 96 188 191 O ATOM 703 CB LEU A 86 22.304 -30.526 7.749 1.00 10.38 C ANISOU 703 CB LEU A 86 1366 1299 1278 -163 205 43 C ATOM 704 CG LEU A 86 22.970 -29.647 6.697 1.00 10.65 C ANISOU 704 CG LEU A 86 1373 1226 1447 -86 221 152 C ATOM 705 CD1 LEU A 86 22.852 -28.174 7.062 1.00 11.89 C ANISOU 705 CD1 LEU A 86 1672 1278 1565 -241 282 165 C ATOM 706 CD2 LEU A 86 24.427 -30.047 6.497 1.00 11.84 C ANISOU 706 CD2 LEU A 86 1398 1510 1588 21 269 163 C ATOM 707 N LYS A 87 23.405 -33.521 7.293 1.00 9.72 N ANISOU 707 N LYS A 87 1179 1329 1182 144 38 131 N ATOM 708 CA LYS A 87 24.409 -34.373 6.666 1.00 10.36 C ANISOU 708 CA LYS A 87 1342 1435 1160 196 -67 67 C ATOM 709 C LYS A 87 23.864 -35.215 5.501 1.00 9.55 C ANISOU 709 C LYS A 87 1284 1128 1214 200 -21 144 C ATOM 710 O LYS A 87 24.421 -35.186 4.408 1.00 9.56 O ANISOU 710 O LYS A 87 1118 1439 1073 179 70 154 O ATOM 711 CB LYS A 87 25.153 -35.242 7.686 1.00 10.94 C ANISOU 711 CB LYS A 87 1268 1680 1208 253 -101 33 C ATOM 712 CG LYS A 87 26.213 -36.130 7.035 1.00 12.11 C ANISOU 712 CG LYS A 87 1487 1752 1359 381 -80 9 C ATOM 713 CD LYS A 87 26.859 -37.071 8.034 1.00 13.81 C ANISOU 713 CD LYS A 87 1755 1833 1658 532 -7 12 C ATOM 714 CE LYS A 87 27.822 -38.026 7.338 1.00 15.74 C ANISOU 714 CE LYS A 87 2073 1996 1909 732 -2 49 C ATOM 715 NZ LYS A 87 28.413 -39.006 8.295 1.00 17.63 N ANISOU 715 NZ LYS A 87 2613 2228 1858 875 -195 159 N ATOM 716 N PRO A 88 22.792 -35.989 5.734 1.00 9.40 N ANISOU 716 N PRO A 88 1220 1220 1128 97 148 183 N ATOM 717 CA PRO A 88 22.235 -36.823 4.662 1.00 9.57 C ANISOU 717 CA PRO A 88 1260 1101 1274 -1 198 309 C ATOM 718 C PRO A 88 21.743 -36.024 3.451 1.00 9.35 C ANISOU 718 C PRO A 88 1051 1042 1460 14 203 283 C ATOM 719 O PRO A 88 21.854 -36.487 2.313 1.00 8.87 O ANISOU 719 O PRO A 88 926 1047 1396 95 42 258 O ATOM 720 CB PRO A 88 21.077 -37.561 5.345 1.00 12.17 C ANISOU 720 CB PRO A 88 1796 1301 1526 -211 405 120 C ATOM 721 CG PRO A 88 20.772 -36.751 6.569 1.00 10.60 C ANISOU 721 CG PRO A 88 1597 1151 1280 -269 307 -51 C ATOM 722 CD PRO A 88 22.083 -36.186 7.008 1.00 10.98 C ANISOU 722 CD PRO A 88 1550 1319 1302 -234 258 58 C ATOM 723 N LEU A 89 21.198 -34.838 3.687 1.00 8.50 N ANISOU 723 N LEU A 89 885 913 1429 2 41 246 N ATOM 724 CA ALEU A 89 20.749 -33.965 2.605 0.50 9.31 C ANISOU 724 CA ALEU A 89 956 1020 1559 36 -56 127 C ATOM 725 CA BLEU A 89 20.758 -33.999 2.579 0.50 9.53 C ANISOU 725 CA BLEU A 89 1001 1062 1559 -10 -135 121 C ATOM 726 C LEU A 89 21.946 -33.489 1.779 1.00 8.61 C ANISOU 726 C LEU A 89 1029 903 1336 90 -172 291 C ATOM 727 O LEU A 89 21.924 -33.493 0.547 1.00 8.98 O ANISOU 727 O LEU A 89 1129 879 1402 8 -374 90 O ATOM 728 CB ALEU A 89 20.012 -32.762 3.195 0.50 10.06 C ANISOU 728 CB ALEU A 89 972 1021 1826 120 -32 81 C ATOM 729 CB BLEU A 89 19.892 -32.841 3.069 0.50 11.25 C ANISOU 729 CB BLEU A 89 1175 1185 1913 85 -214 0 C ATOM 730 CG ALEU A 89 19.214 -31.885 2.232 0.50 9.76 C ANISOU 730 CG ALEU A 89 929 1144 1635 192 56 108 C ATOM 731 CG BLEU A 89 18.411 -33.177 3.242 0.50 12.31 C ANISOU 731 CG BLEU A 89 1294 1454 1928 81 -310 -10 C ATOM 732 CD1ALEU A 89 18.069 -32.681 1.617 0.50 11.29 C ANISOU 732 CD1ALEU A 89 1269 1253 1767 143 -107 -26 C ATOM 733 CD1BLEU A 89 17.673 -31.962 3.771 0.50 13.81 C ANISOU 733 CD1BLEU A 89 1505 1701 2040 270 -244 -94 C ATOM 734 CD2ALEU A 89 18.671 -30.669 2.967 0.50 11.31 C ANISOU 734 CD2ALEU A 89 1154 1306 1835 354 -38 50 C ATOM 735 CD2BLEU A 89 17.798 -33.652 1.926 0.50 13.06 C ANISOU 735 CD2BLEU A 89 1305 1748 1909 16 -360 57 C ATOM 736 N ALA A 90 22.996 -33.070 2.471 1.00 7.95 N ANISOU 736 N ALA A 90 890 867 1262 -76 -194 226 N ATOM 737 CA ALA A 90 24.189 -32.627 1.785 1.00 8.79 C ANISOU 737 CA ALA A 90 970 1176 1192 -179 -81 112 C ATOM 738 C ALA A 90 24.748 -33.767 0.955 1.00 8.10 C ANISOU 738 C ALA A 90 789 1188 1101 -35 -153 241 C ATOM 739 O ALA A 90 25.117 -33.590 -0.202 1.00 9.29 O ANISOU 739 O ALA A 90 1127 1294 1108 -273 -79 133 O ATOM 740 CB ALA A 90 25.215 -32.150 2.783 1.00 10.01 C ANISOU 740 CB ALA A 90 1170 1238 1393 -319 -165 -52 C ATOM 741 N GLN A 91 24.800 -34.954 1.543 1.00 8.29 N ANISOU 741 N GLN A 91 732 1134 1280 199 -96 92 N ATOM 742 CA GLN A 91 25.391 -36.072 0.838 1.00 9.05 C ANISOU 742 CA GLN A 91 840 1274 1321 190 -142 100 C ATOM 743 C GLN A 91 24.565 -36.551 -0.358 1.00 8.54 C ANISOU 743 C GLN A 91 753 1130 1360 68 15 193 C ATOM 744 O GLN A 91 25.119 -36.891 -1.398 1.00 9.31 O ANISOU 744 O GLN A 91 1037 1233 1267 216 -9 45 O ATOM 745 CB GLN A 91 25.755 -37.180 1.813 1.00 10.51 C ANISOU 745 CB GLN A 91 1128 1339 1527 349 -107 157 C ATOM 746 CG GLN A 91 26.857 -36.732 2.778 1.00 11.64 C ANISOU 746 CG GLN A 91 1182 1664 1576 315 -72 285 C ATOM 747 CD GLN A 91 27.568 -37.876 3.449 1.00 13.51 C ANISOU 747 CD GLN A 91 1358 1684 2089 326 -196 356 C ATOM 748 OE1 GLN A 91 26.988 -38.939 3.680 1.00 15.26 O ANISOU 748 OE1 GLN A 91 1721 1804 2271 104 -112 749 O ATOM 749 NE2 GLN A 91 28.837 -37.665 3.778 1.00 14.19 N ANISOU 749 NE2 GLN A 91 1283 1968 2137 400 -286 181 N ATOM 750 N SER A 92 23.243 -36.557 -0.237 1.00 8.15 N ANISOU 750 N SER A 92 696 1008 1391 23 -60 157 N ATOM 751 CA ASER A 92 22.430 -36.938 -1.384 0.50 8.01 C ANISOU 751 CA ASER A 92 666 975 1403 -43 75 210 C ATOM 752 CA BSER A 92 22.385 -36.911 -1.361 0.50 9.71 C ANISOU 752 CA BSER A 92 960 1179 1548 -86 -2 211 C ATOM 753 C SER A 92 22.545 -35.889 -2.487 1.00 8.09 C ANISOU 753 C SER A 92 734 1089 1248 6 -96 107 C ATOM 754 O SER A 92 22.611 -36.230 -3.668 1.00 8.76 O ANISOU 754 O SER A 92 923 1050 1352 65 -23 -5 O ATOM 755 CB ASER A 92 20.969 -37.176 -0.997 0.50 8.22 C ANISOU 755 CB ASER A 92 552 1025 1544 -115 158 187 C ATOM 756 CB BSER A 92 20.928 -36.958 -0.898 0.50 12.67 C ANISOU 756 CB BSER A 92 1192 1645 1975 -227 45 203 C ATOM 757 OG ASER A 92 20.293 -35.952 -0.784 0.50 5.73 O ANISOU 757 OG ASER A 92 456 656 1065 38 191 40 O ATOM 758 OG BSER A 92 20.052 -37.142 -1.989 0.50 15.78 O ANISOU 758 OG BSER A 92 1905 1917 2173 -291 -66 29 O ATOM 759 N HIS A 93 22.605 -34.617 -2.109 1.00 7.84 N ANISOU 759 N HIS A 93 805 954 1219 42 -102 118 N ATOM 760 CA HIS A 93 22.696 -33.566 -3.106 1.00 8.18 C ANISOU 760 CA HIS A 93 805 1028 1272 30 -5 97 C ATOM 761 C HIS A 93 24.029 -33.524 -3.838 1.00 7.79 C ANISOU 761 C HIS A 93 777 1027 1156 70 -14 158 C ATOM 762 O HIS A 93 24.075 -33.226 -5.026 1.00 8.94 O ANISOU 762 O HIS A 93 1089 1182 1126 54 19 55 O ATOM 763 CB HIS A 93 22.210 -32.227 -2.554 1.00 8.07 C ANISOU 763 CB HIS A 93 802 1039 1222 22 -26 162 C ATOM 764 CG HIS A 93 20.716 -32.158 -2.454 1.00 7.17 C ANISOU 764 CG HIS A 93 585 1071 1067 -78 -57 185 C ATOM 765 ND1 HIS A 93 19.989 -32.957 -1.594 1.00 8.95 N ANISOU 765 ND1 HIS A 93 669 1451 1280 71 -81 391 N ATOM 766 CD2 HIS A 93 19.808 -31.442 -3.156 1.00 7.13 C ANISOU 766 CD2 HIS A 93 535 1041 1131 121 -64 172 C ATOM 767 CE1 HIS A 93 18.699 -32.713 -1.757 1.00 9.23 C ANISOU 767 CE1 HIS A 93 702 1557 1248 110 -237 347 C ATOM 768 NE2 HIS A 93 18.561 -31.801 -2.703 1.00 7.63 N ANISOU 768 NE2 HIS A 93 728 1075 1095 36 -140 114 N ATOM 769 N ALA A 94 25.108 -33.880 -3.145 1.00 7.58 N ANISOU 769 N ALA A 94 621 1145 1114 -3 -29 99 N ATOM 770 CA ALA A 94 26.402 -33.971 -3.801 1.00 9.07 C ANISOU 770 CA ALA A 94 853 1394 1199 21 73 -38 C ATOM 771 C ALA A 94 26.527 -35.242 -4.633 1.00 10.90 C ANISOU 771 C ALA A 94 1258 1397 1486 132 64 -74 C ATOM 772 O ALA A 94 26.789 -35.196 -5.832 1.00 13.12 O ANISOU 772 O ALA A 94 1930 1501 1551 30 420 -179 O ATOM 773 CB ALA A 94 27.525 -33.919 -2.773 1.00 9.35 C ANISOU 773 CB ALA A 94 743 1577 1229 70 -86 -43 C ATOM 774 N THR A 95 26.308 -36.382 -3.995 1.00 10.95 N ANISOU 774 N THR A 95 1289 1424 1446 246 94 -118 N ATOM 775 CA ATHR A 95 26.665 -37.649 -4.605 0.50 11.77 C ANISOU 775 CA ATHR A 95 1370 1506 1594 269 106 -154 C ATOM 776 CA BTHR A 95 26.654 -37.673 -4.585 0.50 12.42 C ANISOU 776 CA BTHR A 95 1505 1601 1611 239 70 -159 C ATOM 777 C THR A 95 25.620 -38.191 -5.572 1.00 12.92 C ANISOU 777 C THR A 95 1609 1531 1767 192 40 -190 C ATOM 778 O THR A 95 25.964 -38.740 -6.620 1.00 15.17 O ANISOU 778 O THR A 95 1866 2013 1882 142 91 -335 O ATOM 779 CB ATHR A 95 27.039 -38.685 -3.538 0.50 12.57 C ANISOU 779 CB ATHR A 95 1398 1671 1706 409 95 -119 C ATOM 780 CB BTHR A 95 26.886 -38.739 -3.497 0.50 13.90 C ANISOU 780 CB BTHR A 95 1688 1845 1748 330 41 -79 C ATOM 781 OG1ATHR A 95 28.000 -38.109 -2.641 0.50 13.43 O ANISOU 781 OG1ATHR A 95 1110 1998 1992 474 -36 -160 O ATOM 782 OG1BTHR A 95 25.630 -39.120 -2.918 0.50 14.73 O ANISOU 782 OG1BTHR A 95 1920 1887 1789 140 35 -97 O ATOM 783 CG2ATHR A 95 27.641 -39.914 -4.185 0.50 13.22 C ANISOU 783 CG2ATHR A 95 1494 1723 1805 613 278 -165 C ATOM 784 CG2BTHR A 95 27.808 -38.198 -2.408 0.50 15.23 C ANISOU 784 CG2BTHR A 95 1624 2217 1945 441 -42 -130 C ATOM 785 N LYS A 96 24.350 -38.027 -5.235 1.00 12.38 N ANISOU 785 N LYS A 96 1540 1353 1809 69 -57 -112 N ATOM 786 CA LYS A 96 23.299 -38.539 -6.100 1.00 13.91 C ANISOU 786 CA LYS A 96 1869 1542 1874 11 -88 -166 C ATOM 787 C LYS A 96 22.838 -37.494 -7.109 1.00 12.58 C ANISOU 787 C LYS A 96 1679 1534 1565 33 -75 -186 C ATOM 788 O LYS A 96 22.813 -37.751 -8.310 1.00 14.52 O ANISOU 788 O LYS A 96 2123 1725 1668 76 -294 -442 O ATOM 789 CB LYS A 96 22.114 -39.062 -5.285 1.00 16.61 C ANISOU 789 CB LYS A 96 2171 1843 2296 -235 -52 -138 C ATOM 790 CG LYS A 96 21.058 -39.725 -6.149 1.00 19.52 C ANISOU 790 CG LYS A 96 2700 2219 2496 -305 -112 -228 C ATOM 791 CD LYS A 96 20.129 -40.620 -5.360 1.00 22.40 C ANISOU 791 CD LYS A 96 3014 2701 2795 -464 -72 -239 C ATOM 792 CE LYS A 96 19.565 -41.686 -6.280 1.00 24.04 C ANISOU 792 CE LYS A 96 3283 2901 2949 -679 56 -355 C ATOM 793 NZ LYS A 96 19.281 -41.106 -7.626 1.00 26.57 N ANISOU 793 NZ LYS A 96 3354 3492 3247 -604 -2 -400 N ATOM 794 N HIS A 97 22.500 -36.305 -6.622 1.00 9.71 N ANISOU 794 N HIS A 97 1066 1268 1355 126 -139 -279 N ATOM 795 CA HIS A 97 21.848 -35.304 -7.460 1.00 10.11 C ANISOU 795 CA HIS A 97 1156 1366 1319 116 -11 -53 C ATOM 796 C HIS A 97 22.824 -34.387 -8.182 1.00 9.90 C ANISOU 796 C HIS A 97 974 1542 1244 86 6 -27 C ATOM 797 O HIS A 97 22.456 -33.740 -9.163 1.00 10.72 O ANISOU 797 O HIS A 97 1146 1615 1310 35 65 26 O ATOM 798 CB HIS A 97 20.820 -34.495 -6.662 1.00 9.68 C ANISOU 798 CB HIS A 97 988 1566 1123 -23 79 -13 C ATOM 799 CG HIS A 97 19.846 -35.345 -5.906 1.00 9.57 C ANISOU 799 CG HIS A 97 893 1413 1327 -45 8 -128 C ATOM 800 ND1 HIS A 97 19.219 -36.436 -6.470 1.00 11.02 N ANISOU 800 ND1 HIS A 97 1172 1534 1481 -55 -57 -81 N ATOM 801 CD2 HIS A 97 19.385 -35.259 -4.636 1.00 10.26 C ANISOU 801 CD2 HIS A 97 975 1454 1469 140 18 4 C ATOM 802 CE1 HIS A 97 18.426 -36.994 -5.574 1.00 10.51 C ANISOU 802 CE1 HIS A 97 1031 1419 1540 -77 71 -89 C ATOM 803 NE2 HIS A 97 18.511 -36.302 -4.452 1.00 10.34 N ANISOU 803 NE2 HIS A 97 1003 1403 1522 -15 -30 -42 N ATOM 804 N LYS A 98 24.064 -34.342 -7.698 1.00 9.67 N ANISOU 804 N LYS A 98 1072 1355 1247 110 4 -213 N ATOM 805 CA LYS A 98 25.129 -33.547 -8.322 1.00 10.11 C ANISOU 805 CA LYS A 98 1043 1542 1256 148 124 86 C ATOM 806 C LYS A 98 24.798 -32.057 -8.372 1.00 9.48 C ANISOU 806 C LYS A 98 1019 1426 1153 29 86 68 C ATOM 807 O LYS A 98 24.908 -31.422 -9.421 1.00 10.04 O ANISOU 807 O LYS A 98 1061 1557 1196 84 64 86 O ATOM 808 CB LYS A 98 25.429 -34.046 -9.739 1.00 14.00 C ANISOU 808 CB LYS A 98 1615 2051 1650 210 236 10 C ATOM 809 CG LYS A 98 25.491 -35.549 -9.878 1.00 18.50 C ANISOU 809 CG LYS A 98 2303 2456 2268 132 325 -83 C ATOM 810 CD LYS A 98 26.636 -36.135 -9.091 1.00 21.06 C ANISOU 810 CD LYS A 98 2678 2749 2574 83 79 -124 C ATOM 811 CE LYS A 98 26.799 -37.616 -9.402 1.00 23.55 C ANISOU 811 CE LYS A 98 3027 2947 2971 135 99 -87 C ATOM 812 NZ LYS A 98 27.942 -38.215 -8.664 1.00 25.35 N ANISOU 812 NZ LYS A 98 3095 3172 3363 202 3 -128 N ATOM 813 N ILE A 99 24.422 -31.502 -7.226 1.00 8.77 N ANISOU 813 N ILE A 99 901 1306 1124 324 -91 84 N ATOM 