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*** TRANSFERASE 19-DEC-18 6QAI ***elNémo ID: 23021810221077405Job options:ID = 23021810221077405 JOBID = TRANSFERASE 19-DEC-18 6QAI USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER TRANSFERASE 19-DEC-18 6QAI TITLE 2-DESOXIRIBOSYLTRANSFERASE FROM LEISHMANIA MEXICANA COMPND MOL_ID: 1; COMPND 2 MOLECULE: 2-DEOXYRIBOSYLTRANSFERASE; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LEISHMANIA MEXICANA; SOURCE 3 ORGANISM_TAXID: 5665; SOURCE 4 GENE: LMXM_23_1580; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS DEOXYRIBOSYLTRANSFERASE, ENZYMATIC SYNTHESIS, OLIGOMERIC ASSEMBLY, KEYWDS 2 PURINE NUCLEOSIDE ANALOGUES, PROTEIN CRYSTALLOGRAPHY, TRANSFERASE EXPDTA X-RAY DIFFRACTION AUTHOR N.CRESPO,J.M.MANCHENO REVDAT 1 26-DEC-18 6QAI 0 SPRSDE 26-DEC-18 6QAI 5NBR JRNL AUTH N.CRESPO,P.A.SANCHEZ-MURCIA,F.GAGO,J.CEJUDO-SANCHES, JRNL AUTH 2 M.A.GALMES,J.FERNANDEZ-LUCAS,J.M.MANCHENO JRNL TITL 2'-DEOXYRIBOSYLTRANSFERASE FROM LEISHMANIA MEXICANA, AN JRNL TITL 2 EFFICIENT BIOCATALYST FOR ONE-POT, ONE-STEP SYNTHESIS OF JRNL TITL 3 NUCLEOSIDES FROM POORLY SOLUBLE PURINE BASES. JRNL REF APPL.MICROBIOL.BIOTECHNOL. V. 101 7187 2017 JRNL REFN ISSN 0175-7598 JRNL PMID 28785897 JRNL DOI 10.1007/S00253-017-8450-Y REMARK 2 REMARK 2 RESOLUTION. 1.66 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.14_3260: ???) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.66 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.85 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4 REMARK 3 NUMBER OF REFLECTIONS : 33853 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.171 REMARK 3 R VALUE (WORKING SET) : 0.169 REMARK 3 FREE R VALUE : 0.200 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.910 REMARK 3 FREE R VALUE TEST SET COUNT : 2000 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 39.8636 - 3.9996 0.99 2406 147 0.1393 0.1648 REMARK 3 2 3.9996 - 3.1750 0.99 2340 142 0.1568 0.1876 REMARK 3 3 3.1750 - 2.7738 0.99 2308 147 0.1867 0.2221 REMARK 3 4 2.7738 - 2.5202 0.98 2305 150 0.1847 0.2034 REMARK 3 5 2.5202 - 2.3396 0.98 2288 144 0.1722 0.1923 REMARK 3 6 2.3396 - 2.2017 0.98 2247 140 0.1726 0.2047 REMARK 3 7 2.2017 - 2.0914 0.98 2292 142 0.1790 0.2197 REMARK 3 8 2.0914 - 2.0004 0.97 2245 150 0.1931 0.2445 REMARK 3 9 2.0004 - 1.9234 0.97 2249 134 0.1970 0.2468 REMARK 3 10 1.9234 - 1.8570 0.97 2252 143 0.1906 0.2050 REMARK 3 11 1.8570 - 1.7989 0.96 2248 146 0.2012 0.2339 REMARK 3 12 1.7989 - 1.7475 0.96 2244 135 0.2169 0.2651 REMARK 3 13 1.7475 - 1.7015 0.96 2223 143 0.2205 0.2244 REMARK 3 14 1.7015 - 1.6600 0.96 2206 137 0.2425 0.3020 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.570 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.008 2452 REMARK 3 ANGLE : 0.895 3334 REMARK 3 CHIRALITY : 0.055 366 REMARK 3 PLANARITY : 0.006 436 REMARK 3 DIHEDRAL : 3.712 1993 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 7 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 6 THROUGH 36 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.4917 -0.8844 79.1135 REMARK 3 T TENSOR REMARK 3 T11: 0.1180 T22: 0.1203 REMARK 3 T33: 0.1924 T12: 0.0076 REMARK 3 T13: -0.0163 T23: 0.0213 REMARK 3 L TENSOR REMARK 3 L11: 2.9880 L22: 5.6911 REMARK 3 L33: 3.1305 L12: 0.7772 REMARK 3 L13: -0.6049 L23: -0.6125 REMARK 3 S TENSOR REMARK 3 S11: 0.0811 S12: 0.1807 S13: 0.2308 REMARK 3 S21: -0.1892 S22: -0.0413 S23: 0.1204 REMARK 3 S31: -0.2224 S32: -0.0851 S33: -0.0055 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 37 THROUGH 66 ) REMARK 3 ORIGIN FOR THE GROUP (A): -35.8773 -0.0171 85.1042 REMARK 3 T TENSOR REMARK 3 T11: 0.2134 T22: 0.2661 REMARK 3 T33: 0.2612 T12: 0.0861 REMARK 3 T13: -0.0452 T23: -0.0251 REMARK 3 L TENSOR REMARK 3 L11: 3.5624 L22: 4.5605 REMARK 3 L33: 3.2712 L12: -1.6118 REMARK 3 L13: -0.2534 L23: 0.4411 REMARK 3 S TENSOR REMARK 3 S11: -0.1062 S12: -0.0688 S13: 0.2207 REMARK 3 S21: 0.0915 S22: 0.0602 S23: 0.3197 REMARK 3 S31: -0.5008 S32: -0.7354 S33: -0.0324 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 67 THROUGH 145 ) REMARK 3 ORIGIN FOR THE GROUP (A): -19.4538 -4.8206 96.7774 REMARK 3 T TENSOR REMARK 3 T11: 0.1759 T22: 0.3278 REMARK 3 T33: 0.2245 T12: -0.0080 REMARK 3 T13: -0.0241 T23: -0.0478 REMARK 3 L TENSOR REMARK 3 L11: 1.0059 L22: 1.4419 REMARK 3 L33: 3.8918 L12: -0.2022 REMARK 3 L13: -0.3994 L23: 0.7386 REMARK 3 S TENSOR REMARK 3 S11: 0.0362 S12: -0.5133 S13: 0.0226 REMARK 3 S21: 0.1823 S22: 0.1687 S23: -0.2230 REMARK 3 S31: -0.0960 S32: 0.6634 S33: -0.1110 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 146 THROUGH 158 ) REMARK 3 ORIGIN FOR THE GROUP (A): -22.6391 -18.2044 81.4480 REMARK 3 T TENSOR REMARK 3 T11: 0.2146 T22: 0.0768 REMARK 3 T33: 0.3124 T12: 0.0096 REMARK 3 T13: -0.0297 T23: -0.0096 REMARK 3 L TENSOR REMARK 3 L11: 6.9101 L22: 8.4571 REMARK 3 L33: 4.0550 L12: 0.1619 REMARK 3 L13: -2.5148 L23: -4.3321 REMARK 3 S TENSOR REMARK 3 S11: 0.0223 S12: 0.0034 S13: -0.4503 REMARK 3 S21: -0.1799 S22: 0.0917 S23: 0.5910 REMARK 3 S31: 0.4714 S32: 0.1659 S33: -0.1297 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 8 THROUGH 36 ) REMARK 3 ORIGIN FOR THE GROUP (A): -32.0377 -1.0090 118.2717 REMARK 3 T TENSOR REMARK 3 T11: 0.5201 T22: 0.8271 REMARK 3 T33: 0.3093 T12: -0.0307 REMARK 3 T13: 0.1217 T23: -0.0662 REMARK 3 L TENSOR REMARK 3 L11: 1.4919 L22: 2.7269 REMARK 3 L33: 2.1866 L12: 0.1230 REMARK 3 L13: -1.6957 L23: -0.9724 REMARK 3 S TENSOR REMARK 3 S11: -0.1283 S12: -0.8511 S13: -0.0804 REMARK 3 S21: 0.9001 S22: 0.0521 S23: 0.3097 REMARK 3 S31: 0.0600 S32: -0.1299 S33: 0.0127 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 37 THROUGH 53 ) REMARK 3 ORIGIN FOR THE GROUP (A): -27.4283 -11.7608 111.8464 REMARK 3 T TENSOR REMARK 3 T11: 0.6467 T22: 0.6155 REMARK 3 T33: 0.2639 T12: -0.0601 REMARK 3 T13: 0.0404 T23: 0.0784 REMARK 3 L TENSOR REMARK 3 L11: 3.9557 L22: 1.7377 REMARK 3 L33: 4.9467 L12: -0.7537 REMARK 3 L13: -3.5563 L23: 2.3492 REMARK 3 S TENSOR REMARK 3 S11: -0.1786 S12: -1.4055 S13: -0.7934 REMARK 3 S21: 1.4002 S22: -0.1204 S23: 0.1812 REMARK 3 S31: 0.8561 S32: 0.4639 S33: 0.2721 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 54 THROUGH 157 ) REMARK 3 ORIGIN FOR THE GROUP (A): -33.7384 4.9053 103.1622 REMARK 3 T TENSOR REMARK 3 T11: 0.3050 T22: 0.4296 REMARK 3 T33: 0.2457 T12: 0.0684 REMARK 3 T13: 0.0532 T23: -0.1299 REMARK 3 L TENSOR REMARK 3 L11: 1.9888 L22: 2.9830 REMARK 3 L33: 4.6003 L12: -0.0467 REMARK 3 L13: 0.5536 L23: 1.3083 REMARK 3 S TENSOR REMARK 3 S11: 0.0902 S12: -0.5638 S13: 0.2977 REMARK 3 S21: 0.1210 S22: -0.2687 S23: 0.3086 REMARK 3 S31: -0.8309 S32: -0.6919 S33: -0.2285 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 6QAI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-DEC-18. REMARK 100 THE DEPOSITION ID IS D_1200013555. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 08-FEB-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALBA REMARK 200 BEAMLINE : XALOC REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33859 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.660 REMARK 200 RESOLUTION RANGE LOW (A) : 39.850 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7 REMARK 200 DATA REDUNDANCY : 6.800 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 18.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 2A0K REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 43.25 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 0.2 M MAGNESIUM REMARK 280 CHLORIDE, 0.1 M TRIS-HCL, PH 8.5, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-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 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 40.10450 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.13250 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 40.10450 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.13250 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4590 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 13100 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 O ILE A 45 LIES ON A SPECIAL POSITION. REMARK 375 CG2 ILE A 45 LIES ON A SPECIAL POSITION. REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 PRO A 155 REMARK 465 HIS B 0 REMARK 465 MET B 1 REMARK 465 PRO B 2 REMARK 465 ALA B 3 REMARK 465 THR B 154 REMARK 465 PRO B 155 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 DISTANCE REMARK 500 OD2 ASP A 64 O2 TRS A 202 1.71 REMARK 500 O HOH A 332 O HOH A 405 1.96 REMARK 500 O HOH B 302 O HOH B 329 2.03 REMARK 500 O HOH A 344 O HOH A 412 2.14 REMARK 500 REMARK 500 REMARK: NULL 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 C ILE A 45 O ILE A 45 2557 1.24 REMARK 500 CB ILE A 45 CG2 ILE A 45 2557 1.54 REMARK 500 C ILE A 45 C ILE A 45 2557 2.19 REMARK 500 REMARK 500 REMARK: NULL 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),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 ASP A 64 CB ASP A 64 CG 0.144 REMARK 500 ASP A 64 CG ASP A 64 OD2 0.138 REMARK 500 CYS B 80 CB CYS B 80 SG -0.097 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ASP A 64 CB - CG - OD1 ANGL. DEV. = -9.3 DEGREES REMARK 500 ASP A 64 CB - CG - OD2 ANGL. DEV. = 17.3 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 MET A 1 74.87 -154.36 REMARK 500 ALA A 3 60.42 -153.59 REMARK 500 SER A 75 -165.39 -170.19 REMARK 500 ASN B 44 31.87 -142.64 REMARK 500 ARG B 74 -12.84 69.19 REMARK 500 SER B 75 -154.60 -149.80 REMARK 500 HIS B 152 44.27 -144.50 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 ILE A 45 12.22 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue TRS B 201 DBREF 6QAI A 1 155 UNP E9AWJ0 E9AWJ0_LEIMU 1 155 DBREF 6QAI B 1 155 UNP E9AWJ0 E9AWJ0_LEIMU 1 155 SEQADV 6QAI HIS A 0 UNP E9AWJ0 EXPRESSION TAG SEQADV 6QAI HIS B 0 UNP E9AWJ0 EXPRESSION TAG SEQRES 1 A 156 HIS MET PRO ALA PRO LYS THR ILE TYR ILE ALA GLY PRO SEQRES 2 A 156 ALA VAL PHE HIS PRO ASP ASN GLY GLU ALA TYR TYR ASN SEQRES 3 A 156 ASN VAL ARG ALA LEU MET LYS GLY LYS ASP VAL VAL PRO SEQRES 4 A 156 LEU ILE PRO THR ASP ASN ILE ALA THR GLY ALA VAL ASN SEQRES 5 A 156 ILE ARG ASN LYS ASN ILE ASP MET ILE ARG ALA CYS ASP SEQRES 6 A 156 ALA ILE ILE ALA ASP LEU SER PRO PHE ARG SER LYS GLU SEQRES 7 A 156 PRO ASP CYS GLY THR ALA PHE GLU LEU GLY TYR ALA ALA SEQRES 8 A 156 ALA LEU GLY LYS VAL LEU LEU THR PHE SER THR ASP THR SEQRES 9 A 156 ARG PRO MET VAL GLU LYS TYR GLY SER GLU MET ALA ASP SEQRES 10 A 156 GLY LEU SER VAL GLU ASN PHE GLY LEU PRO PHE ASN LEU SEQRES 11 A 156 MET LEU HIS ASP GLY THR ASP VAL PHE ASP SER PHE GLU SEQRES 12 A 156 ALA ALA PHE ALA TYR PHE VAL GLU HIS HIS LEU THR PRO SEQRES 1 B 156 HIS MET PRO ALA PRO LYS THR ILE TYR ILE ALA GLY PRO SEQRES 2 B 156 ALA VAL PHE HIS PRO ASP ASN GLY GLU ALA TYR TYR ASN SEQRES 3 B 156 ASN VAL ARG ALA LEU MET LYS GLY LYS ASP VAL VAL PRO SEQRES 4 B 156 LEU ILE PRO THR ASP ASN ILE ALA THR GLY ALA VAL ASN SEQRES 5 B 156 ILE ARG ASN LYS ASN ILE ASP MET ILE ARG ALA CYS ASP SEQRES 6 B 156 ALA ILE ILE ALA ASP LEU SER PRO PHE ARG SER LYS GLU SEQRES 7 B 156 PRO ASP CYS GLY THR ALA PHE GLU LEU GLY TYR ALA ALA SEQRES 8 B 156 ALA LEU GLY LYS VAL LEU LEU THR PHE SER THR ASP THR SEQRES 9 B 156 ARG PRO MET VAL GLU LYS TYR GLY SER GLU MET ALA ASP SEQRES 10 B 156 GLY LEU SER VAL GLU ASN PHE GLY LEU PRO PHE ASN LEU SEQRES 11 B 156 MET LEU HIS ASP GLY THR ASP VAL PHE ASP SER PHE GLU SEQRES 12 B 156 ALA ALA PHE ALA TYR PHE VAL GLU HIS HIS LEU THR PRO HET TRS A 201 8 HET TRS A 202 8 HET TRS B 201 8 HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL HETSYN TRS TRIS BUFFER FORMUL 3 TRS 3(C4 H12 N O3 1+) FORMUL 6 HOH *224(H2 O) HELIX 1 AA1 GLY A 11 HIS A 16 5 6 HELIX 2 AA2 GLY A 20 LYS A 32 1 13 HELIX 3 AA3 GLY A 48 CYS A 63 1 16 HELIX 4 AA4 ASP A 79 GLY A 93 1 15 HELIX 5 AA5 PRO A 105 GLY A 111 1 7 HELIX 6 AA6 ASN A 128 HIS A 132 5 5 HELIX 7 AA7 SER A 140 LEU A 153 1 14 HELIX 8 AA8 GLY B 11 HIS B 16 5 6 HELIX 9 AA9 GLY B 20 LYS B 32 1 13 HELIX 10 AB1 GLY B 48 CYS B 63 1 16 HELIX 11 AB2 ASP B 79 LEU B 92 1 14 HELIX 12 AB3 PRO B 105 GLY B 111 1 7 HELIX 13 AB4 ASN B 128 HIS B 132 5 5 HELIX 14 AB5 SER B 140 HIS B 152 1 13 SHEET 1 AA1 4 VAL A 36 LEU A 39 0 SHEET 2 AA1 4 LYS A 5 ALA A 10 1 N ILE A 7 O LEU A 39 SHEET 3 AA1 4 ALA A 65 ASP A 69 1 O ALA A 65 N TYR A 8 SHEET 4 AA1 4 VAL A 95 PHE A 99 1 O LEU A 97 N ALA A 68 SHEET 1 AA2 2 MET A 114 ALA A 115 0 SHEET 2 AA2 2 LEU A 118 SER A 119 -1 O LEU A 118 N ALA A 115 SHEET 1 AA3 4 VAL B 36 LEU B 39 0 SHEET 2 AA3 4 LYS B 5 ALA B 10 1 N ILE B 7 O LEU B 39 SHEET 3 AA3 4 ALA B 65 ASP B 69 1 O ALA B 65 N TYR B 8 SHEET 4 AA3 4 VAL B 95 PHE B 99 1 O LEU B 97 N ALA B 68 SHEET 1 AA4 2 MET B 114 ALA B 115 0 SHEET 2 AA4 2 LEU B 118 SER B 119 -1 O LEU B 118 N ALA B 115 LINK OD1 ASP A 43 N TRS A 201 1555 1555 1.31 LINK OD2 ASP A 64 C3 TRS A 202 1555 2557 1.43 SITE 1 AC1 13 ALA A 10 GLY A 11 VAL A 14 PHE A 15 SITE 2 AC1 13 PRO A 41 ASP A 43 ASN A 56 ASP A 79 SITE 3 AC1 13 GLY A 81 GLU A 85 HOH A 312 ASN B 128 SITE 4 AC1 13 MET B 130 SITE 1 AC2 5 PRO A 4 LYS A 5 THR A 6 ASP A 64 SITE 2 AC2 5 HOH A 322 SITE 1 AC3 11 ASN A 128 ALA B 10 GLY B 11 PHE B 15 SITE 2 AC3 11 ASP B 43 ASN B 56 ASP B 79 GLY B 81 SITE 3 AC3 11 THR B 82 GLU B 85 HOH B 303 CRYST1 80.209 46.265 87.987 90.00 115.06 90.00 C 1 2 1 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.012467 0.000000 0.005830 0.00000 SCALE2 0.000000 0.021615 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012546 0.00000 ATOM 1 N HIS A 0 -33.613 -14.238 64.353 1.00 68.45 N ATOM 2 CA HIS A 0 -34.600 -14.996 65.115 1.00 68.71 C ATOM 3 C HIS A 0 -34.121 -15.202 66.546 1.00 62.99 C ATOM 4 O HIS A 0 -33.082 -15.815 66.788 1.00 67.93 O ATOM 5 CB HIS A 0 -34.888 -16.345 64.452 1.00 77.03 C ATOM 6 CG HIS A 0 -36.019 -17.098 65.084 1.00 81.12 C ATOM 7 ND1 HIS A 0 -35.834 -17.994 66.116 1.00 82.38 N ATOM 8 CD2 HIS A 0 -37.349 -17.088 64.829 1.00 82.11 C ATOM 9 CE1 HIS A 0 -37.001 -18.503 66.470 1.00 83.49 C ATOM 10 NE2 HIS A 0 -37.937 -17.969 65.705 1.00 83.82 N ATOM 11 N MET A 1 -34.896 -14.693 67.484 1.00 46.36 N ATOM 12 CA MET A 1 -34.509 -14.651 68.886 1.00 40.28 C ATOM 13 C MET A 1 -35.776 -14.625 69.733 1.00 39.00 C ATOM 14 O MET A 1 -36.139 -13.570 70.270 1.00 36.73 O ATOM 15 CB MET A 1 -33.642 -13.420 69.157 1.00 40.51 C ATOM 16 CG MET A 1 -32.770 -13.518 70.405 1.00 53.13 C ATOM 17 SD MET A 1 -31.631 -12.119 70.560 1.00 47.42 S ATOM 18 CE MET A 1 -32.792 -10.771 70.267 1.00 41.19 C ATOM 19 N PRO A 2 -36.478 -15.756 69.867 1.00 39.22 N ATOM 20 CA PRO A 2 -37.803 -15.709 70.505 1.00 34.14 C ATOM 21 C PRO A 2 -37.744 -15.477 72.000 1.00 30.69 C ATOM 22 O PRO A 2 -38.701 -14.936 72.569 1.00 29.34 O ATOM 23 CB PRO A 2 -38.401 -17.089 70.182 1.00 33.62 C ATOM 24 CG PRO A 2 -37.197 -17.986 70.051 1.00 40.88 C ATOM 25 CD PRO A 2 -36.097 -17.124 69.464 1.00 40.35 C ATOM 26 N ALA A 3 -36.666 -15.895 72.660 1.00 28.33 N ATOM 27 CA ALA A 3 -36.664 -15.865 74.109 1.00 26.06 C ATOM 28 C ALA A 3 -35.236 -15.740 74.632 1.00 22.61 C ATOM 29 O ALA A 3 -34.770 -16.603 75.388 1.00 26.83 O ATOM 30 CB ALA A 3 -37.331 -17.118 74.663 1.00 32.30 C ATOM 31 N PRO A 4 -34.537 -14.669 74.281 1.00 21.56 N ATOM 32 CA PRO A 4 -33.186 -14.462 74.827 1.00 21.54 C ATOM 33 C PRO A 4 -33.211 -14.258 76.331 1.00 21.57 C ATOM 34 O PRO A 4 -34.206 -13.825 76.915 1.00 20.41 O ATOM 35 CB PRO A 4 -32.723 -13.185 74.131 1.00 23.16 C ATOM 36 CG PRO A 4 -34.015 -12.429 73.892 1.00 27.74 C ATOM 37 CD PRO A 4 -35.004 -13.498 73.517 1.00 25.04 C ATOM 38 N LYS A 5 -32.077 -14.557 76.964 1.00 21.86 N ATOM 39 CA LYS A 5 -31.887 -14.143 78.339 1.00 19.92 C ATOM 40 C LYS A 5 -31.770 -12.630 78.404 1.00 19.41 C ATOM 41 O LYS A 5 -31.331 -11.990 77.446 1.00 21.72 O ATOM 42 CB LYS A 5 -30.616 -14.764 78.913 1.00 23.82 C ATOM 43 CG LYS A 5 -30.694 -16.279 78.970 1.00 32.86 C ATOM 44 CD LYS A 5 -31.419 -16.704 80.224 1.00 38.13 C ATOM 45 CE LYS A 5 -31.138 -18.156 80.549 1.00 46.55 C ATOM 46 NZ LYS A 5 -31.345 -18.994 79.344 1.00 54.47 N ATOM 47 N THR A 6 -32.143 -12.053 79.552 1.00 18.80 N ANISOU 47 N THR A 6 1673 2165 3306 -602 -526 -171 N ATOM 48 CA THR A 6 -32.015 -10.609 79.735 1.00 17.14 C ANISOU 48 CA THR A 6 1396 2039 3078 -468 -499 -106 C ATOM 49 C THR A 6 -31.195 -10.302 80.970 1.00 19.16 C ANISOU 49 C THR A 6 1726 2259 3294 -398 -324 -63 C ATOM 50 O THR A 6 -31.296 -11.001 81.972 1.00 19.93 O ANISOU 50 O THR A 6 1844 2298 3432 -457 -213 -46 O ATOM 51 CB THR A 6 -33.379 -9.917 79.862 1.00 19.85 C ANISOU 51 CB THR A 6 1490 2452 3600 -471 -532 -59 C ATOM 52 OG1 THR A 6 -34.120 -10.500 80.947 1.00 29.10 O ANISOU 52 OG1 THR A 6 2556 3585 4914 -553 -380 -45 O ATOM 53 CG2 THR A 6 -34.215 -10.135 78.585 1.00 22.20 C ANISOU 53 CG2 THR A 6 1728 2811 3898 -534 -752 -80 C ATOM 54 N ILE A 7 -30.418 -9.227 80.917 1.00 16.04 N ANISOU 54 N ILE A 7 1383 1897 2816 -288 -311 -38 N ATOM 55 CA ILE A 7 -29.564 -8.850 82.044 1.00 16.97 C ANISOU 55 CA ILE A 7 1584 1987 2877 -243 -193 -7 C ATOM 56 C ILE A 7 -29.802 -7.388 82.376 1.00 20.80 C ANISOU 56 C ILE A 7 2016 2505 3381 -167 -144 16 C ATOM 57 O ILE A 7 -29.654 -6.523 81.505 1.00 18.60 O ANISOU 57 O ILE A 7 1725 2255 3089 -102 -216 27 O ATOM 58 CB ILE A 7 -28.076 -9.076 81.732 1.00 15.60 C ANISOU 58 CB ILE A 7 1541 1786 2600 -202 -219 -9 C ATOM 59 CG1 ILE A 7 -27.816 -10.540 81.383 1.00 18.21 C ANISOU 59 CG1 ILE A 7 1938 2044 2935 -251 -238 -41 C ATOM 60 CG2 ILE A 7 -27.187 -8.670 82.943 1.00 17.42 C ANISOU 60 CG2 ILE A 7 1836 1999 2781 -177 -155 34 C ATOM 61 CD1 ILE A 7 -26.348 -10.836 81.034 1.00 20.98 C ANISOU 61 CD1 ILE A 7 2380 2353 3237 -184 -230 -41 C ATOM 62 N TYR A 8 -30.115 -7.102 83.641 1.00 17.24 N ANISOU 62 N TYR A 8 1570 2032 2947 -177 -4 23 N ATOM 63 CA TYR A 8 -30.252 -5.712 84.061 1.00 18.72 C ANISOU 63 CA TYR A 8 1752 2212 3149 -104 77 20 C ATOM 64 C TYR A 8 -28.861 -5.169 84.375 1.00 22.20 C ANISOU 64 C TYR A 8 2351 2631 3452 -90 57 17 C ATOM 65 O TYR A 8 -28.099 -5.792 85.113 1.00 18.59 O ANISOU 65 O TYR A 8 2003 2161 2899 -145 57 24 O ATOM 66 CB TYR A 8 -31.175 -5.599 85.281 1.00 18.34 C ANISOU 66 CB TYR A 8 1673 2137 3157 -126 274 6 C ATOM 67 CG TYR A 8 -31.390 -4.177 85.749 1.00 20.42 C ANISOU 67 CG TYR A 8 1953 2358 3447 -42 398 -23 C ATOM 68 CD1 TYR A 8 -32.049 -3.241 84.946 1.00 22.73 C ANISOU 68 CD1 TYR A 8 2094 2643 3900 67 369 -4 C ATOM 69 CD2 TYR A 8 -30.921 -3.745 86.998 1.00 19.63 C ANISOU 69 CD2 TYR A 8 2046 2207 3205 -72 536 -68 C ATOM 70 CE1 TYR A 8 -32.245 -1.931 85.384 1.00 25.31 C ANISOU 70 CE1 TYR A 8 2450 2889 4278 160 505 -33 C ATOM 71 CE2 TYR A 8 -31.114 -2.434 87.436 1.00 21.40 C ANISOU 71 CE2 TYR A 8 2323 2358 3449 -3 670 -123 C ATOM 72 CZ TYR A 8 -31.780 -1.529 86.626 1.00 25.89 C ANISOU 72 CZ TYR A 8 2730 2896 4213 121 670 -107 C ATOM 73 OH TYR A 8 -31.994 -0.226 87.047 1.00 23.87 O ANISOU 73 OH TYR A 8 2533 2528 4008 207 824 -162 O ATOM 74 N ILE A 9 -28.519 -4.037 83.777 1.00 17.76 N ANISOU 74 N ILE A 9 1791 2059 2898 -25 21 21 N ATOM 75 CA ILE A 9 -27.161 -3.487 83.820 1.00 16.24 C ANISOU 75 CA ILE A 9 1708 1847 2617 -32 -19 23 C ATOM 76 C ILE A 9 -27.149 -2.441 84.929 1.00 20.79 C ANISOU 76 C ILE A 9 2377 2360 3162 -42 82 -20 C ATOM 77 O ILE A 9 -27.302 -1.250 84.684 1.00 20.11 O ANISOU 77 O ILE A 9 2297 2217 3128 10 118 -30 O ATOM 78 CB ILE A 9 -26.766 -2.885 82.467 1.00 19.63 C ANISOU 78 CB ILE A 9 2112 2284 3064 19 -95 58 C ATOM 79 CG1 ILE A 9 -27.091 -3.859 81.333 1.00 17.56 C ANISOU 79 CG1 ILE A 9 1795 2076 2803 23 -179 74 C ATOM 80 CG2 ILE A 9 -25.299 -2.515 82.438 1.00 22.66 C ANISOU 80 CG2 ILE A 9 2566 2651 3392 -12 -118 69 C ATOM 81 CD1 ILE A 9 -26.417 -5.216 81.444 1.00 18.16 C ANISOU 81 CD1 ILE A 9 1905 2162 2832 -29 -196 55 C ATOM 82 N ALA A 10 -26.921 -2.881 86.161 1.00 18.86 N ANISOU 82 N ALA A 10 2240 2111 2816 -116 124 -45 N ATOM 83 CA ALA A 10 -27.025 -2.002 87.318 1.00 20.53 C ANISOU 83 CA ALA A 10 2595 2257 2949 -148 238 -113 C ATOM 84 C ALA A 10 -25.685 -1.358 87.655 1.00 19.20 C ANISOU 84 C ALA A 10 2552 2061 2682 -219 133 -132 C ATOM 85 O ALA A 10 -24.631 -1.985 87.547 1.00 20.23 O ANISOU 85 O ALA A 10 2670 2242 2775 -266 -13 -80 O ATOM 86 CB ALA A 10 -27.534 -2.785 88.533 1.00 21.01 C ANISOU 86 CB ALA A 10 2753 2327 2903 -214 344 -126 C ATOM 87 N GLY A 11 -25.738 -0.111 88.095 1.00 17.65 N ANISOU 87 N GLY A 11 2467 1772 2467 -230 214 -210 N ATOM 88 CA GLY A 11 -24.535 0.558 88.553 1.00 20.02 C ANISOU 88 CA GLY A 11 2898 2033 2676 -337 108 -247 C ATOM 89 C GLY A 11 -24.550 2.046 88.270 1.00 28.19 C ANISOU 89 C GLY A 11 3986 2937 3790 -319 178 -309 C ATOM 90 O GLY A 11 -25.451 2.583 87.596 1.00 25.57 O ANISOU 90 O GLY A 11 3573 2543 3598 -194 296 -299 O ATOM 91 N PRO A 12 -23.524 2.738 88.753 1.00 22.22 N ANISOU 91 N PRO A 12 3358 2123 2962 -449 86 -361 N ATOM 92 CA PRO A 12 -23.549 4.202 88.730 1.00 19.99 C ANISOU 92 CA PRO A 12 3187 1668 2738 -462 175 -445 C ATOM 93 C PRO A 12 -23.162 4.816 87.398 1.00 23.34 C ANISOU 93 C PRO A 12 3476 2048 3343 -410 142 -355 C ATOM 94 O PRO A 12 -22.909 6.022 87.337 1.00 26.64 O ANISOU 94 O PRO A 12 3994 2307 3822 -452 184 -402 O ATOM 95 CB PRO A 12 -22.549 4.592 89.837 1.00 27.20 C ANISOU 95 CB PRO A 12 4309 2542 3486 -668 55 -544 C ATOM 96 CG PRO A 12 -21.626 3.417 89.936 1.00 28.95 C ANISOU 96 CG PRO A 12 4421 2936 3644 -741 -167 -444 C ATOM 97 CD PRO A 12 -22.462 2.208 89.642 1.00 23.75 C ANISOU 97 CD PRO A 12 3639 2386 2998 -604 -97 -363 C ATOM 98 N ALA A 13 -23.165 4.027 86.316 1.00 24.75 N ANISOU 98 N ALA A 13 3460 2347 3597 -324 86 -230 N ATOM 99 CA ALA A 13 -22.844 4.620 85.019 1.00 26.23 C ANISOU 99 CA ALA A 13 3564 2493 3911 -280 79 -136 C ATOM 100 C ALA A 13 -23.806 5.740 84.654 1.00 26.55 C ANISOU 100 C ALA A 13 3658 2373 4058 -161 209 -134 C ATOM 101 O ALA A 13 -23.425 6.663 83.925 1.00 26.98 O ANISOU 101 O ALA A 13 3736 2317 4196 -164 219 -74 O ATOM 102 CB ALA A 13 -22.834 3.558 83.922 1.00 22.38 C ANISOU 102 CB ALA A 13 2911 2152 3440 -204 21 -24 C ATOM 103 N VAL A 14 -25.046 5.694 85.156 1.00 24.86 N ANISOU 103 N VAL A 14 3454 2130 3863 -53 323 -186 N ATOM 104 CA VAL A 14 -25.987 6.779 84.907 1.00 26.91 C ANISOU 104 CA VAL A 14 3738 2216 4271 88 456 -179 C ATOM 105 C VAL A 14 -25.456 8.128 85.377 1.00 26.76 C ANISOU 105 C VAL A 14 3920 1970 4277 11 531 -266 C ATOM 106 O VAL A 14 -25.895 9.171 84.875 1.00 30.69 O ANISOU 106 O VAL A 14 4448 2285 4927 121 614 -219 O ATOM 107 CB VAL A 14 -27.357 6.480 85.554 1.00 31.26 C ANISOU 107 CB VAL A 14 4237 2768 4872 209 605 -236 C ATOM 108 CG1 VAL A 14 -27.844 5.118 85.121 1.00 35.91 C ANISOU 108 CG1 VAL A 14 4632 3565 5447 244 518 -159 C ATOM 109 CG2 VAL A 14 -27.264 6.543 87.073 1.00 32.54 C ANISOU 109 CG2 VAL A 14 4596 2873 4893 102 732 -412 C ATOM 110 N PHE A 15 -24.516 8.148 86.325 1.00 27.46 N ANISOU 110 N PHE A 15 4157 2051 4226 -184 486 -386 N ATOM 111 CA PHE A 15 -23.969 9.404 86.833 1.00 25.48 C ANISOU 111 CA PHE A 15 4120 1574 3987 -303 537 -496 C ATOM 112 C PHE A 15 -22.723 9.867 86.073 1.00 25.28 C ANISOU 112 C PHE A 15 4066 1518 4022 -439 410 -409 C ATOM 113 O PHE A 15 -22.149 10.904 86.426 1.00 29.94 O ANISOU 113 O PHE A 15 4793 1962 4622 -559 404 -479 O ATOM 114 CB PHE A 15 -23.661 9.273 88.335 1.00 32.67 C ANISOU 114 CB PHE A 15 5241 2480 4693 -471 536 -687 C ATOM 115 CG PHE A 15 -24.810 8.728 89.139 1.00 30.93 C ANISOU 115 CG PHE A 15 5064 2302 4387 -364 699 -767 C ATOM 116 CD1 PHE A 15 -25.993 9.442 89.251 1.00 40.06 C ANISOU 116 CD1 PHE A 15 6232 3335 5653 -183 924 -800 C ATOM 117 CD2 PHE A 15 -24.718 7.494 89.761 1.00 27.86 C ANISOU 117 CD2 PHE A 15 4652 2119 3815 -429 616 -766 C ATOM 118 CE1 PHE A 15 -27.061 8.938 89.978 1.00 36.25 C ANISOU 118 CE1 PHE A 15 5753 2899 5123 -91 1110 -861 C ATOM 119 CE2 PHE A 15 -25.782 6.981 90.486 1.00 32.90 C ANISOU 119 CE2 PHE A 15 5331 2790 4379 -347 798 -825 C ATOM 120 CZ PHE A 15 -26.954 7.705 90.594 1.00 31.56 C ANISOU 120 CZ PHE A 15 5193 2454 4345 -186 1077 -894 C ATOM 121 N HIS A 16 -22.291 9.102 85.057 1.00 28.40 N ANISOU 121 N HIS A 16 4260 2092 4437 -415 302 -252 N ATOM 122 CA HIS A 16 -21.194 9.500 84.197 1.00 28.17 C ANISOU 122 CA HIS A 16 4178 2040 4485 -523 241 -147 C ATOM 123 C HIS A 16 -21.544 10.802 83.487 1.00 29.68 C ANISOU 123 C HIS A 16 4469 1990 4819 -450 358 -76 C ATOM 124 O HIS A 16 -22.721 11.130 83.321 1.00 29.65 O ANISOU 124 O HIS A 16 4492 1911 4864 -254 446 -52 O ATOM 125 CB HIS A 16 -20.908 8.413 83.162 1.00 26.43 C ANISOU 125 CB HIS A 16 3756 2039 4247 -464 171 -2 C ATOM 126 CG HIS A 16 -20.264 7.187 83.725 1.00 28.11 C ANISOU 126 CG HIS A 16 3861 2453 4368 -547 50 -39 C ATOM 127 ND1 HIS A 16 -20.077 6.041 82.980 1.00 26.95 N ANISOU 127 ND1 HIS A 16 3553 2487 4201 -483 9 53 N ATOM 128 CD2 HIS A 16 -19.768 6.924 84.957 1.00 29.42 C ANISOU 128 CD2 HIS A 16 4075 2651 4453 -684 -46 -151 C ATOM 129 CE1 HIS A 16 -19.497 5.121 83.731 1.00 28.73 C ANISOU 129 CE1 HIS A 16 3712 2834 4371 -558 -98 11 C ATOM 130 NE2 HIS A 16 -19.297 5.631 84.934 1.00 29.56 N ANISOU 130 NE2 HIS A 16 3939 2863 4429 -683 -151 -100 N ATOM 131 N PRO A 17 -20.537 11.575 83.062 1.00 27.44 N ANISOU 131 N PRO A 17 4210 1635 4583 -590 331 -21 N ATOM 132 CA PRO A 17 -20.841 12.867 82.430 1.00 29.27 C ANISOU 132 CA PRO A 17 4543 1684 4895 -514 404 62 C ATOM 133 C PRO A 17 -21.557 12.736 81.094 1.00 25.58 C ANISOU 133 C PRO A 17 4013 1247 4460 -315 439 261 C ATOM 134 O PRO A 17 -22.088 13.738 80.592 1.00 29.82 O ANISOU 134 O PRO A 17 4635 1637 5057 -207 482 343 O ATOM 135 CB PRO A 17 -19.460 13.523 82.269 1.00 31.98 C ANISOU 135 CB PRO A 17 4899 1975 5275 -743 357 86 C ATOM 136 CG PRO A 17 -18.474 12.392 82.317 1.00 33.23 C ANISOU 136 CG PRO A 17 4889 2341 5395 -885 268 90 C ATOM 137 CD PRO A 17 -19.085 11.358 83.234 1.00 29.83 C ANISOU 137 CD PRO A 17 4434 2019 4879 -827 223 -33 C ATOM 138 N ASP A 18 -21.566 11.546 80.503 1.00 25.71 N ANISOU 138 N ASP A 18 3890 1447 4432 -270 399 345 N ATOM 139 CA ASP A 18 -22.336 11.250 79.303 1.00 29.14 C ANISOU 139 CA ASP A 18 4276 1944 4852 -86 383 524 C ATOM 140 C ASP A 18 -23.555 10.401 79.609 1.00 27.83 C ANISOU 140 C ASP A 18 4008 1902 4664 84 337 481 C ATOM 141 O ASP A 18 -24.072 9.727 78.708 1.00 25.21 O ANISOU 141 O ASP A 18 3591 1719 4268 191 258 595 O ATOM 142 CB ASP A 18 -21.472 10.534 78.265 1.00 26.80 C ANISOU 142 CB ASP A 18 3905 1815 4462 -161 357 644 C ATOM 143 CG ASP A 18 -21.113 9.107 78.664 1.00 22.15 C ANISOU 143 CG ASP A 18 3165 1477 3775 -208 287 543 C ATOM 144 OD1 ASP A 18 -20.626 8.346 77.794 1.00 23.07 O ANISOU 144 OD1 ASP A 18 3215 1746 3806 -221 282 619 O ATOM 145 OD2 ASP A 18 -21.272 8.706 79.855 1.00 23.78 O ANISOU 145 OD2 ASP A 18 3335 1720 3979 -236 249 390 O ATOM 146 N ASN A 19 -23.989 10.375 80.874 1.00 21.92 N ANISOU 146 N ASN A 19 3274 1111 3942 87 383 309 N ATOM 147 CA ASN A 19 -25.138 9.582 81.309 1.00 22.98 C ANISOU 147 CA ASN A 19 3298 1364 4068 223 376 255 C ATOM 148 C ASN A 19 -24.947 8.081 81.079 1.00 24.19 C ANISOU 148 C ASN A 19 3311 1793 4087 184 265 262 C ATOM 149 O ASN A 19 -25.924 7.320 81.053 1.00 25.94 O ANISOU 149 O ASN A 19 3416 2128 4310 291 235 267 O ATOM 150 CB ASN A 19 -26.414 10.092 80.630 1.00 29.14 C ANISOU 150 CB ASN A 19 4024 2060 4986 450 386 383 C ATOM 151 CG ASN A 19 -26.637 11.545 80.896 1.00 34.84 C ANISOU 151 CG ASN A 19 4874 2577 5787 490 476 355 C ATOM 152 OD1 ASN A 19 -26.835 11.948 82.043 1.00 38.69 O ANISOU 152 OD1 ASN A 19 5436 2967 6298 470 595 188 O ATOM 153 ND2 ASN A 19 -26.536 12.367 79.850 1.00 31.65 N ANISOU 153 ND2 ASN A 19 4526 2092 5406 533 426 514 N ATOM 154 N GLY A 20 -23.694 7.635 80.949 1.00 23.37 N ANISOU 154 N GLY A 20 3204 1782 3893 28 214 258 N ATOM 155 CA GLY A 20 -23.360 6.237 80.813 1.00 21.70 C ANISOU 155 CA GLY A 20 2880 1789 3577 -8 134 251 C ATOM 156 C GLY A 20 -23.261 5.733 79.384 1.00 17.75 C ANISOU 156 C GLY A 20 2330 1395 3021 39 87 383 C ATOM 157 O GLY A 20 -23.006 4.541 79.198 1.00 19.53 O ANISOU 157 O GLY A 20 2477 1775 3167 19 40 366 O ATOM 158 N GLU A 21 -23.455 6.601 78.385 1.00 19.60 N ANISOU 158 N GLU A 21 2635 1533 3279 99 103 514 N ATOM 159 CA GLU A 21 -23.558 6.140 76.995 1.00 21.43 C ANISOU 159 CA GLU A 21 2874 1867 3401 147 49 640 C ATOM 160 C GLU A 21 -22.339 5.322 76.567 1.00 22.47 C ANISOU 160 C GLU A 21 2985 2117 3436 36 89 627 C ATOM 161 O GLU A 21 -22.482 4.263 75.944 1.00 20.72 O ANISOU 161 O GLU A 21 2738 2033 3100 62 47 625 O ATOM 162 CB GLU A 21 -23.755 7.324 76.050 1.00 27.25 C ANISOU 162 CB GLU A 21 3736 2462 4154 205 63 809 C ATOM 163 CG GLU A 21 -24.039 6.870 74.630 1.00 28.04 C ANISOU 163 CG GLU A 21 3893 2673 4087 256 -22 944 C ATOM 164 CD GLU A 21 -24.041 8.008 73.629 1.00 45.45 C ANISOU 164 CD GLU A 21 6264 4741 6265 293 -10 1145 C ATOM 165 OE1 GLU A 21 -23.425 7.851 72.554 1.00 56.97 O ANISOU 165 OE1 GLU A 21 7844 6256 7547 232 27 1243 O ATOM 166 OE2 GLU A 21 -24.634 9.064 73.926 1.00 44.73 O ANISOU 166 OE2 GLU A 21 6199 4469 6326 384 -17 1210 O ATOM 167 N ALA A 22 -21.123 5.792 76.873 1.00 19.36 N ANISOU 167 N ALA A 22 2592 1660 3106 -92 178 613 N ATOM 168 CA ALA A 22 -19.948 5.010 76.474 1.00 20.47 C ANISOU 168 CA ALA A 22 2661 1906 3211 -177 241 609 C ATOM 169 C ALA A 22 -19.930 3.628 77.136 1.00 20.54 C ANISOU 169 C ALA A 22 2548 2052 3203 -164 176 497 C ATOM 170 O ALA A 22 -19.600 2.623 76.491 1.00 19.87 O ANISOU 170 O ALA A 22 2430 2069 3049 -145 209 497 O ATOM 171 CB ALA A 22 -18.658 5.782 76.797 1.00 19.00 C ANISOU 171 CB ALA A 22 2437 1627 3154 -332 329 618 C ATOM 172 N TYR A 23 -20.268 3.555 78.426 1.00 16.66 N ANISOU 172 N TYR A 23 2017 1548 2767 -176 100 401 N ATOM 173 CA TYR A 23 -20.305 2.270 79.123 1.00 17.87 C ANISOU 173 CA TYR A 23 2083 1810 2898 -166 35 321 C ATOM 174 C TYR A 23 -21.381 1.356 78.542 1.00 18.74 C ANISOU 174 C TYR A 23 2203 1999 2918 -61 -1 320 C ATOM 175 O TYR A 23 -21.126 0.179 78.247 1.00 18.88 O ANISOU 175 O TYR A 23 2178 2100 2896 -49 -4 298 O ATOM 176 CB TYR A 23 -20.552 2.513 80.614 1.00 20.21 C ANISOU 176 CB TYR A 23 2392 2062 3223 -212 -24 232 C ATOM 177 CG TYR A 23 -20.736 1.266 81.456 1.00 18.19 C ANISOU 177 CG TYR A 23 2087 1898 2926 -204 -92 174 C ATOM 178 CD1 TYR A 23 -19.640 0.531 81.893 1.00 23.03 C ANISOU 178 CD1 TYR A 23 2614 2569 3569 -267 -148 174 C ATOM 179 CD2 TYR A 23 -21.996 0.865 81.870 1.00 18.25 C ANISOU 179 CD2 TYR A 23 2124 1921 2888 -135 -96 134 C ATOM 180 CE1 TYR A 23 -19.811 -0.613 82.686 1.00 23.88 C ANISOU 180 CE1 TYR A 23 2702 2737 3636 -253 -218 148 C ATOM 181 CE2 TYR A 23 -22.176 -0.281 82.681 1.00 18.99 C ANISOU 181 CE2 TYR A 23 2197 2081 2939 -144 -139 96 C ATOM 182 CZ TYR A 23 -21.080 -1.006 83.076 1.00 23.78 C ANISOU 182 CZ TYR A 23 2755 2731 3551 -200 -204 109 C ATOM 183 OH TYR A 23 -21.257 -2.125 83.876 1.00 24.55 O ANISOU 183 OH TYR A 23 2855 2870 3603 -203 -253 100 O ATOM 184 N TYR A 24 -22.585 1.886 78.369 1.00 18.07 N ANISOU 184 N TYR A 24 2166 1875 2823 14 -33 343 N ATOM 185 CA TYR A 24 -23.687 1.064 77.870 1.00 20.74 C ANISOU 185 CA TYR A 24 2485 2292 3104 88 -106 343 C ATOM 186 C TYR A 24 -23.460 0.656 76.416 1.00 21.85 C ANISOU 186 C TYR A 24 2693 2491 3119 97 -113 401 C ATOM 187 O TYR A 24 -23.838 -0.452 76.010 1.00 22.15 O ANISOU 187 O TYR A 24 2725 2607 3083 104 -166 359 O ATOM 188 CB TYR A 24 -25.014 1.814 78.001 1.00 19.94 C ANISOU 188 CB TYR A 24 2372 2135 3071 175 -148 374 C ATOM 189 CG TYR A 24 -25.440 2.108 79.441 1.00 16.97 C ANISOU 189 CG TYR A 24 1959 1697 2794 176 -95 291 C ATOM 190 CD1 TYR A 24 -25.358 1.119 80.417 1.00 20.54 C ANISOU 190 CD1 TYR A 24 2371 2210 3225 121 -86 201 C ATOM 191 CD2 TYR A 24 -25.904 3.366 79.801 1.00 22.36 C ANISOU 191 CD2 TYR A 24 2678 2244 3576 232 -37 305 C ATOM 192 CE1 TYR A 24 -25.732 1.390 81.744 1.00 21.27 C ANISOU 192 CE1 TYR A 24 2481 2247 3354 107 -15 124 C ATOM 193 CE2 TYR A 24 -26.288 3.654 81.114 1.00 19.43 C ANISOU 193 CE2 TYR A 24 2317 1802 3265 229 52 205 C ATOM 194 CZ TYR A 24 -26.193 2.651 82.071 1.00 19.58 C ANISOU 194 CZ TYR A 24 2316 1904 3221 158 64 114 C ATOM 195 OH TYR A 24 -26.573 2.939 83.364 1.00 24.07 O ANISOU 195 OH TYR A 24 2942 2403 3799 142 172 16 O ATOM 196 N ASN A 25 -22.868 1.533 75.603 1.00 20.70 N ANISOU 196 N ASN A 25 2639 2295 2933 84 -50 492 N ATOM 197 CA ASN A 25 -22.575 1.132 74.230 1.00 20.10 C ANISOU 197 CA ASN A 25 2675 2272 2689 78 -21 541 C ATOM 198 C ASN A 25 -21.611 -0.044 74.206 1.00 19.97 C ANISOU 198 C ASN A 25 2620 2316 2652 35 79 453 C ATOM 199 O ASN A 25 -21.715 -0.931 73.351 1.00 21.08 O ANISOU 199 O ASN A 25 2846 2514 2651 43 85 419 O ATOM 200 CB ASN A 25 -22.002 2.302 73.429 1.00 21.36 C ANISOU 200 CB ASN A 25 2958 2355 2805 56 73 671 C ATOM 201 CG ASN A 25 -23.084 3.253 72.931 1.00 24.86 C ANISOU 201 CG ASN A 25 3492 2739 3214 132 -48 798 C ATOM 202 OD1 ASN A 25 -24.280 2.938 73.001 1.00 27.05 O ANISOU 202 OD1 ASN A 25 3722 3061 3496 204 -211 788 O ATOM 203 ND2 ASN A 25 -22.673 4.415 72.415 1.00 26.02 N ANISOU 203 ND2 ASN A 25 3757 2777 3352 117 29 933 N ATOM 204 N ASN A 26 -20.651 -0.067 75.135 1.00 18.25 N ANISOU 204 N ASN A 26 2279 2073 2581 -9 150 415 N ATOM 205 CA ASN A 26 -19.736 -1.201 75.195 1.00 19.83 C ANISOU 205 CA ASN A 26 2404 2314 2817 -19 234 352 C ATOM 206 C ASN A 26 -20.452 -2.469 75.664 1.00 18.32 C ANISOU 206 C ASN A 26 2184 2163 2612 18 135 262 C ATOM 207 O ASN A 26 -20.188 -3.560 75.148 1.00 20.62 O ANISOU 207 O ASN A 26 2504 2472 2858 39 195 208 O ATOM 208 CB ASN A 26 -18.556 -0.857 76.109 1.00 19.70 C ANISOU 208 CB ASN A 26 2234 2266 2985 -79 279 360 C ATOM 209 CG ASN A 26 -17.504 -1.956 76.128 1.00 19.29 C ANISOU 209 CG ASN A 26 2060 2243 3026 -64 368 328 C ATOM 210 OD1 ASN A 26 -16.816 -2.199 75.126 1.00 26.42 O ANISOU 210 OD1 ASN A 26 2981 3148 3908 -50 544 342 O ATOM 211 ND2 ASN A 26 -17.406 -2.659 77.264 1.00 25.11 N ANISOU 211 ND2 ASN A 26 2686 2992 3863 -56 259 289 N ATOM 212 N VAL A 27 -21.360 -2.345 76.634 1.00 19.18 N ANISOU 212 N VAL A 27 2252 2269 2768 23 13 243 N ATOM 213 CA VAL A 27 -22.185 -3.477 77.062 1.00 16.75 C ANISOU 213 CA VAL A 27 1924 1989 2453 38 -67 176 C ATOM 214 C VAL A 27 -22.930 -4.053 75.867 1.00 20.85 C ANISOU 214 C VAL A 27 2543 2540 2839 50 -107 152 C ATOM 215 O VAL A 27 -22.923 -5.269 75.634 1.00 20.14 O ANISOU 215 O VAL A 27 2482 2453 2719 43 -98 81 O ATOM 216 CB VAL A 27 -23.152 -3.035 78.174 1.00 16.82 C ANISOU 216 CB VAL A 27 1883 1984 2523 36 -144 171 C ATOM 217 CG1 VAL A 27 -24.244 -4.102 78.402 1.00 18.71 C ANISOU 217 CG1 VAL A 27 2099 2251 2760 36 -209 120 C ATOM 218 CG2 VAL A 27 -22.355 -2.733 79.466 1.00 17.40 C ANISOU 218 CG2 VAL A 27 1907 2027 2677 -5 -125 164 C ATOM 219 N ARG A 28 -23.538 -3.185 75.071 1.00 18.13 N ANISOU 219 N ARG A 28 2272 2209 2409 64 -162 215 N ATOM 220 CA ARG A 28 -24.263 -3.660 73.897 1.00 18.03 C ANISOU 220 CA ARG A 28 2378 2239 2235 55 -253 202 C ATOM 221 C ARG A 28 -23.329 -4.368 72.925 1.00 22.83 C ANISOU 221 C ARG A 28 3129 2845 2699 33 -123 149 C ATOM 222 O ARG A 28 -23.678 -5.416 72.365 1.00 23.82 O ANISOU 222 O ARG A 28 3350 2983 2718 3 -161 59 O ATOM 223 CB ARG A 28 -24.946 -2.487 73.211 1.00 17.65 C ANISOU 223 CB ARG A 28 2389 2198 2118 84 -357 319 C ATOM 224 CG ARG A 28 -26.041 -1.842 74.042 1.00 21.25 C ANISOU 224 CG ARG A 28 2696 2638 2739 132 -467 363 C ATOM 225 CD ARG A 28 -26.585 -0.654 73.249 1.00 21.98 C ANISOU 225 CD ARG A 28 2854 2712 2787 189 -566 506 C ATOM 226 NE ARG A 28 -27.658 0.048 73.926 1.00 29.00 N ANISOU 226 NE ARG A 28 3589 3563 3865 266 -646 558 N ATOM 227 CZ ARG A 28 -28.917 -0.379 73.950 1.00 37.65 C ANISOU 227 CZ ARG A 28 4553 4712 5041 286 -805 554 C ATOM 228 NH1 ARG A 28 -29.244 -1.525 73.357 1.00 28.40 N ANISOU 228 NH1 ARG A 28 3405 3628 3756 209 -925 491 N ATOM 229 NH2 ARG A 28 -29.841 0.340 74.571 1.00 32.04 N ANISOU 229 NH2 ARG A 28 3680 3953 4542 377 -829 607 N ATOM 230 N ALA A 29 -22.133 -3.811 72.705 1.00 19.47 N ANISOU 230 N ALA A 29 2723 2392 2280 40 53 196 N ATOM 231 CA ALA A 29 -21.203 -4.450 71.780 1.00 20.61 C ANISOU 231 CA ALA A 29 2993 2527 2312 33 241 143 C ATOM 232 C ALA A 29 -20.776 -5.829 72.284 1.00 21.21 C ANISOU 232 C ALA A 29 2994 2566 2498 54 311 25 C ATOM 233 O ALA A 29 -20.603 -6.770 71.492 1.00 23.88 O ANISOU 233 O ALA A 29 3476 2877 2718 54 407 -73 O ATOM 234 CB ALA A 29 -19.992 -3.538 71.544 1.00 23.76 C ANISOU 234 CB ALA A 29 3373 2900 2757 28 444 232 C ATOM 235 N LEU A 30 -20.604 -5.975 73.599 1.00 20.88 N ANISOU 235 N LEU A 30 2757 2506 2671 72 265 34 N ATOM 236 CA LEU A 30 -20.207 -7.272 74.129 1.00 22.94 C ANISOU 236 CA LEU A 30 2953 2714 3050 105 311 -42 C ATOM 237 C LEU A 30 -21.289 -8.325 73.911 1.00 21.89 C ANISOU 237 C LEU A 30 2930 2561 2827 75 203 -140 C ATOM 238 O LEU A 30 -20.983 -9.518 73.771 1.00 24.88 O ANISOU 238 