814 CA ILE A 99 23.977 -30.116 -7.150 1.00 8.90 C ANISOU 814 CA ILE A 99 994 1301 1086 210 -79 128 C ATOM 815 C ILE A 99 25.110 -29.225 -6.644 1.00 9.17 C ANISOU 815 C ILE A 99 947 1237 1300 187 -78 177 C ATOM 816 O ILE A 99 25.459 -29.267 -5.468 1.00 9.70 O ANISOU 816 O ILE A 99 1000 1437 1247 67 -215 254 O ATOM 817 CB ILE A 99 22.767 -29.988 -6.196 1.00 8.94 C ANISOU 817 CB ILE A 99 1025 1156 1215 111 -90 165 C ATOM 818 CG1 ILE A 99 21.641 -30.949 -6.604 1.00 9.54 C ANISOU 818 CG1 ILE A 99 1013 1330 1280 136 -43 30 C ATOM 819 CG2 ILE A 99 22.275 -28.548 -6.142 1.00 9.57 C ANISOU 819 CG2 ILE A 99 1039 1183 1414 198 -172 259 C ATOM 820 CD1 ILE A 99 21.225 -30.850 -8.060 1.00 9.93 C ANISOU 820 CD1 ILE A 99 909 1574 1287 163 -299 6 C ATOM 821 N PRO A 100 25.704 -28.415 -7.531 1.00 9.18 N ANISOU 821 N PRO A 100 962 1355 1168 129 -27 222 N ATOM 822 CA PRO A 100 26.763 -27.537 -7.042 1.00 9.95 C ANISOU 822 CA PRO A 100 974 1441 1365 90 91 206 C ATOM 823 C PRO A 100 26.247 -26.563 -5.988 1.00 9.29 C ANISOU 823 C PRO A 100 868 1395 1263 148 63 280 C ATOM 824 O PRO A 100 25.071 -26.186 -6.002 1.00 9.12 O ANISOU 824 O PRO A 100 907 1165 1390 112 161 200 O ATOM 825 CB PRO A 100 27.232 -26.788 -8.296 1.00 10.77 C ANISOU 825 CB PRO A 100 1148 1576 1366 -131 184 235 C ATOM 826 CG PRO A 100 26.200 -27.009 -9.313 1.00 12.97 C ANISOU 826 CG PRO A 100 1481 1907 1539 -162 -38 401 C ATOM 827 CD PRO A 100 25.435 -28.243 -8.968 1.00 9.93 C ANISOU 827 CD PRO A 100 1155 1403 1214 29 108 298 C ATOM 828 N ILE A 101 27.125 -26.152 -5.084 1.00 9.95 N ANISOU 828 N ILE A 101 1059 1380 1340 155 55 148 N ATOM 829 CA ILE A 101 26.726 -25.267 -4.004 1.00 9.87 C ANISOU 829 CA ILE A 101 1088 1365 1295 117 -9 128 C ATOM 830 C ILE A 101 26.143 -23.959 -4.546 1.00 8.61 C ANISOU 830 C ILE A 101 729 1307 1234 -71 69 158 C ATOM 831 O ILE A 101 25.284 -23.347 -3.913 1.00 8.93 O ANISOU 831 O ILE A 101 856 1331 1203 -23 57 133 O ATOM 832 CB ILE A 101 27.883 -25.036 -3.009 1.00 11.22 C ANISOU 832 CB ILE A 101 1238 1553 1470 136 -145 108 C ATOM 833 CG1 ILE A 101 27.383 -24.407 -1.711 1.00 13.02 C ANISOU 833 CG1 ILE A 101 1611 1790 1543 198 -60 -43 C ATOM 834 CG2 ILE A 101 29.012 -24.254 -3.641 1.00 13.29 C ANISOU 834 CG2 ILE A 101 1355 1790 1902 14 -258 336 C ATOM 835 CD1 ILE A 101 26.622 -25.371 -0.831 1.00 15.94 C ANISOU 835 CD1 ILE A 101 1867 2201 1988 218 175 77 C ATOM 836 N LYS A 102 26.587 -23.553 -5.735 1.00 9.10 N ANISOU 836 N LYS A 102 675 1364 1416 104 -15 280 N ATOM 837 CA LYS A 102 26.034 -22.369 -6.396 1.00 10.16 C ANISOU 837 CA LYS A 102 828 1460 1570 51 113 381 C ATOM 838 C LYS A 102 24.510 -22.440 -6.483 1.00 8.43 C ANISOU 838 C LYS A 102 774 1163 1264 56 98 312 C ATOM 839 O LYS A 102 23.820 -21.427 -6.342 1.00 8.68 O ANISOU 839 O LYS A 102 769 1115 1414 7 141 305 O ATOM 840 CB LYS A 102 26.620 -22.223 -7.808 1.00 11.41 C ANISOU 840 CB LYS A 102 998 1647 1689 84 317 424 C ATOM 841 CG LYS A 102 26.299 -20.890 -8.459 1.00 15.41 C ANISOU 841 CG LYS A 102 1619 2051 2184 106 398 238 C ATOM 842 CD LYS A 102 27.113 -19.791 -7.803 1.00 17.82 C ANISOU 842 CD LYS A 102 2257 2080 2434 69 351 -27 C ATOM 843 CE LYS A 102 26.894 -18.441 -8.449 1.00 18.88 C ANISOU 843 CE LYS A 102 2299 2247 2625 -157 403 -23 C ATOM 844 NZ LYS A 102 27.538 -17.412 -7.602 1.00 18.75 N ANISOU 844 NZ LYS A 102 2117 2368 2636 -433 278 -238 N ATOM 845 N TYR A 103 23.984 -23.630 -6.751 1.00 8.43 N ANISOU 845 N TYR A 103 817 1228 1155 80 41 244 N ATOM 846 CA TYR A 103 22.539 -23.777 -6.893 1.00 9.21 C ANISOU 846 CA TYR A 103 781 1363 1353 8 34 284 C ATOM 847 C TYR A 103 21.831 -23.620 -5.543 1.00 8.46 C ANISOU 847 C TYR A 103 895 968 1351 101 82 384 C ATOM 848 O TYR A 103 20.670 -23.206 -5.496 1.00 8.19 O ANISOU 848 O TYR A 103 779 984 1347 47 76 218 O ATOM 849 CB TYR A 103 22.159 -25.104 -7.557 1.00 9.11 C ANISOU 849 CB TYR A 103 990 1273 1199 62 163 272 C ATOM 850 CG TYR A 103 22.624 -25.285 -8.994 1.00 9.21 C ANISOU 850 CG TYR A 103 874 1377 1248 142 175 279 C ATOM 851 CD1 TYR A 103 23.409 -24.328 -9.638 1.00 11.31 C ANISOU 851 CD1 TYR A 103 1236 1823 1237 -51 66 223 C ATOM 852 CD2 TYR A 103 22.308 -26.443 -9.689 1.00 9.91 C ANISOU 852 CD2 TYR A 103 991 1491 1282 230 17 115 C ATOM 853 CE1 TYR A 103 23.839 -24.525 -10.952 1.00 13.14 C ANISOU 853 CE1 TYR A 103 1480 2058 1454 221 236 194 C ATOM 854 CE2 TYR A 103 22.735 -26.648 -10.983 1.00 11.99 C ANISOU 854 CE2 TYR A 103 1216 1914 1424 461 131 219 C ATOM 855 CZ TYR A 103 23.494 -25.692 -11.614 1.00 12.19 C ANISOU 855 CZ TYR A 103 1368 1947 1314 375 178 263 C ATOM 856 OH TYR A 103 23.910 -25.918 -12.909 1.00 14.50 O ANISOU 856 OH TYR A 103 1756 2312 1439 411 357 291 O ATOM 857 N LEU A 104 22.521 -23.958 -4.452 1.00 7.83 N ANISOU 857 N LEU A 104 802 983 1189 -2 77 219 N ATOM 858 CA ALEU A 104 21.984 -23.743 -3.105 0.50 7.60 C ANISOU 858 CA ALEU A 104 683 985 1220 45 69 214 C ATOM 859 CA BLEU A 104 21.965 -23.742 -3.122 0.50 7.51 C ANISOU 859 CA BLEU A 104 712 947 1192 54 -4 249 C ATOM 860 C LEU A 104 21.960 -22.257 -2.783 1.00 7.60 C ANISOU 860 C LEU A 104 765 1009 1112 14 41 212 C ATOM 861 O LEU A 104 21.070 -21.776 -2.080 1.00 7.78 O ANISOU 861 O LEU A 104 806 971 1175 74 107 141 O ATOM 862 CB ALEU A 104 22.798 -24.501 -2.050 0.50 8.30 C ANISOU 862 CB ALEU A 104 748 1096 1307 71 111 248 C ATOM 863 CB BLEU A 104 22.717 -24.562 -2.074 0.50 7.99 C ANISOU 863 CB BLEU A 104 768 977 1292 78 -68 346 C ATOM 864 CG ALEU A 104 22.479 -25.985 -1.843 0.50 9.46 C ANISOU 864 CG ALEU A 104 829 1316 1448 53 323 217 C ATOM 865 CG BLEU A 104 22.652 -26.069 -2.340 0.50 8.64 C ANISOU 865 CG BLEU A 104 922 1100 1261 28 -87 337 C ATOM 866 CD1ALEU A 104 21.060 -26.190 -1.320 0.50 9.56 C ANISOU 866 CD1ALEU A 104 905 1304 1421 36 406 317 C ATOM 867 CD1BLEU A 104 23.488 -26.832 -1.329 0.50 8.77 C ANISOU 867 CD1BLEU A 104 1008 909 1415 1 -127 524 C ATOM 868 CD2ALEU A 104 22.714 -26.782 -3.112 0.50 10.65 C ANISOU 868 CD2ALEU A 104 1141 1316 1590 -22 176 109 C ATOM 869 CD2BLEU A 104 21.216 -26.576 -2.350 0.50 9.81 C ANISOU 869 CD2BLEU A 104 1103 1067 1557 8 -125 371 C ATOM 870 N GLU A 105 22.949 -21.532 -3.296 1.00 8.30 N ANISOU 870 N GLU A 105 841 997 1314 47 19 228 N ATOM 871 CA GLU A 105 22.936 -20.078 -3.205 1.00 8.26 C ANISOU 871 CA GLU A 105 643 1133 1361 -12 7 242 C ATOM 872 C GLU A 105 21.716 -19.542 -3.971 1.00 7.90 C ANISOU 872 C GLU A 105 704 913 1384 -48 131 285 C ATOM 873 O GLU A 105 20.959 -18.712 -3.455 1.00 8.46 O ANISOU 873 O GLU A 105 818 1004 1393 -33 49 187 O ATOM 874 CB GLU A 105 24.217 -19.497 -3.799 1.00 9.03 C ANISOU 874 CB GLU A 105 732 1109 1589 14 42 325 C ATOM 875 CG GLU A 105 24.281 -17.984 -3.725 1.00 10.25 C ANISOU 875 CG GLU A 105 1075 1110 1709 -110 6 209 C ATOM 876 CD GLU A 105 25.408 -17.413 -4.559 1.00 11.53 C ANISOU 876 CD GLU A 105 1231 1317 1829 24 120 241 C ATOM 877 OE1 GLU A 105 26.153 -18.200 -5.183 1.00 12.58 O ANISOU 877 OE1 GLU A 105 1322 1597 1859 -171 109 258 O ATOM 878 OE2 GLU A 105 25.545 -16.173 -4.594 1.00 14.52 O ANISOU 878 OE2 GLU A 105 1633 1442 2441 -243 237 -89 O ATOM 879 N PHE A 106 21.517 -20.023 -5.199 1.00 7.89 N ANISOU 879 N PHE A 106 767 946 1285 -65 54 381 N ATOM 880 CA PHE A 106 20.362 -19.589 -5.993 1.00 8.13 C ANISOU 880 CA PHE A 106 765 1194 1127 36 65 395 C ATOM 881 C PHE A 106 19.038 -19.826 -5.249 1.00 7.09 C ANISOU 881 C PHE A 106 783 837 1071 -53 4 274 C ATOM 882 O PHE A 106 18.173 -18.954 -5.219 1.00 7.47 O ANISOU 882 O PHE A 106 831 880 1128 122 18 183 O ATOM 883 CB PHE A 106 20.272 -20.318 -7.343 1.00 8.59 C ANISOU 883 CB PHE A 106 914 1309 1038 18 254 236 C ATOM 884 CG PHE A 106 21.400 -20.034 -8.314 1.00 9.00 C ANISOU 884 CG PHE A 106 891 1368 1159 141 192 375 C ATOM 885 CD1 PHE A 106 22.154 -18.872 -8.249 1.00 10.60 C ANISOU 885 CD1 PHE A 106 993 1624 1409 72 337 391 C ATOM 886 CD2 PHE A 106 21.663 -20.939 -9.333 1.00 9.72 C ANISOU 886 CD2 PHE A 106 939 1593 1158 232 265 446 C ATOM 887 CE1 PHE A 106 23.173 -18.640 -9.174 1.00 11.93 C ANISOU 887 CE1 PHE A 106 1293 1776 1463 113 418 299 C ATOM 888 CE2 PHE A 106 22.673 -20.707 -10.257 1.00 11.67 C ANISOU 888 CE2 PHE A 106 1259 1814 1361 194 316 392 C ATOM 889 CZ PHE A 106 23.424 -19.559 -10.176 1.00 12.47 C ANISOU 889 CZ PHE A 106 1296 1886 1553 142 463 439 C ATOM 890 N ILE A 107 18.860 -21.011 -4.668 1.00 7.41 N ANISOU 890 N ILE A 107 817 919 1077 17 77 214 N ATOM 891 CA ILE A 107 17.582 -21.308 -4.026 1.00 7.63 C ANISOU 891 CA ILE A 107 774 1051 1071 24 -3 203 C ATOM 892 C ILE A 107 17.398 -20.501 -2.742 1.00 6.95 C ANISOU 892 C ILE A 107 713 897 1027 106 51 227 C ATOM 893 O ILE A 107 16.279 -20.129 -2.392 1.00 7.98 O ANISOU 893 O ILE A 107 802 951 1278 172 148 258 O ATOM 894 CB ILE A 107 17.343 -22.819 -3.809 1.00 8.04 C ANISOU 894 CB ILE A 107 828 918 1307 74 -16 190 C ATOM 895 CG1 ILE A 107 15.841 -23.108 -3.718 1.00 8.05 C ANISOU 895 CG1 ILE A 107 851 862 1344 15 -131 142 C ATOM 896 CG2 ILE A 107 18.094 -23.324 -2.566 1.00 8.79 C ANISOU 896 CG2 ILE A 107 833 1089 1414 3 -136 123 C ATOM 897 CD1 ILE A 107 15.501 -24.585 -3.635 1.00 8.99 C ANISOU 897 CD1 ILE A 107 1173 877 1365 -96 -48 241 C ATOM 898 N SER A 108 18.502 -20.201 -2.061 1.00 7.54 N ANISOU 898 N SER A 108 750 1088 1026 38 54 262 N ATOM 899 CA SER A 108 18.455 -19.355 -0.867 1.00 8.65 C ANISOU 899 CA SER A 108 940 1201 1146 37 0 125 C ATOM 900 C SER A 108 17.945 -17.964 -1.240 1.00 8.20 C ANISOU 900 C SER A 108 641 1203 1272 -27 43 92 C ATOM 901 O SER A 108 17.058 -17.411 -0.581 1.00 9.35 O ANISOU 901 O SER A 108 850 1194 1505 37 21 -25 O ATOM 902 CB SER A 108 19.842 -19.244 -0.222 1.00 9.73 C ANISOU 902 CB SER A 108 802 1539 1356 132 -75 197 C ATOM 903 OG SER A 108 20.291 -20.486 0.297 1.00 10.23 O ANISOU 903 OG SER A 108 1064 1485 1336 100 -15 224 O ATOM 904 N ASP A 109 18.516 -17.407 -2.303 1.00 8.58 N ANISOU 904 N ASP A 109 788 1055 1416 5 -53 138 N ATOM 905 CA ASP A 109 18.076 -16.117 -2.809 1.00 8.56 C ANISOU 905 CA ASP A 109 771 994 1487 -61 22 207 C ATOM 906 C ASP A 109 16.608 -16.160 -3.261 1.00 7.72 C ANISOU 906 C ASP A 109 699 1019 1215 -24 -18 188 C ATOM 907 O ASP A 109 15.860 -15.201 -3.052 1.00 8.66 O ANISOU 907 O ASP A 109 832 948 1507 49 29 174 O ATOM 908 CB ASP A 109 18.976 -15.675 -3.959 1.00 10.37 C ANISOU 908 CB ASP A 109 881 1309 1750 -57 166 289 C ATOM 909 CG ASP A 109 20.345 -15.210 -3.486 1.00 13.28 C ANISOU 909 CG ASP A 109 1262 1627 2157 -103 5 252 C ATOM 910 OD1 ASP A 109 20.544 -15.048 -2.264 1.00 16.33 O ANISOU 910 OD1 ASP A 109 1305 2411 2487 -380 -141 197 O ATOM 911 OD2 ASP A 109 21.223 -14.999 -4.346 1.00 14.90 O ANISOU 911 OD2 ASP A 109 1189 1924 2546 -176 102 334 O ATOM 912 N ALA A 110 16.195 -17.268 -3.871 1.00 7.52 N ANISOU 912 N ALA A 110 645 1024 1188 10 47 269 N ATOM 913 CA ALA A 110 14.807 -17.425 -4.296 1.00 7.88 C ANISOU 913 CA ALA A 110 789 989 1214 -22 -62 19 C ATOM 914 C ALA A 110 13.844 -17.382 -3.111 1.00 7.76 C ANISOU 914 C ALA A 110 862 749 1337 100 -103 74 C ATOM 915 O ALA A 110 12.758 -16.804 -3.206 1.00 8.01 O ANISOU 915 O ALA A 110 766 1024 1252 166 -9 90 O ATOM 916 CB ALA A 110 14.623 -18.719 -5.090 1.00 8.63 C ANISOU 916 CB ALA A 110 898 1066 1315 74 54 74 C ATOM 917 N ILE A 111 14.237 -17.994 -1.998 1.00 7.66 N ANISOU 917 N ILE A 111 754 913 1242 -79 -10 120 N ATOM 918 CA ILE A 111 13.404 -17.974 -0.808 1.00 7.96 C ANISOU 918 CA ILE A 111 834 762 1429 -6 -106 87 C ATOM 919 C ILE A 111 13.185 -16.549 -0.311 1.00 7.91 C ANISOU 919 C ILE A 111 821 827 1355 57 -112 152 C ATOM 920 O ILE A 111 12.056 -16.166 0.004 1.00 8.23 O ANISOU 920 O ILE A 111 838 886 1403 122 -24 59 O ATOM 921 CB ILE A 111 13.984 -18.872 0.295 1.00 7.85 C ANISOU 921 CB ILE A 111 892 802 1287 37 -95 208 C ATOM 922 CG1 ILE A 111 13.852 -20.342 -0.117 1.00 7.90 C ANISOU 922 CG1 ILE A 111 820 713 1466 14 -100 170 C ATOM 923 CG2 ILE A 111 13.285 -18.632 1.635 1.00 8.99 C ANISOU 923 CG2 ILE A 111 1022 1000 1392 45 79 305 C ATOM 924 CD1 ILE A 111 14.693 -21.299 0.715 1.00 8.67 C ANISOU 924 CD1 ILE A 111 1096 782 1415 63 -252 231 C ATOM 925 N ILE A 112 14.256 -15.757 -0.255 1.00 8.25 N ANISOU 925 N ILE A 112 844 1003 1284 -67 40 186 N ATOM 926 CA ILE A 112 14.127 -14.359 0.151 1.00 7.96 C ANISOU 926 CA ILE A 112 800 936 1286 -3 -87 205 C ATOM 927 C ILE A 112 13.214 -13.596 -0.805 1.00 8.26 C ANISOU 927 C ILE A 112 830 1033 1273 13 132 176 C ATOM 928 O ILE A 112 12.344 -12.838 -0.372 1.00 8.04 O ANISOU 928 O ILE A 112 790 1008 1255 -64 73 148 O ATOM 929 CB ILE A 112 15.514 -13.675 0.274 1.00 8.34 C ANISOU 929 CB ILE A 112 737 1006 1423 11 -111 234 C ATOM 930 CG1 ILE A 112 16.343 -14.339 1.383 1.00 8.80 C ANISOU 930 CG1 ILE A 112 864 1331 1147 118 -21 44 C ATOM 931 CG2 ILE A 112 15.376 -12.170 0.488 1.00 9.14 C ANISOU 931 CG2 ILE A 112 951 961 1559 109 -27 45 C ATOM 932 CD1 ILE A 112 15.718 -14.261 2.771 1.00 9.57 C ANISOU 932 CD1 ILE A 112 1260 1221 1155 59 10 67 C ATOM 933 N HIS A 113 13.392 -13.814 -2.105 1.00 7.98 N ANISOU 933 N HIS A 113 657 1035 1337 13 40 232 N ATOM 934 CA HIS A 113 12.547 -13.154 -3.085 1.00 8.22 C ANISOU 934 CA HIS A 113 585 1144 1393 108 93 246 C ATOM 935 C HIS A 113 11.075 -13.513 -2.905 1.00 8.09 C ANISOU 935 C HIS A 113 681 1067 1324 84 -4 261 C ATOM 936 O HIS A 113 10.203 -12.641 -2.933 1.00 8.73 O ANISOU 936 O HIS A 113 732 1030 1554 150 -45 254 O ATOM 937 CB HIS A 113 12.982 -13.512 -4.499 1.00 10.23 C ANISOU 937 CB HIS A 113 1086 1454 1345 22 33 326 C ATOM 938 CG HIS A 113 12.132 -12.873 -5.547 1.00 13.78 C ANISOU 938 CG HIS A 113 1835 1624 1774 221 -80 255 C ATOM 939 ND1 HIS A 113 12.398 -11.622 -6.059 1.00 16.72 N ANISOU 939 ND1 HIS A 113 2455 1875 2023 192 -252 331 N ATOM 940 CD2 HIS A 113 10.995 -13.293 -6.149 1.00 14.77 C ANISOU 940 CD2 HIS A 113 1926 1924 1759 300 -224 105 C ATOM 941 CE1 HIS A 113 11.473 -11.308 -6.947 1.00 17.44 C ANISOU 941 CE1 HIS A 113 2478 2033 2112 407 -308 361 C ATOM 942 NE2 HIS A 113 10.608 -12.304 -7.020 1.00 18.03 N ANISOU 942 NE2 HIS A 113 2529 2126 2195 454 -300 172 N ATOM 943 N VAL A 114 10.798 -14.801 -2.744 1.00 8.28 N ANISOU 943 N VAL A 114 700 980 1464 27 -66 66 N ATOM 944 CA VAL A 114 9.422 -15.269 -2.633 1.00 8.89 C ANISOU 944 CA VAL A 114 764 1119 1493 69 35 54 C ATOM 945 C VAL A 114 8.751 -14.723 -1.370 1.00 8.39 C ANISOU 945 C VAL A 114 725 969 1493 -48 16 19 C ATOM 946 O VAL A 114 7.574 -14.346 -1.387 1.00 8.58 O ANISOU 946 O VAL A 114 637 956 1667 19 45 -88 O ATOM 947 CB VAL A 114 9.338 -16.811 -2.705 1.00 8.89 C ANISOU 947 CB VAL A 114 820 1002 1554 77 -6 28 C ATOM 948 CG1 VAL A 114 7.938 -17.289 -2.315 1.00 10.32 C ANISOU 948 CG1 VAL A 114 964 1066 1891 -11 20 14 C ATOM 949 CG2 VAL A 114 9.695 -17.285 -4.112 1.00 10.20 C ANISOU 949 CG2 VAL A 114 1014 1267 1591 126 -70 -88 C ATOM 950 N LEU A 115 9.508 -14.640 -0.281 1.00 8.10 N ANISOU 950 N LEU A 115 790 925 1361 -95 131 190 N ATOM 951 CA LEU A 115 8.959 -14.084 0.945 1.00 8.66 C ANISOU 951 CA LEU A 115 894 1020 1377 -54 135 114 C ATOM 952 C LEU A 115 8.510 -12.634 0.735 1.00 8.46 C ANISOU 952 C LEU A 115 704 1043 1464 -151 40 131 C ATOM 953 O LEU A 115 7.416 -12.254 1.147 1.00 8.55 O ANISOU 953 O LEU A 115 720 966 1560 -39 97 8 O ATOM 954 CB LEU A 115 9.950 -14.219 2.101 1.00 9.33 C ANISOU 954 CB LEU A 115 997 1073 1473 -90 120 212 C ATOM 955 CG LEU A 115 10.091 -15.652 2.619 1.00 9.28 C ANISOU 955 CG LEU A 115 1135 1076 1313 -116 185 326 C ATOM 956 CD1 LEU A 115 11.308 -15.768 3.522 1.00 9.67 C ANISOU 956 CD1 LEU A 115 1187 1229 1258 -96 169 366 C ATOM 957 CD2 LEU A 115 8.829 -16.092 3.342 1.00 11.35 C ANISOU 957 CD2 LEU A 115 1298 1314 1700 -144 230 461 C ATOM 958 N HIS A 116 9.338 -11.822 0.084 1.00 8.06 N ANISOU 958 N HIS A 116 745 937 1379 -90 -82 142 N ATOM 959 CA HIS A 116 8.923 -10.454 -0.223 1.00 7.81 C ANISOU 959 CA HIS A 116 693 948 1324 -96 -125 273 C ATOM 960 C HIS A 116 7.762 -10.391 -1.208 1.00 8.62 C ANISOU 960 C HIS A 116 818 933 1521 -186 -106 51 C ATOM 961 O HIS A 116 6.893 -9.527 -1.096 1.00 10.38 O ANISOU 961 O HIS A 116 970 1010 1962 99 -88 -63 O ATOM 962 CB HIS A 116 10.091 -9.639 -0.774 1.00 8.63 C ANISOU 962 CB HIS A 116 749 1060 1467 -234 -121 231 C ATOM 963 CG HIS A 116 11.022 -9.127 0.278 1.00 7.88 C ANISOU 963 CG HIS A 116 841 805 1349 -266 -108 163 C ATOM 964 ND1 HIS A 116 10.622 -8.251 1.266 1.00 8.85 N ANISOU 964 ND1 HIS A 116 829 908 1625 -96 34 200 N ATOM 965 CD2 HIS A 116 12.339 -9.357 0.486 1.00 8.68 C ANISOU 965 CD2 HIS A 116 897 923 1477 -213 -50 193 C ATOM 966 CE1 HIS A 116 11.657 -7.965 2.037 1.00 8.73 C ANISOU 966 CE1 HIS A 116 749 942 1626 -114 27 76 C ATOM 967 NE2 HIS A 116 12.711 -8.623 1.585 1.00 8.24 N ANISOU 967 NE2 HIS A 116 860 844 1427 -220 -34 87 N ATOM 968 N SER A 117 7.757 -11.293 -2.184 1.00 7.88 N ANISOU 968 N SER A 117 784 854 1354 -173 -145 141 N ATOM 969 CA SER A 117 6.717 -11.292 -3.201 1.00 9.24 C ANISOU 969 CA SER A 117 723 1236 1551 34 -167 204 C ATOM 970 C SER A 117 5.354 -11.644 -2.610 1.00 8.66 C ANISOU 970 C SER A 117 754 931 1602 5 -128 86 C ATOM 971 O SER A 117 4.333 -11.056 -2.981 1.00 9.92 O ANISOU 971 O SER A 117 808 1104 1854 35 -153 179 O ATOM 972 CB SER A 117 7.073 -12.264 -4.320 1.00 9.96 C ANISOU 972 CB SER A 117 768 1554 1462 146 -251 -37 C ATOM 973 OG SER A 117 6.103 -12.197 -5.341 1.00 12.69 O ANISOU 973 OG SER A 117 1188 1880 1750 256 -343 -175 O ATOM 974 N LYS A 118 5.339 -12.609 -1.695 1.00 8.76 N ANISOU 974 N LYS A 118 752 964 1612 -54 -62 119 N ATOM 975 CA LYS A 118 4.083 -13.082 -1.132 1.00 9.26 C ANISOU 975 CA LYS A 118 805 956 1754 -89 53 205 C ATOM 976 C LYS A 118 3.643 -12.266 0.079 1.00 9.11 C ANISOU 976 C LYS A 118 763 959 1738 -214 144 137 C ATOM 977 O LYS A 118 2.467 -12.271 0.441 1.00 10.42 O ANISOU 977 O LYS A 118 808 1115 2034 -211 223 -66 O ATOM 978 CB LYS A 118 4.183 -14.571 -0.788 1.00 9.30 C ANISOU 978 CB LYS A 118 1028 914 1591 -103 -58 -17 C ATOM 979 CG LYS A 118 4.303 -15.467 -2.018 1.00 10.42 C ANISOU 979 CG LYS A 118 1411 905 1643 -129 25 -21 C ATOM 980 CD LYS A 118 4.331 -16.937 -1.646 1.00 11.38 C ANISOU 980 CD LYS A 118 1422 941 1958 -170 68 -21 C ATOM 981 CE LYS A 118 2.942 -17.436 -1.296 1.00 14.37 C ANISOU 981 CE LYS A 118 1612 1503 2344 -265 138 184 C ATOM 982 NZ LYS A 118 2.030 -17.346 -2.474 1.00 15.20 N ANISOU 982 NZ LYS A 118 1348 1745 2682 -460 -267 -93 N ATOM 983 N HIS A 119 4.581 -11.547 0.689 1.00 9.23 N ANISOU 983 N HIS A 119 817 1022 1666 -90 156 49 N ATOM 984 CA HIS A 119 4.308 -10.809 1.921 1.00 9.64 C ANISOU 984 CA HIS A 119 921 1042 1698 -135 298 8 C ATOM 985 C HIS A 119 4.911 -9.412 1.865 1.00 9.05 C ANISOU 985 C HIS A 119 790 964 1684 -56 138 -84 C ATOM 986 O HIS A 119 5.672 -9.016 2.751 1.00 9.16 O ANISOU 986 O HIS A 119 794 956 1730 -76 58 -3 O ATOM 987 CB HIS A 119 4.851 -11.577 3.128 1.00 9.96 C ANISOU 987 CB HIS A 119 1200 953 1631 -239 331 -59 C ATOM 988 CG HIS A 119 4.495 -13.027 3.110 1.00 10.95 C ANISOU 988 CG HIS A 119 1312 1050 1796 -371 408 27 C ATOM 989 ND1 HIS A 119 3.285 -13.501 3.569 1.00 12.66 N ANISOU 989 ND1 HIS A 119 1508 1217 2085 -260 432 260 N ATOM 990 CD2 HIS A 119 5.176 -14.104 2.655 1.00 11.58 C ANISOU 990 CD2 HIS A 119 1523 1061 1813 -286 252 -5 C ATOM 991 CE1 HIS A 119 3.240 -14.811 3.402 1.00 11.81 C ANISOU 991 CE1 HIS A 119 1422 1085 1979 -366 390 88 C ATOM 992 NE2 HIS A 119 4.374 -15.201 2.849 1.00 11.89 N ANISOU 992 NE2 HIS A 119 1532 1139 1845 -372 385 118 N ATOM 993 N PRO A 120 4.561 -8.642 0.825 1.00 8.97 N ANISOU 993 N PRO A 120 734 976 1697 -17 -65 -2 N ATOM 994 CA PRO A 120 5.209 -7.350 0.655 1.00 9.96 C ANISOU 994 CA PRO A 120 895 1049 1837 -26 19 35 C ATOM 995 C PRO A 120 4.860 -6.418 1.800 1.00 9.50 C ANISOU 995 C PRO A 120 766 1064 1776 16 -102 81 C ATOM 996 O PRO A 120 3.685 -6.279 2.152 1.00 10.01 O ANISOU 996 O PRO A 120 857 1134 1809 19 -141 -126 O ATOM 997 CB PRO A 120 4.611 -6.834 -0.655 1.00 10.55 C ANISOU 997 CB PRO A 120 962 1218 1827 -34 -96 125 C ATOM 998 CG PRO A 120 3.266 -7.523 -0.751 1.00 10.04 C ANISOU 998 CG PRO A 120 909 1047 1856 -135 -41 221 C ATOM 999 CD PRO A 120 3.545 -8.897 -0.214 1.00 9.81 C ANISOU 999 CD PRO A 120 943 1080 1703 5 -75 8 C ATOM 1000 N GLY A 121 5.872 -5.782 2.378 1.00 9.59 N ANISOU 1000 N GLY A 121 992 863 1788 -40 -130 -63 N ATOM 1001 CA GLY A 121 5.656 -4.912 3.523 1.00 10.77 C ANISOU 1001 CA GLY A 121 1169 1112 1811 -12 -40 -29 C ATOM 1002 C GLY A 121 5.533 -5.656 4.840 1.00 10.62 C ANISOU 1002 C GLY A 121 1206 1014 1813 -48 84 -57 C ATOM 1003 O GLY A 121 5.416 -5.028 5.899 1.00 11.97 O ANISOU 1003 O GLY A 121 1464 1137 1946 32 210 -117 O ATOM 1004 N ASP A 122 5.563 -6.988 4.784 1.00 9.89 N ANISOU 1004 N ASP A 122 784 973 2001 -149 -7 0 N ATOM 1005 CA ASP A 122 5.430 -7.789 5.993 1.00 10.98 C ANISOU 1005 CA ASP A 122 947 1151 2073 -50 90 -53 C ATOM 1006 C ASP A 122 6.624 -8.717 6.202 1.00 10.65 C ANISOU 1006 C ASP A 122 876 1135 2036 16 129 68 C ATOM 1007 O ASP A 122 6.519 -9.725 6.892 1.00 13.76 O ANISOU 1007 O ASP A 122 1214 1659 2354 4 243 431 O ATOM 1008 CB ASP A 122 4.132 -8.599 5.959 1.00 13.01 C ANISOU 1008 CB ASP A 122 1347 1366 2227 -74 164 8 C ATOM 1009 CG ASP A 122 3.807 -9.234 7.295 1.00 16.16 C ANISOU 1009 CG ASP A 122 1631 1973 2533 -120 205 -44 C ATOM 1010 OD1 ASP A 122 4.024 -8.578 8.335 1.00 18.62 O ANISOU 1010 OD1 ASP A 122 1958 2545 2571 -198 276 -120 O ATOM 1011 OD2 ASP A 122 3.328 -10.384 7.308 1.00 18.82 O ANISOU 1011 OD2 ASP A 122 2067 2261 2822 -213 232 32 O ATOM 1012 N PHE A 123 7.755 -8.372 5.601 1.00 9.64 N ANISOU 1012 N PHE A 123 810 1006 1847 43 23 36 N ATOM 1013 CA PHE A 123 8.993 -9.132 5.777 1.00 8.60 C ANISOU 1013 CA PHE A 123 860 801 1607 9 -52 1 C ATOM 1014 C PHE A 123 10.061 -8.076 6.031 1.00 9.37 C ANISOU 1014 C PHE A 123 800 976 1784 114 -94 -1 C ATOM 1015 O PHE A 123 10.760 -7.631 5.117 1.00 9.53 O ANISOU 1015 O PHE A 123 975 1015 1628 -61 -116 65 O ATOM 1016 CB PHE A 123 9.266 -9.960 4.514 1.00 8.75 C ANISOU 1016 CB PHE A 123 930 924 1469 0 -43 35 C ATOM 1017 CG PHE A 123 10.483 -10.842 4.591 1.00 8.44 C ANISOU 1017 CG PHE A 123 956 879 1370 -84 -81 22 C ATOM 1018 CD1 PHE A 123 10.829 -11.504 5.763 1.00 9.29 C ANISOU 1018 CD1 PHE A 123 976 973 1578 45 -11 148 C ATOM 1019 CD2 PHE A 123 11.270 -11.035 3.464 1.00 8.59 C ANISOU 1019 CD2 PHE A 123 916 922 1423 -156 27 -9 C ATOM 1020 CE1 PHE A 123 11.955 -12.330 5.807 1.00 9.33 C ANISOU 1020 CE1 PHE A 123 1076 919 1549 7 171 60 C ATOM 1021 CE2 PHE A 123 12.389 -11.859 3.502 1.00 9.02 C ANISOU 1021 CE2 PHE A 123 1106 927 1394 13 -34 -56 C ATOM 1022 CZ PHE A 123 12.734 -12.504 4.677 1.00 8.41 C ANISOU 1022 CZ PHE A 123 1031 812 1353 -128 75 28 C ATOM 1023 N GLY A 124 10.144 -7.646 7.286 1.00 9.60 N ANISOU 1023 N GLY A 124 999 929 1720 267 -189 -276 N ATOM 1024 CA GLY A 124 10.913 -6.462 7.642 1.00 11.25 C ANISOU 1024 CA GLY A 124 1005 1217 2050 209 -293 -367 C ATOM 1025 C GLY A 124 12.409 -6.672 7.601 1.00 9.09 C ANISOU 1025 C GLY A 124 989 861 1602 201 -381 -128 C ATOM 1026 O GLY A 124 12.891 -7.792 7.413 1.00 8.94 O ANISOU 1026 O GLY A 124 966 856 1574 146 -221 -252 O ATOM 1027 N ALA A 125 13.149 -5.590 7.799 1.00 9.59 N ANISOU 1027 N ALA A 125 1160 851 1630 110 -295 -71 N ATOM 1028 CA ALA A 125 14.588 -5.656 7.658 1.00 9.65 C ANISOU 1028 CA ALA A 125 1164 829 1674 19 -390 -49 C ATOM 1029 C ALA A 125 15.223 -6.608 8.663 1.00 8.99 C ANISOU 1029 C ALA A 125 1028 814 1574 17 -317 -17 C ATOM 1030 O ALA A 125 16.152 -7.334 8.326 1.00 8.40 O ANISOU 1030 O ALA A 125 997 940 1255 3 -79 57 O ATOM 1031 CB ALA A 125 15.193 -4.272 7.774 1.00 10.21 C ANISOU 1031 CB ALA A 125 1330 739 1808 35 -313 77 C ATOM 1032 N ASP A 126 14.727 -6.600 9.895 1.00 8.55 N ANISOU 1032 N ASP A 126 1062 756 1428 143 -156 -121 N ATOM 1033 CA ASP A 126 15.246 -7.523 10.901 1.00 9.79 C ANISOU 1033 CA ASP A 126 1230 1049 1439 227 109 -224 C ATOM 1034 C ASP A 126 14.967 -8.976 10.507 1.00 8.93 C ANISOU 1034 C ASP A 126 1015 1077 1299 217 132 -20 C