O LEU A 30 3358 2862 3235 97 286 -229 O ATOM 239 CB LEU A 30 -19.887 -7.147 75.615 1.00 19.95 C ANISOU 239 CB LEU A 30 2379 2327 2873 115 240 13 C ATOM 240 CG LEU A 30 -18.593 -6.395 75.962 1.00 21.17 C ANISOU 240 CG LEU A 30 2390 2484 3169 122 329 90 C ATOM 241 CD1 LEU A 30 -18.649 -6.014 77.448 1.00 23.70 C ANISOU 241 CD1 LEU A 30 2588 2815 3604 90 180 138 C ATOM 242 CD2 LEU A 30 -17.355 -7.240 75.683 1.00 28.47 C ANISOU 242 CD2 LEU A 30 3232 3359 4227 188 501 75 C ATOM 243 N MET A 31 -22.546 -7.913 73.886 1.00 22.54 N ANISOU 243 N MET A 31 3036 2697 2831 25 23 -124 N ATOM 244 CA MET A 31 -23.632 -8.867 73.760 1.00 20.32 C ANISOU 244 CA MET A 31 2814 2402 2506 -34 -105 -209 C ATOM 245 C MET A 31 -24.019 -9.132 72.315 1.00 25.03 C ANISOU 245 C MET A 31 3631 3013 2865 -89 -143 -284 C ATOM 246 O MET A 31 -24.851 -10.008 72.066 1.00 28.14 O ANISOU 246 O MET A 31 4095 3385 3212 -167 -260 -376 O ATOM 247 CB MET A 31 -24.838 -8.365 74.550 1.00 20.78 C ANISOU 247 CB MET A 31 2736 2511 2649 -64 -277 -151 C ATOM 248 CG MET A 31 -24.580 -8.196 75.996 1.00 22.06 C ANISOU 248 CG MET A 31 2743 2654 2984 -34 -239 -100 C ATOM 249 SD MET A 31 -26.208 -7.945 76.765 1.00 31.78 S ANISOU 249 SD MET A 31 3848 3923 4303 -79 -380 -74 S ATOM 250 CE MET A 31 -25.642 -7.411 78.324 1.00 23.61 C ANISOU 250 CE MET A 31 2721 2868 3381 -44 -295 -18 C ATOM 251 N LYS A 32 -23.407 -8.431 71.364 1.00 25.78 N ANISOU 251 N LYS A 32 3859 3138 2800 -69 -45 -248 N ATOM 252 CA LYS A 32 -23.792 -8.557 69.963 1.00 27.16 C ANISOU 252 CA LYS A 32 4299 3338 2682 -134 -99 -304 C ATOM 253 C LYS A 32 -23.653 -9.992 69.460 1.00 27.61 C ANISOU 253 C LYS A 32 4537 3304 2651 -180 -15 -489 C ATOM 254 O LYS A 32 -22.619 -10.634 69.637 1.00 29.95 O ANISOU 254 O LYS A 32 4830 3504 3046 -115 229 -555 O ATOM 255 CB LYS A 32 -22.930 -7.609 69.125 1.00 34.90 C ANISOU 255 CB LYS A 32 5412 4344 3503 -102 69 -221 C ATOM 256 CG LYS A 32 -23.581 -7.147 67.840 1.00 47.64 C ANISOU 256 CG LYS A 32 7288 6024 4789 -169 -74 -185 C ATOM 257 CD LYS A 32 -25.037 -6.665 67.984 1.00 57.68 C ANISOU 257 CD LYS A 32 8470 7371 6073 -204 -434 -98 C ATOM 258 CE LYS A 32 -25.250 -5.512 69.005 1.00 65.95 C ANISOU 258 CE LYS A 32 9245 8434 7378 -123 -487 61 C ATOM 259 NZ LYS A 32 -24.875 -4.176 68.488 1.00 68.94 N ANISOU 259 NZ LYS A 32 9709 8821 7663 -82 -439 226 N ATOM 260 N GLY A 33 -24.694 -10.491 68.805 1.00 33.65 N ANISOU 260 N GLY A 33 5459 4087 3242 -295 -225 -575 N ATOM 261 CA GLY A 33 -24.649 -11.821 68.238 1.00 38.58 C ANISOU 261 CA GLY A 33 6306 4599 3753 -367 -159 -776 C ATOM 262 C GLY A 33 -24.900 -12.960 69.208 1.00 34.88 C ANISOU 262 C GLY A 33 5699 4014 3539 -383 -167 -857 C ATOM 263 O GLY A 33 -24.800 -14.133 68.803 1.00 37.25 O ANISOU 263 O GLY A 33 6193 4177 3784 -437 -86 -1033 O ATOM 264 N LYS A 34 -25.231 -12.661 70.456 1.00 29.52 N ANISOU 264 N LYS A 34 4726 3368 3123 -345 -248 -738 N ATOM 265 CA LYS A 34 -25.544 -13.660 71.460 1.00 25.58 C ANISOU 265 CA LYS A 34 4103 2763 2853 -371 -261 -776 C ATOM 266 C LYS A 34 -27.014 -13.576 71.841 1.00 28.05 C ANISOU 266 C LYS A 34 4274 3148 3234 -494 -530 -739 C ATOM 267 O LYS A 34 -27.663 -12.535 71.696 1.00 29.72 O ANISOU 267 O LYS A 34 4388 3500 3405 -501 -692 -637 O ATOM 268 CB LYS A 34 -24.668 -13.472 72.707 1.00 24.36 C ANISOU 268 CB LYS A 34 3737 2579 2938 -236 -110 -661 C ATOM 269 CG LYS A 34 -23.208 -13.732 72.429 1.00 30.20 C ANISOU 269 CG LYS A 34 4546 3231 3698 -112 154 -691 C ATOM 270 CD LYS A 34 -22.385 -13.378 73.650 1.00 28.13 C ANISOU 270 CD LYS A 34 4047 2973 3667 2 226 -552 C ATOM 271 CE LYS A 34 -21.069 -14.137 73.668 1.00 44.14 C ANISOU 271 CE LYS A 34 6075 4864 5835 127 458 -580 C ATOM 272 NZ LYS A 34 -20.098 -13.577 72.696 1.00 44.48 N ANISOU 272 NZ LYS A 34 6177 4937 5787 191 662 -597 N ATOM 273 N ASP A 35 -27.521 -14.697 72.342 1.00 26.42 N ANISOU 273 N ASP A 35 4046 2829 3165 -585 -558 -813 N ATOM 274 CA ASP A 35 -28.908 -14.868 72.762 1.00 29.85 C ANISOU 274 CA ASP A 35 4321 3303 3720 -725 -769 -793 C ATOM 275 C ASP A 35 -29.153 -14.232 74.131 1.00 26.31 C ANISOU 275 C ASP A 35 3592 2916 3490 -653 -737 -633 C ATOM 276 O ASP A 35 -29.716 -14.870 75.027 1.00 25.64 O ANISOU 276 O ASP A 35 3391 2767 3584 -723 -728 -618 O ATOM 277 CB ASP A 35 -29.228 -16.367 72.796 1.00 38.41 C ANISOU 277 CB ASP A 35 5514 4205 4875 -865 -762 -935 C ATOM 278 CG ASP A 35 -30.711 -16.656 72.777 1.00 55.66 C ANISOU 278 CG ASP A 35 7575 6427 7145 -1070 -1006 -956 C ATOM 279 OD1 ASP A 35 -31.480 -15.793 72.307 1.00 60.17 O ANISOU 279 OD1 ASP A 35 8029 7176 7658 -1095 -1203 -891 O ATOM 280 OD2 ASP A 35 -31.109 -17.744 73.249 1.00 66.00 O ANISOU 280 OD2 ASP A 35 8863 7607 8607 -1172 -960 -1007 O ATOM 281 N VAL A 36 -28.745 -12.978 74.289 1.00 21.73 N ANISOU 281 N VAL A 36 2928 2447 2883 -527 -704 -519 N ATOM 282 CA VAL A 36 -28.872 -12.246 75.551 1.00 19.06 C ANISOU 282 CA VAL A 36 2378 2156 2707 -455 -652 -390 C ATOM 283 C VAL A 36 -28.982 -10.774 75.206 1.00 20.39 C ANISOU 283 C VAL A 36 2482 2449 2816 -377 -718 -297 C ATOM 284 O VAL A 36 -28.309 -10.297 74.288 1.00 25.45 O ANISOU 284 O VAL A 36 3263 3117 3292 -328 -705 -299 O ATOM 285 CB VAL A 36 -27.703 -12.543 76.524 1.00 25.14 C ANISOU 285 CB VAL A 36 3161 2842 3549 -361 -462 -356 C ATOM 286 CG1 VAL A 36 -26.362 -12.205 75.889 1.00 26.49 C ANISOU 286 CG1 VAL A 36 3446 3006 3611 -256 -353 -365 C ATOM 287 CG2 VAL A 36 -27.875 -11.741 77.817 1.00 22.89 C ANISOU 287 CG2 VAL A 36 2713 2611 3374 -315 -425 -242 C ATOM 288 N VAL A 37 -29.855 -10.056 75.917 1.00 20.27 N ANISOU 288 N VAL A 37 2491 2564 2647 -350 -482 -523 N ATOM 289 CA VAL A 37 -30.090 -8.640 75.645 1.00 21.58 C ANISOU 289 CA VAL A 37 2708 2788 2703 -227 -493 -421 C ATOM 290 C VAL A 37 -29.982 -7.819 76.929 1.00 23.89 C ANISOU 290 C VAL A 37 2943 3020 3115 -221 -454 -324 C ATOM 291 O VAL A 37 -30.299 -8.306 78.025 1.00 21.16 O ANISOU 291 O VAL A 37 2493 2663 2885 -288 -465 -342 O ATOM 292 CB VAL A 37 -31.454 -8.436 74.965 1.00 24.99 C ANISOU 292 CB VAL A 37 3105 3385 3006 -151 -657 -474 C ATOM 293 CG1 VAL A 37 -31.539 -9.227 73.687 1.00 26.83 C ANISOU 293 CG1 VAL A 37 3417 3684 3092 -142 -731 -604 C ATOM 294 CG2 VAL A 37 -32.564 -8.867 75.864 1.00 28.99 C ANISOU 294 CG2 VAL A 37 3413 3952 3649 -226 -741 -527 C ATOM 295 N PRO A 38 -29.524 -6.577 76.847 1.00 17.14 N ANISOU 295 N PRO A 38 2170 2109 2232 -139 -400 -223 N ATOM 296 CA PRO A 38 -29.390 -5.750 78.040 1.00 17.83 C ANISOU 296 CA PRO A 38 2224 2122 2428 -125 -385 -169 C ATOM 297 C PRO A 38 -30.652 -4.967 78.344 1.00 18.31 C ANISOU 297 C PRO A 38 2244 2274 2441 -19 -471 -151 C ATOM 298 O PRO A 38 -31.349 -4.490 77.447 1.00 23.92 O ANISOU 298 O PRO A 38 2994 3067 3029 85 -531 -127 O ATOM 299 CB PRO A 38 -28.251 -4.792 77.660 1.00 21.67 C ANISOU 299 CB PRO A 38 2817 2472 2944 -104 -280 -83 C ATOM 300 CG PRO A 38 -28.468 -4.593 76.157 1.00 21.88 C ANISOU 300 CG PRO A 38 2961 2560 2791 -24 -258 -37 C ATOM 301 CD PRO A 38 -29.026 -5.903 75.630 1.00 21.83 C ANISOU 301 CD PRO A 38 2913 2685 2694 -57 -334 -151 C ATOM 302 N LEU A 39 -30.894 -4.796 79.647 1.00 21.32 N ANISOU 302 N LEU A 39 2555 2640 2906 -20 -474 -161 N ATOM 303 CA LEU A 39 -31.938 -3.900 80.149 1.00 23.18 C ANISOU 303 CA LEU A 39 2752 2938 3118 106 -521 -146 C ATOM 304 C LEU A 39 -31.203 -2.775 80.873 1.00 19.97 C ANISOU 304 C LEU A 39 2443 2375 2771 156 -484 -116 C ATOM 305 O LEU A 39 -30.579 -2.999 81.916 1.00 23.76 O ANISOU 305 O LEU A 39 2916 2789 3323 100 -462 -152 O ATOM 306 CB LEU A 39 -32.921 -4.639 81.067 1.00 23.87 C ANISOU 306 CB LEU A 39 2682 3147 3241 78 -530 -193 C ATOM 307 CG LEU A 39 -33.633 -5.815 80.384 1.00 25.60 C ANISOU 307 CG LEU A 39 2779 3487 3460 -13 -576 -247 C ATOM 308 CD1 LEU A 39 -34.495 -6.583 81.383 1.00 29.23 C ANISOU 308 CD1 LEU A 39 3072 4027 4006 -78 -535 -268 C ATOM 309 CD2 LEU A 39 -34.477 -5.324 79.216 1.00 26.29 C ANISOU 309 CD2 LEU A 39 2844 3691 3454 95 -690 -260 C ATOM 310 N ILE A 40 -31.264 -1.577 80.304 1.00 19.71 N ANISOU 310 N ILE A 40 2511 2269 2707 267 -489 -55 N ATOM 311 CA ILE A 40 -30.437 -0.447 80.730 1.00 17.31 C ANISOU 311 CA ILE A 40 2318 1762 2498 287 -454 -33 C ATOM 312 C ILE A 40 -31.283 0.432 81.645 1.00 21.12 C ANISOU 312 C ILE A 40 2803 2244 2978 434 -499 -70 C ATOM 313 O ILE A 40 -32.433 0.735 81.289 1.00 24.26 O ANISOU 313 O ILE A 40 3171 2754 3294 576 -540 -44 O ATOM 314 CB ILE A 40 -29.956 0.377 79.521 1.00 23.27 C ANISOU 314 CB ILE A 40 3211 2390 3239 319 -396 82 C ATOM 315 CG1 ILE A 40 -29.188 -0.481 78.523 1.00 32.95 C ANISOU 315 CG1 ILE A 40 4446 3642 4431 207 -322 116 C ATOM 316 CG2 ILE A 40 -29.144 1.606 79.967 1.00 26.81 C ANISOU 316 CG2 ILE A 40 3760 2586 3843 312 -352 101 C ATOM 317 CD1 ILE A 40 -27.979 -1.070 79.103 1.00 26.02 C ANISOU 317 CD1 ILE A 40 3506 2682 3700 52 -268 60 C ATOM 318 N PRO A 41 -30.766 0.868 82.786 1.00 19.95 N ANISOU 318 N PRO A 41 2688 1979 2911 427 -506 -143 N ATOM 319 CA PRO A 41 -31.554 1.721 83.678 1.00 26.38 C ANISOU 319 CA PRO A 41 3531 2790 3703 593 -537 -202 C ATOM 320 C PRO A 41 -32.119 2.923 82.955 1.00 29.35 C ANISOU 320 C PRO A 41 4002 3079 4073 754 -546 -132 C ATOM 321 O PRO A 41 -31.503 3.478 82.042 1.00 27.10 O ANISOU 321 O PRO A 41 3824 2633 3838 722 -517 -42 O ATOM 322 CB PRO A 41 -30.549 2.158 84.747 1.00 27.34 C ANISOU 322 CB PRO A 41 3729 2741 3919 547 -566 -306 C ATOM 323 CG PRO A 41 -29.540 1.097 84.764 1.00 23.26 C ANISOU 323 CG PRO A 41 3149 2241 3447 368 -560 -312 C ATOM 324 CD PRO A 41 -29.424 0.607 83.334 1.00 18.43 C ANISOU 324 CD PRO A 41 2507 1663 2832 286 -501 -198 C ATOM 325 N THR A 42 -33.298 3.325 83.412 1.00 29.73 N ANISOU 325 N THR A 42 4010 3229 4059 942 -568 -165 N ATOM 326 CA THR A 42 -34.109 4.343 82.777 1.00 42.96 C ANISOU 326 CA THR A 42 5746 4868 5708 1150 -594 -98 C ATOM 327 C THR A 42 -33.802 5.714 83.327 1.00 44.06 C ANISOU 327 C THR A 42 6062 4741 5939 1263 -594 -143 C ATOM 328 O THR A 42 -34.594 6.649 83.123 1.00 45.52 O ANISOU 328 O THR A 42 6307 4878 6110 1487 -614 -111 O ATOM 329 CB THR A 42 -35.588 3.994 82.954 1.00 46.76 C ANISOU 329 CB THR A 42 6044 5616 6106 1305 -619 -122 C ATOM 330 OG1 THR A 42 -35.997 4.296 84.290 1.00 50.05 O ANISOU 330 OG1 THR A 42 6438 6052 6526 1412 -581 -233 O ATOM 331 CG2 THR A 42 -35.801 2.499 82.694 1.00 55.30 C ANISOU 331 CG2 THR A 42 6937 6927 7148 1138 -617 -122 C ATOM 332 N ASP A 43 -32.642 5.842 83.991 1.00 36.69 N ANISOU 332 N ASP A 43 5206 3623 5113 1115 -588 -227 N ATOM 333 CA ASP A 43 -32.297 7.013 84.784 1.00 59.50 C ANISOU 333 CA ASP A 43 8246 6255 8108 1191 -615 -339 C ATOM 334 C ASP A 43 -32.314 8.277 83.927 1.00 67.35 C ANISOU 334 C ASP A 43 9406 6989 9196 1290 -594 -227 C ATOM 335 O ASP A 43 -32.513 9.383 84.444 1.00 60.13 O ANISOU 335 O ASP A 43 8574 5942 8330 1374 -580 -289 O ATOM 336 CB ASP A 43 -30.923 6.796 85.455 1.00 69.14 C ANISOU 336 CB ASP A 43 9484 7337 9450 977 -648 -452 C ATOM 337 CG ASP A 43 -31.014 6.219 86.906 1.00 81.05 C ANISOU 337 CG ASP A 43 10942 8999 10856 1005 -701 -628 C ATOM 338 OD1 ASP A 43 -30.552 5.066 87.229 1.00 88.49 O ANISOU 338 OD1 ASP A 43 11780 10093 11748 869 -708 -639 O ATOM 339 OD2 ASP A 43 -31.548 6.961 87.752 1.00 86.28 O ANISOU 339 OD2 ASP A 43 11689 9623 11471 1183 -727 -749 O ATOM 340 N ASN A 44 -32.136 8.130 82.614 1.00 73.10 N ANISOU 340 N ASN A 44 10155 7708 9910 1237 -546 -39 N ATOM 341 CA ASN A 44 -32.400 9.210 81.673 1.00 86.71 C ANISOU 341 CA ASN A 44 12027 9265 11655 1361 -500 124 C ATOM 342 C ASN A 44 -33.471 8.831 80.657 1.00105.04 C ANISOU 342 C ASN A 44 14307 11822 13781 1545 -538 262 C ATOM 343 O ASN A 44 -33.595 9.492 79.621 1.00103.18 O ANISOU 343 O ASN A 44 14186 11506 13512 1620 -499 435 O ATOM 344 CB ASN A 44 -31.115 9.641 80.967 1.00 86.92 C ANISOU 344 CB ASN A 44 12165 9019 11842 1160 -390 244 C ATOM 345 CG ASN A 44 -30.142 10.322 81.907 1.00 94.27 C ANISOU 345 CG ASN A 44 13106 9716 12996 991 -354 100 C ATOM 346 OD1 ASN A 44 -29.447 9.668 82.684 1.00 94.51 O ANISOU 346 OD1 ASN A 44 13040 9800 13071 830 -398 -50 O ATOM 347 ND2 ASN A 44 -30.113 11.652 81.865 1.00 97.12 N ANISOU 347 ND2 ASN A 44 13577 9831 13492 1037 -288 136 N ATOM 348 N ILE A 45 -34.245 7.774 80.924 1.00129.71 N ANISOU 348 N ILE A 45 17226 15277 16779 1572 -600 186 N ATOM 349 CA ILE A 45 -35.411 7.464 80.101 1.00136.46 C ANISOU 349 CA ILE A 45 17984 16388 17477 1749 -674 265 C ATOM 350 C ILE A 45 -36.567 8.352 80.542 1.00135.68 C ANISOU 350 C ILE A 45 17846 16328 17377 1981 -701 224 C ATOM 351 O ILE A 45 -37.268 8.932 79.704 1.00139.03 O ANISOU 351 O ILE A 45 18359 16736 17730 0 -791 0 O ATOM 352 CB ILE A 45 -35.836 5.983 80.175 1.00136.97 C ANISOU 352 CB ILE A 45 17796 16791 17457 1623 -711 188 C ATOM 353 CG1 ILE A 45 -34.891 5.078 79.390 1.00130.99 C ANISOU 353 CG1 ILE A 45 17057 16051 16663 1388 -674 244 C ATOM 354 CG2 ILE A 45 -37.268 5.693 79.704 1.00140.44 C ANISOU 354 CG2 ILE A 45 18053 17517 17790 0 -822 0 C ATOM 355 CD1 ILE A 45 -35.400 3.640 79.293 1.00126.62 C ANISOU 355 CD1 ILE A 45 16278 15794 16036 1281 -726 170 C ATOM 356 N ALA A 46 -37.063 8.101 81.753 1.00125.92 N ANISOU 356 N ALA A 46 16469 15211 16166 2014 -694 65 N ATOM 357 CA ALA A 46 -38.252 8.762 82.263 1.00113.71 C ANISOU 357 CA ALA A 46 14839 13756 14609 2216 -690 9 C ATOM 358 C ALA A 46 -37.875 9.951 83.127 1.00100.73 C ANISOU 358 C ALA A 46 13373 11840 13062 2258 -633 -71 C ATOM 359 O ALA A 46 -36.794 10.000 83.718 1.00101.18 O ANISOU 359 O ALA A 46 13544 11706 13194 2105 -603 -145 O ATOM 360 CB ALA A 46 -39.118 7.784 83.061 1.00111.11 C ANISOU 360 CB ALA A 46 14240 13738 14238 2235 -678 -104 C ATOM 361 N THR A 47 -38.771 10.923 83.174 1.00 90.38 N ANISOU 361 N THR A 47 12074 10508 11758 2463 -631 -66 N ATOM 362 CA THR A 47 -38.612 12.069 84.046 1.00 83.99 C ANISOU 362 CA THR A 47 11414 9463 11036 2533 -585 -167 C ATOM 363 C THR A 47 -39.446 11.863 85.302 1.00 76.54 C ANISOU 363 C THR A 47 10336 8715 10031 2653 -544 -332 C ATOM 364 O THR A 47 -40.510 11.237 85.272 1.00 72.83 O ANISOU 364 O THR A 47 9643 8540 9490 2751 -539 -324 O ATOM 365 CB THR A 47 -39.022 13.359 83.339 1.00 89.70 C ANISOU 365 CB THR A 47 12265 10001 11817 2700 -596 -56 C ATOM 366 OG1 THR A 47 -40.354 13.219 82.833 1.00 98.11 O ANISOU 366 OG1 THR A 47 13161 11323 12792 2900 -645 3 O ATOM 367 CG2 THR A 47 -38.071 13.650 82.187 1.00 85.95 C ANISOU 367 CG2 THR A 47 11957 9298 11401 2573 -594 123 C ATOM 368 N GLY A 48 -38.940 12.384 86.413 1.00 69.25 N ANISOU 368 N GLY A 48 9543 7629 9140 2634 -509 -485 N ATOM 369 CA GLY A 48 -39.581 12.174 87.690 1.00 56.57 C ANISOU 369 CA GLY A 48 7853 6200 7441 2745 -448 -641 C ATOM 370 C GLY A 48 -38.978 10.996 88.419 1.00 50.97 C ANISOU 370 C GLY A 48 7089 5629 6650 2584 -431 -721 C ATOM 371 O GLY A 48 -38.820 9.912 87.848 1.00 45.12 O ANISOU 371 O GLY A 48 6218 5034 5892 2461 -446 -635 O ATOM 372 N ALA A 49 -38.633 11.206 89.689 1.00 47.88 N ANISOU 372 N ALA A 49 6804 5189 6197 2594 -408 -890 N ATOM 373 CA ALA A 49 -38.027 10.143 90.479 1.00 43.39 C ANISOU 373 CA ALA A 49 6215 4743 5527 2466 -400 -966 C ATOM 374 C ALA A 49 -38.959 8.949 90.630 1.00 36.32 C ANISOU 374 C ALA A 49 5078 4197 4524 2521 -292 -908 C ATOM 375 O ALA A 49 -38.500 7.808 90.672 1.00 37.64 O ANISOU 375 O ALA A 49 5172 4475 4653 2384 -286 -883 O ATOM 376 CB ALA A 49 -37.621 10.682 91.850 1.00 41.44 C ANISOU 376 CB ALA A 49 6140 4410 5195 2510 -411 -1159 C ATOM 377 N VAL A 50 -40.267 9.183 90.709 1.00 42.96 N ANISOU 377 N VAL A 50 5774 5208 5341 2710 -198 -883 N ATOM 378 CA VAL A 50 -41.203 8.072 90.853 1.00 44.06 C ANISOU 378 CA VAL A 50 5637 5677 5428 2730 -72 -821 C ATOM 379 C VAL A 50 -41.149 7.169 89.628 1.00 45.47 C ANISOU 379 C VAL A 50 5633 5947 5695 2577 -138 -685 C ATOM 380 O VAL A 50 -41.069 5.939 89.739 1.00 41.69 O ANISOU 380 O VAL A 50 5005 5644 5192 2453 -83 -651 O ATOM 381 CB VAL A 50 -42.628 8.599 91.096 1.00 47.19 C ANISOU 381 CB VAL A 50 5880 6219 5829 2949 36 -822 C ATOM 382 CG1 VAL A 50 -43.632 7.471 90.965 1.00 44.75 C ANISOU 382 CG1 VAL A 50 5224 6231 5546 2916 156 -734 C ATOM 383 CG2 VAL A 50 -42.719 9.259 92.458 1.00 52.95 C ANISOU 383 CG2 VAL A 50 6775 6910 6434 3102 131 -965 C ATOM 384 N ASN A 51 -41.206 7.769 88.440 1.00 49.90 N ANISOU 384 N ASN A 51 6215 6393 6351 2590 -255 -602 N ATOM 385 CA ASN A 51 -41.269 6.957 87.232 1.00 49.74 C ANISOU 385 CA ASN A 51 6031 6485 6382 2468 -334 -482 C ATOM 386 C ASN A 51 -39.943 6.256 86.962 1.00 44.16 C ANISOU 386 C ASN A 51 5433 5668 5679 2257 -395 -466 C ATOM 387 O ASN A 51 -39.934 5.110 86.498 1.00 37.40 O ANISOU 387 O ASN A 51 4406 4974 4830 2118 -410 -412 O ATOM 388 CB ASN A 51 -41.700 7.812 86.038 1.00 49.74 C ANISOU 388 CB ASN A 51 6060 6404 6436 2566 -441 -387 C ATOM 389 CG ASN A 51 -43.204 8.019 85.992 1.00 66.64 C ANISOU 389 CG ASN A 51 7968 8751 8601 2743 -413 -380 C ATOM 390 OD1 ASN A 51 -43.976 7.084 86.223 1.00 73.62 O ANISOU 390 OD1 ASN A 51 8571 9899 9504 2702 -351 -389 O ATOM 391 ND2 ASN A 51 -43.628 9.241 85.694 1.00 72.86 N ANISOU 391 ND2 ASN A 51 8861 9409 9415 2931 -453 -361 N ATOM 392 N ILE A 52 -38.817 6.921 87.242 1.00 33.12 N ANISOU 392 N ILE A 52 4302 3987 4296 2207 -434 -520 N ATOM 393 CA ILE A 52 -37.516 6.273 87.080 1.00 32.63 C ANISOU 393 CA ILE A 52 4328 3810 4261 1977 -482 -513 C ATOM 394 C ILE A 52 -37.449 5.026 87.942 1.00 31.50 C ANISOU 394 C ILE A 52 4063 3868 4038 1829 -402 -548 C ATOM 395 O ILE A 52 -37.084 3.945 87.469 1.00 30.06 O ANISOU 395 O ILE A 52 3783 3771 3868 1608 -407 -473 O ATOM 396 CB ILE A 52 -36.367 7.241 87.418 1.00 33.21 C ANISOU 396 CB ILE A 52 4667 3548 4403 1931 -534 -595 C ATOM 397 CG1 ILE A 52 -36.341 8.416 86.435 1.00 43.62 C ANISOU 397 CG1 ILE A 52 6106 4652 5816 1970 -566 -496 C ATOM 398 CG2 ILE A 52 -35.019 6.484 87.472 1.00 32.99 C ANISOU 398 CG2 ILE A 52 4677 3443 4414 1652 -570 -605 C ATOM 399 CD1 ILE A 52 -35.624 9.642 86.964 1.00 45.03 C ANISOU 399 CD1 ILE A 52 6492 4529 6087 1944 -576 -587 C ATOM 400 N ARG A 53 -37.806 5.160 89.225 1.00 32.38 N ANISOU 400 N ARG A 53 4200 4049 4054 1969 -316 -657 N ATOM 401 CA ARG A 53 -37.736 4.018 90.136 1.00 30.03 C ANISOU 401 CA ARG A 53 3832 3926 3653 1858 -216 -662 C ATOM 402 C ARG A 53 -38.679 2.910 89.687 1.00 28.48 C ANISOU 402 C ARG A 53 3346 3990 3484 1772 -122 -543 C ATOM 403 O ARG A 53 -38.299 1.734 89.660 1.00 27.41 O ANISOU 403 O ARG A 53 3144 3920 3351 1553 -95 -479 O ATOM 404 CB ARG A 53 -38.057 4.467 91.564 1.00 30.91 C ANISOU 404 CB ARG A 53 4051 4079 3613 2075 -120 -792 C ATOM 405 CG ARG A 53 -38.032 3.360 92.596 1.00 31.61 C ANISOU 405 CG ARG A 53 4112 4348 3552 2007 9 -771 C ATOM 406 CD ARG A 53 -38.433 3.876 93.973 1.00 32.97 C ANISOU 406 CD ARG A 53 4419 4584 3524 2270 124 -898 C ATOM 407 NE ARG A 53 -38.432 2.816 94.977 1.00 37.42 N ANISOU 407 NE ARG A 53 4988 5323 3907 2230 273 -842 N ATOM 408 CZ ARG A 53 -39.482 2.054 95.252 1.00 41.38 C ANISOU 408 CZ ARG A 53 5283 6067 4374 2251 515 -718 C ATOM 409 NH1 ARG A 53 -40.620 2.225 94.579 1.00 38.02 N ANISOU 409 NH1 ARG A 53 4590 5757 4098 2308 602 -663 N ATOM 410 NH2 ARG A 53 -39.389 1.116 96.188 1.00 37.50 N ANISOU 410 NH2 ARG A 53 4844 5697 3709 2216 667 -642 N ATOM 411 N ASN A 54 -39.898 3.273 89.279 1.00 35.47 N ANISOU 411 N ASN A 54 4048 5011 4419 1940 -86 -520 N ATOM 412 CA ASN A 54 -40.847 2.275 88.796 1.00 36.84 C ANISOU 412 CA ASN A 54 3906 5426 4665 1846 -26 -435 C ATOM 413 C ASN A 54 -40.325 1.576 87.549 1.00 32.13 C ANISOU 413 C ASN A 54 3271 4789 4146 1607 -163 -363 C ATOM 414 O ASN A 54 -40.443 0.354 87.421 1.00 30.15 O ANISOU 414 O ASN A 54 2861 4654 3939 1403 -119 -318 O ATOM 415 CB ASN A 54 -42.199 2.927 88.503 1.00 43.03 C ANISOU 415 CB ASN A 54 4480 6359 5513 2096 -9 -444 C ATOM 416 CG ASN A 54 -42.994 3.221 89.762 1.00 51.44 C ANISOU 416 CG ASN A 54 5500 7533 6513 2267 195 -493 C ATOM 417 OD1 ASN A 54 -42.792 2.594 90.803 1.00 44.81 O ANISOU 417 OD1 ASN A 54 4683 6767 5575 2235 361 -502 O ATOM 418 ND2 ASN A 54 -43.909 4.179 89.667 1.00 53.91 N ANISOU 418 ND2 ASN A 54 5771 7850 6865 2445 191 -512 N ATOM 419 N LYS A 55 -39.748 2.341 86.619 1.00 31.09 N ANISOU 419 N LYS A 55 3299 4483 4031 1637 -313 -351 N ATOM 420 CA LYS A 55 -39.248 1.772 85.372 1.00 33.44 C ANISOU 420 CA LYS A 55 3592 4750 4364 1452 -427 -286 C ATOM 421 C LYS A 55 -38.065 0.844 85.628 1.00 27.63 C ANISOU 421 C LYS A 55 2953 3926 3620 1196 -399 -281 C ATOM 422 O LYS A 55 -37.950 -0.219 85.008 1.00 27.44 O ANISOU 422 O LYS A 55 2830 3969 3626 1009 -422 -247 O ATOM 423 CB LYS A 55 -38.821 2.893 84.423 1.00 40.76 C ANISOU 423 CB LYS A 55 4711 5490 5287 1564 -544 -246 C ATOM 424 CG LYS A 55 -39.920 3.716 83.742 1.00 57.02 C ANISOU 424 CG LYS A 55 6690 7627 7349 1825 -624 -216 C ATOM 425 CD LYS A 55 -41.223 2.979 83.512 1.00 61.06 C ANISOU 425 CD LYS A 55 6864 8440 7896 1854 -645 -229 C ATOM 426 CE LYS A 55 -41.875 3.489 82.219 1.00 69.24 C ANISOU 426 CE LYS A 55 7886 9511 8910 1957 -790 -166 C ATOM 427 NZ LYS A 55 -43.334 3.756 82.276 1.00 66.53 N ANISOU 427 NZ LYS A 55 7316 9340 8622 2090 -791 -187 N ATOM 428 N ASN A 56 -37.158 1.236 86.524 1.00 26.27 N ANISOU 428 N ASN A 56 2974 3597 3412 1197 -370 -329 N ATOM 429 CA ASN A 56 -36.036 0.364 86.837 1.00 25.96 C ANISOU 429 CA ASN A 56 3007 3486 3370 988 -363 -328 C ATOM 430 C ASN A 56 -36.517 -0.922 87.488 1.00 20.33 C ANISOU 430 C ASN A 56 2145 2946 2634 892 -252 -301 C ATOM 431 O ASN A 56 -36.018 -2.008 87.170 1.00 24.43 O ANISOU 431 O ASN A 56 2631 3463 3190 698 -254 -261 O ATOM 432 CB ASN A 56 -35.039 1.085 87.740 1.00 26.29 C ANISOU 432 CB ASN A 56 3260 3344 3384 1031 -391 -412 C ATOM 433 CG ASN A 56 -34.309 2.198 87.021 1.00 28.21 C ANISOU 433 CG ASN A 56 3653 3356 3711 1048 -483 -422 C ATOM 434 OD1 ASN A 56 -34.382 2.307 85.798 1.00 28.67 O ANISOU 434 OD1 ASN A 56 3686 3391 3815 1016 -513 -338 O ATOM 435 ND2 ASN A 56 -33.619 3.042 87.775 1.00 28.80 N ANISOU 435 ND2 ASN A 56 3891 3250 3802 1101 -528 -527 N ATOM 436 N ILE A 57 -37.481 -0.817 88.410 1.00 25.35 N ANISOU 436 N ILE A 57 2697 3720 3216 1030 -132 -315 N ATOM 437 CA ILE A 57 -38.004 -2.014 89.062 1.00 27.86 C ANISOU 437 CA ILE A 57 2873 4188 3526 935 20 -257 C ATOM 438 C ILE A 57 -38.648 -2.942 88.039 1.00 27.79 C ANISOU 438 C ILE A 57 2624 4280 3654 770 6 -206 C ATOM 439 O ILE A 57 -38.465 -4.167 88.101 1.00 25.16 O ANISOU 439 O ILE A 57 2237 3953 3369 578 63 -155 O ATOM 440 CB ILE A 57 -38.978 -1.630 90.191 1.00 31.54 C ANISOU 440 CB ILE A 57 3283 4793 3906 1135 192 -270 C ATOM 441 CG1 ILE A 57 -38.187 -1.249 91.454 1.00 28.42 C ANISOU 441 CG1 ILE A 57 3156 4313 3331 1245 219 -328 C ATOM 442 CG2 ILE A 57 -39.907 -2.781 90.508 1.00 28.31 C ANISOU 442 CG2 ILE A 57 2637 4563 3558 1030 384 -178 C ATOM 443 CD1 ILE A 57 -39.054 -0.599 92.520 1.00 31.97 C ANISOU 443 CD1 ILE A 57 3614 4882 3650 1502 379 -374 C ATOM 444 N ASP A 58 -39.399 -2.372 87.079 1.00 27.18 N ANISOU 444 N ASP A 58 2412 4273 3642 855 -89 -229 N ATOM 445 CA ASP A 58 -39.922 -3.137 85.948 1.00 29.82 C ANISOU 445 CA ASP A 58 2542 4698 4092 714 -173 -223 C ATOM 446 C ASP A 58 -38.836 -3.974 85.294 1.00 24.29 C ANISOU 446 C ASP A 58 1962 3867 3399 500 -250 -214 C ATOM 447 O ASP A 58 -39.035 -5.163 85.006 1.00 29.41 O ANISOU 447 O ASP A 58 2479 4555 4139 312 -235 -211 O ATOM 448 CB ASP A 58 -40.515 -2.199 84.884 1.00 27.22 C ANISOU 448 CB ASP A 58 2151 4422 3770 880 -332 -252 C ATOM 449 CG ASP A 58 -41.910 -1.707 85.214 1.00 37.29 C ANISOU 449 CG ASP A 58 3182 5886 5103 1072 -279 -272 C ATOM 450 OD1 ASP A 58 -42.528 -2.179 86.197 1.00 34.96 O ANISOU 450 OD1 ASP A 58 2725 5702 4858 1051 -92 -260 O ATOM 451 OD2 ASP A 58 -42.390 -0.831 84.459 1.00 39.66 O ANISOU 451 OD2 ASP A 58 3453 6222 5395 1261 -416 -288 O ATOM 452 N AMET A 59 -37.680 -3.366 85.030 0.57 23.84 N ANISOU 452 N AMET A 59 2146 3644 3270 526 -325 -216 N ATOM 453 N BMET A 59 -37.681 -3.358 85.006 0.43 24.11 N ANISOU 453 N BMET A 59 2180 3678 3304 527 -328 -216 N ATOM 454 CA AMET A 59 -36.606 -4.100 84.369 0.57 25.15 C ANISOU 454 CA AMET A 59 2413 3694 3447 351 -379 -210 C ATOM 455 CA BMET A 59 -36.593 -4.101 84.373 0.43 25.04 C ANISOU 455 CA BMET A 59 2402 3679 3433 350 -378 -210 C ATOM 456 C AMET A 59 -36.023 -5.176 85.276 0.57 24.20 C ANISOU 456 C AMET A 59 2326 3523 3347 210 -277 -186 C ATOM 457 C BMET A 59 -36.065 -5.195 85.288 0.43 23.69 C ANISOU 457 C BMET A 59 2254 3464 3284 209 -275 -186 C ATOM 458 O AMET A 59 -35.661 -6.260 84.803 0.57 22.46 O ANISOU 458 O AMET A 59 2084 3267 3184 44 -287 -184 O ATOM 459 O BMET A 59 -35.769 -6.304 84.829 0.43 25.19 O ANISOU 459 O BMET A 59 2412 3624 3534 42 -281 -184 O ATOM 460 CB AMET A 59 -35.520 -3.133 83.918 0.57 22.22 C ANISOU 460 CB AMET A 59 2258 3158 3028 410 -448 -206 C ATOM 461 CB BMET A 59 -35.439 -3.176 83.980 0.43 23.31 C ANISOU 461 CB BMET A 59 2403 3287 3167 401 -443 -206 C ATOM 462 CG AMET A 59 -35.907 -2.328 82.710 0.57 24.48 C ANISOU 462 CG AMET A 59 2558 3461 3282 520 -548 -192 C ATOM 463 CG BMET A 59 -35.776 -1.724 83.785 0.43 32.77 C ANISOU 463 CG BMET A 59 3670 4452 4329 603 -490 -204 C ATOM 464 SD AMET A 59 -34.554 -1.252 82.202 0.57 30.64 S ANISOU 464 SD AMET A 59 3596 4003 4042 552 -568 -149 S ATOM 465 SD BMET A 59 -35.530 -1.208 82.082 0.43 44.14 S ANISOU 465 SD BMET A 59 5200 5838 5733 634 -597 -155 S ATOM 466 CE AMET A 59 -34.976 -1.005 80.478 0.57 38.29 C ANISOU 466 CE AMET A 59 4588 5032 4928 626 -664 -93 C ATOM 467 CE BMET A 59 -36.398 -2.532 81.263 0.43 19.06 C ANISOU 467 CE BMET A 59 1814 2869 2561 527 -660 -188 C ATOM 468 N ILE A 60 -35.895 -4.888 86.576 1.00 22.32 N ANISOU 468 N ILE A 60 2163 3272 3044 295 -187 -172 N ATOM 469 CA ILE A 60 -35.387 -5.894 87.502 1.00 19.39 C ANISOU 469 CA ILE A 60 1848 2862 2657 203 -95 -125 C ATOM 470 C ILE A 60 -36.351 -7.068 87.576 1.00 27.92 C ANISOU 470 C ILE A 60 2738 4040 3828 77 25 -69 C ATOM 471 O ILE A 60 -35.941 -8.233 87.551 1.00 24.37 O ANISOU 471 O ILE A 60 2303 3518 3441 -78 57 -28 O ATOM 472 CB ILE A 60 -35.144 -5.274 88.889 1.00 21.12 C ANISOU 472 CB ILE A 60 2209 3074 2740 360 -38 -131 C ATOM 473 CG1 ILE A 60 -34.114 -4.158 88.776 1.00 23.24 C ANISOU 473 CG1 ILE A 60 2648 3206 2976 441 -178 -213 C ATOM 474 CG2 ILE A 60 -34.696 -6.360 89.881 1.00 24.97 C ANISOU 474 CG2 ILE A 60 2775 3541 3171 300 55 -57 C ATOM 475 CD1 ILE A 60 -33.897 -3.373 90.048 1.00 25.57 C ANISOU 475 CD1 ILE A 60 3094 3484 3136 613 -174 -274 C ATOM 476 N ARG A 61 -37.654 -6.788 87.628 1.00 25.62 N ANISOU 476 N ARG A 61 2253 3902 3578 139 94 -69 N ATOM 477 CA ARG A 61 -38.608 -7.890 87.691 1.00 27.89 C ANISOU 477 CA ARG A 61 2317 4271 4008 -11 219 -21 C ATOM 478 C ARG A 61 -38.531 -8.738 86.432 1.00 30.00 C ANISOU 478 C ARG A 61 2495 4488 4416 -206 91 -75 C ATOM 479 O ARG A 61 -38.733 -9.955 86.484 1.00 28.52 O ANISOU 479 O ARG A 61 2220 4255 4360 -393 171 -43 O ATOM 480 CB ARG A 61 -40.039 -7.354 87.886 1.00 24.50 C ANISOU 480 CB ARG A 61 1639 4035 3635 97 308 -28 C ATOM 481 CG ARG A 61 -40.279 -6.666 89.234 1.00 26.47 C ANISOU 481 CG ARG A 61 1967 4353 3739 301 486 19 C ATOM 482 CD ARG A 61 -41.718 -6.195 89.374 1.00 32.66 C ANISOU 482 CD ARG A 61 2469 5337 4605 419 597 8 C ATOM 483 NE ARG A 61 -42.614 -7.323 89.593 1.00 37.61 N ANISOU 483 NE ARG A 61 2825 6048 5419 236 788 86 N ATOM 484 CZ ARG A 61 -43.747 -7.533 88.925 1.00 48.58 C ANISOU 484 CZ ARG A 61 3853 7571 7034 159 768 42 C ATOM 485 NH1 ARG A 61 -44.147 -6.683 87.983 1.00 47.46 N ANISOU 485 NH1 ARG A 61 3597 7515 6921 286 551 -71 N ATOM 486 NH2 ARG A 61 -44.491 -8.597 89.205 1.00 48.98 N ANISOU 486 NH2 ARG A 61 3652 7664 7293 -43 961 114 N ATOM 487 N ALA A 62 -38.225 -8.112 85.296 1.00 27.69 N ANISOU 487 N ALA A 62 2247 4187 4088 -156 -99 -159 N ATOM 488 CA ALA A 62 -38.223 -8.811 84.020 1.00 25.15 C ANISOU 488 CA ALA A 62 1859 3845 3850 -298 -237 -237 C ATOM 489 C ALA A 62 -36.966 -9.641 83.809 1.00 30.49 C ANISOU 489 C ALA A 62 2724 4344 4518 -421 -247 -235 C ATOM 490 O ALA A 62 -37.014 -10.640 83.091 1.00 30.11 O ANISOU 490 O ALA A 62 2621 4251 4567 -576 -298 -298 O ATOM 491 CB ALA A 62 -38.376 -7.805 82.874 1.00 23.83 C ANISOU 491 CB ALA A 62 1703 3749 3602 -161 -420 -305 C ATOM 492 N CYS A 63 -35.860 -9.283 84.458 1.00 23.69 N ANISOU 492 N CYS A 63 2068 3376 3556 -350 -206 -180 N ATOM 493 CA CYS A 63 -34.556 -9.787 84.069 1.00 22.50 C ANISOU 493 CA CYS A 63 2081 3073 3394 -415 -246 -193 C ATOM 494 C CYS A 63 -34.330 -11.237 84.512 1.00 20.84 C ANISOU 494 C CYS A 63 1876 2757 3284 -563 -158 -155 C ATOM 495 O CYS A 63 -34.984 -11.767 85.409 1.00 22.18 O ANISOU 495 O CYS A 63 1973 2945 3510 -608 -31 -80 O ATOM 496 CB CYS A 63 -33.434 -8.886 84.622 1.00 19.01 C ANISOU 496 CB CYS A 63 1817 2556 2852 -293 -256 -164 C ATOM 497 SG CYS A 63 -32.976 -9.152 86.343 1.00 22.41 S ANISOU 497 SG CYS A 63 2345 2938 3232 -244 -153 -82 S ATOM 498 N ASP A 64 -33.405 -11.881 83.803 1.00 20.56 N ANISOU 498 N ASP A 64 1934 2601 3277 -632 -211 -202 N ATOM 499 CA ASP A 64 -32.893 -13.215 84.056 1.00 23.39 C ANISOU 499 CA ASP A 64 2349 2808 3731 -742 -151 -176 C ATOM 500 C ASP A 64 -31.721 -13.097 85.071 1.00 24.50 C ANISOU 500 C ASP A 64 2647 2862 3800 -641 -115 -89 C ATOM 501 O ASP A 64 -31.632 -13.845 86.064 1.00 24.38 O ANISOU 501 O ASP A 64 2685 2774 3805 -652 -22 12 O ATOM 502 CB ASP A 64 -32.546 -13.845 82.655 1.00 33.94 C ANISOU 502 CB ASP A 64 3702 4076 5118 -825 -242 -306 C ATOM 503 CG ASP A 64 -33.853 -14.482 81.860 1.00 23.81 C ANISOU 503 CG ASP A 64 2278 2861 3907 -944 -292 -395 C ATOM 504 OD1 ASP A 64 -34.343 -15.419 82.557 1.00 26.05 O ANISOU 504 OD1 ASP A 64 2518 3076 4304 -1048 -193 -331 O ATOM 505 OD2 ASP A 64 -34.485 -14.251 80.647 1.00 64.61 O ANISOU 505 OD2 ASP A 64 7391 8139 9020 -937 -422 -507 O ATOM 506 N ALA A 65 -30.898 -12.065 84.921 1.00 20.49 N ANISOU 506 N ALA A 65 2210 2371 3205 -531 -189 -118 N ATOM 507 CA ALA A 65 -29.756 -11.835 85.804 1.00 17.07 C ANISOU 507 CA ALA A 65 1891 1872 2724 -436 -206 -77 C ATOM 508 C ALA A 65 -29.552 -10.337 85.958 1.00 18.32 C ANISOU 508 C ALA A 65 2070 2091 2799 -324 -269 -110 C ATOM 509 O ALA A 65 -29.999 -9.543 85.129 1.00 19.69 O ANISOU 509 O ALA A 65 2199 2322 2961 -317 -298 -154 O ATOM 510 CB ALA A 65 -28.494 -12.478 85.248 1.00 21.59 C ANISOU 510 CB ALA A 65 2516 2318 3370 -460 -241 -114 C ATOM 511 N ILE A 66 -28.881 -9.960 87.039 1.00 18.44 N ANISOU 511 N ILE A 66 2167 2082 2756 -226 -303 -94 N ATOM 512 CA ILE A 66 -28.398 -8.602 87.238 1.00 17.48 C ANISOU 512 CA ILE A 66 2084 1960 2598 -135 -386 -154 C ATOM 513 C ILE A 66 -26.880 -8.667 87.251 1.00 18.05 C ANISOU 513 C ILE A 66 2184 1924 2748 -135 -471 -195 C ATOM 514 O ILE A 66 -26.316 -9.562 87.875 1.00 20.14 O ANISOU 514 O ILE A 66 2483 2152 3016 -117 -488 -163 O ATOM 515 CB ILE A 66 -28.953 -7.994 88.540 1.00 20.19 C ANISOU 515 CB ILE A 66 2489 2377 2806 -7 -381 -146 C ATOM 516 CG1 ILE A 66 -28.426 -6.585 88.760 1.00 18.70 C ANISOU 516 CG1 ILE A 66 2354 2148 2605 81 -486 -242 C ATOM 517 CG2 ILE A 66 -28.668 -8.881 89.783 1.00 19.97 C ANISOU 517 CG2 ILE A 66 2550 2348 2689 50 -361 -79 C ATOM 518 CD1 ILE A 66 -29.215 -5.790 89.828 1.00 21.81 C ANISOU 518 CD1 ILE A 66 2816 2623 2849 231 -471 -269 C ATOM 519 N ILE A 67 -26.231 -7.794 86.487 1.00 16.62 N ANISOU 519 N ILE A 67 2112 1579 2623 86 -19 6 N ATOM 520 CA ILE A 67 -24.801 -7.550 86.647 1.00 18.17 C ANISOU 520 CA ILE A 67 2265 1838 2802 70 -4 -46 C ATOM 521 C ILE A 67 -24.673 -6.170 87.263 1.00 19.56 C ANISOU 521 C ILE A 67 2440 2057 2933 12 31 -119 C ATOM 522 O ILE A 67 -25.023 -5.162 86.637 1.00 19.02 O ANISOU 522 O ILE A 67 2455 1907 2863 -18 71 -162 O ATOM 523 CB ILE A 67 -24.028 -7.653 85.328 1.00 16.94 C ANISOU 523 CB ILE A 67 2137 1622 2676 65 20 -76 C ATOM 524 CG1 ILE A 67 -24.053 -9.089 84.826 1.00 17.75 C ANISOU 524 CG1 ILE A 67 2254 1679 2811 132 -15 -11 C ATOM 525 CG2 ILE A 67 -22.580 -7.159 85.538 1.00 17.82 C ANISOU 525 CG2 ILE A 67 2175 1837 2760 21 50 -154 C ATOM 526 CD1 ILE A 67 -23.425 -9.265 83.457 1.00 17.76 C ANISOU 526 CD1 ILE A 67 2294 1616 2837 140 12 -40 C ATOM 527 N ALA A 68 -24.170 -6.121 88.502 1.00 19.01 N ANISOU 527 N ALA A 68 2299 2110 2816 2 15 -136 N ATOM 528 CA ALA A 68 -24.135 -4.901 89.300 1.00 20.81 C ANISOU 528 CA ALA A 68 2535 2382 2988 -57 43 -210 C ATOM 529 C ALA A 68 -22.706 -4.414 89.472 1.00 21.64 C ANISOU 529 C ALA A 68 2577 2583 3060 -136 59 -302 C ATOM 530 O ALA A 68 -21.852 -5.161 89.954 1.00 19.68 O ANISOU 530 O ALA A 68 2220 2462 2794 -105 15 -296 O ATOM 531 CB ALA A 68 -24.758 -5.134 90.676 1.00 20.10 C ANISOU 531 CB ALA A 68 2410 2377 2850 -22 13 -172 C ATOM 532 N ASP A 69 -22.465 -3.160 89.102 1.00 17.76 N ANISOU 532 N ASP A 69 2160 2035 2551 -236 122 -390 N ATOM 533 CA ASP A 69 -21.174 -2.508 89.316 1.00 17.38 C ANISOU 533 CA ASP A 69 2055 2088 2461 -360 154 -501 C ATOM 534 C ASP A 69 -21.124 -2.043 90.770 1.00 18.72 C ANISOU 534 C ASP A 69 2184 2373 2556 -392 128 -550 C ATOM 535 O ASP A 69 -21.748 -1.043 91.144 1.00 21.73 O ANISOU 535 O ASP A 69 2679 2677 2900 -432 165 -589 O ATOM 536 CB ASP A 69 -21.014 -1.341 88.344 1.00 22.73 C ANISOU 536 CB ASP A 69 2870 2628 3136 -478 246 -572 C ATOM 537 CG ASP A 69 -19.652 -0.679 88.445 1.00 29.95 C ANISOU 537 CG ASP A 69 3724 3650 4007 -651 297 -698 C ATOM 538 OD1 ASP A 69 -18.874 -1.051 89.353 1.00 27.90 O ANISOU 538 OD1 ASP A 69 3296 3591 3714 -665 247 -740 O ATOM 539 OD2 ASP A 69 -19.346 0.192 87.601 1.00 30.80 O ANISOU 539 OD2 ASP A 69 3951 3648 4104 -775 388 -757 O ATOM 540 N LEU A 70 -20.364 -2.761 91.604 1.00 19.71 N ANISOU 540 N LEU A 70 2156 2686 2646 -361 63 -553 N ATOM 541 CA LEU A 70 -20.198 -2.402 93.007 1.00 22.10 C ANISOU 541 CA LEU A 70 2410 3125 2862 -387 28 -605 C ATOM 542 C LEU A 70 -18.852 -1.735 93.272 1.00 25.23 C ANISOU 542 C LEU A 70 2707 3678 3201 -535 38 -749 C ATOM 543 O LEU A 70 -18.353 -1.754 94.408 1.00 24.11 O ANISOU 543 O LEU A 70 2465 3719 2978 -542 -19 -799 O ATOM 544 CB LEU A 70 -20.387 -3.637 93.890 1.00 19.98 C ANISOU 544 CB LEU A 70 2061 2965 2566 -240 -59 -504 C ATOM 545 CG LEU A 70 -21.804 -4.236 93.824 1.00 22.81 C ANISOU 545 CG LEU A 70 2514 3187 2964 -137 -58 -376 C ATOM 546 CD1 LEU A 70 -21.854 -5.464 94.726 1.00 23.67 C ANISOU 546 CD1 LEU A 70 2571 3394 3028 -19 -130 -278 C ATOM 547 CD2 LEU A 70 -22.843 -3.199 94.265 1.00 21.20 C ANISOU 547 CD2 LEU A 70 2417 2906 2732 -176 -11 -405 C ATOM 548 N SER A 71 -18.269 -1.110 92.245 1.00 23.07 N ANISOU 548 N SER A 71 2462 3345 2958 -665 115 -824 N ATOM 549 CA SER A 71 -17.034 -0.347 92.408 1.00 24.99 C ANISOU 549 CA SER A 71 2616 3734 3145 -856 148 -980 C ATOM 550 C SER A 71 -17.242 0.811 93.383 1.00 26.44 C ANISOU 550 C SER A 71 2894 3907 3246 -982 169 -1077 C ATOM 551 O SER A 71 -18.369 1.275 93.589 1.00 25.74 O ANISOU 551 O SER A 71 2981 3643 3153 -934 193 -1032 O ATOM 552 CB SER A 71 -16.570 0.203 91.061 1.00 26.33 C ANISOU 552 CB SER A 71 2851 3797 3357 -996 255 -1032 C ATOM 553 OG SER A 71 -16.274 -0.839 90.148 1.00 24.48 O ANISOU 553 OG SER A 71 2526 3586 3188 -886 240 -961 O ATOM 554 N PRO A 72 -16.160 1.312 93.977 1.00 27.12 N ANISOU 554 N PRO A 72 2862 4188 3256 -1145 164 -1222 N ATOM 555 CA PRO A 72 -16.291 2.447 94.896 1.00 25.88 C ANISOU 555 CA PRO A 72 2811 4014 3008 -1285 188 -1333 C ATOM 556 C PRO A 72 -17.005 3.614 94.229 1.00 31.37 C ANISOU 556 C PRO A 72 3793 4410 3717 -1385 309 -1353 C ATOM 557 O PRO A 72 -16.763 3.935 93.062 1.00 31.87 O ANISOU 557 O PRO A 72 3938 4345 3826 -1459 397 -1345 O ATOM 558 CB PRO A 72 -14.834 2.794 95.251 1.00 28.94 C ANISOU 558 CB PRO A 72 3019 4651 3325 -1468 185 -1485 C ATOM 559 CG PRO A 72 -13.985 2.048 94.266 1.00 42.08 C ANISOU 559 CG PRO A 72 4513 6424 5050 -1446 191 -1466 C ATOM 560 CD PRO A 72 -14.773 0.822 93.910 1.00 35.80 C ANISOU 560 CD PRO A 72 3709 5558 4337 -1197 126 -1301 C ATOM 561 N PHE A 73 -17.905 4.241 94.984 1.00 30.18 N ANISOU 561 N PHE A 73 3807 4145 3515 -1348 315 -1355 N ATOM 562 CA PHE A 73 -18.729 5.344 94.493 1.00 30.58 C ANISOU 562 CA PHE A 73 4149 3907 3563 -1359 415 -1341 C ATOM 563 C PHE A 73 -18.732 6.455 95.542 1.00 32.62 C ANISOU 563 C PHE A 73 4517 4154 3723 -1431 437 -1413 C ATOM 564 O PHE A 73 -19.421 6.353 96.565 1.00 35.65 O ANISOU 564 O PHE A 73 4919 4573 4054 -1346 387 -1431 O ATOM 565 CB PHE A 73 -20.148 4.867 94.186 1.00 31.68 C ANISOU 565 CB PHE A 73 4383 3894 3759 -1132 397 -1208 C ATOM 566 CG PHE A 73 -21.050 5.957 93.705 1.00 30.17 C ANISOU 566 CG PHE A 73 4478 3433 3552 -1096 480 -1195 C ATOM 567 CD1 PHE A 73 -20.897 6.471 92.428 1.00 31.99 C ANISOU 567 CD1 PHE A 73 4824 3513 3818 -1113 547 -1132 C ATOM 568 CD2 PHE A 73 -22.032 6.485 94.527 1.00 31.67 C ANISOU 568 CD2 PHE A 73 4797 3553 3683 -994 481 -1204 C ATOM 569 CE1 PHE A 73 -21.712 7.480 91.975 1.00 30.01 C