ATOM 1035 O ASP A 126 15.841 -9.842 10.609 1.00 9.71 O ANISOU 1035 O ASP A 126 1205 1116 1366 269 50 51 O ATOM 1036 CB ASP A 126 14.729 -7.178 12.313 1.00 13.02 C ANISOU 1036 CB ASP A 126 1756 1387 1802 328 410 -330 C ATOM 1037 CG ASP A 126 13.209 -7.059 12.392 1.00 15.59 C ANISOU 1037 CG ASP A 126 2214 1782 1928 307 579 -379 C ATOM 1038 OD1 ASP A 126 12.517 -7.278 11.379 1.00 16.61 O ANISOU 1038 OD1 ASP A 126 2161 1880 2267 234 518 -270 O ATOM 1039 OD2 ASP A 126 12.704 -6.732 13.490 1.00 20.32 O ANISOU 1039 OD2 ASP A 126 2863 2485 2372 404 576 -458 O ATOM 1040 N ALA A 127 13.759 -9.224 10.012 1.00 8.64 N ANISOU 1040 N ALA A 127 962 999 1321 93 103 -93 N ATOM 1041 CA ALA A 127 13.345 -10.557 9.584 1.00 9.28 C ANISOU 1041 CA ALA A 127 982 1182 1361 28 204 57 C ATOM 1042 C ALA A 127 14.193 -11.050 8.407 1.00 8.25 C ANISOU 1042 C ALA A 127 841 980 1314 18 156 -6 C ATOM 1043 O ALA A 127 14.641 -12.202 8.390 1.00 8.10 O ANISOU 1043 O ALA A 127 909 783 1382 102 142 0 O ATOM 1044 CB ALA A 127 11.860 -10.559 9.227 1.00 10.34 C ANISOU 1044 CB ALA A 127 1076 1276 1577 8 133 15 C ATOM 1045 N GLN A 128 14.420 -10.184 7.422 1.00 8.25 N ANISOU 1045 N GLN A 128 809 986 1337 -9 112 -9 N ATOM 1046 CA GLN A 128 15.284 -10.559 6.310 1.00 8.78 C ANISOU 1046 CA GLN A 128 984 1051 1298 57 145 111 C ATOM 1047 C GLN A 128 16.698 -10.878 6.794 1.00 8.12 C ANISOU 1047 C GLN A 128 878 892 1313 -61 200 233 C ATOM 1048 O GLN A 128 17.300 -11.863 6.372 1.00 8.12 O ANISOU 1048 O GLN A 128 1082 838 1164 203 260 111 O ATOM 1049 CB GLN A 128 15.329 -9.475 5.231 1.00 8.29 C ANISOU 1049 CB GLN A 128 934 948 1265 50 114 126 C ATOM 1050 CG GLN A 128 16.265 -9.836 4.087 1.00 8.80 C ANISOU 1050 CG GLN A 128 1051 1086 1206 24 81 -33 C ATOM 1051 CD GLN A 128 16.253 -8.831 2.954 1.00 7.75 C ANISOU 1051 CD GLN A 128 882 865 1196 -70 -15 26 C ATOM 1052 OE1 GLN A 128 15.283 -8.098 2.759 1.00 7.90 O ANISOU 1052 OE1 GLN A 128 939 896 1167 53 -81 -4 O ATOM 1053 NE2 GLN A 128 17.326 -8.812 2.176 1.00 9.23 N ANISOU 1053 NE2 GLN A 128 920 1136 1451 -67 104 19 N ATOM 1054 N GLY A 129 17.231 -10.049 7.685 1.00 7.55 N ANISOU 1054 N GLY A 129 791 848 1229 -14 172 87 N ATOM 1055 CA GLY A 129 18.552 -10.306 8.256 1.00 8.23 C ANISOU 1055 CA GLY A 129 908 876 1342 51 90 124 C ATOM 1056 C GLY A 129 18.640 -11.686 8.885 1.00 7.46 C ANISOU 1056 C GLY A 129 770 767 1296 -37 113 -56 C ATOM 1057 O GLY A 129 19.572 -12.450 8.618 1.00 8.06 O ANISOU 1057 O GLY A 129 810 893 1358 -139 165 -42 O ATOM 1058 N ALA A 130 17.666 -12.013 9.727 1.00 7.56 N ANISOU 1058 N ALA A 130 830 871 1171 25 30 82 N ATOM 1059 CA ALA A 130 17.699 -13.272 10.457 1.00 7.83 C ANISOU 1059 CA ALA A 130 976 831 1167 -9 84 -18 C ATOM 1060 C ALA A 130 17.533 -14.462 9.520 1.00 6.85 C ANISOU 1060 C ALA A 130 739 732 1131 -105 6 209 C ATOM 1061 O ALA A 130 18.276 -15.440 9.614 1.00 7.50 O ANISOU 1061 O ALA A 130 844 856 1147 -49 50 177 O ATOM 1062 CB ALA A 130 16.636 -13.286 11.541 1.00 8.04 C ANISOU 1062 CB ALA A 130 974 1033 1044 -81 193 -152 C ATOM 1063 N MET A 131 16.568 -14.387 8.607 1.00 7.37 N ANISOU 1063 N MET A 131 785 876 1138 -127 59 38 N ATOM 1064 CA MET A 131 16.372 -15.473 7.652 1.00 7.47 C ANISOU 1064 CA MET A 131 751 879 1207 -13 -43 126 C ATOM 1065 C MET A 131 17.595 -15.677 6.753 1.00 6.70 C ANISOU 1065 C MET A 131 638 751 1153 -57 -47 51 C ATOM 1066 O MET A 131 17.967 -16.807 6.444 1.00 7.77 O ANISOU 1066 O MET A 131 787 766 1398 148 -28 -14 O ATOM 1067 CB MET A 131 15.121 -15.228 6.814 1.00 8.62 C ANISOU 1067 CB MET A 131 908 1026 1341 38 -80 97 C ATOM 1068 CG MET A 131 14.787 -16.372 5.865 1.00 9.64 C ANISOU 1068 CG MET A 131 1373 1031 1257 -169 -118 224 C ATOM 1069 SD MET A 131 14.500 -17.977 6.662 1.00 13.63 S ANISOU 1069 SD MET A 131 1965 1550 1663 -706 -373 277 S ATOM 1070 CE MET A 131 12.894 -17.718 7.376 1.00 16.53 C ANISOU 1070 CE MET A 131 2427 1937 1914 17 -159 141 C ATOM 1071 N THR A 132 18.227 -14.581 6.348 1.00 7.35 N ANISOU 1071 N THR A 132 801 822 1167 29 -5 28 N ATOM 1072 CA THR A 132 19.453 -14.660 5.559 1.00 7.66 C ANISOU 1072 CA THR A 132 801 760 1350 14 92 -39 C ATOM 1073 C THR A 132 20.552 -15.398 6.324 1.00 8.10 C ANISOU 1073 C THR A 132 769 887 1422 26 39 29 C ATOM 1074 O THR A 132 21.218 -16.267 5.772 1.00 7.89 O ANISOU 1074 O THR A 132 778 712 1505 47 121 -20 O ATOM 1075 CB THR A 132 19.923 -13.255 5.135 1.00 8.00 C ANISOU 1075 CB THR A 132 942 735 1360 24 142 49 C ATOM 1076 OG1 THR A 132 18.923 -12.681 4.288 1.00 9.06 O ANISOU 1076 OG1 THR A 132 1124 927 1392 99 112 310 O ATOM 1077 CG2 THR A 132 21.240 -13.308 4.369 1.00 9.96 C ANISOU 1077 CG2 THR A 132 1074 1105 1602 146 219 94 C ATOM 1078 N LYS A 133 20.737 -15.065 7.598 1.00 7.46 N ANISOU 1078 N LYS A 133 781 704 1349 -56 -61 -54 N ATOM 1079 CA LYS A 133 21.724 -15.771 8.417 1.00 8.56 C ANISOU 1079 CA LYS A 133 825 1124 1303 32 -6 43 C ATOM 1080 C LYS A 133 21.416 -17.266 8.510 1.00 7.92 C ANISOU 1080 C LYS A 133 741 1011 1255 -22 -25 35 C ATOM 1081 O LYS A 133 22.322 -18.094 8.459 1.00 7.79 O ANISOU 1081 O LYS A 133 686 1080 1191 129 -56 -74 O ATOM 1082 CB LYS A 133 21.807 -15.172 9.825 1.00 10.17 C ANISOU 1082 CB LYS A 133 1062 1332 1467 -75 79 -173 C ATOM 1083 CG LYS A 133 22.621 -13.887 9.921 1.00 10.83 C ANISOU 1083 CG LYS A 133 1155 1393 1564 -248 -211 -21 C ATOM 1084 CD LYS A 133 22.802 -13.440 11.379 1.00 12.00 C ANISOU 1084 CD LYS A 133 1393 1627 1538 -17 -106 -107 C ATOM 1085 CE LYS A 133 23.787 -14.314 12.142 1.00 14.15 C ANISOU 1085 CE LYS A 133 1936 1822 1617 -81 -94 -154 C ATOM 1086 NZ LYS A 133 24.101 -13.736 13.489 1.00 16.43 N ANISOU 1086 NZ LYS A 133 1970 2274 1998 -119 -22 -210 N ATOM 1087 N ALA A 134 20.143 -17.615 8.652 1.00 7.16 N ANISOU 1087 N ALA A 134 756 844 1120 59 -32 -43 N ATOM 1088 CA ALA A 134 19.771 -19.014 8.777 1.00 7.54 C ANISOU 1088 CA ALA A 134 872 861 1129 -9 50 -13 C ATOM 1089 C ALA A 134 20.059 -19.765 7.486 1.00 6.74 C ANISOU 1089 C ALA A 134 646 857 1057 32 -44 58 C ATOM 1090 O ALA A 134 20.530 -20.903 7.517 1.00 7.60 O ANISOU 1090 O ALA A 134 817 950 1118 203 19 38 O ATOM 1091 CB ALA A 134 18.310 -19.146 9.159 1.00 7.63 C ANISOU 1091 CB ALA A 134 682 856 1359 32 91 123 C ATOM 1092 N LEU A 135 19.768 -19.136 6.351 1.00 6.99 N ANISOU 1092 N LEU A 135 716 827 1111 -76 -84 24 N ATOM 1093 CA LEU A 135 20.015 -19.764 5.062 1.00 7.27 C ANISOU 1093 CA LEU A 135 775 842 1145 67 -50 -8 C ATOM 1094 C LEU A 135 21.501 -19.854 4.758 1.00 7.11 C ANISOU 1094 C LEU A 135 739 776 1187 75 -48 55 C ATOM 1095 O LEU A 135 21.960 -20.831 4.153 1.00 7.41 O ANISOU 1095 O LEU A 135 835 743 1236 134 -30 27 O ATOM 1096 CB LEU A 135 19.274 -19.026 3.953 1.00 7.94 C ANISOU 1096 CB LEU A 135 795 965 1254 162 -70 0 C ATOM 1097 CG LEU A 135 17.751 -19.102 4.045 1.00 8.11 C ANISOU 1097 CG LEU A 135 676 950 1452 52 -70 66 C ATOM 1098 CD1 LEU A 135 17.114 -18.122 3.066 1.00 9.51 C ANISOU 1098 CD1 LEU A 135 850 1412 1350 163 -12 1 C ATOM 1099 CD2 LEU A 135 17.250 -20.524 3.793 1.00 11.15 C ANISOU 1099 CD2 LEU A 135 870 1433 1934 -102 -239 16 C ATOM 1100 N GLU A 136 22.261 -18.856 5.201 1.00 7.31 N ANISOU 1100 N GLU A 136 632 889 1254 52 169 87 N ATOM 1101 CA GLU A 136 23.713 -18.911 5.054 1.00 7.30 C ANISOU 1101 CA GLU A 136 612 853 1309 40 149 -69 C ATOM 1102 C GLU A 136 24.303 -20.043 5.894 1.00 7.68 C ANISOU 1102 C GLU A 136 653 897 1366 -45 44 -5 C ATOM 1103 O GLU A 136 25.187 -20.760 5.437 1.00 8.09 O ANISOU 1103 O GLU A 136 700 909 1462 197 99 -50 O ATOM 1104 CB GLU A 136 24.354 -17.576 5.435 1.00 8.58 C ANISOU 1104 CB GLU A 136 865 887 1508 -45 207 -112 C ATOM 1105 CG GLU A 136 24.129 -16.494 4.411 1.00 9.98 C ANISOU 1105 CG GLU A 136 1086 1076 1629 -65 439 -13 C ATOM 1106 CD GLU A 136 24.627 -15.140 4.875 1.00 12.41 C ANISOU 1106 CD GLU A 136 1458 1430 1824 -256 405 -53 C ATOM 1107 OE1 GLU A 136 24.569 -14.855 6.091 1.00 12.60 O ANISOU 1107 OE1 GLU A 136 1373 1322 2089 -92 296 -157 O ATOM 1108 OE2 GLU A 136 25.065 -14.352 4.013 1.00 16.77 O ANISOU 1108 OE2 GLU A 136 2232 1824 2313 -556 834 -181 O ATOM 1109 N LEU A 137 23.811 -20.205 7.120 1.00 7.34 N ANISOU 1109 N LEU A 137 670 866 1250 96 31 -24 N ATOM 1110 CA LEU A 137 24.292 -21.271 7.996 1.00 8.74 C ANISOU 1110 CA LEU A 137 954 1095 1272 166 1 -32 C ATOM 1111 C LEU A 137 24.004 -22.639 7.365 1.00 7.95 C ANISOU 1111 C LEU A 137 764 977 1278 149 -39 146 C ATOM 1112 O LEU A 137 24.856 -23.527 7.343 1.00 8.29 O ANISOU 1112 O LEU A 137 963 865 1319 274 4 41 O ATOM 1113 CB LEU A 137 23.608 -21.156 9.359 1.00 8.97 C ANISOU 1113 CB LEU A 137 1021 1125 1260 299 -10 91 C ATOM 1114 CG LEU A 137 23.991 -22.245 10.363 1.00 10.80 C ANISOU 1114 CG LEU A 137 1152 1611 1341 312 -11 205 C ATOM 1115 CD1 LEU A 137 25.476 -22.173 10.724 1.00 12.60 C ANISOU 1115 CD1 LEU A 137 1239 1947 1600 258 -131 329 C ATOM 1116 CD2 LEU A 137 23.134 -22.125 11.606 1.00 11.96 C ANISOU 1116 CD2 LEU A 137 1458 1649 1435 291 327 102 C ATOM 1117 N PHE A 138 22.790 -22.799 6.856 1.00 7.77 N ANISOU 1117 N PHE A 138 801 1012 1140 88 41 37 N ATOM 1118 CA PHE A 138 22.383 -24.012 6.148 1.00 8.13 C ANISOU 1118 CA PHE A 138 844 962 1280 99 140 -10 C ATOM 1119 C PHE A 138 23.334 -24.314 4.982 1.00 7.81 C ANISOU 1119 C PHE A 138 887 878 1203 122 40 150 C ATOM 1120 O PHE A 138 23.912 -25.402 4.894 1.00 7.66 O ANISOU 1120 O PHE A 138 940 798 1172 191 171 47 O ATOM 1121 CB PHE A 138 20.942 -23.800 5.678 1.00 8.98 C ANISOU 1121 CB PHE A 138 767 1145 1500 21 -83 -28 C ATOM 1122 CG PHE A 138 20.436 -24.808 4.684 1.00 9.46 C ANISOU 1122 CG PHE A 138 899 1022 1672 86 30 -42 C ATOM 1123 CD1 PHE A 138 20.070 -26.084 5.081 1.00 10.12 C ANISOU 1123 CD1 PHE A 138 955 1101 1788 -66 9 -86 C ATOM 1124 CD2 PHE A 138 20.243 -24.443 3.359 1.00 10.79 C ANISOU 1124 CD2 PHE A 138 1178 1259 1660 102 -75 -161 C ATOM 1125 CE1 PHE A 138 19.553 -26.996 4.158 1.00 12.27 C ANISOU 1125 CE1 PHE A 138 1357 1395 1908 -56 95 -39 C ATOM 1126 CE2 PHE A 138 19.734 -25.347 2.438 1.00 11.58 C ANISOU 1126 CE2 PHE A 138 1311 1302 1785 -93 -3 -119 C ATOM 1127 CZ PHE A 138 19.391 -26.626 2.836 1.00 11.67 C ANISOU 1127 CZ PHE A 138 1198 1264 1971 -4 -120 -161 C ATOM 1128 N ARG A 139 23.524 -23.324 4.118 1.00 8.16 N ANISOU 1128 N ARG A 139 958 921 1222 130 141 164 N ATOM 1129 CA ARG A 139 24.374 -23.448 2.934 1.00 10.31 C ANISOU 1129 CA ARG A 139 1140 1392 1384 326 159 268 C ATOM 1130 C ARG A 139 25.824 -23.731 3.317 1.00 9.34 C ANISOU 1130 C ARG A 139 1116 1130 1300 291 337 115 C ATOM 1131 O ARG A 139 26.512 -24.549 2.688 1.00 9.08 O ANISOU 1131 O ARG A 139 1172 972 1305 300 475 126 O ATOM 1132 CB ARG A 139 24.284 -22.135 2.141 1.00 13.47 C ANISOU 1132 CB ARG A 139 1392 1927 1799 335 51 302 C ATOM 1133 CG ARG A 139 24.997 -22.115 0.824 1.00 14.75 C ANISOU 1133 CG ARG A 139 1553 1996 2056 -94 -53 494 C ATOM 1134 CD ARG A 139 24.323 -21.100 -0.089 1.00 11.07 C ANISOU 1134 CD ARG A 139 1237 1291 1676 -139 -233 603 C ATOM 1135 NE ARG A 139 24.783 -19.714 0.072 1.00 10.83 N ANISOU 1135 NE ARG A 139 1077 1477 1560 -264 -130 463 N ATOM 1136 CZ ARG A 139 24.058 -18.721 0.587 1.00 11.09 C ANISOU 1136 CZ ARG A 139 944 1609 1659 -396 -53 504 C ATOM 1137 NH1 ARG A 139 22.828 -18.942 1.034 1.00 12.28 N ANISOU 1137 NH1 ARG A 139 960 1770 1935 -312 49 640 N ATOM 1138 NH2 ARG A 139 24.571 -17.493 0.661 1.00 11.26 N ANISOU 1138 NH2 ARG A 139 938 1595 1745 -378 63 237 N ATOM 1139 N ASN A 140 26.291 -23.046 4.351 1.00 8.94 N ANISOU 1139 N ASN A 140 860 1110 1425 203 187 252 N ATOM 1140 CA ASN A 140 27.667 -23.181 4.769 1.00 9.08 C ANISOU 1140 CA ASN A 140 944 1080 1424 86 86 181 C ATOM 1141 C ASN A 140 27.975 -24.542 5.386 1.00 8.56 C ANISOU 1141 C ASN A 140 724 1047 1479 100 62 182 C ATOM 1142 O ASN A 140 29.056 -25.109 5.186 1.00 9.21 O ANISOU 1142 O ASN A 140 899 1110 1491 153 265 262 O ATOM 1143 CB ASN A 140 28.034 -22.070 5.735 1.00 10.28 C ANISOU 1143 CB ASN A 140 945 1333 1626 98 41 65 C ATOM 1144 CG ASN A 140 29.513 -21.936 5.889 1.00 