ANISOU 569 CE1 PHE A 73 4803 3057 3542 -1022 594 -1073 C ATOM 570 CE2 PHE A 73 -22.859 7.494 94.074 1.00 34.11 C ANISOU 570 CE2 PHE A 73 5331 3651 3979 -894 533 -1150 C ATOM 571 CZ PHE A 73 -22.694 7.993 92.787 1.00 28.79 C ANISOU 571 CZ PHE A 73 4761 2838 3339 -906 582 -1082 C ATOM 572 N ARG A 74 -17.974 7.519 95.279 1.00 35.34 N ANISOU 572 N ARG A 74 4944 4448 4034 -1591 520 -1457 N ATOM 573 CA ARG A 74 -17.895 8.708 96.130 1.00 37.91 C ANISOU 573 CA ARG A 74 5402 4731 4270 -1685 557 -1530 C ATOM 574 C ARG A 74 -17.312 8.413 97.503 1.00 44.64 C ANISOU 574 C ARG A 74 6070 5840 5050 -1743 474 -1628 C ATOM 575 O ARG A 74 -17.323 9.286 98.380 1.00 49.02 O ANISOU 575 O ARG A 74 6725 6374 5526 -1807 488 -1696 O ATOM 576 CB ARG A 74 -19.263 9.381 96.296 1.00 47.21 C ANISOU 576 CB ARG A 74 6834 5672 5430 -1535 580 -1480 C ATOM 577 CG ARG A 74 -19.899 9.815 94.996 1.00 47.53 C ANISOU 577 CG ARG A 74 7069 5470 5521 -1447 648 -1377 C ATOM 578 CD ARG A 74 -20.923 10.888 95.252 1.00 43.39 C ANISOU 578 CD ARG A 74 6797 4742 4946 -1336 682 -1358 C ATOM 579 NE ARG A 74 -21.169 11.683 94.059 1.00 52.51 N ANISOU 579 NE ARG A 74 8152 5692 6109 -1309 757 -1282 N ATOM 580 CZ ARG A 74 -22.354 11.790 93.475 1.00 58.10 C ANISOU 580 CZ ARG A 74 8987 6251 6837 -1096 749 -1189 C ATOM 581 NH1 ARG A 74 -23.405 11.152 93.983 1.00 56.91 N ANISOU 581 NH1 ARG A 74 8782 6133 6709 -902 683 -1167 N ATOM 582 NH2 ARG A 74 -22.486 12.539 92.389 1.00 57.16 N ANISOU 582 NH2 ARG A 74 9045 5971 6703 -1079 811 -1123 N ATOM 583 N SER A 75 -16.821 7.206 97.710 1.00 35.43 N ANISOU 583 N SER A 75 4643 4918 3902 -1704 380 -1632 N ATOM 584 CA SER A 75 -16.170 6.760 98.937 1.00 34.10 C ANISOU 584 CA SER A 75 4263 5037 3654 -1721 278 -1705 C ATOM 585 C SER A 75 -15.562 5.403 98.616 1.00 32.29 C ANISOU 585 C SER A 75 3763 5037 3470 -1644 190 -1671 C ATOM 586 O SER A 75 -15.455 5.021 97.444 1.00 34.58 O ANISOU 586 O SER A 75 4034 5256 3847 -1632 229 -1618 O ATOM 587 CB SER A 75 -17.156 6.703 100.108 1.00 34.14 C ANISOU 587 CB SER A 75 4345 5040 3587 -1598 216 -1703 C ATOM 588 OG SER A 75 -17.972 5.539 100.032 1.00 37.66 O ANISOU 588 OG SER A 75 4729 5518 4061 -1415 147 -1620 O ATOM 589 N LYS A 76 -15.175 4.663 99.645 1.00 33.99 N ANISOU 589 N LYS A 76 3778 5520 3617 -1568 68 -1691 N ATOM 590 CA LYS A 76 -14.749 3.290 99.417 1.00 29.47 C ANISOU 590 CA LYS A 76 2970 5151 3077 -1429 -33 -1631 C ATOM 591 C LYS A 76 -15.928 2.326 99.350 1.00 31.65 C ANISOU 591 C LYS A 76 3297 5328 3401 -1204 -85 -1479 C ATOM 592 O LYS A 76 -15.729 1.129 99.104 1.00 36.23 O ANISOU 592 O LYS A 76 3734 6006 4025 -1034 -153 -1369 O ATOM 593 CB LYS A 76 -13.760 2.867 100.513 1.00 34.17 C ANISOU 593 CB LYS A 76 3343 6068 3572 -1387 -141 -1678 C ATOM 594 CG LYS A 76 -12.477 3.690 100.521 1.00 39.62 C ANISOU 594 CG LYS A 76 3954 6875 4227 -1580 -78 -1801 C ATOM 595 CD LYS A 76 -11.692 3.494 101.809 1.00 44.87 C ANISOU 595 CD LYS A 76 4445 7831 4772 -1544 -181 -1864 C ATOM 596 CE LYS A 76 -10.330 4.160 101.742 1.00 55.69 C ANISOU 596 CE LYS A 76 5694 9364 6104 -1732 -124 -1996 C ATOM 597 NZ LYS A 76 -10.430 5.617 102.010 1.00 64.02 N ANISOU 597 NZ LYS A 76 6934 10269 7121 -1965 -20 -2092 N ATOM 598 N GLU A 77 -17.175 2.833 99.523 1.00 30.26 N ANISOU 598 N GLU A 77 3346 4921 3230 -1155 -28 -1425 N ATOM 599 CA GLU A 77 -18.390 2.025 99.462 1.00 24.83 C ANISOU 599 CA GLU A 77 2725 4110 2601 -926 -41 -1241 C ATOM 600 C GLU A 77 -19.027 2.069 98.083 1.00 26.90 C ANISOU 600 C GLU A 77 3108 4125 2988 -898 41 -1160 C ATOM 601 O GLU A 77 -18.958 3.092 97.402 1.00 30.77 O ANISOU 601 O GLU A 77 3736 4460 3494 -1042 133 -1243 O ATOM 602 CB GLU A 77 -19.418 2.538 100.475 1.00 26.58 C ANISOU 602 CB GLU A 77 3092 4263 2744 -875 -27 -1238 C ATOM 603 CG GLU A 77 -18.925 2.665 101.904 1.00 29.37 C ANISOU 603 CG GLU A 77 3371 4838 2951 -909 -100 -1328 C ATOM 604 CD GLU A 77 -18.808 1.339 102.636 1.00 37.93 C ANISOU 604 CD GLU A 77 4300 6120 3990 -730 -214 -1214 C ATOM 605 OE1 GLU A 77 -17.708 1.036 103.151 1.00 37.63 O ANISOU 605 OE1 GLU A 77 4095 6329 3875 -757 -305 -1283 O ATOM 606 OE2 GLU A 77 -19.822 0.609 102.711 1.00 35.12 O ANISOU 606 OE2 GLU A 77 3998 5680 3668 -564 -210 -1060 O ATOM 607 N PRO A 78 -19.724 0.993 97.710 1.00 24.38 N ANISOU 607 N PRO A 78 2764 3756 2742 -715 12 -1000 N ATOM 608 CA PRO A 78 -20.480 0.996 96.448 1.00 24.13 C ANISOU 608 CA PRO A 78 2849 3501 2818 -670 77 -921 C ATOM 609 C PRO A 78 -21.656 1.961 96.485 1.00 24.25 C ANISOU 609 C PRO A 78 3071 3324 2820 -654 147 -928 C ATOM 610 O PRO A 78 -21.995 2.566 97.501 1.00 27.15 O ANISOU 610 O PRO A 78 3499 3715 3100 -664 152 -984 O ATOM 611 CB PRO A 78 -20.975 -0.447 96.301 1.00 29.50 C ANISOU 611 CB PRO A 78 3447 4205 3556 -489 17 -760 C ATOM 612 CG PRO A 78 -20.211 -1.255 97.292 1.00 25.74 C ANISOU 612 CG PRO A 78 2812 3959 3009 -439 -77 -754 C ATOM 613 CD PRO A 78 -19.835 -0.301 98.403 1.00 23.93 C ANISOU 613 CD PRO A 78 2586 3841 2664 -548 -82 -885 C ATOM 614 N ASP A 79 -22.293 2.079 95.322 1.00 24.64 N ANISOU 614 N ASP A 79 3229 3185 2948 -610 199 -872 N ATOM 615 CA ASP A 79 -23.462 2.932 95.155 1.00 24.26 C ANISOU 615 CA ASP A 79 3376 2953 2890 -548 259 -869 C ATOM 616 C ASP A 79 -24.679 2.293 95.817 1.00 23.19 C ANISOU 616 C ASP A 79 3198 2863 2751 -378 222 -770 C ATOM 617 O ASP A 79 -24.993 1.136 95.537 1.00 22.68 O ANISOU 617 O ASP A 79 3025 2843 2748 -289 178 -656 O ATOM 618 CB ASP A 79 -23.739 3.124 93.661 1.00 20.52 C ANISOU 618 CB ASP A 79 3014 2292 2491 -530 308 -831 C ATOM 619 CG ASP A 79 -25.111 3.722 93.384 1.00 23.19 C ANISOU 619 CG ASP A 79 3521 2468 2823 -394 345 -798 C ATOM 620 OD1 ASP A 79 -25.524 4.644 94.095 1.00 28.90 O ANISOU 620 OD1 ASP A 79 4368 3145 3467 -383 379 -865 O ATOM 621 OD2 ASP A 79 -25.772 3.268 92.423 1.00 25.55 O ANISOU 621 OD2 ASP A 79 3828 2691 3188 -289 336 -711 O ATOM 622 N CYS A 80 -25.363 3.046 96.693 1.00 23.15 N ANISOU 622 N CYS A 80 3287 2843 2666 -341 251 -818 N ATOM 623 CA CYS A 80 -26.512 2.488 97.410 1.00 20.30 C ANISOU 623 CA CYS A 80 2873 2552 2287 -197 233 -736 C ATOM 624 C CYS A 80 -27.679 2.184 96.484 1.00 21.47 C ANISOU 624 C CYS A 80 3042 2605 2512 -69 248 -646 C ATOM 625 O CYS A 80 -28.480 1.282 96.770 1.00 24.02 O ANISOU 625 O CYS A 80 3263 3011 2853 18 225 -553 O ATOM 626 CB ACYS A 80 -26.932 3.410 98.558 0.67 25.90 C ANISOU 626 CB ACYS A 80 3676 3282 2882 -183 268 -823 C ATOM 627 CB BCYS A 80 -27.024 3.484 98.443 0.33 26.15 C ANISOU 627 CB BCYS A 80 3723 3293 2919 -175 274 -822 C ATOM 628 SG ACYS A 80 -27.420 5.049 98.095 0.67 31.59 S ANISOU 628 SG ACYS A 80 4658 3782 3564 -165 357 -929 S ATOM 629 SG BCYS A 80 -26.095 3.576 99.909 0.33 24.64 S ANISOU 629 SG BCYS A 80 3474 3278 2610 -280 238 -909 S ATOM 630 N GLY A 81 -27.813 2.937 95.393 1.00 19.99 N ANISOU 630 N GLY A 81 2992 2247 2357 -61 289 -675 N ATOM 631 CA GLY A 81 -28.871 2.630 94.442 1.00 20.23 C ANISOU 631 CA GLY A 81 3027 2207 2451 67 287 -597 C ATOM 632 C GLY A 81 -28.689 1.269 93.799 1.00 21.00 C ANISOU 632 C GLY A 81 2980 2358 2640 57 234 -495 C ATOM 633 O GLY A 81 -29.644 0.494 93.661 1.00 24.28 O ANISOU 633 O GLY A 81 3313 2821 3092 143 212 -414 O ATOM 634 N THR A 82 -27.461 0.958 93.405 1.00 23.07 N ANISOU 634 N THR A 82 3211 2620 2934 -53 218 -506 N ATOM 635 CA THR A 82 -27.143 -0.361 92.883 1.00 19.72 C ANISOU 635 CA THR A 82 2665 2244 2584 -53 169 -418 C ATOM 636 C THR A 82 -27.355 -1.433 93.941 1.00 19.62 C ANISOU 636 C THR A 82 2525 2378 2551 -21 125 -348 C ATOM 637 O THR A 82 -27.876 -2.511 93.651 1.00 19.15 O ANISOU 637 O THR A 82 2405 2332 2540 26 98 -254 O ATOM 638 CB THR A 82 -25.696 -0.336 92.387 1.00 19.81 C ANISOU 638 CB THR A 82 2662 2254 2613 -167 171 -466 C ATOM 639 OG1 THR A 82 -25.557 0.751 91.460 1.00 22.06 O ANISOU 639 OG1 THR A 82 3099 2385 2897 -216 232 -530 O ATOM 640 CG2 THR A 82 -25.298 -1.633 91.721 1.00 18.90 C ANISOU 640 CG2 THR A 82 2444 2169 2568 -145 127 -386 C ATOM 641 N ALA A 83 -26.939 -1.153 95.182 1.00 20.09 N ANISOU 641 N ALA A 83 2562 2544 2529 -55 120 -395 N ATOM 642 CA ALA A 83 -27.157 -2.096 96.278 1.00 20.30 C ANISOU 642 CA ALA A 83 2499 2704 2510 -19 84 -324 C ATOM 643 C ALA A 83 -28.638 -2.419 96.468 1.00 20.11 C ANISOU 643 C ALA A 83 2471 2682 2489 57 110 -256 C ATOM 644 O ALA A 83 -28.993 -3.583 96.677 1.00 20.95 O ANISOU 644 O ALA A 83 2517 2836 2606 76 90 -158 O ATOM 645 CB ALA A 83 -26.551 -1.548 97.585 1.00 20.17 C ANISOU 645 CB ALA A 83 2477 2803 2383 -62 76 -402 C ATOM 646 N PHE A 84 -29.506 -1.401 96.423 1.00 20.47 N ANISOU 646 N PHE A 84 2583 2682 2514 101 159 -312 N ATOM 647 CA PHE A 84 -30.950 -1.617 96.492 1.00 22.89 C ANISOU 647 CA PHE A 84 2854 3020 2822 180 187 -266 C ATOM 648 C PHE A 84 -31.415 -2.549 95.379 1.00 18.24 C ANISOU 648 C PHE A 84 2216 2387 2329 190 164 -186 C ATOM 649 O PHE A 84 -32.207 -3.473 95.603 1.00 20.92 O ANISOU 649 O PHE A 84 2477 2797 2675 191 166 -112 O ATOM 650 CB PHE A 84 -31.660 -0.262 96.379 1.00 23.64 C ANISOU 650 CB PHE A 84 3042 3059 2881 260 235 -354 C ATOM 651 CG PHE A 84 -33.172 -0.348 96.293 1.00 23.89 C ANISOU 651 CG PHE A 84 3014 3150 2912 366 261 -329 C ATOM 652 CD1 PHE A 84 -33.944 -0.151 97.423 1.00 24.36 C ANISOU 652 CD1 PHE A 84 3032 3334 2888 415 305 -348 C ATOM 653 CD2 PHE A 84 -33.815 -0.589 95.074 1.00 22.15 C ANISOU 653 CD2 PHE A 84 2770 2881 2766 417 243 -297 C ATOM 654 CE1 PHE A 84 -35.331 -0.199 97.359 1.00 25.24 C ANISOU 654 CE1 PHE A 84 3059 3538 2993 510 336 -340 C ATOM 655 CE2 PHE A 84 -35.198 -0.658 95.009 1.00 24.96 C ANISOU 655 CE2 PHE A 84 3039 3332 3114 511 260 -290 C ATOM 656 CZ PHE A 84 -35.953 -0.456 96.140 1.00 23.26 C ANISOU 656 CZ PHE A 84 2763 3256 2819 557 310 -314 C ATOM 657 N GLU A 85 -30.938 -2.309 94.163 1.00 21.42 N ANISOU 657 N GLU A 85 2673 2670 2796 183 147 -204 N ATOM 658 CA GLU A 85 -31.381 -3.115 93.027 1.00 20.18 C ANISOU 658 CA GLU A 85 2484 2464 2720 194 122 -142 C ATOM 659 C GLU A 85 -30.915 -4.553 93.165 1.00 21.23 C ANISOU 659 C GLU A 85 2555 2630 2883 136 88 -55 C ATOM 660 O GLU A 85 -31.634 -5.489 92.801 1.00 19.72 O ANISOU 660 O GLU A 85 2320 2444 2729 128 78 10 O ATOM 661 CB GLU A 85 -30.870 -2.486 91.739 1.00 17.27 C ANISOU 661 CB GLU A 85 2209 1958 2394 200 118 -183 C ATOM 662 CG GLU A 85 -31.471 -1.098 91.489 1.00 21.95 C ANISOU 662 CG GLU A 85 2908 2485 2946 282 153 -257 C ATOM 663 CD GLU A 85 -30.878 -0.419 90.284 1.00 27.58 C ANISOU 663 CD GLU A 85 3755 3044 3679 275 163 -293 C ATOM 664 OE1 GLU A 85 -29.660 -0.589 90.049 1.00 25.47 O ANISOU 664 OE1 GLU A 85 3502 2741 3434 174 165 -302 O ATOM 665 OE2 GLU A 85 -31.617 0.318 89.591 1.00 29.40 O ANISOU 665 OE2 GLU A 85 4080 3199 3892 377 173 -315 O ATOM 666 N LEU A 86 -29.719 -4.749 93.723 1.00 16.65 N ANISOU 666 N LEU A 86 1976 2075 2275 98 69 -58 N ATOM 667 CA LEU A 86 -29.235 -6.090 93.977 1.00 17.25 C ANISOU 667 CA LEU A 86 2018 2178 2356 81 34 26 C ATOM 668 C LEU A 86 -30.115 -6.781 95.007 1.00 17.55 C ANISOU 668 C LEU A 86 2029 2300 2341 77 52 96 C ATOM 669 O LEU A 86 -30.382 -7.981 94.904 1.00 20.22 O ANISOU 669 O LEU A 86 2370 2617 2696 57 43 183 O ATOM 670 CB LEU A 86 -27.784 -6.009 94.459 1.00 19.56 C ANISOU 670 CB LEU A 86 2301 2521 2610 70 2 -8 C ATOM 671 CG LEU A 86 -27.009 -7.308 94.576 1.00 23.93 C ANISOU 671 CG LEU A 86 2836 3097 3160 95 -46 67 C ATOM 672 CD1 LEU A 86 -26.745 -7.935 93.223 1.00 22.08 C ANISOU 672 CD1 LEU A 86 2620 2756 3015 104 -59 93 C ATOM 673 CD2 LEU A 86 -25.671 -7.047 95.314 1.00 22.77 C ANISOU 673 CD2 LEU A 86 2644 3063 2945 102 -84 13 C ATOM 674 N GLY A 87 -30.566 -6.037 96.019 1.00 19.84 N ANISOU 674 N GLY A 87 2307 2677 2555 87 86 56 N ATOM 675 CA GLY A 87 -31.424 -6.638 97.024 1.00 18.08 C ANISOU 675 CA GLY A 87 2058 2545 2268 73 120 118 C ATOM 676 C GLY A 87 -32.768 -7.022 96.435 1.00 20.79 C ANISOU 676 C GLY A 87 2355 2884 2658 52 155 149 C ATOM 677 O GLY A 87 -33.288 -8.104 96.710 1.00 21.61 O ANISOU 677 O GLY A 87 2449 3011 2750 -6 175 231 O ATOM 678 N TYR A 88 -33.312 -6.149 95.590 1.00 20.65 N ANISOU 678 N TYR A 88 2320 2838 2688 96 161 79 N ATOM 679 CA TYR A 88 -34.569 -6.419 94.905 1.00 21.16 C ANISOU 679 CA TYR A 88 2316 2928 2794 91 177 88 C ATOM 680 C TYR A 88 -34.455 -7.681 94.071 1.00 23.18 C ANISOU 680 C TYR A 88 2583 3106 3118 18 145 159 C ATOM 681 O TYR A 88 -35.318 -8.562 94.147 1.00 21.61 O ANISOU 681 O TYR A 88 2335 2956 2919 -59 170 207 O ATOM 682 CB TYR A 88 -34.936 -5.220 94.039 1.00 18.48 C ANISOU 682 CB TYR A 88 1985 2554 2481 188 169 1 C ATOM 683 CG TYR A 88 -36.419 -5.109 93.743 1.00 22.99 C ANISOU 683 CG TYR A 88 2453 3231 3052 230 190 -22 C ATOM 684 CD1 TYR A 88 -37.006 -5.896 92.769 1.00 27.30 C ANISOU 684 CD1 TYR A 88 2940 3776 3658 185 161 6 C ATOM 685 CD2 TYR A 88 -37.214 -4.223 94.452 1.00 24.14 C ANISOU 685 CD2 TYR A 88 2552 3492 3127 318 236 -83 C ATOM 686 CE1 TYR A 88 -38.361 -5.810 92.511 1.00 24.96 C ANISOU 686 CE1 TYR A 88 2517 3616 3352 218 172 -30 C ATOM 687 CE2 TYR A 88 -38.577 -4.110 94.185 1.00 22.81 C ANISOU 687 CE2 TYR A 88 2258 3459 2950 377 252 -116 C ATOM 688 CZ TYR A 88 -39.131 -4.914 93.220 1.00 23.79 C ANISOU 688 CZ TYR A 88 2303 3602 3134 321 217 -91 C ATOM 689 OH TYR A 88 -40.483 -4.822 92.972 1.00 31.63 O ANISOU 689 OH TYR A 88 3140 4768 4110 373 225 -136 O ATOM 690 N ALA A 89 -33.376 -7.788 93.282 1.00 18.32 N ANISOU 690 N ALA A 89 2037 2370 2556 31 97 161 N ATOM 691 CA ALA A 89 -33.160 -8.974 92.452 1.00 18.45 C ANISOU 691 CA ALA A 89 2087 2294 2630 -21 67 221 C ATOM 692 C ALA A 89 -32.956 -10.221 93.305 1.00 19.90 C ANISOU 692 C ALA A 89 2310 2480 2770 -83 79 314 C ATOM 693 O ALA A 89 -33.445 -11.304 92.966 1.00 22.75 O ANISOU 693 O ALA A 89 2697 2797 3152 -160 86 370 O ATOM 694 CB ALA A 89 -31.945 -8.757 91.547 1.00 19.71 C ANISOU 694 CB ALA A 89 2307 2343 2837 20 25 195 C ATOM 695 N ALA A 90 -32.223 -10.094 94.417 1.00 19.60 N ANISOU 695 N ALA A 90 2298 2489 2661 -52 81 330 N ATOM 696 CA ALA A 90 -32.007 -11.250 95.274 1.00 22.80 C ANISOU 696 CA ALA A 90 2771 2889 3002 -85 90 428 C ATOM 697 C ALA A 90 -33.322 -11.791 95.819 1.00 23.60 C ANISOU 697 C ALA A 90 2854 3050 3062 -186 159 475 C ATOM 698 O ALA A 90 -33.521 -13.007 95.856 1.00 25.87 O ANISOU 698 O ALA A 90 3225 3270 3336 -263 177 559 O ATOM 699 CB ALA A 90 -31.069 -10.886 96.428 1.00 22.74 C ANISOU 699 CB ALA A 90 2781 2956 2905 -20 71 425 C ATOM 700 N ALA A 91 -34.226 -10.902 96.253 1.00 22.24 N ANISOU 700 N ALA A 91 2581 3004 2864 -192 205 417 N ATOM 701 CA ALA A 91 -35.514 -11.350 96.781 1.00 22.85 C ANISOU 701 CA ALA A 91 2607 3178 2896 -298 283 446 C ATOM 702 C ALA A 91 -36.326 -12.099 95.726 1.00 23.07 C ANISOU 702 C ALA A 91 2605 3163 2997 -404 289 454 C ATOM 703 O ALA A 91 -37.080 -13.028 96.057 1.00 25.74 O ANISOU 703 O ALA A 91 2955 3526 3300 -544 351 508 O ATOM 704 CB ALA A 91 -36.312 -10.154 97.306 1.00 23.61 C ANISOU 704 CB ALA A 91 2583 3435 2954 -250 328 362 C ATOM 705 N LEU A 92 -36.203 -11.706 94.465 1.00 25.53 N ANISOU 705 N LEU A 92 2888 3414 3399 -352 230 395 N ATOM 706 CA LEU A 92 -36.917 -12.371 93.382 1.00 23.88 C ANISOU 706 CA LEU A 92 2650 3170 3252 -446 219 388 C ATOM 707 C LEU A 92 -36.208 -13.625 92.892 1.00 30.40 C ANISOU 707 C LEU A 92 3630 3816 4105 -504 192 462 C ATOM 708 O LEU A 92 -36.749 -14.334 92.035 1.00 30.29 O ANISOU 708 O LEU A 92 3623 3754 4133 -605 186 458 O ATOM 709 CB LEU A 92 -37.127 -11.397 92.218 1.00 21.92 C ANISOU 709 CB LEU A 92 2322 2936 3069 -348 164 295 C ATOM 710 CG LEU A 92 -37.928 -10.121 92.498 1.00 29.38 C ANISOU 710 CG LEU A 92 3136 4043 3986 -255 184 213 C ATOM 711 CD1 LEU A 92 -38.153 -9.352 91.203 1.00 31.56 C ANISOU 711 CD1 LEU A 92 3376 4301 4314 -153 123 137 C ATOM 712 CD2 LEU A 92 -39.255 -10.428 93.163 1.00 32.04 C ANISOU 712 CD2 LEU A 92 3337 4565 4272 -354 255 206 C ATOM 713 N GLY A 93 -35.024 -13.936 93.415 1.00 22.90 N ANISOU 713 N GLY A 93 2805 2774 3123 -437 174 522 N ATOM 714 CA GLY A 93 -34.357 -15.154 92.995 1.00 23.34 C ANISOU 714 CA GLY A 93 3020 2659 3191 -459 151 592 C ATOM 715 C GLY A 93 -33.586 -15.067 91.700 1.00 23.57 C ANISOU 715 C GLY A 93 3077 2578 3302 -377 82 552 C ATOM 716 O GLY A 93 -33.338 -16.100 91.078 1.00 25.18 O ANISOU 716 O GLY A 93 3401 2641 3526 -410 68 590 O ATOM 717 N LYS A 94 -33.179 -13.871 91.285 1.00 22.01 N ANISOU 717 N LYS A 94 2791 2430 3142 -274 46 475 N ATOM 718 CA LYS A 94 -32.432 -13.702 90.047 1.00 21.28 C ANISOU 718 CA LYS A 94 2726 2243 3116 -205 -5 434 C ATOM 719 C LYS A 94 -30.997 -14.206 90.196 1.00 24.59 C ANISOU 719 C LYS A 94 3241 2582 3520 -114 -33 473 C ATOM 720 O LYS A 94 -30.473 -14.378 91.304 1.00 24.04 O ANISOU 720 O LYS A 94 3198 2552 3383 -73 -28 519 O ATOM 721 CB LYS A 94 -32.379 -12.232 89.622 1.00 20.91 C ANISOU 721 CB LYS A 94 2588 2261 3096 -131 -19 345 C ATOM 722 CG LYS A 94 -33.727 -11.523 89.551 1.00 22.40 C ANISOU 722 CG LYS A 94 2670 2556 3283 -161 0 294 C ATOM 723 CD LYS A 94 -34.666 -12.229 88.581 1.00 24.21 C ANISOU 723 CD LYS A 94 2885 2763 3550 -245 -14 289 C ATOM 724 CE LYS A 94 -35.932 -11.393 88.435 1.00 21.45 C ANISOU 724 CE LYS A 94 2401 2557 3191 -234 -10 222 C ATOM 725 NZ LYS A 94 -36.868 -11.968 87.422 1.00 22.15 N ANISOU 725 NZ LYS A 94 2446 2662 3308 -313 -38 195 N ATOM 726 N VAL A 95 -30.354 -14.435 89.051 1.00 22.05 N ANISOU 726 N VAL A 95 2965 2162 3251 -69 -65 450 N ATOM 727 CA VAL A 95 -28.914 -14.696 89.043 1.00 24.63 C ANISOU 727 CA VAL A 95 3339 2452 3566 44 -94 459 C ATOM 728 C VAL A 95 -28.204 -13.397 89.394 1.00 17.86 C ANISOU 728 C VAL A 95 2378 1710 2700 101 -100 392 C ATOM 729 O VAL A 95 -28.442 -12.364 88.761 1.00 20.10 O ANISOU 729 O VAL A 95 2603 2012 3020 83 -92 321 O ATOM 730 CB VAL A 95 -28.456 -15.220 87.674 1.00 21.62 C ANISOU 730 CB VAL A 95 3025 1950 3239 75 -114 439 C ATOM 731 CG1 VAL A 95 -26.934 -15.294 87.614 1.00 24.44 C ANISOU 731 CG1 VAL A 95 3386 2316 3583 207 -137 426 C ATOM 732 CG2 VAL A 95 -29.101 -16.555 87.354 1.00 26.51 C ANISOU 732 CG2 VAL A 95 3776 2438 3857 5 -106 497 C ATOM 733 N LEU A 96 -27.364 -13.421 90.437 1.00 20.75 N ANISOU 733 N LEU A 96 2730 2153 3002 166 -115 411 N ATOM 734 CA LEU A 96 -26.715 -12.207 90.926 1.00 18.99 C ANISOU 734 CA LEU A 96 2410 2050 2755 190 -119 337 C ATOM 735 C LEU A 96 -25.243 -12.243 90.564 1.00 21.20 C ANISOU 735 C LEU A 96 2661 2358 3035 272 -150 297 C ATOM 736 O LEU A 96 -24.507 -13.135 91.015 1.00 21.02 O ANISOU 736 O LEU A 96 2667 2355 2966 364 -184 345 O ATOM 737 CB LEU A 96 -26.864 -12.070 92.441 1.00 18.38 C ANISOU 737 CB LEU A 96 2313 2081 2588 192 -117 366 C ATOM 738 CG LEU A 96 -28.247 -12.313 93.031 1.00 19.95 C ANISOU 738 CG LEU A 96 2538 2279 2762 116 -76 420 C ATOM 739 CD1 LEU A 96 -28.133 -12.302 94.548 1.00 25.06 C ANISOU 739 CD1 LEU A 96 3186 3034 3302 137 -74 455 C ATOM 740 CD2 LEU A 96 -29.231 -11.244 92.537 1.00 22.39 C ANISOU 740 CD2 LEU A 96 2782 2606 3119 56 -42 351 C ATOM 741 N LEU A 97 -24.807 -11.258 89.791 1.00 20.38 N ANISOU 741 N LEU A 97 2502 2267 2973 244 -133 208 N ATOM 742 CA LEU A 97 -23.404 -11.133 89.407 1.00 17.44 C ANISOU 742 CA LEU A 97 2071 1956 2600 293 -146 148 C ATOM 743 C LEU A 97 -22.929 -9.724 89.717 1.00 18.96 C ANISOU 743 C LEU A 97 2181 2251 2771 224 -123 46 C ATOM 744 O LEU A 97 -23.622 -8.741 89.423 1.00 20.12 O ANISOU 744 O LEU A 97 2356 2348 2940 147 -84 7 O ATOM 745 CB LEU A 97 -23.214 -11.451 87.912 1.00 19.07 C ANISOU 745 CB LEU A 97 2319 2054 2872 302 -128 133 C ATOM 746 CG LEU A 97 -23.694 -12.842 87.482 1.00 20.63 C ANISOU 746 CG LEU A 97 2624 2124 3089 353 -146 219 C ATOM 747 CD1 LEU A 97 -23.652 -12.958 85.961 1.00 22.92 C ANISOU 747 CD1 LEU A 97 2963 2308 3438 345 -125 188 C ATOM 748 CD2 LEU A 97 -22.813 -13.920 88.119 1.00 21.60 C ANISOU 748 CD2 LEU A 97 2763 2287 3156 483 -187 268 C ATOM 749 N THR A 98 -21.742 -9.621 90.325 1.00 17.85 N ANISOU 749 N THR A 98 1946 2260 2578 256 -150 -3 N ATOM 750 CA THR A 98 -21.234 -8.333 90.774 1.00 21.19 C ANISOU 750 CA THR A 98 2295 2790 2964 164 -129 -110 C ATOM 751 C THR A 98 -19.784 -8.174 90.358 1.00 19.71 C ANISOU 751 C THR A 98 1996 2724 2769 156 -128 -200 C ATOM 752 O THR A 98 -19.065 -9.158 90.150 1.00 20.79 O ANISOU 752 O THR A 98 2083 2915 2901 269 -165 -174 O ATOM 753 CB THR A 98 -21.312 -8.186 92.312 1.00 22.68 C ANISOU 753 CB THR A 98 2450 3104 3065 176 -167 -105 C ATOM 754 OG1 THR A 98 -20.344 -9.043 92.935 1.00 22.66 O ANISOU 754 OG1 THR A 98 2370 3241 2999 287 -235 -85 O ATOM 755 CG2 THR A 98 -22.705 -8.538 92.825 1.00 24.09 C ANISOU 755 CG2 THR A 98 2721 3193 3238 191 -161 -9 C ATOM 756 N PHE A 99 -19.359 -6.921 90.221 1.00 17.70 N ANISOU 756 N PHE A 99 1707 2513 2506 21 -78 -312 N ATOM 757 CA PHE A 99 -17.957 -6.656 89.938 1.00 18.49 C ANISOU 757 CA PHE A 99 1673 2767 2586 -28 -64 -419 C ATOM 758 C PHE A 99 -17.539 -5.368 90.619 1.00 22.94 C ANISOU 758 C PHE A 99 2190 3436 3092 -186 -37 -540 C ATOM 759 O PHE A 99 -18.377 -4.557 91.023 1.00 22.66 O ANISOU 759 O PHE A 99 2262 3305 3044 -257 -11 -544 O ATOM 760 CB PHE A 99 -17.678 -6.618 88.420 1.00 21.95 C ANISOU 760 CB PHE A 99 2145 3108 3089 -66 5 -440 C ATOM 761 CG PHE A 99 -18.174 -5.373 87.711 1.00 21.28 C ANISOU 761 CG PHE A 99 2186 2874 3028 -220 95 -488 C ATOM 762 CD1 PHE A 99 -17.363 -4.244 87.603 1.00 22.37 C ANISOU 762 CD1 PHE A 99 2290 3080 3132 -393 165 -614 C ATOM 763 CD2 PHE A 99 -19.433 -5.356 87.110 1.00 19.89 C ANISOU 763 CD2 PHE A 99 2171 2491 2897 -191 110 -409 C ATOM 764 CE1 PHE A 99 -17.804 -3.104 86.931 1.00 23.28 C ANISOU 764 CE1 PHE A 99 2567 3027 3252 -524 254 -649 C ATOM 765 CE2 PHE A 99 -19.879 -4.218 86.438 1.00 22.65 C ANISOU 765 CE2 PHE A 99 2655 2700 3250 -295 185 -448 C ATOM 766 CZ PHE A 99 -19.066 -3.104 86.335 1.00 19.77 C ANISOU 766 CZ PHE A 99 2294 2370 2846 -455 260 -560 C ATOM 767 N SER A 100 -16.222 -5.218 90.789 1.00 22.57 N ANISOU 767 N SER A 100 1975 3602 3000 -236 -46 -647 N ATOM 768 CA SER A 100 -15.653 -3.991 91.326 1.00 24.61 C ANISOU 768 CA SER A 100 2179 3974 3197 -426 -13 -789 C ATOM 769 C SER A 100 -14.269 -3.790 90.733 1.00 24.36 C ANISOU 769 C SER A 100 1980 4121 3155 -530 28 -914 C ATOM 770 O SER A 100 -13.498 -4.747 90.584 1.00 25.08 O ANISOU 770 O SER A 100 1914 4372 3241 -396 -23 -905 O ATOM 771 CB SER A 100 -15.556 -4.023 92.853 1.00 23.62 C ANISOU 771 CB SER A 100 1977 4019 2979 -386 -102 -808 C ATOM 772 OG SER A 100 -14.925 -2.839 93.310 1.00 29.12 O ANISOU 772 OG SER A 100 2620 4832 3611 -592 -68 -964 O ATOM 773 N THR A 101 -13.954 -2.538 90.408 1.00 26.99 N ANISOU 773 N THR A 101 2354 4427 3474 -769 126 -1034 N ATOM 774 CA THR A 101 -12.591 -2.194 90.018 1.00 29.72 C ANISOU 774 CA THR A 101 2520 4983 3791 -924 178 -1180 C ATOM 775 C THR A 101 -11.613 -2.239 91.189 1.00 29.64 C ANISOU 775 C THR A 101 2267 5307 3687 -941 91 -1291 C ATOM 776 O THR A 101 -10.413 -2.011 90.978 1.00 31.99 O ANISOU 776 O THR A 101 2442 5778 3934 -1021 130 -1386 O ATOM 777 CB THR A 101 -12.569 -0.808 89.373 1.00 36.72 C ANISOU 777 CB THR A 101 3557 5721 4673 -1203 321 -1275 C ATOM 778 OG1 THR A 101 -13.065 0.163 90.305 1.00 35.18 O ANISOU 778 OG1 THR A 101 3486 5458 4425 -1319 321 -1322 O ATOM 779 CG2 THR A 101 -13.422 -0.796 88.105 1.00 35.15 C ANISOU 779 CG2 THR A 101 3586 5221 4550 -1164 400 -1170 C ATOM 780 N ASP A 102 -12.087 -2.515 92.408 1.00 33.42 N ANISOU 780 N ASP A 102 2753 5828 4115 -821 -16 -1240 N ATOM 781 CA ASP A 102 -11.227 -2.654 93.588 1.00 33.39 C ANISOU 781 CA ASP A 102 2565 6121 4002 -781 -114 -1314 C ATOM 782 C ASP A 102 -11.767 -3.810 94.426 1.00 33.35 C ANISOU 782 C ASP A 102 2540 6160 3973 -507 -252 -1185 C ATOM 783 O ASP A 102 -12.705 -3.630 95.211 1.00 33.40 O ANISOU 783 O ASP A 102 2695 6042 3954 -483 -277 -1119 O ATOM 784 CB ASP A 102 -11.196 -1.359 94.394 1.00 32.84 C ANISOU 784 CB ASP A 102 2576 6046 3854 -995 -73 -1420 C ATOM 785 CG ASP A 102 -10.150 -1.383 95.506 1.00 36.44 C ANISOU 785 CG ASP A 102 2868 6789 4188 -966 -148 -1498 C ATOM 786 OD1 ASP A 102 -9.951 -0.336 96.153 1.00 43.12 O ANISOU 786 OD1 ASP A 102 3759 7660 4965 -1144 -109 -1597 O ATOM 787 OD2 ASP A 102 -9.545 -2.452 95.740 1.00 38.28 O ANISOU 787 OD2 ASP A 102 2944 7213 4389 -754 -243 -1458 O ATOM 788 N THR A 103 -11.187 -4.995 94.251 1.00 34.01 N ANISOU 788 N THR A 103 2495 6376 4051 -281 -322 -1128 N ATOM 789 CA THR A 103 -11.649 -6.192 94.940 1.00 32.00 C ANISOU 789 CA THR A 103 2282 6114 3762 -1 -436 -980 C ATOM 790 C THR A 103 -10.828 -6.515 96.190 1.00 31.24 C ANISOU 790 C THR A 103 2074 6269 3525 118 -543 -1009 C ATOM 791 O THR A 103 -10.962 -7.618 96.732 1.00 35.60 O ANISOU 791 O THR A 103 2661 6837 4028 370 -635 -890 O ATOM 792 CB THR A 103 -11.635 -7.390 93.991 1.00 30.80 C ANISOU 792 CB THR A 103 2157 5867 3679 207 -435 -869 C ATOM 793 OG1 THR A 103 -10.316 -7.553 93.443 1.00 38.59 O ANISOU 793 OG1 THR A 103 2970 7047 4646 225 -419 -962 O ATOM 794 CG2 THR A 103 -12.655 -7.194 92.854 1.00 28.28 C ANISOU 794 CG2 THR A 103 2052 5209 3485 120 -322 -790 C ATOM 795 N ARG A 104 -9.995 -5.588 96.660 1.00 31.73 N ANISOU 795 N ARG A 104 2042 6496 3516 -56 -518 -1155 N ATOM 796 CA ARG A 104 -9.304 -5.777 97.931 1.00 39.08 C ANISOU 796 CA ARG A 104 2886 7652 4310 41 -612 -1188 C ATOM 797 C ARG A 104 -10.320 -5.920 99.064 1.00 36.37 C ANISOU 797 C ARG A 104 2666 7246 3909 121 -689 -1097 C ATOM 798 O ARG A 104 -11.375 -5.284 99.045 1.00 37.51 O ANISOU 798 O ARG A 104 2931 7225 4096 -13 -649 -1087 O ATOM 799 CB ARG A 104 -8.378 -4.598 98.232 1.00 37.95 C ANISOU 799 CB ARG A 104 2635 7678 4105 -199 -559 -1370 C ATOM 800 CG ARG A 104 -7.115 -4.519 97.381 1.00 45.40 C ANISOU 800 CG ARG A 104 3424 8770 5055 -261 -497 -1475 C ATOM 801 CD ARG A 104 -6.332 -3.253 97.716 1.00 47.25 C ANISOU 801 CD ARG A 104 3580 9149 5223 -532 -431 -1653 C ATOM 802 NE ARG A 104 -7.184 -2.079 97.589 1.00 43.25 N ANISOU 802 NE ARG A 104 3244 8422 4767 -784 -336 -1681 N ATOM 803 CZ ARG A 104 -6.962 -0.905 98.163 1.00 41.88 C ANISOU 803 CZ ARG A 104 3095 8286 4533 -1014 -284 -1801 C ATOM 804 NH1 ARG A 104 -5.888 -0.717 98.923 1.00 44.89 N ANISOU 804 NH1 ARG A 104 3312 8942 4804 -1043 -321 -1915 N ATOM 805 NH2 ARG A 104 -7.824 0.088 97.980 1.00 41.97 N ANISOU 805 NH2 ARG A 104 3304 8052 4590 -1208 -194 -1809 N ATOM 806 N PRO A 105 -10.025 -6.733 100.077 1.00 36.49 N ANISOU 806 N PRO A 105 2664 7389 3811 338 -795 -1035 N ATOM 807 CA PRO A 105 -10.916 -6.787 101.249 1.00 39.89 C ANISOU 807 CA PRO A 105 3217 7780 4160 396 -858 -958 C ATOM 808 C PRO A 105 -11.095 -5.403 101.863 1.00 37.67 C ANISOU 808 C PRO A 105 2940 7535 3839 140 -821 -1091 C ATOM 809 O PRO A 105 -10.242 -4.524 101.726 1.00 40.29 O ANISOU 809 O PRO A 105 3163 7978 4166 -47 -769 -1245 O ATOM 810 CB PRO A 105 -10.185 -7.733 102.212 1.00 43.91 C ANISOU 810 CB PRO A 105 3685 8461 4537 642 -962 -909 C ATOM 811 CG PRO A 105 -9.216 -8.496 101.356 1.00 48.14 C ANISOU 811 CG PRO A 105 4120 9060 5110 776 -958 -912 C ATOM 812 CD PRO A 105 -8.817 -7.557 100.256 1.00 40.87 C ANISOU 812 CD PRO A 105 3093 8143 4291 533 -854 -1046 C ATOM 813 N MET A 106 -12.227 -5.213 102.545 1.00 31.98 N ANISOU 813 N MET A 106 2363 6708 3078 130 -839 -1031 N ATOM 814 CA MET A 106 -12.521 -3.915 103.155 1.00 36.53 C ANISOU 814 CA MET A 106 2988 7282 3609 -99 -797 -1154 C ATOM 815 C MET A 106 -11.430 -3.474 104.130 1.00 36.00 C ANISOU 815 C MET A 106 2802 7450 3428 -145 -835 -1275 C ATOM 816 O MET A 106 -11.071 -2.291 104.171 1.00 36.51 O ANISOU 816 O MET A 106 2846 7536 3491 -383 -768 -1424 O ATOM 817 CB MET A 106 -13.882 -3.965 103.856 1.00 30.86 C ANISOU 817 CB MET A 106 2444 6447 2833 -53 -819 -1062 C ATOM 818 CG MET A 106 -15.048 -4.178 102.888 1.00 31.55 C ANISOU 818 CG MET A 106 2714 6196 3076 -42 -706 -923 C ATOM 819 SD MET A 106 -16.649 -4.084 103.735 1.00 33.77 S ANISOU 819 SD MET A 106 3234 6275 3320 -9 -653 -803 S ATOM 820 CE MET A 106 -16.765 -2.320 104.045 1.00 36.89 C ANISOU 820 CE MET A 106 3681 6649 3684 -272 -578 -999 C ATOM 821 N VAL A 107 -10.891 -4.401 104.929 1.00 36.26 N ANISOU 821 N VAL A 107 2770 7648 3358 80 -939 -1213 N ATOM 822 CA VAL A 107 -9.896 -3.995 105.918 1.00 41.27 C ANISOU 822 CA VAL A 107 3284 8524 3875 45 -987 -1333 C ATOM 823 C VAL A 107 -8.611 -3.540 105.241 1.00 45.74 C ANISOU 823 C VAL A 107 3660 9239 4478 -85 -937 -1480 C ATOM 824 O VAL A 107 -7.841 -2.765 105.823 1.00 42.70 O ANISOU 824 O VAL A 107 3173 9030 4020 -227 -935 -1625 O ATOM 825 CB VAL A 107 -9.606 -5.117 106.939 1.00 45.47 C ANISOU 825 CB VAL A 107 3805 9195 4277 332 -1110 -1232 C ATOM 826 CG1 VAL A 107 -10.826 -5.385 107.808 1.00 41.58 C ANISOU 826 CG1 VAL A 107 3511 8576 3712 419 -1145 -1104 C ATOM 827 CG2 VAL A 107 -9.116 -6.390 106.253 1.00 44.13 C ANISOU 827 CG2 VAL A 107 3589 9034 4146 572 -1143 -1130 C ATOM 828 N GLU A 108 -8.351 -4.000 104.018 1.00 43.52 N ANISOU 828 N GLU A 108 3332 8901 4301 -47 -891 -1449 N ATOM 829 CA GLU A 108 -7.201 -3.478 103.292 1.00 42.72 C ANISOU 829 CA GLU A 108 3069 8934 4229 -201 -821 -1592 C ATOM 830 C GLU A 108 -7.508 -2.105 102.704 1.00 45.86 C ANISOU 830 C GLU A 108 3543 9181 4701 -530 -688 -1697 C ATOM 831 O GLU A 108 -6.663 -1.201 102.760 1.00 46.63 O ANISOU 831 O GLU A 108 3549 9408 4762 -737 -630 -1850 O ATOM 832 CB GLU A 108 -6.769 -4.466 102.210 1.00 40.90 C ANISOU 832 CB GLU A 108 2773 8701 4068 -35 -816 -1527 C ATOM 833 CG GLU A 108 -5.417 -4.158 101.587 1.00 66.21 C ANISOU 833 CG GLU A 108 5783 12108 7264 -138 -762 -1672 C ATOM 834 CD GLU A 108 -5.050 -5.107 100.454 1.00 66.54 C ANISOU 834 CD GLU A 108 5777 12131 7373 23 -749 -1611 C ATOM 835 OE1 GLU A 108 -5.593 -6.232 100.408 1.00 55.85 O ANISOU 835 OE1 GLU A 108 4515 10666 6041 278 -813 -1454 O ATOM 836 OE2 GLU A 108 -4.205 -4.727 99.613 1.00 67.82 O ANISOU 836 OE2 GLU A 108 5821 12388 7559 -109 -669 -1721 O ATOM 837 N LYS A 109 -8.720 -1.934 102.162 1.00 41.50 N ANISOU 837 N LYS A 109 3172 8353 4244 -579 -634 -1614 N ATOM 838 CA LYS A 109 -9.167 -0.629 101.683 1.00 40.87 C ANISOU 838 CA LYS A 109 3223 8084 4224 -865 -507 -1697 C ATOM 839 C LYS A 109 -9.092 0.438 102.768 1.00 42.45 C ANISOU 839 C LYS A 109 3464 8337 4326 -1034 -499 -1809 C ATOM 840 O LYS A 109 -8.595 1.547 102.536 1.00 44.01 O ANISOU 840 O LYS A 109 3676 8522 4524 -1283 -397 -1936 O ATOM 841 CB LYS A 109 -10.601 -0.738 101.178 1.00 34.17 C ANISOU 841 CB LYS A 109 2568 6950 3465 -838 -479 -1583 C ATOM 842 CG LYS A 109 -10.734 -1.531 99.907 1.00 34.07 C ANISOU 842 CG LYS A 109 2540 6838 3568 -737 -456 -1492 C ATOM 843 CD LYS A 109 -12.187 -1.599 99.457 1.00 30.56 C ANISOU 843 CD LYS A 109 2276 6129 3206 -721 -432 -1393 C ATOM 844 CE LYS A 109 -12.270 -2.376 98.165 1.00 35.70 C ANISOU 844 CE LYS A 109 2902 6686 3976 -628 -406 -1309 C ATOM 845 NZ LYS A 109 -13.650 -2.597 97.699 1.00 34.39 N ANISOU 845 NZ LYS A 109 2954 6211 3902 -556 -357 -1161 N ATOM 846 N TYR A 110 -9.626 0.135 103.950 1.00 40.00 N ANISOU 846 N TYR A 110 3199 8070 3929 -905 -597 -1759 N ATOM 847 CA TYR A 110 -9.682 1.097 105.041 1.00 39.97 C ANISOU 847 CA TYR A 110 3258 8100 3829 -1046 -597 -1857 C ATOM 848 C TYR A 110 -8.420 1.111 105.888 1.00 49.98 C ANISOU 848 C TYR A 110 4330 9677 4983 -1045 -665 -1962 C ATOM 849 O TYR A 110 -8.257 2.021 106.705 1.00 50.36 O ANISOU 849 O TYR A 110 4408 9773 4953 -1200 -655 -2071 O ATOM 850 CB TYR A 110 -10.899 0.810 105.929 1.00 39.36 C ANISOU 850 CB TYR A 110 3336 7925 3695 -913 -662 -1759 C ATOM 851 CG TYR A 110 -12.198 1.269 105.304 1.00 36.25 C ANISOU 851 CG TYR A 110 3161 7227 3384 -989 -573 -1714 C ATOM 852 CD1 TYR A 110 -13.003 0.391 104.584 1.00 35.74 C ANISOU 852 CD1 TYR A 110 3145 7039 3397 -839 -585 -1577 C ATOM 853 CD2 TYR A 110 -12.602 2.593 105.408 1.00 44.23 C ANISOU 853 CD2 TYR A 110 4342 8070 4393 -1203 -474 -1810 C ATOM 854 CE1 TYR A 110 -14.192 0.827 103.998 1.00 42.75 C ANISOU 854 CE1 TYR A 110 4226 7664 4353 -905 -502 -1549 C ATOM 855 CE2 TYR A 110 -13.774 3.033 104.832 1.00 39.07 C ANISOU 855 CE2 TYR A 110 3904 7135 3807 -1246 -387 -1774 C ATOM 856 CZ TYR A 110 -14.564 2.151 104.132 1.00 39.90 C ANISOU 856 CZ TYR A 110 4035 7141 3983 -1099 -402 -1650 C ATOM 857 OH TYR A 110 -15.725 2.613 103.560 1.00 40.13 O ANISOU 857 OH TYR A 110 4275 6901 4071 -1135 -313 -1627 O ATOM 858 N GLY A 111 -7.534 0.134 105.714 1.00 44.08 N ANISOU 858 N GLY A 111 3392 9137 4218 -868 -733 -1937 N ATOM 859 CA GLY A 111 -6.281 0.104 106.445 1.00 47.28 C ANISOU 859 CA GLY A 111 3594 9860 4509 -851 -798 -2046 C ATOM 860 C GLY A 111 -6.380 -0.320 107.891 1.00 53.09 C ANISOU 860 C GLY A 111 4326 10735 5109 -679 -932 -2013 C ATOM 861 O GLY A 111 -5.353 -0.330 108.581 1.00 51.68 O ANISOU 861 O GLY A 111 3977 10833 4824 -657 -996 -2110 O ATOM 862 N SER A 112 -7.571 -0.653 108.380 1.00 46.54 N ANISOU 862 N SER A 112 3679 9736 4269 -561 -971 -1884 N ATOM 863 CA SER A 112 -7.749 -1.137 109.745 1.00 51.30 C ANISOU 863 CA SER A 112 4311 10450 4731 -382 -1092 -1830 C ATOM 864 C SER A 112 -9.131 -1.774 109.856 1.00 46.49 C ANISOU 864 C SER A 112 3909 9620 4135 -226 -1109 -1650 C ATOM 865 O SER A 112 -9.940 -1.736 108.917 1.00 44.36 O ANISOU 865 O SER A 112 3747 9126 3983 -274 -1031 -1587 O ATOM 866 CB SER A 112 -7.554 -0.014 110.773 1.00 51.89 C ANISOU 866 CB SER A 112 4396 10613 4706 -578 -1094 -1976 C ATOM 867 OG SER A 112 -8.431 1.078 110.549 1.00 56.18 O ANISOU 867 OG SER A 112 5123 10914 5307 -807 -988 -2019 O ATOM 868 N GLU A 113 -9.381 -2.391 111.014 1.00 49.04 N ANISOU 868 N GLU A 113 4290 10017 4327 -34 -1209 -1567 N ATOM 869 CA GLU A 113 -10.694 -2.919 111.357 1.00 44.27 C ANISOU 869 CA GLU A 113 3895 9230 3695 95 -1218 -1404 C ATOM 870 C GLU A 113 -11.623 -1.856 111.923 1.00 49.34 C ANISOU 870 C GLU A 113 4697 9751 4299 -85 -1160 -1463 C ATOM 871 O GLU A 113 -12.786 -2.161 112.215 1.00 47.12 O ANISOU 871 O GLU A 113 4593 9326 3983 -4 -1146 -1344 O ATOM 872 CB GLU A 113 -10.567 -4.071 112.356 1.00 62.02 C ANISOU 872 CB GLU A 113 6171 11590 5805 379 -1333 -1276 C ATOM 873 CG GLU A 113 -9.991 -5.349 111.773 1.00 72.91 C ANISOU 873 CG GLU A 113 7478 13005 7219 618 -1379 -1168 C ATOM 874 CD GLU A 113 -10.506 -6.588 112.477 1.00 77.19 C ANISOU 874 CD GLU A 113 8181 13489 7658 895 -1446 -971 C ATOM 875 OE1 GLU A 113 -11.741 -6.711 112.641 1.00 68.59 O ANISOU 875 OE1 GLU A 113 7291 12210 6561 897 -1406 -853 O ATOM 876 OE2 GLU A 113 -9.674 -7.432 112.876 1.00 82.51 O ANISOU 876 OE2 GLU A 113 8793 14305 8251 1108 -1531 -937 O ATOM 877 N MET A 114 -11.145 -0.628 112.090 1.00 49.34 N ANISOU 877 N MET A 114 4652 9801 4295 -324 -1117 -1642 N ATOM 878 CA MET A 114 -11.992 0.479 112.508 1.00 44.68 C ANISOU 878 CA MET A 114 4237 9061 3679 -502 -1045 -1713 C ATOM 879 C MET A 114 -11.444 1.749 111.881 1.00 51.17 C ANISOU 879 C MET A 114 5022 9836 4583 -791 -949 -1886 C ATOM 880 O MET A 114 -10.244 2.023 111.974 1.00 55.51 O ANISOU 880 O MET A 114 5400 10579 5113 -878 -973 -2001 O ATOM 881 CB MET A 114 -12.040 0.610 114.033 1.00 50.42 C ANISOU 881 CB MET A 114 5019 9910 4229 -450 -1120 -1736 C ATOM 882 CG MET A 114 -12.689 1.897 114.510 1.00 56.85 C ANISOU 882 CG MET A 114 6004 10590 5007 -648 -1042 -1846 C ATOM 883 SD MET A 114 -13.568 1.689 116.064 1.00 64.37 S ANISOU 883 SD MET A 114 7131 11561 5768 -507 -1093 -1777 S ATOM 884 CE MET A 114 -14.685 0.366 115.619 1.00 47.66 C ANISOU 884 CE MET A 114 5110 9318 3680 -268 -1079 -1539 C ATOM 885 N ALA A 115 -12.325 2.516 111.245 1.00 49.48 N ANISOU 885 N ALA A 115 4981 9364 4455 -933 -832 -1902 N ATOM 886 CA ALA A 115 -11.933 3.711 110.509 1.00 49.46 C ANISOU 886 CA ALA A 115 5003 9250 4538 -1201 -718 -2037 C ATOM 887 C ALA A 115 -12.912 4.820 110.850 1.00 52.21 C ANISOU 887 C ALA A 115 5607 9366 4865 -1326 -631 -2089 C ATOM 888 O ALA A 115 -14.124 4.646 110.691 1.00 48.03 O ANISOU 888 O ALA A 115 5241 8652 4355 -1232 -594 -1998 O ATOM 889 CB ALA A 115 -11.912 3.448 109.000 1.00 42.75 C ANISOU 889 CB ALA A 115 4120 8278 3845 -1225 -643 -1988 C ATOM 890 N ASP A 116 -12.388 5.943 111.349 1.00 60.20 N ANISOU 890 N ASP A 116 6654 10393 5824 -1525 -597 -2237 N ATOM 891 CA ASP A 116 -13.208 7.094 111.739 1.00 60.69 C ANISOU 891 CA ASP A 116 6978 10228 5853 -1636 -514 -2300 C ATOM 892 C ASP A 116 -14.299 6.694 112.729 1.00 52.35 C ANISOU 892 C ASP A 116 6048 9150 4691 -1448 -562 -2222 C ATOM 893 O ASP A 116 -15.450 7.129 112.624 1.00 55.36 O ANISOU 893 O ASP A 116 6652 9298 5086 -1423 -478 -2194 O ATOM 894 CB ASP A 116 -13.822 7.780 110.516 1.00 57.47 C ANISOU 894 CB ASP A 116 6750 9507 5577 -1739 -370 -2288 C ATOM 895 CG ASP A 116 -12.792 8.135 109.469 1.00 62.90 C ANISOU 895 CG ASP A 116 7332 10206 6361 -1923 -303 -2346 C ATOM 896 OD1 ASP A 116 -12.767 7.469 108.412 1.00 63.08 O ANISOU 896 OD1 ASP A 116 7273 10204 6489 -1863 -286 -2263 O ATOM 897 OD2 ASP A 116 -12.011 9.083 109.696 1.00 67.38 O ANISOU 