11.52 C ANISOU 1144 CG ASN A 140 1167 1324 1884 80 5 28 C ATOM 1145 OD1 ASN A 140 30.052 -22.163 6.964 1.00 13.04 O ANISOU 1145 OD1 ASN A 140 1271 1939 1744 363 -291 -10 O ATOM 1146 ND2 ASN A 140 30.192 -21.599 4.799 1.00 11.54 N ANISOU 1146 ND2 ASN A 140 1064 1469 1852 -3 31 20 N ATOM 1147 N ASP A 141 27.023 -25.068 6.146 1.00 8.51 N ANISOU 1147 N ASP A 141 741 1147 1343 202 95 284 N ATOM 1148 CA ASP A 141 27.194 -26.388 6.725 1.00 8.61 C ANISOU 1148 CA ASP A 141 851 1036 1382 194 96 244 C ATOM 1149 C ASP A 141 27.143 -27.445 5.625 1.00 8.30 C ANISOU 1149 C ASP A 141 803 984 1365 161 197 338 C ATOM 1150 O ASP A 141 27.877 -28.427 5.673 1.00 9.26 O ANISOU 1150 O ASP A 141 940 1003 1573 350 166 197 O ATOM 1151 CB ASP A 141 26.178 -26.643 7.840 1.00 8.92 C ANISOU 1151 CB ASP A 141 901 1181 1307 72 287 178 C ATOM 1152 CG ASP A 141 26.544 -25.931 9.141 1.00 10.07 C ANISOU 1152 CG ASP A 141 971 1352 1503 -26 106 333 C ATOM 1153 OD1 ASP A 141 27.637 -25.332 9.219 1.00 10.80 O ANISOU 1153 OD1 ASP A 141 1015 1474 1613 -108 156 166 O ATOM 1154 OD2 ASP A 141 25.739 -25.978 10.092 1.00 11.49 O ANISOU 1154 OD2 ASP A 141 1179 1698 1486 -254 302 214 O ATOM 1155 N ILE A 142 26.309 -27.233 4.612 1.00 7.88 N ANISOU 1155 N ILE A 142 866 851 1275 150 157 55 N ATOM 1156 CA ILE A 142 26.330 -28.110 3.444 1.00 9.45 C ANISOU 1156 CA ILE A 142 890 1291 1408 360 181 110 C ATOM 1157 C ILE A 142 27.685 -28.024 2.730 1.00 9.30 C ANISOU 1157 C ILE A 142 900 1224 1407 360 155 94 C ATOM 1158 O ILE A 142 28.258 -29.039 2.342 1.00 8.60 O ANISOU 1158 O ILE A 142 891 1083 1294 395 73 -28 O ATOM 1159 CB ILE A 142 25.187 -27.775 2.460 1.00 8.53 C ANISOU 1159 CB ILE A 142 770 1162 1307 266 257 22 C ATOM 1160 CG1 ILE A 142 23.842 -28.167 3.069 1.00 10.15 C ANISOU 1160 CG1 ILE A 142 921 1381 1553 170 240 -61 C ATOM 1161 CG2 ILE A 142 25.390 -28.530 1.153 1.00 10.02 C ANISOU 1161 CG2 ILE A 142 1017 1448 1340 373 128 145 C ATOM 1162 CD1 ILE A 142 22.651 -27.723 2.246 1.00 13.36 C ANISOU 1162 CD1 ILE A 142 1129 1885 2061 215 113 47 C ATOM 1163 N ALA A 143 28.198 -26.808 2.575 1.00 9.37 N ANISOU 1163 N ALA A 143 1088 1155 1315 386 387 176 N ATOM 1164 CA ALA A 143 29.482 -26.599 1.912 1.00 9.96 C ANISOU 1164 CA ALA A 143 1137 1182 1464 383 356 196 C ATOM 1165 C ALA A 143 30.604 -27.390 2.592 1.00 9.30 C ANISOU 1165 C ALA A 143 918 1132 1481 244 257 78 C ATOM 1166 O ALA A 143 31.490 -27.925 1.921 1.00 8.96 O ANISOU 1166 O ALA A 143 960 980 1462 276 400 -28 O ATOM 1167 CB ALA A 143 29.826 -25.117 1.860 1.00 11.53 C ANISOU 1167 CB ALA A 143 1237 1274 1870 377 462 325 C ATOM 1168 N ALA A 144 30.578 -27.467 3.922 1.00 8.87 N ANISOU 1168 N ALA A 144 860 1122 1387 253 264 62 N ATOM 1169 CA ALA A 144 31.595 -28.234 4.649 1.00 9.21 C ANISOU 1169 CA ALA A 144 797 1315 1385 64 91 37 C ATOM 1170 C ALA A 144 31.509 -29.717 4.288 1.00 8.14 C ANISOU 1170 C ALA A 144 713 1128 1252 119 -10 -3 C ATOM 1171 O ALA A 144 32.532 -30.385 4.110 1.00 8.54 O ANISOU 1171 O ALA A 144 764 1082 1399 206 -89 -6 O ATOM 1172 CB ALA A 144 31.447 -28.034 6.156 1.00 10.52 C ANISOU 1172 CB ALA A 144 1270 1343 1382 -47 146 -175 C ATOM 1173 N LYS A 145 30.285 -30.230 4.182 1.00 7.74 N ANISOU 1173 N LYS A 145 763 1042 1135 87 23 -22 N ATOM 1174 CA LYS A 145 30.074 -31.619 3.773 1.00 8.41 C ANISOU 1174 CA LYS A 145 916 1049 1229 90 88 -42 C ATOM 1175 C LYS A 145 30.525 -31.838 2.327 1.00 6.98 C ANISOU 1175 C LYS A 145 631 863 1155 176 -106 -14 C ATOM 1176 O LYS A 145 31.098 -32.872 2.001 1.00 8.08 O ANISOU 1176 O LYS A 145 893 861 1313 252 -140 -154 O ATOM 1177 CB LYS A 145 28.605 -32.030 3.929 1.00 8.71 C ANISOU 1177 CB LYS A 145 824 1202 1282 65 105 3 C ATOM 1178 CG LYS A 145 28.036 -31.868 5.330 1.00 10.93 C ANISOU 1178 CG LYS A 145 1159 1478 1513 105 181 43 C ATOM 1179 CD LYS A 145 28.834 -32.653 6.352 1.00 12.41 C ANISOU 1179 CD LYS A 145 1177 2019 1518 41 186 66 C ATOM 1180 CE LYS A 145 28.178 -32.597 7.721 1.00 13.42 C ANISOU 1180 CE LYS A 145 1472 2183 1444 91 252 230 C ATOM 1181 NZ LYS A 145 29.038 -33.221 8.762 1.00 15.74 N ANISOU 1181 NZ LYS A 145 1753 2562 1664 97 141 174 N ATOM 1182 N TYR A 146 30.256 -30.868 1.461 1.00 7.73 N ANISOU 1182 N TYR A 146 807 1044 1083 302 -118 -30 N ATOM 1183 CA TYR A 146 30.719 -30.946 0.074 1.00 8.37 C ANISOU 1183 CA TYR A 146 813 1236 1129 214 1 0 C ATOM 1184 C TYR A 146 32.249 -31.010 0.015 1.00 8.32 C ANISOU 1184 C TYR A 146 777 1161 1223 255 -136 -61 C ATOM 1185 O TYR A 146 32.820 -31.800 -0.739 1.00 8.61 O ANISOU 1185 O TYR A 146 953 1242 1076 324 -9 -150 O ATOM 1186 CB TYR A 146 30.220 -29.732 -0.710 1.00 8.69 C ANISOU 1186 CB TYR A 146 789 1191 1322 163 -60 110 C ATOM 1187 CG TYR A 146 28.823 -29.853 -1.298 1.00 8.04 C ANISOU 1187 CG TYR A 146 820 1091 1144 181 -19 72 C ATOM 1188 CD1 TYR A 146 27.874 -30.725 -0.770 1.00 8.36 C ANISOU 1188 CD1 TYR A 146 786 1236 1153 50 -127 16 C ATOM 1189 CD2 TYR A 146 28.448 -29.061 -2.374 1.00 9.74 C ANISOU 1189 CD2 TYR A 146 993 1362 1344 93 -164 205 C ATOM 1190 CE1 TYR A 146 26.593 -30.816 -1.325 1.00 8.30 C ANISOU 1190 CE1 TYR A 146 833 1247 1072 1 0 113 C ATOM 1191 CE2 TYR A 146 27.183 -29.147 -2.928 1.00 10.41 C ANISOU 1191 CE2 TYR A 146 898 1494 1561 7 -147 227 C ATOM 1192 CZ TYR A 146 26.259 -30.025 -2.404 1.00 8.78 C ANISOU 1192 CZ TYR A 146 709 1268 1357 23 -94 165 C ATOM 1193 OH TYR A 146 25.002 -30.130 -2.965 1.00 9.04 O ANISOU 1193 OH TYR A 146 703 1285 1447 27 -53 145 O ATOM 1194 N LYS A 147 32.920 -30.186 0.812 1.00 8.26 N ANISOU 1194 N LYS A 147 723 1238 1177 268 -4 -21 N ATOM 1195 CA LYS A 147 34.379 -30.210 0.812 1.00 9.31 C ANISOU 1195 CA LYS A 147 804 1307 1423 258 -59 -16 C ATOM 1196 C LYS A 147 34.913 -31.559 1.280 1.00 8.16 C ANISOU 1196 C LYS A 147 720 1258 1120 227 -69 -97 C ATOM 1197 O LYS A 147 35.878 -32.080 0.728 1.00 9.33 O ANISOU 1197 O LYS A 147 768 1342 1432 280 202 -186 O ATOM 1198 CB LYS A 147 34.950 -29.086 1.670 1.00 9.53 C ANISOU 1198 CB LYS A 147 801 1385 1434 262 2 -101 C ATOM 1199 CG LYS A 147 36.474 -29.094 1.713 1.00 11.89 C ANISOU 1199 CG LYS A 147 1042 1550 1924 133 -132 -101 C ATOM 1200 CD LYS A 147 37.010 -27.900 2.489 1.00 14.02 C ANISOU 1200 CD LYS A 147 1310 1783 2233 100 -42 -184 C ATOM 1201 CE LYS A 147 38.525 -27.930 2.617 1.00 16.67 C ANISOU 1201 CE LYS A 147 1502 2242 2590 279 -2 169 C ATOM 1202 NZ LYS A 147 38.978 -28.833 3.714 1.00 17.82 N ANISOU 1202 NZ LYS A 147 1720 2260 2788 318 -37 236 N ATOM 1203 N GLU A 148 34.285 -32.123 2.302 1.00 7.96 N ANISOU 1203 N GLU A 148 685 1174 1162 247 -100 -65 N ATOM 1204 CA AGLU A 148 34.672 -33.444 2.777 0.50 9.79 C ANISOU 1204 CA AGLU A 148 939 1444 1336 234 -95 -31 C ATOM 1205 CA BGLU A 148 34.636 -33.446 2.793 0.50 9.15 C ANISOU 1205 CA BGLU A 148 896 1298 1281 217 -139 -31 C ATOM 1206 C GLU A 148 34.662 -34.446 1.633 1.00 9.66 C ANISOU 1206 C GLU A 148 873 1425 1370 281 -123 -7 C ATOM 1207 O GLU A 148 35.598 -35.241 1.484 1.00 9.85 O ANISOU 1207 O GLU A 148 939 1344 1458 311 -215 -36 O ATOM 1208 CB AGLU A 148 33.744 -33.910 3.895 0.50 12.41 C ANISOU 1208 CB AGLU A 148 1188 1948 1577 171 -55 71 C ATOM 1209 CB BGLU A 148 33.603 -33.865 3.843 0.50 10.47 C ANISOU 1209 CB BGLU A 148 1115 1476 1386 204 -122 118 C ATOM 1210 CG AGLU A 148 33.864 -33.092 5.159 0.50 14.19 C ANISOU 1210 CG AGLU A 148 1547 2209 1635 211 60 -8 C ATOM 1211 CG BGLU A 148 33.837 -35.217 4.474 0.50 9.21 C ANISOU 1211 CG BGLU A 148 1077 1172 1250 243 -137 -1 C ATOM 1212 CD AGLU A 148 32.750 -33.366 6.145 0.50 15.82 C ANISOU 1212 CD AGLU A 148 1850 2443 1716 64 169 -99 C ATOM 1213 CD BGLU A 148 32.843 -35.534 5.579 0.50 10.06 C ANISOU 1213 CD BGLU A 148 1195 1324 1302 218 -174 13 C ATOM 1214 OE1AGLU A 148 32.165 -34.469 6.090 0.50 15.56 O ANISOU 1214 OE1AGLU A 148 2072 2456 1383 34 112 82 O ATOM 1215 OE1BGLU A 148 31.816 -34.839 5.693 0.50 9.62 O ANISOU 1215 OE1BGLU A 148 1166 1381 1109 -67 -200 -82 O ATOM 1216 OE2AGLU A 148 32.464 -32.471 6.972 0.50 14.32 O ANISOU 1216 OE2AGLU A 148 1547 2458 1437 70 262 -257 O ATOM 1217 OE2BGLU A 148 33.096 -36.487 6.341 0.50 12.99 O ANISOU 1217 OE2BGLU A 148 1766 1581 1588 228 65 97 O ATOM 1218 N LEU A 149 33.616 -34.387 0.814 1.00 8.73 N ANISOU 1218 N LEU A 149 857 1248 1212 65 -200 89 N ATOM 1219 CA LEU A 149 33.438 -35.287 -0.323 1.00 9.30 C ANISOU 1219 CA LEU A 149 1011 1207 1315 194 -151 -12 C ATOM 1220 C LEU A 149 34.272 -34.908 -1.542 1.00 9.13 C ANISOU 1220 C LEU A 149 1002 1198 1267 294 -95 -72 C ATOM 1221 O LEU A 149 34.348 -35.675 -2.495 1.00 11.17 O ANISOU 1221 O LEU A 149 1485 1308 1451 240 135 -264 O ATOM 1222 CB LEU A 149 31.963 -35.331 -0.734 1.00 9.96 C ANISOU 1222 CB LEU A 149 970 1394 1418 145 -145 72 C ATOM 1223 CG LEU A 149 30.978 -35.807 0.330 1.00 9.51 C ANISOU 1223 CG LEU A 149 780 1270 1563 128 -104 44 C ATOM 1224 CD1 LEU A 149 29.550 -35.485 -0.087 1.00 12.56 C ANISOU 1224 CD1 LEU A 149 1077 1760 1933 239 -251 99 C ATOM 1225 CD2 LEU A 149 31.148 -37.300 0.578 1.00 12.05 C ANISOU 1225 CD2 LEU A 149 1119 1524 1935 215 -17 200 C ATOM 1226 N GLY A 150 34.886 -33.728 -1.520 1.00 9.39 N ANISOU 1226 N GLY A 150 1009 1280 1278 208 -2 19 N ATOM 1227 CA GLY A 150 35.605 -33.224 -2.683 1.00 9.60 C ANISOU 1227 CA GLY A 150 991 1307 1349 274 0 0 C ATOM 1228 C GLY A 150 34.671 -32.883 -3.829 1.00 9.60 C ANISOU 1228 C GLY A 150 1036 1247 1361 191 59 -52 C ATOM 1229 O GLY A 150 35.079 -32.874 -4.989 1.00 10.02 O ANISOU 1229 O GLY A 150 995 1420 1389 181 92 70 O ATOM 1230 N PHE A 151 33.417 -32.594 -3.506 1.00 9.49 N ANISOU 1230 N PHE A 151 854 1340 1410 54 -131 37 N ATOM 1231 CA PHE A 151 32.431 -32.328 -4.538 1.00 10.40 C ANISOU 1231 CA PHE A 151 1051 1369 1528 -64 1 146 C ATOM 1232 C PHE A 151 32.426 -30.879 -4.962 1.00 11.71 C ANISOU 1232 C PHE A 151 1166 1487 1796 -105 -52 100 C ATOM 1233 O PHE A 151 32.382 -29.985 -4.125 1.00 13.17 O ANISOU 1233 O PHE A 151 1828 1459 1715 -162 41 12 O ATOM 1234 CB PHE A 151 31.028 -32.711 -4.082 1.00 11.08 C ANISOU 1234 CB PHE A 151 938 1525 1745 51 -19 187 C ATOM 1235 CG PHE A 151 29.983 -32.407 -5.102 1.00 11.45 C ANISOU 1235 CG PHE A 151 1043 1375 1931 127 29 187 C ATOM 1236 CD1 PHE A 151 29.915 -33.147 -6.272 1.00 11.65 C ANISOU 1236 CD1 PHE A 151 989 1616 1820 -32 -190 177 C ATOM 1237 CD2 PHE A 151 29.081 -31.372 -4.915 1.00 12.08 C ANISOU 1237 CD2 PHE A 151 996 1452 2140 87 -47 333 C ATOM 1238 CE1 PHE A 151 28.969 -32.864 -7.230 1.00 13.82 C ANISOU 1238 CE1 PHE A 151 1233 1851 2166 8 -283 290 C ATOM 1239 CE2 PHE A 151 28.131 -31.087 -5.873 1.00 13.57 C ANISOU 1239 CE2 PHE A 151 1263 1594 2297 91 -117 311 C ATOM 1240 CZ PHE A 151 28.079 -31.829 -7.031 1.00 13.30 C ANISOU 1240 CZ PHE A 151 1114 1804 2133 -5 -181 243 C ATOM 1241 N GLN A 152 32.452 -30.655 -6.270 1.00 11.51 N ANISOU 1241 N GLN A 152 1294 1323 1755 -43 -163 2 N ATOM 1242 CA GLN A 152 32.376 -29.310 -6.816 1.00 12.55 C ANISOU 1242 CA GLN A 152 1350 1485 1934 -97 -171 62 C ATOM 1243 C GLN A 152 31.143 -29.168 -7.708 1.00 14.57 C ANISOU 1243 C GLN A 152 1601 1876 2058 106 -258 2 C ATOM 1244 O GLN A 152 30.410 -28.188 -7.612 1.00 17.62 O ANISOU 1244 O GLN A 152 1945 2045 2704 195 -260 -11 O ATOM 1245 CB GLN A 152 33.658 -28.972 -7.583 1.00 11.94 C ANISOU 1245 CB GLN A 152 1279 1577 1679 -98 -66 78 C ATOM 1246 CG GLN A 152 34.851 -28.692 -6.677 1.00 12.46 C ANISOU 1246 CG GLN A 152 1375 1508 1849 -59 -67 -14 C ATOM 1247 CD GLN A 152 34.744 -27.350 -5.987 1.00 12.23 C ANISOU 1247 CD GLN A 152 1204 1431 2010 -12 -86 -58 C ATOM 1248 OE1 GLN A 152 33.849 -26.555 -6.287 1.00 14.30 O ANISOU 1248 OE1 GLN A 152 1540 1565 2325 46 -144 27 O ATOM 1249 NE2 GLN A 152 35.661 -27.082 -5.066 1.00 12.84 N ANISOU 1249 NE2 GLN A 152 1339 1456 2081 -121 -154 -51 N ATOM 1250 N GLY A 153 30.899 -30.163 -8.555 1.00 16.62 N ANISOU 1250 N GLY A 153 1867 2151 2295 235 -541 -89 N ATOM 1251 CA GLY A 153 29.764 -30.122 -9.475 1.00 19.13 C ANISOU 1251 CA GLY A 153 2147 2665 2454 294 -595 -113 C ATOM 1252 C GLY A 153 