897 OD2 ASP A 116 7901 10809 6891 -2131 -262 -2476 O ATOM 898 N GLY A 117 -13.944 5.838 113.681 1.00 50.41 N ANISOU 898 N GLY A 117 5668 9154 4333 -1299 -689 -2181 N ATOM 899 CA GLY A 117 -14.880 5.445 114.711 1.00 55.73 C ANISOU 899 CA GLY A 117 6461 9831 4881 -1129 -727 -2104 C ATOM 900 C GLY A 117 -15.949 4.476 114.274 1.00 51.39 C ANISOU 900 C GLY A 117 5967 9189 4368 -936 -709 -1933 C ATOM 901 O GLY A 117 -16.860 4.191 115.056 1.00 51.02 O ANISOU 901 O GLY A 117 6041 9127 4219 -805 -709 -1860 O ATOM 902 N LEU A 118 -15.864 3.952 113.052 1.00 45.13 N ANISOU 902 N LEU A 118 5092 8343 3713 -917 -688 -1866 N ATOM 903 CA LEU A 118 -16.843 3.022 112.513 1.00 40.78 C ANISOU 903 CA LEU A 118 4585 7705 3203 -751 -669 -1708 C ATOM 904 C LEU A 118 -16.130 1.746 112.090 1.00 47.67 C ANISOU 904 C LEU A 118 5263 8735 4113 -611 -767 -1601 C ATOM 905 O LEU A 118 -15.119 1.803 111.381 1.00 46.89 O ANISOU 905 O LEU A 118 5014 8698 4103 -694 -779 -1659 O ATOM 906 CB LEU A 118 -17.579 3.642 111.323 1.00 43.54 C ANISOU 906 CB LEU A 118 5063 7792 3690 -848 -539 -1726 C ATOM 907 CG LEU A 118 -18.446 4.869 111.614 1.00 48.53 C ANISOU 907 CG LEU A 118 5927 8216 4295 -935 -426 -1809 C ATOM 908 CD1 LEU A 118 -18.995 5.431 110.316 1.00 41.11 C ANISOU 908 CD1 LEU A 118 5106 7014 3500 -1008 -305 -1818 C ATOM 909 CD2 LEU A 118 -19.584 4.497 112.550 1.00 48.14 C ANISOU 909 CD2 LEU A 118 5989 8180 4123 -770 -415 -1729 C ATOM 910 N SER A 119 -16.672 0.598 112.490 1.00 40.14 N ANISOU 910 N SER A 119 4328 7833 3089 -395 -821 -1439 N ATOM 911 CA SER A 119 -15.965 -0.654 112.255 1.00 43.09 C ANISOU 911 CA SER A 119 4553 8342 3478 -225 -920 -1326 C ATOM 912 C SER A 119 -16.048 -1.088 110.790 1.00 36.49 C ANISOU 912 C SER A 119 3667 7394 2802 -219 -883 -1268 C ATOM 913 O SER A 119 -16.980 -0.756 110.053 1.00 39.49 O ANISOU 913 O SER A 119 4156 7588 3259 -285 -792 -1258 O ATOM 914 CB SER A 119 -16.502 -1.757 113.165 1.00 51.58 C ANISOU 914 CB SER A 119 5708 9469 4421 5 -979 -1153 C ATOM 915 OG SER A 119 -17.859 -2.027 112.898 1.00 51.52 O ANISOU 915 OG SER A 119 5856 9299 4420 53 -897 -1037 O ATOM 916 N VAL A 120 -15.045 -1.859 110.383 1.00 40.75 N ANISOU 916 N VAL A 120 4044 8053 3387 -123 -955 -1233 N ATOM 917 CA VAL A 120 -14.887 -2.350 109.017 1.00 39.18 C ANISOU 917 CA VAL A 120 3773 7775 3336 -103 -932 -1184 C ATOM 918 C VAL A 120 -15.054 -3.865 109.043 1.00 36.24 C ANISOU 918 C VAL A 120 3414 7416 2939 168 -1003 -985 C ATOM 919 O VAL A 120 -14.320 -4.557 109.766 1.00 40.03 O ANISOU 919 O VAL A 120 3833 8046 3329 325 -1091 -944 O ATOM 920 CB VAL A 120 -13.508 -1.967 108.453 1.00 41.18 C ANISOU 920 CB VAL A 120 3837 8148 3663 -214 -930 -1315 C ATOM 921 CG1 VAL A 120 -13.362 -2.379 106.983 1.00 37.09 C ANISOU 921 CG1 VAL A 120 3257 7535 3300 -209 -887 -1275 C ATOM 922 CG2 VAL A 120 -13.242 -0.478 108.654 1.00 40.81 C ANISOU 922 CG2 VAL A 120 3806 8088 3611 -483 -858 -1501 C ATOM 923 N GLU A 121 -15.999 -4.375 108.253 1.00 34.34 N ANISOU 923 N GLU A 121 3274 6988 2785 221 -952 -858 N ATOM 924 CA GLU A 121 -16.246 -5.812 108.184 1.00 33.41 C ANISOU 924 CA GLU A 121 3221 6809 2666 459 -988 -651 C ATOM 925 C GLU A 121 -14.977 -6.556 107.775 1.00 42.01 C ANISOU 925 C GLU A 121 4152 8032 3777 591 -1071 -654 C ATOM 926 O GLU A 121 -14.217 -6.100 106.918 1.00 38.65 O ANISOU 926 O GLU A 121 3582 7645 3458 482 -1046 -771 O ATOM 927 CB GLU A 121 -17.389 -6.111 107.201 1.00 31.00 C ANISOU 927 CB GLU A 121 3059 6182 2539 439 -857 -517 C ATOM 928 CG GLU A 121 -18.744 -5.580 107.686 1.00 31.84 C ANISOU 928 CG GLU A 121 3334 6126 2637 355 -749 -480 C ATOM 929 CD GLU A 121 -19.914 -5.915 106.757 1.00 34.42 C ANISOU 929 CD GLU A 121 3777 6175 3125 343 -631 -355 C ATOM 930 OE1 GLU A 121 -21.069 -5.606 107.129 1.00 39.62 O ANISOU 930 OE1 GLU A 121 4553 6725 3775 300 -543 -316 O ATOM 931 OE2 GLU A 121 -19.685 -6.494 105.683 1.00 37.13 O ANISOU 931 OE2 GLU A 121 4088 6429 3593 381 -628 -302 O ATOM 932 N ASN A 122 -14.750 -7.711 108.406 1.00 37.62 N ANISOU 932 N ASN A 122 3654 7509 3131 823 -1138 -518 N ATOM 933 CA ASN A 122 -13.494 -8.449 108.289 1.00 41.44 C ANISOU 933 CA ASN A 122 4019 8111 3614 980 -1202 -524 C ATOM 934 C ASN A 122 -13.765 -9.900 107.887 1.00 36.14 C ANISOU 934 C ASN A 122 3483 7284 2965 1210 -1211 -328 C ATOM 935 O ASN A 122 -13.416 -10.843 108.597 1.00 43.04 O ANISOU 935 O ASN A 122 4431 8188 3735 1413 -1270 -236 O ATOM 936 CB ASN A 122 -12.729 -8.387 109.606 1.00 42.82 C ANISOU 936 CB ASN A 122 4141 8496 3632 1046 -1283 -583 C ATOM 937 CG ASN A 122 -11.297 -8.886 109.485 1.00 48.49 C ANISOU 937 CG ASN A 122 4691 9395 4337 1180 -1346 -641 C ATOM 938 OD1 ASN A 122 -10.749 -9.001 108.386 1.00 45.58 O ANISOU 938 OD1 ASN A 122 4213 9024 4083 1169 -1315 -682 O ATOM 939 ND2 ASN A 122 -10.686 -9.196 110.628 1.00 49.50 N ANISOU 939 ND2 ASN A 122 4802 9692 4315 1314 -1432 -648 N ATOM 940 N PHE A 123 -14.372 -10.076 106.712 1.00 36.97 N ANISOU 940 N PHE A 123 3631 7208 3207 1173 -1148 -269 N ATOM 941 CA PHE A 123 -14.738 -11.390 106.196 1.00 36.41 C ANISOU 941 CA PHE A 123 3715 6943 3174 1354 -1137 -88 C ATOM 942 C PHE A 123 -14.043 -11.699 104.880 1.00 39.69 C ANISOU 942 C PHE A 123 4022 7328 3729 1386 -1118 -126 C ATOM 943 O PHE A 123 -14.463 -12.616 104.163 1.00 41.88 O ANISOU 943 O PHE A 123 4431 7407 4075 1487 -1087 3 O ATOM 944 CB PHE A 123 -16.256 -11.495 106.018 1.00 39.20 C ANISOU 944 CB PHE A 123 4259 7083 3551 1299 -1068 48 C ATOM 945 CG PHE A 123 -17.019 -11.416 107.303 1.00 38.54 C ANISOU 945 CG PHE A 123 4322 6999 3321 1287 -1058 115 C ATOM 946 CD1 PHE A 123 -16.824 -12.359 108.300 1.00 44.85 C ANISOU 946 CD1 PHE A 123 5255 7804 3981 1462 -1104 226 C ATOM 947 CD2 PHE A 123 -17.928 -10.392 107.523 1.00 37.11 C ANISOU 947 CD2 PHE A 123 4169 6746 3183 1069 -959 57 C ATOM 948 CE1 PHE A 123 -17.526 -12.287 109.486 1.00 51.07 C ANISOU 948 CE1 PHE A 123 6183 8599 4623 1446 -1088 289 C ATOM 949 CE2 PHE A 123 -18.625 -10.311 108.708 1.00 41.73 C ANISOU 949 CE2 PHE A 123 4883 7347 3627 1061 -939 111 C ATOM 950 CZ PHE A 123 -18.420 -11.262 109.695 1.00 41.05 C ANISOU 950 CZ PHE A 123 4914 7338 3347 1260 -1019 233 C ATOM 951 N GLY A 124 -13.001 -10.944 104.540 1.00 35.43 N ANISOU 951 N GLY A 124 3260 6973 3227 1286 -1125 -303 N ATOM 952 CA GLY A 124 -12.304 -11.149 103.285 1.00 41.71 C ANISOU 952 CA GLY A 124 3946 7760 4142 1297 -1092 -352 C ATOM 953 C GLY A 124 -13.083 -10.751 102.053 1.00 40.36 C ANISOU 953 C GLY A 124 3797 7411 4128 1154 -1011 -346 C ATOM 954 O GLY A 124 -12.776 -11.231 100.959 1.00 40.41 O ANISOU 954 O GLY A 124 3781 7340 4233 1207 -978 -332 O ATOM 955 N LEU A 125 -14.101 -9.879 102.198 1.00 35.17 N ANISOU 955 N LEU A 125 3187 6686 3490 979 -975 -361 N ATOM 956 CA LEU A 125 -14.930 -9.437 101.083 1.00 30.39 C ANISOU 956 CA LEU A 125 2672 5814 3060 805 -841 -349 C ATOM 957 C LEU A 125 -14.649 -7.966 100.777 1.00 34.89 C ANISOU 957 C LEU A 125 3126 6451 3681 544 -780 -533 C ATOM 958 O LEU A 125 -14.233 -7.207 101.660 1.00 32.41 O ANISOU 958 O LEU A 125 2723 6329 3263 456 -823 -651 O ATOM 959 CB LEU A 125 -16.422 -9.623 101.388 1.00 30.69 C ANISOU 959 CB LEU A 125 2942 5599 3120 776 -771 -208 C ATOM 960 CG LEU A 125 -16.856 -10.994 101.917 1.00 38.37 C ANISOU 960 CG LEU A 125 4079 6484 4015 985 -812 -22 C ATOM 961 CD1 LEU A 125 -18.337 -10.977 102.326 1.00 33.78 C ANISOU 961 CD1 LEU A 125 3691 5702 3443 898 -727 85 C ATOM 962 CD2 LEU A 125 -16.569 -12.108 100.903 1.00 33.06 C ANISOU 962 CD2 LEU A 125 3448 5697 3417 1134 -816 62 C ATOM 963 N PRO A 126 -14.839 -7.529 99.530 1.00 31.38 N ANISOU 963 N PRO A 126 2696 5846 3382 410 -679 -565 N ATOM 964 CA PRO A 126 -14.487 -6.151 99.168 1.00 30.81 C ANISOU 964 CA PRO A 126 2546 5814 3345 159 -611 -738 C ATOM 965 C PRO A 126 -15.531 -5.111 99.546 1.00 28.61 C ANISOU 965 C PRO A 126 2423 5375 3074 -5 -535 -757 C ATOM 966 O PRO A 126 -15.276 -3.909 99.373 1.00 28.59 O ANISOU 966 O PRO A 126 2401 5382 3079 -215 -476 -901 O ATOM 967 CB PRO A 126 -14.328 -6.224 97.639 1.00 30.23 C ANISOU 967 CB PRO A 126 2464 5610 3411 114 -529 -740 C ATOM 968 CG PRO A 126 -14.803 -7.579 97.231 1.00 37.33 C ANISOU 968 CG PRO A 126 3460 6367 4356 330 -551 -567 C ATOM 969 CD PRO A 126 -15.402 -8.268 98.390 1.00 32.94 C ANISOU 969 CD PRO A 126 3005 5805 3706 477 -620 -447 C ATOM 970 N PHE A 127 -16.678 -5.531 100.063 1.00 26.94 N ANISOU 970 N PHE A 127 2369 5017 2849 85 -529 -622 N ATOM 971 CA PHE A 127 -17.759 -4.614 100.387 1.00 25.66 C ANISOU 971 CA PHE A 127 2350 4707 2692 -32 -453 -635 C ATOM 972 C PHE A 127 -18.722 -5.334 101.328 1.00 24.94 C ANISOU 972 C PHE A 127 2369 4574 2533 100 -476 -494 C ATOM 973 O PHE A 127 -18.546 -6.512 101.655 1.00 26.55 O ANISOU 973 O PHE A 127 2565 4833 2690 266 -545 -383 O ATOM 974 CB PHE A 127 -18.462 -4.078 99.125 1.00 22.98 C ANISOU 974 CB PHE A 127 2116 4122 2494 -131 -341 -629 C ATOM 975 CG PHE A 127 -18.640 -5.099 98.030 1.00 25.20 C ANISOU 975 CG PHE A 127 2413 4280 2883 -26 -332 -512 C ATOM 976 CD1 PHE A 127 -19.313 -6.297 98.268 1.00 28.91 C ANISOU 976 CD1 PHE A 127 2950 4686 3351 130 -363 -354 C ATOM 977 CD2 PHE A 127 -18.117 -4.868 96.764 1.00 22.24 C ANISOU 977 CD2 PHE A 127 2000 3850 2600 -97 -285 -565 C ATOM 978 CE1 PHE A 127 -19.469 -7.249 97.254 1.00 23.28 C ANISOU 978 CE1 PHE A 127 2270 3847 2729 213 -353 -258 C ATOM 979 CE2 PHE A 127 -18.270 -5.818 95.731 1.00 25.71 C ANISOU 979 CE2 PHE A 127 2463 4174 3130 2 -276 -466 C ATOM 980 CZ PHE A 127 -18.930 -7.006 95.984 1.00 28.12 C ANISOU 980 CZ PHE A 127 2838 4413 3434 157 -314 -318 C ATOM 981 N ASN A 128 -19.722 -4.589 101.783 1.00 22.65 N ANISOU 981 N ASN A 128 2191 4187 2226 25 -412 -504 N ATOM 982 CA ASN A 128 -20.726 -5.062 102.729 1.00 24.68 C ANISOU 982 CA ASN A 128 2550 4417 2409 110 -407 -392 C ATOM 983 C ASN A 128 -21.190 -6.475 102.395 1.00 23.74 C ANISOU 983 C ASN A 128 2485 4202 2333 245 -415 -215 C ATOM 984 O ASN A 128 -21.543 -6.772 101.247 1.00 27.44 O ANISOU 984 O ASN A 128 2979 4515 2932 238 -370 -167 O ATOM 985 CB ASN A 128 -21.897 -4.083 102.696 1.00 25.44 C ANISOU 985 CB ASN A 128 2755 4370 2541 17 -305 -424 C ATOM 986 CG ASN A 128 -22.891 -4.316 103.806 1.00 27.04 C ANISOU 986 CG ASN A 128 3041 4588 2646 74 -283 -348 C ATOM 987 OD1 ASN A 128 -23.585 -5.339 103.831 1.00 28.73 O ANISOU 987 OD1 ASN A 128 3302 4742 2871 156 -270 -202 O ATOM 988 ND2 ASN A 128 -22.977 -3.359 104.731 1.00 27.75 N ANISOU 988 ND2 ASN A 128 3159 4754 2631 16 -270 -451 N ATOM 989 N LEU A 129 -21.183 -7.346 103.411 1.00 25.55 N ANISOU 989 N LEU A 129 2751 4519 2438 364 -472 -119 N ATOM 990 CA LEU A 129 -21.421 -8.772 103.196 1.00 26.84 C ANISOU 990 CA LEU A 129 2993 4592 2613 494 -487 46 C ATOM 991 C LEU A 129 -22.817 -9.079 102.647 1.00 25.45 C ANISOU 991 C LEU A 129 2931 4205 2534 442 -385 145 C ATOM 992 O LEU A 129 -23.007 -10.149 102.053 1.00 25.60 O ANISOU 992 O LEU A 129 3016 4104 2607 503 -380 256 O ATOM 993 CB LEU A 129 -21.190 -9.541 104.505 1.00 28.69 C ANISOU 993 CB LEU A 129 3286 4950 2667 628 -558 130 C ATOM 994 CG LEU A 129 -22.151 -9.213 105.652 1.00 29.52 C ANISOU 994 CG LEU A 129 3483 5070 2663 580 -506 159 C ATOM 995 CD1 LEU A 129 -23.396 -10.120 105.639 1.00 28.93 C ANISOU 995 CD1 LEU A 129 3564 4822 2605 584 -420 323 C ATOM 996 CD2 LEU A 129 -21.427 -9.272 107.024 1.00 27.07 C ANISOU 996 CD2 LEU A 129 3163 4976 2145 676 -603 141 C ATOM 997 N MET A 130 -23.797 -8.193 102.850 1.00 24.77 N ANISOU 997 N MET A 130 2868 4080 2463 338 -306 102 N ATOM 998 CA MET A 130 -25.112 -8.437 102.254 1.00 24.97 C ANISOU 998 CA MET A 130 2962 3945 2581 290 -216 176 C ATOM 999 C MET A 130 -25.034 -8.511 100.738 1.00 24.16 C ANISOU 999 C MET A 130 2835 3710 2636 266 -204 164 C ATOM 1000 O MET A 130 -25.873 -9.158 100.105 1.00 23.63 O ANISOU 1000 O MET A 130 2820 3516 2642 253 -160 246 O ATOM 1001 CB MET A 130 -26.098 -7.351 102.671 1.00 22.20 C ANISOU 1001 CB MET A 130 2617 3603 2215 213 -138 108 C ATOM 1002 CG MET A 130 -26.375 -7.334 104.172 1.00 26.13 C ANISOU 1002 CG MET A 130 3156 4223 2550 233 -131 128 C ATOM 1003 SD MET A 130 -26.986 -8.910 104.857 1.00 29.78 S ANISOU 1003 SD MET A 130 3728 4664 2923 285 -110 321 S ATOM 1004 CE MET A 130 -28.624 -9.025 104.122 1.00 30.47 C ANISOU 1004 CE MET A 130 3827 4625 3125 192 11 367 C ATOM 1005 N LEU A 131 -24.040 -7.862 100.146 1.00 21.78 N ANISOU 1005 N LEU A 131 2454 3443 2379 246 -237 56 N ATOM 1006 CA LEU A 131 -23.948 -7.760 98.704 1.00 23.18 C ANISOU 1006 CA LEU A 131 2615 3500 2691 213 -215 31 C ATOM 1007 C LEU A 131 -23.243 -8.950 98.081 1.00 24.89 C ANISOU 1007 C LEU A 131 2827 3687 2941 303 -264 102 C ATOM 1008 O LEU A 131 -23.013 -8.946 96.871 1.00 23.30 O ANISOU 1008 O LEU A 131 2611 3401 2842 285 -249 78 O ATOM 1009 CB LEU A 131 -23.227 -6.468 98.323 1.00 23.24 C ANISOU 1009 CB LEU A 131 2561 3548 2722 127 -206 -119 C ATOM 1010 CG LEU A 131 -23.701 -5.192 99.038 1.00 23.08 C ANISOU 1010 CG LEU A 131 2569 3556 2643 50 -163 -211 C ATOM 1011 CD1 LEU A 131 -22.862 -3.992 98.591 1.00 27.52 C ANISOU 1011 CD1 LEU A 131 3104 4132 3221 -57 -147 -361 C ATOM 1012 CD2 LEU A 131 -25.171 -4.920 98.820 1.00 27.31 C ANISOU 1012 CD2 LEU A 131 3184 3971 3223 44 -90 -171 C ATOM 1013 N HIS A 132 -22.909 -9.964 98.872 1.00 23.73 N ANISOU 1013 N HIS A 132 2712 3602 2702 411 -318 188 N ATOM 1014 CA HIS A 132 -22.131 -11.113 98.426 1.00 24.96 C ANISOU 1014 CA HIS A 132 2882 3738 2862 536 -373 251 C ATOM 1015 C HIS A 132 -22.944 -12.371 98.691 1.00 27.23 C ANISOU 1015 C HIS A 132 3330 3898 3120 589 -355 407 C ATOM 1016 O HIS A 132 -23.311 -12.632 99.844 1.00 29.74 O ANISOU 1016 O HIS A 132 3715 4261 3323 611 -357 471 O ATOM 1017 CB HIS A 132 -20.797 -11.162 99.185 1.00 24.70 C ANISOU 1017 CB HIS A 132 2754 3914 2716 646 -467 202 C ATOM 1018 CG HIS A 132 -19.782 -12.095 98.600 1.00 26.18 C ANISOU 1018 CG HIS A 132 2915 4121 2910 798 -527 225 C ATOM 1019 ND1 HIS A 132 -19.765 -13.447 98.874 1.00 32.50 N ANISOU 1019 ND1 HIS A 132 3848 4856 3646 964 -565 359 N ATOM 1020 CD2 HIS A 132 -18.739 -11.867 97.766 1.00 28.31 C ANISOU 1020 CD2 HIS A 132 3050 4472 3233 817 -548 128 C ATOM 1021 CE1 HIS A 132 -18.754 -14.010 98.235 1.00 33.58 C ANISOU 1021 CE1 HIS A 132 3931 5032 3796 1102 -614 341 C ATOM 1022 NE2 HIS A 132 -18.120 -13.074 97.549 1.00 31.25 N ANISOU 1022 NE2 HIS A 132 3459 4839 3575 1012 -603 199 N ATOM 1023 N ASP A 133 -23.218 -13.155 97.643 1.00 28.50 N ANISOU 1023 N ASP A 133 3564 3894 3370 598 -332 464 N ATOM 1024 CA ASP A 133 -24.032 -14.362 97.781 1.00 24.54 C ANISOU 1024 CA ASP A 133 3236 3244 2844 609 -301 603 C ATOM 1025 C ASP A 133 -23.232 -15.657 97.626 1.00 31.02 C ANISOU 1025 C ASP A 133 4167 3999 3619 777 -355 684 C ATOM 1026 O ASP A 133 -23.826 -16.730 97.459 1.00 34.53 O ANISOU 1026 O ASP A 133 4788 4273 4058 774 -322 791 O ATOM 1027 CB ASP A 133 -25.201 -14.326 96.786 1.00 27.65 C ANISOU 1027 CB ASP A 133 3660 3487 3359 469 -225 607 C ATOM 1028 CG ASP A 133 -24.814 -14.769 95.368 1.00 31.00 C ANISOU 1028 CG ASP A 133 4098 3792 3887 498 -235 591 C ATOM 1029 OD1 ASP A 133 -23.620 -14.767 94.995 1.00 28.57 O ANISOU 1029 OD1 ASP A 133 3731 3540 3585 606 -287 543 O ATOM 1030 OD2 ASP A 133 -25.744 -15.099 94.597 1.00 30.39 O ANISOU 1030 OD2 ASP A 133 4082 3581 3885 405 -188 616 O ATOM 1031 N GLY A 134 -21.899 -15.596 97.683 1.00 30.85 N ANISOU 1031 N GLY A 134 4051 4114 3556 924 -435 628 N ATOM 1032 CA GLY A 134 -21.068 -16.752 97.439 1.00 34.11 C ANISOU 1032 CA GLY A 134 4554 4480 3924 1123 -491 689 C ATOM 1033 C GLY A 134 -20.385 -16.773 96.085 1.00 30.45 C ANISOU 1033 C GLY A 134 4010 3989 3570 1163 -496 614 C ATOM 1034 O GLY A 134 -19.341 -17.433 95.947 1.00 35.01 O ANISOU 1034 O GLY A 134 4585 4618 4100 1364 -559 617 O ATOM 1035 N THR A 135 -20.946 -16.090 95.084 1.00 28.08 N ANISOU 1035 N THR A 135 3650 3614 3403 996 -432 550 N ATOM 1036 CA THR A 135 -20.305 -16.004 93.779 1.00 26.64 C ANISOU 1036 CA THR A 135 3393 3414 3316 1017 -426 473 C ATOM 1037 C THR A 135 -19.049 -15.139 93.849 1.00 31.11 C ANISOU 1037 C THR A 135 3738 4220 3864 1056 -467 344 C ATOM 1038 O THR A 135 -18.989 -14.165 94.602 1.00 29.19 O ANISOU 1038 O THR A 135 3385 4124 3584 971 -476 280 O ATOM 1039 CB THR A 135 -21.281 -15.415 92.764 1.00 28.89 C ANISOU 1039 CB THR A 135 3683 3568 3726 830 -351 440 C ATOM 1040 OG1 THR A 135 -22.550 -16.080 92.881 1.00 32.66 O ANISOU 1040 OG1 THR A 135 4326 3873 4209 755 -312 542 O ATOM 1041 CG2 THR A 135 -20.751 -15.550 91.343 1.00 27.51 C ANISOU 1041 CG2 THR A 135 3485 3331 3636 857 -335 385 C ATOM 1042 N ASP A 136 -18.035 -15.505 93.054 1.00 28.77 N ANISOU 1042 N ASP A 136 3375 3969 3587 1175 -487 296 N ATOM 1043 CA ASP A 136 -16.868 -14.643 92.861 1.00 30.55 C ANISOU 1043 CA ASP A 136 3368 4427 3812 1164 -503 152 C ATOM 1044 C ASP A 136 -17.301 -13.212 92.553 1.00 27.35 C ANISOU 1044 C ASP A 136 2883 4028 3481 919 -435 58 C ATOM 1045 O ASP A 136 -18.278 -12.983 91.826 1.00 28.07 O ANISOU 1045 O ASP A 136 3075 3930 3660 798 -369 84 O ATOM 1046 CB ASP A 136 -16.004 -15.133 91.686 1.00 33.41 C ANISOU 1046 CB ASP A 136 3680 4795 4219 1273 -492 107 C ATOM 1047 CG ASP A 136 -15.126 -16.324 92.024 1.00 41.30 C ANISOU 1047 CG ASP A 136 4697 5874 5121 1561 -572 152 C ATOM 1048 OD1 ASP A 136 -15.257 -16.901 93.121 1.00 43.80 O ANISOU 1048 OD1 ASP A 136 5112 6195 5336 1665 -629 238 O ATOM 1049 OD2 ASP A 136 -14.297 -16.692 91.154 1.00 43.02 O ANISOU 1049 OD2 ASP A 136 4855 6129 5361 1651 -557 98 O ATOM 1050 N VAL A 137 -16.553 -12.245 93.092 1.00 25.52 N ANISOU 1050 N VAL A 137 2476 4016 3202 852 -453 -58 N ATOM 1051 CA VAL A 137 -16.643 -10.852 92.664 1.00 23.91 C ANISOU 1051 CA VAL A 137 2204 3825 3057 631 -382 -171 C ATOM 1052 C VAL A 137 -15.697 -10.652 91.484 1.00 22.11 C ANISOU 1052 C VAL A 137 1864 3655 2881 605 -339 -268 C ATOM 1053 O VAL A 137 -14.483 -10.863 91.608 1.00 25.55 O ANISOU 1053 O VAL A 137 2133 4312 3263 693 -382 -340 O ATOM 1054 CB VAL A 137 -16.305 -9.880 93.808 1.00 25.42 C ANISOU 1054 CB VAL A 137 2287 4209 3164 539 -411 -262 C ATOM 1055 CG1 VAL A 137 -16.510 -8.445 93.349 1.00 23.57 C ANISOU 1055 CG1 VAL A 137 2042 3932 2982 307 -325 -371 C ATOM 1056 CG2 VAL A 137 -17.171 -10.173 95.042 1.00 29.80 C ANISOU 1056 CG2 VAL A 137 2950 4727 3646 588 -452 -164 C ATOM 1057 N PHE A 138 -16.244 -10.227 90.344 1.00 22.25 N ANISOU 1057 N PHE A 138 1968 3495 2993 486 -254 -274 N ATOM 1058 CA PHE A 138 -15.454 -10.068 89.135 1.00 23.41 C ANISOU 1058 CA PHE A 138 2040 3671 3185 451 -196 -354 C ATOM 1059 C PHE A 138 -14.782 -8.701 89.106 1.00 23.58 C ANISOU 1059 C PHE A 138 1937 3831 3191 248 -138 -501 C ATOM 1060 O PHE A 138 -15.065 -7.822 89.921 1.00 24.06 O ANISOU 1060 O PHE A 138 2001 3923 3217 128 -139 -541 O ATOM 1061 CB PHE A 138 -16.354 -10.336 87.926 1.00 20.60 C ANISOU 1061 CB PHE A 138 1855 3057 2916 432 -138 -285 C ATOM 1062 CG PHE A 138 -16.983 -11.690 88.010 1.00 21.20 C ANISOU 1062 CG PHE A 138 2060 2998 2996 598 -190 -154 C ATOM 1063 CD1 PHE A 138 -18.281 -11.843 88.462 1.00 22.04 C ANISOU 1063 CD1 PHE A 138 2308 2952 3116 568 -202 -59 C ATOM 1064 CD2 PHE A 138 -16.225 -12.824 87.731 1.00 21.68 C ANISOU 1064 CD2 PHE A 138 2101 3101 3036 786 -225 -132 C ATOM 1065 CE1 PHE A 138 -18.826 -13.117 88.604 1.00 21.40 C ANISOU 1065 CE1 PHE A 138 2357 2748 3027 690 -239 57 C ATOM 1066 CE2 PHE A 138 -16.768 -14.105 87.881 1.00 24.34 C ANISOU 1066 CE2 PHE A 138 2595 3292 3361 934 -268 -11 C ATOM 1067 CZ PHE A 138 -18.075 -14.235 88.320 1.00 22.58 C ANISOU 1067 CZ PHE A 138 2521 2905 3151 866 -271 83 C ATOM 1068 N AASP A 139 -13.855 -8.539 88.162 0.66 22.28 N ANISOU 1068 N AASP A 139 1671 3752 3045 203 -78 -590 N ATOM 1069 N BASP A 139 -13.861 -8.526 88.161 0.34 22.76 N ANISOU 1069 N BASP A 139 1731 3810 3105 200 -77 -590 N ATOM 1070 CA AASP A 139 -13.046 -7.329 88.099 0.66 26.02 C ANISOU 1070 CA AASP A 139 2018 4377 3491 -12 -10 -743 C ATOM 1071 CA BASP A 139 -13.052 -7.318 88.131 0.34 26.24 C ANISOU 1071 CA BASP A 139 2045 4407 3518 -13 -12 -743 C ATOM 1072 C AASP A 139 -13.671 -6.224 87.259 0.66 20.39 C ANISOU 1072 C AASP A 139 1467 3452 2827 -223 104 -765 C ATOM 1073 C BASP A 139 -13.512 -6.308 87.085 0.34 27.01 C ANISOU 1073 C BASP A 139 2288 4306 3669 -216 112 -772 C ATOM 1074 O AASP A 139 -13.269 -5.064 87.384 0.66 25.41 O ANISOU 1074 O AASP A 139 2072 4152 3432 -434 168 -878 O ATOM 1075 O BASP A 139 -12.841 -5.286 86.905 0.34 21.50 O ANISOU 1075 O BASP A 139 1525 3699 2945 -421 191 -898 O ATOM 1076 CB AASP A 139 -11.661 -7.652 87.527 0.66 31.36 C ANISOU 1076 CB AASP A 139 2483 5286 4147 24 13 -842 C ATOM 1077 CB BASP A 139 -11.570 -7.674 87.925 0.34 30.81 C ANISOU 1077 CB BASP A 139 2377 5275 4056 41 -17 -849 C ATOM 1078 CG AASP A 139 -10.885 -8.614 88.391 0.66 31.28 C ANISOU 1078 CG AASP A 139 2291 5528 4065 250 -106 -843 C ATOM 1079 CG BASP A 139 -11.212 -7.948 86.470 0.34 31.26 C ANISOU 1079 CG BASP A 139 2442 5270 4164 46 74 -863 C ATOM 1080 OD1AASP A 139 -11.035 -8.561 89.633 0.66 34.19 O ANISOU 1080 OD1AASP A 139 2634 5984 4372 284 -194 -830 O ATOM 1081 OD1BASP A 139 -12.091 -8.334 85.674 0.34 30.30 O ANISOU 1081 OD1BASP A 139 2519 4888 4107 98 101 -760 O ATOM 1082 OD2AASP A 139 -10.118 -9.423 87.826 0.66 38.07 O ANISOU 1082 OD2AASP A 139 3043 6502 4920 410 -112 -858 O ATOM 1083 OD2BASP A 139 -10.022 -7.783 86.124 0.34 39.56 O ANISOU 1083 OD2BASP A 139 3289 6558 5185 -5 119 -987 O ATOM 1084 N SER A 140 -14.638 -6.556 86.407 1.00 22.22 N ANISOU 1084 N SER A 140 1885 3435 3124 -168 130 -662 N ATOM 1085 CA SER A 140 -15.113 -5.651 85.364 1.00 23.59 C ANISOU 1085 CA SER A 140 2216 3415 3331 -320 235 -679 C ATOM 1086 C SER A 140 -16.445 -6.183 84.880 1.00 21.39 C ANISOU 1086 C SER A 140 2125 2895 3107 -212 209 -549 C ATOM 1087 O SER A 140 -16.772 -7.343 85.120 1.00 19.06 O ANISOU 1087 O SER A 140 1825 2589 2829 -45 133 -460 O ATOM 1088 CB SER A 140 -14.156 -5.582 84.164 1.00 23.39 C ANISOU 1088 CB SER A 140 2132 3442 3311 -388 329 -752 C ATOM 1089 OG SER A 140 -13.973 -6.875 83.590 1.00 21.76 O ANISOU 1089 OG SER A 140 1890 3245 3133 -194 292 -692 O ATOM 1090 N PHE A 141 -17.198 -5.335 84.168 1.00 18.61 N ANISOU 1090 N PHE A 141 1945 2354 2772 -310 275 -542 N ATOM 1091 CA PHE A 141 -18.367 -5.848 83.464 1.00 20.21 C ANISOU 1091 CA PHE A 141 2299 2359 3021 -214 253 -439 C ATOM 1092 C PHE A 141 -17.979 -6.993 82.533 1.00 20.14 C ANISOU 1092 C PHE A 141 2267 2344 3043 -104 247 -407 C ATOM 1093 O PHE A 141 -18.676 -8.015 82.469 1.00 18.59 O ANISOU 1093 O PHE A 141 2120 2067 2875 21 185 -318 O ATOM 1094 CB PHE A 141 -19.063 -4.749 82.649 1.00 19.38 C ANISOU 1094 CB PHE A 141 2379 2073 2912 -310 325 -448 C ATOM 1095 CG PHE A 141 -20.295 -5.256 81.947 1.00 19.39 C ANISOU 1095 CG PHE A 141 2510 1909 2950 -207 287 -356 C ATOM 1096 CD1 PHE A 141 -21.493 -5.319 82.638 1.00 20.95 C ANISOU 1096 CD1 PHE A 141 2745 2058 3156 -148 225 -295 C ATOM 1097 CD2 PHE A 141 -20.228 -5.783 80.663 1.00 22.27 C ANISOU 1097 CD2 PHE A 141 2933 2195 3334 -168 309 -336 C ATOM 1098 CE1 PHE A 141 -22.637 -5.857 82.020 1.00 21.42 C ANISOU 1098 CE1 PHE A 141 2890 2004 3246 -66 184 -222 C ATOM 1099 CE2 PHE A 141 -21.352 -6.313 80.041 1.00 22.52 C ANISOU 1099 CE2 PHE A 141 3067 2098 3391 -82 262 -263 C ATOM 1100 CZ PHE A 141 -22.552 -6.357 80.719 1.00 22.38 C ANISOU 1100 CZ PHE A 141 3072 2046 3384 -37 198 -209 C ATOM 1101 N GLU A 142 -16.906 -6.803 81.750 1.00 18.55 N ANISOU 1101 N GLU A 142 2005 2216 2826 -164 323 -484 N ATOM 1102 CA GLU A 142 -16.406 -7.846 80.849 1.00 21.11 C ANISOU 1102 CA GLU A 142 2301 2552 3167 -51 329 -471 C ATOM 1103 C GLU A 142 -16.286 -9.187 81.561 1.00 21.94 C ANISOU 1103 C GLU A 142 2325 2733 3279 138 230 -413 C ATOM 1104 O GLU A 142 -16.728 -10.220 81.043 1.00 20.61 O ANISOU 1104 O GLU A 142 2245 2451 3136 263 196 -343 O ATOM 1105 CB GLU A 142 -15.050 -7.431 80.266 1.00 21.58 C ANISOU 1105 CB GLU A 142 2241 2765 3195 -145 427 -584 C ATOM 1106 CG GLU A 142 -15.147 -6.455 79.094 1.00 21.47 C ANISOU 1106 CG GLU A 142 2373 2619 3167 -302 546 -618 C ATOM 1107 CD GLU A 142 -15.311 -4.982 79.488 1.00 29.19 C ANISOU 1107 CD GLU A 142 3424 3555 4111 -503 605 -668 C ATOM 1108 OE1 GLU A 142 -15.294 -4.133 78.552 1.00 30.37 O ANISOU 1108 OE1 GLU A 142 3719 3590 4231 -635 713 -697 O ATOM 1109 OE2 GLU A 142 -15.446 -4.673 80.699 1.00 27.99 O ANISOU 1109 OE2 GLU A 142 3209 3474 3952 -526 550 -679 O ATOM 1110 N ALA A 143 -15.696 -9.193 82.758 1.00 20.81 N ANISOU 1110 N ALA A 143 2031 2775 3100 162 181 -444 N ATOM 1111 CA ALA A 143 -15.475 -10.468 83.430 1.00 19.31 C ANISOU 1111 CA ALA A 143 1786 2657 2894 364 89 -386 C ATOM 1112 C ALA A 143 -16.782 -11.067 83.928 1.00 17.73 C ANISOU 1112 C ALA A 143 1739 2283 2715 426 23 -263 C ATOM 1113 O ALA A 143 -16.962 -12.295 83.880 1.00 20.55 O ANISOU 1113 O ALA A 143 2165 2568 3074 579 -25 -187 O ATOM 1114 CB ALA A 143 -14.486 -10.288 84.591 1.00 21.10 C ANISOU 1114 CB ALA A 143 1810 3149 3058 384 45 -454 C ATOM 1115 N ALA A 144 -17.687 -10.224 84.435 1.00 15.89 N ANISOU 1115 N ALA A 144 1565 1984 2489 307 25 -247 N ATOM 1116 CA ALA A 144 -18.971 -10.716 84.919 1.00 19.57 C ANISOU 1116 CA ALA A 144 2151 2315 2970 343 -25 -143 C ATOM 1117 C ALA A 144 -19.798 -11.262 83.768 1.00 19.14 C ANISOU 1117 C ALA A 144 2241 2067 2966 357 -10 -90 C ATOM 1118 O ALA A 144 -20.421 -12.326 83.890 1.00 17.82 O ANISOU 1118 O ALA A 144 2160 1806 2806 434 -54 -7 O ATOM 1119 CB ALA A 144 -19.728 -9.598 85.648 1.00 17.50 C ANISOU 1119 CB ALA A 144 1905 2048 2697 223 -15 -155 C ATOM 1120 N PHE A 145 -19.747 -10.586 82.622 1.00 17.53 N ANISOU 1120 N PHE A 145 2075 1803 2784 279 53 -142 N ATOM 1121 CA PHE A 145 -20.541 -11.032 81.486 1.00 20.28 C ANISOU 1121 CA PHE A 145 2558 1982 3167 290 58 -103 C ATOM 1122 C PHE A 145 -19.963 -12.309 80.903 1.00 21.57 C ANISOU 1122 C PHE A 145 2744 2120 3333 412 46 -86 C ATOM 1123 O PHE A 145 -20.704 -13.223 80.516 1.00 18.30 O ANISOU 1123 O PHE A 145 2444 1572 2936 456 14 -28 O ATOM 1124 CB PHE A 145 -20.620 -9.934 80.420 1.00 18.41 C ANISOU 1124 CB PHE A 145 2379 1684 2931 189 128 -158 C ATOM 1125 CG PHE A 145 -21.408 -10.349 79.212 1.00 21.13 C ANISOU 1125 CG PHE A 145 2858 1874 3294 208 123 -127 C ATOM 1126 CD1 PHE A 145 -22.742 -10.694 79.342 1.00 21.14 C ANISOU 1126 CD1 PHE A 145 2931 1787 3315 215 66 -66 C ATOM 1127 CD2 PHE A 145 -20.800 -10.455 77.977 1.00 20.81 C ANISOU 1127 CD2 PHE A 145 2861 1799 3245 216 176 -165 C ATOM 1128 CE1 PHE A 145 -23.481 -11.125 78.225 1.00 20.70 C ANISOU 1128 CE1 PHE A 145 2985 1703 3177 211 34 -46 C ATOM 1129 CE2 PHE A 145 -21.531 -10.897 76.851 1.00 23.64 C ANISOU 1129 CE2 PHE A 145 3347 2044 3591 235 153 -139 C ATOM 1130 CZ PHE A 145 -22.864 -11.227 76.990 1.00 21.30 C ANISOU 1130 CZ PHE A 145 3107 1753 3232 223 55 -81 C ATOM 1131 N ALA A 146 -18.638 -12.407 80.846 1.00 19.16 N ANISOU 1131 N ALA A 146 2250 1856 3172 22 -84 -177 N ATOM 1132 CA ALA A 146 -18.039 -13.643 80.365 1.00 23.04 C ANISOU 1132 CA ALA A 146 2777 2402 3577 173 -147 -123 C ATOM 1133 C ALA A 146 -18.433 -14.818 81.256 1.00 18.61 C ANISOU 1133 C ALA A 146 2299 1791 2980 181 -184 -122 C ATOM 1134 O ALA A 146 -18.680 -15.921 80.764 1.00 19.41 O ANISOU 1134 O ALA A 146 2486 1797 3091 283 -199 -121 O ATOM 1135 CB ALA A 146 -16.526 -13.475 80.282 1.00 21.50 C ANISOU 1135 CB ALA A 146 2452 2349 3370 227 -142 -20 C ATOM 1136 N TYR A 147 -18.521 -14.594 82.580 1.00 17.57 N ANISOU 1136 N TYR A 147 2175 1705 2796 67 -179 -126 N ATOM 1137 CA TYR A 147 -19.022 -15.649 83.453 1.00 17.89 C ANISOU 1137 CA TYR A 147 2287 1700 2810 93 -172 -69 C ATOM 1138 C TYR A 147 -20.476 -16.013 83.121 1.00 18.99 C ANISOU 1138 C TYR A 147 2473 1628 3115 95 -121 -91 C ATOM 1139 O TYR A 147 -20.823 -17.197 83.059 1.00 18.80 O ANISOU 1139 O TYR A 147 2480 1489 3174 161 -141 -37 O ATOM 1140 CB TYR A 147 -18.864 -15.213 84.907 1.00 19.50 C ANISOU 1140 CB TYR A 147 2545 2027 2837 -35 -162 -67 C ATOM 1141 CG TYR A 147 -19.137 -16.275 85.942 1.00 18.21 C ANISOU 1141 CG TYR A 147 2444 1885 2589 15 -139 68 C ATOM 1142 CD1 TYR A 147 -18.105 -17.048 86.449 1.00 22.88 C ANISOU 1142 CD1 TYR A 147 2964 2661 3069 76 -251 256 C ATOM 1143 CD2 TYR A 147 -20.420 -16.465 86.454 1.00 20.26 C ANISOU 1143 CD2 TYR A 147 2795 1986 2917 16 21 77 C ATOM 1144 CE1 TYR A 147 -18.338 -18.005 87.440 1.00 24.11 C ANISOU 1144 CE1 TYR A 147 3159 2854 3148 139 -213 446 C ATOM 1145 CE2 TYR A 147 -20.672 -17.423 87.422 1.00 25.87 C ANISOU 1145 CE2 TYR A 147 3551 2712 3566 80 84 250 C ATOM 1146 CZ TYR A 147 -19.623 -18.187 87.912 1.00 28.59 C ANISOU 1146 CZ TYR A 147 3845 3254 3763 143 -38 431 C ATOM 1147 OH TYR A 147 -19.862 -19.139 88.883 1.00 34.32 O ANISOU 1147 OH TYR A 147 4599 4010 4433 227 41 666 O ATOM 1148 N PHE A 148 -21.337 -15.012 82.908 1.00 20.72 N ANISOU 1148 N PHE A 148 2664 1768 3439 15 -53 -133 N ATOM 1149 CA PHE A 148 -22.702 -15.287 82.458 1.00 20.50 C ANISOU 1149 CA PHE A 148 2590 1562 3637 -1 -54 -73 C ATOM 1150 C PHE A 148 -22.723 -16.123 81.179 1.00 19.08 C ANISOU 1150 C PHE A 148 2434 1338 3479 32 -243 -99 C ATOM 1151 O PHE A 148 -23.484 -17.088 81.072 1.00 20.81 O ANISOU 1151 O PHE A 148 2660 1469 3779 0 -307 -65 O ATOM 1152 CB PHE A 148 -23.449 -13.970 82.238 1.00 17.62 C ANISOU 1152 CB PHE A 148 2130 1159 3404 -57 60 -37 C ATOM 1153 CG PHE A 148 -24.886 -14.179 81.812 1.00 21.69 C ANISOU 1153 CG PHE A 148 2508 1639 4092 -77 28 108 C ATOM 1154 CD1 PHE A 148 -25.211 -14.354 80.473 1.00 25.04 C ANISOU 1154 CD1 PHE A 148 2859 2060 4596 -106 -195 152 C ATOM 1155 CD2 PHE A 148 -25.893 -14.249 82.759 1.00 22.38 C ANISOU 1155 CD2 PHE A 148 2536 1672 4295 -73 203 213 C ATOM 1156 CE1 PHE A 148 -26.513 -14.564 80.102 1.00 24.39 C ANISOU 1156 CE1 PHE A 148 2607 1929 4730 -163 -295 312 C ATOM 1157 CE2 PHE A 148 -27.203 -14.454 82.388 1.00 26.90 C ANISOU 1157 CE2 PHE A 148 2906 2210 5105 -87 160 378 C ATOM 1158 CZ PHE A 148 -27.511 -14.610 81.060 1.00 29.00 C ANISOU 1158 CZ PHE A 148 3062 2481 5474 -145 -114 435 C ATOM 1159 N VAL A 149 -21.922 -15.745 80.179 1.00 20.07 N ANISOU 1159 N VAL A 149 2590 1572 3464 82 -302 -161 N ATOM 1160 CA VAL A 149 -21.890 -16.509 78.924 1.00 20.62 C ANISOU 1160 CA VAL A 149 2786 1599 3450 117 -442 -233 C ATOM 1161 C VAL A 149 -21.520 -17.968 79.172 1.00 18.76 C ANISOU 1161 C VAL A 149 2686 1237 3206 186 -429 -290 C ATOM 1162 O VAL A 149 -22.089 -18.888 78.568 1.00 22.61 O ANISOU 1162 O VAL A 149 3306 1552 3731 133 -543 -378 O ATOM 1163 CB VAL A 149 -20.929 -15.845 77.923 1.00 20.15 C ANISOU 1163 CB VAL A 149 2762 1690 3203 213 -410 -253 C ATOM 1164 CG1 VAL A 149 -20.601 -16.789 76.752 1.00 22.28 C ANISOU 1164 CG1 VAL A 149 3276 1911 3279 297 -463 -369 C ATOM 1165 CG2 VAL A 149 -21.531 -14.524 77.408 1.00 21.89 C ANISOU 1165 CG2 VAL A 149 2847 1984 3487 146 -433 -155 C ATOM 1166 N GLU A 150 -20.545 -18.210 80.053 1.00 20.95 N ANISOU 1166 N GLU A 150 2927 1583 3448 289 -300 -224 N ATOM 1167 CA GLU A 150 -20.078 -19.571 80.275 1.00 20.26 C ANISOU 1167 CA GLU A 150 2928 1364 3405 402 -231 -203 C ATOM 1168 C GLU A 150 -21.120 -20.418 80.989 1.00 21.82 C ANISOU 1168 C GLU A 150 3115 1396 3782 316 -239 -149 C ATOM 1169 O GLU A 150 -21.270 -21.603 80.680 1.00 22.78 O ANISOU 1169 O GLU A 150 3349 1355 3950 328 -202 -185 O ATOM 1170 CB GLU A 150 -18.776 -19.540 81.076 1.00 19.81 C ANISOU 1170 CB GLU A 150 2754 1483 3291 527 -127 -39 C ATOM 1171 CG GLU A 150 -18.300 -20.898 81.579 1.00 21.53 C ANISOU 1171 CG GLU A 150 2981 1579 3621 672 -16 103 C ATOM 1172 CD GLU A 150 -17.837 -21.827 80.475 1.00 22.94 C ANISOU 1172 CD GLU A 150 3337 1534 3845 833 120 14 C ATOM 1173 OE1 GLU A 150 -17.671 -23.041 80.737 1.00 29.05 O ANISOU 1173 OE1 GLU A 150 4146 2163 4730 917 225 89 O ATOM 1174 OE2 GLU A 150 -17.622 -21.354 79.332 1.00 29.10 O ANISOU 1174 OE2 GLU A 150 4239 2332 4486 857 129 -136 O ATOM 1175 N HIS A 151 -21.869 -19.826 81.926 1.00 21.49 N ANISOU 1175 N HIS A 151 2947 1410 3808 224 -227 -51 N ATOM 1176 CA HIS A 151 -22.677 -20.607 82.854 1.00 23.32 C ANISOU 1176 CA HIS A 151 3132 1559 4170 191 -152 79 C ATOM 1177 C HIS A 151 -24.183 -20.447 82.702 1.00 21.31 C ANISOU 1177 C HIS A 151 2781 1267 4049 46 -194 103 C ATOM 1178 O HIS A 151 -24.925 -21.311 83.179 1.00 27.99 O ANISOU 1178 O HIS A 151 3572 2013 5050 19 -151 201 O ATOM 1179 CB HIS A 151 -22.307 -20.241 84.297 1.00 24.19 C ANISOU 1179 CB HIS A 151 3191 1752 4249 253 -28 244 C ATOM 1180 CG HIS A 151 -20.916 -20.638 84.665 1.00 22.48 C ANISOU 1180 CG HIS A 151 2979 1704 3858 381 -15 333 C ATOM 1181 ND1 HIS A 151 -20.534 -21.956 84.805 1.00 27.79 N ANISOU 1181 ND1 HIS A 151 3648 2250 4662 514 50 478 N ATOM 1182 CD2 HIS A 151 -19.804 -19.896 84.887 1.00 24.82 C ANISOU 1182 CD2 HIS A 151 3239 2269 3921 389 -62 342 C ATOM 1183 CE1 HIS A 151 -19.253 -22.007 85.129 1.00 27.24 C ANISOU 1183 CE1 HIS A 151 3512 2390 4449 625 51 620 C ATOM 1184 NE2 HIS A 151 -18.788 -20.771 85.186 1.00 22.53 N ANISOU 1184 NE2 HIS A 151 2885 2047 3627 531 -46 539 N ATOM 1185 N HIS A 152 -24.652 -19.372 82.084 1.00 23.75 N ANISOU 1185 N HIS A 152 3023 1648 4354 -29 -267 65 N ATOM 1186 CA HIS A 152 -26.081 -19.069 82.116 1.00 26.92 C ANISOU 1186 CA HIS A 152 3246 2025 4959 -123 -279 184 C ATOM 1187 C HIS A 152 -26.679 -18.815 80.747 1.00 33.39 C ANISOU 1187 C HIS A 152 4006 2822 5858 -232 -527 154 C ATOM 1188 O HIS A 152 -27.899 -18.635 80.649 1.00 40.15 O ANISOU 1188 O HIS A 152 4656 3647 6951 -306 -594 309 O ATOM 1189 CB HIS A 152 -26.343 -17.854 83.018 1.00 26.43 C ANISOU 1189 CB HIS A 152 3104 2039 4900 -87 -64 275 C ATOM 1190 CG HIS A 152 -25.969 -18.092 84.444 1.00 28.86 C ANISOU 1190 CG HIS A 152 3499 2329 5140 -12 149 334 C ATOM 1191 ND1 HIS A 152 -26.658 -18.973 85.251 1.00 31.90 N ANISOU 1191 ND1 HIS A 152 3825 2638 5657 13 259 482 N ATOM 1192 CD2 HIS A 152 -24.965 -17.592 85.201 1.00 29.89 C ANISOU 1192 CD2 HIS A 152 3769 2481 5106 38 263 293 C ATOM 1193 CE1 HIS A 152 -26.098 -18.997 86.448 1.00 37.02 C ANISOU 1193 CE1 HIS A 152 4597 3280 6187 96 452 556 C ATOM 1194 NE2 HIS A 152 -25.068 -18.169 86.443 1.00 32.72 N ANISOU 1194 NE2 HIS A 152 4189 2780 5464 101 449 444 N ATOM 1195 N LEU A 153 -25.869 -18.791 79.692 1.00 29.75 N ANISOU 1195 N LEU A 153 3714 2371 5220 -234 -677 -8 N ATOM 1196 CA LEU A 153 -26.392 -18.397 78.388 1.00 40.87 C ANISOU 1196 CA LEU A 153 5111 3771 6647 -357 -961 -17 C ATOM 1197 C LEU A 153 -27.145 -19.541 77.721 1.00 51.67 C ANISOU 1197 C LEU A 153 6547 5012 8073 -517 -1212 -74 C ATOM 1198 O LEU A 153 -28.353 -19.445 77.480 1.00 55.33 O ANISOU 1198 O LEU A 153 6811 5458 8753 -652 -1399 100 O ATOM 1199 CB LEU A 153 -25.256 -17.903 77.501 1.00 35.07 C ANISOU 1199 CB LEU A 153 4583 3091 5649 -293 -1020 -181 C ATOM 1200 CG LEU A 153 -25.636 -17.325 76.151 1.00 43.39 C ANISOU 1200 CG LEU A 153 5658 4260 6569 -395 -1287 -159 C ATOM 1201 CD1 LEU A 153 -26.694 -16.237 76.321 1.00 37.03 C ANISOU 1201 CD1 LEU A 153 4499 3509 6060 -468 -1312 149 C ATOM 1202 CD2 LEU A 153 -24.388 -16.798 75.473 1.00 45.45 C ANISOU 1202 CD2 LEU A 153 6094 4705 6469 -222 -1160 -261 C ATOM 1203 N THR A 154 -26.451 -20.634 77.419 1.00 59.90 N ANISOU 1203 N THR A 154 7862 5951 8945 -499 -1192 -296 N ATOM 1204 CA THR A 154 -27.077 -21.745 76.703 1.00 73.77 C ANISOU 1204 CA THR A 154 9751 7558 10720 -682 -1398 -419 C ATOM 1205 C THR A 154 -27.531 -22.854 77.648 1.00 75.14 C ANISOU 1205 C THR A 154 9831 7556 11164 -694 -1252 -346 C ATOM 1206 O THR A 154 -26.961 -23.041 78.721 1.00 72.94 O ANISOU 1206 O THR A 154 9513 7274 10927 -525 -967 -269 O ATOM 1207 CB THR A 154 -26.124 -22.343 75.648 1.00 82.50 C ANISOU 1207 CB THR A 154 11266 8603 11476 -664 -1403 -738 C ATOM 1208 OG1 THR A 154 -25.142 -23.162 76.296 1.00 88.11 O ANISOU 1208 OG1 THR A 154 12097 9181 12202 -484 -1063 -810 O ATOM 1209 CG2 THR A 154 -25.428 -21.237 74.865 1.00 76.69 C ANISOU 1209 CG2 THR A 154 10654 8057 10428 -574 -1466 -789 C TER 1210 THR A 154 ATOM 1211 N PRO B 4 -48.825 -10.369 116.967 1.00 60.83 N ATOM 1212 CA PRO B 4 -47.663 -9.546 117.321 1.00 62.20 C ATOM 1213 C PRO B 4 -46.763 -9.269 116.116 1.00 66.43 C ATOM 1214 O PRO B 4 -46.062 -10.161 115.634 1.00 65.87 O ATOM 1215 CB PRO B 4 -46.940 -10.394 118.369 1.00 59.80 C ATOM 1216 CG PRO B 4 -47.300 -11.798 118.030 1.00 61.91 C ATOM 1217 CD PRO B 4 -48.673 -11.769 117.402 1.00 63.47 C ATOM 1218 N LYS B 5 -46.792 -8.028 115.642 1.00 61.85 N ATOM 1219 CA LYS B 5 -46.043 -7.639 114.457 1.00 63.89 C ATOM 1220 C LYS B 5 -44.535 -7.683 114.709 1.00 59.82 C ATOM 1221 O LYS B 5 -44.065 -7.698 115.849 1.00 59.44 O ATOM 1222 CB LYS B 5 -46.460 -6.240 114.013 1.00 60.74 C ATOM 1223 CG LYS B 5 -47.507 -6.244 112.928 1.00 62.43 C ATOM 1224 CD LYS B 5 -48.381 -5.018 113.014 1.00 65.35 C ATOM 1225 CE LYS B 5 -49.781 -5.325 112.512 1.00 73.54 C ATOM 1226 NZ LYS B 5 -50.051 -4.688 111.189 1.00 71.14 N ATOM 1227 N THR B 6 -43.771 -7.705 113.613 1.00 56.10 N ATOM 1228 CA THR B 6 -42.314 -7.673 113.667 1.00 51.35 C ATOM 1229 C THR B 6 -41.787 -6.623 112.698 1.00 42.65 C ATOM 1230 O THR B 6 -42.284 -6.498 111.577 1.00 47.70 O ATOM 1231 CB THR B 6 -41.700 -9.033 113.317 1.00 52.25 C ATOM 1232 OG1 THR B 6 -42.131 -9.428 112.011 1.00 54.22 O ATOM 1233 CG2 THR B 6 -42.133 -10.093 114.314 1.00 55.74 C ATOM 1234 N ILE B 7 -40.773 -5.876 113.134 1.00 48.14 N ATOM 1235 CA ILE B 7 -40.114 -4.868 112.310 1.00 44.08 C ATOM 1236 C ILE B 7 -38.630 -5.193 112.238 1.00 35.18 C ATOM 1237 O ILE B 7 -37.977 -5.383 113.277 1.00 34.27 O ATOM 1238 CB ILE B 7 -40.311 -3.446 112.860 1.00 45.81 C ATOM 1239 CG1 ILE B 7 -41.797 -3.093 112.932 1.00 45.78 C ATOM 1240 CG2 ILE B 7 -39.552 -2.445 111.994 1.00 40.22 C ATOM 1241 CD1 ILE B 7 -42.045 -1.629 113.235 1.00 48.53 C ATOM 1242 N TYR B 8 -38.100 -5.245 111.013 1.00 52.20 N ANISOU 1242 N TYR B 8 5256 8835 5742 -1175 1591 -307 N ATOM 1243 CA TYR B 8 -36.668 -5.397 110.809 1.00 45.55 C ANISOU 1243 CA TYR B 8 4597 7880 4831 -1118 1462 -312 C ATOM 1244 C TYR B 8 -35.982 -4.054 111.014 1.00 38.14 C ANISOU 1244 C TYR B 8 3673 6991 3826 -944 1336 -434 C ATOM 1245 O TYR B 8 -36.362 -3.056 110.395 1.00 38.74 O ANISOU 1245 O TYR B 8 3622 7099 4000 -913 1262 -538 O ATOM 1246 CB TYR B 8 -36.374 -5.934 109.407 1.00 40.75 C ANISOU 1246 CB TYR B 8 4002 7123 4360 -1254 1354 -312 C ATOM 1247 CG TYR B 8 -34.918 -6.254 109.211 1.00 36.20 C ANISOU 1247 CG TYR B 8 3611 6407 3734 -1195 1265 -282 C ATOM 1248 CD1 TYR B 8 -34.147 -5.568 108.281 1.00 34.39 C ANISOU 1248 CD1 TYR B 8 3395 6099 3573 -1146 1092 -370 C ATOM 1249 CD2 TYR B 8 -34.299 -7.222 109.982 1.00 40.55 C ANISOU 1249 CD2 TYR B 8 4319 6910 4179 -1173 1367 -150 C ATOM 1250 CE1 TYR B 8 -32.799 -5.850 108.113 1.00 33.36 C ANISOU 1250 CE1 TYR B 8 3415 5840 3420 -1085 1025 -327 C ATOM 1251 CE2 TYR B 8 -32.958 -7.511 109.824 1.00 39.94 C ANISOU 1251 CE2 TYR B 8 4386 6716 4073 -1103 1294 -94 C ATOM 1252 CZ TYR B 8 -32.205 -6.822 108.895 1.00 37.27 C ANISOU 1252 CZ TYR B 8 4045 6298 3817 -1061 1123 -183 C ATOM 1253 OH TYR B 8 -30.869 -7.126 108.754 1.00 39.60 O ANISOU 1253 OH TYR B 8 4465 6476 4105 -987 1066 -110 O ATOM 1254 N ILE B 9 -34.967 -4.034 111.877 1.00 37.67 N ANISOU 1254 N ILE B 9 3770 6940 3601 -837 1312 -416 N ATOM 1255 CA ILE B 9 -34.305 -2.799 112.289 1.00 37.15 C ANISOU 1255 CA ILE B 9 3741 6933 3443 -696 1210 -539 C ATOM 1256 C ILE B 9 -33.028 -2.689 111.461 1.00 36.22 C ANISOU 1256 C ILE B 9 3684 6695 3383 -677 1022 -567 C ATOM 1257 O ILE B 9 -31.964 -3.159 111.851 1.00 36.93 O ANISOU 1257 O ILE B 9 3896 6755 3379 -641 969 -495 O ATOM 1258 CB ILE B 9 -34.031 -2.785 113.793 1.00 38.71 C ANISOU 1258 CB ILE B 9 4066 7240 3403 -608 1286 -509 C ATOM 1259 CG1 ILE B 9 -35.325 -3.062 114.558 1.00 42.43 C ANISOU 1259 CG1 ILE B 9 4488 7800 3833 -631 1509 -456 C ATOM 1260 CG2 ILE B 9 -33.424 -1.459 114.220 1.00 38.51 C ANISOU 1260 CG2 ILE B 9 4086 7275 3272 -496 1185 -662 C ATOM 1261 CD1 ILE B 9 -36.441 -2.085 114.251 1.00 40.93 C ANISOU 1261 CD1 ILE B 9 4128 7661 3762 -616 1576 -557 C ATOM 1262 N ALA B 10 -33.137 -2.063 110.295 1.00 36.67 N ANISOU 1262 N ALA B 10 3649 6684 3602 -694 929 -660 N ATOM 1263 CA ALA B 10 -32.036 -1.990 109.343 1.00 32.22 C ANISOU 1263 CA ALA B 10 3137 5980 3125 -685 778 -682 C ATOM 1264 C ALA B 10 -31.279 -0.677 109.504 1.00 33.55 C ANISOU 1264 C ALA B 10 3316 6171 3262 -563 666 -820 C ATOM 1265 O ALA B 10 -31.881 0.383 109.708 1.00 33.02 O ANISOU 1265 O ALA B 10 3176 6182 3189 -507 696 -936 O ATOM 1266 CB ALA B 10 -32.567 -2.130 107.914 1.00 31.30 C ANISOU 1266 CB ALA B 10 2939 5763 3189 -784 744 -696 C ATOM 1267 N GLY B 11 -29.953 -0.749 109.440 1.00 31.34 N ANISOU 1267 N GLY B 11 3126 5816 2967 -524 554 -802 N ATOM 1268 CA GLY B 11 -29.153 0.450 109.504 1.00 30.23 C ANISOU 1268 CA GLY B 11 2993 5679 2816 -436 442 -938 C ATOM 1269 C GLY B 11 -27.757 0.211 110.035 1.00 32.63 C ANISOU 1269 C GLY B 11 3384 5978 3034 -398 337 -881 C ATOM 1270 O GLY B 11 -27.452 -0.847 110.587 1.00 34.59 O ANISOU 1270 O GLY B 11 3695 6253 3196 -413 366 -724 O ATOM 1271 N PRO B 12 -26.880 1.206 109.873 1.00 30.60 N ANISOU 1271 N PRO B 12 3126 5693 2809 -345 218 -999 N ATOM 1272 CA PRO B 12 -25.461 1.030 110.192 1.00 29.98 C ANISOU 1272 CA PRO B 12 3092 5608 2693 -318 91 -937 C ATOM 1273 C PRO B 12 -25.111 1.232 111.658 1.00 32.80 C ANISOU 1273 C PRO B 12 3501 6153 2807 -299 46 -947 C ATOM 1274 O PRO B 12 -23.927 1.389 111.974 1.00 34.01 O ANISOU 1274 O PRO B 12 3665 6337 2921 -281 -92 -929 O ATOM 1275 CB PRO B 12 -24.791 2.104 109.323 1.00 32.51 C ANISOU 1275 CB PRO B 12 3372 5810 3169 -287 -5 -1078 C ATOM 1276 CG PRO B 12 -25.805 3.204 109.254 1.00 34.79 C ANISOU 1276 CG PRO B 12 3625 6133 3461 -273 67 -1257 C ATOM 1277 CD PRO B 12 -27.162 2.530 109.282 1.00 36.90 C ANISOU 1277 CD PRO B 12 3866 6449 3705 -310 205 -1184 C ATOM 1278 N ALA B 13 -26.102 1.249 112.556 1.00 33.21 N ANISOU 1278 N ALA B 13 3587 6336 2694 -308 159 -972 N ATOM 1279 CA ALA B 13 -25.794 1.303 113.983 1.00 36.11 C ANISOU 1279 CA ALA B 13 4040 6886 2796 -297 125 -964 C ATOM 1280 C ALA B 13 -24.815 0.209 114.380 1.00 36.02 C ANISOU 1280 C ALA B 13 4060 6913 2711 -283 42 -747 C ATOM 1281 O ALA B 13 -23.995 0.404 115.285 1.00 37.53 O ANISOU 1281 O ALA B 13 4295 7242 2722 -271 -84 -737 O ATOM 1282 CB ALA B 13 -27.081 1.187 114.801 1.00 40.24 C ANISOU 1282 CB ALA B 13 4609 7512 3170 -301 305 -971 C ATOM 1283 N VAL B 14 -24.858 -0.931 113.686 1.00 44.65 N ANISOU 1283 N VAL B 14 5134 7884 3945 -287 110 -569 N ATOM 1284 CA VAL B 14 -24.022 -2.077 114.017 1.00 43.60 C ANISOU 1284 CA VAL B 14 5035 7765 3765 -253 82 -328 C ATOM 1285 C VAL B 14 -22.530 -1.770 113.903 1.00 44.20 C ANISOU 1285 C VAL B 14 5067 7842 3886 -215 -115 -296 C ATOM 1286 O VAL B 14 -21.711 -2.464 114.517 1.00 44.39 O ANISOU 1286 O VAL B 14 5103 7949 3812 -169 -177 -101 O ATOM 1287 CB VAL B 14 -24.432 -3.269 113.122 1.00 43.62 C ANISOU 1287 CB VAL B 14 5044 7588 3941 -280 232 -174 C ATOM 1288 CG1 VAL B 14 -23.870 -3.111 111.702 1.00 38.66 C ANISOU 1288 CG1 VAL B 14 4367 6751 3572 -290 179 -204 C ATOM 1289 CG2 VAL B 14 -24.000 -4.579 113.746 1.00 49.93 C ANISOU 1289 CG2 VAL B 14 5910 8414 4645 -238 296 91 C ATOM 1290 N PHE B 15 -22.156 -0.723 113.161 1.00 34.68 N ANISOU 1290 N PHE B 15 3798 6552 2826 -229 -211 -472 N ATOM 1291 CA PHE B 15 -20.760 -0.337 112.968 1.00 34.70 C ANISOU 1291 CA PHE B 15 3736 6541 2908 -206 -390 -457 C ATOM 1292 C PHE B 15 -20.269 0.666 114.010 1.00 36.41 C ANISOU 1292 C PHE B 15 3954 6958 2922 -233 -552 -599 C ATOM 1293 O PHE B 15 -19.071 0.987 114.035 1.00 38.64 O ANISOU 1293 O PHE B 15 4166 7271 3243 -232 -723 -581 O ATOM 1294 CB PHE B 15 -20.569 0.241 111.557 1.00 32.50 C ANISOU 1294 CB PHE B 15 3400 6041 2907 -211 -390 -569 C ATOM 1295 CG PHE B 15 -21.015 -0.685 110.455 1.00 33.04 C ANISOU 1295 CG PHE B 15 3491 5905 3159 -209 -244 -453 C ATOM 1296 CD1 PHE B 15 -22.041 -0.321 109.595 1.00 33.68 C ANISOU 1296 CD1 PHE B 15 3577 5875 3344 -246 -147 -589 C ATOM 1297 CD2 PHE B 15 -20.404 -1.918 110.281 1.00 37.55 C ANISOU 1297 CD2 PHE B 15 4082 6394 3790 -173 -199 -203 C ATOM 1298 CE1 PHE B 15 -22.449 -1.174 108.581 1.00 28.46 C ANISOU 1298 CE1 PHE B 15 2949 5036 2826 -273 -30 -495 C ATOM 1299 CE2 PHE B 15 -20.813 -2.773 109.278 1.00 38.50 C ANISOU 1299 CE2 PHE B 15 4256 6311 4062 -194 -50 -113 C ATOM 1300 CZ PHE B 15 -21.835 -2.401 108.426 1.00 33.74 C ANISOU 1300 CZ PHE B 15 3666 5609 3543 -257 23 -269 C ATOM 1301 N HIS B 16 -21.158 1.147 114.883 1.00 37.50 N ANISOU 1301 N HIS B 16 4174 7231 2843 -264 -494 -735 N ATOM 1302 CA HIS B 16 -20.760 2.039 115.955 1.00 39.50 C ANISOU 1302 CA HIS B 16 4474 7673 2861 -310 -628 -878 C ATOM 1303 C HIS B 16 -19.832 1.307 116.919 1.00 41.73 C ANISOU 1303 C HIS B 16 4760 8145 2949 -293 -776 -670 C ATOM 1304 O HIS B 16 -19.829 0.076 116.977 1.00 42.08 O ANISOU 1304 O HIS B 16 4804 8189 2995 -230 -712 -416 O ATOM 1305 CB HIS B 16 -21.987 2.550 116.707 1.00 41.35 C ANISOU 1305 CB HIS B 16 4825 7990 2895 -334 -485 -1036 C ATOM 1306 CG HIS B 16 -22.800 3.542 115.938 1.00 67.36 C ANISOU 1306 CG HIS B 16 8104 11140 6349 -344 -365 -1256 C ATOM 1307 ND1 HIS B 16 -24.126 3.796 116.220 1.00 74.59 N ANISOU 1307 ND1 HIS B 16 9080 12065 7194 -336 -170 -1344 N ATOM 1308 CD2 HIS B 16 -22.476 4.341 114.895 1.00 73.46 C ANISOU 1308 CD2 HIS B 16 8801 11756 7355 -348 -401 -1387 C ATOM 1309 CE1 HIS B 16 -24.583 4.711 115.382 1.00 77.35 C ANISOU 1309 CE1 HIS B 16 9383 12280 7725 -328 -99 -1509 C ATOM 1310 NE2 HIS B 16 -23.602 5.057 114.568 1.00 72.02 N ANISOU 1310 NE2 HIS B 16 8635 11501 7230 -335 -235 -1543 N ATOM 1311 N PRO B 17 -19.034 2.047 117.690 1.00 44.72 N ANISOU 1311 N PRO B 17 5144 8693 3153 -353 -973 -768 N ATOM 1312 CA PRO B 17 -18.160 1.382 118.668 1.00 46.18 C ANISOU 1312 CA PRO B 17 5320 9099 3126 -337 -1141 -556 C ATOM 1313 C PRO B 17 -18.886 0.435 119.612 1.00 59.53 C ANISOU 1313 C PRO B 17 7135 10918 4566 -284 -1019 -390 C ATOM 1314 O PRO B 17 -18.305 -0.581 120.018 1.00 53.22 O ANISOU 1314 O PRO B 17 6306 10219 3694 -214 -1076 -109 O ATOM 1315 CB PRO B 17 -17.538 2.563 119.420 1.00 48.25 C ANISOU 1315 CB PRO B 17 5607 9533 3191 -454 -1350 -773 C ATOM 1316 CG PRO B 17 -17.498 3.649 118.415 1.00 49.14 C ANISOU 1316 CG PRO B 17 5662 9449 3560 -505 -1331 -1017 C ATOM 1317 CD PRO B 17 -18.764 3.492 117.606 1.00 44.20 C ANISOU 1317 CD PRO B 17 5078 8615 3102 -443 -1065 -1061 C ATOM 1318 N ASP B 18 -20.134 0.725 119.985 1.00 47.65 N ANISOU 1318 N ASP B 18 5765 9408 2933 -303 -836 -538 N ATOM 1319 CA ASP B 18 -20.841 -0.159 120.900 1.00 53.31 C ANISOU 1319 CA ASP B 18 6604 10234 3416 -252 -698 -381 C ATOM 1320 C ASP B 18 -21.638 -1.238 120.172 1.00 49.63 C ANISOU 1320 C ASP B 18 6113 9587 3158 -185 -463 -216 C ATOM 1321 O ASP B 18 -22.535 -1.841 120.771 1.00 49.18 O ANISOU 1321 O ASP B 18 6159 9568 2959 -157 -282 -137 O ATOM 1322 CB ASP B 18 -21.736 0.649 121.853 1.00 50.74 C ANISOU 1322 CB ASP B 18 6451 10014 2814 -307 -607 -602 C ATOM 1323 CG ASP B 18 -22.905 1.344 121.151 1.00 52.78 C ANISOU 1323 CG ASP B 18 6714 10089 3253 -327 -397 -818 C ATOM 1324 OD1 ASP B 18 -23.014 1.278 119.912 1.00 54.91 O ANISOU 1324 OD1 ASP B 18 6855 10163 3845 -311 -349 -818 O ATOM 1325 OD2 ASP B 18 -23.730 1.959 121.866 1.00 54.23 O ANISOU 1325 OD2 ASP B 18 7035 10326 3244 -352 -271 -978 O ATOM 1326 N ASN B 19 -21.312 -1.503 118.906 1.00 49.86 N ANISOU 1326 N ASN B 19 6018 9415 3512 -169 -456 -162 N ATOM 1327 CA ASN B 19 -22.002 -2.488 118.072 1.00 51.66 C ANISOU 1327 CA ASN B 19 6228 9449 3950 -138 -245 -30 C ATOM 1328 C ASN B 19 -23.497 -2.208 117.969 1.00 45.13 C ANISOU 1328 C ASN B 19 5452 8562 3132 -180 -39 -186 C ATOM 1329 O ASN B 19 -24.287 -3.118 117.698 1.00 48.30 O ANISOU 1329 O ASN B 19 5871 8871 3612 -176 153 -69 O ATOM 1330 CB ASN B 19 -21.761 -3.914 118.579 1.00 47.72 C ANISOU 1330 CB ASN B 19 5772 8995 3364 -61 -171 289 C ATOM 1331 CG ASN B 19 -20.337 -4.375 118.347 1.00 61.20 C ANISOU 1331 CG ASN B 19 7389 10703 5160 3 -329 499 C ATOM 1332 OD1 ASN B 19 -19.530 -3.659 117.751 1.00 62.12 O ANISOU 1332 OD1 ASN B 19 7403 10778 5424 -20 -492 403 O ATOM 1333 ND2 ASN B 19 -20.017 -5.569 118.827 1.00 68.90 N ANISOU 1333 ND2 ASN B 19 8397 11724 6057 91 -265 799 N ATOM 1334 N GLY B 20 -23.895 -0.953 118.168 1.00 44.11 N ANISOU 1334 N GLY B 20 5343 8480 2938 -224 -64 -444 N ATOM 1335 CA GLY B 20 -25.288 -0.573 118.099 1.00 43.67 C ANISOU 1335 CA GLY B 20 5312 8378 2902 -248 134 -581 C ATOM 1336 C GLY B 20 -26.061 -0.782 119.377 1.00 44.56 C ANISOU 1336 C GLY B 20 5555 8640 2736 -235 271 -555 C ATOM 1337 O GLY B 20 -27.293 -0.696 119.351 1.00 45.11 O ANISOU 1337 O GLY B 20 5630 8668 2842 -243 473 -614 O ATOM 1338 N GLU B 21 -25.368 -1.044 120.491 1.00 46.80 N ANISOU 1338 N GLU B 21 5940 9099 2743 -212 168 -459 N ATOM 1339 CA GLU B 21 -26.027 -1.352 121.760 1.00 51.28 C ANISOU 1339 CA GLU B 21 6660 9808 3016 -189 306 -406 C ATOM 1340 C GLU B 21 -27.009 -0.257 122.159 1.00 49.82 C ANISOU 1340 C GLU B 21 6553 9636 2738 -219 441 -649 C ATOM 1341 O GLU B 21 -28.168 -0.536 122.493 1.00 50.43 O ANISOU 1341 O GLU B 21 6679 9699 2785 -200 681 -625 O ATOM 1342 CB GLU B 21 -24.972 -1.558 122.850 1.00 57.74 C ANISOU 1342 CB GLU B 21 7576 10836 3527 -166 118 -295 C ATOM 1343 CG GLU B 21 -25.549 -1.747 124.248 1.00 54.56 C ANISOU 1343 CG GLU B 21 7368 10595 2768 -141 240 -257 C ATOM 1344 CD GLU B 21 -24.483 -1.840 125.342 1.00 63.79 C ANISOU 1344 CD GLU B 21 8640 11986 3613 -128 18 -159 C ATOM 1345 OE1 GLU B 21 -23.448 -1.145 125.242 1.00 57.52 O ANISOU 1345 OE1 GLU B 21 7792 11232 2832 -181 -242 -254 O ATOM 1346 OE2 GLU B 21 -24.685 -2.612 126.303 1.00 64.91 O ANISOU 1346 OE2 GLU B 21 8910 12193 3558 -66 105 21 O ATOM 1347 N ALA B 22 -26.563 1.002 122.132 1.00 49.81 N ANISOU 1347 N ALA B 22 6568 9655 2704 -264 310 -879 N ATOM 1348 CA ALA B 22 -27.435 2.092 122.566 1.00 50.71 C ANISOU 1348 CA ALA B 22 6781 9767 2717 -283 464 -1107 C ATOM 1349 C ALA B 22 -28.619 2.262 121.623 1.00 57.00 C ANISOU 1349 C ALA B 22 7453 10397 3808 -261 675 -1155 C ATOM 1350 O ALA B 22 -29.752 2.468 122.073 1.00 58.39 O ANISOU 1350 O ALA B 22 7687 10573 3927 -237 911 -1198 O ATOM 1351 CB ALA B 22 -26.641 3.393 122.665 1.00 51.19 C ANISOU 1351 CB ALA B 22 6892 9787 2770 -340 284 -1320 C ATOM 1352 N TYR B 23 -28.367 2.183 120.314 1.00 47.46 N ANISOU 1352 N TYR B 23 6072 9052 2911 -267 595 -1140 N ATOM 1353 CA TYR B 23 -29.437 2.320 119.326 1.00 44.56 C ANISOU 1353 CA TYR B 23 5566 8544 2818 -255 757 -1171 C ATOM 1354 C TYR B 23 -30.512 1.262 119.534 1.00 45.11 C ANISOU 1354 C TYR B 23 5615 8619 2905 -244 966 -999 C ATOM 1355 O TYR B 23 -31.703 1.578 119.625 1.00 45.63 O ANISOU 1355 O TYR B 23 5653 8671 3015 -228 1175 -1046 O ATOM 1356 CB TYR B 23 -28.857 2.229 117.910 1.00 41.95 C ANISOU 1356 CB TYR B 23 5084 8075 2782 -271 615 -1153 C ATOM 1357 CG TYR B 23 -29.894 2.344 116.810 1.00 40.36 C ANISOU 1357 CG TYR B 23 4735 7747 2851 -269 743 -1174 C ATOM 1358 CD1 TYR B 23 -30.506 3.559 116.537 1.00 52.71 C ANISOU 1358 CD1 TYR B 23 6262 9272 4493 -241 826 -1353 C ATOM 1359 CD2 TYR B 23 -30.270 1.239 116.060 1.00 39.28 C ANISOU 1359 CD2 TYR B 23 4504 7536 2885 -298 785 -1010 C ATOM 1360 CE1 TYR B 23 -31.456 3.678 115.541 1.00 52.40 C ANISOU 1360 CE1 TYR B 23 6071 9146 4693 -231 925 -1350 C ATOM 1361 CE2 TYR B 23 -31.223 1.347 115.055 1.00 41.25 C ANISOU 1361 CE2 TYR B 23 4613 7697 3362 -316 873 -1028 C ATOM 1362 CZ TYR B 23 -31.812 2.573 114.805 1.00 47.75 C ANISOU 1362 CZ TYR B 23 5379 8508 4257 -276 932 -1190 C ATOM 1363 OH TYR B 23 -32.762 2.706 113.813 1.00 45.47 O ANISOU 1363 OH TYR B 23 4932 8157 4187 -284 1003 -1188 O ATOM 1364 N TYR B 24 -30.102 -0.005 119.630 1.00 46.95 N ANISOU 1364 N TYR B 24 5859 8869 3112 -250 929 -788 N ATOM 1365 CA TYR B 24 -31.072 -1.088 119.764 1.00 47.05 C ANISOU 1365 CA TYR B 24 5852 8864 3162 -256 1137 -621 C ATOM 1366 C TYR B 24 -31.779 -1.043 121.112 1.00 48.36 C ANISOU 1366 C TYR B 24 6160 9147 3067 -220 1325 -615 C ATOM 1367 O TYR B 24 -32.978 -1.331 121.191 1.00 49.69 O ANISOU 1367 O TYR B 24 6285 9291 3305 -224 1556 -573 O ATOM 1368 CB TYR B 24 -30.389 -2.437 119.570 1.00 45.46 C ANISOU 1368 CB TYR B 24 5655 8630 2988 -263 1078 -395 C ATOM 1369 CG TYR B 24 -29.795 -2.620 118.199 1.00 43.06 C ANISOU 1369 CG TYR B 24 5230 8179 2952 -298 944 -381 C ATOM 1370 CD1 TYR B 24 -30.502 -2.255 117.059 1.00 46.40 C ANISOU 1370 CD1 TYR B 24 5518 8484 3630 -347 984 -478 C ATOM 1371 CD2 TYR B 24 -28.533 -3.171 118.042 1.00 42.72 C ANISOU 1371 CD2 TYR B 24 5209 8117 2904 -276 785 -256 C ATOM 1372 CE1 TYR B 24 -29.959 -2.429 115.798 1.00 46.60 C ANISOU 1372 CE1 TYR B 24 5461 8367 3877 -381 871 -467 C ATOM 1373 CE2 TYR B 24 -27.979 -3.345 116.791 1.00 41.45 C ANISOU 1373 CE2 TYR B 24 4959 7803 2987 -302 690 -239 C ATOM 1374 CZ TYR B 24 -28.700 -2.978 115.671 1.00 42.34 C ANISOU 1374 CZ TYR B 24 4966 7790 3331 -358 736 -352 C ATOM 1375 OH TYR B 24 -28.140 -3.156 114.430 1.00 40.42 O ANISOU 1375 OH TYR B 24 4662 7387 3306 -384 650 -336 O ATOM 1376 N ASN B 25 -31.055 -0.703 122.187 1.00 50.14 N ANISOU 1376 N ASN B 25 6560 9505 2986 -192 1232 -651 N ATOM 1377 CA ASN B 25 -31.714 -0.528 123.479 1.00 52.79 C ANISOU 1377 CA ASN B 25 7069 9944 3046 -158 1418 -670 C ATOM 1378 C ASN B 25 -32.805 0.529 123.391 1.00 52.94 C ANISOU 1378 C ASN B 25 7059 9893 3163 -148 1605 -848 C ATOM 1379 O ASN B 25 -33.888 0.371 123.966 1.00 54.46 O ANISOU 1379 O ASN B 25 7297 10049 3345 -114 1853 -797 O ATOM 1380 CB ASN B 25 -30.692 -0.144 124.551 1.00 54.78 C ANISOU 1380 CB ASN B 25 7522 10319 2974 -148 1238 -712 C ATOM 1381 CG ASN B 25 -29.963 -1.340 125.116 1.00 67.36 C ANISOU 1381 CG ASN B 25 9184 12021 4388 -119 1151 -473 C ATOM 1382 OD1 ASN B 25 -30.400 -2.480 124.955 1.00 63.56 O ANISOU 1382 OD1 ASN B 25 8653 11510 3986 -95 1297 -274 O ATOM 1383 ND2 ASN B 25 -28.839 -1.089 125.781 1.00 69.70 N ANISOU 1383 ND2 ASN B 25 9593 12420 4471 -122 912 -479 N ATOM 1384 N ASN B 26 -32.533 1.617 122.669 1.00 61.73 N ANISOU 1384 N ASN B 26 8097 10948 4411 -165 1497 -1035 N ATOM 1385 CA ASN B 26 -33.545 2.647 122.475 1.00 51.65 C ANISOU 1385 CA ASN B 26 6778 9564 3285 -132 1673 -1169 C ATOM 1386 C ASN B 26 -34.715 2.102 121.667 1.00 50.63 C ANISOU 1386 C ASN B 26 6428 9392 3418 -132 1858 -1070 C ATOM 1387 O ASN B 26 -35.881 2.374 121.983 1.00 52.15 O ANISOU 1387 O ASN B 26 6604 9532 3678 -88 2093 -1058 O ATOM 1388 CB ASN B 26 -32.914 3.863 121.797 1.00 51.97 C ANISOU 1388 CB ASN B 26 6783 9532 3433 -144 1514 -1367 C ATOM 1389 CG ASN B 26 -33.888 5.006 121.610 1.00 63.11 C ANISOU 1389 CG ASN B 26 8164 10817 4999 -88 1702 -1485 C ATOM 1390 OD1 ASN B 26 -34.261 5.682 122.568 1.00 69.23 O ANISOU 1390 OD1 ASN B 26 9122 11549 5635 -47 1840 -1549 O ATOM 1391 ND2 ASN B 26 -34.292 5.242 120.365 1.00 69.13 N ANISOU 1391 ND2 ASN B 26 8705 11514 6047 -77 1712 -1504 N ATOM 1392 N VAL B 27 -34.424 1.296 120.645 1.00 48.59 N ANISOU 1392 N VAL B 27 6013 9089 3362 -182 1731 -963 N ATOM 1393 CA VAL B 27 -35.485 0.674 119.855 1.00 47.86 C ANISOU 1393 CA VAL B 27 5719 8931 3535 -215 1862 -854 C ATOM 1394 C VAL B 27 -36.314 -0.263 120.725 1.00 54.57 C ANISOU 1394 C VAL B 27 6616 9830 4287 -217 2095 -698 C ATOM 1395 O VAL B 27 -37.550 -0.211 120.723 1.00 55.86 O ANISOU 1395 O VAL B 27 6667 9986 4572 -212 2316 -671 O ATOM 1396 CB VAL B 27 -34.888 -0.069 118.646 1.00 45.56 C ANISOU 1396 CB VAL B 27 5308 8555 3448 -285 1673 -773 C ATOM 1397 CG1 VAL B 27 -35.940 -0.980 118.014 1.00 45.38 C ANISOU 1397 CG1 VAL B 27 5120 8483 3641 -357 1807 -640 C ATOM 1398 CG2 VAL B 27 -34.311 0.920 117.622 1.00 43.58 C ANISOU 1398 CG2 VAL B 27 4977 8232 3348 -276 1490 -923 C ATOM 1399 N ARG B 28 -35.643 -1.141 121.479 1.00 50.77 N ANISOU 1399 N ARG B 28 6294 9401 3594 -217 2056 -579 N ATOM 1400 CA ARG B 28 -36.356 -2.057 122.368 1.00 52.84 C ANISOU 1400 CA ARG B 28 6631 9701 3746 -209 2292 -422 C ATOM 1401 C ARG B 28 -37.260 -1.308 123.337 1.00 57.51 C ANISOU 1401 C ARG B 28 7323 10283 4245 -134 2509 -487 C ATOM 1402 O ARG B 28 -38.418 -1.693 123.538 1.00 60.88 O ANISOU 1402 O ARG B 28 7684 10659 4789 -130 2750 -395 O ATOM 1403 CB ARG B 28 -35.362 -2.922 123.138 1.00 53.76 C ANISOU 1403 CB ARG B 28 6936 9881 3610 -187 2202 -288 C ATOM 1404 CG ARG B 28 -34.585 -3.858 122.250 1.00 63.06 C ANISOU 1404 CG ARG B 28 8035 10984 4940 -239 2034 -164 C ATOM 1405 CD ARG B 28 -34.087 -5.064 123.007 1.00 69.33 C ANISOU 1405 CD ARG B 28 8974 11818 5550 -207 2074 51 C ATOM 1406 NE ARG B 28 -33.333 -5.940 122.118 1.00 72.49 N ANISOU 1406 NE ARG B 28 9308 12121 6113 -247 1946 175 N ATOM 1407 CZ ARG B 28 -32.054 -5.760 121.813 1.00 73.66 C ANISOU 1407 CZ ARG B 28 9471 12283 6234 -221 1691 169 C ATOM 1408 NH1 ARG B 28 -31.384 -4.740 122.335 1.00 72.44 N ANISOU 1408 NH1 ARG B 28 9389 12246 5889 -176 1519 36 N ATOM 1409 NH2 ARG B 28 -31.445 -6.602 120.990 1.00 78.29 N ANISOU 1409 NH2 ARG B 28 10004 12756 6986 -249 1623 297 N ATOM 1410 N ALA B 29 -36.750 -0.230 123.939 1.00 58.07 N ANISOU 1410 N ALA B 29 7563 10372 4130 -79 2430 -641 N ATOM 1411 CA ALA B 29 -37.530 0.520 124.918 1.00 60.82 C ANISOU 1411 CA ALA B 29 8059 10670 4377 -2 2647 -701 C ATOM 1412 C ALA B 29 -38.790 1.113 124.300 1.00 58.03 C ANISOU 1412 C ALA B 29 7501 10232 4315 26 2842 -731 C ATOM 1413 O ALA B 29 -39.853 1.121 124.931 1.00 60.07 O ANISOU 1413 O ALA B 29 7788 10442 4594 86 3114 -665 O ATOM 1414 CB ALA B 29 -36.669 1.621 125.536 1.00 65.71 C ANISOU 1414 CB ALA B 29 8902 11301 4764 25 2505 -878 C ATOM 1415 N LEU B 30 -38.690 1.620 123.073 1.00 55.76 N ANISOU 1415 N LEU B 30 7003 9925 4258 -6 2709 -815 N ATOM 1416 CA LEU B 30 -39.832 2.264 122.430 1.00 64.23 C ANISOU 1416 CA LEU B 30 7865 10927 5612 32 2861 -827 C ATOM 1417 C LEU B 30 -40.919 1.265 122.052 1.00 67.95 C ANISOU 1417 C LEU B 30 8115 11399 6303 -17 3012 -649 C ATOM 1418 O LEU B 30 -42.109 1.598 122.101 1.00 73.00 O ANISOU 1418 O LEU B 30 8634 11992 7110 38 3227 -596 O ATOM 1419 CB LEU B 30 -39.373 3.018 121.182 1.00 62.58 C ANISOU 1419 CB LEU B 30 7499 10696 5583 14 2661 -950 C ATOM 1420 CG LEU B 30 -38.603 4.306 121.456 1.00 66.07 C ANISOU 1420 CG LEU B 30 8121 11089 5893 69 2568 -1141 C ATOM 1421 CD1 LEU B 30 -37.615 4.572 120.338 1.00 65.43 C ANISOU 1421 CD1 LEU B 30 7943 11007 5909 18 2297 -1239 C ATOM 1422 CD2 LEU B 30 -39.559 5.476 121.636 1.00 62.57 C ANISOU 1422 CD2 LEU B 30 7675 10542 5556 183 2790 -1188 C ATOM 1423 N MET B 31 -40.539 0.053 121.663 1.00 68.56 N ANISOU 1423 N MET B 31 8136 11517 6397 -122 2908 -545 N ATOM 1424 CA MET B 31 -41.506 -0.928 121.196 1.00 70.58 C ANISOU 1424 CA MET B 31 8184 11754 6881 -205 3025 -388 C ATOM 1425 C MET B 31 -42.033 -1.821 122.313 1.00 77.77 C ANISOU 1425 C MET B 31 9222 12647 7679 -190 3257 -240 C ATOM 1426 O MET B 31 -42.951 -2.611 122.072 1.00 80.74 O ANISOU 1426 O MET B 31 9437 12989 8251 -258 3393 -108 O ATOM 1427 CB MET B 31 -40.887 -1.777 120.072 1.00 66.94 C ANISOU 1427 CB MET B 31 7602 11304 6528 -340 2816 -352 C ATOM 1428 CG MET B 31 -40.316 -0.933 118.929 1.00 69.22 C ANISOU 1428 CG MET B 31 7777 11598 6925 -349 2592 -493 C ATOM 1429 SD MET B 31 -39.637 -1.815 117.493 1.00 71.15 S ANISOU 1429 SD MET B 31 7920 11766 7349 -491 2334 -447 S ATOM 1430 CE MET B 31 -40.713 -3.236 117.443 1.00 65.27 C ANISOU 1430 CE MET B 31 7051 11010 6741 -634 2524 -262 C ATOM 1431 N LYS B 32 -41.498 -1.698 123.526 1.00 78.17 N ANISOU 1431 N LYS B 32 9562 12714 7425 -106 3306 -260 N ATOM 1432 CA LYS B 32 -41.965 -2.510 124.641 1.00 82.53 C ANISOU 1432 CA LYS B 32 10269 13239 7850 -74 3539 -118 C ATOM 1433 C LYS B 32 -43.408 -2.164 124.990 1.00 81.79 C ANISOU 1433 C LYS B 32 10073 13087 7917 -4 3841 -62 C ATOM 1434 O LYS B 32 -43.726 -1.008 125.290 1.00 76.14 O ANISOU 1434 O LYS B 32 9393 12363 7174 108 3920 -151 O ATOM 1435 CB LYS B 32 -41.060 -2.305 125.857 1.00 86.00 C ANISOU 1435 CB LYS B 32 11055 13713 7906 3 3501 -164 C ATOM 1436 CG LYS B 32 -41.060 -3.467 126.848 1.00 91.90 C ANISOU 1436 CG LYS B 32 11997 14441 8481 -6 3648 -10 C ATOM 1437 CD LYS B 32 -40.518 -4.744 126.216 1.00 93.21 C ANISOU 1437 CD LYS B 32 12077 14616 8724 -97 3523 125 C ATOM 1438 CE LYS B 32 -39.873 -5.658 127.252 1.00 92.79 C ANISOU 1438 CE LYS B 32 12283 14581 8393 -95 3538 237 C ATOM 1439 NZ LYS B 32 -39.489 -6.976 126.666 1.00 89.99 N ANISOU 1439 NZ LYS B 32 11853 14191 8146 -168 3483 398 N ATOM 1440 N GLY B 33 -44.279 -3.170 124.943 1.00 86.40 N ANISOU 1440 N GLY B 33 10512 13641 8676 -54 3992 108 N ATOM 1441 CA GLY B 33 -45.656 -3.005 125.364 1.00 91.70 C ANISOU 1441 CA GLY B 33 10907 14534 9401 -81 4101 127 C ATOM 1442 C GLY B 33 -46.597 -2.485 124.305 1.00 90.72 C ANISOU 1442 C GLY B 33 10468 14370 9633 -61 4121 173 C ATOM 1443 O GLY B 33 -47.654 -1.944 124.648 1.00 88.91 O ANISOU 1443 O GLY B 33 10101 14206 9475 -107 4279 96 O ATOM 1444 N LYS B 34 -46.249 -2.634 123.021 1.00 85.68 N ANISOU 1444 N LYS B 34 9759 13541 9256 -145 4042 164 N ATOM 1445 CA LYS B 34 -47.043 -2.077 121.931 1.00 79.77 C ANISOU 1445 CA LYS B 34 8690 12788 8831 -186 4001 155 C ATOM 1446 C LYS B 34 -47.379 -3.119 120.865 1.00 75.85 C ANISOU 1446 C LYS B 34 7950 12290 8579 -385 3883 238 C ATOM 1447 O LYS B 34 -47.698 -2.749 119.731 1.00 83.71 O ANISOU 1447 O LYS B 34 8701 13303 9802 -453 3736 206 O ATOM 1448 CB LYS B 34 -46.328 -0.871 121.306 1.00 68.24 C ANISOU 1448 CB LYS B 34 7243 11343 7342 -138 3796 -27 C ATOM 1449 CG LYS B 34 -46.640 0.467 121.997 1.00 74.27 C ANISOU 1449 CG LYS B 34 8108 12078 8034 55 3965 -88 C ATOM 1450 CD LYS B 34 -45.916 0.608 123.337 1.00 83.18 C ANISOU 1450 CD LYS B 34 9604 13213 8786 158 4027 -144 C ATOM 1451 CE LYS B 34 -46.486 1.725 124.212 1.00 81.71 C ANISOU 1451 CE LYS B 34 9404 13209 8434 291 4096 -222 C ATOM 1452 NZ LYS B 34 -47.671 1.267 124.994 1.00 83.91 N ANISOU 1452 NZ LYS B 34 9578 13565 8738 178 4338 -206 N ATOM 1453 N ASP B 35 -47.311 -4.411 121.205 1.00 74.89 N ANISOU 1453 N ASP B 35 7903 12149 8404 -474 3942 352 N ATOM 1454 CA ASP B 35 -47.695 -5.533 120.337 1.00 77.95 C ANISOU 1454 CA ASP B 35 8102 12508 9007 -675 3870 443 C ATOM 1455 C ASP B 35 -46.786 -5.668 119.116 1.00 70.42 C ANISOU 1455 C ASP B 35 7125 11550 8080 -810 3567 336 C ATOM 1456 O ASP B 35 -47.138 -6.334 118.134 1.00 59.89 O ANISOU 1456 O ASP B 35 5617 10190 6947 -988 3464 375 O ATOM 1457 CB ASP B 35 -49.164 -5.438 119.893 1.00 85.24 C ANISOU 1457 CB ASP B 35 8691 13450 10248 -722 3967 548 C ATOM 1458 CG ASP B 35 -49.726 -6.778 119.420 1.00 92.99 C ANISOU 1458 CG ASP B 35 9526 14406 11400 -929 3962 675 C ATOM 1459 OD1 ASP B 35 -49.525 -7.788 120.125 1.00 96.10 O ANISOU 1459 OD1 ASP B 35 10067 14804 11641 -955 4056 768 O ATOM 1460 OD2 ASP B 35 -50.355 -6.825 118.339 1.00 96.87 O ANISOU 1460 OD2 ASP B 35 9758 14889 12158 -1074 3844 676 O ATOM 1461 N VAL B 36 -45.616 -5.047 119.169 1.00 61.19 N ANISOU 1461 N VAL B 36 6135 10412 6703 -729 3418 208 N ATOM 1462 CA VAL B 36 -44.612 -5.135 118.119 1.00 57.94 C ANISOU 1462 CA VAL B 36 5728 10003 6283 -823 3144 121 C ATOM 1463 C VAL B 36 -43.315 -5.614 118.753 1.00 58.66 C ANISOU 1463 C VAL B 36 6111 10083 6095 -783 3103 116 C ATOM 1464 O VAL B 36 -43.056 -5.367 119.936 1.00 57.61 O ANISOU 1464 O VAL B 36 6177 9974 5738 -648 3218 119 O ATOM 1465 CB VAL B 36 -44.420 -3.778 117.411 1.00 60.33 C ANISOU 1465 CB VAL B 36 5923 10362 6640 -747 2977 -20 C ATOM 1466 CG1 VAL B 36 -45.663 -3.421 116.625 1.00 58.74 C ANISOU 1466 CG1 VAL B 36 5414 10172 6730 -791 2984 20 C ATOM 1467 CG2 VAL B 36 -44.127 -2.695 118.432 1.00 60.03 C ANISOU 1467 CG2 VAL B 36 6053 10355 6402 -550 3067 -104 C ATOM 1468 N VAL B 37 -42.503 -6.317 117.970 1.00 58.55 N ANISOU 1468 N VAL B 37 8396 8711 5140 -2190 2737 -1290 N ATOM 1469 CA VAL B 37 -41.220 -6.807 118.470 1.00 57.56 C ANISOU 1469 CA VAL B 37 8502 8592 4775 -2162 2672 -1011 C ATOM 1470 C VAL B 37 -40.142 -6.516 117.430 1.00 51.72 C ANISOU 1470 C VAL B 37 7675 7851 4126 -1988 2437 -978 C ATOM 1471 O VAL B 37 -40.366 -6.710 116.224 1.00 53.27 O ANISOU 1471 O VAL B 37 7693 7968 4579 -1936 2413 -1091 O ATOM 1472 CB VAL B 37 -41.290 -8.302 118.830 1.00 64.38 C ANISOU 1472 CB VAL B 37 9568 9323 5570 -2292 2901 -819 C ATOM 1473 CG1 VAL B 37 -41.601 -9.140 117.619 1.00 61.20 C ANISOU 1473 CG1 VAL B 37 9034 8752 5467 -2327 2988 -915 C ATOM 1474 CG2 VAL B 37 -39.994 -8.768 119.470 1.00 68.80 C ANISOU 1474 CG2 VAL B 37 10381 9932 5827 -2200 2820 -468 C ATOM 1475 N PRO B 38 -38.984 -6.005 117.836 1.00 51.48 N ANISOU 1475 N PRO B 38 7738 7924 3896 -1893 2255 -855 N ATOM 1476 CA PRO B 38 -37.938 -5.709 116.856 1.00 45.94 C ANISOU 1476 CA PRO B 38 6955 7215 3287 -1745 2040 -848 C ATOM 1477 C PRO B 38 -37.219 -6.968 116.414 1.00 55.05 C ANISOU 1477 C PRO B 38 8212 8295 4409 -1741 2044 -645 C ATOM 1478 O PRO B 38 -37.031 -7.919 117.177 1.00 56.83 O ANISOU 1478 O PRO B 38 8649 8515 4428 -1797 2155 -409 O ATOM 1479 CB PRO B 38 -36.990 -4.775 117.615 1.00 57.27 C ANISOU 1479 CB PRO B 38 8454 8799 4506 -1686 1875 -823 C ATOM 1480 CG PRO B 38 -37.156 -5.174 119.046 1.00 53.83 C ANISOU 1480 CG PRO B 38 8207 8481 3767 -1783 1987 -686 C ATOM 1481 CD PRO B 38 -38.606 -5.579 119.197 1.00 55.00 C ANISOU 1481 CD PRO B 38 8339 8527 4032 -1917 2232 -763 C ATOM 1482 N LEU B 39 -36.825 -6.957 115.152 1.00 50.18 N ANISOU 1482 N LEU B 39 7452 7607 4005 -1653 1933 -716 N ATOM 1483 CA LEU B 39 -35.988 -7.995 114.578 1.00 43.80 C ANISOU 1483 CA LEU B 39 6724 6723 3195 -1632 1908 -538 C ATOM 1484 C LEU B 39 -34.620 -7.350 114.372 1.00 44.36 C ANISOU 1484 C LEU B 39 6792 6909 3155 -1495 1625 -503 C ATOM 1485 O LEU B 39 -34.435 -6.559 113.444 1.00 44.29 O ANISOU 1485 O LEU B 39 6604 6879 3346 -1403 1495 -682 O ATOM 1486 CB LEU B 39 -36.593 -8.510 113.279 1.00 46.36 C ANISOU 1486 CB LEU B 39 6855 6897 3862 -1653 2004 -689 C ATOM 1487 CG LEU B 39 -37.849 -9.372 113.369 1.00 47.71 C ANISOU 1487 CG LEU B 39 7001 6943 4186 -1811 2290 -760 C ATOM 1488 CD1 LEU B 39 -38.212 -9.901 111.984 1.00 44.96 C ANISOU 1488 CD1 LEU B 39 6413 6489 4183 -1807 2330 -937 C ATOM 1489 CD2 LEU B 39 -37.658 -10.507 114.357 1.00 50.87 C ANISOU 1489 CD2 LEU B 39 7702 7230 4396 -1917 2489 -463 C ATOM 1490 N ILE B 40 -33.666 -7.684 115.238 1.00 46.37 N ANISOU 1490 N ILE B 40 7236 7291 3092 -1458 1524 -271 N ATOM 1491 CA ILE B 40 -32.356 -7.035 115.223 1.00 49.55 C ANISOU 1491 CA ILE B 40 7606 7852 3371 -1338 1242 -285 C ATOM 1492 C ILE B 40 -31.405 -7.815 114.321 1.00 51.06 C ANISOU 1492 C ILE B 40 7812 7996 3593 -1265 1105 -149 C ATOM 1493 O ILE B 40 -31.304 -9.044 114.453 1.00 60.56 O ANISOU 1493 O ILE B 40 9192 9123 4693 -1266 1192 139 O ATOM 1494 CB ILE B 40 -31.792 -6.898 116.647 1.00 56.17 C ANISOU 1494 CB ILE B 40 8582 8923 3835 -1294 1161 -153 C ATOM 1495 CG1 ILE B 40 -32.765 -6.105 117.524 1.00 59.32 C ANISOU 1495 CG1 ILE B 40 8967 9359 4213 -1393 1309 -302 C ATOM 1496 CG2 ILE B 40 -30.425 -6.227 116.629 1.00 52.28 C ANISOU 1496 CG2 ILE B 40 8008 8608 3249 -1185 877 -234 C ATOM 1497 CD1 ILE B 40 -33.151 -4.763 116.940 1.00 57.73 C ANISOU 1497 CD1 ILE B 40 8566 9074 4294 -1416 1295 -608 C ATOM 1498 N PRO B 41 -30.699 -7.148 113.401 1.00 43.49 N ANISOU 1498 N PRO B 41 6687 7040 2796 -1193 912 -324 N ATOM 1499 CA PRO B 41 -29.763 -7.853 112.513 1.00 40.50 C ANISOU 1499 CA PRO B 41 6305 6634 2450 -1128 754 -215 C ATOM 1500 C PRO B 41 -28.804 -8.748 113.286 1.00 49.99 C ANISOU 1500 C PRO B 41 7688 7982 3324 -1030 604 127 C ATOM 1501 O PRO B 41 -28.397 -8.437 114.405 1.00 51.76 O ANISOU 1501 O PRO B 41 7965 8418 3282 -956 513 178 O ATOM 1502 CB PRO B 41 -29.016 -6.712 111.810 1.00 47.74 C ANISOU 1502 CB PRO B 41 7022 7572 3547 -1044 552 -472 C ATOM 1503 CG PRO B 41 -29.966 -5.574 111.840 1.00 44.32 C ANISOU 1503 CG PRO B 41 6493 7049 3299 -1071 701 -688 C ATOM 1504 CD PRO B 41 -30.748 -5.705 113.122 1.00 46.47 C ANISOU 1504 CD PRO B 41 6893 7404 3360 -1160 857 -603 C ATOM 1505 N THR B 42 -28.447 -9.871 112.668 1.00 51.34 N ANISOU 1505 N THR B 42 7856 7916 3737 -891 547 356 N ATOM 1506 CA THR B 42 -27.689 -10.926 113.324 1.00 62.64 C ANISOU 1506 CA THR B 42 9466 9379 4954 -701 450 753 C ATOM 1507 C THR B 42 -26.181 -10.735 113.217 1.00 68.97 C ANISOU 1507 C THR B 42 10154 10431 5621 -502 65 768 C ATOM 1508 O THR B 42 -25.433 -11.701 113.411 1.00 74.92 O ANISOU 1508 O THR B 42 10998 11176 6291 -267 -55 1094 O ATOM 1509 CB THR B 42 -28.069 -12.286 112.739 1.00 61.66 C ANISOU 1509 CB THR B 42 9418 8836 5175 -648 642 990 C ATOM 1510 OG1 THR B 42 -27.722 -12.321 111.351 1.00 56.17 O ANISOU 1510 OG1 THR B 42 8480 7958 4904 -609 510 825 O ATOM 1511 CG2 THR B 42 -29.560 -12.538 112.901 1.00 65.60 C ANISOU 1511 CG2 THR B 42 10007 9126 5793 -876 1055 929 C ATOM 1512 N ASP B 43 -25.716 -9.515 112.939 1.00 63.80 N ANISOU 1512 N ASP B 43 9309 10000 4934 -585 -101 413 N ATOM 1513 CA ASP B 43 -24.302 -9.299 112.646 1.00 61.35 C ANISOU 1513 CA ASP B 43 8834 9905 4571 -442 -436 336 C ATOM 1514 C ASP B 43 -23.380 -9.641 113.816 1.00 62.55 C ANISOU 1514 C ASP B 43 9060 10305 4402 -220 -614 519 C ATOM 1515 O ASP B 43 -22.159 -9.661 113.629 1.00 58.97 O ANISOU 1515 O ASP B 43 8464 9957 3986 -73 -876 467 O ATOM 1516 CB ASP B 43 -24.092 -7.852 112.193 1.00 59.51 C ANISOU 1516 CB ASP B 43 8399 9635 4577 -554 -453 -118 C ATOM 1517 CG ASP B 43 -24.761 -7.558 110.849 1.00 57.00 C ANISOU 1517 CG ASP B 43 7989 9053 4615 -669 -328 -299 C ATOM 1518 OD1 ASP B 43 -24.108 -6.971 109.965 1.00 56.45 O ANISOU 1518 OD1 ASP B 43 7753 8881 4814 -634 -430 -507 O ATOM 1519 OD2 ASP B 43 -25.940 -7.927 110.674 1.00 46.54 O ANISOU 1519 OD2 ASP B 43 6745 7537 3401 -748 -97 -229 O ATOM 1520 N ASN B 44 -23.916 -9.922 115.007 1.00 73.35 N ANISOU 1520 N ASN B 44 10648 11752 5469 -202 -469 715 N ATOM 1521 CA ASN B 44 -23.077 -10.478 116.063 1.00 81.49 C ANISOU 1521 CA ASN B 44 11789 12994 6179 30 -634 948 C ATOM 1522 C ASN B 44 -23.824 -11.516 116.893 1.00 83.90 C ANISOU 1522 C ASN B 44 12437 13193 6249 112 -407 1379 C ATOM 1523 O ASN B 44 -23.570 -11.657 118.094 1.00 89.68 O ANISOU 1523 O ASN B 44 13309 14116 6649 206 -447 1504 O ATOM 1524 CB ASN B 44 -22.510 -9.389 116.971 1.00 87.30 C ANISOU 1524 CB ASN B 44 12403 14032 6734 -35 -751 636 C ATOM 1525 CG ASN B 44 -21.140 -9.754 117.513 1.00 98.91 C ANISOU 1525 CG ASN B 44 13788 15788 8007 187 -1038 724 C ATOM 1526 OD1 ASN B 44 -20.743 -10.921 117.481 1.00104.38 O ANISOU 1526 OD1 ASN B 44 14577 16445 8639 432 -1128 1086 O ATOM 1527 ND2 ASN B 44 -20.411 -8.762 118.008 1.00101.48 N ANISOU 1527 ND2 ASN B 44 13907 16394 8254 107 -1151 395 N ATOM 1528 N ILE B 45 -24.751 -12.243 116.273 1.00 83.83 N ANISOU 1528 N ILE B 45 12559 12867 6426 50 -132 1602 N ATOM 1529 CA ILE B 45 -25.278 -13.479 116.840 1.00 88.26 C ANISOU 1529 CA ILE B 45 13445 13195 6896 143 131 2063 C ATOM 1530 C ILE B 45 -25.047 -14.675 115.925 1.00 93.72 C ANISOU 1530 C ILE B 45 14189 13508 7911 356 205 2374 C ATOM 1531 O ILE B 45 -25.148 -15.822 116.388 1.00101.56 O ANISOU 1531 O ILE B 45 15426 14248 8916 502 392 2749 O ATOM 1532 CB ILE B 45 -26.780 -13.351 117.196 1.00 85.99 C ANISOU 1532 CB ILE B 45 13315 12753 6603 -155 551 2031 C ATOM 1533 CG1 ILE B 45 -27.229 -14.468 118.144 1.00 92.86 C ANISOU 1533 CG1 ILE B 45 14446 13465 7374 -85 812 2438 C ATOM 1534 CG2 ILE B 45 -27.638 -13.392 115.964 1.00 81.02 C ANISOU 1534 CG2 ILE B 45 12569 11703 6513 -359 773 1818 C ATOM 1535 CD1 ILE B 45 -26.600 -14.403 119.515 1.00100.43 C ANISOU 1535 CD1 ILE B 45 15529 14763 7867 20 610 2555 C ATOM 1536 N ALA B 46 -24.710 -14.449 114.655 1.00 84.10 N ANISOU 1536 N ALA B 46 12703 12147 7106 316 56 2131 N ATOM 1537 CA ALA B 46 -24.318 -15.490 113.717 1.00 74.98 C ANISOU 1537 CA ALA B 46 11535 10602 6352 484 67 2313 C ATOM 1538 C ALA B 46 -22.841 -15.342 113.368 1.00 72.26 C ANISOU 1538 C ALA B 46 10970 10547 5937 751 -374 2286 C ATOM 1539 O ALA B 46 -22.258 -14.259 113.480 1.00 74.17 O ANISOU 1539 O ALA B 46 10988 11222 5971 695 -660 1980 O ATOM 1540 CB ALA B 46 -25.167 -15.433 112.442 1.00 67.95 C ANISOU 1540 CB ALA B 46 10471 9303 6043 199 261 2009 C ATOM 1541 N THR B 47 -22.236 -16.447 112.937 1.00 68.68 N ANISOU 1541 N THR B 47 10580 9843 5673 1030 -394 2584 N ATOM 1542 CA THR B 47 -20.805 -16.508 112.666 1.00 68.84 C ANISOU 1542 CA THR B 47 10380 10096 5679 1289 -790 2555 C ATOM 1543 C THR B 47 -20.569 -16.638 111.168 1.00 65.23 C ANISOU 1543 C THR B 47 9704 9344 5735 1248 -852 2385 C ATOM 1544 O THR B 47 -21.136 -17.525 110.520 1.00 66.39 O ANISOU 1544 O THR B 47 9956 8975 6295 1200 -568 2512 O ATOM 1545 CB THR B 47 -20.149 -17.680 113.401 1.00 73.03 C ANISOU 1545 CB THR B 47 11081 10557 6109 1607 -790 2927 C ATOM 1546 OG1 THR B 47 -20.432 -17.589 114.804 1.00 86.30 O ANISOU 1546 OG1 THR B 47 12952 12474 7363 1613 -715 3053 O ATOM 1547 CG2 THR B 47 -18.639 -17.662 113.190 1.00 61.91 C ANISOU 1547 CG2 THR B 47 9394 9414 4713 1817 -1183 2800 C ATOM 1548 N GLY B 48 -19.730 -15.766 110.632 1.00 48.40 N ANISOU 1548 N GLY B 48 7250 7514 3627 1209 -1190 2035 N ATOM 1549 CA GLY B 48 -19.388 -15.799 109.215 1.00 44.54 C ANISOU 1549 CA GLY B 48 6518 6765 3638 1139 -1276 1808 C ATOM 1550 C GLY B 48 -20.342 -14.989 108.359 1.00 47.72 C ANISOU 1550 C GLY B 48 6792 6964 4376 757 -1115 1421 C ATOM 1551 O GLY B 48 -21.520 -14.814 108.669 1.00 45.97 O ANISOU 1551 O GLY B 48 6703 6616 4147 552 -837 1397 O ATOM 1552 N ALA B 49 -19.816 -14.493 107.239 1.00 37.00 N ANISOU 1552 N ALA B 49 5166 5586 3305 685 -1285 1113 N ATOM 1553 CA ALA B 49 -20.604 -13.614 106.385 1.00 