29.611 -31.426 -10.234 1.00 22.28 C ANISOU 1252 C GLY A 153 2475 3052 2935 166 -592 -158 C ATOM 1253 O GLY A 153 30.503 -32.276 -10.212 1.00 23.46 O ANISOU 1253 O GLY A 153 2589 3197 3125 243 -574 -251 O ATOM 1254 OXT GLY A 153 28.597 -31.670 -10.888 1.00 24.25 O ANISOU 1254 OXT GLY A 153 2615 3448 3148 93 -689 -190 O TER 1255 GLY A 153 HETATM 1256 S SO4 A1156 7.942 -18.705 -20.681 1.00 18.57 S ANISOU 1256 S SO4 A1156 1870 3134 2049 -359 -263 394 S HETATM 1257 O1 SO4 A1156 8.395 -19.950 -21.304 1.00 24.93 O ANISOU 1257 O1 SO4 A1156 2935 3657 2879 -209 -77 292 O HETATM 1258 O2 SO4 A1156 6.695 -18.289 -21.312 1.00 22.62 O ANISOU 1258 O2 SO4 A1156 2495 3418 2682 -278 -384 646 O HETATM 1259 O3 SO4 A1156 7.743 -18.983 -19.260 1.00 20.49 O ANISOU 1259 O3 SO4 A1156 2356 3224 2204 -226 -253 847 O HETATM 1260 O4 SO4 A1156 8.996 -17.697 -20.847 1.00 19.12 O ANISOU 1260 O4 SO4 A1156 2011 3089 2162 -357 -310 524 O HETATM 1261 S SO4 A1157 28.758 -16.651 17.556 1.00 21.10 S ANISOU 1261 S SO4 A1157 2887 2439 2691 -630 -309 256 S HETATM 1262 O1 SO4 A1157 27.427 -17.254 17.562 1.00 24.75 O ANISOU 1262 O1 SO4 A1157 3106 3199 3098 -709 -353 135 O HETATM 1263 O2 SO4 A1157 29.748 -17.716 17.401 1.00 26.23 O ANISOU 1263 O2 SO4 A1157 3533 3203 3231 -256 -222 300 O HETATM 1264 O3 SO4 A1157 29.001 -16.000 18.836 1.00 21.36 O ANISOU 1264 O3 SO4 A1157 2879 2748 2486 -850 -683 383 O HETATM 1265 O4 SO4 A1157 28.881 -15.689 16.462 1.00 24.05 O ANISOU 1265 O4 SO4 A1157 3289 3086 2761 -581 -346 410 O HETATM 1266 FE HEM A1154 16.777 -31.091 -3.448 1.00 6.79 FE ANISOU 1266 FE HEM A1154 654 942 983 -30 -38 90 FE HETATM 1267 CHA HEM A1154 15.598 -34.295 -3.878 1.00 7.63 C ANISOU 1267 CHA HEM A1154 732 1166 1001 -1 -102 22 C HETATM 1268 CHB HEM A1154 15.497 -31.081 -0.265 1.00 7.03 C ANISOU 1268 CHB HEM A1154 529 989 1152 -2 -64 45 C HETATM 1269 CHC HEM A1154 17.843 -27.851 -3.012 1.00 7.22 C ANISOU 1269 CHC HEM A1154 643 1107 991 101 -4 174 C HETATM 1270 CHD HEM A1154 17.890 -31.011 -6.674 1.00 7.28 C ANISOU 1270 CHD HEM A1154 620 1011 1135 89 -73 63 C HETATM 1271 NA HEM A1154 15.732 -32.420 -2.313 1.00 6.78 N ANISOU 1271 NA HEM A1154 543 950 1081 -1 4 79 N HETATM 1272 C1A HEM A1154 15.395 -33.713 -2.654 1.00 7.03 C ANISOU 1272 C1A HEM A1154 553 1044 1073 -54 -185 25 C HETATM 1273 C2A HEM A1154 14.787 -34.347 -1.511 1.00 7.25 C ANISOU 1273 C2A HEM A1154 711 1037 1004 -14 -99 67 C HETATM 1274 C3A HEM A1154 14.744 -33.457 -0.521 1.00 7.67 C ANISOU 1274 C3A HEM A1154 649 1144 1118 -54 -43 93 C HETATM 1275 C4A HEM A1154 15.329 -32.229 -1.005 1.00 6.41 C ANISOU 1275 C4A HEM A1154 487 884 1062 -6 64 39 C HETATM 1276 CMA HEM A1154 14.180 -33.685 0.890 1.00 7.91 C ANISOU 1276 CMA HEM A1154 786 1193 1025 -38 111 41 C HETATM 1277 CAA HEM A1154 14.292 -35.806 -1.477 1.00 8.17 C ANISOU 1277 CAA HEM A1154 832 1017 1255 -53 -136 159 C HETATM 1278 CBA HEM A1154 15.286 -36.649 -0.663 1.00 8.43 C ANISOU 1278 CBA HEM A1154 754 1032 1414 -74 -37 152 C HETATM 1279 CGA HEM A1154 16.698 -36.674 -1.209 1.00 8.57 C ANISOU 1279 CGA HEM A1154 919 1073 1262 -30 -33 121 C HETATM 1280 O1A HEM A1154 16.895 -37.108 -2.376 1.00 10.69 O ANISOU 1280 O1A HEM A1154 1226 1307 1526 4 81 -61 O HETATM 1281 O2A HEM A1154 17.635 -36.286 -0.456 1.00 9.52 O ANISOU 1281 O2A HEM A1154 877 1374 1364 7 -43 47 O HETATM 1282 NB HEM A1154 16.684 -29.731 -1.931 1.00 6.28 N ANISOU 1282 NB HEM A1154 590 869 924 20 -64 -135 N HETATM 1283 C1B HEM A1154 16.133 -29.928 -0.680 1.00 6.76 C ANISOU 1283 C1B HEM A1154 570 944 1055 28 -47 43 C HETATM 1284 C2B HEM A1154 16.321 -28.734 0.110 1.00 6.84 C ANISOU 1284 C2B HEM A1154 548 1164 883 -47 9 44 C HETATM 1285 C3B HEM A1154 16.962 -27.844 -0.657 1.00 7.40 C ANISOU 1285 C3B HEM A1154 748 1019 1044 82 -87 142 C HETATM 1286 C4B HEM A1154 17.196 -28.449 -1.952 1.00 6.90 C ANISOU 1286 C4B HEM A1154 600 1007 1014 6 -118 200 C HETATM 1287 CMB HEM A1154 15.852 -28.564 1.574 1.00 7.76 C ANISOU 1287 CMB HEM A1154 787 1181 980 -123 87 104 C HETATM 1288 CAB HEM A1154 17.392 -26.415 -0.283 1.00 8.55 C ANISOU 1288 CAB HEM A1154 862 1143 1241 -38 -81 211 C HETATM 1289 CBB HEM A1154 16.587 -25.619 0.431 1.00 9.34 C ANISOU 1289 CBB HEM A1154 1080 1248 1220 158 -179 204 C HETATM 1290 NC HEM A1154 17.730 -29.697 -4.606 1.00 6.95 N ANISOU 1290 NC HEM A1154 608 957 1074 21 0 155 N HETATM 1291 C1C HEM A1154 18.016 -28.397 -4.263 1.00 6.87 C ANISOU 1291 C1C HEM A1154 595 956 1058 7 55 194 C HETATM 1292 C2C HEM A1154 18.508 -27.711 -5.440 1.00 7.63 C ANISOU 1292 C2C HEM A1154 641 1064 1193 1 51 215 C HETATM 1293 C3C HEM A1154 18.506 -28.596 -6.448 1.00 7.82 C ANISOU 1293 C3C HEM A1154 846 1013 1110 126 -36 171 C HETATM 1294 C4C HEM A1154 18.027 -29.856 -5.941 1.00 7.50 C ANISOU 1294 C4C HEM A1154 766 878 1205 147 -45 36 C HETATM 1295 CMC HEM A1154 18.937 -26.231 -5.462 1.00 8.90 C ANISOU 1295 CMC HEM A1154 852 1063 1464 -133 105 302 C HETATM 1296 CAC HEM A1154 18.910 -28.414 -7.925 1.00 9.99 C ANISOU 1296 CAC HEM A1154 959 1440 1394 245 16 196 C HETATM 1297 CBC HEM A1154 19.142 -27.224 -8.476 1.00 10.48 C ANISOU 1297 CBC HEM A1154 976 1479 1525 160 69 244 C HETATM 1298 ND HEM A1154 16.771 -32.429 -4.996 1.00 7.20 N ANISOU 1298 ND HEM A1154 703 1029 1002 23 -161 -110 N HETATM 1299 C1D HEM A1154 17.273 -32.164 -6.265 1.00 7.40 C ANISOU 1299 C1D HEM A1154 603 1159 1050 88 -60 -12 C HETATM 1300 C2D HEM A1154 17.002 -33.285 -7.125 1.00 8.36 C ANISOU 1300 C2D HEM A1154 893 1214 1067 127 -150 -74 C HETATM 1301 C3D HEM A1154 16.292 -34.294 -6.258 1.00 9.08 C ANISOU 1301 C3D HEM A1154 903 1351 1194 72 -161 -75 C HETATM 1302 C4D HEM A1154 16.183 -33.687 -4.959 1.00 7.80 C ANISOU 1302 C4D HEM A1154 764 1051 1145 29 -84 -1 C HETATM 1303 CMD HEM A1154 17.347 -33.456 -8.614 1.00 9.83 C ANISOU 1303 CMD HEM A1154 1176 1603 953 61 -20 -138 C HETATM 1304 CAD HEM A1154 15.743 -35.649 -6.713 1.00 9.81 C ANISOU 1304 CAD HEM A1154 1103 1254 1369 -175 -289 -159 C HETATM 1305 CBD HEM A1154 14.318 -35.306 -7.171 1.00 11.85 C ANISOU 1305 CBD HEM A1154 1415 1519 1567 -347 -246 -81 C HETATM 1306 CGD HEM A1154 13.518 -36.477 -7.669 1.00 14.90 C ANISOU 1306 CGD HEM A1154 2215 1526 1917 -163 -175 18 C HETATM 1307 O1D HEM A1154 13.718 -36.878 -8.841 1.00 16.52 O ANISOU 1307 O1D HEM A1154 2838 1403 2034 -158 -229 -137 O HETATM 1308 O2D HEM A1154 12.658 -36.979 -6.903 1.00 17.24 O ANISOU 1308 O2D HEM A1154 2132 1904 2513 -336 3 -250 O HETATM 1309 C1 GOL A1158 8.598 -37.244 -4.226 1.00 21.28 C ANISOU 1309 C1 GOL A1158 2369 2845 2872 -750 -483 471 C HETATM 1310 O1 GOL A1158 7.780 -37.574 -5.329 1.00 20.28 O ANISOU 1310 O1 GOL A1158 2242 2664 2797 -832 -640 518 O HETATM 1311 C2 GOL A1158 9.710 -36.319 -4.702 1.00 21.03 C ANISOU 1311 C2 GOL A1158 2333 2757 2901 -644 -449 412 C HETATM 1312 O2 GOL A1158 9.226 -34.997 -4.784 1.00 19.04 O ANISOU 1312 O2 GOL A1158 2223 2094 2915 -584 -328 291 O HETATM 1313 C3 GOL A1158 10.906 -36.360 -3.761 1.00 21.33 C ANISOU 1313 C3 GOL A1158 2186 3122 2795 -750 -295 452 C HETATM 1314 O3 GOL A1158 12.040 -35.916 -4.470 1.00 21.67 O ANISOU 1314 O3 GOL A1158 2056 3255 2921 -680 -220 575 O HETATM 1315 C1 GOL A1159 7.560 -10.969 -8.275 1.00 56.39 C ANISOU 1315 C1 GOL A1159 7136 7193 7092 27 -87 -27 C HETATM 1316 O1 GOL A1159 7.919 -12.323 -8.434 1.00 55.80 O ANISOU 1316 O1 GOL A1159 7052 7160 6990 13 -141 -32 O HETATM 1317 C2 GOL A1159 8.742 -10.078 -8.640 1.00 56.71 C ANISOU 1317 C2 GOL A1159 7178 7221 7145 35 -68 -30 C HETATM 1318 O2 GOL A1159 8.445 -8.741 -8.306 1.00 56.87 O ANISOU 1318 O2 GOL A1159 7196 7261 7149 37 -68 -71 O HETATM 1319 C3 GOL A1159 9.010 -10.177 -10.137 1.00 56.82 C ANISOU 1319 C3 GOL A1159 7199 7218 7171 31 -48 -26 C HETATM 1320 O3 GOL A1159 10.354 -10.544 -10.355 1.00 56.55 O ANISOU 1320 O3 GOL A1159 7167 7164 7154 43 -52 5 O HETATM 1321 C1 GOL A1160 18.618 -11.066 22.624 1.00 33.56 C ANISOU 1321 C1 GOL A1160 4360 4234 4154 -109 -24 35 C HETATM 1322 O1 GOL A1160 18.237 -12.114 23.490 1.00 34.89 O ANISOU 1322 O1 GOL A1160 4578 4295 4381 -138 119 44 O HETATM 1323 C2 GOL A1160 18.717 -11.609 21.206 1.00 33.00 C ANISOU 1323 C2 GOL A1160 4253 4187 4099 -120 -97 -82 C HETATM 1324 O2 GOL A1160 19.204 -12.928 21.267 1.00 30.79 O ANISOU 1324 O2 GOL A1160 3993 4032 3673 -153 -124 -147 O HETATM 1325 C3 GOL A1160 19.673 -10.750 20.385 1.00 33.05 C ANISOU 1325 C3 GOL A1160 4277 4176 4104 -102 -118 -110 C HETATM 1326 O3 GOL A1160 19.302 -10.788 19.022 1.00 33.43 O ANISOU 1326 O3 GOL A1160 4217 4194 4289 -148 -289 -190 O HETATM 1327 C1 GOL A1161 16.448 -13.100 -7.224 1.00 42.62 C ANISOU 1327 C1 GOL A1161 5216 5608 5370 -70 15 109 C HETATM 1328 O1 GOL A1161 16.553 -12.848 -5.840 1.00 42.30 O ANISOU 1328 O1 GOL A1161 5213 5579 5281 -17 71 178 O HETATM 1329 C2 GOL A1161 16.579 -14.595 -7.482 1.00 42.51 C ANISOU 1329 C2 GOL A1161 5236 5562 5353 -77 -10 146 C HETATM 1330 O2 GOL A1161 15.522 -15.269 -6.839 1.00 42.09 O ANISOU 1330 O2 GOL A1161 5202 5569 5221 -104 3 192 O HETATM 1331 C3 GOL A1161 17.914 -15.095 -6.945 1.00 42.42 C ANISOU 1331 C3 GOL A1161 5259 5511 5346 -86 17 82 C HETATM 1332 O3 GOL A1161 18.583 -15.834 -7.944 1.00 42.12 O ANISOU 1332 O3 GOL A1161 5273 5414 5317 -97 37 -3 O HETATM 1333 O HOH A1155 15.076 -30.282 -4.255 1.00 7.46 O ANISOU 1333 O HOH A1155 786 1063 985 46 0 65 O HETATM 1334 O HOH Z 1 26.117 -17.938 11.644 1.00 33.28 O ANISOU 1334 O HOH Z 1 4398 5891 2355 -538 766 180 O HETATM 1335 O HOH Z 2 28.796 -20.301 14.498 1.00 44.91 O ANISOU 1335 O HOH Z 2 4008 6667 6385 2060 -454 491 O HETATM 1336 O HOH Z 3 27.403 -15.323 12.080 1.00 41.03 O ANISOU 1336 O HOH Z 3 3256 7003 5329 -108 -422 -1595 O HETATM 1337 O HOH Z 4 21.507 -18.845 19.822 1.00 40.68 O ANISOU 1337 O HOH Z 4 7084 5503 2867 30 105 1405 O HETATM 1338 O HOH Z 5 24.366 -19.980 18.670 1.00 39.33 O ANISOU 1338 O HOH Z 5 3465 7019 4460 -104 486 -405 O HETATM 1339 O HOH Z 6 23.563 -13.231 21.288 1.00 41.70 O ANISOU 1339 O HOH Z 6 5540 6957 3345 -1398 -2350 237 O HETATM 1340 O HOH Z 7 24.798 -14.723 18.338 1.00 30.23 O ANISOU 1340 O HOH Z 7 4310 4035 3140 -601 -317 -522 O HETATM 1341 O HOH Z 8 24.771 -22.750 14.744 1.00 31.00 O ANISOU 1341 O HOH Z 8 4332 3388 4056 61 -1304 80 O HETATM 1342 O HOH Z 9 23.487 -10.592 18.424 1.00 40.86 O ANISOU 1342 O HOH Z 9 4523 6057 4943 -1318 -679 233 O HETATM 1343 O HOH Z 10 22.283 -7.489 16.407 1.00 32.53 O ANISOU 1343 O HOH Z 10 4559 3424 4376 -604 -482 -314 O HETATM 1344 O HOH Z 11 14.839 -17.546 20.887 1.00 15.78 O ANISOU 1344 O HOH Z 11 1620 2248 2128 -158 96 698 O HETATM 1345 O HOH Z 12 21.704 -15.433 21.886 1.00 23.02 O ANISOU 1345 O HOH Z 12 3018 3687 2042 -614 -1000 -407 O HETATM 1346 O HOH Z 13 19.122 -21.303 23.078 1.00 23.41 O ANISOU 1346 O HOH Z 13 2546 3612 2737 -555 239 -378 O HETATM 1347 O HOH Z 14 21.227 -19.605 24.024 1.00 22.14 O ANISOU 1347 O HOH Z 14 3545 2561 2305 -622 -157 586 O HETATM 1348 O HOH Z 15 19.463 -20.551 20.220 1.00 42.30 O ANISOU 1348 O HOH Z 15 5974 7470 2627 18 -41 -1232 O HETATM 1349 O HOH Z 16 19.946 -14.861 24.258 1.00 43.99 O ANISOU 1349 O HOH Z 16 3089 8413 5209 -792 -838 -321 O HETATM 1350 O HOH Z 17 12.948 -11.977 17.968 1.00 25.42 O ANISOU 1350 O HOH Z 17 3632 2796 3230 919 945 -344 O HETATM 1351 O HOH Z 18 4.355 -10.448 12.976 1.00 27.64 O ANISOU 1351 O HOH Z 18 3007 3026 4466 582 -337 33 O HETATM 1352 O HOH Z 19 20.480 -9.327 15.658 1.00 22.28 O ANISOU 1352 O HOH Z 19 4174 1966 2325 -540 325 299 O HETATM 1353 O HOH Z 20 24.028 -12.878 16.221 1.00 34.66 O ANISOU 1353 O HOH Z 20 4041 4692 4434 -1137 -1057 974 O HETATM 1354 O HOH Z 21 20.172 -10.889 11.761 1.00 10.67 O ANISOU 1354 O HOH Z 21 1465 1084 1502 -74 -102 236 O HETATM 1355 O HOH Z 22 22.888 -20.483 16.117 1.00 57.36 O ANISOU 1355 O HOH Z 22 5774 5750 10268 -572 391 -531 O HETATM 1356 O HOH Z 23 0.979 -28.195 5.369 1.00 43.38 O ANISOU 1356 O HOH Z 23 4107 4312 8060 -427 877 604 O HETATM 1357 O HOH Z 24 9.345 -17.613 16.599 1.00 10.71 O ANISOU 1357 O HOH Z 24 