38.63 C ANISOU 1553 CA ALA B 49 5241 5660 3775 395 -1161 749 C ATOM 1554 C ALA B 49 -21.789 -14.338 105.751 1.00 42.95 C ANISOU 1554 C ALA B 49 5847 5777 4694 276 -838 804 C ATOM 1555 O ALA B 49 -22.832 -13.719 105.513 1.00 36.79 O ANISOU 1555 O ALA B 49 5036 4950 3994 65 -654 587 O ATOM 1556 CB ALA B 49 -19.717 -12.996 105.301 1.00 38.56 C ANISOU 1556 CB ALA B 49 4966 5707 3978 377 -1387 441 C ATOM 1557 N VAL B 50 -21.656 -15.636 105.469 1.00 41.80 N ANISOU 1557 N VAL B 50 5772 5332 4778 409 -745 1065 N ATOM 1558 CA VAL B 50 -22.733 -16.353 104.788 1.00 33.97 C ANISOU 1558 CA VAL B 50 4789 3949 4168 251 -409 1038 C ATOM 1559 C VAL B 50 -23.946 -16.492 105.702 1.00 35.82 C ANISOU 1559 C VAL B 50 5248 4127 4236 106 -76 1139 C ATOM 1560 O VAL B 50 -25.079 -16.194 105.309 1.00 39.30 O ANISOU 1560 O VAL B 50 5603 4493 4835 -127 146 897 O ATOM 1561 CB VAL B 50 -22.240 -17.726 104.294 1.00 37.33 C ANISOU 1561 CB VAL B 50 5253 4036 4894 409 -337 1271 C ATOM 1562 CG1 VAL B 50 -23.393 -18.522 103.711 1.00 43.39 C ANISOU 1562 CG1 VAL B 50 6031 4417 6036 198 72 1203 C ATOM 1563 CG2 VAL B 50 -21.137 -17.557 103.254 1.00 42.30 C ANISOU 1563 CG2 VAL B 50 5624 4713 5734 513 -647 1112 C ATOM 1564 N ASN B 51 -23.734 -16.951 106.936 1.00 39.41 N ANISOU 1564 N ASN B 51 5983 4644 4348 259 -29 1492 N ATOM 1565 CA ASN B 51 -24.874 -17.160 107.821 1.00 42.71 C ANISOU 1565 CA ASN B 51 6641 4979 4609 112 324 1602 C ATOM 1566 C ASN B 51 -25.438 -15.847 108.351 1.00 38.79 C ANISOU 1566 C ASN B 51 6091 4819 3830 -63 274 1352 C ATOM 1567 O ASN B 51 -26.639 -15.766 108.627 1.00 41.01 O ANISOU 1567 O ASN B 51 6442 5022 4120 -278 578 1259 O ATOM 1568 CB ASN B 51 -24.490 -18.094 108.968 1.00 52.38 C ANISOU 1568 CB ASN B 51 8222 6148 5533 363 427 2094 C ATOM 1569 CG ASN B 51 -24.447 -19.551 108.535 1.00 68.25 C ANISOU 1569 CG ASN B 51 10382 7668 7882 466 705 2354 C ATOM 1570 OD1 ASN B 51 -25.321 -20.019 107.800 1.00 77.54 O ANISOU 1570 OD1 ASN B 51 11500 8498 9465 218 1032 2177 O ATOM 1571 ND2 ASN B 51 -23.433 -20.274 108.989 1.00 72.24 N ANISOU 1571 ND2 ASN B 51 11071 8161 8215 842 593 2757 N ATOM 1572 N ILE B 52 -24.602 -14.813 108.491 1.00 39.16 N ANISOU 1572 N ILE B 52 6009 5234 3637 11 -72 1210 N ATOM 1573 CA ILE B 52 -25.125 -13.493 108.843 1.00 36.86 C ANISOU 1573 CA ILE B 52 5654 5213 3138 -173 -81 920 C ATOM 1574 C ILE B 52 -26.067 -12.998 107.759 1.00 32.30 C ANISOU 1574 C ILE B 52 4878 4479 2916 -370 68 578 C ATOM 1575 O ILE B 52 -27.169 -12.513 108.044 1.00 32.11 O ANISOU 1575 O ILE B 52 4878 4486 2837 -542 286 430 O ATOM 1576 CB ILE B 52 -23.979 -12.491 109.079 1.00 38.17 C ANISOU 1576 CB ILE B 52 5702 5771 3031 -90 -432 772 C ATOM 1577 CG1 ILE B 52 -23.210 -12.835 110.352 1.00 41.27 C ANISOU 1577 CG1 ILE B 52 6263 6463 2956 111 -575 1066 C ATOM 1578 CG2 ILE B 52 -24.514 -11.073 109.196 1.00 35.28 C ANISOU 1578 CG2 ILE B 52 5261 5596 2548 -298 -385 419 C ATOM 1579 CD1 ILE B 52 -21.879 -12.129 110.429 1.00 47.83 C ANISOU 1579 CD1 ILE B 52 6910 7697 3566 217 -939 898 C ATOM 1580 N ARG B 53 -25.657 -13.123 106.497 1.00 33.17 N ANISOU 1580 N ARG B 53 4779 4449 3376 -326 -48 445 N ATOM 1581 CA ARG B 53 -26.519 -12.677 105.407 1.00 27.08 C ANISOU 1581 CA ARG B 53 3799 3586 2903 -455 75 129 C ATOM 1582 C ARG B 53 -27.818 -13.476 105.371 1.00 31.88 C ANISOU 1582 C ARG B 53 4433 3989 3689 -603 435 131 C ATOM 1583 O ARG B 53 -28.907 -12.900 105.253 1.00 33.80 O ANISOU 1583 O ARG B 53 4588 4310 3944 -734 609 -105 O ATOM 1584 CB ARG B 53 -25.772 -12.784 104.077 1.00 24.04 C ANISOU 1584 CB ARG B 53 3197 3102 2837 -364 -112 13 C ATOM 1585 CG ARG B 53 -26.633 -12.413 102.843 1.00 28.39 C ANISOU 1585 CG ARG B 53 3513 3598 3675 -442 4 -298 C ATOM 1586 CD ARG B 53 -25.782 -12.415 101.587 1.00 28.35 C ANISOU 1586 CD ARG B 53 3313 3529 3928 -342 -197 -406 C ATOM 1587 NE ARG B 53 -26.562 -12.048 100.396 1.00 26.46 N ANISOU 1587 NE ARG B 53 2847 3297 3910 -367 -102 -687 N ATOM 1588 CZ ARG B 53 -27.287 -12.902 99.682 1.00 30.07 C ANISOU 1588 CZ ARG B 53 3148 3637 4642 -432 70 -772 C ATOM 1589 NH1 ARG B 53 -27.356 -14.187 100.026 1.00 32.39 N ANISOU 1589 NH1 ARG B 53 3520 3721 5064 -508 216 -594 N ATOM 1590 NH2 ARG B 53 -27.953 -12.465 98.619 1.00 31.06 N ANISOU 1590 NH2 ARG B 53 3095 3865 4839 -366 129 -996 N ATOM 1591 N ASN B 54 -27.726 -14.802 105.512 1.00 32.44 N ANISOU 1591 N ASN B 54 4236 4739 3349 -1075 -413 922 N ATOM 1592 CA ASN B 54 -28.914 -15.641 105.431 1.00 32.78 C ANISOU 1592 CA ASN B 54 4353 4730 3374 -1284 -331 1003 C ATOM 1593 C ASN B 54 -29.888 -15.350 106.565 1.00 32.19 C ANISOU 1593 C ASN B 54 4291 4837 3102 -1503 -166 1043 C ATOM 1594 O ASN B 54 -31.102 -15.282 106.345 1.00 39.82 O ANISOU 1594 O ASN B 54 5136 5908 4083 -1663 -7 999 O ATOM 1595 CB ASN B 54 -28.517 -17.115 105.432 1.00 39.88 C ANISOU 1595 CB ASN B 54 5513 5368 4271 -1299 -493 1156 C ATOM 1596 CG ASN B 54 -27.822 -17.531 104.155 1.00 47.19 C ANISOU 1596 CG ASN B 54 6409 6122 5401 -1099 -622 1090 C ATOM 1597 OD1 ASN B 54 -28.095 -16.990 103.082 1.00 49.66 O ANISOU 1597 OD1 ASN B 54 6524 6489 5855 -1041 -551 955 O ATOM 1598 ND2 ASN B 54 -26.922 -18.503 104.261 1.00 54.65 N ANISOU 1598 ND2 ASN B 54 7561 6858 6344 -977 -816 1180 N ATOM 1599 N LYS B 55 -29.383 -15.185 107.789 1.00 38.56 N ANISOU 1599 N LYS B 55 5232 5705 3714 -1510 -200 1115 N ATOM 1600 CA LYS B 55 -30.294 -14.936 108.900 1.00 44.11 C ANISOU 1600 CA LYS B 55 5964 6596 4200 -1722 -25 1149 C ATOM 1601 C LYS B 55 -30.926 -13.551 108.796 1.00 39.62 C ANISOU 1601 C LYS B 55 5125 6274 3655 -1686 150 953 C ATOM 1602 O LYS B 55 -32.100 -13.374 109.144 1.00 40.06 O ANISOU 1602 O LYS B 55 5087 6506 3627 -1856 345 917 O ATOM 1603 CB LYS B 55 -29.568 -15.136 110.229 1.00 40.19 C ANISOU 1603 CB LYS B 55 5715 6095 3460 -1726 -124 1275 C ATOM 1604 CG LYS B 55 -29.605 -16.594 110.671 1.00 45.25 C ANISOU 1604 CG LYS B 55 6683 6527 3983 -1876 -212 1504 C ATOM 1605 CD LYS B 55 -28.853 -16.834 111.971 1.00 59.75 C ANISOU 1605 CD LYS B 55 8769 8323 5609 -1812 -341 1598 C ATOM 1606 CE LYS B 55 -27.743 -17.853 111.770 1.00 59.32 C ANISOU 1606 CE LYS B 55 8953 7991 5595 -1643 -627 1727 C ATOM 1607 NZ LYS B 55 -28.188 -19.224 112.143 1.00 59.68 N ANISOU 1607 NZ LYS B 55 9281 7802 5592 -1776 -636 1872 N ATOM 1608 N ASN B 56 -30.179 -12.565 108.292 1.00 35.95 N ANISOU 1608 N ASN B 56 4532 5823 3306 -1466 87 817 N ATOM 1609 CA ASN B 56 -30.754 -11.244 108.064 1.00 32.00 C ANISOU 1609 CA ASN B 56 3816 5500 2843 -1402 229 629 C ATOM 1610 C ASN B 56 -31.841 -11.303 107.001 1.00 32.04 C ANISOU 1610 C ASN B 56 3642 5528 3003 -1432 326 555 C ATOM 1611 O ASN B 56 -32.925 -10.730 107.176 1.00 35.95 O ANISOU 1611 O ASN B 56 3987 6215 3457 -1486 489 450 O ATOM 1612 CB ASN B 56 -29.670 -10.256 107.648 1.00 29.96 C ANISOU 1612 CB ASN B 56 3501 5202 2681 -1192 132 517 C ATOM 1613 CG ASN B 56 -28.786 -9.830 108.816 1.00 36.42 C ANISOU 1613 CG ASN B 56 4433 6076 3330 -1169 60 524 C ATOM 1614 OD1 ASN B 56 -29.036 -10.180 109.968 1.00 37.58 O ANISOU 1614 OD1 ASN B 56 4712 6303 3263 -1291 89 609 O ATOM 1615 ND2 ASN B 56 -27.749 -9.075 108.516 1.00 32.11 N ANISOU 1615 ND2 ASN B 56 3840 5494 2867 -1029 -34 431 N ATOM 1616 N ILE B 57 -31.578 -12.018 105.902 1.00 35.36 N ANISOU 1616 N ILE B 57 4072 5768 3596 -1386 219 593 N ATOM 1617 CA ILE B 57 -32.598 -12.210 104.871 1.00 29.33 C ANISOU 1617 CA ILE B 57 3156 5019 2969 -1423 279 524 C ATOM 1618 C ILE B 57 -33.819 -12.923 105.442 1.00 38.50 C ANISOU 1618 C ILE B 57 4299 6294 4036 -1688 409 580 C ATOM 1619 O ILE B 57 -34.960 -12.551 105.149 1.00 37.78 O ANISOU 1619 O ILE B 57 4033 6318 4004 -1666 498 437 O ATOM 1620 CB ILE B 57 -32.003 -12.966 103.665 1.00 30.37 C ANISOU 1620 CB ILE B 57 3344 4923 3272 -1334 129 559 C ATOM 1621 CG1 ILE B 57 -31.175 -12.008 102.804 1.00 30.22 C ANISOU 1621 CG1 ILE B 57 3253 4865 3365 -1093 72 449 C ATOM 1622 CG2 ILE B 57 -33.101 -13.650 102.840 1.00 34.18 C ANISOU 1622 CG2 ILE B 57 3740 5393 3853 -1454 161 536 C ATOM 1623 CD1 ILE B 57 -30.453 -12.670 101.646 1.00 35.34 C ANISOU 1623 CD1 ILE B 57 3954 5315 4157 -985 -58 465 C ATOM 1624 N ASP B 58 -33.603 -13.960 106.258 1.00 40.74 N ANISOU 1624 N ASP B 58 4805 6481 4194 -1861 379 754 N ATOM 1625 CA ASP B 58 -34.720 -14.639 106.912 1.00 45.82 C ANISOU 1625 CA ASP B 58 5482 7164 4763 -2051 482 769 C ATOM 1626 C ASP B 58 -35.585 -13.661 107.697 1.00 45.20 C ANISOU 1626 C ASP B 58 5246 7334 4594 -2026 644 622 C ATOM 1627 O ASP B 58 -36.818 -13.737 107.652 1.00 51.44 O ANISOU 1627 O ASP B 58 5891 8236 5418 -2103 752 528 O ATOM 1628 CB ASP B 58 -34.199 -15.736 107.843 1.00 46.86 C ANISOU 1628 CB ASP B 58 5930 7136 4739 -2203 415 980 C ATOM 1629 CG ASP B 58 -33.793 -16.988 107.099 1.00 55.24 C ANISOU 1629 CG ASP B 58 7174 7916 5900 -2264 266 1114 C ATOM 1630 OD1 ASP B 58 -34.179 -17.127 105.921 1.00 60.03 O ANISOU 1630 OD1 ASP B 58 7639 8479 6689 -2247 248 1032 O ATOM 1631 OD2 ASP B 58 -33.081 -17.831 107.686 1.00 58.26 O ANISOU 1631 OD2 ASP B 58 7856 8105 6175 -2302 148 1291 O ATOM 1632 N MET B 59 -34.954 -12.733 108.424 1.00 41.23 N ANISOU 1632 N MET B 59 4770 6922 3974 -1917 654 593 N ATOM 1633 CA MET B 59 -35.718 -11.772 109.212 1.00 39.46 C ANISOU 1633 CA MET B 59 4422 6912 3659 -1878 797 446 C ATOM 1634 C MET B 59 -36.497 -10.807 108.320 1.00 40.23 C ANISOU 1634 C MET B 59 4258 7115 3911 -1710 843 241 C ATOM 1635 O MET B 59 -37.622 -10.419 108.650 1.00 41.90 O ANISOU 1635 O MET B 59 4326 7491 4104 -1717 961 119 O ATOM 1636 CB MET B 59 -34.781 -11.025 110.165 1.00 39.43 C ANISOU 1636 CB MET B 59 4537 6952 3492 -1797 775 455 C ATOM 1637 CG MET B 59 -34.161 -11.946 111.215 1.00 42.44 C ANISOU 1637 CG MET B 59 5197 7245 3684 -1942 720 652 C ATOM 1638 SD MET B 59 -32.949 -11.165 112.293 1.00 51.47 S ANISOU 1638 SD MET B 59 6499 8431 4624 -1835 641 662 S ATOM 1639 CE MET B 59 -33.574 -9.537 112.348 1.00 40.12 C ANISOU 1639 CE MET B 59 4830 7198 3218 -1685 778 399 C ATOM 1640 N ILE B 60 -35.927 -10.413 107.184 1.00 35.18 N ANISOU 1640 N ILE B 60 3563 6385 3418 -1551 744 202 N ATOM 1641 CA ILE B 60 -36.653 -9.536 106.271 1.00 32.85 C ANISOU 1641 CA ILE B 60 3065 6158 3260 -1374 761 22 C ATOM 1642 C ILE B 60 -37.867 -10.255 105.697 1.00 34.15 C ANISOU 1642 C ILE B 60 3102 6354 3519 -1466 788 -10 C ATOM 1643 O ILE B 60 -38.954 -9.675 105.587 1.00 41.87 O ANISOU 1643 O ILE B 60 3902 7480 4526 -1392 854 -160 O ATOM 1644 CB ILE B 60 -35.712 -9.024 105.168 1.00 37.00 C ANISOU 1644 CB ILE B 60 3592 6558 3907 -1198 649 4 C ATOM 1645 CG1 ILE B 60 -34.528 -8.301 105.810 1.00 31.51 C ANISOU 1645 CG1 ILE B 60 3008 5855 3109 -1135 631 23 C ATOM 1646 CG2 ILE B 60 -36.468 -8.122 104.193 1.00 38.93 C ANISOU 1646 CG2 ILE B 60 3672 6848 4271 -1001 648 -168 C ATOM 1647 CD1 ILE B 60 -33.375 -8.088 104.869 1.00 31.77 C ANISOU 1647 CD1 ILE B 60 3088 5727 3255 -1013 511 45 C ATOM 1648 N ARG B 61 -37.712 -11.536 105.346 1.00 36.44 N ANISOU 1648 N ARG B 61 3484 6508 3852 -1632 732 124 N ATOM 1649 CA ARG B 61 -38.858 -12.303 104.859 1.00 40.09 C ANISOU 1649 CA ARG B 61 3838 6999 4397 -1757 758 91 C ATOM 1650 C ARG B 61 -39.941 -12.434 105.923 1.00 46.97 C ANISOU 1650 C ARG B 61 4641 8053 5153 -1915 910 56 C ATOM 1651 O ARG B 61 -41.134 -12.473 105.597 1.00 52.56 O ANISOU 1651 O ARG B 61 5158 8889 5924 -1948 965 -57 O ATOM 1652 CB ARG B 61 -38.420 -13.696 104.407 1.00 40.78 C ANISOU 1652 CB ARG B 61 4084 6875 4536 -1927 667 246 C ATOM 1653 CG ARG B 61 -37.562 -13.698 103.168 1.00 45.43 C ANISOU 1653 CG ARG B 61 4698 7299 5264 -1786 521 256 C ATOM 1654 CD ARG B 61 -37.339 -15.102 102.645 1.00 57.88 C ANISOU 1654 CD ARG B 61 6419 8665 6906 -1952 425 378 C ATOM 1655 NE ARG B 61 -36.818 -15.063 101.281 1.00 66.97 N ANISOU 1655 NE ARG B 61 7540 9696 8209 -1812 294 337 N ATOM 1656 CZ ARG B 61 -37.568 -14.875 100.199 1.00 76.38 C ANISOU 1656 CZ ARG B 61 8564 10934 9524 -1730 264 198 C ATOM 1657 NH1 ARG B 61 -38.882 -14.721 100.314 1.00 81.07 N ANISOU 1657 NH1 ARG B 61 8987 11695 10122 -1775 350 89 N ATOM 1658 NH2 ARG B 61 -37.003 -14.846 98.999 1.00 73.42 N ANISOU 1658 NH2 ARG B 61 8191 10447 9260 -1602 139 165 N ATOM 1659 N ALA B 62 -39.547 -12.514 107.192 1.00 48.81 N ANISOU 1659 N ALA B 62 5024 8309 5211 -2017 977 147 N ATOM 1660 CA ALA B 62 -40.505 -12.701 108.272 1.00 49.23 C ANISOU 1660 CA ALA B 62 5037 8534 5135 -2188 1134 127 C ATOM 1661 C ALA B 62 -41.151 -11.400 108.728 1.00 52.70 C ANISOU 1661 C ALA B 62 5287 9206 5531 -2029 1236 -60 C ATOM 1662 O ALA B 62 -42.232 -11.441 109.320 1.00 52.91 O ANISOU 1662 O ALA B 62 5186 9419 5497 -2138 1374 -134 O ATOM 1663 CB ALA B 62 -39.824 -13.375 109.466 1.00 49.72 C ANISOU 1663 CB ALA B 62 5372 8513 5006 -2362 1157 312 C ATOM 1664 N CYS B 63 -40.528 -10.254 108.467 1.00 48.58 N ANISOU 1664 N CYS B 63 4746 8674 5036 -1778 1175 -144 N ATOM 1665 CA CYS B 63 -41.011 -9.014 109.057 1.00 49.41 C ANISOU 1665 CA CYS B 63 4730 8966 5077 -1625 1263 -312 C ATOM 1666 C CYS B 63 -42.312 -8.553 108.402 1.00 45.72 C ANISOU 1666 C CYS B 63 3992 8657 4723 -1520 1297 -498 C ATOM 1667 O CYS B 63 -42.703 -9.009 107.322 1.00 52.23 O ANISOU 1667 O CYS B 63 4721 9433 5690 -1521 1225 -510 O ATOM 1668 CB CYS B 63 -39.946 -7.917 108.955 1.00 44.56 C ANISOU 1668 CB CYS B 63 4202 8271 4458 -1399 1182 -351 C ATOM 1669 SG CYS B 63 -39.773 -7.143 107.332 1.00 42.18 S ANISOU 1669 SG CYS B 63 3797 7867 4361 -1132 1048 -457 S ATOM 1670 N ASP B 64 -43.004 -7.652 109.101 1.00 50.89 N ANISOU 1670 N ASP B 64 4524 9510 5302 -1426 1403 -649 N ATOM 1671 CA ASP B 64 -44.145 -6.924 108.560 1.00 55.17 C ANISOU 1671 CA ASP B 64 4810 10217 5935 -1255 1415 -854 C ATOM 1672 C ASP B 64 -43.716 -5.605 107.929 1.00 53.70 C ANISOU 1672 C ASP B 64 4627 9959 5816 -929 1308 -970 C ATOM 1673 O ASP B 64 -44.265 -5.196 106.900 1.00 51.27 O ANISOU 1673 O ASP B 64 4180 9665 5633 -755 1224 -1083 O ATOM 1674 CB ASP B 64 -45.185 -6.664 109.661 1.00 61.01 C ANISOU 1674 CB ASP B 64 5405 11221 6555 -1318 1591 -970 C ATOM 1675 CG ASP B 64 -45.761 -7.946 110.251 1.00 58.75 C ANISOU 1675 CG ASP B 64 5104 11021 6198 -1658 1716 -868 C ATOM 1676 OD1 ASP B 64 -45.369 -8.332 111.372 1.00 59.88 O ANISOU 1676 OD1 ASP B 64 5412 11162 6176 -1831 1814 -754 O ATOM 1677 OD2 ASP B 64 -46.613 -8.569 109.591 1.00 65.26 O ANISOU 1677 OD2 ASP B 64 5761 11911 7125 -1757 1715 -902 O ATOM 1678 N ALA B 65 -42.737 -4.933 108.528 1.00 49.94 N ANISOU 1678 N ALA B 65 4324 9399 5250 -847 1304 -945 N ATOM 1679 CA ALA B 65 -42.212 -3.685 108.002 1.00 46.74 C ANISOU 1679 CA ALA B 65 3967 8895 4896 -564 1211 -1042 C ATOM 1680 C ALA B 65 -40.722 -3.607 108.296 1.00 41.15 C ANISOU 1680 C ALA B 65 3498 8010 4126 -591 1164 -920 C ATOM 1681 O ALA B 65 -40.187 -4.345 109.129 1.00 41.66 O ANISOU 1681 O ALA B 65 3686 8064 4080 -795 1208 -784 O ATOM 1682 CB ALA B 65 -42.927 -2.465 108.596 1.00 45.04 C ANISOU 1682 CB ALA B 65 3659 8832 4624 -365 1281 -1242 C ATOM 1683 N ILE B 66 -40.053 -2.708 107.584 1.00 40.45 N ANISOU 1683 N ILE B 66 3482 7783 4104 -384 1068 -971 N ATOM 1684 CA ILE B 66 -38.643 -2.411 107.794 1.00 37.08 C ANISOU 1684 CA ILE B 66 3259 7205 3624 -383 1021 -898 C ATOM 1685 C ILE B 66 -38.535 -0.928 108.118 1.00 37.61 C ANISOU 1685 C ILE B 66 3389 7256 3644 -162 1031 -1061 C ATOM 1686 O ILE B 66 -39.167 -0.097 107.457 1.00 37.50 O ANISOU 1686 O ILE B 66 3304 7233 3713 58 998 -1197 O ATOM 1687 CB ILE B 66 -37.787 -2.796 106.565 1.00 35.65 C ANISOU 1687 CB ILE B 66 3136 6844 3567 -373 903 -798 C ATOM 1688 CG1 ILE B 66 -36.319 -2.421 106.768 1.00 33.24 C ANISOU 1688 CG1 ILE B 66 3017 6408 3205 -375 860 -745 C ATOM 1689 CG2 ILE B 66 -38.328 -2.169 105.274 1.00 35.07 C ANISOU 1689 CG2 ILE B 66 2972 6721 3633 -151 831 -906 C ATOM 1690 CD1 ILE B 66 -35.399 -2.941 105.635 1.00 30.38 C ANISOU 1690 CD1 ILE B 66 2699 5889 2955 -396 762 -634 C ATOM 1691 N ILE B 67 -37.800 -0.604 109.177 1.00 34.58 N ANISOU 1691 N ILE B 67 3156 6865 3119 -216 1067 -1054 N ATOM 1692 CA ILE B 67 -37.401 0.769 109.450 1.00 39.31 C ANISOU 1692 CA ILE B 67 3882 7384 3670 -32 1055 -1196 C ATOM 1693 C ILE B 67 -35.910 0.848 109.171 1.00 34.67 C ANISOU 1693 C ILE B 67 3477 6620 3077 -81 966 -1120 C ATOM 1694 O ILE B 67 -35.098 0.263 109.900 1.00 39.23 O ANISOU 1694 O ILE B 67 4148 7212 3547 -259 959 -1012 O ATOM 1695 CB ILE B 67 -37.729 1.201 110.883 1.00 35.76 C ANISOU 1695 CB ILE B 67 3471 7063 3052 -47 1158 -1282 C ATOM 1696 CG1 ILE B 67 -39.248 1.253 111.068 1.00 38.10 C ANISOU 1696 CG1 ILE B 67 3561 7552 3364 23 1254 -1390 C ATOM 1697 CG2 ILE B 67 -37.124 2.562 111.156 1.00 44.30 C ANISOU 1697 CG2 ILE B 67 4738 8012 4082 119 1123 -1420 C ATOM 1698 CD1 ILE B 67 -39.715 1.667 112.470 1.00 42.99 C ANISOU 1698 CD1 ILE B 67 4196 8326 3811 18 1382 -1489 C ATOM 1699 N ALA B 68 -35.555 1.556 108.106 1.00 35.97 N ANISOU 1699 N ALA B 68 3700 6620 3348 75 891 -1178 N ATOM 1700 CA ALA B 68 -34.184 1.641 107.629 1.00 31.58 C ANISOU 1700 CA ALA B 68 3292 5900 2805 22 813 -1123 C ATOM 1701 C ALA B 68 -33.603 3.004 107.971 1.00 35.23 C ANISOU 1701 C ALA B 68 3955 6224 3205 125 788 -1270 C ATOM 1702 O ALA B 68 -34.188 4.037 107.635 1.00 33.77 O ANISOU 1702 O ALA B 68 3821 5947 3062 334 785 -1404 O ATOM 1703 CB ALA B 68 -34.109 1.402 106.117 1.00 29.10 C ANISOU 1703 CB ALA B 68 2936 5469 2651 91 749 -1072 C ATOM 1704 N ASP B 69 -32.460 2.996 108.645 1.00 36.58 N ANISOU 1704 N ASP B 69 4255 6366 3277 -26 752 -1244 N ATOM 1705 CA ASP B 69 -31.689 4.206 108.921 1.00 29.38 C ANISOU 1705 CA ASP B 69 3556 5279 2329 7 697 -1365 C ATOM 1706 C ASP B 69 -30.839 4.523 107.688 1.00 31.87 C ANISOU 1706 C ASP B 69 3969 5321 2818 2 597 -1296 C ATOM 1707 O ASP B 69 -29.796 3.906 107.467 1.00 29.31 O ANISOU 1707 O ASP B 69 3638 4943 2554 -160 525 -1161 O ATOM 1708 CB ASP B 69 -30.823 3.984 110.158 1.00 33.38 C ANISOU 1708 CB ASP B 69 4137 5867 2680 -173 665 -1346 C ATOM 1709 CG ASP B 69 -30.026 5.196 110.544 1.00 40.65 C ANISOU 1709 CG ASP B 69 5267 6624 3554 -176 602 -1491 C ATOM 1710 OD1 ASP B 69 -29.282 5.109 111.548 1.00 43.59 O ANISOU 1710 OD1 ASP B 69 5704 7060 3797 -313 549 -1497 O ATOM 1711 OD2 ASP B 69 -30.142 6.234 109.866 1.00 36.06 O ANISOU 1711 OD2 ASP B 69 4802 5840 3058 -46 593 -1598 O ATOM 1712 N LEU B 70 -31.282 5.485 106.872 1.00 32.08 N ANISOU 1712 N LEU B 70 4095 5178 2917 188 593 -1393 N ATOM 1713 CA LEU B 70 -30.547 5.928 105.693 1.00 30.77 C ANISOU 1713 CA LEU B 70 4069 4741 2882 178 523 -1333 C ATOM 1714 C LEU B 70 -29.693 7.172 105.963 1.00 33.23 C ANISOU 1714 C LEU B 70 4638 4829 3158 125 487 -1441 C ATOM 1715 O LEU B 70 -29.392 7.941 105.044 1.00 33.20 O ANISOU 1715 O LEU B 70 4818 4568 3228 161 457 -1445 O ATOM 1716 CB LEU B 70 -31.518 6.165 104.530 1.00 31.81 C ANISOU 1716 CB LEU B 70 4193 4794 3098 405 520 -1346 C ATOM 1717 CG LEU B 70 -32.283 4.915 104.081 1.00 32.55 C ANISOU 1717 CG LEU B 70 4030 5086 3250 422 539 -1242 C ATOM 1718 CD1 LEU B 70 -33.222 5.192 102.882 1.00 28.52 C ANISOU 1718 CD1 LEU B 70 3510 4507 2820 659 504 -1272 C ATOM 1719 CD2 LEU B 70 -31.321 3.782 103.738 1.00 30.28 C ANISOU 1719 CD2 LEU B 70 3670 4800 3035 205 504 -1053 C ATOM 1720 N SER B 71 -29.285 7.371 107.209 1.00 31.30 N ANISOU 1720 N SER B 71 4429 4672 2792 20 487 -1527 N ATOM 1721 CA SER B 71 -28.397 8.471 107.551 1.00 36.65 C ANISOU 1721 CA SER B 71 5340 5149 3436 -79 440 -1640 C ATOM 1722 C SER B 71 -27.072 8.340 106.798 1.00 34.02 C ANISOU 1722 C SER B 71 5032 4669 3224 -297 384 -1523 C ATOM 1723 O SER B 71 -26.670 7.232 106.427 1.00 36.52 O ANISOU 1723 O SER B 71 5159 5102 3613 -388 369 -1366 O ATOM 1724 CB SER B 71 -28.140 8.485 109.053 1.00 37.71 C ANISOU 1724 CB SER B 71 5473 5451 3403 -173 432 -1744 C ATOM 1725 OG SER B 71 -29.300 8.885 109.759 1.00 39.91 O ANISOU 1725 OG SER B 71 5770 5842 3551 28 507 -1898 O ATOM 1726 N PRO B 72 -26.370 9.451 106.566 1.00 35.22 N ANISOU 1726 N PRO B 72 5417 4567 3397 -390 359 -1605 N ATOM 1727 CA PRO B 72 -25.063 9.365 105.903 1.00 36.28 C ANISOU 1727 CA PRO B 72 5547 4598 3639 -633 331 -1515 C ATOM 1728 C PRO B 72 -24.139 8.405 106.637 1.00 37.59 C ANISOU 1728 C PRO B 72 5484 5002 3796 -818 271 -1463 C ATOM 1729 O PRO B 72 -24.046 8.413 107.871 1.00 38.91 O ANISOU 1729 O PRO B 72 5636 5306 3842 -856 225 -1556 O ATOM 1730 CB PRO B 72 -24.534 10.804 105.960 1.00 42.31 C ANISOU 1730 CB PRO B 72 6614 5079 4382 -743 319 -1656 C ATOM 1731 CG PRO B 72 -25.721 11.658 106.270 1.00 53.45 C ANISOU 1731 CG PRO B 72 8230 6378 5702 -480 336 -1794 C ATOM 1732 CD PRO B 72 -26.646 10.809 107.065 1.00 42.23 C ANISOU 1732 CD PRO B 72 6582 5267 4198 -311 355 -1802 C ATOM 1733 N PHE B 73 -23.459 7.566 105.863 1.00 35.49 N ANISOU 1733 N PHE B 73 5053 4785 3645 -914 264 -1321 N ATOM 1734 CA PHE B 73 -22.550 6.557 106.391 1.00 31.97 C ANISOU 1734 CA PHE B 73 4384 4553 3211 -1045 185 -1261 C ATOM 1735 C PHE B 73 -21.240 6.641 105.619 1.00 32.66 C ANISOU 1735 C PHE B 73 4411 4574 3425 -1246 176 -1238 C ATOM 1736 O PHE B 73 -21.190 6.262 104.442 1.00 36.39 O ANISOU 1736 O PHE B 73 4834 4989 4002 -1223 234 -1131 O ATOM 1737 CB PHE B 73 -23.158 5.158 106.289 1.00 33.31 C ANISOU 1737 CB PHE B 73 4366 4900 3389 -918 183 -1111 C ATOM 1738 CG PHE B 73 -22.239 4.069 106.748 1.00 34.66 C ANISOU 1738 CG PHE B 73 4346 5253 3571 -1013 82 -1036 C ATOM 1739 CD1 PHE B 73 -21.931 3.926 108.091 1.00 35.91 C ANISOU 1739 CD1 PHE B 73 4488 5560 3594 -1066 -12 -1091 C ATOM 1740 CD2 PHE B 73 -21.654 3.206 105.832 1.00 33.42 C ANISOU 1740 CD2 PHE B 73 4040 5112 3545 -1031 68 -921 C ATOM 1741 CE1 PHE B 73 -21.082 2.922 108.526 1.00 35.36 C ANISOU 1741 CE1 PHE B 73 4265 5648 3522 -1118 -137 -1020 C ATOM 1742 CE2 PHE B 73 -20.794 2.197 106.252 1.00 35.29 C ANISOU 1742 CE2 PHE B 73 4109 5506 3795 -1076 -47 -864 C ATOM 1743 CZ PHE B 73 -20.510 2.055 107.608 1.00 34.77 C ANISOU 1743 CZ PHE B 73 4036 5580 3594 -1113 -160 -909 C ATOM 1744 N ARG B 74 -20.198 7.148 106.287 1.00 43.15 N ANISOU 1744 N ARG B 74 5734 5925 4735 -1448 107 -1353 N ATOM 1745 CA ARG B 74 -18.832 7.232 105.764 1.00 49.82 C ANISOU 1745 CA ARG B 74 6463 6771 5694 -1680 98 -1369 C ATOM 1746 C ARG B 74 -18.687 8.243 104.632 1.00 53.81 C ANISOU 1746 C ARG B 74 7164 7011 6270 -1795 222 -1380 C ATOM 1747 O ARG B 74 -17.569 8.594 104.242 1.00 64.45 O ANISOU 1747 O ARG B 74 8457 8337 7695 -2042 248 -1424 O ATOM 1748 CB ARG B 74 -18.354 5.860 105.300 1.00 50.47 C ANISOU 1748 CB ARG B 74 6265 7044 5869 -1636 66 -1238 C ATOM 1749 CG ARG B 74 -18.103 4.903 106.439 1.00 47.74 C ANISOU 1749 CG ARG B 74 5745 6942 5453 -1582 -87 -1230 C ATOM 1750 CD ARG B 74 -17.049 3.925 106.044 1.00 38.42 C ANISOU 1750 CD ARG B 74 4294 5919 4384 -1618 -153 -1177 C ATOM 1751 NE ARG B 74 -16.927 2.832 106.991 1.00 40.10 N ANISOU 1751 NE ARG B 74 4379 6333 4526 -1510 -314 -1128 N ATOM 1752 CZ ARG B 74 -16.208 2.919 108.099 1.00 37.29 C ANISOU 1752 CZ ARG B 74 3971 6100 4099 -1564 -462 -1210 C ATOM 1753 NH1 ARG B 74 -15.583 4.053 108.373 1.00 43.26 N ANISOU 1753 NH1 ARG B 74 4783 6787 4868 -1713 -453 -1336 N ATOM 1754 NH2 ARG B 74 -16.120 1.889 108.925 1.00 46.40 N ANISOU 1754 NH2 ARG B 74 5056 7404 5172 -1440 -614 -1137 N ATOM 1755 N SER B 75 -19.805 8.706 104.095 1.00 43.69 N ANISOU 1755 N SER B 75 6112 5534 4955 -1620 298 -1341 N ATOM 1756 CA SER B 75 -19.831 9.781 103.119 1.00 40.83 C ANISOU 1756 CA SER B 75 6026 4870 4615 -1694 397 -1346 C ATOM 1757 C SER B 75 -21.151 10.515 103.307 1.00 42.67 C ANISOU 1757 C SER B 75 6538 4919 4754 -1453 400 -1393 C ATOM 1758 O SER B 75 -21.746 10.472 104.387 1.00 44.63 O ANISOU 1758 O SER B 75 6767 5273 4915 -1325 339 -1478 O ATOM 1759 CB SER B 75 -19.660 9.215 101.701 1.00 37.56 C ANISOU 1759 CB SER B 75 5540 4440 4290 -1688 488 -1194 C ATOM 1760 OG SER B 75 -20.793 8.445 101.356 1.00 36.72 O ANISOU 1760 OG SER B 75 5387 4391 4172 -1398 482 -1091 O ATOM 1761 N LYS B 76 -21.631 11.165 102.254 1.00 37.20 N ANISOU 1761 N LYS B 76 6104 3964 4068 -1374 468 -1343 N ATOM 1762 CA LYS B 76 -22.959 11.760 102.291 1.00 39.66 C ANISOU 1762 CA LYS B 76 6648 4120 4303 -1079 454 -1387 C ATOM 1763 C LYS B 76 -24.047 10.799 101.837 1.00 36.32 C ANISOU 1763 C LYS B 76 6055 3851 3892 -791 452 -1282 C ATOM 1764 O LYS B 76 -25.225 11.176 101.829 1.00 37.28 O ANISOU 1764 O LYS B 76 6304 3900 3961 -517 435 -1328 O ATOM 1765 CB LYS B 76 -22.988 13.035 101.448 1.00 43.33 C ANISOU 1765 CB LYS B 76 7527 4189 4746 -1107 494 -1397 C ATOM 1766 CG LYS B 76 -22.119 14.133 102.033 1.00 52.77 C ANISOU 1766 CG LYS B 76 8910 5212 5926 -1367 482 -1509 C ATOM 1767 CD LYS B 76 -22.397 15.472 101.386 1.00 63.83 C ANISOU 1767 CD LYS B 76 10696 6252 7303 -1295 487 -1469 C ATOM 1768 CE LYS B 76 -21.352 15.800 100.339 1.00 70.17 C ANISOU 1768 CE LYS B 76 11592 6921 8148 -1592 582 -1340 C ATOM 1769 NZ LYS B 76 -19.995 15.350 100.752 1.00 74.47 N ANISOU 1769 NZ LYS B 76 11844 7689 8761 -1944 616 -1367 N ATOM 1770 N GLU B 77 -23.685 9.565 101.486 1.00 32.94 N ANISOU 1770 N GLU B 77 5338 3643 3536 -842 462 -1159 N ATOM 1771 CA GLU B 77 -24.533 8.482 101.011 1.00 31.44 C ANISOU 1771 CA GLU B 77 4959 3612 3373 -637 458 -1053 C ATOM 1772 C GLU B 77 -24.884 7.533 102.146 1.00 30.20 C ANISOU 1772 C GLU B 77 4546 3742 3186 -585 413 -1069 C ATOM 1773 O GLU B 77 -24.053 7.285 103.023 1.00 32.86 O ANISOU 1773 O GLU B 77 4772 4204 3509 -753 378 -1102 O ATOM 1774 CB GLU B 77 -23.826 7.687 99.911 1.00 33.89 C ANISOU 1774 CB GLU B 77 5144 3960 3773 -742 496 -915 C ATOM 1775 CG GLU B 77 -23.350 8.520 98.730 1.00 39.97 C ANISOU 1775 CG GLU B 77 6167 4468 4551 -842 567 -876 C ATOM 1776 CD GLU B 77 -24.474 8.895 97.775 1.00 40.85 C ANISOU 1776 CD GLU B 77 6496 4404 4619 -589 562 -830 C ATOM 1777 OE1 GLU B 77 -25.229 7.993 97.353 1.00 36.53 O ANISOU 1777 OE1 GLU B 77 5793 3994 4094 -404 533 -765 O ATOM 1778 OE2 GLU B 77 -24.601 10.093 97.445 1.00 45.68 O ANISOU 1778 OE2 GLU B 77 7449 4734 5172 -574 574 -864 O ATOM 1779 N PRO B 78 -26.092 6.972 102.141 1.00 29.14 N ANISOU 1779 N PRO B 78 4316 3724 3033 -367 411 -1045 N ATOM 1780 CA PRO B 78 -26.461 5.984 103.168 1.00 34.72 C ANISOU 1780 CA PRO B 78 4798 4700 3694 -351 391 -1035 C ATOM 1781 C PRO B 78 -25.614 4.717 103.058 1.00 35.49 C ANISOU 1781 C PRO B 78 4688 4938 3858 -492 360 -906 C ATOM 1782 O PRO B 78 -24.798 4.547 102.153 1.00 32.14 O ANISOU 1782 O PRO B 78 4253 4436 3524 -582 364 -838 O ATOM 1783 CB PRO B 78 -27.941 5.696 102.875 1.00 31.76 C ANISOU 1783 CB PRO B 78 4361 4399 3308 -114 415 -1034 C ATOM 1784 CG PRO B 78 -28.406 6.834 101.992 1.00 33.40 C ANISOU 1784 CG PRO B 78 4800 4364 3524 45 419 -1093 C ATOM 1785 CD PRO B 78 -27.199 7.264 101.213 1.00 33.12 C ANISOU 1785 CD PRO B 78 4922 4119 3545 -131 422 -1034 C ATOM 1786 N ASP B 79 -25.814 3.813 104.018 1.00 28.53 N ANISOU 1786 N ASP B 79 3654 4266 2919 -503 330 -877 N ATOM 1787 CA ASP B 79 -25.112 2.530 104.037 1.00 25.04 C ANISOU 1787 CA ASP B 79 3041 3947 2525 -594 275 -757 C ATOM 1788 C ASP B 79 -25.671 1.571 102.976 1.00 28.00 C ANISOU 1788 C ASP B 79 3324 4326 2989 -505 291 -639 C ATOM 1789 O ASP B 79 -26.880 1.337 102.915 1.00 25.95 O ANISOU 1789 O ASP B 79 3038 4118 2706 -388 325 -633 O ATOM 1790 CB ASP B 79 -25.239 1.921 105.442 1.00 26.84 C ANISOU 1790 CB ASP B 79 3203 4367 2630 -629 231 -752 C ATOM 1791 CG ASP B 79 -24.939 0.419 105.482 1.00 24.88 C ANISOU 1791 CG ASP B 79 2814 4229 2409 -661 165 -606 C ATOM 1792 OD1 ASP B 79 -23.931 -0.009 104.889 1.00 27.17 O ANISOU 1792 OD1 ASP B 79 3038 4483 2803 -711 109 -555 O ATOM 1793 OD2 ASP B 79 -25.696 -0.337 106.152 1.00 30.11 O ANISOU 1793 OD2 ASP B 79 3442 5017 2983 -641 174 -548 O ATOM 1794 N CYS B 80 -24.778 0.981 102.163 1.00 25.78 N ANISOU 1794 N CYS B 80 2976 4010 2809 -563 264 -563 N ATOM 1795 CA CYS B 80 -25.223 0.077 101.093 1.00 22.79 C ANISOU 1795 CA CYS B 80 2532 3618 2510 -481 271 -468 C ATOM 1796 C CYS B 80 -25.867 -1.194 101.623 1.00 25.23 C ANISOU 1796 C CYS B 80 2730 4062 2796 -457 232 -387 C ATOM 1797 O CYS B 80 -26.752 -1.752 100.966 1.00 23.55 O ANISOU 1797 O CYS B 80 2481 3848 2617 -379 246 -343 O ATOM 1798 CB ACYS B 80 -24.080 -0.223 100.120 0.63 24.49 C ANISOU 1798 CB ACYS B 80 2709 3773 2822 -540 267 -428 C ATOM 1799 CB BCYS B 80 -24.028 -0.374 100.268 0.37 24.86 C ANISOU 1799 CB BCYS B 80 2736 3842 2867 -547 255 -422 C ATOM 1800 SG ACYS B 80 -22.656 -0.978 100.816 0.63 26.74 S ANISOU 1800 SG ACYS B 80 2847 4177 3136 -652 179 -412 S ATOM 1801 SG BCYS B 80 -23.560 0.711 99.025 0.37 22.12 S ANISOU 1801 SG BCYS B 80 2522 3321 2560 -577 340 -460 S ATOM 1802 N GLY B 81 -25.420 -1.703 102.775 1.00 22.21 N ANISOU 1802 N GLY B 81 2305 3787 2346 -534 174 -362 N ATOM 1803 CA GLY B 81 -26.052 -2.902 103.304 1.00 24.96 C ANISOU 1803 CA GLY B 81 2599 4236 2650 -539 146 -268 C ATOM 1804 C GLY B 81 -27.501 -2.661 103.680 1.00 27.13 C ANISOU 1804 C GLY B 81 2874 4588 2846 -499 232 -305 C ATOM 1805 O GLY B 81 -28.366 -3.512 103.458 1.00 27.74 O ANISOU 1805 O GLY B 81 2890 4712 2937 -494 251 -243 O ATOM 1806 N THR B 82 -27.786 -1.481 104.222 1.00 27.11 N ANISOU 1806 N THR B 82 2933 4603 2764 -470 286 -426 N ATOM 1807 CA THR B 82 -29.152 -1.089 104.540 1.00 22.56 C ANISOU 1807 CA THR B 82 2333 4121 2117 -394 376 -503 C ATOM 1808 C THR B 82 -29.964 -0.905 103.269 1.00 23.89 C ANISOU 1808 C THR B 82 2464 4221 2391 -264 400 -528 C ATOM 1809 O THR B 82 -31.132 -1.309 103.211 1.00 25.11 O ANISOU 1809 O THR B 82 2512 4490 2540 -220 445 -539 O ATOM 1810 CB THR B 82 -29.133 0.201 105.357 1.00 26.46 C ANISOU 1810 CB THR B 82 2928 4621 2505 -362 412 -650 C ATOM 1811 OG1 THR B 82 -28.335 -0.002 106.541 1.00 28.54 O ANISOU 1811 OG1 THR B 82 3229 4959 2655 -486 366 -633 O ATOM 1812 CG2 THR B 82 -30.543 0.610 105.802 1.00 26.02 C ANISOU 1812 CG2 THR B 82 2824 4697 2363 -255 512 -760 C ATOM 1813 N ALA B 83 -29.357 -0.274 102.266 1.00 22.39 N ANISOU 1813 N ALA B 83 2365 3857 2286 -210 371 -543 N ATOM 1814 CA ALA B 83 -29.989 -0.127 100.952 1.00 21.99 C ANISOU 1814 CA ALA B 83 2319 3721 2316 -78 367 -550 C ATOM 1815 C ALA B 83 -30.385 -1.481 100.369 1.00 23.56 C ANISOU 1815 C ALA B 83 2388 3981 2583 -104 338 -451 C ATOM 1816 O ALA B 83 -31.484 -1.639 99.822 1.00 24.63 O ANISOU 1816 O ALA B 83 2447 4167 2743 -9 340 -482 O ATOM 1817 CB ALA B 83 -29.033 0.610 100.010 1.00 22.20 C ANISOU 1817 CB ALA B 83 2496 3543 2394 -71 351 -547 C ATOM 1818 N PHE B 84 -29.484 -2.466 100.449 1.00 23.65 N ANISOU 1818 N PHE B 84 2376 3982 2627 -225 295 -345 N ATOM 1819 CA PHE B 84 -29.793 -3.809 99.966 1.00 22.37 C ANISOU 1819 CA PHE B 84 2130 3844 2525 -260 257 -254 C ATOM 1820 C PHE B 84 -31.003 -4.377 100.683 1.00 21.63 C ANISOU 1820 C PHE B 84 1930 3910 2377 -310 296 -254 C ATOM 1821 O PHE B 84 -31.901 -4.953 100.057 1.00 23.63 O ANISOU 1821 O PHE B 84 2098 4199 2681 -294 290 -252 O ATOM 1822 CB PHE B 84 -28.576 -4.715 100.165 1.00 23.61 C ANISOU 1822 CB PHE B 84 2302 3960 2710 -354 193 -156 C ATOM 1823 CG PHE B 84 -28.812 -6.173 99.812 1.00 21.11 C ANISOU 1823 CG PHE B 84 1943 3632 2445 -395 139 -61 C ATOM 1824 CD1 PHE B 84 -29.407 -7.043 100.716 1.00 23.65 C ANISOU 1824 CD1 PHE B 84 2241 4041 2706 -500 138 5 C ATOM 1825 CD2 PHE B 84 -28.374 -6.684 98.602 1.00 23.59 C ANISOU 1825 CD2 PHE B 84 2270 3838 2855 -342 92 -39 C ATOM 1826 CE1 PHE B 84 -29.602 -8.379 100.402 1.00 27.62 C ANISOU 1826 CE1 PHE B 84 2746 4494 3255 -559 83 93 C ATOM 1827 CE2 PHE B 84 -28.558 -8.024 98.287 1.00 22.11 C ANISOU 1827 CE2 PHE B 84 2073 3613 2714 -375 31 33 C ATOM 1828 CZ PHE B 84 -29.169 -8.871 99.185 1.00 21.79 C ANISOU 1828 CZ PHE B 84 2024 3630 2625 -489 20 102 C ATOM 1829 N GLU B 85 -31.025 -4.252 102.010 1.00 22.44 N ANISOU 1829 N GLU B 85 2036 4123 2368 -389 341 -261 N ATOM 1830 CA GLU B 85 -32.116 -4.818 102.780 1.00 26.25 C ANISOU 1830 CA GLU B 85 2421 4779 2774 -476 410 -255 C ATOM 1831 C GLU B 85 -33.428 -4.128 102.454 1.00 27.26 C ANISOU 1831 C GLU B 85 2429 5018 2910 -358 479 -392 C ATOM 1832 O GLU B 85 -34.480 -4.774 102.430 1.00 26.67 O ANISOU 1832 O GLU B 85 2211 5078 2843 -418 522 -399 O ATOM 1833 CB GLU B 85 -31.806 -4.714 104.272 1.00 26.59 C ANISOU 1833 CB GLU B 85 2521 4921 2659 -576 451 -241 C ATOM 1834 CG GLU B 85 -30.610 -5.556 104.653 1.00 27.22 C ANISOU 1834 CG GLU B 85 2704 4916 2722 -675 353 -103 C ATOM 1835 CD GLU B 85 -30.119 -5.299 106.058 1.00 33.68 C ANISOU 1835 CD GLU B 85 3609 5816 3371 -744 355 -99 C ATOM 1836 OE1 GLU B 85 -30.227 -4.149 106.548 1.00 30.54 O ANISOU 1836 OE1 GLU B 85 3226 5479 2899 -688 411 -228 O ATOM 1837 OE2 GLU B 85 -29.584 -6.248 106.660 1.00 34.23 O ANISOU 1837 OE2 GLU B 85 3756 5876 3375 -841 284 29 O ATOM 1838 N LEU B 86 -33.377 -2.826 102.173 1.00 27.77 N ANISOU 1838 N LEU B 86 2551 5023 2977 -189 481 -510 N ATOM 1839 CA LEU B 86 -34.578 -2.112 101.761 1.00 27.90 C ANISOU 1839 CA LEU B 86 2469 5124 3008 -15 511 -653 C ATOM 1840 C LEU B 86 -35.087 -2.630 100.424 1.00 24.04 C ANISOU 1840 C LEU B 86 1902 4595 2636 50 438 -636 C ATOM 1841 O LEU B 86 -36.300 -2.787 100.242 1.00 27.42 O ANISOU 1841 O LEU B 86 2149 5185 3083 102 455 -720 O ATOM 1842 CB LEU B 86 -34.297 -0.612 101.684 1.00 29.90 C ANISOU 1842 CB LEU B 86 2870 5257 3233 166 502 -768 C ATOM 1843 CG LEU B 86 -35.495 0.314 101.461 1.00 34.12 C ANISOU 1843 CG LEU B 86 3338 5868 3758 404 517 -942 C ATOM 1844 CD1 LEU B 86 -36.464 0.240 102.639 1.00 30.93 C ANISOU 1844 CD1 LEU B 86 2771 5714 3268 373 619 -1032 C ATOM 1845 CD2 LEU B 86 -35.004 1.746 101.246 1.00 33.77 C ANISOU 1845 CD2 LEU B 86 3528 5611 3691 571 481 -1024 C ATOM 1846 N GLY B 87 -34.172 -2.909 99.485 1.00 24.88 N ANISOU 1846 N GLY B 87 2129 4508 2815 43 356 -542 N ATOM 1847 CA GLY B 87 -34.578 -3.446 98.190 1.00 28.26 C ANISOU 1847 CA GLY B 87 2513 4891 3334 101 277 -527 C ATOM 1848 C GLY B 87 -35.161 -4.842 98.311 1.00 28.65 C ANISOU 1848 C GLY B 87 2410 5056 3418 -66 277 -470 C ATOM 1849 O GLY B 87 -36.138 -5.182 97.640 1.00 26.43 O ANISOU 1849 O GLY B 87 1997 4857 3189 -28 237 -528 O ATOM 1850 N TYR B 88 -34.561 -5.669 99.169 1.00 25.85 N ANISOU 1850 N TYR B 88 2088 4703 3031 -259 308 -359 N ATOM 1851 CA TYR B 88 -35.099 -6.996 99.437 1.00 27.53 C ANISOU 1851 CA TYR B 88 2209 4995 3256 -452 317 -289 C ATOM 1852 C TYR B 88 -36.519 -6.896 99.982 1.00 27.14 C ANISOU 1852 C TYR B 88 2017 5128 3168 -479 391 -381 C ATOM 1853 O TYR B 88 -37.439 -7.573 99.503 1.00 29.27 O ANISOU 1853 O TYR B 88 2195 5432 3496 -532 365 -401 O ATOM 1854 CB TYR B 88 -34.171 -7.733 100.422 1.00 25.94 C ANISOU 1854 CB TYR B 88 2130 4736 2991 -620 325 -148 C ATOM 1855 CG TYR B 88 -34.272 -9.239 100.321 1.00 29.06 C ANISOU 1855 CG TYR B 88 2546 5075 3422 -799 282 -33 C ATOM 1856 CD1 TYR B 88 -33.298 -9.981 99.669 1.00 30.74 C ANISOU 1856 CD1 TYR B 88 2888 5086 3706 -783 171 55 C ATOM 1857 CD2 TYR B 88 -35.354 -9.918 100.881 1.00 30.12 C ANISOU 1857 CD2 TYR B 88 2602 5328 3517 -972 350 -23 C ATOM 1858 CE1 TYR B 88 -33.401 -11.359 99.567 1.00 31.44 C ANISOU 1858 CE1 TYR B 88 3034 5086 3826 -931 117 151 C ATOM 1859 CE2 TYR B 88 -35.462 -11.293 100.784 1.00 32.61 C ANISOU 1859 CE2 TYR B 88 2973 5556 3860 -1159 309 83 C ATOM 1860 CZ TYR B 88 -34.484 -12.006 100.126 1.00 30.79 C ANISOU 1860 CZ TYR B 88 2881 5116 3702 -1139 185 173 C ATOM 1861 OH TYR B 88 -34.605 -13.378 100.033 1.00 38.01 O ANISOU 1861 OH TYR B 88 3890 5908 4643 -1315 130 272 O ATOM 1862 N ALA B 89 -36.717 -6.016 100.969 1.00 26.75 N ANISOU 1862 N ALA B 89 1960 5184 3021 -432 477 -451 N ATOM 1863 CA ALA B 89 -38.038 -5.811 101.548 1.00 29.75 C ANISOU 1863 CA ALA B 89 2211 5734 3358 -433 549 -553 C ATOM 1864 C ALA B 89 -39.013 -5.235 100.521 1.00 33.51 C ANISOU 1864 C ALA B 89 2563 6254 3915 -235 487 -694 C ATOM 1865 O ALA B 89 -40.190 -5.603 100.507 1.00 33.79 O ANISOU 1865 O ALA B 89 2453 6415 3970 -279 503 -756 O ATOM 1866 CB ALA B 89 -37.920 -4.893 102.760 1.00 33.92 C ANISOU 1866 CB ALA B 89 2776 6351 3761 -393 640 -614 C ATOM 1867 N ALA B 90 -38.540 -4.337 99.647 1.00 30.79 N ANISOU 1867 N ALA B 90 2281 5809 3609 -16 412 -747 N ATOM 1868 CA ALA B 90 -39.426 -3.731 98.654 1.00 40.25 C ANISOU 1868 CA ALA B 90 3402 7031 4862 204 324 -874 C ATOM 1869 C ALA B 90 -39.926 -4.767 97.657 1.00 32.03 C ANISOU 1869 C ALA B 90 2281 5980 3908 130 239 -845 C ATOM 1870 O ALA B 90 -41.095 -4.737 97.243 1.00 35.96 O ANISOU 1870 O ALA B 90 2643 6585 4434 201 194 -949 O ATOM 1871 CB ALA B 90 -38.701 -2.600 97.925 1.00 35.52 C ANISOU 1871 CB ALA B 90 2949 6285 4265 450 258 -914 C ATOM 1872 N ALA B 91 -39.054 -5.693 97.261 1.00 28.66 N ANISOU 1872 N ALA B 91 1937 5428 3524 -10 207 -714 N ATOM 1873 CA ALA B 91 -39.461 -6.728 96.317 1.00 31.65 C ANISOU 1873 CA ALA B 91 2266 5777 3985 -89 119 -693 C ATOM 1874 C ALA B 91 -40.512 -7.657 96.921 1.00 36.98 C ANISOU 1874 C ALA B 91 2804 6581 4666 -301 180 -697 C ATOM 1875 O ALA B 91 -41.340 -8.222 96.191 1.00 34.37 O ANISOU 1875 O ALA B 91 2371 6290 4399 -330 113 -748 O ATOM 1876 CB ALA B 91 -38.222 -7.506 95.865 1.00 28.98 C ANISOU 1876 CB ALA B 91 2059 5268 3683 -187 73 -563 C ATOM 1877 N LEU B 92 -40.507 -7.813 98.242 1.00 37.35 N ANISOU 1877 N LEU B 92 2853 6701 4638 -453 307 -651 N ATOM 1878 CA LEU B 92 -41.460 -8.655 98.957 1.00 33.85 C ANISOU 1878 CA LEU B 92 2299 6385 4176 -672 392 -647 C ATOM 1879 C LEU B 92 -42.733 -7.912 99.346 1.00 40.17 C ANISOU 1879 C LEU B 92 2911 7408 4943 -578 451 -810 C ATOM 1880 O LEU B 92 -43.641 -8.517 99.931 1.00 39.50 O ANISOU 1880 O LEU B 92 2702 7466 4839 -757 536 -832 O ATOM 1881 CB LEU B 92 -40.788 -9.244 100.207 1.00 35.96 C ANISOU 1881 CB LEU B 92 2692 6619 4351 -885 494 -507 C ATOM 1882 CG LEU B 92 -39.539 -10.092 99.930 1.00 37.40 C ANISOU 1882 CG LEU B 92 3059 6592 4562 -986 427 -346 C ATOM 1883 CD1 LEU B 92 -39.019 -10.722 101.196 1.00 40.75 C ANISOU 1883 CD1 LEU B 92 3614 6994 4875 -1190 507 -208 C ATOM 1884 CD2 LEU B 92 -39.821 -11.170 98.887 1.00 40.50 C ANISOU 1884 CD2 LEU B 92 3431 6890 5065 -1081 331 -325 C ATOM 1885 N GLY B 93 -42.836 -6.627 99.024 1.00 36.30 N ANISOU 1885 N GLY B 93 2400 6950 4444 -303 406 -930 N ATOM 1886 CA GLY B 93 -44.034 -5.885 99.345 1.00 39.48 C ANISOU 1886 CA GLY B 93 2623 7559 4818 -180 441 -1100 C ATOM 1887 C GLY B 93 -44.183 -5.521 100.800 1.00 44.54 C ANISOU 1887 C GLY B 93 3242 8332 5350 -247 592 -1123 C ATOM 1888 O GLY B 93 -45.304 -5.285 101.255 1.00 45.76 O ANISOU 1888 O GLY B 93 3213 8696 5479 -233 655 -1254 O ATOM 1889 N LYS B 94 -43.084 -5.469 101.550 1.00 36.40 N ANISOU 1889 N LYS B 94 2387 7196 4247 -319 649 -1010 N ATOM 1890 CA LYS B 94 -43.149 -5.067 102.945 1.00 39.94 C ANISOU 1890 CA LYS B 94 2840 7762 4572 -370 783 -1035 C ATOM 1891 C LYS B 94 -43.468 -3.579 103.054 1.00 37.65 C ANISOU 1891 C LYS B 94 2512 7538 4255 -82 771 -1205 C ATOM 1892 O LYS B 94 -43.306 -2.808 102.105 1.00 41.40 O ANISOU 1892 O LYS B 94 3028 7911 4791 158 653 -1266 O ATOM 1893 CB LYS B 94 -41.826 -5.366 103.660 1.00 35.70 C ANISOU 1893 CB LYS B 94 2516 7091 3957 -504 820 -874 C ATOM 1894 CG LYS B 94 -41.355 -6.810 103.535 1.00 39.88 C ANISOU 1894 CG LYS B 94 3130 7511 4510 -757 806 -694 C ATOM 1895 CD LYS B 94 -42.410 -7.786 104.048 1.00 44.25 C ANISOU 1895 CD LYS B 94 3568 8207 5039 -990 899 -685 C ATOM 1896 CE LYS B 94 -41.869 -9.207 104.100 1.00 39.89 C ANISOU 1896 CE LYS B 94 3154 7515 4487 -1248 887 -496 C ATOM 1897 NZ LYS B 94 -42.790 -10.138 104.821 1.00 42.09 N ANISOU 1897 NZ LYS B 94 3367 7917 4708 -1511 1001 -469 N ATOM 1898 N VAL B 95 -43.934 -3.181 104.236 1.00 42.05 N ANISOU 1898 N VAL B 95 3011 8256 4711 -102 893 -1282 N ATOM 1899 CA VAL B 95 -44.062 -1.765 104.556 1.00 42.57 C ANISOU 1899 CA VAL B 95 3089 8352 4734 163 892 -1432 C ATOM 1900 C VAL B 95 -42.670 -1.165 104.696 1.00 42.49 C ANISOU 1900 C VAL B 95 3325 8133 4685 229 863 -1359 C ATOM 1901 O VAL B 95 -41.840 -1.658 105.470 1.00 43.28 O ANISOU 1901 O VAL B 95 3546 8193 4708 36 930 -1236 O ATOM 1902 CB VAL B 95 -44.886 -1.573 105.841 1.00 45.27 C ANISOU 1902 CB VAL B 95 3306 8926 4969 108 1044 -1534 C ATOM 1903 CG1 VAL B 95 -44.884 -0.112 106.273 1.00 45.30 C ANISOU 1903 CG1 VAL B 95 3365 8927 4921 383 1044 -1685 C ATOM 1904 CG2 VAL B 95 -46.312 -2.076 105.650 1.00 49.39 C ANISOU 1904 CG2 VAL B 95 3555 9677 5533 51 1078 -1636 C ATOM 1905 N LEU B 96 -42.410 -0.094 103.955 1.00 38.86 N ANISOU 1905 N LEU B 96 2955 7538 4272 499 758 -1436 N ATOM 1906 CA LEU B 96 -41.083 0.511 103.897 1.00 39.91 C ANISOU 1906 CA LEU B 96 3326 7455 4382 561 726 -1380 C ATOM 1907 C LEU B 96 -41.113 1.854 104.609 1.00 40.21 C ANISOU 1907 C LEU B 96 3460 7472 4344 755 757 -1518 C ATOM 1908 O LEU B 96 -41.839 2.761 104.194 1.00 41.63 O ANISOU 1908 O LEU B 96 3615 7647 4557 1011 692 -1655 O ATOM 1909 CB LEU B 96 -40.623 0.698 102.452 1.00 37.77 C ANISOU 1909 CB LEU B 96 3146 6993 4212 704 588 -1348 C ATOM 1910 CG LEU B 96 -40.728 -0.491 101.495 1.00 36.23 C ANISOU 1910 CG LEU B 96 2860 6797 4107 574 527 -1244 C ATOM 1911 CD1 LEU B 96 -40.165 -0.099 100.134 1.00 40.34 C ANISOU 1911 CD1 LEU B 96 3511 7118 4698 750 398 -1225 C ATOM 1912 CD2 LEU B 96 -39.968 -1.688 102.047 1.00 38.36 C ANISOU 1912 CD2 LEU B 96 3160 7064 4352 271 598 -1078 C ATOM 1913 N LEU B 97 -40.304 1.982 105.659 1.00 41.02 N ANISOU 1913 N LEU B 97 3696 7550 4340 641 840 -1483 N ATOM 1914 CA LEU B 97 -40.158 3.223 106.407 1.00 41.01 C ANISOU 1914 CA LEU B 97 3834 7494 4254 796 870 -1610 C ATOM 1915 C LEU B 97 -38.676 3.539 106.503 1.00 38.37 C ANISOU 1915 C LEU B 97 3755 6950 3875 737 847 -1544 C ATOM 1916 O LEU B 97 -37.860 2.641 106.723 1.00 39.85 O ANISOU 1916 O LEU B 97 3966 7144 4032 509 867 -1405 O ATOM 1917 CB LEU B 97 -40.782 3.118 107.809 1.00 38.95 C ANISOU 1917 CB LEU B 97 3475 7453 3871 702 1008 -1672 C ATOM 1918 CG LEU B 97 -42.274 2.766 107.819 1.00 43.63 C ANISOU 1918 CG LEU B 97 3793 8289 4495 724 1054 -1755 C ATOM 1919 CD1 LEU B 97 -42.762 2.414 109.224 1.00 47.44 C ANISOU 1919 CD1 LEU B 97 4188 8995 4841 564 1218 -1781 C ATOM 1920 CD2 LEU B 97 -43.083 3.915 107.252 1.00 48.24 C ANISOU 1920 CD2 LEU B 97 4335 8852 5140 1055 973 -1934 C ATOM 1921 N THR B 98 -38.328 4.804 106.291 1.00 37.19 N ANISOU 1921 N THR B 98 3809 6600 3722 936 793 -1646 N ATOM 1922 CA THR B 98 -36.935 5.233 106.297 1.00 41.93 C ANISOU 1922 CA THR B 98 4667 6983 4282 872 761 -1614 C ATOM 1923 C THR B 98 -36.807 6.527 107.082 1.00 41.64 C ANISOU 1923 C THR B 98 4832 6832 4157 989 774 -1760 C ATOM 1924 O THR B 98 -37.773 7.275 107.246 1.00 38.97 O ANISOU 1924 O THR B 98 4467 6519 3821 1192 780 -1888 O ATOM 1925 CB THR B 98 -36.385 5.467 104.882 1.00 38.32 C ANISOU 1925 CB THR B 98 4339 6294 3928 962 657 -1570 C ATOM 1926 OG1 THR B 98 -37.025 6.617 104.313 1.00 36.78 O ANISOU 1926 OG1 THR B 98 4256 5945 3775 1239 585 -1679 O ATOM 1927 CG2 THR B 98 -36.607 4.248 103.990 1.00 33.64 C ANISOU 1927 CG2 THR B 98 3552 5800 3428 881 633 -1444 C ATOM 1928 N PHE B 99 -35.593 6.787 107.566 1.00 37.98 N ANISOU 1928 N PHE B 99 4572 6245 3614 853 767 -1750 N ATOM 1929 CA PHE B 99 -35.303 8.070 108.185 1.00 38.07 C ANISOU 1929 CA PHE B 99 4828 6089 3548 940 758 -1892 C ATOM 1930 C PHE B 99 -33.848 8.424 107.916 1.00 36.25 C ANISOU 1930 C PHE B 99 4844 5623 3307 804 687 -1871 C ATOM 1931 O PHE B 99 -33.055 7.595 107.459 1.00 38.32 O ANISOU 1931 O PHE B 99 5052 5907 3601 631 662 -1752 O ATOM 1932 CB PHE B 99 -35.623 8.072 109.695 1.00 46.81 C ANISOU 1932 CB PHE B 99 5889 7387 4509 881 851 -1962 C ATOM 1933 CG PHE B 99 -34.667 7.270 110.540 1.00 38.95 C ANISOU 1933 CG PHE B 99 4900 6499 3402 611 867 -1864 C ATOM 1934 CD1 PHE B 99 -33.594 7.885 111.172 1.00 45.15 C ANISOU 1934 CD1 PHE B 99 5914 7152 4088 517 818 -1921 C ATOM 1935 CD2 PHE B 99 -34.856 5.908 110.727 1.00 42.84 C ANISOU 1935 CD2 PHE B 99 5180 7214 3881 445 915 -1715 C ATOM 1936 CE1 PHE B 99 -32.722 7.156 111.964 1.00 41.32 C ANISOU 1936 CE1 PHE B 99 5427 6776 3495 286 801 -1832 C ATOM 1937 CE2 PHE B 99 -33.983 5.172 111.521 1.00 45.60 C ANISOU 1937 CE2 PHE B 99 5563 7646 4119 215 907 -1612 C ATOM 1938 CZ PHE B 99 -32.921 5.800 112.143 1.00 41.74 C ANISOU 1938 CZ PHE B 99 5283 7045 3532 147 843 -1672 C ATOM 1939 N SER B 100 -33.519 9.686 108.159 1.00 38.59 N ANISOU 1939 N SER B 100 5410 5688 3564 873 654 -1998 N ATOM 1940 CA SER B 100 -32.143 10.144 108.055 1.00 39.86 C ANISOU 1940 CA SER B 100 5812 5625 3707 704 587 -2012 C ATOM 1941 C SER B 100 -31.951 11.314 109.008 1.00 41.53 C ANISOU 1941 C SER B 100 6263 5697 3820 714 584 -2170 C ATOM 1942 O SER B 100 -32.856 12.128 109.203 1.00 42.09 O ANISOU 1942 O SER B 100 6392 5711 3889 919 611 -2277 O ATOM 1943 CB SER B 100 -31.792 10.553 106.618 1.00 36.08 C ANISOU 1943 CB SER B 100 5497 4866 3347 760 517 -1971 C ATOM 1944 OG SER B 100 -30.559 11.247 106.571 1.00 41.79 O ANISOU 1944 OG SER B 100 6484 5328 4068 574 462 -1990 O ATOM 1945 N THR B 101 -30.765 11.387 109.609 1.00 39.64 N ANISOU 1945 N THR B 101 6141 5415 3505 486 537 -2192 N ATOM 1946 CA THR B 101 -30.440 12.545 110.435 1.00 42.78 C ANISOU 1946 CA THR B 101 6804 5640 3810 465 514 -2349 C ATOM 1947 C THR B 101 -30.143 13.790 109.607 1.00 45.74 C ANISOU 1947 C THR B 101 7430 5651 4296 479 470 -2442 C ATOM 1948 O THR B 101 -29.963 14.870 110.179 1.00 51.06 O ANISOU 1948 O THR B 101 8269 6184 4947 469 441 -2599 O ATOM 1949 CB THR B 101 -29.247 12.235 111.344 1.00 41.34 C ANISOU 1949 CB THR B 101 6624 5549 3535 212 437 -2344 C ATOM 1950 OG1 THR B 101 -28.152 11.744 110.556 1.00 43.82 O ANISOU 1950 OG1 THR B 101 6878 5809 3964 -23 380 -2236 O ATOM 1951 CG2 THR B 101 -29.629 11.189 112.372 1.00 41.18 C ANISOU 1951 CG2 THR B 101 6363 5882 3402 178 496 -2275 C ATOM 1952 N ASP B 102 -30.090 13.665 108.280 1.00 47.17 N ANISOU 1952 N ASP B 102 7619 5691 4611 528 431 -2330 N ATOM 1953 CA ASP B 102 -29.820 14.789 107.384 1.00 52.02 C ANISOU 1953 CA ASP B 102 8501 5933 5330 565 358 -2322 C ATOM 1954 C ASP B 102 -30.739 14.621 106.180 1.00 50.86 C ANISOU 1954 C ASP B 102 8315 5736 5272 804 359 -2211 C ATOM 1955 O ASP B 102 -30.445 13.835 105.275 1.00 44.55 O ANISOU 1955 O ASP B 102 7451 4951 4525 741 356 -2065 O ATOM 1956 CB ASP B 102 -28.351 14.822 106.965 1.00 51.86 C ANISOU 1956 CB ASP B 102 8621 5729 5355 248 306 -2228 C ATOM 1957 CG ASP B 102 -28.010 16.027 106.090 1.00 50.87 C ANISOU 1957 CG ASP B 102 8810 5205 5315 225 260 -2188 C ATOM 1958 OD1 ASP B 102 -28.881 16.899 105.882 1.00 55.55 O ANISOU 1958 OD1 ASP B 102 9543 5646 5919 477 239 -2243 O ATOM 1959 OD2 ASP B 102 -26.856 16.104 105.619 1.00 54.18 O ANISOU 1959 OD2 ASP B 102 9331 5471 5782 -65 253 -2093 O ATOM 1960 N THR B 103 -31.853 15.351 106.168 1.00 51.49 N ANISOU 1960 N THR B 103 8432 5766 5365 1084 350 -2284 N ATOM 1961 CA THR B 103 -32.823 15.217 105.090 1.00 48.59 C ANISOU 1961 CA THR B 103 8000 5388 5072 1339 314 -2194 C ATOM 1962 C THR B 103 -32.736 16.347 104.064 1.00 48.52 C ANISOU 1962 C THR B 103 8324 4997 5115 1440 214 -2141 C ATOM 1963 O THR B 103 -33.685 16.551 103.300 1.00 50.82 O ANISOU 1963 O THR B 103 8612 5257 5439 1708 150 -2102 O ATOM 1964 CB THR B 103 -34.238 15.121 105.663 1.00 50.54 C ANISOU 1964 CB THR B 103 8017 5889 5295 1602 350 -2290 C ATOM 1965 OG1 THR B 103 -34.536 16.302 106.421 1.00 55.88 O ANISOU 1965 OG1 THR B 103 8863 6445 5923 1720 340 -2453 O ATOM 1966 CG2 THR B 103 -34.365 13.894 106.556 1.00 52.20 C ANISOU 1966 CG2 THR B 103 7909 6481 5443 1478 457 -2286 C ATOM 1967 N ARG B 104 -31.621 17.076 104.023 1.00 49.20 N ANISOU 1967 N ARG B 104 8699 4800 5197 1219 190 -2128 N ATOM 1968 CA ARG B 104 -31.432 18.075 102.982 1.00 50.28 C ANISOU 1968 CA ARG B 104 9183 4564 5358 1260 110 -2032 C ATOM 1969 C ARG B 104 -31.366 17.386 101.619 1.00 51.53 C ANISOU 1969 C ARG B 104 9322 4701 5557 1255 97 -1835 C ATOM 1970 O ARG B 104 -30.892 16.254 101.520 1.00 53.69 O ANISOU 1970 O ARG B 104 9389 5160 5851 1087 158 -1769 O ATOM 1971 CB ARG B 104 -30.145 18.860 103.216 1.00 48.84 C ANISOU 1971 CB ARG B 104 9281 4113 5164 948 111 -2036 C ATOM 1972 CG ARG B 104 -30.069 19.579 104.553 1.00 50.36 C ANISOU 1972 CG ARG B 104 9519 4305 5310 923 111 -2238 C ATOM 1973 CD ARG B 104 -28.720 20.260 104.716 1.00 57.18 C ANISOU 1973 CD ARG B 104 10626 4926 6176 573 102 -2232 C ATOM 1974 NE ARG B 104 -27.635 19.292 104.841 1.00 53.55 N ANISOU 1974 NE ARG B 104 9980 4633 5733 239 151 -2168 N ATOM 1975 CZ ARG B 104 -26.393 19.504 104.415 1.00 55.81 C ANISOU 1975 CZ ARG B 104 10401 4752 6052 -107 165 -2070 C ATOM 1976 NH1 ARG B 104 -26.079 20.654 103.834 1.00 55.99 N ANISOU 1976 NH1 ARG B 104 10767 4426 6081 -179 144 -2018 N ATOM 1977 NH2 ARG B 104 -25.467 18.566 104.567 1.00 52.71 N ANISOU 1977 NH2 ARG B 104 9792 4555 5681 -391 207 -2022 N ATOM 1978 N PRO B 105 -31.841 18.037 100.556 1.00 50.29 N ANISOU 1978 N PRO B 105 9389 4324 5393 1445 11 -1741 N ATOM 1979 CA PRO B 105 -31.713 17.440 99.219 1.00 44.75 C ANISOU 1979 CA PRO B 105 8709 3589 4706 1426 -3 -1553 C ATOM 1980 C PRO B 105 -30.259 17.157 98.874 1.00 43.97 C ANISOU 1980 C PRO B 105 8723 3370 4614 1029 84 -1437 C ATOM 1981 O PRO B 105 -29.342 17.812 99.373 1.00 48.99 O ANISOU 1981 O PRO B 105 9532 3843 5238 778 120 -1472 O ATOM 1982 CB PRO B 105 -32.313 18.506 98.296 1.00 47.84 C ANISOU 1982 CB PRO B 105 9421 3712 5042 1666 -124 -1487 C ATOM 1983 CG PRO B 105 -33.274 19.247 99.171 1.00 53.49 C ANISOU 1983 CG PRO B 105 10112 4466 5745 1940 -185 -1666 C ATOM 1984 CD PRO B 105 -32.630 19.281 100.529 1.00 59.55 C ANISOU 1984 CD PRO B 105 10796 5301 6528 1722 -88 -1809 C ATOM 1985 N MET B 106 -30.056 16.161 97.998 1.00 43.21 N ANISOU 1985 N MET B 106 8510 3370 4539 964 118 -1306 N ATOM 1986 CA MET B 106 -28.699 15.735 97.665 1.00 42.21 C ANISOU 1986 CA MET B 106 8427 3187 4425 581 222 -1206 C ATOM 1987 C MET B 106 -27.865 16.894 97.130 1.00 50.34 C ANISOU 1987 C MET B 106 9846 3873 5409 369 241 -1118 C ATOM 1988 O MET B 106 -26.684 17.028 97.471 1.00 46.61 O ANISOU 1988 O MET B 106 9405 3351 4953 8 325 -1121 O ATOM 1989 CB MET B 106 -28.734 14.599 96.643 1.00 39.59 C ANISOU 1989 CB MET B 106 7954 2977 4111 592 251 -1079 C ATOM 1990 CG MET B 106 -29.149 13.262 97.211 1.00 38.04 C ANISOU 1990 CG MET B 106 7363 3134 3957 664 272 -1147 C ATOM 1991 SD MET B 106 -29.036 11.967 95.960 1.00 41.39 S ANISOU 1991 SD MET B 106 7596 3708 4423 628 300 -971 S ATOM 1992 CE MET B 106 -27.277 11.614 95.972 1.00 39.36 C ANISOU 1992 CE MET B 106 7271 3469 4216 141 431 -875 C ATOM 1993 N VAL B 107 -28.464 17.740 96.288 1.00 50.60 N ANISOU 1993 N VAL B 107 10167 3687 5372 577 160 -1041 N ATOM 1994 CA VAL B 107 -27.726 18.854 95.700 1.00 47.88 C ANISOU 1994 CA VAL B 107 10227 3016 4949 375 185 -943 C ATOM 1995 C VAL B 107 -27.275 19.827 96.783 1.00 56.14 C ANISOU 1995 C VAL B 107 11396 3930 6004 231 186 -1072 C ATOM 1996 O VAL B 107 -26.194 20.422 96.688 1.00 51.36 O ANISOU 1996 O VAL B 107 10988 3152 5376 -111 262 -1026 O ATOM 1997 CB VAL B 107 -28.580 19.550 94.620 1.00 50.95 C ANISOU 1997 CB VAL B 107 10920 3213 5227 669 73 -843 C ATOM 1998 CG1 VAL B 107 -28.554 18.747 93.304 1.00 48.68 C ANISOU 1998 CG1 VAL B 107 10614 2989 4894 669 101 -679 C ATOM 1999 CG2 VAL B 107 -30.008 19.750 95.110 1.00 60.18 C ANISOU 1999 CG2 VAL B 107 11979 4479 6409 1113 -76 -972 C ATOM 2000 N GLU B 108 -28.077 19.989 97.837 1.00 55.71 N ANISOU 2000 N GLU B 108 11209 3977 5980 475 110 -1245 N ATOM 2001 CA GLU B 108 -27.654 20.805 98.972 1.00 58.62 C ANISOU 2001 CA GLU B 108 11663 4253 6356 343 109 -1394 C ATOM 2002 C GLU B 108 -26.463 20.172 99.680 1.00 55.92 C ANISOU 2002 C GLU B 108 11101 4075 6072 -47 207 -1438 C ATOM 2003 O GLU B 108 -25.462 20.842 99.960 1.00 55.62 O ANISOU 2003 O GLU B 108 11215 3888 6031 -359 242 -1454 O ATOM 2004 CB GLU B 108 -28.814 20.986 99.948 1.00 58.11 C ANISOU 2004 CB GLU B 108 11464 4317 6298 697 27 -1583 C ATOM 2005 CG GLU B 108 -29.816 22.041 99.541 1.00 73.81 C ANISOU 2005 CG GLU B 108 13730 6090 8225 1044 -89 -1591 C ATOM 2006 CD GLU B 108 -30.836 22.306 100.628 1.00 78.74 C ANISOU 2006 CD GLU B 108 14207 6854 8858 1348 -142 -1804 C ATOM 2007 OE1 GLU B 108 -30.498 22.115 101.816 1.00 71.79 O ANISOU 2007 OE1 GLU B 108 13152 6123 8003 1213 -84 -1955 O ATOM 2008 OE2 GLU B 108 -31.972 22.705 100.293 1.00 84.77 O ANISOU 2008 OE2 GLU B 108 15024 7594 9589 1718 -242 -1825 O ATOM 2009 N LYS B 109 -26.558 18.870 99.973 1.00 48.72 N ANISOU 2009 N LYS B 109 9822 3483 5205 -36 242 -1460 N ATOM 2010 CA LYS B 109 -25.479 18.164 100.656 1.00 49.18 C ANISOU 2010 CA LYS B 109 9645 3736 5306 -377 311 -1502 C ATOM 2011 C LYS B 109 -24.171 18.265 99.886 1.00 54.65 C ANISOU 2011 C LYS B 109 10433 4312 6019 -773 402 -1368 C ATOM 2012 O LYS B 109 -23.107 18.474 100.479 1.00 53.39 O ANISOU 2012 O LYS B 109 10220 4180 5885 -1097 434 -1423 O ATOM 2013 CB LYS B 109 -25.859 16.694 100.853 1.00 48.98 C ANISOU 2013 CB LYS B 109 9254 4053 5304 -283 334 -1510 C ATOM 2014 CG LYS B 109 -27.097 16.478 101.701 1.00 48.05 C ANISOU 2014 CG LYS B 109 8972 4129 5154 62 278 -1650 C ATOM 2015 CD LYS B 109 -27.464 15.004 101.768 1.00 43.88 C ANISOU 2015 CD LYS B 109 8106 3935 4631 130 315 -1629 C ATOM 2016 CE LYS B 109 -28.498 14.769 102.849 1.00 43.19 C ANISOU 2016 CE LYS B 109 7816 4099 4496 379 296 -1780 C ATOM 2017 NZ LYS B 109 -29.151 13.444 102.779 1.00 38.73 N ANISOU 2017 NZ LYS B 109 6947 3846 3925 506 330 -1744 N ATOM 2018 N TYR B 110 -24.228 18.109 98.563 1.00 53.18 N ANISOU 2018 N TYR B 110 10364 4027 5814 -752 448 -1198 N ATOM 2019 CA TYR B 110 -23.018 18.085 97.757 1.00 45.66 C ANISOU 2019 CA TYR B 110 9455 3025 4868 -1125 567 -1072 C ATOM 2020 C TYR B 110 -22.559 19.470 97.319 1.00 58.53 C ANISOU 2020 C TYR B 110 11471 4340 6427 -1281 588 -1019 C ATOM 2021 O TYR B 110 -21.369 19.649 97.041 1.00 58.44 O ANISOU 2021 O TYR B 110 11458 4325 6423 -1658 697 -973 O ATOM 2022 CB TYR B 110 -23.226 17.182 96.529 1.00 46.18 C ANISOU 2022 CB TYR B 110 9459 3163 4926 -1051 624 -921 C ATOM 2023 CG TYR B 110 -23.051 15.717 96.866 1.00 44.56 C ANISOU 2023 CG TYR B 110 8845 3281 4804 -1097 658 -958 C ATOM 2024 CD1 TYR B 110 -24.143 14.907 97.149 1.00 38.55 C ANISOU 2024 CD1 TYR B 110 7913 2681 4052 -770 584 -1010 C ATOM 2025 CD2 TYR B 110 -21.785 15.158 96.934 1.00 43.30 C ANISOU 2025 CD2 TYR B 110 8447 3296 4711 -1465 759 -951 C ATOM 2026 CE1 TYR B 110 -23.977 13.576 97.477 1.00 34.89 C ANISOU 2026 CE1 TYR B 110 7066 2538 3652 -814 608 -1025 C ATOM 2027 CE2 TYR B 110 -21.608 13.835 97.260 1.00 47.22 C ANISOU 2027 CE2 TYR B 110 8573 4087 5280 -1502 772 -987 C ATOM 2028 CZ TYR B 110 -22.705 13.047 97.530 1.00 41.31 C ANISOU 2028 CZ TYR B 110 7644 3518 4535 -1159 688 -993 C ATOM 2029 OH TYR B 110 -22.508 11.727 97.854 1.00 39.16 O ANISOU 2029 OH TYR B 110 6932 3609 4337 -1156 678 -963 O ATOM 2030 N GLY B 111 -23.459 20.452 97.269 1.00 61.04 N ANISOU 2030 N GLY B 111 12104 4414 6674 -1003 487 -1033 N ATOM 2031 CA GLY B 111 -23.108 21.804 96.892 1.00 62.80 C ANISOU 2031 CA GLY B 111 12736 4314 6812 -1131 493 -987 C ATOM 2032 C GLY B 111 -23.287 22.124 95.422 1.00 69.07 C ANISOU 2032 C GLY B 111 13839 4921 7485 -1078 523 -800 C ATOM 2033 O GLY B 111 -23.363 23.306 95.064 1.00 65.66 O ANISOU 2033 O GLY B 111 13812 4188 6947 -1068 488 -760 O ATOM 2034 N SER B 112 -23.356 21.108 94.561 1.00 65.65 N ANISOU 2034 N SER B 112 13243 4653 7049 -1042 580 -688 N ATOM 2035 CA SER B 112 -23.581 21.309 93.136 1.00 68.77 C ANISOU 2035 CA SER B 112 13920 4904 7306 -967 598 -519 C ATOM 2036 C SER B 112 -24.279 20.078 92.576 1.00 65.72 C ANISOU 2036 C SER B 112 13294 4732 6944 -716 572 -464 C ATOM 2037 O SER B 112 -24.599 19.133 93.306 1.00 49.44 O ANISOU 2037 O SER B 112 10871 2909 5004 -608 543 -556 O ATOM 2038 CB SER B 112 -22.266 21.581 92.396 1.00 73.42 C ANISOU 2038 CB SER B 112 14628 5438 7831 -1412 778 -423 C ATOM 2039 OG SER B 112 -21.296 20.589 92.688 1.00 66.13 O ANISOU 2039 OG SER B 112 13293 4807 7029 -1707 908 -458 O ATOM 2040 N GLU B 113 -24.519 20.095 91.264 1.00 64.88 N ANISOU 2040 N GLU B 113 13405 4540 6706 -628 577 -321 N ATOM 2041 CA GLU B 113 -25.072 18.945 90.561 1.00 58.45 C ANISOU 2041 CA GLU B 113 12394 3914 5899 -426 558 -258 C ATOM 2042 C GLU B 113 -23.991 17.999 90.052 1.00 55.36 C ANISOU 2042 C GLU B 113 11788 3701 5544 -763 746 -195 C ATOM 2043 O GLU B 113 -24.305 17.052 89.322 1.00 49.23 O ANISOU 2043 O GLU B 113 10886 3059 4760 -639 750 -132 O ATOM 2044 CB GLU B 113 -25.963 19.406 89.403 1.00 65.65 C ANISOU 2044 CB GLU B 113 13635 4671 6638 -123 440 -156 C ATOM 2045 CG GLU B 113 -27.334 19.910 89.846 1.00 70.48 C ANISOU 2045 CG GLU B 113 14306 5229 7246 327 220 -240 C ATOM 2046 CD GLU B 113 -28.306 20.085 88.689 1.00 78.52 C ANISOU 2046 CD GLU B 113 15546 6181 8107 665 74 -159 C ATOM 2047 OE1 GLU B 113 -28.439 21.224 88.185 1.00 84.05 O ANISOU 2047 OE1 GLU B 113 16674 6614 8646 721 9 -113 O ATOM 2048 OE2 GLU B 113 -28.942 19.085 88.287 1.00 73.19 O ANISOU 2048 OE2 GLU B 113 14623 5722 7464 873 14 -151 O ATOM 2049 N MET B 114 -22.730 18.238 90.417 1.00 51.40 N ANISOU 2049 N MET B 114 11222 3222 5086 -1177 894 -224 N ATOM 2050 CA MET B 114 -21.638 17.322 90.113 1.00 50.75 C ANISOU 2050 CA MET B 114 10843 3370 5068 -1496 1070 -204 C ATOM 2051 C MET B 114 -20.594 17.417 91.213 1.00 53.95 C ANISOU 2051 C MET B 114 11001 3898 5598 -1826 1140 -322 C ATOM 2052 O MET B 114 -20.222 18.518 91.627 1.00 59.55 O ANISOU 2052 O MET B 114 11913 4439 6275 -1977 1137 -363 O ATOM 2053 CB MET B 114 -20.985 17.623 88.756 1.00 58.88 C ANISOU 2053 CB MET B 114 12095 4327 5951 -1690 1208 -86 C ATOM 2054 CG MET B 114 -19.734 16.778 88.515 1.00 58.99 C ANISOU 2054 CG MET B 114 11751 4615 6046 -2026 1397 -99 C ATOM 2055 SD MET B 114 -19.024 16.894 86.856 1.00 76.60 S ANISOU 2055 SD MET B 114 14169 6823 8113 -2216 1572 13 S ATOM 2056 CE MET B 114 -18.204 18.485 86.936 1.00 78.14 C ANISOU 2056 CE MET B 114 14701 6777 8211 -2546 1650 -1 C ATOM 2057 N ALA B 115 -20.123 16.265 91.678 1.00 51.28 N ANISOU 2057 N ALA B 115 10228 3858 5399 -1930 1188 -380 N ATOM 2058 CA ALA B 115 -19.022 16.208 92.624 1.00 61.44 C ANISOU 2058 CA ALA B 115 11218 5328 6799 -2241 1242 -495 C ATOM 2059 C ALA B 115 -18.141 15.035 92.239 1.00 59.90 C ANISOU 2059 C ALA B 115 10620 5454 6685 -2413 1360 -485 C ATOM 2060 O ALA B 115 -18.653 13.952 91.947 1.00 49.04 O ANISOU 2060 O ALA B 115 9078 4207 5348 -2234 1343 -448 O ATOM 2061 CB ALA B 115 -19.524 16.055 94.065 1.00 62.06 C ANISOU 2061 CB ALA B 115 11139 5468 6974 -2107 1103 -634 C ATOM 2062 N ASP B 116 -16.827 15.260 92.212 1.00 66.58 N ANISOU 2062 N ASP B 116 11308 6432 7559 -2742 1473 -526 N ATOM 2063 CA ASP B 116 -15.863 14.213 91.867 1.00 74.77 C ANISOU 2063 CA ASP B 116 11924 7804 8680 -2879 1573 -543 C ATOM 2064 C ASP B 116 -16.176 13.594 90.506 1.00 61.13 C ANISOU 2064 C ASP B 116 10263 6084 6880 -2755 1654 -423 C ATOM 2065 O ASP B 116 -16.037 12.385 90.308 1.00 58.98 O ANISOU 2065 O ASP B 116 9660 6062 6686 -2681 1671 -423 O ATOM 2066 CB ASP B 116 -15.807 13.134 92.950 1.00 86.45 C ANISOU 2066 CB ASP B 116 12965 9571 10312 -2807 1476 -640 C ATOM 2067 CG ASP B 116 -14.877 13.500 94.089 1.00102.74 C ANISOU 2067 CG ASP B 116 14815 11767 12454 -3015 1433 -775 C ATOM 2068 OD1 ASP B 116 -14.963 14.637 94.597 1.00109.11 O ANISOU 2068 OD1 ASP B 116 15887 12357 13214 -3099 1396 -814 O ATOM 2069 OD2 ASP B 116 -14.057 12.640 94.475 1.00107.73 O ANISOU 2069 OD2 ASP B 116 15020 12720 13192 -3073 1420 -844 O ATOM 2070 N GLY B 117 -16.621 14.428 89.567 1.00 56.87 N ANISOU 2070 N GLY B 117 10165 5263 6179 -2713 1689 -321 N ATOM 2071 CA GLY B 117 -16.879 13.972 88.214 1.00 51.12 C ANISOU 2071 CA GLY B 117 9547 4524 5351 -2605 1759 -210 C ATOM 2072 C GLY B 117 -18.153 13.182 88.023 1.00 52.78 C ANISOU 2072 C GLY B 117 9794 4704 5554 -2250 1647 -145 C ATOM 2073 O GLY B 117 -18.376 12.666 86.924 1.00 49.44 O ANISOU 2073 O GLY B 117 9427 4303 5054 -2142 1689 -61 O ATOM 2074 N LEU B 118 -19.002 13.094 89.047 1.00 49.80 N ANISOU 2074 N LEU B 118 9395 4276 5251 -2062 1501 -190 N ATOM 2075 CA LEU B 118 -20.214 12.283 89.025 1.00 50.69 C ANISOU 2075 CA LEU B 118 9495 4382 5384 -1727 1385 -152 C ATOM 2076 C LEU B 118 -21.415 13.167 89.321 1.00 51.86 C ANISOU 2076 C LEU B 118 9995 4251 5458 -1441 1219 -154 C ATOM 2077 O LEU B 118 -21.384 13.960 90.266 1.00 44.79 O ANISOU 2077 O LEU B 118 9163 3266 4591 -1488 1163 -239 O ATOM 2078 CB LEU B 118 -20.126 11.157 90.056 1.00 46.65 C ANISOU 2078 CB LEU B 118 8538 4134 5051 -1731 1349 -243 C ATOM 2079 CG LEU B 118 -18.955 10.202 89.854 1.00 49.31 C ANISOU 2079 CG LEU B 118 8460 4801 5475 -1947 1476 -261 C ATOM 2080 CD1 LEU B 118 -18.640 9.481 91.158 1.00 50.77 C ANISOU 2080 CD1 LEU B 118 8208 5263 5821 -1963 1391 -380 C ATOM 2081 CD2 LEU B 118 -19.278 9.209 88.752 1.00 52.67 C ANISOU 2081 CD2 LEU B 118 8813 5341 5858 -1768 1504 -168 C ATOM 2082 N ASER B 119 -22.471 13.022 88.522 0.43 42.09 N ANISOU 2082 N ASER B 119 8956 2909 4126 -1117 1122 -73 N ATOM 2083 N BSER B 119 -22.475 13.024 88.527 0.57 41.54 N ANISOU 2083 N BSER B 119 8887 2839 4056 -1116 1122 -74 N ATOM 2084 CA ASER B 119 -23.644 13.868 88.683 0.43 42.95 C ANISOU 2084 CA ASER B 119 9347 2813 4159 -785 940 -86 C ATOM 2085 CA BSER B 119 -23.622 13.908 88.680 0.57 42.96 C ANISOU 2085 CA BSER B 119 9356 2809 4157 -792 942 -86 C ATOM 2086 C ASER B 119 -24.336 13.585 90.012 0.43 41.36 C ANISOU 2086 C ASER B 119 8921 2701 4093 -594 815 -229 C ATOM 2087 C BSER B 119 -24.405 13.570 89.948 0.57 41.72 C ANISOU 2087 C BSER B 119 8976 2744 4133 -572 808 -223 C ATOM 2088 O ASER B 119 -24.230 12.497 90.586 0.43 39.88 O ANISOU 2088 O ASER B 119 8347 2774 4033 -616 828 -293 O ATOM 2089 O BSER B 119 -24.414 12.430 90.421 0.57 40.73 O ANISOU 2089 O BSER B 119 8468 2881 4128 -556 811 -280 O ATOM 2090 CB ASER B 119 -24.626 13.659 87.529 0.43 45.02 C ANISOU 2090 CB ASER B 119 9785 3023 4296 -454 835 8 C ATOM 2091 CB BSER B 119 -24.530 13.837 87.448 0.57 43.89 C ANISOU 2091 CB BSER B 119 9694 2851 4131 -485 847 17 C ATOM 2092 OG ASER B 119 -24.031 13.987 86.290 0.43 47.08 O ANISOU 2092 OG ASER B 119 10284 3203 4400 -615 946 117 O ATOM 2093 OG BSER B 119 -25.174 12.580 87.346 0.57 43.98 O ANISOU 2093 OG BSER B 119 9447 3042 4221 -263 781 7 O ATOM 2094 N VAL B 120 -25.054 14.593 90.499 1.00 41.52 N ANISOU 2094 N VAL B 120 9134 2572 4070 -391 685 -281 N ATOM 2095 CA VAL B 120 -25.809 14.509 91.743 1.00 47.61 C ANISOU 2095 CA VAL B 120 9711 3443 4935 -178 568 -433 C ATOM 2096 C VAL B 120 -27.289 14.591 91.403 1.00 46.20 C ANISOU 2096 C VAL B 120 9577 3269 4709 284 389 -437 C ATOM 2097 O VAL B 120 -27.723 15.542 90.740 1.00 47.78 O ANISOU 2097 O VAL B 120 10096 3271 4787 431 308 -371 O ATOM 2098 CB VAL B 120 -25.410 15.636 92.714 1.00 42.98 C ANISOU 2098 CB VAL B 120 9254 2722 4353 -323 566 -520 C ATOM 2099 CG1 VAL B 120 -26.294 15.622 93.966 1.00 41.90 C ANISOU 2099 CG1 VAL B 120 8937 2701 4284 -68 448 -687 C ATOM 2100 CG2 VAL B 120 -23.929 15.538 93.070 1.00 43.59 C ANISOU 2100 CG2 VAL B 120 9218 2857 4488 -790 724 -533 C ATOM 2101 N GLU B 121 -28.060 13.602 91.857 1.00 44.14 N ANISOU 2101 N GLU B 121 8980 3258 4533 502 324 -524 N ATOM 2102 CA GLU B 121 -29.490 13.577 91.575 1.00 36.59 C ANISOU 2102 CA GLU B 121 7963 2386 3554 920 153 -549 C ATOM 2103 C GLU B 121 -30.165 14.824 92.125 1.00 51.89 C ANISOU 2103 C GLU B 121 10067 4193 5455 1115 44 -628 C ATOM 2104 O GLU B 121 -29.849 15.289 93.225 1.00 47.80 O ANISOU 2104 O GLU B 121 9530 3650 4981 1006 82 -733 O ATOM 2105 CB GLU B 121 -30.132 12.326 92.174 1.00 38.34 C ANISOU 2105 CB GLU B 121 7745 2943 3881 1061 129 -651 C ATOM 2106 CG GLU B 121 -29.627 11.030 91.580 1.00 38.97 C ANISOU 2106 CG GLU B 121 7610 3196 4001 910 207 -567 C ATOM 2107 CD GLU B 121 -30.411 9.828 92.075 1.00 43.17 C ANISOU 2107 CD GLU B 121 7670 4104 4631 1040 156 -628 C ATOM 2108 OE1 GLU B 121 -31.286 10.009 92.948 1.00 40.21 O ANISOU 2108 OE1 GLU B 121 7167 3834 4278 1237 93 -762 O ATOM 2109 OE2 GLU B 121 -30.164 8.707 91.584 1.00 45.96 O ANISOU 2109 OE2 GLU B 121 7791 4641 5030 940 187 -547 O ATOM 2110 N ASN B 122 -31.109 15.358 91.352 1.00 52.33 N ANISOU 2110 N ASN B 122 10289 4175 5419 1411 -103 -589 N ATOM 2111 CA ASN B 122 -31.725 16.653 91.630 1.00 55.12 C ANISOU 2111 CA ASN B 122 10878 4358 5707 1612 -218 -649 C ATOM 2112 C ASN B 122 -33.250 16.515 91.601 1.00 45.45 C ANISOU 2112 C ASN B 122 9449 3329 4492 2030 -394 -742 C ATOM 2113 O ASN B 122 -33.943 17.108 90.773 1.00 55.48 O ANISOU 2113 O ASN B 122 10935 4500 5646 2268 -540 -704 O ATOM 2114 CB ASN B 122 -31.226 17.691 90.624 1.00 56.66 C ANISOU 2114 CB ASN B 122 11570 4223 5735 1519 -224 -510 C ATOM 2115 CG ASN B 122 -31.747 19.085 90.909 1.00 60.71 C ANISOU 2115 CG ASN B 122 12381 4517 6170 1708 -342 -569 C ATOM 2116 OD1 ASN B 122 -31.743 19.544 92.054 1.00 58.04 O ANISOU 2116 OD1 ASN B 122 11984 4162 5907 1698 -330 -697 O ATOM 2117 ND2 ASN B 122 -32.193 19.770 89.864 1.00 66.48 N ANISOU 2117 ND2 ASN B 122 13452 5073 6733 1887 -462 -487 N ATOM 2118 N PHE B 123 -33.776 15.711 92.529 1.00 53.34 N ANISOU 2118 N PHE B 123 10019 4629 5617 2104 -378 -874 N ATOM 2119 CA PHE B 123 -35.211 15.464 92.629 1.00 47.13 C ANISOU 2119 CA PHE B 123 8956 4094 4858 2445 -514 -984 C ATOM 2120 C PHE B 123 -35.780 15.905 93.973 1.00 48.88 C ANISOU 2120 C PHE B 123 9010 4424 5137 2561 -509 -1168 C ATOM 2121 O PHE B 123 -36.855 15.442 94.367 1.00 51.64 O ANISOU 2121 O PHE B 123 9017 5067 5539 2761 -559 -1285 O ATOM 2122 CB PHE B 123 -35.520 13.986 92.382 1.00 47.83 C ANISOU 2122 CB PHE B 123 8648 4499 5025 2434 -495 -978 C ATOM 2123 CG PHE B 123 -35.175 13.525 90.996 1.00 47.81 C ANISOU 2123 CG PHE B 123 8791 4421 4954 2382 -522 -821 C ATOM 2124 CD1 PHE B 123 -34.130 12.637 90.780 1.00 43.07 C ANISOU 2124 CD1 PHE B 123 8147 3828 4392 2104 -382 -729 C ATOM 2125 CD2 PHE B 123 -35.885 13.993 89.906 1.00 49.18 C ANISOU 2125 CD2 PHE B 123 9159 4520 5006 2615 -690 -778 C ATOM 2126 CE1 PHE B 123 -33.808 12.221 89.506 1.00 45.41 C ANISOU 2126 CE1 PHE B 123 8584 4058 4613 2058 -393 -594 C ATOM 2127 CE2 PHE B 123 -35.569 13.579 88.631 1.00 43.85 C ANISOU 2127 CE2 PHE B 123 8635 3783 4240 2564 -709 -645 C ATOM 2128 CZ PHE B 123 -34.529 12.689 88.433 1.00 47.39 C ANISOU 2128 CZ PHE B 123 9033 4239 4733 2284 -554 -550 C ATOM 2129 N GLY B 124 -35.088 16.798 94.679 1.00 50.64 N ANISOU 2129 N GLY B 124 9469 4427 5345 2424 -444 -1202 N ATOM 2130 CA GLY B 124 -35.557 17.239 95.975 1.00 51.55 C ANISOU 2130 CA GLY B 124 9452 4637 5498 2522 -428 -1385 C ATOM 2131 C GLY B 124 -35.498 16.183 97.049 1.00 49.46 C ANISOU 2131 C GLY B 124 8775 4696 5323 2387 -298 -1484 C ATOM 2132 O GLY B 124 -36.110 16.354 98.110 1.00 53.82 O ANISOU 2132 O GLY B 124 9149 5410 5892 2497 -277 -1644 O ATOM 2133 N LEU B 125 -34.767 15.091 96.805 1.00 47.72 N ANISOU 2133 N LEU B 125 8414 4576 5142 2150 -206 -1392 N ATOM 2134 CA LEU B 125 -34.685 13.940 97.681 1.00 44.16 C ANISOU 2134 CA LEU B 125 7588 4442 4748 2015 -94 -1458 C ATOM 2135 C LEU B 125 -33.349 13.916 98.420 1.00 42.53 C ANISOU 2135 C LEU B 125 7477 4148 4533 1684 27 -1466 C ATOM 2136 O LEU B 125 -32.326 14.361 97.886 1.00 41.67 O ANISOU 2136 O LEU B 125 7664 3767 4403 1489 43 -1369 O ATOM 2137 CB LEU B 125 -34.858 12.640 96.884 1.00 42.91 C ANISOU 2137 CB LEU B 125 7189 4484 4631 2001 -96 -1362 C ATOM 2138 CG LEU B 125 -36.215 12.441 96.195 1.00 41.45 C ANISOU 2138 CG LEU B 125 6831 4460 4458 2294 -227 -1373 C ATOM 2139 CD1 LEU B 125 -36.241 11.128 95.444 1.00 43.90 C ANISOU 2139 CD1 LEU B 125 6919 4950 4811 2231 -226 -1284 C ATOM 2140 CD2 LEU B 125 -37.358 12.495 97.190 1.00 43.11 C ANISOU 2140 CD2 LEU B 125 6754 4936 4688 2464 -230 -1538 C ATOM 2141 N PRO B 126 -33.325 13.393 99.650 1.00 42.02 N ANISOU 2141 N PRO B 126 7166 4329 4471 1594 111 -1579 N ATOM 2142 CA PRO B 126 -32.084 13.395 100.438 1.00 40.33 C ANISOU 2142 CA PRO B 126 7035 4061 4227 1285 195 -1608 C ATOM 2143 C PRO B 126 -31.082 12.318 100.052 1.00 40.44 C ANISOU 2143 C PRO B 126 6978 4135 4251 1028 257 -1497 C ATOM 2144 O PRO B 126 -29.935 12.381 100.515 1.00 41.32 O ANISOU 2144 O PRO B 126 7161 4186 4352 731 308 -1488 O ATOM 2145 CB PRO B 126 -32.588 13.185 101.873 1.00 39.46 C ANISOU 2145 CB PRO B 126 6687 4228 4080 1321 249 -1764 C ATOM 2146 CG PRO B 126 -33.867 12.440 101.714 1.00 45.00 C ANISOU 2146 CG PRO B 126 7070 5216 4814 1542 241 -1764 C ATOM 2147 CD PRO B 126 -34.485 12.924 100.431 1.00 43.86 C ANISOU 2147 CD PRO B 126 7057 4897 4712 1766 128 -1691 C ATOM 2148 N PHE B 127 -31.463 11.347 99.224 1.00 36.51 N ANISOU 2148 N PHE B 127 6291 3783 3798 1097 246 -1391 N ATOM 2149 CA PHE B 127 -30.562 10.265 98.838 1.00 30.96 C ANISOU 2149 CA PHE B 127 5401 3200 3163 812 297 -1222 C ATOM 2150 C PHE B 127 -31.055 9.672 97.527 1.00 29.17 C ANISOU 2150 C PHE B 127 5121 2989 2975 944 253 -1107 C ATOM 2151 O PHE B 127 -32.020 10.152 96.926 1.00 37.25 O ANISOU 2151 O PHE B 127 6263 3922 3968 1241 171 -1153 O ATOM 2152 CB PHE B 127 -30.463 9.188 99.929 1.00 30.70 C ANISOU 2152 CB PHE B 127 5007 3507 3150 668 346 -1230 C ATOM 2153 CG PHE B 127 -31.740 8.991 100.711 1.00 32.31 C ANISOU 2153 CG PHE B 127 5011 3951 3316 892 346 -1358 C ATOM 2154 CD1 PHE B 127 -31.783 9.241 102.075 1.00 32.19 C ANISOU 2154 CD1 PHE B 127 4951 4055 3225 857 388 -1488 C ATOM 2155 CD2 PHE B 127 -32.888 8.537 100.080 1.00 32.31 C ANISOU 2155 CD2 PHE B 127 4851 4078 3347 1121 308 -1359 C ATOM 2156 CE1 PHE B 127 -32.958 9.065 102.800 1.00 39.66 C ANISOU 2156 CE1 PHE B 127 5700 5250 4119 1047 419 -1616 C ATOM 2157 CE2 PHE B 127 -34.067 8.352 100.790 1.00 30.92 C ANISOU 2157 CE2 PHE B 127 4449 4159 3140 1303 328 -1493 C ATOM 2158 CZ PHE B 127 -34.107 8.613 102.157 1.00 36.83 C ANISOU 2158 CZ PHE B 127 5152 5030 3810 1255 396 -1611 C ATOM 2159 N ASN B 128 -30.378 8.606 97.106 1.00 27.92 N ANISOU 2159 N ASN B 128 4781 2951 2877 735 293 -971 N ATOM 2160 CA ASN B 128 -30.638 7.956 95.827 1.00 29.74 C ANISOU 2160 CA ASN B 128 4972 3191 3136 809 257 -859 C ATOM 2161 C ASN B 128 -32.125 7.649 95.658 1.00 28.97 C ANISOU 2161 C ASN B 128 4714 3252 3042 1115 170 -929 C ATOM 2162 O ASN B 128 -32.774 7.126 96.569 1.00 30.27 O ANISOU 2162 O ASN B 128 4603 3670 3229 1152 183 -1010 O ATOM 2163 CB ASN B 128 -29.795 6.681 95.763 1.00 28.81 C ANISOU 2163 CB ASN B 128 4610 3247 3090 562 313 -747 C ATOM 2164 CG ASN B 128 -29.858 6.006 94.412 1.00 27.41 C ANISOU 2164 CG ASN B 128 4423 3060 2932 602 287 -639 C ATOM 2165 OD1 ASN B 128 -30.909 5.521 94.015 1.00 29.26 O ANISOU 2165 OD1 ASN B 128 4537 3403 3175 796 213 -654 O ATOM 2166 ND2 ASN B 128 -28.731 5.969 93.699 1.00 27.79 N ANISOU 2166 ND2 ASN B 128 4585 2995 2980 412 352 -544 N ATOM 2167 N LEU B 129 -32.674 7.993 94.485 1.00 32.13 N ANISOU 2167 N LEU B 129 5287 3511 3408 1329 80 -904 N ATOM 2168 CA LEU B 129 -34.122 7.927 94.312 1.00 35.16 C ANISOU 2168 CA LEU B 129 5530 4037 3793 1655 -30 -1007 C ATOM 2169 C LEU B 129 -34.675 6.510 94.434 1.00 28.76 C ANISOU 2169 C LEU B 129 4301 3565 3062 1602 -25 -998 C ATOM 2170 O LEU B 129 -35.872 6.354 94.697 1.00 33.47 O ANISOU 2170 O LEU B 129 4676 4367 3675 1804 -79 -1119 O ATOM 2171 CB LEU B 129 -34.529 8.541 92.968 1.00 34.01 C ANISOU 2171 CB LEU B 129 5652 3682 3588 1868 -159 -951 C ATOM 2172 CG LEU B 129 -34.017 7.892 91.679 1.00 36.13 C ANISOU 2172 CG LEU B 129 6013 3878 3837 1790 -169 -812 C ATOM 2173 CD1 LEU B 129 -34.907 6.739 91.227 1.00 32.96 C ANISOU 2173 CD1 LEU B 129 5280 3751 3491 1892 -252 -828 C ATOM 2174 CD2 LEU B 129 -33.938 8.953 90.583 1.00 35.40 C ANISOU 2174 CD2 LEU B 129 6342 3479 3630 1895 -251 -723 C ATOM 2175 N MET B 130 -33.860 5.475 94.210 1.00 26.93 N ANISOU 2175 N MET B 130 3959 3395 2880 1340 34 -868 N ATOM 2176 CA MET B 130 -34.358 4.115 94.405 1.00 24.06 C ANISOU 2176 CA MET B 130 3241 3314 2588 1265 37 -857 C ATOM 2177 C MET B 130 -34.812 3.876 95.849 1.00 27.08 C ANISOU 2177 C MET B 130 3381 3928 2980 1210 107 -950 C ATOM 2178 O MET B 130 -35.666 3.016 96.093 1.00 28.34 O ANISOU 2178 O MET B 130 3255 4333 3178 1211 104 -987 O ATOM 2179 CB MET B 130 -33.286 3.095 94.010 1.00 24.83 C ANISOU 2179 CB MET B 130 3303 3399 2730 1008 84 -711 C ATOM 2180 CG MET B 130 -32.979 3.041 92.507 1.00 26.28 C ANISOU 2180 CG MET B 130 3668 3425 2893 1054 30 -626 C ATOM 2181 SD MET B 130 -34.408 2.862 91.389 1.00 28.27 S ANISOU 2181 SD MET B 130 3869 3743 3128 1345 -133 -684 S ATOM 2182 CE MET B 130 -34.825 1.131 91.590 1.00 26.66 C ANISOU 2182 CE MET B 130 3284 3816 3028 1196 -138 -675 C ATOM 2183 N LEU B 131 -34.261 4.618 96.811 1.00 26.19 N ANISOU 2183 N LEU B 131 3387 3745 2821 1143 176 -993 N ATOM 2184 CA LEU B 131 -34.553 4.388 98.226 1.00 27.57 C ANISOU 2184 CA LEU B 131 3369 4137 2971 1067 256 -1073 C ATOM 2185 C LEU B 131 -35.826 5.068 98.688 1.00 33.04 C ANISOU 2185 C LEU B 131 3980 4954 3621 1331 247 -1260 C ATOM 2186 O LEU B 131 -36.130 5.030 99.888 1.00 38.41 O ANISOU 2186 O LEU B 131 4522 5821 4252 1288 332 -1349 O ATOM 2187 CB LEU B 131 -33.391 4.878 99.097 1.00 27.45 C ANISOU 2187 CB LEU B 131 3512 4011 2909 882 319 -1058 C ATOM 2188 CG LEU B 131 -32.016 4.403 98.626 1.00 27.43 C ANISOU 2188 CG LEU B 131 3588 3883 2950 646 326 -905 C ATOM 2189 CD1 LEU B 131 -30.895 4.968 99.502 1.00 29.18 C ANISOU 2189 CD1 LEU B 131 3937 4018 3130 466 369 -922 C ATOM 2190 CD2 LEU B 131 -31.962 2.888 98.594 1.00 30.01 C ANISOU 2190 CD2 LEU B 131 3673 4395 3336 506 331 -797 C ATOM 2191 N HIS B 132 -36.571 5.681 97.773 1.00 31.83 N ANISOU 2191 N HIS B 132 3909 4706 3479 1598 139 -1314 N ATOM 2192 CA HIS B 132 -37.698 6.533 98.111 1.00 35.48 C ANISOU 2192 CA HIS B 132 4340 5213 3930 1804 85 -1427 C ATOM 2193 C HIS B 132 -38.916 6.026 97.363 1.00 38.11 C ANISOU 2193 C HIS B 132 4445 5721 4315 1932 -19 -1444 C ATOM 2194 O HIS B 132 -38.928 6.043 96.133 1.00 41.21 O ANISOU 2194 O HIS B 132 4954 5984 4720 2034 -135 -1384 O ATOM 2195 CB HIS B 132 -37.407 7.983 97.728 1.00 41.03 C ANISOU 2195 CB HIS B 132 5419 5583 4586 1970 11 -1446 C ATOM 2196 CG HIS B 132 -38.359 8.967 98.333 1.00 47.57 C ANISOU 2196 CG HIS B 132 6243 6445 5388 2173 -26 -1580 C ATOM 2197 ND1 HIS B 132 -39.617 9.198 97.819 1.00 45.62 N ANISOU 2197 ND1 HIS B 132 5880 6299 5153 2413 -151 -1643 N ATOM 2198 CD2 HIS B 132 -38.238 9.772 99.415 1.00 42.74 C ANISOU 2198 CD2 HIS B 132 5725 5787 4728 2177 39 -1678 C ATOM 2199 CE1 HIS B 132 -40.226 10.110 98.556 1.00 52.23 C ANISOU 2199 CE1 HIS B 132 6736 7153 5956 2569 -155 -1775 C ATOM 2200 NE2 HIS B 132 -39.412 10.474 99.531 1.00 51.67 N ANISOU 2200 NE2 HIS B 132 6797 6986 5850 2431 -38 -1795 N ATOM 2201 N ASP B 133 -39.943 5.595 98.097 1.00 41.37 N ANISOU 2201 N ASP B 133 4552 6425 4742 1910 21 -1530 N ATOM 2202 CA ASP B 133 -41.125 4.994 97.491 1.00 39.38 C ANISOU 2202 CA ASP B 133 4052 6374 4535 1972 -67 -1569 C ATOM 2203 C ASP B 133 -42.351 5.901 97.533 1.00 48.95 C ANISOU 2203 C ASP B 133 5213 7661 5723 2234 -159 -1722 C ATOM 2204 O ASP B 133 -43.462 5.433 97.265 1.00 50.01 O ANISOU 2204 O ASP B 133 5100 8016 5885 2271 -214 -1798 O ATOM 2205 CB ASP B 133 -41.433 3.649 98.160 1.00 38.40 C ANISOU 2205 CB ASP B 133 3614 6530 4444 1702 48 -1548 C ATOM 2206 CG ASP B 133 -42.187 3.792 99.488 1.00 44.79 C ANISOU 2206 CG ASP B 133 4244 7562 5212 1662 159 -1658 C ATOM 2207 OD1 ASP B 133 -42.205 4.892 100.077 1.00 49.52 O ANISOU 2207 OD1 ASP B 133 4965 8092 5757 1816 174 -1747 O ATOM 2208 OD2 ASP B 133 -42.753 2.781 99.955 1.00 42.74 O ANISOU 2208 OD2 ASP B 133 3739 7535 4965 1462 239 -1653 O ATOM 2209 N GLY B 134 -42.183 7.181 97.877 1.00 49.40 N ANISOU 2209 N GLY B 134 5502 7540 5727 2410 -177 -1779 N ATOM 2210 CA GLY B 134 -43.276 8.130 97.973 1.00 53.09 C ANISOU 2210 CA GLY B 134 5946 8062 6165 2684 -269 -1932 C ATOM 2211 C GLY B 134 -43.600 8.557 99.393 1.00 58.57 C ANISOU 2211 C GLY B 134 6537 8892 6824 2682 -142 -2057 C ATOM 2212 O GLY B 134 -44.117 9.665 99.595 1.00 59.80 O ANISOU 2212 O GLY B 134 6791 8988 6941 2929 -205 -2177 O ATOM 2213 N THR B 135 -43.318 7.705 100.376 1.00 50.74 N ANISOU 2213 N THR B 135 5366 8080 5832 2414 32 -2030 N ATOM 2214 CA THR B 135 -43.550 8.066 101.766 1.00 51.12 C ANISOU 2214 CA THR B 135 5343 8258 5822 2390 167 -2139 C ATOM 2215 C THR B 135 -42.517 9.095 102.211 1.00 49.18 C ANISOU 2215 C THR B 135 5446 7718 5521 2426 192 -2132 C ATOM 2216 O THR B 135 -41.382 9.112 101.724 1.00 49.80 O ANISOU 2216 O THR B 135 5766 7549 5607 2332 174 -2011 O ATOM 2217 CB THR B 135 -43.470 6.827 102.654 1.00 59.25 C ANISOU 2217 CB THR B 135 6135 9539 6837 2069 337 -2085 C ATOM 2218 OG1 THR B 135 -44.109 5.733 101.986 1.00 66.27 O ANISOU 2218 OG1 THR B 135 6778 10610 7792 1966 302 -2044 O ATOM 2219 CG2 THR B 135 -44.157 7.081 103.997 1.00 61.07 C ANISOU 2219 CG2 THR B 135 6218 9990 6993 2067 468 -2222 C ATOM 2220 N ASP B 136 -42.926 9.970 103.131 1.00 51.01 N ANISOU 2220 N ASP B 136 5710 7978 5694 2558 237 -2277 N ATOM 2221 CA ASP B 136 -42.014 10.979 103.648 1.00 46.07 C ANISOU 2221 CA ASP B 136 5421 7073 5010 2573 263 -2297 C ATOM 2222 C ASP B 136 -40.807 10.310 104.297 1.00 43.16 C ANISOU 2222 C ASP B 136 5111 6686 4603 2252 393 -2194 C ATOM 2223 O ASP B 136 -40.892 9.199 104.825 1.00 45.75 O ANISOU 2223 O ASP B 136 5194 7272 4917 2042 499 -2145 O ATOM 2224 CB ASP B 136 -42.722 11.873 104.666 1.00 58.61 C ANISOU 2224 CB ASP B 136 6994 8742 6534 2747 308 -2487 C ATOM 2225 CG ASP B 136 -44.069 12.359 104.174 1.00 71.70 C ANISOU 2225 CG ASP B 136 8510 10512 8220 3063 186 -2615 C ATOM 2226 OD1 ASP B 136 -44.841 11.531 103.645 1.00 72.06 O ANISOU 2226 OD1 ASP B 136 8266 10797 8317 3054 151 -2602 O ATOM 2227 OD2 ASP B 136 -44.362 13.566 104.331 1.00 78.32 O ANISOU 2227 OD2 ASP B 136 9530 11204 9026 3316 118 -2740 O ATOM 2228 N VAL B 137 -39.671 10.990 104.240 1.00 49.59 N ANISOU 2228 N VAL B 137 6264 7189 5390 2201 375 -2159 N ATOM 2229 CA VAL B 137 -38.472 10.544 104.939 1.00 46.67 C ANISOU 2229 CA VAL B 137 5977 6795 4960 1915 476 -2096 C ATOM 2230 C VAL B 137 -38.499 11.164 106.328 1.00 48.08 C ANISOU 2230 C VAL B 137 6216 7020 5031 1904 565 -2231 C ATOM 2231 O VAL B 137 -38.540 12.391 106.471 1.00 47.60 O ANISOU 2231 O VAL B 137 6385 6751 4948 2064 522 -2344 O ATOM 2232 CB VAL B 137 -37.194 10.927 104.174 1.00 42.24 C ANISOU 2232 CB VAL B 137 5738 5893 4419 1826 411 -2007 C ATOM 2233 CG1 VAL B 137 -35.967 10.391 104.890 1.00 45.26 C ANISOU 2233 CG1 VAL B 137 6166 6297 4733 1528 493 -1959 C ATOM 2234 CG2 VAL B 137 -37.245 10.378 102.754 1.00 41.83 C ANISOU 2234 CG2 VAL B 137 5648 5789 4456 1868 323 -1880 C ATOM 2235 N PHE B 138 -38.503 10.317 107.352 1.00 45.52 N ANISOU 2235 N PHE B 138 5700 6963 4631 1715 686 -2218 N ATOM 2236 CA PHE B 138 -38.651 10.791 108.715 1.00 48.04 C ANISOU 2236 CA PHE B 138 6055 7372 4826 1708 780 -2345 C ATOM 2237 C PHE B 138 -37.303 11.252 109.263 1.00 44.95 C ANISOU 2237 C PHE B 138 5963 6770 4347 1540 778 -2348 C ATOM 2238 O PHE B 138 -36.254 11.072 108.640 1.00 49.30 O ANISOU 2238 O PHE B 138 6651 7146 4934 1402 718 -2248 O ATOM 2239 CB PHE B 138 -39.278 9.699 109.578 1.00 47.24 C ANISOU 2239 CB PHE B 138 5648 7642 4661 1567 906 -2317 C ATOM 2240 CG PHE B 138 -40.590 9.208 109.049 1.00 55.08 C ANISOU 2240 CG PHE B 138 6332 8855 5740 1683 905 -2330 C ATOM 2241 CD1 PHE B 138 -40.656 8.066 108.272 1.00 52.32 C ANISOU 2241 CD1 PHE B 138 5797 8605 5477 1554 880 -2186 C ATOM 2242 CD2 PHE B 138 -41.759 9.910 109.301 1.00 53.79 C ANISOU 2242 CD2 PHE B 138 6066 8800 5573 1923 916 -2501 C ATOM 2243 CE1 PHE B 138 -41.866 7.621 107.766 1.00 51.94 C ANISOU 2243 CE1 PHE B 138 5471 8757 5505 1638 863 -2214 C ATOM 2244 CE2 PHE B 138 -42.968 9.469 108.800 1.00 56.29 C ANISOU 2244 CE2 PHE B 138 6085 9338 5966 2020 898 -2532 C ATOM 2245 CZ PHE B 138 -43.021 8.326 108.032 1.00 56.62 C ANISOU 2245 CZ PHE B 138 5950 9474 6090 1867 869 -2390 C ATOM 2246 N ASP B 139 -37.342 11.876 110.440 1.00 47.09 N ANISOU 2246 N ASP B 139 6333 7064 4495 1549 840 -2481 N ATOM 2247 CA ASP B 139 -36.148 12.472 111.024 1.00 52.96 C ANISOU 2247 CA ASP B 139 7373 7605 5147 1399 818 -2523 C ATOM 2248 C ASP B 139 -35.420 11.546 111.983 1.00 47.64 C ANISOU 2248 C ASP B 139 6638 7121 4342 1131 870 -2442 C ATOM 2249 O ASP B 139 -34.275 11.837 112.348 1.00 55.38 O ANISOU 2249 O ASP B 139 7834 7957 5252 968 818 -2452 O ATOM 2250 CB ASP B 139 -36.506 13.764 111.763 1.00 67.13 C ANISOU 2250 CB ASP B 139 9354 9283 6870 1557 834 -2726 C ATOM 2251 CG ASP B 139 -37.295 14.722 110.904 1.00 84.23 C ANISOU 2251 CG ASP B 139 11583 11269 9153 1853 759 -2807 C ATOM 2252 OD1 ASP B 139 -38.543 14.644 110.921 1.00 89.33 O ANISOU 2252 OD1 ASP B 139 12004 12115 9822 2066 791 -2866 O ATOM 2253 OD2 ASP B 139 -36.664 15.546 110.207 1.00 91.64 O ANISOU 2253 OD2 ASP B 139 12795 11870 10156 1867 657 -2809 O ATOM 2254 N SER B 140 -36.049 10.455 112.407 1.00 48.58 N ANISOU 2254 N SER B 140 6477 7555 4425 1070 957 -2362 N ATOM 2255 CA SER B 140 -35.496 9.619 113.462 1.00 44.36 C ANISOU 2255 CA SER B 140 5902 7207 3744 836 1002 -2283 C ATOM 2256 C SER B 140 -36.235 8.292 113.466 1.00 50.46 C ANISOU 2256 C SER B 140 6368 8270 4536 751 1085 -2150 C ATOM 2257 O SER B 140 -37.286 8.144 112.836 1.00 53.39 O ANISOU 2257 O SER B 140 6545 8726 5015 883 1117 -2162 O ATOM 2258 CB SER B 140 -35.621 10.295 114.826 1.00 53.27 C ANISOU 2258 CB SER B 140 7164 8383 4694 863 1063 -2431 C ATOM 2259 OG SER B 140 -36.990 10.464 115.150 1.00 51.69 O ANISOU 2259 OG SER B 140 6799 8359 4483 1038 1178 -2533 O ATOM 2260 N PHE B 141 -35.670 7.324 114.196 1.00 47.31 N ANISOU 2260 N PHE B 141 5938 8012 4024 517 1105 -2025 N ATOM 2261 CA PHE B 141 -36.375 6.063 114.393 1.00 53.85 C ANISOU 2261 CA PHE B 141 6525 9093 4841 394 1197 -1897 C ATOM 2262 C PHE B 141 -37.707 6.289 115.096 1.00 53.85 C ANISOU 2262 C PHE B 141 6392 9293 4775 502 1337 -2017 C ATOM 2263 O PHE B 141 -38.716 5.671 114.736 1.00 50.07 O ANISOU 2263 O PHE B 141 5673 8977 4373 505 1402 -1986 O ATOM 2264 CB PHE B 141 -35.522 5.074 115.185 1.00 50.86 C ANISOU 2264 CB PHE B 141 6199 8800 4327 137 1185 -1742 C ATOM 2265 CG PHE B 141 -36.209 3.760 115.424 1.00 50.28 C ANISOU 2265 CG PHE B 141 5936 8939 4228 -18 1278 -1597 C ATOM 2266 CD1 PHE B 141 -36.133 2.749 114.482 1.00 51.01 C ANISOU 2266 CD1 PHE B 141 5907 9021 4454 -121 1235 -1438 C ATOM 2267 CD2 PHE B 141 -36.952 3.542 116.575 1.00 55.32 C ANISOU 2267 CD2 PHE B 141 6536 9777 4706 -69 1414 -1625 C ATOM 2268 CE1 PHE B 141 -36.777 1.543 114.683 1.00 46.40 C ANISOU 2268 CE1 PHE B 141 5183 8597 3852 -283 1314 -1308 C ATOM 2269 CE2 PHE B 141 -37.595 2.338 116.777 1.00 59.56 C ANISOU 2269 CE2 PHE B 141 6926 10486 5219 -239 1505 -1491 C ATOM 2270 CZ PHE B 141 -37.504 1.338 115.828 1.00 47.47 C ANISOU 2270 CZ PHE B 141 5290 8917 3829 -351 1449 -1332 C ATOM 2271 N GLU B 142 -37.727 7.172 116.101 1.00 57.64 N ANISOU 2271 N GLU B 142 7022 9769 5109 584 1382 -2168 N ATOM 2272 CA GLU B 142 -38.964 7.463 116.822 1.00 60.90 C ANISOU 2272 CA GLU B 142 7311 10384 5446 697 1527 -2306 C ATOM 2273 C GLU B 142 -40.050 7.968 115.881 1.00 60.18 C ANISOU 2273 C GLU B 142 7043 10295 5528 937 1523 -2417 C ATOM 2274 O GLU B 142 -41.205 7.539 115.964 1.00 57.87 O ANISOU 2274 O GLU B 142 6495 10241 5253 957 1624 -2447 O ATOM 2275 CB GLU B 142 -38.709 8.488 117.929 1.00 61.24 C ANISOU 2275 CB GLU B 142 7585 10373 5311 778 1557 -2472 C ATOM 2276 CG GLU B 142 -37.947 7.948 119.115 1.00 75.50 C ANISOU 2276 CG GLU B 142 9530 12258 6897 560 1580 -2388 C ATOM 2277 CD GLU B 142 -36.524 8.458 119.165 1.00 94.37 C ANISOU 2277 CD GLU B 142 12203 14406 9248 505 1420 -2386 C ATOM 2278 OE1 GLU B 142 -35.884 8.546 118.095 1.00 97.92 O ANISOU 2278 OE1 GLU B 142 12683 14662 9860 506 1294 -2330 O ATOM 2279 OE2 GLU B 142 -36.045 8.772 120.275 1.00104.03 O ANISOU 2279 OE2 GLU B 142 13618 15638 10271 454 1417 -2448 O ATOM 2280 N ALA B 143 -39.701 8.889 114.980 1.00 51.13 N ANISOU 2280 N ALA B 143 6038 8885 4505 1118 1396 -2482 N ATOM 2281 CA ALA B 143 -40.700 9.410 114.056 1.00 55.22 C ANISOU 2281 CA ALA B 143 6418 9387 5177 1373 1356 -2581 C ATOM 2282 C ALA B 143 -41.205 8.310 113.128 1.00 52.57 C ANISOU 2282 C ALA B 143 5811 9188 4977 1293 1338 -2445 C ATOM 2283 O ALA B 143 -42.413 8.173 112.909 1.00 54.48 O ANISOU 2283 O ALA B 143 5802 9623 5277 1400 1375 -2517 O ATOM 2284 CB ALA B 143 -40.126 10.585 113.265 1.00 58.47 C ANISOU 2284 CB ALA B 143 7093 9446 5677 1558 1214 -2649 C ATOM 2285 N ALA B 144 -40.292 7.495 112.591 1.00 49.95 N ANISOU 2285 N ALA B 144 5522 8767 4690 1098 1275 -2260 N ATOM 2286 CA ALA B 144 -40.703 6.383 111.739 1.00 50.64 C ANISOU 2286 CA ALA B 144 5378 8965 4896 996 1256 -2128 C ATOM 2287 C ALA B 144 -41.532 5.365 112.516 1.00 50.97 C ANISOU 2287 C ALA B 144 5188 9317 4863 814 1397 -2091 C ATOM 2288 O ALA B 144 -42.510 4.819 111.992 1.00 51.07 O ANISOU 2288 O ALA B 144 4955 9483 4965 815 1410 -2092 O ATOM 2289 CB ALA B 144 -39.475 5.709 111.120 1.00 41.74 C ANISOU 2289 CB ALA B 144 4365 7680 3815 818 1172 -1945 C ATOM 2290 N PHE B 145 -41.156 5.090 113.767 1.00 47.97 N ANISOU 2290 N PHE B 145 4896 9024 4307 644 1499 -2058 N ATOM 2291 CA PHE B 145 -41.905 4.104 114.537 1.00 49.90 C ANISOU 2291 CA PHE B 145 4962 9538 4460 446 1645 -2006 C ATOM 2292 C PHE B 145 -43.268 4.644 114.952 1.00 58.99 C ANISOU 2292 C PHE B 145 5920 10905 5587 605 1758 -2203 C ATOM 2293 O PHE B 145 -44.247 3.892 114.999 1.00 60.50 O ANISOU 2293 O PHE B 145 5870 11325 5793 496 1850 -2195 O ATOM 2294 CB PHE B 145 -41.117 3.661 115.768 1.00 55.80 C ANISOU 2294 CB PHE B 145 5888 10310 5002 231 1712 -1906 C ATOM 2295 CG PHE B 145 -41.844 2.653 116.605 1.00 61.97 C ANISOU 2295 CG PHE B 145 6539 11342 5666 13 1870 -1837 C ATOM 2296 CD1 PHE B 145 -42.217 2.947 117.907 1.00 65.36 C ANISOU 2296 CD1 PHE B 145 7008 11930 5893 0 2019 -1928 C ATOM 2297 CD2 PHE B 145 -42.184 1.417 116.078 1.00 57.08 C ANISOU 2297 CD2 PHE B 145 5772 10788 5130 -185 1877 -1686 C ATOM 2298 CE1 PHE B 145 -42.896 2.019 118.673 1.00 65.15 C ANISOU 2298 CE1 PHE B 145 6880 12130 5746 -216 2180 -1860 C ATOM 2299 CE2 PHE B 145 -42.863 0.486 116.842 1.00 62.41 C ANISOU 2299 CE2 PHE B 145 6353 11668 5691 -409 2029 -1620 C ATOM 2300 CZ PHE B 145 -43.222 0.790 118.140 1.00 57.56 C ANISOU 2300 CZ PHE B 145 5781 11218 4872 -428 2186 -1703 C ATOM 2301 N ALA B 146 -43.350 5.942 115.260 1.00 68.32 N ANISOU 2301 N ALA B 146 7210 12017 6730 857 1751 -2390 N ATOM 2302 CA ALA B 146 -44.640 6.543 115.592 1.00 67.76 C ANISOU 2302 CA ALA B 146 6950 12151 6646 1050 1844 -2600 C ATOM 2303 C ALA B 146 -45.572 6.527 114.388 1.00 68.10 C ANISOU 2303 C ALA B 146 6747 12248 6881 1206 1755 -2655 C ATOM 2304 O ALA B 146 -46.786 6.343 114.529 1.00 75.18 O ANISOU 2304 O ALA B 146 7368 13412 7785 1238 1842 -2764 O ATOM 2305 CB ALA B 146 -44.442 7.971 116.097 1.00 68.37 C ANISOU 2305 CB ALA B 146 7238 12091 6650 1305 1830 -2788 C ATOM 2306 N TYR B 147 -45.019 6.728 113.194 1.00 61.80 N ANISOU 2306 N TYR B 147 6047 11206 6228 1302 1577 -2588 N ATOM 2307 CA TYR B 147 -45.810 6.598 111.976 1.00 64.99 C ANISOU 2307 CA TYR B 147 6244 11648 6799 1432 1467 -2616 C ATOM 2308 C TYR B 147 -46.320 5.170 111.803 1.00 69.92 C ANISOU 2308 C TYR B 147 6622 12488 7456 1156 1530 -2497 C ATOM 2309 O TYR B 147 -47.474 4.962 111.412 1.00 72.00 O ANISOU 2309 O TYR B 147 6614 12954 7787 1214 1532 -2592 O ATOM 2310 CB TYR B 147 -44.966 7.036 110.779 1.00 57.47 C ANISOU 2310 CB TYR B 147 5498 10371 5966 1559 1276 -2541 C ATOM 2311 CG TYR B 147 -45.685 7.042 109.454 1.00 65.21 C ANISOU 2311 CG TYR B 147 6327 11350 7099 1730 1131 -2571 C ATOM 2312 CD1 TYR B 147 -45.703 5.909 108.652 1.00 63.61 C ANISOU 2312 CD1 TYR B 147 5992 11193 6983 1547 1089 -2429 C ATOM 2313 CD2 TYR B 147 -46.327 8.186 108.992 1.00 65.45 C ANISOU 2313 CD2 TYR B 147 6372 11320 7176 2080 1022 -2741 C ATOM 2314 CE1 TYR B 147 -46.348 5.905 107.435 1.00 69.61 C ANISOU 2314 CE1 TYR B 147 6631 11953 7865 1701 946 -2462 C ATOM 2315 CE2 TYR B 147 -46.978 8.190 107.770 1.00 71.97 C ANISOU 2315 CE2 TYR B 147 7079 12147 8120 2246 866 -2765 C ATOM 2316 CZ TYR B 147 -46.983 7.044 106.997 1.00 73.28 C ANISOU 2316 CZ TYR B 147 7108 12372 8362 2051 831 -2628 C ATOM 2317 OH TYR B 147 -47.619 7.019 105.777 1.00 77.16 O ANISOU 2317 OH TYR B 147 7495 12868 8954 2207 669 -2658 O ATOM 2318 N PHE B 148 -45.479 4.173 112.103 1.00 66.94 N ANISOU 2318 N PHE B 148 6344 12064 7026 853 1575 -2296 N ATOM 2319 CA PHE B 148 -45.896 2.778 111.985 1.00 59.51 C ANISOU 2319 CA PHE B 148 5223 11281 6108 569 1635 -2169 C ATOM 2320 C PHE B 148 -47.106 2.484 112.872 1.00 62.46 C ANISOU 2320 C PHE B 148 5361 11981 6391 479 1816 -2277 C ATOM 2321 O PHE B 148 -48.129 1.979 112.398 1.00 64.88 O ANISOU 2321 O PHE B 148 5407 12466 6777 439 1828 -2327 O ATOM 2322 CB PHE B 148 -44.727 1.848 112.332 1.00 58.74 C ANISOU 2322 CB PHE B 148 5320 11058 5940 281 1649 -1940 C ATOM 2323 CG PHE B 148 -45.102 0.388 112.379 1.00 61.33 C ANISOU 2323 CG PHE B 148 5524 11513 6265 -31 1720 -1797 C ATOM 2324 CD1 PHE B 148 -45.520 -0.204 113.572 1.00 66.18 C ANISOU 2324 CD1 PHE B 148 6100 12322 6723 -250 1899 -1770 C ATOM 2325 CD2 PHE B 148 -45.044 -0.393 111.233 1.00 59.45 C ANISOU 2325 CD2 PHE B 148 5231 11184 6171 -109 1611 -1690 C ATOM 2326 CE1 PHE B 148 -45.874 -1.545 113.619 1.00 58.19 C ANISOU 2326 CE1 PHE B 148 5009 11396 5703 -550 1967 -1634 C ATOM 2327 CE2 PHE B 148 -45.391 -1.736 111.271 1.00 58.48 C ANISOU 2327 CE2 PHE B 148 5026 11145 6047 -400 1672 -1563 C ATOM 2328 CZ PHE B 148 -45.807 -2.312 112.467 1.00 62.45 C ANISOU 2328 CZ PHE B 148 5504 11827 6398 -625 1849 -1533 C ATOM 2329 N VAL B 149 -47.007 2.796 114.167 1.00 62.65 N ANISOU 2329 N VAL B 149 5472 12093 6241 441 1962 -2323 N ATOM 2330 CA VAL B 149 -48.055 2.389 115.103 1.00 71.18 C ANISOU 2330 CA VAL B 149 6347 13490 7208 305 2165 -2402 C ATOM 2331 C VAL B 149 -49.394 3.025 114.752 1.00 79.45 C ANISOU 2331 C VAL B 149 7099 14750 8337 545 2173 -2643 C ATOM 2332 O VAL B 149 -50.449 2.404 114.936 1.00 84.44 O ANISOU 2332 O VAL B 149 7462 15658 8962 407 2294 -2698 O ATOM 2333 CB VAL B 149 -47.642 2.709 116.554 1.00 72.70 C ANISOU 2333 CB VAL B 149 6722 13725 7177 250 2315 -2415 C ATOM 2334 CG1 VAL B 149 -46.439 1.873 116.964 1.00 74.70 C ANISOU 2334 CG1 VAL B 149 7236 13818 7330 -21 2306 -2169 C ATOM 2335 CG2 VAL B 149 -47.346 4.187 116.719 1.00 76.12 C ANISOU 2335 CG2 VAL B 149 7302 14032 7589 583 2255 -2590 C ATOM 2336 N GLU B 150 -49.387 4.252 114.229 1.00 74.90 N ANISOU 2336 N GLU B 150 6571 14048 7838 904 2038 -2793 N ATOM 2337 CA GLU B 150 -50.652 4.887 113.884 1.00 71.66 C ANISOU 2337 CA GLU B 150 5890 13838 7501 1166 2018 -3030 C ATOM 2338 C GLU B 150 -51.276 4.282 112.632 1.00 72.66 C ANISOU 2338 C GLU B 150 5795 14018 7795 1151 1892 -3014 C ATOM 2339 O GLU B 150 -52.505 4.179 112.550 1.00 77.80 O ANISOU 2339 O GLU B 150 6132 14952 8478 1194 1939 -3172 O ATOM 2340 CB GLU B 150 -50.464 6.393 113.694 1.00 81.44 C ANISOU 2340 CB GLU B 150 7286 14894 8762 1569 1894 -3191 C ATOM 2341 CG GLU B 150 -51.438 7.245 114.493 1.00 98.24 C ANISOU 2341 CG GLU B 150 9265 17255 10807 1794 2007 -3452 C ATOM 2342 CD GLU B 150 -51.327 8.720 114.157 1.00104.23 C ANISOU 2342 CD GLU B 150 10195 17801 11607 2213 1853 -3613 C ATOM 2343 OE1 GLU B 150 -52.269 9.270 113.544 1.00105.29 O ANISOU 2343 OE1 GLU B 150 10142 18033 11831 2497 1748 -3789 O ATOM 2344 OE2 GLU B 150 -50.291 9.329 114.502 1.00102.93 O ANISOU 2344 OE2 GLU B 150 10368 17361 11379 2254 1827 -3564 O ATOM 2345 N HIS B 151 -50.464 3.856 111.659 1.00 67.43 N ANISOU 2345 N HIS B 151 5283 13103 7234 1085 1737 -2836 N ATOM 2346 CA HIS B 151 -50.996 3.411 110.379 1.00 69.86 C ANISOU 2346 CA HIS B 151 5422 13427 7694 1113 1592 -2834 C ATOM 2347 C HIS B 151 -50.891 1.912 110.140 1.00 72.81 C ANISOU 2347 C HIS B 151 5736 13831 8096 736 1638 -2645 C ATOM 2348 O HIS B 151 -51.356 1.444 109.095 1.00 78.95 O ANISOU 2348 O HIS B 151 6375 14629 8994 731 1527 -2646 O ATOM 2349 CB HIS B 151 -50.290 4.145 109.231 1.00 66.08 C ANISOU 2349 CB HIS B 151 5156 12632 7321 1375 1358 -2801 C ATOM 2350 CG HIS B 151 -50.534 5.621 109.214 1.00 77.19 C ANISOU 2350 CG HIS B 151 6631 13975 8723 1775 1271 -2992 C ATOM 2351 ND1 HIS B 151 -49.968 6.478 110.132 1.00 79.80 N ANISOU 2351 ND1 HIS B 151 7173 14198 8950 1872 1341 -3035 N ATOM 2352 CD2 HIS B 151 -51.273 6.395 108.383 1.00 82.62 C ANISOU 2352 CD2 HIS B 151 7230 14671 9490 2109 1107 -3152 C ATOM 2353 CE1 HIS B 151 -50.356 7.714 109.877 1.00 84.28 C ANISOU 2353 CE1 HIS B 151 7784 14699 9540 2244 1231 -3212 C ATOM 2354 NE2 HIS B 151 -51.147 7.692 108.819 1.00 84.08 N ANISOU 2354 NE2 HIS B 151 7582 14743 9622 2401 1082 -3282 N ATOM 2355 N HIS B 152 -50.310 1.146 111.062 1.00 77.23 N ANISOU 2355 N HIS B 152 6416 14386 8543 428 1787 -2486 N ATOM 2356 CA HIS B 152 -50.043 -0.270 110.817 1.00 76.96 C ANISOU 2356 CA HIS B 152 6397 14311 8532 79 1808 -2282 C ATOM 2357 C HIS B 152 -50.222 -1.096 112.092 1.00 89.42 C ANISOU 2357 C HIS B 152 7961 16059 9954 -249 2034 -2205 C ATOM 2358 O HIS B 152 -49.412 -1.967 112.414 1.00 95.68 O ANISOU 2358 O HIS B 152 8949 16718 10686 -509 2065 -1993 O ATOM 2359 CB HIS B 152 -48.644 -0.452 110.232 1.00 69.90 C ANISOU 2359 CB HIS B 152 5794 13082 7682 55 1670 -2084 C ATOM 2360 CG HIS B 152 -48.460 0.205 108.898 1.00 63.19 C ANISOU 2360 CG HIS B 152 4975 12057 6977 335 1459 -2132 C ATOM 2361 ND1 HIS B 152 -47.958 1.481 108.757 1.00 63.05 N ANISOU 2361 ND1 HIS B 152 5113 11881 6962 638 1365 -2211 N ATOM 2362 CD2 HIS B 152 -48.735 -0.229 107.645 1.00 61.53 C ANISOU 2362 CD2 HIS B 152 4678 11799 6902 356 1323 -2113 C ATOM 2363 CE1 HIS B 152 -47.918 1.800 107.475 1.00 59.24 C ANISOU 2363 CE1 HIS B 152 4649 11256 6604 832 1183 -2227 C ATOM 2364 NE2 HIS B 152 -48.388 0.781 106.779 1.00 59.32 N ANISOU 2364 NE2 HIS B 152 4508 11339 6693 672 1152 -2172 N ATOM 2365 N LEU B 153 -51.301 -0.826 112.828 1.00 94.22 N ANISOU 2365 N LEU B 153 8343 16968 10488 -233 2193 -2381 N ATOM 2366 CA LEU B 153 -51.757 -1.686 113.926 1.00 89.95 C ANISOU 2366 CA LEU B 153 7734 16640 9801 -564 2425 -2330 C ATOM 2367 C LEU B 153 -50.696 -1.953 114.998 1.00 86.87 C ANISOU 2367 C LEU B 153 7659 16115 9233 -739 2516 -2147 C ATOM 2368 O LEU B 153 -49.717 -1.217 115.130 1.00 82.13 O ANISOU 2368 O LEU B 153 7292 15315 8599 -566 2431 -2121 O ATOM 2369 CB LEU B 153 -52.255 -3.021 113.361 1.00 89.87 C ANISOU 2369 CB LEU B 153 7591 16684 9871 -867 2436 -2228 C ATOM 2370 CG LEU B 153 -53.753 -3.339 113.313 1.00 91.60 C ANISOU 2370 CG LEU B 153 7431 17246 10125 -958 2552 -2401 C ATOM 2371 CD1 LEU B 153 -54.541 -2.213 112.666 1.00 91.55 C ANISOU 2371 CD1 LEU B 153 7177 17380 10229 -571 2444 -2670 C ATOM 2372 CD2 LEU B 153 -53.976 -4.643 112.557 1.00 91.90 C ANISOU 2372 CD2 LEU B 153 7412 17242 10265 -1247 2512 -2273 C TER 2373 LEU B 153 HETATM 2374 C TRS A 201 -29.150 3.516 89.078 1.00 41.60 C HETATM 2375 C1 TRS A 201 -29.949 2.930 90.231 1.00 29.65 C HETATM 2376 C2 TRS A 201 -28.700 2.401 88.111 1.00 39.57 C HETATM 2377 C3 TRS A 201 -27.970 4.228 89.760 1.00 35.08 C HETATM 2378 N TRS A 201 -29.968 4.457 88.231 1.00 55.69 N HETATM 2379 O1 TRS A 201 -31.268 2.722 89.818 1.00 38.90 O HETATM 2380 O2 TRS A 201 -28.264 1.171 88.690 1.00 23.08 O HETATM 2381 O3 TRS A 201 -27.996 4.149 91.195 1.00 33.40 O HETATM 2382 C TRS A 202 -37.608 -14.746 79.294 0.54 38.43 C HETATM 2383 C1 TRS A 202 -36.979 -15.782 80.218 0.54 33.68 C HETATM 2384 C2 TRS A 202 -36.748 -13.487 79.245 0.54 39.09 C HETATM 2385 C3 TRS A 202 -39.025 -14.412 79.749 0.54 38.18 C HETATM 2386 N TRS A 202 -37.681 -15.323 77.909 0.54 38.08 N HETATM 2387 O1 TRS A 202 -36.714 -15.248 81.506 0.54 36.23 O HETATM 2388 O2 TRS A 202 -35.365 -13.795 79.256 0.54 36.53 O HETATM 2389 O3 TRS A 202 -39.084 -13.172 80.430 0.54 41.54 O HETATM 2390 C TRS B 201 -26.588 -3.942 108.179 1.00 32.30 C HETATM 2391 C1 TRS B 201 -27.659 -2.865 108.093 1.00 35.86 C HETATM 2392 C2 TRS B 201 -25.209 -3.325 107.964 1.00 32.73 C HETATM 2393 C3 TRS B 201 -26.800 -5.004 107.115 1.00 30.22 C HETATM 2394 N TRS B 201 -26.655 -4.568 109.505 1.00 44.37 N HETATM 2395 O1 TRS B 201 -28.888 -3.341 108.606 1.00 29.59 O HETATM 2396 O2 TRS B 201 -25.083 -2.855 106.627 1.00 25.88 O HETATM 2397 O3 TRS B 201 -27.226 -6.209 107.697 1.00 47.30 O HETATM 2398 O HOH A 301 -23.070 -2.990 69.222 1.00 35.31 O HETATM 2399 O HOH A 302 -8.895 4.182 106.291 1.00 54.08 O HETATM 2400 O HOH A 303 -5.363 -7.989 101.876 1.00 59.28 O HETATM 2401 O HOH A 304 -15.922 -14.460 103.989 1.00 48.50 O HETATM 2402 O HOH A 305 -41.988 -3.058 93.609 1.00 40.02 O HETATM 2403 O HOH A 306 -30.308 -15.809 70.205 1.00 60.50 O HETATM 2404 O HOH A 307 -11.786 -3.418 85.780 1.00 41.10 O HETATM 2405 O HOH A 308 -11.298 -7.778 83.399 1.00 43.89 O HETATM 2406 O HOH A 309 -3.744 -2.308 99.369 1.00 49.63 O HETATM 2407 O HOH A 310 -21.871 -19.019 90.341 1.00 47.95 O HETATM 2408 O HOH A 311 -20.334 1.202 85.542 1.00 37.16 O HETATM 2409 O HOH A 312 -32.236 5.180 89.406 1.00 48.44 O HETATM 2410 O HOH A 313 -15.819 -24.567 79.926 1.00 30.62 O HETATM 2411 O HOH A 314 -21.032 -23.537 79.061 1.00 31.94 O HETATM 2412 O HOH A 315 -20.850 -11.304 71.859 1.00 49.72 O HETATM 2413 O HOH A 316 -15.212 -18.437 89.557 1.00 39.72 O HETATM 2414 O HOH A 317 -43.324 -4.571 86.653 1.00 36.50 O HETATM 2415 O HOH A 318 -33.382 -17.159 84.178 1.00 32.34 O HETATM 2416 O HOH A 319 -21.466 4.974 98.240 1.00 36.49 O HETATM 2417 O HOH A 320 -45.453 2.945 83.512 1.00 47.59 O HETATM 2418 O HOH A 321 -26.797 -9.043 68.294 1.00 57.15 O HETATM 2419 O HOH A 322 -37.660 -13.158 83.260 1.00 31.29 O HETATM 2420 O HOH A 323 -23.545 -6.061 106.419 1.00 32.30 O HETATM 2421 O HOH A 324 -11.235 1.534 91.581 1.00 44.05 O HETATM 2422 O HOH A 325 -15.855 -2.135 95.657 1.00 27.63 O HETATM 2423 O HOH A 326 -23.295 14.954 78.607 1.00 41.85 O HETATM 2424 O HOH A 327 -16.358 -16.756 95.514 1.00 44.64 O HETATM 2425 O HOH A 328 -11.261 -9.433 105.829 1.00 38.83 O HETATM 2426 O HOH A 329 -14.381 -0.008 97.125 1.00 32.25 O HETATM 2427 O HOH A 330 -18.353 -21.286 89.290 1.00 47.27 O HETATM 2428 O HOH A 331 -17.827 -7.644 104.171 1.00 27.38 O HETATM 2429 O HOH A 332 -42.395 -8.808 91.788 1.00 47.14 O HETATM 2430 O HOH A 333 -14.029 -4.824 76.317 1.00 38.34 O HETATM 2431 O HOH A 334 -30.634 -15.567 93.686 1.00 31.86 O HETATM 2432 O HOH A 335 -11.839 1.171 97.288 1.00 38.61 O HETATM 2433 O HOH A 336 -17.378 -19.322 77.611 1.00 27.99 O HETATM 2434 O HOH A 337 -30.186 -17.435 75.743 1.00 50.09 O HETATM 2435 O HOH A 338 -22.077 2.026 102.313 1.00 26.87 O HETATM 2436 O HOH A 339 -27.804 -10.009 70.746 1.00 55.95 O HETATM 2437 O HOH A 340 -20.626 -11.654 92.026 1.00 24.45 O HETATM 2438 O HOH A 341 -31.784 -15.079 95.990 1.00 54.00 O HETATM 2439 O HOH A 342 -16.687 -2.318 81.202 1.00 29.44 O HETATM 2440 O HOH A 343 -40.089 -18.721 67.173 1.00 52.31 O HETATM 2441 O HOH A 344 -16.685 0.584 87.219 1.00 47.71 O HETATM 2442 O HOH A 345 -18.075 4.064 90.683 1.00 44.28 O HETATM 2443 O HOH A 346 -19.788 9.191 75.339 1.00 22.99 O HETATM 2444 O HOH A 347 -25.856 1.032 85.180 1.00 22.57 O HETATM 2445 O HOH A 348 -33.211 -15.953 86.786 1.00 27.81 O HETATM 2446 O HOH A 349 -20.734 -9.834 95.520 1.00 24.44 O HETATM 2447 O HOH A 350 -26.297 7.158 94.840 1.00 31.86 O HETATM 2448 O HOH A 351 -17.111 -16.817 78.708 1.00 23.32 O HETATM 2449 O HOH A 352 -20.995 1.031 92.856 1.00 22.58 O HETATM 2450 O HOH A 353 -14.864 4.157 91.099 1.00 45.86 O HETATM 2451 O HOH A 354 -16.118 7.710 93.263 1.00 35.52 O HETATM 2452 O HOH A 355 -28.566 7.178 81.927 1.00 39.49 O HETATM 2453 O HOH A 356 -21.221 -12.795 95.434 1.00 26.30 O HETATM 2454 O HOH A 357 -22.702 -0.588 70.808 1.00 29.02 O HETATM 2455 O HOH A 358 -21.287 -0.887 104.495 1.00 30.42 O HETATM 2456 O HOH A 359 -28.300 -15.988 95.117 1.00 35.06 O HETATM 2457 O HOH A 360 -12.545 -7.088 104.962 1.00 29.78 O HETATM 2458 O HOH A 361 -23.434 -3.057 85.290 1.00 25.93 O HETATM 2459 O HOH A 362 -17.822 2.295 88.543 1.00 32.15 O HETATM 2460 O HOH A 363 -14.429 -1.509 78.666 1.00 30.27 O HETATM 2461 O HOH A 364 -19.858 -5.969 68.949 1.00 40.92 O HETATM 2462 O HOH A 365 -24.503 -10.742 95.380 1.00 25.13 O HETATM 2463 O HOH A 366 -24.078 -17.847 89.011 1.00 34.01 O HETATM 2464 O HOH A 367 -26.315 2.350 74.796 1.00 29.51 O HETATM 2465 O HOH A 368 -18.402 2.743 73.986 1.00 22.71 O HETATM 2466 O HOH A 369 -10.821 -5.347 90.102 1.00 35.65 O HETATM 2467 O HOH A 370 -24.380 -15.906 90.735 1.00 29.59 O HETATM 2468 O HOH A 371 -23.031 -12.314 93.237 1.00 25.98 O HETATM 2469 O HOH A 372 -12.730 -11.129 93.765 1.00 33.31 O HETATM 2470 O HOH A 373 -22.039 -19.993 75.996 1.00 43.51 O HETATM 2471 O HOH A 374 -41.742 4.326 92.739 1.00 44.55 O HETATM 2472 O HOH A 375 -20.045 6.195 80.182 1.00 21.84 O HETATM 2473 O HOH A 376 -15.650 5.195 102.470 1.00 38.54 O HETATM 2474 O HOH A 377 -39.288 13.748 90.681 1.00 47.07 O HETATM 2475 O HOH A 378 -22.839 1.249 86.013 1.00 31.56 O HETATM 2476 O HOH A 379 -14.146 -3.045 74.840 1.00 51.90 O HETATM 2477 O HOH A 380 -19.024 -23.044 77.568 1.00 33.11 O HETATM 2478 O HOH A 381 -19.223 -1.812 101.395 1.00 28.19 O HETATM 2479 O HOH A 382 -17.144 -1.285 72.471 1.00 31.88 O HETATM 2480 O HOH A 383 -41.881 -0.179 96.527 1.00 40.27 O HETATM 2481 O HOH A 384 -15.989 -8.036 110.931 1.00 53.74 O HETATM 2482 O HOH A 385 -17.748 12.083 98.541 1.00 54.77 O HETATM 2483 O HOH A 386 -34.005 -17.068 72.088 1.00 29.99 O HETATM 2484 O HOH A 387 -23.879 -21.018 79.135 1.00 36.94 O HETATM 2485 O HOH A 388 -42.655 -0.780 88.821 1.00 46.13 O HETATM 2486 O HOH A 389 -12.825 -12.553 90.015 1.00 42.11 O HETATM 2487 O HOH A 390 -22.160 10.440 74.321 1.00 28.94 O HETATM 2488 O HOH A 391 -15.171 -8.304 104.607 1.00 29.52 O HETATM 2489 O HOH A 392 -16.508 -1.498 100.335 1.00 33.58 O HETATM 2490 O HOH A 393 -18.555 -10.842 74.552 1.00 32.77 O HETATM 2491 O HOH A 394 -16.362 -2.595 83.861 1.00 26.25 O HETATM 2492 O HOH A 395 -41.779 -5.708 84.284 1.00 34.32 O HETATM 2493 O HOH A 396 -15.262 6.993 107.034 1.00 44.70 O HETATM 2494 O HOH A 397 -27.862 -8.092 72.467 1.00 33.78 O HETATM 2495 O HOH A 398 -26.858 -15.862 92.034 1.00 28.99 O HETATM 2496 O HOH A 399 -28.197 -3.961 72.190 1.00 34.91 O HETATM 2497 O HOH A 400 -13.501 -14.876 89.039 1.00 41.38 O HETATM 2498 O HOH A 401 -21.520 -24.305 83.410 1.00 30.02 O HETATM 2499 O HOH A 402 -20.918 -14.490 101.330 1.00 42.29 O HETATM 2500 O HOH A 403 -32.667 -1.557 77.758 1.00 32.64 O HETATM 2501 O HOH A 404 -26.524 -5.964 72.029 1.00 33.89 O HETATM 2502 O HOH A 405 -41.766 -7.458 93.067 1.00 46.78 O HETATM 2503 O HOH A 406 -27.264 6.533 78.564 1.00 42.09 O HETATM 2504 O HOH A 407 -37.577 2.089 98.282 1.00 28.38 O HETATM 2505 O HOH A 408 -46.666 6.692 85.110 1.00 51.20 O HETATM 2506 O HOH A 409 -41.957 11.554 90.284 1.00 51.44 O HETATM 2507 O HOH A 410 -11.365 4.760 114.609 1.00 48.66 O HETATM 2508 O HOH A 411 -31.204 -18.023 90.412 1.00 45.68 O HETATM 2509 O HOH A 412 -17.396 -0.383 85.450 1.00 42.06 O HETATM 2510 O HOH A 413 -13.305 -2.808 81.542 1.00 39.85 O HETATM 2511 O HOH A 414 -25.894 -17.171 72.431 1.00 34.47 O HETATM 2512 O HOH A 415 -22.160 -12.915 102.715 1.00 32.15 O HETATM 2513 O HOH A 416 -22.674 -19.008 93.369 1.00 50.14 O HETATM 2514 O HOH A 417 -15.293 -13.113 96.623 1.00 39.83 O HETATM 2515 O HOH A 418 -12.750 -11.235 87.463 1.00 24.35 O HETATM 2516 O HOH A 419 -14.160 -13.247 94.625 1.00 35.20 O HETATM 2517 O HOH A 420 -42.230 10.606 88.119 1.00 43.81 O HETATM 2518 O HOH A 421 -18.169 -17.997 91.322 1.00 32.93 O HETATM 2519 O HOH A 422 -19.654 4.805 72.520 1.00 21.37 O HETATM 2520 O HOH A 423 -23.492 -23.662 80.339 1.00 44.86 O HETATM 2521 O HOH A 424 -8.950 -4.952 92.176 1.00 39.00 O HETATM 2522 O HOH A 425 -17.851 -2.089 107.422 1.00 35.42 O HETATM 2523 O HOH A 426 -9.412 5.977 112.064 1.00 47.18 O HETATM 2524 O HOH A 427 -10.859 -10.563 83.918 1.00 42.31 O HETATM 2525 O HOH A 428 -7.050 -2.507 93.901 1.00 53.49 O HETATM 2526 O HOH A 429 -30.116 5.479 80.101 1.00 54.50 O HETATM 2527 O HOH A 430 -6.042 1.960 100.724 1.00 56.13 O HETATM 2528 O HOH A 431 -12.860 -15.243 94.366 1.00 52.77 O HETATM 2529 O HOH A 432 -20.315 7.326 73.261 1.00 27.48 O HETATM 2530 O HOH A 433 -12.764 -10.305 96.218 1.00 53.09 O HETATM 2531 O HOH A 434 -27.324 -2.380 69.789 1.00 49.23 O HETATM 2532 O HOH A 435 -23.248 -18.630 100.154 1.00 51.90 O HETATM 2533 O HOH A 436 -23.566 -15.993 100.715 1.00 39.21 O HETATM 2534 O HOH A 437 -19.699 -2.784 105.926 1.00 31.68 O HETATM 2535 O HOH A 438 -29.494 0.603 70.718 1.00 46.54 O HETATM 2536 O HOH A 439 -32.447 -17.985 88.368 1.00 39.27 O HETATM 2537 O HOH A 440 -9.588 -4.398 88.207 1.00 58.90 O HETATM 2538 O HOH A 441 -17.240 8.271 82.737 1.00 29.56 O HETATM 2539 O HOH A 442 -24.808 0.741 70.016 1.00 48.18 O HETATM 2540 O HOH A 443 -26.360 -19.392 89.813 1.00 47.04 O HETATM 2541 O HOH A 444 -20.394 0.472 70.018 1.00 37.54 O HETATM 2542 O HOH A 445 -18.502 0.869 71.965 1.00 28.72 O HETATM 2543 O HOH A 446 -9.127 -10.224 104.866 1.00 47.35 O HETATM 2544 O HOH A 447 -38.188 -19.276 77.591 1.00 44.76 O HETATM 2545 O HOH A 448 -15.910 3.587 84.293 1.00 45.23 O HETATM 2546 O HOH A 449 -20.901 -3.389 67.895 1.00 44.39 O HETATM 2547 O HOH A 450 -28.943 -20.536 88.278 1.00 45.21 O HETATM 2548 O HOH A 451 -30.588 -19.680 86.492 1.00 41.77 O HETATM 2549 O HOH A 452 -47.400 4.653 82.996 1.00 28.79 O HETATM 2550 O HOH A 453 -30.595 -17.738 83.811 1.00 36.69 O HETATM 2551 O HOH A 454 -11.688 5.885 117.301 1.00 57.74 O HETATM 2552 O HOH A 455 -28.190 -18.043 91.342 1.00 42.79 O HETATM 2553 O HOH A 456 -34.762 -19.439 84.191 1.00 48.24 O HETATM 2554 O HOH A 457 -13.772 -1.895 84.112 1.00 37.28 O HETATM 2555 O HOH A 458 -34.156 -20.104 88.021 1.00 49.87 O HETATM 2556 O HOH A 459 -19.059 -1.298 68.382 1.00 51.64 O HETATM 2557 O HOH B 301 -23.640 1.054 124.738 1.00 43.94 O HETATM 2558 O HOH B 302 -26.015 -9.242 115.829 1.00 62.56 O HETATM 2559 O HOH B 303 -25.236 -7.571 107.761 1.00 38.18 O HETATM 2560 O HOH B 304 -21.811 -6.244 109.800 1.00 48.20 O HETATM 2561 O HOH B 305 -30.774 6.314 91.340 1.00 37.49 O HETATM 2562 O HOH B 306 -20.553 6.087 100.494 1.00 43.22 O HETATM 2563 O HOH B 307 -23.980 9.794 109.995 1.00 42.05 O HETATM 2564 O HOH B 308 -33.384 14.376 110.284 1.00 50.47 O HETATM 2565 O HOH B 309 -32.632 -14.673 98.980 1.00 49.30 O HETATM 2566 O HOH B 310 -17.738 0.581 105.980 1.00 38.24 O HETATM 2567 O HOH B 311 -32.560 11.500 94.655 1.00 36.50 O HETATM 2568 O HOH B 312 -43.770 0.679 98.784 1.00 50.41 O HETATM 2569 O HOH B 313 -22.176 4.825 102.217 1.00 35.23 O HETATM 2570 O HOH B 314 -27.670 8.598 98.206 1.00 29.65 O HETATM 2571 O HOH B 315 -20.518 13.499 85.589 1.00 42.74 O HETATM 2572 O HOH B 316 -33.385 0.953 111.906 1.00 33.60 O HETATM 2573 O HOH B 317 -24.920 12.214 84.486 1.00 38.52 O HETATM 2574 O HOH B 318 -20.428 11.336 99.520 1.00 47.99 O HETATM 2575 O HOH B 319 -17.474 -15.712 106.628 1.00 43.02 O HETATM 2576 O HOH B 320 -39.735 6.662 104.377 1.00 40.67 O HETATM 2577 O HOH B 321 -28.002 1.475 126.149 1.00 51.06 O HETATM 2578 O HOH B 322 -37.222 6.869 101.598 1.00 35.83 O HETATM 2579 O HOH B 323 -29.487 -1.906 112.403 1.00 33.87 O HETATM 2580 O HOH B 324 -21.726 -2.494 123.304 1.00 43.52 O HETATM 2581 O HOH B 325 -18.510 -2.009 115.754 1.00 57.18 O HETATM 2582 O HOH B 326 -29.169 10.710 104.239 1.00 37.80 O HETATM 2583 O HOH B 327 -32.910 18.552 94.368 1.00 45.92 O HETATM 2584 O HOH B 328 -27.316 4.507 106.366 1.00 28.33 O HETATM 2585 O HOH B 329 -26.997 -7.691 116.694 1.00 65.43 O HETATM 2586 O HOH B 330 -38.425 3.544 100.461 1.00 38.48 O HETATM 2587 O HOH B 331 -32.627 14.173 94.563 1.00 41.72 O HETATM 2588 O HOH B 332 -24.068 5.449 97.519 1.00 30.31 O HETATM 2589 O HOH B 333 -20.856 -18.040 107.780 1.00 44.85 O HETATM 2590 O HOH B 334 -40.133 4.446 102.694 1.00 38.37 O HETATM 2591 O HOH B 335 -31.300 16.687 95.213 1.00 45.62 O HETATM 2592 O HOH B 336 -24.514 6.338 109.743 1.00 45.92 O HETATM 2593 O HOH B 337 -27.277 10.842 99.889 1.00 42.63 O HETATM 2594 O HOH B 338 -39.721 6.943 100.921 1.00 40.88 O HETATM 2595 O HOH B 339 -34.001 -1.479 126.133 1.00 47.50 O HETATM 2596 O HOH B 340 -20.403 8.127 108.979 1.00 49.29 O HETATM 2597 O HOH B 341 -28.890 1.936 112.401 1.00 32.57 O HETATM 2598 O HOH B 342 -26.424 -10.355 97.401 1.00 23.50 O HETATM 2599 O HOH B 343 -38.154 -16.282 107.427 1.00 46.39 O HETATM 2600 O HOH B 344 -25.726 -15.898 101.844 1.00 38.30 O HETATM 2601 O HOH B 345 -44.017 4.513 94.580 1.00 54.17 O HETATM 2602 O HOH B 346 -38.303 7.522 93.624 1.00 38.63 O HETATM 2603 O HOH B 347 -25.428 2.633 119.018 1.00 37.73 O HETATM 2604 O HOH B 348 -20.703 3.595 120.179 1.00 44.28 O HETATM 2605 O HOH B 349 -32.865 -15.364 111.190 1.00 48.71 O HETATM 2606 O HOH B 350 -29.490 -14.736 97.514 1.00 35.79 O HETATM 2607 O HOH B 351 -26.246 13.911 109.910 1.00 53.37 O HETATM 2608 O HOH B 352 -20.061 21.225 90.075 1.00 51.09 O HETATM 2609 O HOH B 353 -19.264 -17.364 105.776 1.00 52.68 O HETATM 2610 O HOH B 354 -31.290 14.577 88.487 1.00 48.02 O HETATM 2611 O HOH B 355 -26.075 11.316 92.625 1.00 38.80 O HETATM 2612 O HOH B 356 -39.745 9.370 94.834 1.00 40.81 O HETATM 2613 O HOH B 357 -32.907 8.162 115.340 1.00 46.46 O HETATM 2614 O HOH B 358 -32.952 -3.880 126.312 1.00 59.56 O HETATM 2615 O HOH B 359 -27.440 9.156 93.537 1.00 40.10 O HETATM 2616 O HOH B 360 -17.193 17.890 90.026 1.00 49.74 O HETATM 2617 O HOH B 361 -17.479 12.618 95.967 1.00 52.26 O HETATM 2618 O HOH B 362 -17.560 20.338 89.529 1.00 45.62 O HETATM 2619 O HOH B 363 -32.557 3.274 126.299 1.00 57.27 O HETATM 2620 O HOH B 364 -17.432 8.858 108.899 1.00 47.72 O HETATM 2621 O HOH B 365 -55.474 7.302 108.491 1.00 46.41 O CONECT 338 2378 CONECT 2374 2375 2376 2377 2378 CONECT 2375 2374 2379 CONECT 2376 2374 2380 CONECT 2377 2374 2381 CONECT 2378 338 2374 CONECT 2379 2375 CONECT 2380 2376 CONECT 2381 2377 CONECT 2382 2383 2384 2385 2386 CONECT 2383 2382 2387 CONECT 2384 2382 2388 CONECT 2385 2382 2389 CONECT 2386 2382 CONECT 2387 2383 CONECT 2388 2384 CONECT 2389 2385 CONECT 2390 2391 2392 2393 2394 CONECT 2391 2390 2395 CONECT 2392 2390 2396 CONECT 2393 2390 2397 CONECT 2394 2390 CONECT 2395 2391 CONECT 2396 2392 CONECT 2397 2393 MASTER 460 0 3 14 12 0 9 6 2593 2 25 24 END If you find results from this site helpful for your research, please cite one of our papers:
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