1301 1392 1375 -232 127 150 O HETATM 1358 O HOH Z 25 9.164 -13.758 23.111 1.00 32.59 O ANISOU 1358 O HOH Z 25 5467 3777 3135 -817 1764 -823 O HETATM 1359 O HOH Z 26 13.911 -13.709 21.470 1.00 39.66 O ANISOU 1359 O HOH Z 26 6528 5258 3283 1531 1024 -853 O HETATM 1360 O HOH Z 27 10.295 -12.202 12.205 1.00 26.68 O ANISOU 1360 O HOH Z 27 2639 3587 3911 763 744 265 O HETATM 1361 O HOH Z 28 8.164 -21.927 12.749 1.00 17.34 O ANISOU 1361 O HOH Z 28 2535 1769 2283 -184 226 -128 O HETATM 1362 O HOH Z 29 5.714 -19.238 13.446 1.00 27.53 O ANISOU 1362 O HOH Z 29 2127 5838 2495 -974 -366 1064 O HETATM 1363 O HOH Z 30 4.143 -16.494 12.186 1.00 19.36 O ANISOU 1363 O HOH Z 30 1848 2529 2976 310 -596 -374 O HETATM 1364 O HOH Z 31 3.895 -12.690 14.339 1.00 46.98 O ANISOU 1364 O HOH Z 31 4012 5695 8140 1032 -1 -554 O HETATM 1365 O HOH Z 32 5.378 -16.934 15.138 1.00 34.95 O ANISOU 1365 O HOH Z 32 3829 6245 3203 946 1140 768 O HETATM 1366 O HOH Z 33 15.686 -14.221 -14.958 1.00 36.20 O ANISOU 1366 O HOH Z 33 6775 3356 3622 1069 -139 720 O HETATM 1367 O HOH Z 34 14.596 -14.058 -12.356 1.00 31.43 O ANISOU 1367 O HOH Z 34 4377 3642 3922 1096 459 274 O HETATM 1368 O HOH Z 35 14.347 -24.266 -18.907 1.00 19.74 O ANISOU 1368 O HOH Z 35 2299 2684 2517 134 -40 124 O HETATM 1369 O HOH Z 36 1.588 -20.993 10.239 1.00 18.87 O ANISOU 1369 O HOH Z 36 1219 2937 3013 383 604 1333 O HETATM 1370 O HOH Z 37 1.279 -17.507 4.087 1.00 13.42 O ANISOU 1370 O HOH Z 37 1492 1851 1756 176 -177 150 O HETATM 1371 O HOH Z 38 0.799 -25.427 4.597 1.00 18.91 O ANISOU 1371 O HOH Z 38 2097 1965 3124 -395 1093 196 O HETATM 1372 O HOH Z 39 7.690 -26.577 8.276 1.00 26.70 O ANISOU 1372 O HOH Z 39 2843 2520 4780 836 805 638 O HETATM 1373 O HOH Z 40 5.436 -22.527 13.121 1.00 30.54 O ANISOU 1373 O HOH Z 40 3969 4658 2976 -2510 178 355 O HETATM 1374 O HOH Z 41 2.324 -26.345 7.829 1.00 52.65 O ANISOU 1374 O HOH Z 41 7469 4342 8190 132 -455 -39 O HETATM 1375 O HOH Z 42 -0.388 -25.263 0.993 1.00 17.38 O ANISOU 1375 O HOH Z 42 1904 2147 2551 -64 -581 -423 O HETATM 1376 O HOH Z 43 -1.576 -22.671 -2.349 1.00 15.68 O ANISOU 1376 O HOH Z 43 1471 2464 2021 441 -194 -334 O HETATM 1377 O HOH Z 44 -0.191 -18.340 0.224 1.00 38.67 O ANISOU 1377 O HOH Z 44 4831 3769 6091 -692 -521 1530 O HETATM 1378 O HOH Z 45 2.392 -30.395 4.715 1.00 39.31 O ANISOU 1378 O HOH Z 45 2626 4697 7610 53 -470 173 O HETATM 1379 O HOH Z 46 3.443 -26.161 -9.740 1.00 19.97 O ANISOU 1379 O HOH Z 46 1850 3914 1821 -871 -544 617 O HETATM 1380 O HOH Z 47 12.942 -29.564 16.159 1.00 38.79 O ANISOU 1380 O HOH Z 47 3725 8036 2976 -183 859 52 O HETATM 1381 O HOH Z 48 7.963 -17.789 -8.393 1.00 25.17 O ANISOU 1381 O HOH Z 48 2649 3518 3394 1221 381 1606 O HETATM 1382 O HOH Z 49 7.177 -15.560 -6.185 1.00 40.37 O ANISOU 1382 O HOH Z 49 6151 3142 6045 517 -1632 570 O HETATM 1383 O HOH Z 50 1.944 -20.293 -5.291 1.00 40.72 O ANISOU 1383 O HOH Z 50 4471 6011 4989 -1804 -1111 1584 O HETATM 1384 O HOH Z 51 23.639 -22.506 19.598 1.00 40.55 O ANISOU 1384 O HOH Z 51 5204 6393 3808 -609 -459 217 O HETATM 1385 O HOH Z 52 24.618 -38.664 10.632 1.00 21.61 O ANISOU 1385 O HOH Z 52 2081 2431 3697 -351 5 -85 O HETATM 1386 O HOH Z 53 16.137 -17.223 -9.576 1.00 24.22 O ANISOU 1386 O HOH Z 53 2531 3566 3102 -154 364 199 O HETATM 1387 O HOH Z 54 9.700 -14.235 -9.761 1.00 34.01 O ANISOU 1387 O HOH Z 54 3633 3386 5903 635 -1264 -7 O HETATM 1388 O HOH Z 55 18.609 -34.024 17.136 1.00 50.03 O ANISOU 1388 O HOH Z 55 6708 6186 6114 -589 -704 -212 O HETATM 1389 O HOH Z 56 26.675 -42.745 10.026 1.00 21.82 O ANISOU 1389 O HOH Z 56 2764 3068 2456 -373 45 201 O HETATM 1390 O HOH Z 57 13.457 -22.109 -17.213 1.00 22.32 O ANISOU 1390 O HOH Z 57 1722 4500 2257 168 -63 -461 O HETATM 1391 O HOH Z 58 16.812 -16.507 -16.818 1.00 26.49 O ANISOU 1391 O HOH Z 58 2557 4299 3208 1358 1168 1771 O HETATM 1392 O HOH Z 59 12.393 -15.488 -12.480 1.00 32.19 O ANISOU 1392 O HOH Z 59 5099 2605 4527 -724 601 -787 O HETATM 1393 O HOH Z 60 9.468 -16.675 -10.543 1.00 27.41 O ANISOU 1393 O HOH Z 60 3003 3131 4280 335 -688 1195 O HETATM 1394 O HOH Z 61 24.341 -15.786 -11.098 1.00 25.75 O ANISOU 1394 O HOH Z 61 3640 3097 3047 -188 228 240 O HETATM 1395 O HOH Z 62 16.583 -25.812 -18.704 1.00 16.26 O ANISOU 1395 O HOH Z 62 1992 2588 1596 -81 218 347 O HETATM 1396 O HOH Z 63 22.384 -18.892 -13.508 1.00 11.76 O ANISOU 1396 O HOH Z 63 1178 1812 1478 3 284 457 O HETATM 1397 O HOH Z 64 22.562 -27.883 -14.226 1.00 16.97 O ANISOU 1397 O HOH Z 64 2068 2491 1886 31 -117 406 O HETATM 1398 O HOH Z 65 21.041 -19.050 -15.848 1.00 12.04 O ANISOU 1398 O HOH Z 65 1428 1590 1554 20 211 249 O HETATM 1399 O HOH Z 66 20.344 -30.552 -21.243 1.00 24.75 O ANISOU 1399 O HOH Z 66 1773 3922 3706 -182 -63 -264 O HETATM 1400 O HOH Z 67 16.652 -31.042 -21.441 1.00 30.68 O ANISOU 1400 O HOH Z 67 4521 4781 2356 -495 -493 391 O HETATM 1401 O HOH Z 68 1.571 -13.700 -3.853 1.00 38.07 O ANISOU 1401 O HOH Z 68 4292 4983 5187 197 -115 -2932 O HETATM 1402 O HOH Z 69 16.943 -35.768 -11.525 1.00 26.09 O ANISOU 1402 O HOH Z 69 2533 3820 3559 960 -1257 -894 O HETATM 1403 O HOH Z 70 24.082 -33.637 -13.694 1.00 30.90 O ANISOU 1403 O HOH Z 70 3454 5296 2990 482 -263 -992 O HETATM 1404 O HOH Z 71 9.041 -3.853 9.362 1.00 20.30 O ANISOU 1404 O HOH Z 71 2107 2599 3005 -42 80 -175 O HETATM 1405 O HOH Z 72 19.843 -38.048 -13.434 1.00 54.35 O ANISOU 1405 O HOH Z 72 7957 7528 5164 -710 -2013 -1313 O HETATM 1406 O HOH Z 73 10.681 -34.483 -17.425 1.00 23.61 O ANISOU 1406 O HOH Z 73 1615 4446 2908 239 89 -363 O HETATM 1407 O HOH Z 74 19.033 -35.092 -15.212 1.00 45.50 O ANISOU 1407 O HOH Z 74 6987 6937 3361 347 799 -1115 O HETATM 1408 O HOH Z 75 11.984 -37.933 -16.618 1.00 37.54 O ANISOU 1408 O HOH Z 75 4587 4930 4747 125 -1984 -1296 O HETATM 1409 O HOH Z 76 16.275 -10.724 14.693 1.00 26.05 O ANISOU 1409 O HOH Z 76 4767 2013 3116 40 392 29 O HETATM 1410 O HOH Z 77 7.468 -9.149 12.978 1.00 39.90 O ANISOU 1410 O HOH Z 77 6651 4155 4354 -37 -236 332 O HETATM 1411 O HOH Z 78 18.009 -35.366 -20.772 1.00 41.45 O ANISOU 1411 O HOH Z 78 3109 8316 4322 -1492 -227 -840 O HETATM 1412 O HOH Z 79 14.202 -28.666 -20.348 1.00 31.37 O ANISOU 1412 O HOH Z 79 3749 5039 3130 -1573 35 935 O HETATM 1413 O HOH Z 80 19.228 -12.182 -0.156 1.00 21.06 O ANISOU 1413 O HOH Z 80 2902 2101 2999 706 106 245 O HETATM 1414 O HOH Z 81 3.898 -31.135 -15.895 1.00 29.34 O ANISOU 1414 O HOH Z 81 2606 4243 4296 -1187 626 -2064 O HETATM 1415 O HOH Z 82 7.864 -31.457 -22.693 1.00 42.39 O ANISOU 1415 O HOH Z 82 7144 6361 2599 -133 -951 -165 O HETATM 1416 O HOH Z 83 11.396 -34.462 -20.219 1.00 36.57 O ANISOU 1416 O HOH Z 83 2939 4754 6201 810 -169 -1864 O HETATM 1417 O HOH Z 84 12.666 -26.050 -20.223 1.00 46.63 O ANISOU 1417 O HOH Z 84 5265 6030 6421 -1517 -1134 -811 O HETATM 1418 O HOH Z 85 11.578 -24.181 -19.113 1.00 42.85 O ANISOU 1418 O HOH Z 85 5341 4089 6851 -516 1866 1629 O HETATM 1419 O HOH Z 86 10.517 -22.102 -19.495 1.00 41.12 O ANISOU 1419 O HOH Z 86 5002 5416 5206 2115 -337 541 O HETATM 1420 O HOH Z 87 10.324 -23.850 -24.253 1.00 35.11 O ANISOU 1420 O HOH Z 87 3960 4962 4414 -1311 587 590 O HETATM 1421 O HOH Z 88 4.405 -19.596 -19.764 1.00 22.26 O ANISOU 1421 O HOH Z 88 2304 3570 2584 -190 -476 1416 O HETATM 1422 O HOH Z 89 2.599 -23.175 -21.868 1.00 21.63 O ANISOU 1422 O HOH Z 89 2751 2633 2834 -89 -1196 883 O HETATM 1423 O HOH Z 90 9.586 -17.145 -16.600 1.00 42.77 O ANISOU 1423 O HOH Z 90 5374 4841 6035 1111 -89 1619 O HETATM 1424 O HOH Z 91 -0.478 -22.723 -15.622 1.00 28.09 O ANISOU 1424 O HOH Z 91 1260 4962 4450 692 -384 2051 O HETATM 1425 O HOH Z 92 5.821 -26.069 -24.553 1.00 35.52 O ANISOU 1425 O HOH Z 92 4494 4888 4112 -55 3 -473 O HETATM 1426 O HOH Z 93 2.462 -28.834 -16.254 1.00 27.34 O ANISOU 1426 O HOH Z 93 3045 5022 2320 -27 -566 -337 O HETATM 1427 O HOH Z 94 -0.144 -30.101 -15.322 1.00 38.75 O ANISOU 1427 O HOH Z 94 6140 4641 3939 68 -821 -1043 O HETATM 1428 O HOH Z 95 0.122 -30.721 -6.210 1.00 15.34 O ANISOU 1428 O HOH Z 95 1367 1719 2739 -217 235 102 O HETATM 1429 O HOH Z 96 -2.680 -28.306 -12.226 1.00 32.49 O ANISOU 1429 O HOH Z 96 2024 4645 5673 282 -289 129 O HETATM 1430 O HOH Z 97 2.602 -35.941 -8.284 1.00 17.37 O ANISOU 1430 O HOH Z 97 1523 2900 2175 -128 -131 -266 O HETATM 1431 O HOH Z 98 5.523 -37.872 -7.588 1.00 29.11 O ANISOU 1431 O HOH Z 98 4449 3987 2623 334 -582 -362 O HETATM 1432 O HOH Z 99 7.379 -34.700 -12.420 1.00 20.86 O ANISOU 1432 O HOH Z 99 1888 3890 2146 -573 163 -884 O HETATM 1433 O HOH Z 100 -0.815 -23.796 -4.617 1.00 23.30 O ANISOU 1433 O HOH Z 100 2759 3373 2718 40 -55 -963 O HETATM 1434 O HOH Z 101 2.041 -38.207 -6.837 1.00 45.55 O ANISOU 1434 O HOH Z 101 3547 5380 8377 728 872 948 O HETATM 1435 O HOH Z 103 2.069 -30.689 -2.068 1.00 30.80 O ANISOU 1435 O HOH Z 103 1730 5162 4807 -619 -631 -2193 O HETATM 1436 O HOH Z 104 10.407 -33.369 3.459 1.00 11.25 O ANISOU 1436 O HOH Z 104 1700 1068 1505 110 414 261 O HETATM 1437 O HOH Z 105 4.850 -30.823 5.544 1.00 23.86 O ANISOU 1437 O HOH Z 105 2287 4020 2757 -138 1030 248 O HETATM 1438 O HOH Z 106 11.521 -31.962 8.286 1.00 10.16 O ANISOU 1438 O HOH Z 106 1387 873 1599 79 -86 17 O HETATM 1439 O HOH Z 107 8.970 -28.802 8.447 1.00 20.91 O ANISOU 1439 O HOH Z 107 2188 3174 2581 443 -257 -52 O HETATM 1440 O HOH Z 108 13.023 -30.169 13.631 1.00 17.52 O ANISOU 1440 O HOH Z 108 1923 2518 2213 -368 -175 972 O HETATM 1441 O HOH Z 109 14.014 -28.328 17.720 1.00 30.63 O ANISOU 1441 O HOH Z 109 5419 3436 2783 229 -831 577 O HETATM 1442 O HOH Z 110 7.982 -28.517 11.457 1.00 33.51 O ANISOU 1442 O HOH Z 110 5365 3773 3594 -1752 -1162 366 O HETATM 1443 O HOH Z 111 14.249 -32.677 13.348 1.00 21.27 O ANISOU 1443 O HOH Z 111 2537 2598 2946 -206 194 -829 O HETATM 1444 O HOH Z 112 17.667 -27.814 18.645 1.00 29.90 O ANISOU 1444 O HOH Z 112 3510 4010 3836 -6 -182 1110 O HETATM 1445 O HOH Z 113 17.182 -23.241 22.487 1.00 21.15 O ANISOU 1445 O HOH Z 113 2323 2865 2846 114 -349 483 O HETATM 1446 O HOH Z 114 23.251 -23.914 16.898 1.00 25.96 O ANISOU 1446 O HOH Z 114 2823 3802 3237 661 -598 -978 O HETATM 1447 O HOH Z 115 20.238 -22.971 19.032 1.00 22.24 O ANISOU 1447 O HOH Z 115 2494 4146 1809 -118 -497 -565 O HETATM 1448 O HOH Z 116 18.092 -24.792 20.816 1.00 34.10 O ANISOU 1448 O HOH Z 116 7025 3083 2849 -1064 -443 -509 O HETATM 1449 O HOH Z 117 16.770 -19.506 20.973 1.00 27.06 O ANISOU 1449 O HOH Z 117 2313 2227 5741 193 616 1020 O HETATM 1450 O HOH Z 118 25.431 -26.067 16.583 1.00 37.21 O ANISOU 1450 O HOH Z 118 4902 3972 5261 -632 -1186 532 O HETATM 1451 O HOH Z 119 25.196 -25.195 12.911 1.00 24.32 O ANISOU 1451 O HOH Z 119 2807 3572 2862 -1251 -641 986 O HETATM 1452 O HOH Z 120 19.091 -24.888 11.682 1.00 9.97 O ANISOU 1452 O HOH Z 120 1098 1214 1474 17 15 -307 O HETATM 1453 O HOH Z 121 30.171 -34.419 12.078 1.00 42.24 O ANISOU 1453 O HOH Z 121 3804 6825 5420 -1227 1284 -37 O HETATM 1454 O HOH Z 122 26.406 -29.801 9.933 1.00 17.73 O ANISOU 1454 O HOH Z 122 2303 1758 2676 92 -313 263 O HETATM 1455 O HOH Z 123 28.879 -31.270 12.686 1.00 35.53 O ANISOU 1455 O HOH Z 123 3713 5644 4141 -1243 -2618 -868 O HETATM 1456 O HOH Z 124 26.502 -36.936 11.504 1.00 17.85 O ANISOU 1456 O HOH Z 124 2277 2204 2301 -120 -63 197 O HETATM 1457 O HOH Z 125 21.898 -38.449 9.941 1.00 10.39 O ANISOU 1457 O HOH Z 125 1608 1101 1239 -20 158 94 O HETATM 1458 O HOH Z 126 19.790 -32.784 15.078 1.00 23.97 O ANISOU 1458 O HOH Z 126 3637 3325 2142 -460 -315 647 O HETATM 1459 O HOH Z 127 17.439 -35.115 6.013 1.00 10.32 O ANISOU 1459 O HOH Z 127 1268 1281 1372 -63 -75 70 O HETATM 1460 O HOH Z 128 17.768 -36.251 14.509 1.00 37.49 O ANISOU 1460 O HOH Z 128 4081 6064 4098 -1069 1226 561 O HETATM 1461 O HOH Z 129 25.959 -40.470 8.909 1.00 17.87 O ANISOU 1461 O HOH Z 129 2002 1967 2820 -251 -460 -294 O HETATM 1462 O HOH Z 130 29.233 -38.205 10.970 1.00 37.64 O ANISOU 1462 O HOH Z 130 4972 4709 4617 -322 787 -2122 O HETATM 1463 O HOH Z 131 22.219 -39.181 2.212 1.00 13.17 O ANISOU 1463 O HOH Z 131 1370 1473 2159 109 508 145 O HETATM 1464 O HOH Z 132 28.076 -41.511 1.537 1.00 37.09 O ANISOU 1464 O HOH Z 132 4290 6610 3190 -1029 -343 648 O HETATM 1465 O HOH Z 133 26.122 -40.561 0.731 1.00 31.71 O ANISOU 1465 O HOH Z 133 3345 2888 5812 136 1383 -1528 O HETATM 1466 O HOH Z 134 24.309 -39.634 4.227 1.00 19.96 O ANISOU 1466 O HOH Z 134 1814 2474 3296 603 554 1575 O HETATM 1467 O HOH Z 135 23.056 -40.183 -0.440 1.00 34.32 O ANISOU 1467 O HOH Z 135 5393 3127 4519 465 1474 -1150 O HETATM 1468 O HOH Z 136 27.604 -41.770 -6.675 1.00 24.98 O ANISOU 1468 O HOH Z 136 2699 2522 4270 175 309 596 O HETATM 1469 O HOH Z 137 28.098 -39.243 -0.232 1.00 23.55 O ANISOU 1469 O HOH Z 137 2200 2641 4103 -104 441 -346 O HETATM 1470 O HOH Z 138 23.327 -38.217 -11.230 1.00 38.22 O ANISOU 1470 O HOH Z 138 4404 6584 3532 1634 1384 233 O HETATM 1471 O HOH Z 139 24.020 -40.110 -9.208 1.00 36.02 O ANISOU 1471 O HOH Z 139 5977 3959 3751 -272 758 -1365 O HETATM 1472 O HOH Z 140 21.241 -39.300 -10.175 1.00 49.23 O ANISOU 1472 O HOH Z 140 8610 5975 4118 -544 -662 -1027 O HETATM 1473 O HOH Z 141 19.071 -37.356 -9.037 1.00 26.19 O ANISOU 1473 O HOH Z 141 1850 5348 2754 295 -80 -2125 O HETATM 1474 O HOH Z 142 20.577 -34.606 -10.859 1.00 16.70 O ANISOU 1474 O HOH Z 142 1790 2346 2207 295 -528 -234 O HETATM 1475 O HOH Z 143 29.292 -39.539 -6.841 1.00 30.74 O ANISOU 1475 O HOH Z 143 2604 2973 6101 302 1224 203 O HETATM 1476 O HOH Z 144 28.780 -36.518 -7.098 1.00 27.69 O ANISOU 1476 O HOH Z 144 3570 3649 3300 548 1389 243 O HETATM 1477 O HOH Z 145 26.027 -15.769 -9.000 1.00 24.93 O ANISOU 1477 O HOH Z 145 2595 4368 2508 50 509 74 O HETATM 1478 O HOH Z 146 24.473 -15.533 -7.230 1.00 31.62 O ANISOU 1478 O HOH Z 146 3724 3978 4311 -69 1428 547 O HETATM 1479 O HOH Z 147 27.951 -15.321 -5.445 1.00 12.38 O ANISOU 1479 O HOH Z 147 1015 1852 1835 -277 -112 230 O HETATM 1480 O HOH Z 148 16.825 -18.337 -7.731 1.00 24.70 O ANISOU 1480 O HOH Z 148 2559 4594 2232 865 593 1034 O HETATM 1481 O HOH Z 149 21.451 -11.973 -1.885 1.00 26.50 O ANISOU 1481 O HOH Z 149 2603 2914 4549 -786 778 -1663 O HETATM 1482 O HOH Z 150 21.421 -16.157 -6.658 1.00 23.44 O ANISOU 1482 O HOH Z 150 3542 2361 3001 -454 1309 86 O HETATM 1483 O HOH Z 151 19.598 -14.910 0.139 1.00 27.48 O ANISOU 1483 O HOH Z 151 2127 3945 4369 -496 199 -1213 O HETATM 1484 O HOH Z 152 10.247 -10.346 -4.398 1.00 22.05 O ANISOU 1484 O HOH Z 152 2460 3017 2898 -7 370 740 O HETATM 1485 O HOH Z 153 4.135 -14.045 -5.315 1.00 23.89 O ANISOU 1485 O HOH Z 153 3468 2616 2993 -17 -253 273 O HETATM 1486 O HOH Z 154 1.768 -11.133 -3.619 1.00 31.50 O ANISOU 1486 O HOH Z 154 1912 3338 6715 726 269 154 O HETATM 1487 O HOH Z 155 0.337 -19.432 -3.066 1.00 27.63 O ANISOU 1487 O HOH Z 155 2753 2925 4820 -504 -686 143 O HETATM 1488 O HOH Z 156 0.733 -14.479 -0.053 1.00 21.67 O ANISOU 1488 O HOH Z 156 1694 1677 4860 -12 459 -358 O HETATM 1489 O HOH Z 157 2.167 -4.588 3.694 1.00 33.71 O ANISOU 1489 O HOH Z 157 3628 3755 5423 -982 1583 -2237 O HETATM 1490 O HOH Z 158 6.974 -5.196 8.249 1.00 28.07 O ANISOU 1490 O HOH Z 158 4784 3059 2821 -1345 -975 934 O HETATM 1491 O HOH Z 159 1.839 -5.424 6.499 1.00 39.58 O ANISOU 1491 O HOH Z 159 4659 4906 5474 -1167 1615 -721 O HETATM 1492 O HOH Z 160 8.511 -6.689 2.733 1.00 14.27 O ANISOU 1492 O HOH Z 160 1080 1897 2445 10 -22 278 O HETATM 1493 O HOH Z 161 3.128 -5.821 8.643 1.00 34.85 O ANISOU 1493 O HOH Z 161 4998 4178 4065 441 1117 -811 O HETATM 1494 O HOH Z 162 8.248 -11.391 8.892 1.00 30.46 O ANISOU 1494 O HOH Z 162 2975 4073 4525 823 1696 105 O HETATM 1495 O HOH Z 163 6.133 -7.467 9.463 1.00 24.26 O ANISOU 1495 O HOH Z 163 2686 4304 2225 490 63 -313 O HETATM 1496 O HOH Z 164 12.592 -5.559 4.705 1.00 15.04 O ANISOU 1496 O HOH Z 164 1967 1595 2149 -558 -994 789 O HETATM 1497 O HOH Z 165 8.655 -8.817 9.520 1.00 23.40 O ANISOU 1497 O HOH Z 165 1892 3996 3003 -368 1005 830 O HETATM 1498 O HOH Z 166 9.954 -8.267 11.730 1.00 30.88 O ANISOU 1498 O HOH Z 166 3640 4792 3300 600 886 -839 O HETATM 1499 O HOH Z 167 13.309 -4.242 10.754 1.00 17.65 O ANISOU 1499 O HOH Z 167 2613 1901 2192 651 -334 -205 O HETATM 1500 O HOH Z 168 17.902 -9.487 12.413 1.00 17.15 O ANISOU 1500 O HOH Z 168 1573 2195 2749 257 -539 -639 O HETATM 1501 O HOH Z 169 15.336 -5.703 4.216 1.00 12.47 O ANISOU 1501 O HOH Z 169 1780 1244 1712 181 -346 126 O HETATM 1502 O HOH Z 170 21.892 -11.209 7.644 1.00 9.84 O ANISOU 1502 O HOH Z 170 1103 1071 1564 22 30 79 O HETATM 1503 O HOH Z 171 19.454 -10.909 2.347 1.00 13.23 O ANISOU 1503 O HOH Z 171 1664 1641 1722 537 424 593 O HETATM 1504 O HOH Z 172 24.845 -17.382 9.522 1.00 30.44 O ANISOU 1504 O HOH Z 172 2820 2545 6200 53 -1049 -331 O HETATM 1505 O HOH Z 173 20.476 -23.277 9.451 1.00 16.03 O ANISOU 1505 O HOH Z 173 1840 2002 2246 417 330 555 O HETATM 1506 O HOH Z 174 27.665 -15.378 2.638 1.00 21.62 O ANISOU 1506 O HOH Z 174 2994 2982 2236 507 271 -343 O HETATM 1507 O HOH Z 175 24.275 -12.167 6.694 1.00 13.31 O ANISOU 1507 O HOH Z 175 1341 1336 2377 -138 245 -257 O HETATM 1508 O HOH Z 176 25.800 -15.838 8.308 1.00 19.04 O ANISOU 1508 O HOH Z 176 1910 2705 2618 -132 -309 -360 O HETATM 1509 O HOH Z 177 21.236 -16.471 2.180 1.00 22.30 O ANISOU 1509 O HOH Z 177 1548 2498 4424 60 96 -881 O HETATM 1510 O HOH Z 178 23.496 -14.908 1.481 1.00 20.05 O ANISOU 1510 O HOH Z 178 2288 1739 3587 -167 1350 327 O HETATM 1511 O HOH Z 179 32.250 -21.760 8.518 1.00 30.77 O ANISOU 1511 O HOH Z 179 2289 6000 3401 -1182 -540 325 O HETATM 1512 O HOH Z 180 28.648 -22.816 9.185 1.00 23.71 O ANISOU 1512 O HOH Z 180 3254 2746 3007 -681 99 -627 O HETATM 1513 O HOH Z 181 31.847 -24.537 5.039 1.00 21.34 O ANISOU 1513 O HOH Z 181 1326 1950 4832 170 105 -49 O HETATM 1514 O HOH Z 182 32.947 -22.081 4.565 1.00 18.46 O ANISOU 1514 O HOH Z 182 1570 1996 3445 135 1070 -50 O HETATM 1515 O HOH Z 183 28.254 -24.343 11.795 1.00 31.73 O ANISOU 1515 O HOH Z 183 4566 4835 2655 1983 -1161 -520 O HETATM 1516 O HOH Z 184 28.667 -29.175 8.292 1.00 13.74 O ANISOU 1516 O HOH Z 184 1820 1545 1853 400 123 282 O HETATM 1517 O HOH Z 185 26.500 -28.144 12.025 1.00 21.04 O ANISOU 1517 O HOH Z 185 2597 2461 2935 132 312 169 O HETATM 1518 O HOH Z 186 29.983 -26.990 9.378 1.00 25.30 O ANISOU 1518 O HOH Z 186 3281 3408 2923 -779 -531 -329 O HETATM 1519 O HOH Z 187 32.434 -26.562 -0.424 1.00 19.68 O ANISOU 1519 O HOH Z 187 2611 1839 3027 251 842 626 O HETATM 1520 O HOH Z 188 30.715 -30.936 8.948 1.00 21.11 O ANISOU 1520 O HOH Z 188 2174 2182 3663 686 -312 -40 O HETATM 1521 O HOH Z 189 38.155 -27.306 6.230 1.00 23.58 O ANISOU 1521 O HOH Z 189 1688 2551 4720 -297 638 -486 O HETATM 1522 O HOH Z 190 30.086 -35.062 3.669 1.00 12.48 O ANISOU 1522 O HOH Z 190 1649 1332 1758 -62 -85 -55 O HETATM 1523 O HOH Z 191 30.098 -35.509 7.666 1.00 18.49 O ANISOU 1523 O HOH Z 191 2033 2555 2435 122 371 108 O HETATM 1524 O HOH Z 192 33.732 -38.562 7.118 1.00 17.92 O ANISOU 1524 O HOH Z 192 1401 2619 2786 -287 421 -477 O HETATM 1525 O HOH Z 193 35.465 -32.633 -7.624 1.00 26.18 O ANISOU 1525 O HOH Z 193 2340 5860 1746 -1254 -246 673 O HETATM 1526 O HOH Z 194 33.284 -28.275 -2.422 1.00 22.87 O ANISOU 1526 O HOH Z 194 2641 2880 3168 -465 109 -138 O HETATM 1527 O HOH Z 195 31.461 -27.622 -3.319 1.00 21.65 O ANISOU 1527 O HOH Z 195 1703 3824 2699 158 507 -257 O HETATM 1528 O HOH Z 196 29.773 -27.137 -5.339 1.00 19.06 O ANISOU 1528 O HOH Z 196 1277 3225 2739 712 125 421 O HETATM 1529 O HOH Z 197 32.219 -24.858 -5.265 1.00 42.23 O ANISOU 1529 O HOH Z 197 3694 6754 5595 1080 1811 -1765 O HETATM 1530 O HOH Z 198 31.374 -25.488 -8.259 1.00 31.34 O ANISOU 1530 O HOH Z 198 3996 2880 5029 407 764 20 O HETATM 1531 O HOH Z 199 32.720 -32.713 -8.303 1.00 20.20 O ANISOU 1531 O HOH Z 199 2398 3120 2155 217 -358 -826 O HETATM 1532 O HOH Z 200 27.001 -29.588 -12.083 1.00 26.19 O ANISOU 1532 O HOH Z 200 2633 4259 3059 -620 -168 -835 O HETATM 1533 O HOH Z 201 16.183 -38.411 -9.015 1.00 36.43 O ANISOU 1533 O HOH Z 201 5127 3455 5257 116 -1944 -820 O HETATM 1534 O HOH Z 202 13.447 -38.173 -4.996 1.00 28.86 O ANISOU 1534 O HOH Z 202 4033 2731 4199 -1534 -1043 211 O HETATM 1535 O HOH Z 203 14.926 -39.085 -3.012 1.00 20.78 O ANISOU 1535 O HOH Z 203 2543 2358 2991 -316 -305 -752 O HETATM 1536 O HOH Z 204 18.419 -39.610 -2.296 1.00 16.83 O ANISOU 1536 O HOH Z 204 2472 1620 2299 -640 427 -151 O HETATM 1537 O HOH Z 205 14.143 -35.309 -10.934 1.00 19.72 O ANISOU 1537 O HOH Z 205 2331 2407 2752 -292 -607 719 O HETATM 1538 O HOH Z 206 12.140 -18.582 -21.363 1.00 35.12 O ANISOU 1538 O HOH Z 206 3270 4764 5307 1059 -501 979 O HETATM 1539 O HOH Z 207 8.785 -20.725 -23.682 1.00 24.09 O ANISOU 1539 O HOH Z 207 1334 3764 4055 112 167 -975 O HETATM 1540 O HOH Z 208 24.811 -17.362 18.845 1.00 33.98 O ANISOU 1540 O HOH Z 208 3832 4642 4434 -201 -1555 -1008 O HETATM 1541 O HOH Z 209 27.493 -14.083 19.710 1.00 34.01 O ANISOU 1541 O HOH Z 209 4148 2839 5933 -712 1714 -1069 O HETATM 1542 O HOH Z 210 30.900 -19.249 18.956 1.00 18.98 O ANISOU 1542 O HOH Z 210 3107 2393 1710 454 468 76 O HETATM 1543 O HOH Z 211 7.443 -34.581 -6.501 1.00 17.73 O ANISOU 1543 O HOH Z 211 1518 2058 3160 -356 -91 -118 O HETATM 1544 O HOH Z 212 8.315 -12.876 -11.197 1.00 40.15 O ANISOU 1544 O HOH Z 212 4949 6784 3520 -693 -121 -723 O HETATM 1545 O HOH Z 213 9.096 -10.451 -13.035 1.00 28.91 O ANISOU 1545 O HOH Z 213 2844 4936 3203 -685 -405 694 O HETATM 1546 O HOH Z 214 12.719 -10.143 -10.145 1.00 21.15 O ANISOU 1546 O HOH Z 214 3944 1543 2549 -43 -1354 126 O HETATM 1547 O HOH Z 215 15.154 -11.285 21.883 1.00 36.89 O ANISOU 1547 O HOH Z 215 3959 6034 4022 -341 -27 -2171 O HETATM 1548 O HOH Z 216 17.138 -10.283 17.361 1.00 31.94 O ANISOU 1548 O HOH Z 216 5061 2859 4212 528 804 666 O HETATM 1549 O HOH Z 217 16.151 -10.512 -6.756 1.00 36.54 O ANISOU 1549 O HOH Z 217 6146 1935 5802 -287 -2576 17 O HETATM 1550 O HOH Z 218 16.822 -14.746 -10.485 1.00 33.54 O ANISOU 1550 O HOH Z 218 5023 3318 4402 593 467 1241 O HETATM 1551 O HOH Z 219 16.613 -12.558 -3.420 1.00 16.47 O ANISOU 1551 O HOH Z 219 1791 1458 3007 -270 164 134 O CONECT 768 1266 CONECT 1256 1257 1258 1259 1260 CONECT 1257 1256 CONECT 1258 1256 CONECT 1259 1256 CONECT 1260 1256 CONECT 1261 1262 1263 1264 1265 CONECT 1262 1261 CONECT 1263 1261 CONECT 1264 1261 CONECT 1265 1261 CONECT 1266 768 1271 1282 1290 CONECT 1266 1298 1333 CONECT 1267 1272 1302 CONECT 1268 1275 1283 CONECT 1269 1286 1291 CONECT 1270 1294 1299 CONECT 1271 1266 1272 1275 CONECT 1272 1267 1271 1273 CONECT 1273 1272 1274 1277 CONECT 1274 1273 1275 1276 CONECT 1275 1268 1271 1274 CONECT 1276 1274 CONECT 1277 1273 1278 CONECT 1278 1277 1279 CONECT 1279 1278 1280 1281 CONECT 1280 1279 CONECT 1281 1279 CONECT 1282 1266 1283 1286 CONECT 1283 1268 1282 1284 CONECT 1284 1283 1285 1287 CONECT 1285 1284 1286 1288 CONECT 1286 1269 1282 1285 CONECT 1287 1284 CONECT 1288 1285 1289 CONECT 1289 1288 CONECT 1290 1266 1291 1294 CONECT 1291 1269 1290 1292 CONECT 1292 1291 1293 1295 CONECT 1293 1292 1294 1296 CONECT 1294 1270 1290 1293 CONECT 1295 1292 CONECT 1296 1293 1297 CONECT 1297 1296 CONECT 1298 1266 1299 1302 CONECT 1299 1270 1298 1300 CONECT 1300 1299 1301 1303 CONECT 1301 1300 1302 1304 CONECT 1302 1267 1298 1301 CONECT 1303 1300 CONECT 1304 1301 1305 CONECT 1305 1304 1306 CONECT 1306 1305 1307 1308 CONECT 1307 1306 CONECT 1308 1306 CONECT 1309 1310 1311 CONECT 1310 1309 CONECT 1311 1309 1312 1313 CONECT 1312 1311 CONECT 1313 1311 1314 CONECT 1314 1313 CONECT 1315 1316 1317 CONECT 1316 1315 CONECT 1317 1315 1318 1319 CONECT 1318 1317 CONECT 1319 1317 1320 CONECT 1320 1319 CONECT 1321 1322 1323 CONECT 1322 1321 CONECT 1323 1321 1324 1325 CONECT 1324 1323 CONECT 1325 1323 1326 CONECT 1326 1325 CONECT 1327 1328 1329 CONECT 1328 1327 CONECT 1329 1327 1330 1331 CONECT 1330 1329 CONECT 1331 1329 1332 CONECT 1332 1331 CONECT 1333 1266 MASTER 284 0 7 8 0 0 18 6 1550 1 80 12 END